CNRS Nantes University US2B US2B
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***  h_eNOS  ***

elNémo ID: 2412161419583470538

Job options:

ID        	=	 2412161419583470538
JOBID     	=	 h_eNOS
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER h_eNOS

HEADER    OXIDOREDUCTASE/INHIBITOR                05-JUL-19   6PP1              
TITLE     STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN   
TITLE    2 COMPLEX WITH 7-(3-(AMINOMETHYL)-4-(CYCLOPROPYLMETHOXY)PHENYL)-4-     
TITLE    3 METHYLQUINOLIN-2-AMINE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CONSTITUTIVE NOS,CNOS,EC-NOS,ENDOTHELIAL NOS,ENOS,NOS TYPE  
COMPND   5 III,NOSIII;                                                          
COMPND   6 EC: 1.14.13.39;                                                      
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL: ENDOTHELIAL;                                                   
SOURCE   6 GENE: NOS3;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE INHIBITOR, HEME ENZYME, OXIDOREDUCTASE,         
KEYWDS   2 OXIDOREDUCTASE-INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   11-OCT-23 6PP1    1       LINK                                     
REVDAT   2   27-MAY-20 6PP1    1       JRNL                                     
REVDAT   1   29-APR-20 6PP1    0                                                
JRNL        AUTH   M.A.CINELLI,C.T.REIDL,H.LI,G.CHREIFI,T.L.POULOS,             
JRNL        AUTH 2 R.B.SILVERMAN                                                
JRNL        TITL   FIRST CONTACT: 7-PHENYL-2-AMINOQUINOLINES, POTENT AND        
JRNL        TITL 2 SELECTIVE NEURONAL NITRIC OXIDE SYNTHASE INHIBITORS THAT     
JRNL        TITL 3 TARGET AN ISOFORM-SPECIFIC ASPARTATE.                        
JRNL        REF    J.MED.CHEM.                   V.  63  4528 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   32302123                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B01573                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1-2575_1496: ???)                       
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 190937                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9620                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.7251 -  5.4664    1.00     6195   298  0.1725 0.1878        
REMARK   3     2  5.4664 -  4.3396    1.00     6150   313  0.1303 0.1534        
REMARK   3     3  4.3396 -  3.7913    1.00     6104   324  0.1367 0.1546        
REMARK   3     4  3.7913 -  3.4448    1.00     6106   323  0.1544 0.1994        
REMARK   3     5  3.4448 -  3.1979    1.00     6069   336  0.1705 0.2023        
REMARK   3     6  3.1979 -  3.0094    1.00     6102   296  0.1787 0.2149        
REMARK   3     7  3.0094 -  2.8587    1.00     6087   310  0.1812 0.2365        
REMARK   3     8  2.8587 -  2.7343    1.00     6070   318  0.1787 0.2003        
REMARK   3     9  2.7343 -  2.6290    1.00     6092   348  0.1714 0.1989        
REMARK   3    10  2.6290 -  2.5383    1.00     6070   326  0.1736 0.2053        
REMARK   3    11  2.5383 -  2.4589    1.00     6055   329  0.1816 0.2178        
REMARK   3    12  2.4589 -  2.3886    1.00     6059   333  0.1858 0.2268        
REMARK   3    13  2.3886 -  2.3258    1.00     6093   314  0.1873 0.2215        
REMARK   3    14  2.3258 -  2.2690    1.00     6081   328  0.1886 0.2265        
REMARK   3    15  2.2690 -  2.2174    1.00     6050   318  0.1963 0.2535        
REMARK   3    16  2.2174 -  2.1702    1.00     6116   307  0.1962 0.2433        
REMARK   3    17  2.1702 -  2.1268    1.00     6031   317  0.2038 0.2578        
REMARK   3    18  2.1268 -  2.0867    1.00     6057   352  0.2105 0.2515        
REMARK   3    19  2.0867 -  2.0494    1.00     6026   358  0.2258 0.2712        
REMARK   3    20  2.0494 -  2.0147    1.00     6055   332  0.2347 0.2643        
REMARK   3    21  2.0147 -  1.9822    1.00     6034   322  0.2438 0.2938        
REMARK   3    22  1.9822 -  1.9517    1.00     6122   327  0.2698 0.3096        
REMARK   3    23  1.9517 -  1.9230    1.00     6036   304  0.2715 0.3015        
REMARK   3    24  1.9230 -  1.8959    1.00     6118   319  0.2935 0.3319        
REMARK   3    25  1.8959 -  1.8703    1.00     6033   314  0.2946 0.3264        
REMARK   3    26  1.8703 -  1.8460    1.00     6025   335  0.3147 0.3183        
REMARK   3    27  1.8460 -  1.8229    1.00     6106   302  0.3364 0.3412        
REMARK   3    28  1.8229 -  1.8009    0.98     5910   325  0.3645 0.3782        
REMARK   3    29  1.8009 -  1.7800    0.95     5767   309  0.4010 0.4186        
REMARK   3    30  1.7800 -  1.7600    0.91     5498   283  0.4323 0.4101        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          13817                                  
REMARK   3   ANGLE     :  0.989          18838                                  
REMARK   3   CHIRALITY :  0.057           1952                                  
REMARK   3   PLANARITY :  0.006           2414                                  
REMARK   3   DIHEDRAL  : 14.685           8051                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  64.1152  31.7528-185.4689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4660 T22:   0.4984                                     
REMARK   3      T33:   0.4178 T12:   0.1989                                     
REMARK   3      T13:   0.1330 T23:   0.2329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8069 L22:   1.5632                                     
REMARK   3      L33:   1.8844 L12:   0.3099                                     
REMARK   3      L13:  -0.4300 L23:  -0.4917                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2146 S12:   0.3936 S13:   0.2946                       
REMARK   3      S21:   0.0366 S22:   0.2154 S23:   0.3404                       
REMARK   3      S31:  -0.6046 S32:  -0.5913 S33:  -0.1456                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  74.2725   8.5331-157.6460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2254 T22:   0.1905                                     
REMARK   3      T33:   0.2369 T12:  -0.0533                                     
REMARK   3      T13:  -0.0200 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9753 L22:   1.2994                                     
REMARK   3      L33:   2.2637 L12:  -0.1525                                     
REMARK   3      L13:  -0.4720 L23:  -0.6575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0746 S12:  -0.0144 S13:   0.0484                       
REMARK   3      S21:   0.2375 S22:   0.0591 S23:   0.0113                       
REMARK   3      S31:  -0.0999 S32:  -0.0993 S33:  -0.1151                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  92.9342 -34.0559-195.2398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5301 T22:   0.3169                                     
REMARK   3      T33:   0.3344 T12:  -0.0048                                     
REMARK   3      T13:  -0.0354 T23:   0.0766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5747 L22:   1.4792                                     
REMARK   3      L33:   1.3904 L12:   0.0733                                     
REMARK   3      L13:   0.2993 L23:   0.0121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1215 S12:  -0.1959 S13:  -0.1937                       
REMARK   3      S21:   0.1850 S22:  -0.0086 S23:   0.1182                       
REMARK   3      S31:   0.5071 S32:  -0.1639 S33:  -0.0729                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): 103.3264 -10.3973-222.6280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2338 T22:   0.1852                                     
REMARK   3      T33:   0.2433 T12:   0.0496                                     
REMARK   3      T13:  -0.0068 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7935 L22:   0.8182                                     
REMARK   3      L33:   2.3770 L12:   0.2476                                     
REMARK   3      L13:   0.2468 L23:  -0.0655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0238 S12:   0.0276 S13:  -0.0350                       
REMARK   3      S21:  -0.0804 S22:   0.0619 S23:  -0.0355                       
REMARK   3      S31:  -0.0467 S32:   0.1721 S33:  -0.0437                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6PP1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240135.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 191106                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200   FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.04100                            
REMARK 200  R SYM FOR SHELL            (I) : 2.04100                            
REMARK 200   FOR SHELL         : 0.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4D1P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG3350, 0.1M BIS-TRIS 0.2-0.3M   
REMARK 280  MG ACETATE, 0.1M GDCL3 10% GLYCEROL, 5 MM TCEP, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       76.51500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -157.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     SER A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     LYS A    67                                                      
REMARK 465     LYS A   108                                                      
REMARK 465     LEU A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ARG A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ALA A   119                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     LEU B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     PRO B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     HIS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     SER B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     LEU B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     LYS B    67                                                      
REMARK 465     ARG B   107                                                      
REMARK 465     LYS B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     ARG B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     PRO B   118                                                      
REMARK 465     ALA C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     SER C    44                                                      
REMARK 465     LEU C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     PRO C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     PRO C    50                                                      
REMARK 465     GLU C    51                                                      
REMARK 465     HIS C    52                                                      
REMARK 465     SER C    53                                                      
REMARK 465     PRO C    54                                                      
REMARK 465     PRO C    55                                                      
REMARK 465     SER C    56                                                      
REMARK 465     SER C    57                                                      
REMARK 465     PRO C    58                                                      
REMARK 465     LEU C    59                                                      
REMARK 465     THR C    60                                                      
REMARK 465     GLN C    61                                                      
REMARK 465     PRO C    62                                                      
REMARK 465     PRO C    63                                                      
REMARK 465     GLU C    64                                                      
REMARK 465     GLY C    65                                                      
REMARK 465     PRO C    66                                                      
REMARK 465     LYS C    67                                                      
REMARK 465     ARG C   107                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     LEU C   109                                                      
REMARK 465     GLN C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     ARG C   112                                                      
REMARK 465     PRO C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     GLY C   116                                                      
REMARK 465     PRO C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     ALA D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     SER D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     PRO D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     PRO D    50                                                      
REMARK 465     GLU D    51                                                      
REMARK 465     HIS D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     PRO D    54                                                      
REMARK 465     PRO D    55                                                      
REMARK 465     SER D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     PRO D    58                                                      
REMARK 465     LEU D    59                                                      
REMARK 465     THR D    60                                                      
REMARK 465     GLN D    61                                                      
REMARK 465     PRO D    62                                                      
REMARK 465     PRO D    63                                                      
REMARK 465     GLU D    64                                                      
REMARK 465     GLY D    65                                                      
REMARK 465     PRO D    66                                                      
REMARK 465     LYS D    67                                                      
REMARK 465     LYS D   108                                                      
REMARK 465     LEU D   109                                                      
REMARK 465     GLN D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     ARG D   112                                                      
REMARK 465     PRO D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     PRO D   115                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     PRO D   117                                                      
REMARK 465     PRO D   118                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   609     O    HOH C   693              1.99            
REMARK 500   OD1  ASP B   384     O8   BTB C   505              2.06            
REMARK 500   OE2  GLU D   321     O4   BTB D   505              2.14            
REMARK 500   NH2  ARG C   128     OE2  GLU C   154              2.14            
REMARK 500   OE2  GLU A   298     O8   BTB A   506              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  89      -87.37    -94.01                                   
REMARK 500    PRO A 106       92.75    -67.24                                   
REMARK 500    SER A 143      177.83    123.52                                   
REMARK 500    GLN A 144     -130.05     74.06                                   
REMARK 500    THR A 162     -166.01   -127.36                                   
REMARK 500    ARG A 202       38.42   -161.19                                   
REMARK 500    GLN A 256     -157.60   -144.76                                   
REMARK 500    SER A 260      153.04    -44.47                                   
REMARK 500    HIS A 277       13.61   -144.22                                   
REMARK 500    PHE A 286       52.24   -143.02                                   
REMARK 500    ALA A 351       72.74   -155.07                                   
REMARK 500    ARG A 372     -133.76   -111.58                                   
REMARK 500    PRO A 479       46.25    -79.63                                   
REMARK 500    ASN B 283       25.35   -150.01                                   
REMARK 500    ALA B 351       72.02   -156.31                                   
REMARK 500    ARG B 372     -128.30   -117.00                                   
REMARK 500    GLN C  89      -88.99    -72.92                                   
REMARK 500    HIS C 277       45.51    -72.44                                   
REMARK 500    ASN C 283       35.64   -154.12                                   
REMARK 500    ASP C 297      -24.73     88.42                                   
REMARK 500    ALA C 351       68.45   -156.54                                   
REMARK 500    ARG C 372     -133.61   -114.61                                   
REMARK 500    CYS C 441      119.52   -162.33                                   
REMARK 500    ASP D 258        7.87    -68.92                                   
REMARK 500    ASN D 283       25.95   -142.07                                   
REMARK 500    ALA D 351       68.39   -156.35                                   
REMARK 500    ARG D 372     -130.64   -117.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  94   SG                                                     
REMARK 620 2 CYS A  99   SG  110.3                                              
REMARK 620 3 CYS B  94   SG  119.0 108.0                                        
REMARK 620 4 CYS B  99   SG  106.5 105.4 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 184   SG                                                     
REMARK 620 2 HEM A 501   NA  100.3                                              
REMARK 620 3 HEM A 501   NB  100.2  86.7                                        
REMARK 620 4 HEM A 501   NC   95.3 164.5  90.3                                  
REMARK 620 5 HEM A 501   ND   98.2  91.6 161.4  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD A 509  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BTB A 504   O3                                                     
REMARK 620 2 BTB A 504   O4   63.0                                              
REMARK 620 3 BTB A 504   N    68.1  67.1                                        
REMARK 620 4 BTB A 504   O6   86.1 123.1  57.0                                  
REMARK 620 5 BTB A 504   O8  132.9  98.9  64.8  67.6                            
REMARK 620 6 HOH A 616   O    55.2  91.8 122.8 108.8 169.0                      
REMARK 620 7 HOH A 618   O    71.2 132.6 106.9  62.2 121.6  50.3                
REMARK 620 8 HOH A 732   O   138.3 147.0 137.4  87.6  81.0  88.6  69.5          
REMARK 620 9 HOH D 601   O    67.2  57.8 119.9 149.6 141.8  44.2  94.4 102.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD D 509  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 601   O                                                      
REMARK 620 2 THR D 319   O    86.2                                              
REMARK 620 3 GLU D 321   OE1  75.4  70.2                                        
REMARK 620 4 BTB D 505   O3  147.7  81.5 126.7                                  
REMARK 620 5 BTB D 505   O4  127.0  88.5  53.5  82.5                            
REMARK 620 6 BTB D 505   N   137.2 135.2 105.4  65.6  59.0                      
REMARK 620 7 BTB D 505   O6   80.3 158.9 121.0 101.5 112.6  62.5                
REMARK 620 8 BTB D 505   O8   80.8 141.0  71.0 126.0  71.1  60.4  52.4          
REMARK 620 9 HOH D 782   O    76.0  77.4 137.6  72.2 152.5 116.8  83.6 133.2    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 184   SG                                                     
REMARK 620 2 HEM B 502   NA   99.4                                              
REMARK 620 3 HEM B 502   NB  100.4  87.2                                        
REMARK 620 4 HEM B 502   NC   99.6 161.1  89.1                                  
REMARK 620 5 HEM B 502   ND  101.1  89.1 158.5  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD B 510  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 319   O                                                      
REMARK 620 2 GLU B 321   OE1  69.3                                              
REMARK 620 3 BTB B 505   O3   85.6 123.3                                        
REMARK 620 4 BTB B 505   O4   80.8  66.8  59.2                                  
REMARK 620 5 BTB B 505   N   140.7 105.3  64.4  62.5                            
REMARK 620 6 BTB B 505   O6  152.3 125.7 100.1 125.4  63.2                      
REMARK 620 7 BTB B 505   O8  131.6  63.5 129.3  90.0  65.7  63.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD B 511  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 706   O                                                      
REMARK 620 2 BTB C 504   N   120.7                                              
REMARK 620 3 BTB C 504   O3  139.8  70.0                                        
REMARK 620 4 BTB C 504   O4   75.7  67.4  74.2                                  
REMARK 620 5 BTB C 504   O8   81.3  58.4 127.1  94.7                            
REMARK 620 6 BTB C 504   O6  126.6  57.3  92.5 124.2  51.1                      
REMARK 620 7 HOH C 604   O   116.3 121.3  57.8 116.6 146.5  98.5                
REMARK 620 8 HOH C 733   O    72.0 133.7  74.8  74.8 152.9 154.0  55.6          
REMARK 620 9 HOH C 756   O    75.0 142.3 122.3 147.3  95.0  85.5  65.5  82.5    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  94   SG                                                     
REMARK 620 2 CYS C  99   SG  108.1                                              
REMARK 620 3 CYS D  94   SG  119.4 104.8                                        
REMARK 620 4 CYS D  99   SG  105.5 106.2 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 184   SG                                                     
REMARK 620 2 HEM C 501   NA  101.9                                              
REMARK 620 3 HEM C 501   NB  102.1  85.0                                        
REMARK 620 4 HEM C 501   NC   96.1 162.0  90.9                                  
REMARK 620 5 HEM C 501   ND   98.6  90.4 159.4  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 184   SG                                                     
REMARK 620 2 HEM D 502   NA  101.0                                              
REMARK 620 3 HEM D 502   NB   98.7  88.1                                        
REMARK 620 4 HEM D 502   NC   98.5 160.4  87.7                                  
REMARK 620 5 HEM D 502   ND  102.7  87.6 158.5  89.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OU1 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OU1 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 511                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OU1 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OU1 D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD D 509                  
DBREF  6PP1 A   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6PP1 B   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6PP1 C   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6PP1 D   41   480  UNP    P29474   NOS3_HUMAN      41    480             
SEQADV 6PP1 GLU A  298  UNP  P29474    ASP   298 VARIANT                        
SEQADV 6PP1 GLU B  298  UNP  P29474    ASP   298 VARIANT                        
SEQADV 6PP1 GLU C  298  UNP  P29474    ASP   298 VARIANT                        
SEQADV 6PP1 GLU D  298  UNP  P29474    ASP   298 VARIANT                        
SEQRES   1 A  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 A  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 A  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 A  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 A  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 A  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 A  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 A  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 A  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 A  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 A  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 A  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 A  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 A  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 A  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 A  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 A  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 A  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 A  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 A  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 A  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 A  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 A  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 A  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 A  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 A  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 A  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 A  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 A  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 A  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 A  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 A  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 A  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 A  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 B  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 B  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 B  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 B  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 B  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 B  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 B  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 B  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 B  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 B  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 B  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 B  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 B  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 B  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 B  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 B  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 B  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 B  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 B  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 B  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 B  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 B  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 B  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 B  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 B  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 B  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 B  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 B  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 B  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 B  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 B  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 B  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 B  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 B  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 C  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 C  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 C  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 C  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 C  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 C  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 C  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 C  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 C  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 C  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 C  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 C  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 C  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 C  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 C  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 C  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 C  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 C  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 C  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 C  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 C  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 C  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 C  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 C  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 C  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 C  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 C  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 C  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 C  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 C  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 C  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 C  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 C  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 C  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 D  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 D  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 D  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 D  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 D  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 D  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 D  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 D  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 D  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 D  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 D  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 D  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 D  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 D  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 D  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 D  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 D  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 D  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 D  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 D  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 D  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 D  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 D  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 D  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 D  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 D  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 D  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 D  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 D  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 D  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 D  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 D  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 D  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 D  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
HET    HEM  A 501      43                                                       
HET    H4B  A 502      17                                                       
HET    OU1  A 503      25                                                       
HET    BTB  A 504      14                                                       
HET    BTB  A 505      14                                                       
HET    BTB  A 506      14                                                       
HET    GOL  A 507       6                                                       
HET     CL  A 508       1                                                       
HET     GD  A 509       1                                                       
HET     ZN  B 501       1                                                       
HET    HEM  B 502      43                                                       
HET    H4B  B 503      17                                                       
HET    OU1  B 504      25                                                       
HET    BTB  B 505      14                                                       
HET    BTB  B 506      14                                                       
HET    BTB  B 507      14                                                       
HET    GOL  B 508       6                                                       
HET     CL  B 509       1                                                       
HET     GD  B 510       1                                                       
HET     GD  B 511       1                                                       
HET    HEM  C 501      43                                                       
HET    H4B  C 502      17                                                       
HET    OU1  C 503      25                                                       
HET    BTB  C 504      14                                                       
HET    BTB  C 505      14                                                       
HET    BTB  C 506      14                                                       
HET    GOL  C 507       6                                                       
HET     CL  C 508       1                                                       
HET     ZN  D 501       1                                                       
HET    HEM  D 502      43                                                       
HET    H4B  D 503      17                                                       
HET    OU1  D 504      25                                                       
HET    BTB  D 505      14                                                       
HET    BTB  D 506      14                                                       
HET    GOL  D 507       6                                                       
HET     CL  D 508       1                                                       
HET     GD  D 509       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     OU1 7-[3-(AMINOMETHYL)-4-(CYCLOPROPYLMETHOXY)PHENYL]-4-              
HETNAM   2 OU1  METHYLQUINOLIN-2-AMINE                                          
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      GD GADOLINIUM ATOM                                                  
HETNAM      ZN ZINC ION                                                         
HETSYN     HEM HEME                                                             
HETSYN     BTB BIS-TRIS BUFFER                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  H4B    4(C9 H15 N5 O3)                                              
FORMUL   7  OU1    4(C21 H23 N3 O)                                              
FORMUL   8  BTB    11(C8 H19 N O5)                                              
FORMUL  11  GOL    4(C3 H8 O3)                                                  
FORMUL  12   CL    4(CL 1-)                                                     
FORMUL  13   GD    4(GD)                                                        
FORMUL  14   ZN    2(ZN 2+)                                                     
FORMUL  42  HOH   *747(H2 O)                                                    
HELIX    1 AA1 THR A   83  ALA A   88  5                                   6    
HELIX    2 AA2 GLU A  121  ILE A  138  1                                  18    
HELIX    3 AA3 GLN A  144  GLY A  161  1                                  18    
HELIX    4 AA4 ARG A  166  ASN A  180  1                                  15    
HELIX    5 AA5 GLY A  186  TRP A  190  5                                   5    
HELIX    6 AA6 SER A  203  ASN A  220  1                                  18    
HELIX    7 AA7 ARG A  221  ASN A  223  5                                   3    
HELIX    8 AA8 ASN A  267  GLN A  276  1                                  10    
HELIX    9 AA9 PRO A  306  VAL A  310  5                                   5    
HELIX   10 AB1 LEU A  320  GLY A  327  5                                   8    
HELIX   11 AB2 SER A  359  THR A  364  1                                   6    
HELIX   12 AB3 THR A  364  ASP A  369  1                                   6    
HELIX   13 AB4 ILE A  375  MET A  383  1                                   9    
HELIX   14 AB5 THR A  389  SER A  392  5                                   4    
HELIX   15 AB6 LEU A  393  ALA A  413  1                                  21    
HELIX   16 AB7 ASP A  419  GLY A  439  1                                  21    
HELIX   17 AB8 ASP A  444  VAL A  449  1                                   6    
HELIX   18 AB9 SER A  453  GLN A  462  5                                  10    
HELIX   19 AC1 THR B   83  ALA B   88  5                                   6    
HELIX   20 AC2 PRO B  120  ILE B  138  1                                  19    
HELIX   21 AC3 SER B  143  GLY B  161  1                                  19    
HELIX   22 AC4 ARG B  166  ASN B  180  1                                  15    
HELIX   23 AC5 GLY B  186  TRP B  190  5                                   5    
HELIX   24 AC6 SER B  203  ASN B  220  1                                  18    
HELIX   25 AC7 ARG B  221  ASN B  223  5                                   3    
HELIX   26 AC8 ASN B  267  HIS B  277  1                                  11    
HELIX   27 AC9 PRO B  306  VAL B  310  5                                   5    
HELIX   28 AD1 LEU B  320  GLY B  327  5                                   8    
HELIX   29 AD2 SER B  359  THR B  364  1                                   6    
HELIX   30 AD3 THR B  364  ASP B  369  1                                   6    
HELIX   31 AD4 ILE B  375  MET B  383  1                                   9    
HELIX   32 AD5 THR B  389  SER B  392  5                                   4    
HELIX   33 AD6 LEU B  393  LYS B  414  1                                  22    
HELIX   34 AD7 ASP B  419  GLY B  439  1                                  21    
HELIX   35 AD8 ASP B  444  VAL B  449  1                                   6    
HELIX   36 AD9 SER B  453  GLN B  462  5                                  10    
HELIX   37 AE1 THR C   83  ALA C   88  5                                   6    
HELIX   38 AE2 PRO C  120  ILE C  138  1                                  19    
HELIX   39 AE3 SER C  143  GLY C  161  1                                  19    
HELIX   40 AE4 ARG C  166  ASN C  180  1                                  15    
HELIX   41 AE5 GLY C  186  TRP C  190  5                                   5    
HELIX   42 AE6 SER C  203  ASN C  220  1                                  18    
HELIX   43 AE7 ARG C  221  ASN C  223  5                                   3    
HELIX   44 AE8 ASN C  267  HIS C  277  1                                  11    
HELIX   45 AE9 PRO C  306  VAL C  310  5                                   5    
HELIX   46 AF1 LEU C  320  GLY C  327  5                                   8    
HELIX   47 AF2 SER C  359  THR C  364  1                                   6    
HELIX   48 AF3 THR C  364  ASP C  369  1                                   6    
HELIX   49 AF4 ILE C  375  MET C  383  1                                   9    
HELIX   50 AF5 THR C  389  SER C  392  5                                   4    
HELIX   51 AF6 LEU C  393  ALA C  413  1                                  21    
HELIX   52 AF7 ASP C  419  GLY C  439  1                                  21    
HELIX   53 AF8 ASP C  444  VAL C  449  1                                   6    
HELIX   54 AF9 SER C  453  GLN C  462  5                                  10    
HELIX   55 AG1 THR D   83  ALA D   88  5                                   6    
HELIX   56 AG2 PRO D  120  ILE D  138  1                                  19    
HELIX   57 AG3 SER D  143  GLY D  161  1                                  19    
HELIX   58 AG4 ARG D  166  ASN D  180  1                                  15    
HELIX   59 AG5 GLY D  186  TRP D  190  5                                   5    
HELIX   60 AG6 SER D  203  ASN D  220  1                                  18    
HELIX   61 AG7 ARG D  221  ASN D  223  5                                   3    
HELIX   62 AG8 ASN D  267  HIS D  277  1                                  11    
HELIX   63 AG9 PRO D  306  VAL D  310  5                                   5    
HELIX   64 AH1 LEU D  320  GLY D  327  5                                   8    
HELIX   65 AH2 SER D  359  THR D  364  1                                   6    
HELIX   66 AH3 THR D  364  ASP D  369  1                                   6    
HELIX   67 AH4 ILE D  375  MET D  383  1                                   9    
HELIX   68 AH5 THR D  389  SER D  392  5                                   4    
HELIX   69 AH6 LEU D  393  LYS D  414  1                                  22    
HELIX   70 AH7 ASP D  419  GLY D  439  1                                  21    
HELIX   71 AH8 ASP D  444  VAL D  449  1                                   6    
HELIX   72 AH9 SER D  453  GLN D  462  5                                  10    
SHEET    1 AA1 2 ARG A  70  LYS A  72  0                                        
SHEET    2 AA1 2 ILE A  79  TYR A  81 -1  O  THR A  80   N  VAL A  71           
SHEET    1 AA2 4 GLN A 194  ASP A 197  0                                        
SHEET    2 AA2 4 ALA A 227  VAL A 230  1  O  ILE A 228   N  PHE A 196           
SHEET    3 AA2 4 PHE A 353  SER A 354 -1  O  SER A 354   N  ALA A 227           
SHEET    4 AA2 4 ALA A 335  VAL A 336 -1  N  VAL A 336   O  PHE A 353           
SHEET    1 AA3 3 ARG A 242  ILE A 243  0                                        
SHEET    2 AA3 3 LEU A 291  GLN A 294 -1  O  GLN A 294   N  ARG A 242           
SHEET    3 AA3 3 GLU A 301  PHE A 303 -1  O  PHE A 303   N  LEU A 291           
SHEET    1 AA4 2 GLY A 253  TYR A 254  0                                        
SHEET    2 AA4 2 ARG A 262  GLY A 263 -1  O  ARG A 262   N  TYR A 254           
SHEET    1 AA5 2 GLU A 312  PRO A 314  0                                        
SHEET    2 AA5 2 ARG A 329  TYR A 331 -1  O  TRP A 330   N  VAL A 313           
SHEET    1 AA6 3 LEU A 346  PHE A 348  0                                        
SHEET    2 AA6 3 LEU A 340  ILE A 343 -1  N  LEU A 341   O  PHE A 348           
SHEET    3 AA6 3 ALA A 472  ARG A 474 -1  O  ARG A 474   N  LEU A 340           
SHEET    1 AA7 2 TYR A 357  MET A 358  0                                        
SHEET    2 AA7 2 ILE A 417  VAL A 418  1  O  VAL A 418   N  TYR A 357           
SHEET    1 AA8 2 ARG B  70  LYS B  72  0                                        
SHEET    2 AA8 2 ILE B  79  TYR B  81 -1  O  THR B  80   N  VAL B  71           
SHEET    1 AA9 4 GLN B 194  ASP B 197  0                                        
SHEET    2 AA9 4 ALA B 227  VAL B 230  1  O  ILE B 228   N  PHE B 196           
SHEET    3 AA9 4 PHE B 353  SER B 354 -1  O  SER B 354   N  ALA B 227           
SHEET    4 AA9 4 ALA B 335  VAL B 336 -1  N  VAL B 336   O  PHE B 353           
SHEET    1 AB1 3 ARG B 242  ILE B 243  0                                        
SHEET    2 AB1 3 LEU B 291  GLN B 294 -1  O  GLN B 294   N  ARG B 242           
SHEET    3 AB1 3 GLU B 301  PHE B 303 -1  O  PHE B 303   N  LEU B 291           
SHEET    1 AB2 2 GLY B 253  TYR B 254  0                                        
SHEET    2 AB2 2 ARG B 262  GLY B 263 -1  O  ARG B 262   N  TYR B 254           
SHEET    1 AB3 2 GLU B 312  PRO B 314  0                                        
SHEET    2 AB3 2 ARG B 329  TYR B 331 -1  O  TRP B 330   N  VAL B 313           
SHEET    1 AB4 3 LEU B 346  PHE B 348  0                                        
SHEET    2 AB4 3 LEU B 340  ILE B 343 -1  N  LEU B 341   O  PHE B 348           
SHEET    3 AB4 3 ALA B 472  ARG B 474 -1  O  ARG B 474   N  LEU B 340           
SHEET    1 AB5 2 TYR B 357  MET B 358  0                                        
SHEET    2 AB5 2 ILE B 417  VAL B 418  1  O  VAL B 418   N  TYR B 357           
SHEET    1 AB6 2 ARG C  70  LYS C  72  0                                        
SHEET    2 AB6 2 ILE C  79  TYR C  81 -1  O  THR C  80   N  VAL C  71           
SHEET    1 AB7 4 GLN C 194  ASP C 197  0                                        
SHEET    2 AB7 4 ALA C 227  VAL C 230  1  O  ILE C 228   N  PHE C 196           
SHEET    3 AB7 4 PHE C 353  SER C 354 -1  O  SER C 354   N  ALA C 227           
SHEET    4 AB7 4 ALA C 335  VAL C 336 -1  N  VAL C 336   O  PHE C 353           
SHEET    1 AB8 3 ARG C 242  ILE C 243  0                                        
SHEET    2 AB8 3 LEU C 291  GLN C 294 -1  O  GLN C 294   N  ARG C 242           
SHEET    3 AB8 3 GLU C 301  PHE C 303 -1  O  PHE C 303   N  LEU C 291           
SHEET    1 AB9 2 GLY C 253  ARG C 255  0                                        
SHEET    2 AB9 2 VAL C 261  GLY C 263 -1  O  ARG C 262   N  TYR C 254           
SHEET    1 AC1 2 GLU C 312  PRO C 314  0                                        
SHEET    2 AC1 2 ARG C 329  TYR C 331 -1  O  TRP C 330   N  VAL C 313           
SHEET    1 AC2 3 LEU C 346  PHE C 348  0                                        
SHEET    2 AC2 3 LEU C 340  ILE C 343 -1  N  LEU C 341   O  PHE C 348           
SHEET    3 AC2 3 ALA C 472  ARG C 474 -1  O  ARG C 474   N  LEU C 340           
SHEET    1 AC3 2 TYR C 357  MET C 358  0                                        
SHEET    2 AC3 2 ILE C 417  VAL C 418  1  O  VAL C 418   N  TYR C 357           
SHEET    1 AC4 2 ARG D  70  LYS D  72  0                                        
SHEET    2 AC4 2 ILE D  79  TYR D  81 -1  O  THR D  80   N  VAL D  71           
SHEET    1 AC5 4 GLN D 194  ASP D 197  0                                        
SHEET    2 AC5 4 ALA D 227  VAL D 230  1  O  ILE D 228   N  PHE D 196           
SHEET    3 AC5 4 PHE D 353  SER D 354 -1  O  SER D 354   N  ALA D 227           
SHEET    4 AC5 4 ALA D 335  VAL D 336 -1  N  VAL D 336   O  PHE D 353           
SHEET    1 AC6 3 ARG D 242  ILE D 243  0                                        
SHEET    2 AC6 3 LEU D 291  GLN D 294 -1  O  GLN D 294   N  ARG D 242           
SHEET    3 AC6 3 GLU D 301  PHE D 303 -1  O  PHE D 303   N  LEU D 291           
SHEET    1 AC7 2 GLY D 253  ARG D 255  0                                        
SHEET    2 AC7 2 VAL D 261  GLY D 263 -1  O  ARG D 262   N  TYR D 254           
SHEET    1 AC8 2 GLU D 312  PRO D 314  0                                        
SHEET    2 AC8 2 ARG D 329  TYR D 331 -1  O  TRP D 330   N  VAL D 313           
SHEET    1 AC9 3 LEU D 346  PHE D 348  0                                        
SHEET    2 AC9 3 LEU D 340  ILE D 343 -1  N  LEU D 341   O  PHE D 348           
SHEET    3 AC9 3 ALA D 472  ARG D 474 -1  O  ARG D 474   N  LEU D 340           
SHEET    1 AD1 2 TYR D 357  MET D 358  0                                        
SHEET    2 AD1 2 ILE D 417  VAL D 418  1  O  VAL D 418   N  TYR D 357           
LINK         SG  CYS A  94                ZN    ZN B 501     1555   1555  2.32  
LINK         SG  CYS A  99                ZN    ZN B 501     1555   1555  2.31  
LINK         SG  CYS A 184                FE   HEM A 501     1555   1555  2.32  
LINK         O3  BTB A 504                GD    GD A 509     1555   1555  2.64  
LINK         O4  BTB A 504                GD    GD A 509     1555   1555  2.72  
LINK         N   BTB A 504                GD    GD A 509     1555   1555  2.83  
LINK         O6  BTB A 504                GD    GD A 509     1555   1555  2.73  
LINK         O8  BTB A 504                GD    GD A 509     1555   1555  2.82  
LINK        GD    GD A 509                 O   HOH A 616     1555   1555  2.76  
LINK        GD    GD A 509                 O   HOH A 618     1555   1555  2.78  
LINK        GD    GD A 509                 O   HOH A 732     1555   1555  2.78  
LINK        GD    GD A 509                 O   HOH D 601     1555   1455  3.12  
LINK        GD    GD A 509                 O   HOH D 804     1555   1455  3.02  
LINK         O   HOH A 601                GD    GD D 509     1655   1555  2.68  
LINK         SG  CYS B  94                ZN    ZN B 501     1555   1555  2.40  
LINK         SG  CYS B  99                ZN    ZN B 501     1555   1555  2.36  
LINK         SG  CYS B 184                FE   HEM B 502     1555   1555  2.31  
LINK         O   THR B 319                GD    GD B 510     1555   1555  2.39  
LINK         OE1 GLU B 321                GD    GD B 510     1555   1555  2.66  
LINK         O3  BTB B 505                GD    GD B 510     1555   1555  2.61  
LINK         O4  BTB B 505                GD    GD B 510     1555   1555  2.66  
LINK         N   BTB B 505                GD    GD B 510     1555   1555  2.76  
LINK         O6  BTB B 505                GD    GD B 510     1555   1555  2.74  
LINK         O8  BTB B 505                GD    GD B 510     1555   1555  2.68  
LINK        GD    GD B 511                 O   HOH B 706     1555   1555  2.78  
LINK        GD    GD B 511                 N   BTB C 504     1555   1555  2.85  
LINK        GD    GD B 511                 O3  BTB C 504     1555   1555  2.32  
LINK        GD    GD B 511                 O4  BTB C 504     1555   1555  2.73  
LINK        GD    GD B 511                 O8  BTB C 504     1555   1555  2.79  
LINK        GD    GD B 511                 O6  BTB C 504     1555   1555  2.81  
LINK        GD    GD B 511                 O   HOH C 604     1555   1555  2.73  
LINK        GD    GD B 511                 O   HOH C 733     1555   1555  2.77  
LINK        GD    GD B 511                 O   HOH C 756     1555   1555  2.80  
LINK         SG  CYS C  94                ZN    ZN D 501     1555   1555  2.36  
LINK         SG  CYS C  99                ZN    ZN D 501     1555   1555  2.29  
LINK         SG  CYS C 184                FE   HEM C 501     1555   1555  2.40  
LINK         SG  CYS D  94                ZN    ZN D 501     1555   1555  2.42  
LINK         SG  CYS D  99                ZN    ZN D 501     1555   1555  2.36  
LINK         SG  CYS D 184                FE   HEM D 502     1555   1555  2.27  
LINK         O   THR D 319                GD    GD D 509     1555   1555  2.34  
LINK         OE1 GLU D 321                GD    GD D 509     1555   1555  2.71  
LINK         O3  BTB D 505                GD    GD D 509     1555   1555  2.67  
LINK         O4  BTB D 505                GD    GD D 509     1555   1555  2.71  
LINK         N   BTB D 505                GD    GD D 509     1555   1555  2.75  
LINK         O6  BTB D 505                GD    GD D 509     1555   1555  2.67  
LINK         O8  BTB D 505                GD    GD D 509     1555   1555  2.76  
LINK        GD    GD D 509                 O   HOH D 782     1555   1555  2.68  
CISPEP   1 SER A  470    PRO A  471          0         0.38                     
CISPEP   2 GLN B  257    ASP B  258          0        24.66                     
CISPEP   3 SER B  470    PRO B  471          0        -0.52                     
CISPEP   4 SER C  470    PRO C  471          0        -3.87                     
CISPEP   5 SER D  470    PRO D  471          0         0.16                     
SITE     1 AC1 17 TRP A 178  ALA A 181  PRO A 182  ARG A 183                    
SITE     2 AC1 17 CYS A 184  SER A 226  PHE A 353  SER A 354                    
SITE     3 AC1 17 TRP A 356  MET A 358  GLU A 361  TRP A 447                    
SITE     4 AC1 17 PHE A 473  TYR A 475  H4B A 502  OU1 A 503                    
SITE     5 AC1 17 HOH A 617                                                     
SITE     1 AC2 14 SER A 102  ARG A 365  ALA A 446  TRP A 447                    
SITE     2 AC2 14 HEM A 501  OU1 A 503  GOL A 507  HOH A 604                    
SITE     3 AC2 14 HOH A 631  HOH A 658  TRP B 445  PHE B 460                    
SITE     4 AC2 14 GLN B 462  GLU B 463                                          
SITE     1 AC3 10 PHE A 105  VAL A 336  PHE A 353  TRP A 356                    
SITE     2 AC3 10 TYR A 357  GLU A 361  TRP A 447  HEM A 501                    
SITE     3 AC3 10 H4B A 502  GOL A 507                                          
SITE     1 AC4 13 TRP A 322  VAL A 381  CYS A 382  ASP A 384                    
SITE     2 AC4 13  GD A 509  HOH A 616  HOH A 618  TRP D 322                    
SITE     3 AC4 13 ALA D 325  LEU D 326  ASP D 378  CYS D 382                    
SITE     4 AC4 13 HOH D 601                                                     
SITE     1 AC5  4 GLU A 377  THR A 387  ARG A 388  ASP D 384                    
SITE     1 AC6  1 GLU A 298                                                     
SITE     1 AC7  5 ARG A 365  HIS A 371  H4B A 502  OU1 A 503                    
SITE     2 AC7  5 HOH A 631                                                     
SITE     1 AC8  4 GLN A 247  TYR A 357  ASN A 366  HOH A 610                    
SITE     1 AC9  5 BTB A 504  HOH A 616  HOH A 618  HOH A 732                    
SITE     2 AC9  5 HOH D 804                                                     
SITE     1 AD1  4 CYS A  94  CYS A  99  CYS B  94  CYS B  99                    
SITE     1 AD2 17 TRP B 178  PRO B 182  ARG B 183  CYS B 184                    
SITE     2 AD2 17 SER B 226  PHE B 353  SER B 354  TRP B 356                    
SITE     3 AD2 17 GLU B 361  PHE B 473  TYR B 475  H4B B 503                    
SITE     4 AD2 17 OU1 B 504  HOH B 616  HOH B 635  HOH B 727                    
SITE     5 AD2 17 HOH B 731                                                     
SITE     1 AD3 13 TRP A 445  PHE A 460  GLU A 463  SER B 102                    
SITE     2 AD3 13 ARG B 365  ALA B 446  TRP B 447  HEM B 502                    
SITE     3 AD3 13 OU1 B 504  GOL B 508  HOH B 606  HOH B 620                    
SITE     4 AD3 13 HOH B 680                                                     
SITE     1 AD4 11 PHE B 105  VAL B 336  PHE B 353  TRP B 356                    
SITE     2 AD4 11 TYR B 357  GLU B 361  TRP B 447  TYR B 475                    
SITE     3 AD4 11 HEM B 502  H4B B 503  GOL B 508                               
SITE     1 AD5  8 THR B 319  GLU B 321   GD B 510  SER C 260                    
SITE     2 AD5  8 VAL C 261  TYR C 373  ASN C 374  ASP C 378                    
SITE     1 AD6  2 GLU B 298  GLU D 167                                          
SITE     1 AD7  1 GLU B 377                                                     
SITE     1 AD8  6 ARG B 365  HIS B 371  TRP B 447  H4B B 503                    
SITE     2 AD8  6 OU1 B 504  HOH B 620                                          
SITE     1 AD9  4 GLN B 247  TYR B 357  ASN B 366  HOH B 679                    
SITE     1 AE1  3 THR B 319  GLU B 321  BTB B 505                               
SITE     1 AE2  5 HOH B 706  BTB C 504  HOH C 604  HOH C 733                    
SITE     2 AE2  5 HOH C 756                                                     
SITE     1 AE3 16 TRP C 178  PRO C 182  ARG C 183  CYS C 184                    
SITE     2 AE3 16 SER C 226  PHE C 353  SER C 354  TRP C 356                    
SITE     3 AE3 16 MET C 358  GLU C 361  TRP C 447  TYR C 475                    
SITE     4 AE3 16 H4B C 502  OU1 C 503  HOH C 602  HOH C 702                    
SITE     1 AE4 11 SER C 102  ARG C 365  ALA C 446  TRP C 447                    
SITE     2 AE4 11 HEM C 501  OU1 C 503  GOL C 507  HOH C 617                    
SITE     3 AE4 11 HOH C 645  TRP D 445  PHE D 460                               
SITE     1 AE5 11 PHE C 105  VAL C 336  PHE C 353  TRP C 356                    
SITE     2 AE5 11 GLU C 361  TRP C 447  TYR C 475  HEM C 501                    
SITE     3 AE5 11 H4B C 502  GOL C 507  HOH C 704                               
SITE     1 AE6  9 TRP B 322  ALA B 325  LEU B 326  ASP B 378                    
SITE     2 AE6  9  GD B 511  VAL C 381  CYS C 382  ASP C 384                    
SITE     3 AE6  9 HOH C 604                                                     
SITE     1 AE7  3 ASP B 384  GLU C 377  ARG C 388                               
SITE     1 AE8  1 GLU C 298                                                     
SITE     1 AE9  6 ARG C 365  HIS C 371  TRP C 447  H4B C 502                    
SITE     2 AE9  6 OU1 C 503  HOH C 617                                          
SITE     1 AF1  3 GLN C 247  TYR C 357  ASN C 366                               
SITE     1 AF2  4 CYS C  94  CYS C  99  CYS D  94  CYS D  99                    
SITE     1 AF3 17 TRP D 178  PRO D 182  ARG D 183  CYS D 184                    
SITE     2 AF3 17 SER D 226  PHE D 353  SER D 354  TRP D 356                    
SITE     3 AF3 17 GLU D 361  TRP D 447  PHE D 473  TYR D 475                    
SITE     4 AF3 17 H4B D 503  OU1 D 504  HOH D 648  HOH D 762                    
SITE     5 AF3 17 HOH D 770                                                     
SITE     1 AF4 12 TRP C 445  PHE C 460  SER D 102  ARG D 365                    
SITE     2 AF4 12 ALA D 446  TRP D 447  HEM D 502  OU1 D 504                    
SITE     3 AF4 12 GOL D 507  HOH D 603  HOH D 605  HOH D 685                    
SITE     1 AF5 11 PHE D 105  VAL D 336  PHE D 353  GLY D 355                    
SITE     2 AF5 11 TRP D 356  TYR D 357  GLU D 361  TRP D 447                    
SITE     3 AF5 11 HEM D 502  H4B D 503  GOL D 507                               
SITE     1 AF6  5 ASN A 374  ASP A 378  THR D 319  GLU D 321                    
SITE     2 AF6  5  GD D 509                                                     
SITE     1 AF7  2 ASP D 297  GLU D 298                                          
SITE     1 AF8  6 ARG D 365  HIS D 371  TRP D 447  H4B D 503                    
SITE     2 AF8  6 OU1 D 504  HOH D 603                                          
SITE     1 AF9  4 GLN D 247  TYR D 357  ASN D 366  HOH D 776                    
SITE     1 AG1  5 HOH A 601  THR D 319  GLU D 321  BTB D 505                    
SITE     2 AG1  5 HOH D 782                                                     
CRYST1   59.585  153.030  108.781  90.00  90.78  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016783  0.000000  0.000227        0.00000                         
SCALE2      0.000000  0.006535  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009194        0.00000                         
ATOM      1  N   PHE A  68      76.751  38.409-158.997  1.00 63.74           N  
ANISOU    1  N   PHE A  68    12552   5169   6497   -463   1946    -29       N  
ATOM      2  CA  PHE A  68      77.358  38.039-160.280  1.00 67.08           C  
ANISOU    2  CA  PHE A  68    12742   5677   7069   -478   1826      9       C  
ATOM      3  C   PHE A  68      77.640  36.532-160.390  1.00 64.56           C  
ANISOU    3  C   PHE A  68    12213   5478   6840   -524   1628     26       C  
ATOM      4  O   PHE A  68      78.624  36.037-159.838  1.00 70.12           O  
ANISOU    4  O   PHE A  68    12927   6203   7513   -719   1445    -34       O  
ATOM      5  CB  PHE A  68      78.640  38.834-160.487  1.00 70.09           C  
ANISOU    5  CB  PHE A  68    13196   6011   7422   -677   1750    -51       C  
ATOM      6  CG  PHE A  68      78.406  40.304-160.654  1.00 73.60           C  
ANISOU    6  CG  PHE A  68    13823   6342   7802   -624   1943    -55       C  
ATOM      7  CD1 PHE A  68      79.229  41.229-160.041  1.00 75.98           C  
ANISOU    7  CD1 PHE A  68    14335   6551   7981   -810   1936   -130       C  
ATOM      8  CD2 PHE A  68      77.349  40.757-161.426  1.00 71.91           C  
ANISOU    8  CD2 PHE A  68    13563   6115   7643   -389   2129     24       C  
ATOM      9  CE1 PHE A  68      79.003  42.585-160.201  1.00 79.38           C  
ANISOU    9  CE1 PHE A  68    14946   6867   8348   -762   2121   -131       C  
ATOM     10  CE2 PHE A  68      77.118  42.107-161.590  1.00 79.48           C  
ANISOU   10  CE2 PHE A  68    14691   6964   8542   -331   2309     27       C  
ATOM     11  CZ  PHE A  68      77.945  43.024-160.979  1.00 77.92           C  
ANISOU   11  CZ  PHE A  68    14719   6663   8222   -518   2310    -54       C  
ATOM     12  N   PRO A  69      76.788  35.816-161.125  1.00 60.45           N  
ANISOU   12  N   PRO A  69    11500   5040   6429   -344   1663    115       N  
ATOM     13  CA  PRO A  69      76.869  34.349-161.142  1.00 59.10           C  
ANISOU   13  CA  PRO A  69    11151   4975   6329   -367   1500    140       C  
ATOM     14  C   PRO A  69      78.202  33.858-161.685  1.00 50.21           C  
ANISOU   14  C   PRO A  69     9902   3902   5275   -542   1294    111       C  
ATOM     15  O   PRO A  69      78.685  34.331-162.717  1.00 53.62           O  
ANISOU   15  O   PRO A  69    10257   4342   5774   -551   1301    129       O  
ATOM     16  CB  PRO A  69      75.710  33.939-162.058  1.00 57.53           C  
ANISOU   16  CB  PRO A  69    10768   4858   6233   -137   1600    255       C  
ATOM     17  CG  PRO A  69      74.822  35.118-162.131  1.00 61.74           C  
ANISOU   17  CG  PRO A  69    11411   5321   6727     20   1825    283       C  
ATOM     18  CD  PRO A  69      75.719  36.313-162.007  1.00 63.99           C  
ANISOU   18  CD  PRO A  69    11876   5499   6940   -113   1845    206       C  
ATOM     19  N   ARG A  70      78.793  32.903-160.974  1.00 52.36           N  
ANISOU   19  N   ARG A  70    10143   4221   5528   -676   1111     66       N  
ATOM     20  CA  ARG A  70      80.008  32.243-161.428  1.00 52.27           C  
ANISOU   20  CA  ARG A  70     9926   4339   5595   -812    892     36       C  
ATOM     21  C   ARG A  70      79.647  31.128-162.411  1.00 52.74           C  
ANISOU   21  C   ARG A  70     9663   4590   5786   -675    826     99       C  
ATOM     22  O   ARG A  70      78.714  30.354-162.172  1.00 51.49           O  
ANISOU   22  O   ARG A  70     9436   4495   5634   -554    846    138       O  
ATOM     23  CB  ARG A  70      80.782  31.688-160.231  1.00 53.27           C  
ANISOU   23  CB  ARG A  70    10127   4469   5646   -996    712    -32       C  
ATOM     24  CG  ARG A  70      82.045  30.932-160.595  1.00 58.14           C  
ANISOU   24  CG  ARG A  70    10518   5225   6348  -1125    480    -54       C  
ATOM     25  CD  ARG A  70      82.621  30.157-159.412  1.00 64.28           C  
ANISOU   25  CD  ARG A  70    11331   6034   7059  -1264    292    -96       C  
ATOM     26  NE  ARG A  70      83.033  28.811-159.814  1.00 79.71           N  
ANISOU   26  NE  ARG A  70    12992   8166   9126  -1237    114    -70       N  
ATOM     27  CZ  ARG A  70      83.701  27.958-159.041  1.00 82.85           C  
ANISOU   27  CZ  ARG A  70    13347   8628   9505  -1342    -82    -90       C  
ATOM     28  NH1 ARG A  70      84.048  28.302-157.807  1.00 92.43           N  
ANISOU   28  NH1 ARG A  70    14787   9752  10582  -1495   -140   -135       N  
ATOM     29  NH2 ARG A  70      84.025  26.757-159.507  1.00 75.84           N  
ANISOU   29  NH2 ARG A  70    12197   7889   8730  -1293   -219    -61       N  
ATOM     30  N   VAL A  71      80.398  31.042-163.508  1.00 48.24           N  
ANISOU   30  N   VAL A  71     8903   4110   5315   -703    751    105       N  
ATOM     31  CA  VAL A  71      80.081  30.184-164.650  1.00 48.36           C  
ANISOU   31  CA  VAL A  71     8636   4289   5448   -575    715    161       C  
ATOM     32  C   VAL A  71      81.322  29.370-164.990  1.00 42.05           C  
ANISOU   32  C   VAL A  71     7639   3610   4727   -694    513    124       C  
ATOM     33  O   VAL A  71      82.377  29.945-165.279  1.00 47.97           O  
ANISOU   33  O   VAL A  71     8398   4335   5492   -821    472     90       O  
ATOM     34  CB  VAL A  71      79.642  31.015-165.868  1.00 55.81           C  
ANISOU   34  CB  VAL A  71     9551   5219   6436   -456    867    221       C  
ATOM     35  CG1 VAL A  71      79.581  30.164-167.098  1.00 47.35           C  
ANISOU   35  CG1 VAL A  71     8198   4319   5473   -369    803    264       C  
ATOM     36  CG2 VAL A  71      78.310  31.701-165.605  1.00 62.27           C  
ANISOU   36  CG2 VAL A  71    10526   5938   7194   -301   1071    277       C  
ATOM     37  N   LYS A  72      81.201  28.046-164.972  1.00 40.20           N  
ANISOU   37  N   LYS A  72     7226   3503   4545   -651    395    134       N  
ATOM     38  CA  LYS A  72      82.338  27.160-165.188  1.00 40.81           C  
ANISOU   38  CA  LYS A  72     7118   3689   4699   -744    206    103       C  
ATOM     39  C   LYS A  72      82.169  26.359-166.472  1.00 42.96           C  
ANISOU   39  C   LYS A  72     7139   4101   5082   -631    190    140       C  
ATOM     40  O   LYS A  72      81.067  25.896-166.787  1.00 42.11           O  
ANISOU   40  O   LYS A  72     6977   4039   4985   -492    254    185       O  
ATOM     41  CB  LYS A  72      82.514  26.194-164.013  1.00 42.69           C  
ANISOU   41  CB  LYS A  72     7372   3947   4900   -805     63     78       C  
ATOM     42  CG  LYS A  72      83.603  25.139-164.211  1.00 45.38           C  
ANISOU   42  CG  LYS A  72     7506   4406   5330   -870   -131     61       C  
ATOM     43  CD  LYS A  72      84.097  24.605-162.860  1.00 51.85           C  
ANISOU   43  CD  LYS A  72     8406   5207   6087   -981   -282     34       C  
ATOM     44  CE  LYS A  72      84.994  23.378-163.015  1.00 56.17           C  
ANISOU   44  CE  LYS A  72     8736   5876   6731  -1003   -468     34       C  
ATOM     45  NZ  LYS A  72      85.525  22.901-161.703  1.00 60.37           N  
ANISOU   45  NZ  LYS A  72     9346   6394   7198  -1112   -626     20       N  
ATOM     46  N   ASN A  73      83.266  26.196-167.210  1.00 40.48           N  
ANISOU   46  N   ASN A  73     6676   3858   4848   -697    106    120       N  
ATOM     47  CA  ASN A  73      83.353  25.209-168.280  1.00 41.00           C  
ANISOU   47  CA  ASN A  73     6505   4060   5015   -618     55    137       C  
ATOM     48  C   ASN A  73      84.044  23.969-167.730  1.00 43.16           C  
ANISOU   48  C   ASN A  73     6665   4402   5331   -670   -122    109       C  
ATOM     49  O   ASN A  73      85.206  24.038-167.317  1.00 44.73           O  
ANISOU   49  O   ASN A  73     6850   4599   5546   -797   -228     75       O  
ATOM     50  CB  ASN A  73      84.120  25.740-169.487  1.00 39.40           C  
ANISOU   50  CB  ASN A  73     6202   3893   4875   -644     89    136       C  
ATOM     51  CG  ASN A  73      84.187  24.722-170.605  1.00 40.18           C  
ANISOU   51  CG  ASN A  73     6077   4125   5065   -561     50    148       C  
ATOM     52  OD1 ASN A  73      84.894  23.724-170.504  1.00 45.27           O  
ANISOU   52  OD1 ASN A  73     6590   4840   5770   -592    -77    122       O  
ATOM     53  ND2 ASN A  73      83.435  24.966-171.679  1.00 42.30           N  
ANISOU   53  ND2 ASN A  73     6309   4425   5338   -451    161    190       N  
ATOM     54  N   TRP A  74      83.341  22.839-167.750  1.00 39.06           N  
ANISOU   54  N   TRP A  74     6061   3945   4833   -573   -154    128       N  
ATOM     55  CA  TRP A  74      83.801  21.620-167.094  1.00 38.74           C  
ANISOU   55  CA  TRP A  74     5947   3950   4822   -603   -310    112       C  
ATOM     56  C   TRP A  74      84.750  20.795-167.943  1.00 45.07           C  
ANISOU   56  C   TRP A  74     6535   4851   5737   -599   -401     98       C  
ATOM     57  O   TRP A  74      85.355  19.847-167.430  1.00 41.72           O  
ANISOU   57  O   TRP A  74     6043   4460   5349   -626   -537     88       O  
ATOM     58  CB  TRP A  74      82.590  20.773-166.677  1.00 41.28           C  
ANISOU   58  CB  TRP A  74     6292   4280   5112   -509   -294    139       C  
ATOM     59  CG  TRP A  74      81.923  21.410-165.521  1.00 37.56           C  
ANISOU   59  CG  TRP A  74     6033   3707   4530   -535   -233    146       C  
ATOM     60  CD1 TRP A  74      80.947  22.363-165.558  1.00 42.52           C  
ANISOU   60  CD1 TRP A  74     6786   4273   5096   -477    -72    172       C  
ATOM     61  CD2 TRP A  74      82.243  21.214-164.136  1.00 42.88           C  
ANISOU   61  CD2 TRP A  74     6835   4325   5134   -626   -327    126       C  
ATOM     62  NE1 TRP A  74      80.616  22.751-164.272  1.00 42.85           N  
ANISOU   62  NE1 TRP A  74     7031   4216   5035   -523    -46    164       N  
ATOM     63  CE2 TRP A  74      81.397  22.058-163.387  1.00 45.04           C  
ANISOU   63  CE2 TRP A  74     7318   4498   5299   -622   -205    134       C  
ATOM     64  CE3 TRP A  74      83.144  20.385-163.457  1.00 51.16           C  
ANISOU   64  CE3 TRP A  74     7841   5399   6198   -704   -501    109       C  
ATOM     65  CZ2 TRP A  74      81.427  22.101-161.992  1.00 49.43           C  
ANISOU   65  CZ2 TRP A  74     8055   4976   5751   -703   -249    117       C  
ATOM     66  CZ3 TRP A  74      83.172  20.431-162.072  1.00 55.24           C  
ANISOU   66  CZ3 TRP A  74     8530   5846   6613   -786   -558    100       C  
ATOM     67  CH2 TRP A  74      82.320  21.284-161.356  1.00 51.45           C  
ANISOU   67  CH2 TRP A  74     8270   5265   6015   -790   -432    100       C  
ATOM     68  N   GLU A  75      84.885  21.122-169.228  1.00 46.95           N  
ANISOU   68  N   GLU A  75     6673   5136   6028   -558   -325    102       N  
ATOM     69  CA  GLU A  75      85.841  20.426-170.077  1.00 42.06           C  
ANISOU   69  CA  GLU A  75     5861   4606   5512   -554   -390     86       C  
ATOM     70  C   GLU A  75      87.245  20.985-169.880  1.00 47.78           C  
ANISOU   70  C   GLU A  75     6554   5329   6272   -681   -454     63       C  
ATOM     71  O   GLU A  75      88.215  20.228-169.792  1.00 48.25           O  
ANISOU   71  O   GLU A  75     6480   5445   6407   -708   -569     51       O  
ATOM     72  CB  GLU A  75      85.413  20.543-171.541  1.00 41.77           C  
ANISOU   72  CB  GLU A  75     5741   4624   5506   -466   -278    100       C  
ATOM     73  CG  GLU A  75      86.383  19.903-172.492  1.00 46.04           C  
ANISOU   73  CG  GLU A  75     6099   5249   6145   -457   -317     79       C  
ATOM     74  CD  GLU A  75      86.046  20.133-173.959  1.00 51.25           C  
ANISOU   74  CD  GLU A  75     6696   5961   6817   -388   -204     90       C  
ATOM     75  OE1 GLU A  75      84.886  20.482-174.286  1.00 45.64           O  
ANISOU   75  OE1 GLU A  75     6057   5238   6045   -321   -115    122       O  
ATOM     76  OE2 GLU A  75      86.965  19.956-174.782  1.00 50.01           O  
ANISOU   76  OE2 GLU A  75     6413   5858   6728   -399   -205     71       O  
ATOM     77  N   VAL A  76      87.360  22.303-169.759  1.00 47.75           N  
ANISOU   77  N   VAL A  76     6672   5255   6214   -761   -382     60       N  
ATOM     78  CA  VAL A  76      88.651  22.973-169.696  1.00 47.31           C  
ANISOU   78  CA  VAL A  76     6586   5199   6188   -900   -428     41       C  
ATOM     79  C   VAL A  76      88.967  23.353-168.252  1.00 52.91           C  
ANISOU   79  C   VAL A  76     7443   5837   6823  -1031   -520     25       C  
ATOM     80  O   VAL A  76      90.136  23.391-167.846  1.00 51.41           O  
ANISOU   80  O   VAL A  76     7192   5676   6665  -1155   -636     12       O  
ATOM     81  CB  VAL A  76      88.646  24.207-170.617  1.00 49.51           C  
ANISOU   81  CB  VAL A  76     6911   5444   6455   -921   -283     47       C  
ATOM     82  CG1 VAL A  76      89.909  25.013-170.442  1.00 66.09           C  
ANISOU   82  CG1 VAL A  76     9007   7530   8573  -1089   -322     27       C  
ATOM     83  CG2 VAL A  76      88.481  23.773-172.076  1.00 48.94           C  
ANISOU   83  CG2 VAL A  76     6686   5458   6452   -806   -209     62       C  
ATOM     84  N   GLY A  77      87.927  23.625-167.466  1.00 50.43           N  
ANISOU   84  N   GLY A  77     7322   5434   6404  -1005   -471     30       N  
ATOM     85  CA  GLY A  77      88.090  24.103-166.105  1.00 50.84           C  
ANISOU   85  CA  GLY A  77     7559   5401   6358  -1130   -533     11       C  
ATOM     86  C   GLY A  77      88.068  25.608-165.945  1.00 53.96           C  
ANISOU   86  C   GLY A  77     8152   5680   6669  -1228   -425     -7       C  
ATOM     87  O   GLY A  77      88.301  26.097-164.836  1.00 56.97           O  
ANISOU   87  O   GLY A  77     8705   5983   6959  -1355   -475    -31       O  
ATOM     88  N   SER A  78      87.784  26.356-167.008  1.00 49.91           N  
ANISOU   88  N   SER A  78     7636   5149   6179  -1175   -277      7       N  
ATOM     89  CA  SER A  78      87.838  27.807-166.948  1.00 46.28           C  
ANISOU   89  CA  SER A  78     7368   4568   5649  -1267   -166     -7       C  
ATOM     90  C   SER A  78      86.576  28.383-166.312  1.00 52.41           C  
ANISOU   90  C   SER A  78     8387   5216   6310  -1198    -37      2       C  
ATOM     91  O   SER A  78      85.488  27.809-166.404  1.00 48.31           O  
ANISOU   91  O   SER A  78     7849   4719   5788  -1041     17     34       O  
ATOM     92  CB  SER A  78      88.032  28.383-168.354  1.00 52.35           C  
ANISOU   92  CB  SER A  78     8045   5363   6484  -1231    -54     14       C  
ATOM     93  OG  SER A  78      87.063  27.878-169.254  1.00 48.98           O  
ANISOU   93  OG  SER A  78     7526   4991   6092  -1043     32     55       O  
ATOM     94  N   ILE A  79      86.732  29.554-165.690  1.00 51.63           N  
ANISOU   94  N   ILE A  79     8521   4980   6118  -1318     22    -26       N  
ATOM     95  CA  ILE A  79      85.689  30.214-164.916  1.00 50.36           C  
ANISOU   95  CA  ILE A  79     8623   4674   5836  -1274    151    -27       C  
ATOM     96  C   ILE A  79      85.518  31.641-165.420  1.00 48.84           C  
ANISOU   96  C   ILE A  79     8598   4352   5607  -1283    330    -20       C  
ATOM     97  O   ILE A  79      86.507  32.351-165.631  1.00 47.99           O  
ANISOU   97  O   ILE A  79     8516   4211   5506  -1438    309    -49       O  
ATOM     98  CB  ILE A  79      86.046  30.234-163.413  1.00 52.86           C  
ANISOU   98  CB  ILE A  79     9120   4921   6044  -1427     47    -77       C  
ATOM     99  CG1 ILE A  79      86.388  28.832-162.913  1.00 60.33           C  
ANISOU   99  CG1 ILE A  79     9898   5994   7029  -1432   -147    -76       C  
ATOM    100  CG2 ILE A  79      84.935  30.873-162.603  1.00 56.20           C  
ANISOU  100  CG2 ILE A  79     9825   5191   6339  -1370    199    -80       C  
ATOM    101  CD1 ILE A  79      85.198  27.990-162.614  1.00 56.58           C  
ANISOU  101  CD1 ILE A  79     9419   5540   6537  -1267   -109    -43       C  
ATOM    102  N   THR A  80      84.264  32.065-165.603  1.00 50.22           N  
ANISOU  102  N   THR A  80     8884   4451   5744  -1118    507     22       N  
ATOM    103  CA  THR A  80      83.918  33.466-165.836  1.00 48.74           C  
ANISOU  103  CA  THR A  80     8914   4106   5501  -1106    696     34       C  
ATOM    104  C   THR A  80      82.786  33.869-164.891  1.00 57.15           C  
ANISOU  104  C   THR A  80    10224   5034   6456  -1019    829     39       C  
ATOM    105  O   THR A  80      82.173  33.031-164.221  1.00 48.04           O  
ANISOU  105  O   THR A  80     9045   3927   5280   -950    786     44       O  
ATOM    106  CB  THR A  80      83.501  33.738-167.294  1.00 55.29           C  
ANISOU  106  CB  THR A  80     9618   4982   6409   -957    813    104       C  
ATOM    107  OG1 THR A  80      82.288  33.037-167.596  1.00 57.96           O  
ANISOU  107  OG1 THR A  80     9849   5400   6774   -745    862    166       O  
ATOM    108  CG2 THR A  80      84.595  33.310-168.284  1.00 52.92           C  
ANISOU  108  CG2 THR A  80     9075   4818   6214  -1033    700     98       C  
ATOM    109  N   TYR A  81      82.521  35.173-164.841  1.00 51.71           N  
ANISOU  109  N   TYR A  81     9782   4168   5698  -1021   1002     40       N  
ATOM    110  CA  TYR A  81      81.398  35.751-164.115  1.00 46.80           C  
ANISOU  110  CA  TYR A  81     9363   3441   4976   -896   1166     49       C  
ATOM    111  C   TYR A  81      80.503  36.502-165.088  1.00 52.20           C  
ANISOU  111  C   TYR A  81    10040   4101   5693   -694   1362    127       C  
ATOM    112  O   TYR A  81      80.991  37.297-165.896  1.00 53.62           O  
ANISOU  112  O   TYR A  81    10220   4254   5900   -726   1408    135       O  
ATOM    113  CB  TYR A  81      81.884  36.697-163.016  1.00 54.75           C  
ANISOU  113  CB  TYR A  81    10602   4355   5846  -1045   1176    -36       C  
ATOM    114  CG  TYR A  81      82.563  35.943-161.915  1.00 58.00           C  
ANISOU  114  CG  TYR A  81    11030   4802   6204  -1218    987    -99       C  
ATOM    115  CD1 TYR A  81      83.910  35.630-162.001  1.00 59.50           C  
ANISOU  115  CD1 TYR A  81    11118   5052   6437  -1424    795   -139       C  
ATOM    116  CD2 TYR A  81      81.850  35.497-160.809  1.00 63.17           C  
ANISOU  116  CD2 TYR A  81    11789   5443   6771  -1169    997   -112       C  
ATOM    117  CE1 TYR A  81      84.534  34.910-161.010  1.00 60.58           C  
ANISOU  117  CE1 TYR A  81    11250   5240   6529  -1572    607   -185       C  
ATOM    118  CE2 TYR A  81      82.469  34.782-159.808  1.00 62.46           C  
ANISOU  118  CE2 TYR A  81    11714   5392   6626  -1323    815   -160       C  
ATOM    119  CZ  TYR A  81      83.813  34.493-159.916  1.00 61.10           C  
ANISOU  119  CZ  TYR A  81    11432   5285   6497  -1520    615   -194       C  
ATOM    120  OH  TYR A  81      84.448  33.777-158.936  1.00 65.28           O  
ANISOU  120  OH  TYR A  81    11960   5869   6975  -1665    421   -232       O  
ATOM    121  N   ASP A  82      79.199  36.251-165.010  1.00 52.46           N  
ANISOU  121  N   ASP A  82    10058   4151   5724   -488   1473    188       N  
ATOM    122  CA  ASP A  82      78.233  36.910-165.887  1.00 57.98           C  
ANISOU  122  CA  ASP A  82    10729   4847   6455   -276   1649    274       C  
ATOM    123  C   ASP A  82      77.772  38.189-165.201  1.00 64.92           C  
ANISOU  123  C   ASP A  82    11842   5601   7222   -233   1818    240       C  
ATOM    124  O   ASP A  82      76.848  38.189-164.386  1.00 67.02           O  
ANISOU  124  O   ASP A  82    12198   5839   7427   -130   1913    243       O  
ATOM    125  CB  ASP A  82      77.071  35.973-166.210  1.00 56.01           C  
ANISOU  125  CB  ASP A  82    10315   4700   6267    -79   1676    368       C  
ATOM    126  CG  ASP A  82      76.242  36.452-167.396  1.00 61.57           C  
ANISOU  126  CG  ASP A  82    10918   5448   7029    125   1807    475       C  
ATOM    127  OD1 ASP A  82      75.656  37.548-167.307  1.00 70.32           O  
ANISOU  127  OD1 ASP A  82    12151   6478   8089    228   1968    486       O  
ATOM    128  OD2 ASP A  82      76.182  35.736-168.423  1.00 61.88           O  
ANISOU  128  OD2 ASP A  82    10756   5600   7155    182   1747    550       O  
ATOM    129  N   THR A  83      78.436  39.302-165.530  1.00 69.20           N  
ANISOU  129  N   THR A  83    12493   6063   7735   -317   1864    208       N  
ATOM    130  CA  THR A  83      78.025  40.599-165.008  1.00 67.27           C  
ANISOU  130  CA  THR A  83    12483   5692   7384   -273   2039    181       C  
ATOM    131  C   THR A  83      76.899  41.219-165.823  1.00 62.60           C  
ANISOU  131  C   THR A  83    11860   5095   6831    -24   2226    277       C  
ATOM    132  O   THR A  83      76.190  42.093-165.314  1.00 66.49           O  
ANISOU  132  O   THR A  83    12527   5495   7242     76   2399    275       O  
ATOM    133  CB  THR A  83      79.214  41.558-164.963  1.00 64.64           C  
ANISOU  133  CB  THR A  83    12295   5273   6995   -478   2011    108       C  
ATOM    134  OG1 THR A  83      79.731  41.738-166.285  1.00 63.97           O  
ANISOU  134  OG1 THR A  83    12074   5225   7007   -485   1988    153       O  
ATOM    135  CG2 THR A  83      80.311  41.006-164.071  1.00 66.15           C  
ANISOU  135  CG2 THR A  83    12514   5481   7140   -727   1821     18       C  
ATOM    136  N   LEU A  84      76.715  40.770-167.066  1.00 58.78           N  
ANISOU  136  N   LEU A  84    11159   4713   6463     79   2195    366       N  
ATOM    137  CA  LEU A  84      75.664  41.307-167.924  1.00 58.97           C  
ANISOU  137  CA  LEU A  84    11125   4754   6527    315   2350    470       C  
ATOM    138  C   LEU A  84      74.279  40.929-167.418  1.00 62.64           C  
ANISOU  138  C   LEU A  84    11555   5258   6987    514   2449    527       C  
ATOM    139  O   LEU A  84      73.302  41.642-167.687  1.00 60.38           O  
ANISOU  139  O   LEU A  84    11294   4951   6698    708   2618    598       O  
ATOM    140  CB  LEU A  84      75.875  40.813-169.356  1.00 51.99           C  
ANISOU  140  CB  LEU A  84    10013   3987   5755    354   2269    553       C  
ATOM    141  CG  LEU A  84      74.857  41.161-170.439  1.00 54.63           C  
ANISOU  141  CG  LEU A  84    10233   4381   6141    589   2382    679       C  
ATOM    142  CD1 LEU A  84      74.751  42.682-170.642  1.00 55.43           C  
ANISOU  142  CD1 LEU A  84    10515   4356   6191    645   2548    682       C  
ATOM    143  CD2 LEU A  84      75.235  40.469-171.743  1.00 52.33           C  
ANISOU  143  CD2 LEU A  84     9723   4219   5940    583   2270    747       C  
ATOM    144  N   SER A  85      74.182  39.813-166.689  1.00 63.73           N  
ANISOU  144  N   SER A  85    11632   5456   7127    469   2349    503       N  
ATOM    145  CA  SER A  85      72.919  39.382-166.102  1.00 63.34           C  
ANISOU  145  CA  SER A  85    11551   5443   7070    636   2440    553       C  
ATOM    146  C   SER A  85      72.282  40.469-165.248  1.00 63.34           C  
ANISOU  146  C   SER A  85    11785   5315   6967    716   2646    529       C  
ATOM    147  O   SER A  85      71.053  40.571-165.183  1.00 60.68           O  
ANISOU  147  O   SER A  85    11413   5001   6641    921   2794    608       O  
ATOM    148  CB  SER A  85      73.154  38.129-165.258  1.00 64.64           C  
ANISOU  148  CB  SER A  85    11675   5658   7227    524   2295    505       C  
ATOM    149  OG  SER A  85      74.220  38.350-164.348  1.00 67.03           O  
ANISOU  149  OG  SER A  85    12165   5866   7438    301   2217    384       O  
ATOM    150  N   ALA A  86      73.100  41.300-164.604  1.00 72.40           N  
ANISOU  150  N   ALA A  86    13168   6330   8009    555   2663    428       N  
ATOM    151  CA  ALA A  86      72.595  42.346-163.722  1.00 76.88           C  
ANISOU  151  CA  ALA A  86    13991   6766   8456    606   2861    399       C  
ATOM    152  C   ALA A  86      71.712  43.368-164.435  1.00 79.46           C  
ANISOU  152  C   ALA A  86    14327   7060   8803    824   3067    493       C  
ATOM    153  O   ALA A  86      71.127  44.223-163.760  1.00 83.94           O  
ANISOU  153  O   ALA A  86    15095   7523   9275    901   3260    492       O  
ATOM    154  CB  ALA A  86      73.770  43.053-163.046  1.00 75.32           C  
ANISOU  154  CB  ALA A  86    14033   6445   8139    367   2817    279       C  
ATOM    155  N   GLN A  87      71.587  43.302-165.764  1.00 69.47           N  
ANISOU  155  N   GLN A  87    12859   5884   7652    925   3034    582       N  
ATOM    156  CA  GLN A  87      70.781  44.245-166.531  1.00 69.61           C  
ANISOU  156  CA  GLN A  87    12869   5885   7694   1132   3211    683       C  
ATOM    157  C   GLN A  87      69.458  43.666-167.011  1.00 76.43           C  
ANISOU  157  C   GLN A  87    13504   6888   8649   1374   3267    821       C  
ATOM    158  O   GLN A  87      68.767  44.319-167.801  1.00 77.40           O  
ANISOU  158  O   GLN A  87    13570   7031   8807   1554   3387    927       O  
ATOM    159  CB  GLN A  87      71.554  44.750-167.746  1.00 67.66           C  
ANISOU  159  CB  GLN A  87    12573   5636   7497   1080   3148    698       C  
ATOM    160  CG  GLN A  87      72.400  45.975-167.491  1.00 85.01           C  
ANISOU  160  CG  GLN A  87    15034   7670   9599    940   3212    612       C  
ATOM    161  CD  GLN A  87      73.855  45.624-167.301  1.00 87.92           C  
ANISOU  161  CD  GLN A  87    15435   8022   9951    660   3021    501       C  
ATOM    162  OE1 GLN A  87      74.272  45.217-166.215  1.00 91.43           O  
ANISOU  162  OE1 GLN A  87    15975   8438  10325    511   2951    411       O  
ATOM    163  NE2 GLN A  87      74.641  45.767-168.366  1.00 79.99           N  
ANISOU  163  NE2 GLN A  87    14344   7041   9007    586   2936    515       N  
ATOM    164  N   ALA A  88      69.096  42.462-166.573  1.00 72.33           N  
ANISOU  164  N   ALA A  88    12849   6468   8166   1378   3180    828       N  
ATOM    165  CA  ALA A  88      67.911  41.797-167.102  1.00 78.67           C  
ANISOU  165  CA  ALA A  88    13404   7425   9062   1584   3205    965       C  
ATOM    166  C   ALA A  88      66.657  42.624-166.839  1.00 87.79           C  
ANISOU  166  C   ALA A  88    14621   8548  10187   1803   3453   1059       C  
ATOM    167  O   ALA A  88      66.467  43.152-165.741  1.00 87.33           O  
ANISOU  167  O   ALA A  88    14786   8368  10027   1794   3596   1010       O  
ATOM    168  CB  ALA A  88      67.769  40.407-166.486  1.00 69.61           C  
ANISOU  168  CB  ALA A  88    12140   6367   7941   1530   3084    946       C  
ATOM    169  N   GLN A  89      65.803  42.739-167.860  1.00 99.78           N  
ANISOU  169  N   GLN A  89    15944  10183  11786   1997   3503   1206       N  
ATOM    170  CA  GLN A  89      64.549  43.473-167.734  1.00108.38           C  
ANISOU  170  CA  GLN A  89    17051  11271  12859   2218   3732   1331       C  
ATOM    171  C   GLN A  89      63.400  42.541-167.368  1.00110.77           C  
ANISOU  171  C   GLN A  89    17166  11710  13210   2344   3762   1432       C  
ATOM    172  O   GLN A  89      63.101  42.361-166.183  1.00119.64           O  
ANISOU  172  O   GLN A  89    18414  12772  14272   2327   3851   1395       O  
ATOM    173  CB  GLN A  89      64.224  44.230-169.026  1.00110.52           C  
ANISOU  173  CB  GLN A  89    17221  11593  13180   2358   3779   1451       C  
ATOM    174  CG  GLN A  89      62.926  45.035-168.948  1.00114.48           C  
ANISOU  174  CG  GLN A  89    17734  12099  13666   2587   4014   1602       C  
ATOM    175  CD  GLN A  89      62.911  46.241-169.869  1.00115.98           C  
ANISOU  175  CD  GLN A  89    17978  12239  13852   2682   4105   1670       C  
ATOM    176  OE1 GLN A  89      63.414  46.192-170.994  1.00115.43           O  
ANISOU  176  OE1 GLN A  89    17793  12229  13836   2653   3974   1680       O  
ATOM    177  NE2 GLN A  89      62.337  47.340-169.388  1.00114.26           N  
ANISOU  177  NE2 GLN A  89    17947  11904  13564   2794   4336   1724       N  
ATOM    178  N   GLN A  90      62.755  41.947-168.374  1.00103.19           N  
ANISOU  178  N   GLN A  90    15913  10940  12354   2462   3686   1565       N  
ATOM    179  CA  GLN A  90      61.586  41.111-168.131  1.00 99.70           C  
ANISOU  179  CA  GLN A  90    15271  10648  11964   2586   3716   1687       C  
ATOM    180  C   GLN A  90      61.936  39.961-167.193  1.00 88.94           C  
ANISOU  180  C   GLN A  90    13920   9278  10594   2452   3610   1580       C  
ATOM    181  O   GLN A  90      63.001  39.347-167.300  1.00 83.08           O  
ANISOU  181  O   GLN A  90    13184   8521   9861   2275   3417   1462       O  
ATOM    182  CB  GLN A  90      61.034  40.566-169.451  1.00 98.19           C  
ANISOU  182  CB  GLN A  90    14755  10676  11877   2688   3602   1831       C  
ATOM    183  CG  GLN A  90      59.517  40.483-169.508  1.00 98.61           C  
ANISOU  183  CG  GLN A  90    14624  10874  11969   2885   3719   2032       C  
ATOM    184  CD  GLN A  90      58.872  41.848-169.653  1.00 97.96           C  
ANISOU  184  CD  GLN A  90    14644  10725  11850   3038   3927   2143       C  
ATOM    185  OE1 GLN A  90      59.366  42.702-170.392  1.00 98.32           O  
ANISOU  185  OE1 GLN A  90    14763  10712  11882   3044   3933   2124       O  
ATOM    186  NE2 GLN A  90      57.769  42.064-168.941  1.00 93.24           N  
ANISOU  186  NE2 GLN A  90    14049  10119  11258   3152   4061   2253       N  
ATOM    187  N   ASP A  91      61.040  39.686-166.253  1.00 81.21           N  
ANISOU  187  N   ASP A  91    12949   8304   9601   2523   3723   1632       N  
ATOM    188  CA  ASP A  91      61.262  38.607-165.306  1.00 75.22           C  
ANISOU  188  CA  ASP A  91    12211   7535   8833   2411   3639   1538       C  
ATOM    189  C   ASP A  91      60.995  37.261-165.971  1.00 76.44           C  
ANISOU  189  C   ASP A  91    12062   7891   9092   2426   3473   1607       C  
ATOM    190  O   ASP A  91      59.981  37.079-166.650  1.00 81.26           O  
ANISOU  190  O   ASP A  91    12435   8668   9773   2577   3501   1777       O  
ATOM    191  CB  ASP A  91      60.374  38.784-164.076  1.00 80.35           C  
ANISOU  191  CB  ASP A  91    12962   8109   9457   2463   3772   1573       C  
ATOM    192  CG  ASP A  91      61.015  39.661-163.019  1.00 84.65           C  
ANISOU  192  CG  ASP A  91    13853   8433   9877   2349   3862   1435       C  
ATOM    193  OD1 ASP A  91      62.187  40.054-163.199  1.00 89.01           O  
ANISOU  193  OD1 ASP A  91    14559   8897  10362   2215   3807   1307       O  
ATOM    194  OD2 ASP A  91      60.347  39.953-162.007  1.00 91.21           O  
ANISOU  194  OD2 ASP A  91    14804   9177  10675   2389   3987   1465       O  
ATOM    195  N   GLY A  92      61.913  36.323-165.778  1.00 67.74           N  
ANISOU  195  N   GLY A  92    10965   6780   7995   2241   3271   1492       N  
ATOM    196  CA  GLY A  92      61.733  34.980-166.263  1.00 62.06           C  
ANISOU  196  CA  GLY A  92     9987   6240   7354   2208   3092   1556       C  
ATOM    197  C   GLY A  92      60.813  34.184-165.360  1.00 64.21           C  
ANISOU  197  C   GLY A  92    10198   6562   7637   2263   3157   1607       C  
ATOM    198  O   GLY A  92      60.241  34.697-164.390  1.00 61.69           O  
ANISOU  198  O   GLY A  92    10029   6131   7279   2356   3355   1599       O  
ATOM    199  N   PRO A  93      60.656  32.900-165.668  1.00 56.99           N  
ANISOU  199  N   PRO A  93     9064   5825   6764   2194   2998   1662       N  
ATOM    200  CA  PRO A  93      59.689  32.059-164.951  1.00 56.60           C  
ANISOU  200  CA  PRO A  93     8901   5880   6724   2228   3050   1722       C  
ATOM    201  C   PRO A  93      60.198  31.411-163.669  1.00 55.23           C  
ANISOU  201  C   PRO A  93     8896   5620   6469   2051   3008   1584       C  
ATOM    202  O   PRO A  93      59.396  30.783-162.969  1.00 52.02           O  
ANISOU  202  O   PRO A  93     8413   5285   6067   2072   3060   1613       O  
ATOM    203  CB  PRO A  93      59.376  30.985-166.000  1.00 57.44           C  
ANISOU  203  CB  PRO A  93     8658   6254   6912   2192   2851   1788       C  
ATOM    204  CG  PRO A  93      60.668  30.820-166.729  1.00 51.72           C  
ANISOU  204  CG  PRO A  93     7960   5515   6176   2029   2647   1686       C  
ATOM    205  CD  PRO A  93      61.247  32.212-166.831  1.00 50.91           C  
ANISOU  205  CD  PRO A  93     8104   5205   6036   2090   2772   1668       C  
ATOM    206  N   CYS A  94      61.484  31.518-163.341  1.00 52.79           N  
ANISOU  206  N   CYS A  94     8799   5170   6090   1873   2904   1437       N  
ATOM    207  CA  CYS A  94      62.047  30.743-162.242  1.00 48.70           C  
ANISOU  207  CA  CYS A  94     8406   4602   5497   1688   2814   1315       C  
ATOM    208  C   CYS A  94      61.955  31.508-160.926  1.00 53.57           C  
ANISOU  208  C   CYS A  94     9317   5015   6025   1706   2989   1235       C  
ATOM    209  O   CYS A  94      61.885  32.738-160.905  1.00 55.91           O  
ANISOU  209  O   CYS A  94     9769   5167   6308   1813   3142   1222       O  
ATOM    210  CB  CYS A  94      63.505  30.379-162.521  1.00 49.71           C  
ANISOU  210  CB  CYS A  94     8576   4706   5603   1475   2580   1188       C  
ATOM    211  SG  CYS A  94      63.793  29.317-163.980  1.00 49.11           S  
ANISOU  211  SG  CYS A  94     8152   4871   5635   1413   2324   1215       S  
ATOM    212  N   THR A  95      61.960  30.763-159.825  1.00 47.43           N  
ANISOU  212  N   THR A  95     8617   4222   5180   1597   2962   1172       N  
ATOM    213  CA  THR A  95      61.976  31.329-158.485  1.00 59.62           C  
ANISOU  213  CA  THR A  95    10453   5575   6625   1577   3092   1075       C  
ATOM    214  C   THR A  95      62.959  30.542-157.632  1.00 56.48           C  
ANISOU  214  C   THR A  95    10193   5140   6125   1339   2925    952       C  
ATOM    215  O   THR A  95      63.319  29.410-157.977  1.00 51.39           O  
ANISOU  215  O   THR A  95     9389   4633   5505   1227   2737    967       O  
ATOM    216  CB  THR A  95      60.593  31.305-157.811  1.00 64.58           C  
ANISOU  216  CB  THR A  95    11035   6217   7284   1735   3278   1155       C  
ATOM    217  OG1 THR A  95      60.217  29.950-157.500  1.00 53.38           O  
ANISOU  217  OG1 THR A  95     9444   4964   5873   1656   3181   1182       O  
ATOM    218  CG2 THR A  95      59.536  31.976-158.695  1.00 56.38           C  
ANISOU  218  CG2 THR A  95     9817   5237   6367   1980   3418   1311       C  
ATOM    219  N   PRO A  96      63.406  31.114-156.506  1.00 53.85           N  
ANISOU  219  N   PRO A  96    10167   4619   5673   1259   2986    834       N  
ATOM    220  CA  PRO A  96      64.271  30.354-155.586  1.00 56.66           C  
ANISOU  220  CA  PRO A  96    10659   4945   5922   1038   2825    729       C  
ATOM    221  C   PRO A  96      63.763  28.963-155.273  1.00 57.02           C  
ANISOU  221  C   PRO A  96    10534   5144   5987   1002   2744    780       C  
ATOM    222  O   PRO A  96      64.572  28.058-155.034  1.00 58.73           O  
ANISOU  222  O   PRO A  96    10755   5398   6161    826   2546    732       O  
ATOM    223  CB  PRO A  96      64.292  31.235-154.328  1.00 54.79           C  
ANISOU  223  CB  PRO A  96    10762   4497   5560   1022   2976    627       C  
ATOM    224  CG  PRO A  96      64.122  32.624-154.863  1.00 57.49           C  
ANISOU  224  CG  PRO A  96    11190   4723   5930   1165   3147    636       C  
ATOM    225  CD  PRO A  96      63.229  32.512-156.071  1.00 53.39           C  
ANISOU  225  CD  PRO A  96    10360   4357   5568   1359   3195    790       C  
ATOM    226  N   ARG A  97      62.454  28.747-155.289  1.00 50.18           N  
ANISOU  226  N   ARG A  97     9506   4370   5189   1161   2886    881       N  
ATOM    227  CA  ARG A  97      61.931  27.452-154.890  1.00 55.09           C  
ANISOU  227  CA  ARG A  97     9984   5130   5819   1113   2824    923       C  
ATOM    228  C   ARG A  97      61.717  26.472-156.045  1.00 47.45           C  
ANISOU  228  C   ARG A  97     8693   4377   4960   1120   2698   1025       C  
ATOM    229  O   ARG A  97      61.521  25.281-155.781  1.00 48.33           O  
ANISOU  229  O   ARG A  97     8688   4597   5077   1038   2597   1038       O  
ATOM    230  CB  ARG A  97      60.633  27.635-154.108  1.00 61.35           C  
ANISOU  230  CB  ARG A  97    10783   5907   6621   1249   3036    971       C  
ATOM    231  CG  ARG A  97      60.807  27.285-152.619  1.00 73.10           C  
ANISOU  231  CG  ARG A  97    12504   7290   7981   1125   3039    878       C  
ATOM    232  CD  ARG A  97      60.044  28.238-151.724  1.00 88.02           C  
ANISOU  232  CD  ARG A  97    14579   9023   9840   1248   3275    869       C  
ATOM    233  NE  ARG A  97      58.639  28.298-152.106  1.00 97.48           N  
ANISOU  233  NE  ARG A  97    15548  10327  11163   1449   3434   1008       N  
ATOM    234  CZ  ARG A  97      57.693  27.521-151.591  1.00100.35           C  
ANISOU  234  CZ  ARG A  97    15784  10793  11549   1471   3488   1069       C  
ATOM    235  NH1 ARG A  97      57.999  26.626-150.661  1.00 98.56           N  
ANISOU  235  NH1 ARG A  97    15655  10568  11226   1310   3402   1002       N  
ATOM    236  NH2 ARG A  97      56.438  27.642-152.004  1.00100.73           N  
ANISOU  236  NH2 ARG A  97    15609  10947  11717   1651   3623   1204       N  
ATOM    237  N   ARG A  98      61.761  26.912-157.304  1.00 50.58           N  
ANISOU  237  N   ARG A  98     8930   4837   5451   1206   2674   1080       N  
ATOM    238  CA  ARG A  98      61.545  25.976-158.402  1.00 47.28           C  
ANISOU  238  CA  ARG A  98     8178   4632   5155   1200   2509   1140       C  
ATOM    239  C   ARG A  98      62.025  26.587-159.711  1.00 45.55           C  
ANISOU  239  C   ARG A  98     7860   4439   5009   1247   2442   1154       C  
ATOM    240  O   ARG A  98      61.745  27.753-159.997  1.00 46.09           O  
ANISOU  240  O   ARG A  98     8002   4427   5081   1387   2606   1202       O  
ATOM    241  CB  ARG A  98      60.068  25.605-158.538  1.00 47.32           C  
ANISOU  241  CB  ARG A  98     7960   4789   5229   1338   2639   1274       C  
ATOM    242  CG  ARG A  98      59.158  26.823-158.403  1.00 61.33           C  
ANISOU  242  CG  ARG A  98     9801   6493   7010   1550   2914   1358       C  
ATOM    243  CD  ARG A  98      57.960  26.691-159.294  1.00 62.53           C  
ANISOU  243  CD  ARG A  98     9637   6840   7282   1707   2973   1513       C  
ATOM    244  NE  ARG A  98      57.243  27.946-159.485  1.00 59.66           N  
ANISOU  244  NE  ARG A  98     9285   6411   6973   1920   3157   1583       N  
ATOM    245  CZ  ARG A  98      57.691  28.963-160.220  1.00 52.86           C  
ANISOU  245  CZ  ARG A  98     8490   5469   6127   1999   3179   1588       C  
ATOM    246  NH1 ARG A  98      58.879  28.899-160.799  1.00 54.20           N  
ANISOU  246  NH1 ARG A  98     8722   5613   6260   1873   3030   1518       N  
ATOM    247  NH2 ARG A  98      56.961  30.057-160.357  1.00 59.54           N  
ANISOU  247  NH2 ARG A  98     9351   6246   7026   2201   3347   1671       N  
ATOM    248  N   CYS A  99      62.722  25.781-160.501  1.00 43.45           N  
ANISOU  248  N   CYS A  99     7432   4281   4798   1135   2209   1118       N  
ATOM    249  CA  CYS A  99      63.234  26.191-161.802  1.00 42.54           C  
ANISOU  249  CA  CYS A  99     7206   4208   4748   1158   2124   1128       C  
ATOM    250  C   CYS A  99      62.293  25.702-162.895  1.00 48.82           C  
ANISOU  250  C   CYS A  99     7689   5213   5647   1256   2100   1246       C  
ATOM    251  O   CYS A  99      61.865  24.538-162.886  1.00 44.54           O  
ANISOU  251  O   CYS A  99     6978   4808   5138   1200   2006   1265       O  
ATOM    252  CB  CYS A  99      64.648  25.649-162.026  1.00 39.46           C  
ANISOU  252  CB  CYS A  99     6838   3803   4350    975   1891   1013       C  
ATOM    253  SG  CYS A  99      65.309  25.843-163.711  1.00 43.21           S  
ANISOU  253  SG  CYS A  99     7139   4367   4913    979   1761   1022       S  
ATOM    254  N   LEU A 100      61.957  26.607-163.820  1.00 49.43           N  
ANISOU  254  N   LEU A 100     7700   5311   5771   1399   2186   1328       N  
ATOM    255  CA  LEU A 100      61.111  26.309-164.969  1.00 49.02           C  
ANISOU  255  CA  LEU A 100     7358   5460   5809   1495   2156   1448       C  
ATOM    256  C   LEU A 100      61.861  26.524-166.280  1.00 49.32           C  
ANISOU  256  C   LEU A 100     7317   5540   5883   1471   2025   1436       C  
ATOM    257  O   LEU A 100      61.255  26.871-167.295  1.00 44.44           O  
ANISOU  257  O   LEU A 100     6536   5031   5318   1592   2052   1545       O  
ATOM    258  CB  LEU A 100      59.840  27.159-164.943  1.00 50.32           C  
ANISOU  258  CB  LEU A 100     7480   5640   5998   1713   2387   1591       C  
ATOM    259  CG  LEU A 100      58.882  26.926-163.774  1.00 49.99           C  
ANISOU  259  CG  LEU A 100     7470   5591   5934   1764   2543   1630       C  
ATOM    260  CD1 LEU A 100      57.697  27.881-163.841  1.00 50.53           C  
ANISOU  260  CD1 LEU A 100     7491   5669   6038   2003   2784   1779       C  
ATOM    261  CD2 LEU A 100      58.420  25.467-163.717  1.00 48.00           C  
ANISOU  261  CD2 LEU A 100     7004   5518   5714   1657   2410   1642       C  
ATOM    262  N   GLY A 101      63.179  26.313-166.275  1.00 44.96           N  
ANISOU  262  N   GLY A 101     6872   4908   5301   1316   1882   1309       N  
ATOM    263  CA  GLY A 101      63.972  26.573-167.466  1.00 44.91           C  
ANISOU  263  CA  GLY A 101     6812   4927   5324   1288   1775   1290       C  
ATOM    264  C   GLY A 101      63.625  25.699-168.654  1.00 45.68           C  
ANISOU  264  C   GLY A 101     6636   5237   5486   1280   1637   1343       C  
ATOM    265  O   GLY A 101      63.881  26.092-169.793  1.00 45.77           O  
ANISOU  265  O   GLY A 101     6575   5295   5521   1314   1599   1374       O  
ATOM    266  N   SER A 102      63.043  24.523-168.422  1.00 41.38           N  
ANISOU  266  N   SER A 102     5946   4815   4960   1228   1563   1354       N  
ATOM    267  CA  SER A 102      62.736  23.620-169.523  1.00 42.42           C  
ANISOU  267  CA  SER A 102     5834   5141   5141   1196   1423   1393       C  
ATOM    268  C   SER A 102      61.398  23.924-170.192  1.00 46.08           C  
ANISOU  268  C   SER A 102     6110   5756   5644   1346   1507   1550       C  
ATOM    269  O   SER A 102      61.063  23.265-171.180  1.00 46.42           O  
ANISOU  269  O   SER A 102     5950   5969   5717   1320   1392   1593       O  
ATOM    270  CB  SER A 102      62.746  22.165-169.031  1.00 45.65           C  
ANISOU  270  CB  SER A 102     6177   5613   5553   1056   1295   1332       C  
ATOM    271  OG  SER A 102      61.656  21.918-168.169  1.00 46.63           O  
ANISOU  271  OG  SER A 102     6271   5769   5675   1101   1399   1397       O  
ATOM    272  N   LEU A 103      60.619  24.876-169.680  1.00 43.09           N  
ANISOU  272  N   LEU A 103     5790   5321   5261   1502   1703   1641       N  
ATOM    273  CA  LEU A 103      59.330  25.167-170.292  1.00 42.90           C  
ANISOU  273  CA  LEU A 103     5567   5450   5282   1658   1782   1806       C  
ATOM    274  C   LEU A 103      59.545  25.912-171.606  1.00 47.95           C  
ANISOU  274  C   LEU A 103     6154   6130   5934   1737   1755   1866       C  
ATOM    275  O   LEU A 103      60.365  26.834-171.688  1.00 44.64           O  
ANISOU  275  O   LEU A 103     5917   5556   5488   1760   1805   1820       O  
ATOM    276  CB  LEU A 103      58.441  25.977-169.354  1.00 47.05           C  
ANISOU  276  CB  LEU A 103     6172   5900   5807   1820   2015   1891       C  
ATOM    277  CG  LEU A 103      57.565  25.141-168.403  1.00 53.96           C  
ANISOU  277  CG  LEU A 103     6966   6845   6690   1792   2059   1915       C  
ATOM    278  CD1 LEU A 103      58.422  24.286-167.487  1.00 51.28           C  
ANISOU  278  CD1 LEU A 103     6776   6406   6303   1602   1964   1760       C  
ATOM    279  CD2 LEU A 103      56.652  26.031-167.592  1.00 58.98           C  
ANISOU  279  CD2 LEU A 103     7671   7410   7328   1975   2313   2011       C  
ATOM    280  N   VAL A 104      58.822  25.487-172.640  1.00 49.72           N  
ANISOU  280  N   VAL A 104     6133   6565   6193   1764   1670   1968       N  
ATOM    281  CA  VAL A 104      58.978  26.103-173.957  1.00 46.07           C  
ANISOU  281  CA  VAL A 104     5610   6161   5733   1832   1629   2034       C  
ATOM    282  C   VAL A 104      58.481  27.542-173.934  1.00 50.46           C  
ANISOU  282  C   VAL A 104     6241   6633   6297   2050   1828   2156       C  
ATOM    283  O   VAL A 104      59.162  28.456-174.409  1.00 62.48           O  
ANISOU  283  O   VAL A 104     7899   8043   7798   2094   1864   2146       O  
ATOM    284  CB  VAL A 104      58.248  25.273-175.022  1.00 44.69           C  
ANISOU  284  CB  VAL A 104     5159   6241   5579   1800   1485   2119       C  
ATOM    285  CG1 VAL A 104      58.284  25.986-176.377  1.00 47.75           C  
ANISOU  285  CG1 VAL A 104     5486   6698   5958   1887   1454   2208       C  
ATOM    286  CG2 VAL A 104      58.866  23.898-175.126  1.00 42.50           C  
ANISOU  286  CG2 VAL A 104     4845   6016   5289   1584   1295   1985       C  
ATOM    287  N   PHE A 105      57.291  27.763-173.380  1.00 54.47           N  
ANISOU  287  N   PHE A 105     6665   7192   6838   2192   1970   2277       N  
ATOM    288  CA  PHE A 105      56.750  29.108-173.223  1.00 66.86           C  
ANISOU  288  CA  PHE A 105     8316   8666   8420   2419   2185   2398       C  
ATOM    289  C   PHE A 105      56.724  29.483-171.748  1.00 80.09           C  
ANISOU  289  C   PHE A 105    10203  10150  10078   2455   2372   2341       C  
ATOM    290  O   PHE A 105      55.955  28.888-170.975  1.00 69.38           O  
ANISOU  290  O   PHE A 105     8759   8861   8742   2455   2420   2366       O  
ATOM    291  CB  PHE A 105      55.348  29.206-173.826  1.00 60.57           C  
ANISOU  291  CB  PHE A 105     7248   8084   7681   2589   2224   2606       C  
ATOM    292  CG  PHE A 105      55.313  28.972-175.307  1.00 56.64           C  
ANISOU  292  CG  PHE A 105     6560   7774   7185   2565   2049   2677       C  
ATOM    293  CD1 PHE A 105      54.682  27.860-175.831  1.00 63.54           C  
ANISOU  293  CD1 PHE A 105     7167   8897   8079   2471   1887   2721       C  
ATOM    294  CD2 PHE A 105      55.934  29.854-176.171  1.00 69.05           C  
ANISOU  294  CD2 PHE A 105     8235   9270   8731   2624   2048   2694       C  
ATOM    295  CE1 PHE A 105      54.663  27.634-177.196  1.00 71.97           C  
ANISOU  295  CE1 PHE A 105     8078  10135   9131   2436   1722   2779       C  
ATOM    296  CE2 PHE A 105      55.919  29.638-177.536  1.00 70.35           C  
ANISOU  296  CE2 PHE A 105     8243   9607   8879   2586   1887   2749       C  
ATOM    297  CZ  PHE A 105      55.280  28.525-178.048  1.00 74.65           C  
ANISOU  297  CZ  PHE A 105     8525  10401   9440   2503   1724   2798       C  
ATOM    298  N   PRO A 106      57.547  30.434-171.308  1.00 99.93           N  
ANISOU  298  N   PRO A 106    13002  12422  12547   2473   2479   2262       N  
ATOM    299  CA  PRO A 106      57.477  30.888-169.911  1.00105.86           C  
ANISOU  299  CA  PRO A 106    13978  12979  13264   2513   2670   2212       C  
ATOM    300  C   PRO A 106      56.181  31.623-169.593  1.00108.43           C  
ANISOU  300  C   PRO A 106    14254  13316  13629   2763   2905   2377       C  
ATOM    301  O   PRO A 106      56.098  32.841-169.787  1.00117.01           O  
ANISOU  301  O   PRO A 106    15474  14296  14688   2855   3020   2431       O  
ATOM    302  CB  PRO A 106      58.689  31.822-169.785  1.00107.26           C  
ANISOU  302  CB  PRO A 106    14461  12911  13382   2467   2711   2101       C  
ATOM    303  CG  PRO A 106      59.609  31.426-170.906  1.00105.85           C  
ANISOU  303  CG  PRO A 106    14204  12810  13205   2329   2493   2044       C  
ATOM    304  CD  PRO A 106      58.712  30.986-172.020  1.00105.58           C  
ANISOU  304  CD  PRO A 106    13859  13029  13229   2410   2408   2189       C  
ATOM    305  N   ARG A 107      55.178  30.890-169.104  1.00 95.00           N  
ANISOU  305  N   ARG A 107    12377  11757  11964   2769   2915   2439       N  
ATOM    306  CA  ARG A 107      53.886  31.451-168.692  1.00 91.00           C  
ANISOU  306  CA  ARG A 107    11828  11263  11487   2909   3046   2581       C  
ATOM    307  C   ARG A 107      53.308  32.442-169.711  1.00 95.34           C  
ANISOU  307  C   ARG A 107    12298  11879  12048   3045   3080   2741       C  
ATOM    308  O   ARG A 107      52.099  32.687-169.753  1.00 96.61           O  
ANISOU  308  O   ARG A 107    12317  12145  12245   3156   3142   2892       O  
ATOM    309  CB  ARG A 107      54.020  32.129-167.326  1.00 98.87           C  
ANISOU  309  CB  ARG A 107    13135  11998  12434   2935   3231   2506       C  
ATOM    310  CG  ARG A 107      52.694  32.556-166.702  1.00110.83           C  
ANISOU  310  CG  ARG A 107    14611  13518  13980   3071   3380   2637       C  
ATOM    311  CD  ARG A 107      52.888  33.701-165.715  1.00115.59           C  
ANISOU  311  CD  ARG A 107    15559  13838  14522   3131   3582   2596       C  
ATOM    312  NE  ARG A 107      51.903  34.765-165.898  1.00113.34           N  
ANISOU  312  NE  ARG A 107    15263  13550  14252   3306   3734   2766       N  
ATOM    313  CZ  ARG A 107      50.917  35.031-165.047  1.00111.52           C  
ANISOU  313  CZ  ARG A 107    15053  13277  14041   3407   3885   2840       C  
ATOM    314  NH1 ARG A 107      50.783  34.314-163.939  1.00109.78           N  
ANISOU  314  NH1 ARG A 107    14872  13016  13824   3343   3905   2754       N  
ATOM    315  NH2 ARG A 107      50.067  36.021-165.298  1.00111.36           N  
ANISOU  315  NH2 ARG A 107    15018  13261  14034   3571   4025   2999       N  
ATOM    316  N   PRO A 120      50.672  55.335-171.240  1.00132.33           N  
ANISOU  316  N   PRO A 120    19968  14294  16016   5150   6246   3697       N  
ATOM    317  CA  PRO A 120      52.035  54.894-170.930  1.00129.23           C  
ANISOU  317  CA  PRO A 120    19728  13811  15560   4888   6114   3452       C  
ATOM    318  C   PRO A 120      53.086  56.004-170.882  1.00128.78           C  
ANISOU  318  C   PRO A 120    20024  13507  15400   4806   6214   3303       C  
ATOM    319  O   PRO A 120      53.266  56.749-171.843  1.00122.11           O  
ANISOU  319  O   PRO A 120    19192  12645  14560   4879   6225   3341       O  
ATOM    320  CB  PRO A 120      52.345  53.928-172.077  1.00122.13           C  
ANISOU  320  CB  PRO A 120    18516  13147  14739   4811   5833   3442       C  
ATOM    321  CG  PRO A 120      51.030  53.306-172.377  1.00123.49           C  
ANISOU  321  CG  PRO A 120    18354  13557  15011   4968   5793   3653       C  
ATOM    322  CD  PRO A 120      49.981  54.377-172.123  1.00129.46           C  
ANISOU  322  CD  PRO A 120    19194  14231  15764   5208   6051   3832       C  
ATOM    323  N   GLU A 121      53.749  56.120-169.735  1.00132.69           N  
ANISOU  323  N   GLU A 121    20809  13808  15798   4652   6289   3140       N  
ATOM    324  CA  GLU A 121      55.093  56.670-169.663  1.00124.16           C  
ANISOU  324  CA  GLU A 121    20012  12540  14623   4465   6271   2932       C  
ATOM    325  C   GLU A 121      56.125  55.564-169.500  1.00113.27           C  
ANISOU  325  C   GLU A 121    18573  11222  13243   4213   6031   2742       C  
ATOM    326  O   GLU A 121      57.318  55.853-169.354  1.00102.86           O  
ANISOU  326  O   GLU A 121    17470   9763  11850   4025   5982   2555       O  
ATOM    327  CB  GLU A 121      55.212  57.679-168.515  1.00127.34           C  
ANISOU  327  CB  GLU A 121    20808  12671  14906   4449   6511   2868       C  
ATOM    328  CG  GLU A 121      55.032  57.087-167.129  1.00129.32           C  
ANISOU  328  CG  GLU A 121    21126  12865  15144   4350   6502   2793       C  
ATOM    329  CD  GLU A 121      56.051  57.623-166.143  1.00132.17           C  
ANISOU  329  CD  GLU A 121    21860  12979  15379   4142   6543   2579       C  
ATOM    330  OE1 GLU A 121      57.166  57.980-166.586  1.00128.78           O  
ANISOU  330  OE1 GLU A 121    21560  12477  14891   3997   6472   2442       O  
ATOM    331  OE2 GLU A 121      55.736  57.693-164.932  1.00133.52           O  
ANISOU  331  OE2 GLU A 121    22198  13029  15506   4122   6648   2553       O  
ATOM    332  N   GLN A 122      55.674  54.305-169.492  1.00113.36           N  
ANISOU  332  N   GLN A 122    18296  11437  13339   4203   5876   2789       N  
ATOM    333  CA  GLN A 122      56.576  53.165-169.594  1.00111.32           C  
ANISOU  333  CA  GLN A 122    17919  11272  13107   3991   5621   2634       C  
ATOM    334  C   GLN A 122      57.294  53.148-170.935  1.00101.37           C  
ANISOU  334  C   GLN A 122    16536  10092  11887   3947   5454   2599       C  
ATOM    335  O   GLN A 122      58.389  52.582-171.048  1.00105.31           O  
ANISOU  335  O   GLN A 122    17041  10588  12382   3748   5273   2434       O  
ATOM    336  CB  GLN A 122      55.794  51.862-169.413  1.00119.59           C  
ANISOU  336  CB  GLN A 122    18665  12527  14246   4018   5496   2717       C  
ATOM    337  CG  GLN A 122      54.703  51.668-170.469  1.00126.07           C  
ANISOU  337  CG  GLN A 122    19166  13574  15162   4223   5482   2947       C  
ATOM    338  CD  GLN A 122      54.015  50.318-170.391  1.00124.38           C  
ANISOU  338  CD  GLN A 122    18647  13580  15033   4226   5341   3026       C  
ATOM    339  OE1 GLN A 122      54.555  49.360-169.837  1.00116.50           O  
ANISOU  339  OE1 GLN A 122    17633  12593  14038   4056   5200   2891       O  
ATOM    340  NE2 GLN A 122      52.811  50.236-170.952  1.00129.00           N  
ANISOU  340  NE2 GLN A 122    18977  14340  15698   4413   5357   3239       N  
ATOM    341  N   LEU A 123      56.687  53.742-171.964  1.00 87.04           N  
ANISOU  341  N   LEU A 123    14602   8347  10121   4128   5500   2757       N  
ATOM    342  CA  LEU A 123      57.313  53.755-173.283  1.00 81.48           C  
ANISOU  342  CA  LEU A 123    13784   7715   9461   4092   5336   2739       C  
ATOM    343  C   LEU A 123      58.586  54.595-173.279  1.00 83.74           C  
ANISOU  343  C   LEU A 123    14369   7779   9668   3943   5356   2567       C  
ATOM    344  O   LEU A 123      59.587  54.213-173.899  1.00 82.62           O  
ANISOU  344  O   LEU A 123    14186   7660   9547   3788   5167   2457       O  
ATOM    345  CB  LEU A 123      56.318  54.272-174.325  1.00 83.69           C  
ANISOU  345  CB  LEU A 123    13888   8111   9799   4326   5392   2957       C  
ATOM    346  CG  LEU A 123      56.721  54.249-175.804  1.00 80.64           C  
ANISOU  346  CG  LEU A 123    13346   7831   9464   4323   5223   2986       C  
ATOM    347  CD1 LEU A 123      57.005  52.821-176.268  1.00 79.71           C  
ANISOU  347  CD1 LEU A 123    12951   7923   9413   4197   4955   2946       C  
ATOM    348  CD2 LEU A 123      55.640  54.883-176.662  1.00 76.92           C  
ANISOU  348  CD2 LEU A 123    12736   7455   9033   4568   5309   3212       C  
ATOM    349  N   LEU A 124      58.571  55.734-172.572  1.00 80.66           N  
ANISOU  349  N   LEU A 124    14289   7172   9187   3980   5583   2547       N  
ATOM    350  CA  LEU A 124      59.741  56.608-172.535  1.00 82.42           C  
ANISOU  350  CA  LEU A 124    14811   7177   9326   3832   5612   2390       C  
ATOM    351  C   LEU A 124      60.908  55.951-171.803  1.00 81.48           C  
ANISOU  351  C   LEU A 124    14799   6998   9162   3557   5469   2171       C  
ATOM    352  O   LEU A 124      62.065  56.117-172.203  1.00 80.53           O  
ANISOU  352  O   LEU A 124    14771   6802   9023   3386   5354   2042       O  
ATOM    353  CB  LEU A 124      59.382  57.944-171.881  1.00 98.25           C  
ANISOU  353  CB  LEU A 124    17128   8966  11236   3935   5895   2425       C  
ATOM    354  CG  LEU A 124      60.143  59.190-172.360  1.00102.43           C  
ANISOU  354  CG  LEU A 124    17914   9300  11704   3897   5972   2366       C  
ATOM    355  CD1 LEU A 124      59.369  59.914-173.453  1.00106.08           C  
ANISOU  355  CD1 LEU A 124    18276   9808  12222   4139   6061   2559       C  
ATOM    356  CD2 LEU A 124      60.474  60.143-171.214  1.00102.66           C  
ANISOU  356  CD2 LEU A 124    18340   9069  11596   3821   6178   2264       C  
ATOM    357  N   SER A 125      60.629  55.202-170.732  1.00 77.42           N  
ANISOU  357  N   SER A 125    14273   6515   8628   3508   5471   2135       N  
ATOM    358  CA  SER A 125      61.697  54.503-170.021  1.00 80.06           C  
ANISOU  358  CA  SER A 125    14693   6807   8921   3251   5322   1935       C  
ATOM    359  C   SER A 125      62.410  53.502-170.925  1.00 76.71           C  
ANISOU  359  C   SER A 125    14025   6535   8588   3133   5046   1881       C  
ATOM    360  O   SER A 125      63.643  53.403-170.909  1.00 71.08           O  
ANISOU  360  O   SER A 125    13414   5747   7847   2916   4914   1721       O  
ATOM    361  CB  SER A 125      61.122  53.795-168.796  1.00 76.20           C  
ANISOU  361  CB  SER A 125    14203   6346   8405   3245   5370   1935       C  
ATOM    362  OG  SER A 125      59.921  54.433-168.391  1.00 94.96           O  
ANISOU  362  OG  SER A 125    16629   8681  10771   3451   5592   2089       O  
ATOM    363  N   GLN A 126      61.650  52.733-171.705  1.00 77.71           N  
ANISOU  363  N   GLN A 126    13826   6878   8821   3265   4954   2018       N  
ATOM    364  CA  GLN A 126      62.259  51.771-172.614  1.00 69.82           C  
ANISOU  364  CA  GLN A 126    12596   6028   7906   3164   4699   1983       C  
ATOM    365  C   GLN A 126      62.925  52.446-173.808  1.00 75.10           C  
ANISOU  365  C   GLN A 126    13288   6655   8590   3144   4645   1985       C  
ATOM    366  O   GLN A 126      63.947  51.955-174.296  1.00 70.64           O  
ANISOU  366  O   GLN A 126    12678   6111   8052   2973   4456   1888       O  
ATOM    367  CB  GLN A 126      61.212  50.781-173.109  1.00 76.01           C  
ANISOU  367  CB  GLN A 126    13034   7058   8787   3305   4618   2136       C  
ATOM    368  CG  GLN A 126      60.474  50.042-172.018  1.00 80.93           C  
ANISOU  368  CG  GLN A 126    13605   7739   9407   3332   4666   2157       C  
ATOM    369  CD  GLN A 126      59.433  49.123-172.602  1.00 81.66           C  
ANISOU  369  CD  GLN A 126    13349   8081   9595   3463   4581   2321       C  
ATOM    370  OE1 GLN A 126      58.245  49.442-172.618  1.00 91.72           O  
ANISOU  370  OE1 GLN A 126    14540   9421  10888   3655   4716   2494       O  
ATOM    371  NE2 GLN A 126      59.877  47.988-173.122  1.00 78.19           N  
ANISOU  371  NE2 GLN A 126    12704   7785   9218   3357   4352   2276       N  
ATOM    372  N   ALA A 127      62.363  53.553-174.297  1.00 74.11           N  
ANISOU  372  N   ALA A 127    13235   6472   8449   3315   4809   2102       N  
ATOM    373  CA  ALA A 127      62.990  54.270-175.404  1.00 74.68           C  
ANISOU  373  CA  ALA A 127    13357   6489   8528   3298   4773   2108       C  
ATOM    374  C   ALA A 127      64.293  54.927-174.963  1.00 72.80           C  
ANISOU  374  C   ALA A 127    13423   6030   8209   3083   4785   1928       C  
ATOM    375  O   ALA A 127      65.316  54.820-175.651  1.00 73.78           O  
ANISOU  375  O   ALA A 127    13538   6142   8351   2931   4636   1856       O  
ATOM    376  CB  ALA A 127      62.028  55.316-175.974  1.00 70.20           C  
ANISOU  376  CB  ALA A 127    12805   5906   7961   3542   4955   2284       C  
ATOM    377  N   ARG A 128      64.275  55.608-173.812  1.00 69.17           N  
ANISOU  377  N   ARG A 128    13234   5395   7652   3058   4960   1860       N  
ATOM    378  CA  ARG A 128      65.490  56.232-173.300  1.00 70.47           C  
ANISOU  378  CA  ARG A 128    13694   5356   7726   2837   4969   1688       C  
ATOM    379  C   ARG A 128      66.598  55.205-173.142  1.00 70.31           C  
ANISOU  379  C   ARG A 128    13601   5388   7727   2584   4731   1540       C  
ATOM    380  O   ARG A 128      67.728  55.424-173.596  1.00 69.88           O  
ANISOU  380  O   ARG A 128    13620   5266   7665   2407   4627   1452       O  
ATOM    381  CB  ARG A 128      65.212  56.939-171.970  1.00 81.13           C  
ANISOU  381  CB  ARG A 128    15333   6534   8958   2840   5182   1640       C  
ATOM    382  CG  ARG A 128      64.722  58.372-172.105  1.00 85.13           C  
ANISOU  382  CG  ARG A 128    16054   6886   9406   2999   5427   1726       C  
ATOM    383  CD  ARG A 128      64.818  59.128-170.785  1.00 95.99           C  
ANISOU  383  CD  ARG A 128    17776   8054  10642   2930   5615   1638       C  
ATOM    384  NE  ARG A 128      63.543  59.183-170.074  1.00113.60           N  
ANISOU  384  NE  ARG A 128    20008  10301  12854   3130   5807   1758       N  
ATOM    385  CZ  ARG A 128      63.148  58.297-169.162  1.00127.30           C  
ANISOU  385  CZ  ARG A 128    21668  12114  14584   3108   5782   1743       C  
ATOM    386  NH1 ARG A 128      63.926  57.269-168.841  1.00126.77           N  
ANISOU  386  NH1 ARG A 128    21519  12118  14529   2900   5570   1609       N  
ATOM    387  NH2 ARG A 128      61.970  58.437-168.568  1.00132.10           N  
ANISOU  387  NH2 ARG A 128    22286  12727  15179   3295   5971   1871       N  
ATOM    388  N   ASP A 129      66.278  54.057-172.527  1.00 66.56           N  
ANISOU  388  N   ASP A 129    12971   5037   7282   2565   4642   1523       N  
ATOM    389  CA  ASP A 129      67.260  52.994-172.353  1.00 65.05           C  
ANISOU  389  CA  ASP A 129    12694   4905   7116   2339   4414   1396       C  
ATOM    390  C   ASP A 129      67.820  52.526-173.695  1.00 69.52           C  
ANISOU  390  C   ASP A 129    13052   5586   7775   2293   4226   1428       C  
ATOM    391  O   ASP A 129      69.035  52.335-173.842  1.00 60.74           O  
ANISOU  391  O   ASP A 129    11982   4435   6659   2074   4084   1318       O  
ATOM    392  CB  ASP A 129      66.624  51.831-171.582  1.00 73.08           C  
ANISOU  392  CB  ASP A 129    13559   6048   8160   2370   4365   1403       C  
ATOM    393  CG  ASP A 129      67.107  50.475-172.058  1.00 88.91           C  
ANISOU  393  CG  ASP A 129    15310   8217  10255   2262   4114   1375       C  
ATOM    394  OD1 ASP A 129      68.158  50.008-171.569  1.00 94.65           O  
ANISOU  394  OD1 ASP A 129    16105   8902  10957   2035   3979   1235       O  
ATOM    395  OD2 ASP A 129      66.433  49.873-172.927  1.00 93.53           O  
ANISOU  395  OD2 ASP A 129    15628   8977  10931   2400   4049   1500       O  
ATOM    396  N   PHE A 130      66.949  52.337-174.691  1.00 74.37           N  
ANISOU  396  N   PHE A 130    13440   6348   8467   2492   4222   1586       N  
ATOM    397  CA  PHE A 130      67.418  51.845-175.984  1.00 68.80           C  
ANISOU  397  CA  PHE A 130    12538   5763   7838   2452   4045   1627       C  
ATOM    398  C   PHE A 130      68.270  52.888-176.698  1.00 60.65           C  
ANISOU  398  C   PHE A 130    11672   4596   6776   2375   4073   1602       C  
ATOM    399  O   PHE A 130      69.282  52.544-177.317  1.00 61.87           O  
ANISOU  399  O   PHE A 130    11781   4771   6957   2209   3918   1549       O  
ATOM    400  CB  PHE A 130      66.241  51.424-176.865  1.00 72.76           C  
ANISOU  400  CB  PHE A 130    12766   6465   8416   2677   4031   1808       C  
ATOM    401  CG  PHE A 130      66.615  51.239-178.317  1.00 75.33           C  
ANISOU  401  CG  PHE A 130    12934   6892   8794   2666   3892   1874       C  
ATOM    402  CD1 PHE A 130      67.276  50.096-178.734  1.00 64.89           C  
ANISOU  402  CD1 PHE A 130    11445   5692   7520   2521   3678   1830       C  
ATOM    403  CD2 PHE A 130      66.319  52.218-179.259  1.00 75.57           C  
ANISOU  403  CD2 PHE A 130    13000   6894   8821   2798   3981   1984       C  
ATOM    404  CE1 PHE A 130      67.635  49.933-180.061  1.00 63.78           C  
ANISOU  404  CE1 PHE A 130    11178   5643   7414   2503   3560   1893       C  
ATOM    405  CE2 PHE A 130      66.674  52.054-180.587  1.00 67.43           C  
ANISOU  405  CE2 PHE A 130    11840   5955   7826   2780   3855   2047       C  
ATOM    406  CZ  PHE A 130      67.332  50.914-180.987  1.00 61.23           C  
ANISOU  406  CZ  PHE A 130    10892   5292   7080   2631   3648   2000       C  
ATOM    407  N   ILE A 131      67.875  54.165-176.631  1.00 67.74           N  
ANISOU  407  N   ILE A 131    12766   5353   7618   2491   4275   1646       N  
ATOM    408  CA  ILE A 131      68.689  55.220-177.233  1.00 71.53           C  
ANISOU  408  CA  ILE A 131    13431   5686   8061   2411   4316   1618       C  
ATOM    409  C   ILE A 131      70.072  55.250-176.598  1.00 70.11           C  
ANISOU  409  C   ILE A 131    13434   5377   7827   2120   4240   1437       C  
ATOM    410  O   ILE A 131      71.085  55.435-177.283  1.00 63.11           O  
ANISOU  410  O   ILE A 131    12575   4454   6949   1968   4151   1396       O  
ATOM    411  CB  ILE A 131      67.995  56.588-177.110  1.00 70.05           C  
ANISOU  411  CB  ILE A 131    13449   5354   7813   2586   4562   1691       C  
ATOM    412  CG1 ILE A 131      66.655  56.590-177.849  1.00 80.09           C  
ANISOU  412  CG1 ILE A 131    14521   6768   9144   2872   4626   1889       C  
ATOM    413  CG2 ILE A 131      68.917  57.672-177.639  1.00 69.59           C  
ANISOU  413  CG2 ILE A 131    13606   5126   7711   2478   4604   1647       C  
ATOM    414  CD1 ILE A 131      66.783  56.399-179.347  1.00 90.26           C  
ANISOU  414  CD1 ILE A 131    15618   8178  10500   2909   4496   1988       C  
ATOM    415  N   ASN A 132      70.134  55.073-175.280  1.00 67.74           N  
ANISOU  415  N   ASN A 132    13259   5013   7467   2033   4275   1332       N  
ATOM    416  CA  ASN A 132      71.423  55.001-174.603  1.00 72.76           C  
ANISOU  416  CA  ASN A 132    14047   5551   8048   1746   4182   1164       C  
ATOM    417  C   ASN A 132      72.254  53.836-175.122  1.00 68.26           C  
ANISOU  417  C   ASN A 132    13260   5120   7556   1584   3940   1127       C  
ATOM    418  O   ASN A 132      73.466  53.974-175.320  1.00 75.88           O  
ANISOU  418  O   ASN A 132    14295   6027   8508   1364   3848   1043       O  
ATOM    419  CB  ASN A 132      71.211  54.878-173.094  1.00 71.83           C  
ANISOU  419  CB  ASN A 132    14077   5369   7848   1697   4249   1075       C  
ATOM    420  CG  ASN A 132      70.508  56.076-172.520  1.00 74.23           C  
ANISOU  420  CG  ASN A 132    14628   5517   8058   1831   4502   1104       C  
ATOM    421  OD1 ASN A 132      70.820  57.211-172.872  1.00 80.83           O  
ANISOU  421  OD1 ASN A 132    15654   6211   8846   1821   4609   1105       O  
ATOM    422  ND2 ASN A 132      69.537  55.837-171.650  1.00 80.98           N  
ANISOU  422  ND2 ASN A 132    15488   6396   8885   1961   4608   1136       N  
ATOM    423  N   GLN A 133      71.625  52.674-175.330  1.00 65.52           N  
ANISOU  423  N   GLN A 133    12649   4957   7287   1683   3838   1193       N  
ATOM    424  CA  GLN A 133      72.338  51.525-175.880  1.00 64.29           C  
ANISOU  424  CA  GLN A 133    12283   4941   7205   1548   3618   1173       C  
ATOM    425  C   GLN A 133      72.948  51.867-177.229  1.00 62.89           C  
ANISOU  425  C   GLN A 133    12055   4776   7062   1512   3567   1224       C  
ATOM    426  O   GLN A 133      74.105  51.536-177.510  1.00 67.39           O  
ANISOU  426  O   GLN A 133    12607   5352   7646   1302   3437   1157       O  
ATOM    427  CB  GLN A 133      71.394  50.334-176.048  1.00 63.26           C  
ANISOU  427  CB  GLN A 133    11879   5008   7148   1695   3540   1261       C  
ATOM    428  CG  GLN A 133      70.982  49.598-174.795  1.00 66.27           C  
ANISOU  428  CG  GLN A 133    12253   5415   7512   1686   3532   1205       C  
ATOM    429  CD  GLN A 133      70.063  48.433-175.132  1.00 70.38           C  
ANISOU  429  CD  GLN A 133    12488   6140   8112   1828   3451   1306       C  
ATOM    430  OE1 GLN A 133      70.447  47.510-175.863  1.00 65.59           O  
ANISOU  430  OE1 GLN A 133    11686   5665   7568   1765   3282   1325       O  
ATOM    431  NE2 GLN A 133      68.829  48.491-174.633  1.00 72.10           N  
ANISOU  431  NE2 GLN A 133    12680   6390   8324   2020   3578   1379       N  
ATOM    432  N   TYR A 134      72.163  52.524-178.080  1.00 63.34           N  
ANISOU  432  N   TYR A 134    12086   4845   7133   1717   3672   1353       N  
ATOM    433  CA  TYR A 134      72.608  52.851-179.429  1.00 57.31           C  
ANISOU  433  CA  TYR A 134    11272   4105   6399   1707   3632   1421       C  
ATOM    434  C   TYR A 134      73.850  53.739-179.409  1.00 59.69           C  
ANISOU  434  C   TYR A 134    11799   4232   6647   1497   3658   1323       C  
ATOM    435  O   TYR A 134      74.843  53.458-180.091  1.00 67.12           O  
ANISOU  435  O   TYR A 134    12682   5207   7614   1334   3541   1299       O  
ATOM    436  CB  TYR A 134      71.462  53.528-180.181  1.00 65.38           C  
ANISOU  436  CB  TYR A 134    12259   5153   7431   1975   3758   1578       C  
ATOM    437  CG  TYR A 134      71.798  53.881-181.609  1.00 71.84           C  
ANISOU  437  CG  TYR A 134    13026   6001   8270   1986   3721   1664       C  
ATOM    438  CD1 TYR A 134      71.412  53.056-182.658  1.00 77.83           C  
ANISOU  438  CD1 TYR A 134    13526   6959   9085   2070   3598   1775       C  
ATOM    439  CD2 TYR A 134      72.501  55.043-181.910  1.00 83.83           C  
ANISOU  439  CD2 TYR A 134    14763   7348   9741   1906   3809   1636       C  
ATOM    440  CE1 TYR A 134      71.721  53.378-183.965  1.00 85.41           C  
ANISOU  440  CE1 TYR A 134    14452   7949  10051   2075   3565   1856       C  
ATOM    441  CE2 TYR A 134      72.817  55.367-183.208  1.00 83.81           C  
ANISOU  441  CE2 TYR A 134    14722   7370   9752   1911   3780   1717       C  
ATOM    442  CZ  TYR A 134      72.424  54.535-184.229  1.00 83.29           C  
ANISOU  442  CZ  TYR A 134    14403   7505   9739   1998   3659   1827       C  
ATOM    443  OH  TYR A 134      72.741  54.866-185.517  1.00 86.21           O  
ANISOU  443  OH  TYR A 134    14748   7899  10108   1998   3632   1909       O  
ATOM    444  N   TYR A 135      73.809  54.824-178.639  1.00 69.41           N  
ANISOU  444  N   TYR A 135    13292   5281   7801   1495   3817   1268       N  
ATOM    445  CA  TYR A 135      74.937  55.744-178.613  1.00 74.97           C  
ANISOU  445  CA  TYR A 135    14220   5818   8447   1294   3851   1180       C  
ATOM    446  C   TYR A 135      76.133  55.194-177.849  1.00 74.08           C  
ANISOU  446  C   TYR A 135    14140   5690   8316   1004   3718   1032       C  
ATOM    447  O   TYR A 135      77.265  55.608-178.126  1.00 68.75           O  
ANISOU  447  O   TYR A 135    13556   4943   7624    799   3680    973       O  
ATOM    448  CB  TYR A 135      74.482  57.097-178.061  1.00 75.78           C  
ANISOU  448  CB  TYR A 135    14601   5729   8461   1385   4070   1175       C  
ATOM    449  CG  TYR A 135      73.747  57.867-179.134  1.00 73.66           C  
ANISOU  449  CG  TYR A 135    14325   5451   8213   1609   4186   1323       C  
ATOM    450  CD1 TYR A 135      74.442  58.645-180.053  1.00 77.98           C  
ANISOU  450  CD1 TYR A 135    14964   5915   8752   1535   4203   1343       C  
ATOM    451  CD2 TYR A 135      72.369  57.757-179.279  1.00 72.51           C  
ANISOU  451  CD2 TYR A 135    14061   5394   8097   1889   4268   1451       C  
ATOM    452  CE1 TYR A 135      73.781  59.326-181.063  1.00 78.42           C  
ANISOU  452  CE1 TYR A 135    15010   5964   8822   1740   4300   1484       C  
ATOM    453  CE2 TYR A 135      71.698  58.438-180.283  1.00 72.56           C  
ANISOU  453  CE2 TYR A 135    14047   5403   8120   2094   4362   1597       C  
ATOM    454  CZ  TYR A 135      72.413  59.214-181.172  1.00 76.47           C  
ANISOU  454  CZ  TYR A 135    14645   5806   8602   2019   4374   1611       C  
ATOM    455  OH  TYR A 135      71.755  59.877-182.170  1.00 70.71           O  
ANISOU  455  OH  TYR A 135    13900   5081   7886   2220   4460   1760       O  
ATOM    456  N   SER A 136      75.917  54.247-176.930  1.00 74.36           N  
ANISOU  456  N   SER A 136    14094   5802   8358    979   3642    978       N  
ATOM    457  CA  SER A 136      77.043  53.528-176.343  1.00 68.97           C  
ANISOU  457  CA  SER A 136    13389   5143   7673    713   3484    858       C  
ATOM    458  C   SER A 136      77.779  52.705-177.391  1.00 64.26           C  
ANISOU  458  C   SER A 136    12571   4682   7161    615   3319    890       C  
ATOM    459  O   SER A 136      79.015  52.739-177.463  1.00 67.80           O  
ANISOU  459  O   SER A 136    13053   5101   7606    377   3237    817       O  
ATOM    460  CB  SER A 136      76.558  52.624-175.207  1.00 76.27           C  
ANISOU  460  CB  SER A 136    14260   6130   8589    731   3436    810       C  
ATOM    461  OG  SER A 136      75.934  53.383-174.184  1.00 88.43           O  
ANISOU  461  OG  SER A 136    16020   7543  10037    805   3598    777       O  
ATOM    462  N   SER A 137      77.033  51.966-178.218  1.00 62.06           N  
ANISOU  462  N   SER A 137    12065   4559   6956    792   3274   1002       N  
ATOM    463  CA  SER A 137      77.634  51.067-179.198  1.00 59.44           C  
ANISOU  463  CA  SER A 137    11518   4372   6696    713   3125   1039       C  
ATOM    464  C   SER A 137      78.462  51.791-180.251  1.00 62.72           C  
ANISOU  464  C   SER A 137    11984   4736   7109    619   3143   1064       C  
ATOM    465  O   SER A 137      79.296  51.152-180.906  1.00 72.61           O  
ANISOU  465  O   SER A 137    13104   6081   8405    483   3028   1063       O  
ATOM    466  CB  SER A 137      76.549  50.248-179.899  1.00 68.98           C  
ANISOU  466  CB  SER A 137    12493   5755   7963    936   3088   1165       C  
ATOM    467  OG  SER A 137      75.801  51.071-180.788  1.00 77.43           O  
ANISOU  467  OG  SER A 137    13583   6810   9029   1132   3200   1282       O  
ATOM    468  N   ILE A 138      78.234  53.084-180.465  1.00 65.64           N  
ANISOU  468  N   ILE A 138    12541   4966   7431    692   3293   1092       N  
ATOM    469  CA  ILE A 138      79.019  53.850-181.427  1.00 73.30           C  
ANISOU  469  CA  ILE A 138    13582   5874   8394    598   3322   1115       C  
ATOM    470  C   ILE A 138      79.963  54.821-180.721  1.00 79.65           C  
ANISOU  470  C   ILE A 138    14636   6495   9132    386   3382    999       C  
ATOM    471  O   ILE A 138      80.431  55.777-181.332  1.00 74.92           O  
ANISOU  471  O   ILE A 138    14163   5796   8508    333   3455   1016       O  
ATOM    472  CB  ILE A 138      78.123  54.594-182.432  1.00 64.31           C  
ANISOU  472  CB  ILE A 138    12457   4724   7254    834   3436   1252       C  
ATOM    473  CG1 ILE A 138      77.118  55.469-181.692  1.00 61.91           C  
ANISOU  473  CG1 ILE A 138    12327   4296   6898   1012   3602   1263       C  
ATOM    474  CG2 ILE A 138      77.414  53.619-183.355  1.00 66.54           C  
ANISOU  474  CG2 ILE A 138    12475   5210   7598    996   3348   1373       C  
ATOM    475  CD1 ILE A 138      76.461  56.499-182.559  1.00 66.17           C  
ANISOU  475  CD1 ILE A 138    12945   4775   7423   1204   3738   1383       C  
ATOM    476  N   LYS A 139      80.231  54.596-179.432  1.00 85.64           N  
ANISOU  476  N   LYS A 139    15475   7210   9854    261   3349    884       N  
ATOM    477  CA  LYS A 139      81.140  55.438-178.650  1.00 90.54           C  
ANISOU  477  CA  LYS A 139    16330   7672  10398     38   3387    768       C  
ATOM    478  C   LYS A 139      80.665  56.887-178.581  1.00 91.67           C  
ANISOU  478  C   LYS A 139    16736   7633  10464    141   3583    785       C  
ATOM    479  O   LYS A 139      81.478  57.815-178.534  1.00 90.35           O  
ANISOU  479  O   LYS A 139    16756   7331  10241    -28   3633    730       O  
ATOM    480  CB  LYS A 139      82.568  55.383-179.207  1.00 92.75           C  
ANISOU  480  CB  LYS A 139    16564   7972  10706   -224   3288    729       C  
ATOM    481  CG  LYS A 139      83.325  54.090-178.942  1.00 92.69           C  
ANISOU  481  CG  LYS A 139    16353   8108  10755   -396   3102    676       C  
ATOM    482  CD  LYS A 139      84.549  53.972-179.850  1.00 94.79           C  
ANISOU  482  CD  LYS A 139    16517   8429  11070   -594   3027    681       C  
ATOM    483  CE  LYS A 139      85.305  55.296-179.978  1.00 98.03           C  
ANISOU  483  CE  LYS A 139    17141   8683  11423   -746   3119    646       C  
ATOM    484  NZ  LYS A 139      86.676  55.225-179.399  1.00 97.13           N  
ANISOU  484  NZ  LYS A 139    17039   8563  11302  -1065   3018    540       N  
ATOM    485  N   ARG A 140      79.350  57.108-178.574  1.00 94.19           N  
ANISOU  485  N   ARG A 140    17069   7944  10776    416   3702    866       N  
ATOM    486  CA  ARG A 140      78.812  58.464-178.619  1.00 98.55           C  
ANISOU  486  CA  ARG A 140    17856   8328  11260    546   3902    903       C  
ATOM    487  C   ARG A 140      77.883  58.752-177.445  1.00 96.55           C  
ANISOU  487  C   ARG A 140    17749   7999  10937    676   4029    875       C  
ATOM    488  O   ARG A 140      76.993  59.600-177.539  1.00 91.64           O  
ANISOU  488  O   ARG A 140    17250   7289  10281    882   4206    946       O  
ATOM    489  CB  ARG A 140      78.100  58.726-179.945  1.00102.14           C  
ANISOU  489  CB  ARG A 140    18209   8832  11767    774   3961   1057       C  
ATOM    490  CG  ARG A 140      78.125  60.183-180.351  1.00107.92           C  
ANISOU  490  CG  ARG A 140    19182   9384  12441    813   4130   1090       C  
ATOM    491  CD  ARG A 140      79.555  60.682-180.452  1.00111.54           C  
ANISOU  491  CD  ARG A 140    19770   9743  12867    517   4091    999       C  
ATOM    492  NE  ARG A 140      80.283  60.007-181.522  1.00111.04           N  
ANISOU  492  NE  ARG A 140    19495   9814  12881    414   3946   1038       N  
ATOM    493  CZ  ARG A 140      81.467  60.395-181.982  1.00106.69           C  
ANISOU  493  CZ  ARG A 140    19001   9212  12323    188   3914   1000       C  
ATOM    494  NH1 ARG A 140      82.067  61.459-181.463  1.00108.42           N  
ANISOU  494  NH1 ARG A 140    19484   9249  12463     34   4006    919       N  
ATOM    495  NH2 ARG A 140      82.050  59.719-182.964  1.00 98.17           N  
ANISOU  495  NH2 ARG A 140    17719   8269  11314    113   3796   1045       N  
ATOM    496  N   SER A 141      78.070  58.045-176.337  1.00 94.83           N  
ANISOU  496  N   SER A 141    17519   7817  10695    561   3947    778       N  
ATOM    497  CA  SER A 141      77.427  58.452-175.102  1.00 94.83           C  
ANISOU  497  CA  SER A 141    17713   7716  10601    625   4077    729       C  
ATOM    498  C   SER A 141      78.070  59.738-174.594  1.00 95.19           C  
ANISOU  498  C   SER A 141    18087   7552  10529    469   4195    645       C  
ATOM    499  O   SER A 141      79.262  59.985-174.794  1.00 91.25           O  
ANISOU  499  O   SER A 141    17643   7010  10017    225   4114    578       O  
ATOM    500  CB  SER A 141      77.535  57.351-174.048  1.00 94.27           C  
ANISOU  500  CB  SER A 141    17553   7738  10526    523   3949    646       C  
ATOM    501  OG  SER A 141      76.930  56.149-174.497  1.00 90.76           O  
ANISOU  501  OG  SER A 141    16813   7484  10187    663   3844    723       O  
ATOM    502  N   GLY A 142      77.261  60.574-173.956  1.00 96.87           N  
ANISOU  502  N   GLY A 142    18519   7635  10653    610   4394    655       N  
ATOM    503  CA  GLY A 142      77.781  61.781-173.347  1.00107.12           C  
ANISOU  503  CA  GLY A 142    20153   8726  11822    466   4519    572       C  
ATOM    504  C   GLY A 142      78.010  62.927-174.310  1.00114.65           C  
ANISOU  504  C   GLY A 142    21237   9555  12769    492   4629    625       C  
ATOM    505  O   GLY A 142      79.143  63.407-174.430  1.00118.31           O  
ANISOU  505  O   GLY A 142    21817   9938  13198    248   4581    553       O  
ATOM    506  N   SER A 143      76.946  63.299-175.042  1.00113.40           N  
ANISOU  506  N   SER A 143    21036   9397  12653    784   4765    761       N  
ATOM    507  CA  SER A 143      76.719  64.570-175.741  1.00112.79           C  
ANISOU  507  CA  SER A 143    21139   9170  12546    898   4943    835       C  
ATOM    508  C   SER A 143      76.445  64.402-177.232  1.00109.39           C  
ANISOU  508  C   SER A 143    20488   8844  12230   1055   4899    974       C  
ATOM    509  O   SER A 143      76.450  63.286-177.766  1.00 96.65           O  
ANISOU  509  O   SER A 143    18581   7424  10719   1071   4730   1013       O  
ATOM    510  CB  SER A 143      77.877  65.565-175.576  1.00115.33           C  
ANISOU  510  CB  SER A 143    21736   9309  12775    634   4975    733       C  
ATOM    511  OG  SER A 143      78.609  65.718-176.785  1.00111.26           O  
ANISOU  511  OG  SER A 143    21135   8812  12326    550   4897    773       O  
ATOM    512  N   GLN A 144      76.189  65.541-177.888  1.00117.55           N  
ANISOU  512  N   GLN A 144    21682   9745  13238   1174   5060   1053       N  
ATOM    513  CA  GLN A 144      75.977  65.688-179.326  1.00116.71           C  
ANISOU  513  CA  GLN A 144    21437   9696  13212   1315   5050   1190       C  
ATOM    514  C   GLN A 144      74.609  65.162-179.746  1.00105.02           C  
ANISOU  514  C   GLN A 144    19731   8367  11806   1636   5073   1341       C  
ATOM    515  O   GLN A 144      73.588  65.539-179.157  1.00105.41           O  
ANISOU  515  O   GLN A 144    19868   8366  11816   1836   5236   1386       O  
ATOM    516  CB  GLN A 144      77.112  65.010-180.109  1.00120.58           C  
ANISOU  516  CB  GLN A 144    21749  10296  13772   1094   4839   1160       C  
ATOM    517  CG  GLN A 144      77.277  65.443-181.578  1.00129.30           C  
ANISOU  517  CG  GLN A 144    22802  11404  14923   1152   4841   1275       C  
ATOM    518  CD  GLN A 144      77.493  66.943-181.774  1.00138.49           C  
ANISOU  518  CD  GLN A 144    24275  12337  16006   1139   5023   1283       C  
ATOM    519  OE1 GLN A 144      77.580  67.714-180.816  1.00147.43           O  
ANISOU  519  OE1 GLN A 144    25678  13296  17042   1074   5153   1196       O  
ATOM    520  NE2 GLN A 144      77.585  67.358-183.032  1.00135.19           N  
ANISOU  520  NE2 GLN A 144    23826  11915  15623   1199   5035   1390       N  
ATOM    521  N   ALA A 145      74.576  64.313-180.779  1.00 87.37           N  
ANISOU  521  N   ALA A 145    17205   6318   9672   1683   4918   1425       N  
ATOM    522  CA  ALA A 145      73.321  63.752-181.259  1.00 83.48           C  
ANISOU  522  CA  ALA A 145    16475   5993   9251   1968   4915   1574       C  
ATOM    523  C   ALA A 145      72.647  62.891-180.200  1.00 89.93           C  
ANISOU  523  C   ALA A 145    17185   6910  10076   2029   4895   1539       C  
ATOM    524  O   ALA A 145      71.432  62.675-180.270  1.00 84.41           O  
ANISOU  524  O   ALA A 145    16352   6308   9410   2283   4955   1658       O  
ATOM    525  CB  ALA A 145      73.567  62.937-182.531  1.00 76.29           C  
ANISOU  525  CB  ALA A 145    15287   5268   8432   1959   4731   1655       C  
ATOM    526  N   HIS A 146      73.414  62.400-179.224  1.00104.62           N  
ANISOU  526  N   HIS A 146    19097   8751  11902   1798   4809   1384       N  
ATOM    527  CA  HIS A 146      72.838  61.673-178.098  1.00 98.70           C  
ANISOU  527  CA  HIS A 146    18290   8069  11142   1837   4804   1339       C  
ATOM    528  C   HIS A 146      71.845  62.549-177.342  1.00 88.52           C  
ANISOU  528  C   HIS A 146    17202   6654   9776   2027   5045   1378       C  
ATOM    529  O   HIS A 146      70.658  62.216-177.232  1.00 81.06           O  
ANISOU  529  O   HIS A 146    16123   5810   8866   2260   5109   1482       O  
ATOM    530  CB  HIS A 146      73.965  61.192-177.181  1.00 93.75           C  
ANISOU  530  CB  HIS A 146    17733   7413  10473   1533   4680   1164       C  
ATOM    531  CG  HIS A 146      73.515  60.257-176.104  1.00 88.69           C  
ANISOU  531  CG  HIS A 146    17006   6863   9829   1542   4633   1115       C  
ATOM    532  ND1 HIS A 146      74.308  59.935-175.024  1.00 87.60           N  
ANISOU  532  ND1 HIS A 146    16972   6683   9631   1302   4557    964       N  
ATOM    533  CD2 HIS A 146      72.358  59.573-175.941  1.00 84.86           C  
ANISOU  533  CD2 HIS A 146    16339   6512   9391   1757   4651   1201       C  
ATOM    534  CE1 HIS A 146      73.659  59.094-174.241  1.00 85.92           C  
ANISOU  534  CE1 HIS A 146    16654   6566   9425   1372   4533    958       C  
ATOM    535  NE2 HIS A 146      72.473  58.859-174.774  1.00 85.34           N  
ANISOU  535  NE2 HIS A 146    16405   6599   9419   1645   4592   1100       N  
ATOM    536  N   GLU A 147      72.315  63.689-176.827  1.00 89.57           N  
ANISOU  536  N   GLU A 147    17663   6567   9803   1926   5189   1301       N  
ATOM    537  CA  GLU A 147      71.427  64.636-176.157  1.00102.64           C  
ANISOU  537  CA  GLU A 147    19544   8081  11375   2102   5440   1343       C  
ATOM    538  C   GLU A 147      70.234  64.987-177.038  1.00 98.73           C  
ANISOU  538  C   GLU A 147    18933   7641  10939   2427   5558   1538       C  
ATOM    539  O   GLU A 147      69.082  64.959-176.587  1.00 87.65           O  
ANISOU  539  O   GLU A 147    17494   6275   9533   2645   5687   1625       O  
ATOM    540  CB  GLU A 147      72.187  65.913-175.795  1.00114.50           C  
ANISOU  540  CB  GLU A 147    21416   9332  12757   1945   5572   1250       C  
ATOM    541  CG  GLU A 147      73.406  65.750-174.906  1.00120.04           C  
ANISOU  541  CG  GLU A 147    22264   9963  13381   1609   5467   1063       C  
ATOM    542  CD  GLU A 147      74.258  67.014-174.884  1.00130.46           C  
ANISOU  542  CD  GLU A 147    23912  11057  14600   1440   5567    990       C  
ATOM    543  OE1 GLU A 147      74.704  67.451-175.969  1.00135.03           O  
ANISOU  543  OE1 GLU A 147    24475  11608  15222   1420   5543   1037       O  
ATOM    544  OE2 GLU A 147      74.465  67.584-173.792  1.00134.06           O  
ANISOU  544  OE2 GLU A 147    24649  11361  14928   1324   5674    891       O  
ATOM    545  N   GLN A 148      70.503  65.311-178.308  1.00 90.05           N  
ANISOU  545  N   GLN A 148    17770   6553   9892   2456   5512   1616       N  
ATOM    546  CA  GLN A 148      69.459  65.760-179.226  1.00 92.80           C  
ANISOU  546  CA  GLN A 148    18027   6944  10287   2750   5616   1807       C  
ATOM    547  C   GLN A 148      68.425  64.664-179.478  1.00 91.48           C  
ANISOU  547  C   GLN A 148    17515   7027  10217   2942   5526   1927       C  
ATOM    548  O   GLN A 148      67.215  64.919-179.435  1.00 91.33           O  
ANISOU  548  O   GLN A 148    17449   7043  10208   3203   5668   2063       O  
ATOM    549  CB  GLN A 148      70.102  66.219-180.541  1.00101.11           C  
ANISOU  549  CB  GLN A 148    19078   7968  11370   2702   5554   1856       C  
ATOM    550  CG  GLN A 148      69.224  67.098-181.433  1.00112.26           C  
ANISOU  550  CG  GLN A 148    20511   9347  12797   2975   5701   2040       C  
ATOM    551  CD  GLN A 148      68.093  66.332-182.096  1.00118.93           C  
ANISOU  551  CD  GLN A 148    21021  10430  13736   3221   5632   2211       C  
ATOM    552  OE1 GLN A 148      68.322  65.486-182.961  1.00122.23           O  
ANISOU  552  OE1 GLN A 148    21189  11024  14227   3179   5434   2248       O  
ATOM    553  NE2 GLN A 148      66.864  66.619-181.683  1.00124.04           N  
ANISOU  553  NE2 GLN A 148    21663  11088  14377   3472   5797   2322       N  
ATOM    554  N   ARG A 149      68.885  63.439-179.767  1.00 87.24           N  
ANISOU  554  N   ARG A 149    16729   6668   9751   2814   5293   1884       N  
ATOM    555  CA  ARG A 149      67.959  62.336-180.019  1.00 83.02           C  
ANISOU  555  CA  ARG A 149    15863   6376   9303   2972   5192   1991       C  
ATOM    556  C   ARG A 149      67.071  62.070-178.807  1.00 78.90           C  
ANISOU  556  C   ARG A 149    15349   5874   8757   3076   5303   1988       C  
ATOM    557  O   ARG A 149      65.898  61.715-178.968  1.00 79.08           O  
ANISOU  557  O   ARG A 149    15174   6042   8830   3301   5336   2130       O  
ATOM    558  CB  ARG A 149      68.743  61.079-180.426  1.00 75.27           C  
ANISOU  558  CB  ARG A 149    14655   5556   8389   2784   4929   1924       C  
ATOM    559  CG  ARG A 149      67.910  59.840-180.787  1.00 73.26           C  
ANISOU  559  CG  ARG A 149    14051   5562   8223   2913   4796   2026       C  
ATOM    560  CD  ARG A 149      66.872  60.108-181.867  1.00 74.55           C  
ANISOU  560  CD  ARG A 149    14058   5836   8432   3174   4838   2231       C  
ATOM    561  NE  ARG A 149      66.087  58.913-182.202  1.00 72.76           N  
ANISOU  561  NE  ARG A 149    13497   5866   8282   3278   4702   2327       N  
ATOM    562  CZ  ARG A 149      64.843  58.956-182.670  1.00 73.95           C  
ANISOU  562  CZ  ARG A 149    13483   6147   8468   3528   4756   2507       C  
ATOM    563  NH1 ARG A 149      64.246  60.133-182.845  1.00 77.65           N  
ANISOU  563  NH1 ARG A 149    14092   6506   8905   3710   4948   2613       N  
ATOM    564  NH2 ARG A 149      64.192  57.837-182.955  1.00 72.34           N  
ANISOU  564  NH2 ARG A 149    12977   6182   8329   3594   4620   2586       N  
ATOM    565  N   LEU A 150      67.600  62.274-177.594  1.00 79.19           N  
ANISOU  565  N   LEU A 150    15617   5765   8708   2912   5365   1835       N  
ATOM    566  CA  LEU A 150      66.799  62.093-176.381  1.00 88.18           C  
ANISOU  566  CA  LEU A 150    16800   6901   9805   2998   5487   1830       C  
ATOM    567  C   LEU A 150      65.597  63.033-176.347  1.00 88.64           C  
ANISOU  567  C   LEU A 150    16948   6895   9838   3278   5738   1983       C  
ATOM    568  O   LEU A 150      64.501  62.638-175.928  1.00 83.04           O  
ANISOU  568  O   LEU A 150    16107   6290   9153   3454   5809   2081       O  
ATOM    569  CB  LEU A 150      67.662  62.319-175.137  1.00 88.81           C  
ANISOU  569  CB  LEU A 150    17157   6811   9775   2759   5518   1641       C  
ATOM    570  CG  LEU A 150      68.800  61.353-174.808  1.00 86.47           C  
ANISOU  570  CG  LEU A 150    16795   6572   9488   2472   5288   1481       C  
ATOM    571  CD1 LEU A 150      69.716  61.985-173.773  1.00 91.48           C  
ANISOU  571  CD1 LEU A 150    17761   7003   9995   2238   5345   1314       C  
ATOM    572  CD2 LEU A 150      68.267  60.028-174.300  1.00 83.15           C  
ANISOU  572  CD2 LEU A 150    16132   6338   9122   2504   5178   1487       C  
ATOM    573  N   GLN A 151      65.783  64.289-176.763  1.00 95.45           N  
ANISOU  573  N   GLN A 151    18037   7579  10650   3320   5881   2011       N  
ATOM    574  CA  GLN A 151      64.680  65.241-176.668  1.00102.04           C  
ANISOU  574  CA  GLN A 151    18983   8332  11454   3585   6134   2156       C  
ATOM    575  C   GLN A 151      63.614  64.972-177.720  1.00 90.47           C  
ANISOU  575  C   GLN A 151    17218   7062  10095   3848   6109   2369       C  
ATOM    576  O   GLN A 151      62.422  65.167-177.456  1.00 90.49           O  
ANISOU  576  O   GLN A 151    17171   7104  10107   4083   6264   2510       O  
ATOM    577  CB  GLN A 151      65.184  66.680-176.798  1.00116.38           C  
ANISOU  577  CB  GLN A 151    21144   9893  13183   3555   6301   2126       C  
ATOM    578  CG  GLN A 151      66.675  66.879-176.580  1.00125.48           C  
ANISOU  578  CG  GLN A 151    22505  10902  14269   3234   6206   1928       C  
ATOM    579  CD  GLN A 151      67.116  66.665-175.141  1.00134.15           C  
ANISOU  579  CD  GLN A 151    23786  11914  15272   3039   6227   1761       C  
ATOM    580  OE1 GLN A 151      66.299  66.435-174.248  1.00142.65           O  
ANISOU  580  OE1 GLN A 151    24864  13017  16322   3147   6333   1790       O  
ATOM    581  NE2 GLN A 151      68.423  66.741-174.912  1.00132.27           N  
ANISOU  581  NE2 GLN A 151    23702  11578  14978   2743   6121   1592       N  
ATOM    582  N   GLU A 152      64.016  64.523-178.909  1.00 87.08           N  
ANISOU  582  N   GLU A 152    16584   6759   9741   3808   5913   2402       N  
ATOM    583  CA  GLU A 152      63.043  64.353-179.983  1.00 97.79           C  
ANISOU  583  CA  GLU A 152    17673   8298  11185   4047   5882   2610       C  
ATOM    584  C   GLU A 152      62.108  63.180-179.709  1.00 90.20           C  
ANISOU  584  C   GLU A 152    16401   7578  10293   4148   5799   2688       C  
ATOM    585  O   GLU A 152      60.905  63.272-179.979  1.00 87.40           O  
ANISOU  585  O   GLU A 152    15896   7333   9979   4394   5883   2872       O  
ATOM    586  CB  GLU A 152      63.750  64.181-181.325  1.00106.01           C  
ANISOU  586  CB  GLU A 152    18598   9408  12275   3964   5694   2626       C  
ATOM    587  CG  GLU A 152      62.950  64.750-182.485  1.00116.50           C  
ANISOU  587  CG  GLU A 152    19826  10797  13641   4207   5744   2836       C  
ATOM    588  CD  GLU A 152      63.729  64.758-183.778  1.00121.37           C  
ANISOU  588  CD  GLU A 152    20390  11442  14283   4112   5585   2848       C  
ATOM    589  OE1 GLU A 152      64.518  63.811-183.990  1.00119.11           O  
ANISOU  589  OE1 GLU A 152    19974  11256  14027   3912   5375   2749       O  
ATOM    590  OE2 GLU A 152      63.561  65.713-184.571  1.00122.43           O  
ANISOU  590  OE2 GLU A 152    20619  11494  14404   4235   5676   2959       O  
ATOM    591  N   VAL A 153      62.628  62.071-179.174  1.00 82.94           N  
ANISOU  591  N   VAL A 153    15378   6746   9389   3959   5635   2556       N  
ATOM    592  CA  VAL A 153      61.720  61.005-178.760  1.00 81.65           C  
ANISOU  592  CA  VAL A 153    14953   6789   9281   4047   5581   2623       C  
ATOM    593  C   VAL A 153      60.806  61.505-177.648  1.00 83.93           C  
ANISOU  593  C   VAL A 153    15379   6992   9519   4191   5822   2674       C  
ATOM    594  O   VAL A 153      59.597  61.253-177.673  1.00 84.78           O  
ANISOU  594  O   VAL A 153    15294   7244   9676   4398   5879   2839       O  
ATOM    595  CB  VAL A 153      62.487  59.725-178.363  1.00 84.01           C  
ANISOU  595  CB  VAL A 153    15134   7184   9604   3814   5364   2470       C  
ATOM    596  CG1 VAL A 153      63.176  59.117-179.588  1.00 76.05           C  
ANISOU  596  CG1 VAL A 153    13938   6300   8659   3711   5127   2465       C  
ATOM    597  CG2 VAL A 153      63.496  59.991-177.261  1.00 84.56           C  
ANISOU  597  CG2 VAL A 153    15497   7049   9583   3589   5407   2264       C  
ATOM    598  N   GLU A 154      61.357  62.264-176.690  1.00 85.19           N  
ANISOU  598  N   GLU A 154    15878   6914   9575   4084   5972   2543       N  
ATOM    599  CA  GLU A 154      60.537  62.904-175.660  1.00 88.80           C  
ANISOU  599  CA  GLU A 154    16515   7256   9968   4221   6228   2596       C  
ATOM    600  C   GLU A 154      59.412  63.725-176.279  1.00 91.40           C  
ANISOU  600  C   GLU A 154    16803   7598  10327   4519   6400   2817       C  
ATOM    601  O   GLU A 154      58.241  63.581-175.908  1.00 92.05           O  
ANISOU  601  O   GLU A 154    16768   7769  10437   4710   6511   2960       O  
ATOM    602  CB  GLU A 154      61.400  63.806-174.773  1.00101.53           C  
ANISOU  602  CB  GLU A 154    18535   8590  11452   4056   6364   2429       C  
ATOM    603  CG  GLU A 154      62.023  63.143-173.554  1.00108.51           C  
ANISOU  603  CG  GLU A 154    19518   9437  12274   3827   6300   2247       C  
ATOM    604  CD  GLU A 154      62.805  64.130-172.693  1.00116.93           C  
ANISOU  604  CD  GLU A 154    20998  10230  13199   3668   6443   2098       C  
ATOM    605  OE1 GLU A 154      62.174  64.953-171.990  1.00119.47           O  
ANISOU  605  OE1 GLU A 154    21541  10410  13444   3790   6691   2152       O  
ATOM    606  OE2 GLU A 154      64.054  64.087-172.730  1.00117.69           O  
ANISOU  606  OE2 GLU A 154    21200  10256  13260   3416   6306   1933       O  
ATOM    607  N   ALA A 155      59.758  64.608-177.219  1.00 93.53           N  
ANISOU  607  N   ALA A 155    17171   7775  10592   4559   6426   2853       N  
ATOM    608  CA  ALA A 155      58.744  65.450-177.845  1.00 95.46           C  
ANISOU  608  CA  ALA A 155    17389   8019  10861   4843   6587   3065       C  
ATOM    609  C   ALA A 155      57.800  64.621-178.707  1.00 97.21           C  
ANISOU  609  C   ALA A 155    17205   8533  11198   5008   6448   3249       C  
ATOM    610  O   ALA A 155      56.587  64.858-178.708  1.00 99.62           O  
ANISOU  610  O   ALA A 155    17405   8910  11536   5252   6579   3438       O  
ATOM    611  CB  ALA A 155      59.408  66.550-178.673  1.00 96.99           C  
ANISOU  611  CB  ALA A 155    17791   8042  11020   4830   6632   3055       C  
ATOM    612  N   GLU A 156      58.338  63.634-179.432  1.00 91.42           N  
ANISOU  612  N   GLU A 156    16239   7971  10525   4872   6182   3201       N  
ATOM    613  CA  GLU A 156      57.500  62.792-180.282  1.00 90.54           C  
ANISOU  613  CA  GLU A 156    15743   8145  10513   5001   6030   3367       C  
ATOM    614  C   GLU A 156      56.459  62.045-179.458  1.00 90.36           C  
ANISOU  614  C   GLU A 156    15539   8269  10524   5094   6067   3442       C  
ATOM    615  O   GLU A 156      55.282  61.980-179.831  1.00 91.86           O  
ANISOU  615  O   GLU A 156    15513   8619  10771   5309   6100   3646       O  
ATOM    616  CB  GLU A 156      58.369  61.808-181.063  1.00 87.18           C  
ANISOU  616  CB  GLU A 156    15136   7857  10130   4806   5742   3276       C  
ATOM    617  CG  GLU A 156      58.175  61.845-182.562  1.00 95.08           C  
ANISOU  617  CG  GLU A 156    15946   8997  11184   4902   5617   3421       C  
ATOM    618  CD  GLU A 156      59.209  61.006-183.287  1.00 96.39           C  
ANISOU  618  CD  GLU A 156    16000   9250  11373   4685   5356   3313       C  
ATOM    619  OE1 GLU A 156      58.822  60.035-183.969  1.00 98.07           O  
ANISOU  619  OE1 GLU A 156    15907   9709  11648   4704   5170   3395       O  
ATOM    620  OE2 GLU A 156      60.413  61.310-183.155  1.00100.53           O  
ANISOU  620  OE2 GLU A 156    16746   9599  11851   4490   5339   3147       O  
ATOM    621  N   VAL A 157      56.878  61.463-178.332  1.00 88.62           N  
ANISOU  621  N   VAL A 157    15402   8001  10268   4927   6057   3286       N  
ATOM    622  CA  VAL A 157      55.921  60.801-177.451  1.00 88.93           C  
ANISOU  622  CA  VAL A 157    15304   8153  10332   5004   6110   3354       C  
ATOM    623  C   VAL A 157      54.983  61.825-176.819  1.00 92.31           C  
ANISOU  623  C   VAL A 157    15901   8451  10721   5218   6404   3480       C  
ATOM    624  O   VAL A 157      53.768  61.611-176.760  1.00 93.64           O  
ANISOU  624  O   VAL A 157    15872   8762  10946   5409   6464   3663       O  
ATOM    625  CB  VAL A 157      56.652  59.959-176.392  1.00 85.96           C  
ANISOU  625  CB  VAL A 157    14999   7742   9919   4768   6028   3153       C  
ATOM    626  CG1 VAL A 157      55.656  59.354-175.418  1.00 86.22           C  
ANISOU  626  CG1 VAL A 157    14923   7866   9969   4848   6103   3229       C  
ATOM    627  CG2 VAL A 157      57.454  58.856-177.063  1.00 82.44           C  
ANISOU  627  CG2 VAL A 157    14348   7448   9526   4583   5736   3055       C  
ATOM    628  N   ALA A 158      55.523  62.951-176.347  1.00 94.17           N  
ANISOU  628  N   ALA A 158    16504   8414  10862   5187   6590   3391       N  
ATOM    629  CA  ALA A 158      54.670  64.006-175.803  1.00 97.96           C  
ANISOU  629  CA  ALA A 158    17170   8750  11301   5396   6882   3514       C  
ATOM    630  C   ALA A 158      53.608  64.428-176.814  1.00103.23           C  
ANISOU  630  C   ALA A 158    17636   9541  12044   5674   6929   3763       C  
ATOM    631  O   ALA A 158      52.430  64.567-176.472  1.00102.59           O  
ANISOU  631  O   ALA A 158    17470   9514  11994   5884   7077   3936       O  
ATOM    632  CB  ALA A 158      55.517  65.207-175.375  1.00 99.68           C  
ANISOU  632  CB  ALA A 158    17817   8656  11402   5309   7053   3380       C  
ATOM    633  N   ALA A 159      54.002  64.596-178.079  1.00116.53           N  
ANISOU  633  N   ALA A 159    19232  11282  13763   5676   6794   3791       N  
ATOM    634  CA  ALA A 159      53.069  65.042-179.111  1.00121.70           C  
ANISOU  634  CA  ALA A 159    19708  12051  14482   5931   6823   4025       C  
ATOM    635  C   ALA A 159      52.150  63.916-179.580  1.00123.19           C  
ANISOU  635  C   ALA A 159    19467  12566  14774   6013   6647   4175       C  
ATOM    636  O   ALA A 159      50.922  64.051-179.541  1.00126.64           O  
ANISOU  636  O   ALA A 159    19756  13104  15258   6239   6754   4377       O  
ATOM    637  CB  ALA A 159      53.840  65.629-180.297  1.00124.15           C  
ANISOU  637  CB  ALA A 159    20092  12297  14783   5894   6738   4004       C  
ATOM    638  N   THR A 160      52.724  62.795-180.028  1.00117.80           N  
ANISOU  638  N   THR A 160    18579  12051  14128   5828   6377   4082       N  
ATOM    639  CA  THR A 160      51.938  61.748-180.670  1.00112.85           C  
ANISOU  639  CA  THR A 160    17547  11739  13593   5888   6185   4222       C  
ATOM    640  C   THR A 160      51.636  60.554-179.772  1.00100.77           C  
ANISOU  640  C   THR A 160    15856  10342  12090   5793   6112   4174       C  
ATOM    641  O   THR A 160      50.708  59.798-180.074  1.00100.53           O  
ANISOU  641  O   THR A 160    15504  10560  12133   5880   6011   4320       O  
ATOM    642  CB  THR A 160      52.646  61.239-181.934  1.00119.15           C  
ANISOU  642  CB  THR A 160    18191  12664  14417   5766   5921   4183       C  
ATOM    643  OG1 THR A 160      53.828  60.513-181.569  1.00122.87           O  
ANISOU  643  OG1 THR A 160    18736  13088  14862   5494   5778   3953       O  
ATOM    644  CG2 THR A 160      53.028  62.400-182.841  1.00117.10           C  
ANISOU  644  CG2 THR A 160    18104  12261  14127   5842   5983   4225       C  
ATOM    645  N   GLY A 161      52.382  60.358-178.688  1.00 96.84           N  
ANISOU  645  N   GLY A 161    15571   9689  11533   5613   6154   3977       N  
ATOM    646  CA  GLY A 161      52.189  59.214-177.824  1.00 97.64           C  
ANISOU  646  CA  GLY A 161    15541   9901  11656   5509   6077   3921       C  
ATOM    647  C   GLY A 161      53.053  58.018-178.156  1.00 98.05           C  
ANISOU  647  C   GLY A 161    15443  10079  11731   5278   5800   3775       C  
ATOM    648  O   GLY A 161      53.240  57.146-177.300  1.00 94.54           O  
ANISOU  648  O   GLY A 161    14977   9661  11284   5142   5743   3670       O  
ATOM    649  N   THR A 162      53.572  57.947-179.376  1.00 95.22           N  
ANISOU  649  N   THR A 162    14985   9798  11396   5234   5629   3771       N  
ATOM    650  CA  THR A 162      54.531  56.920-179.751  1.00 91.51           C  
ANISOU  650  CA  THR A 162    14411   9417  10942   5010   5376   3624       C  
ATOM    651  C   THR A 162      55.745  57.614-180.356  1.00 91.14           C  
ANISOU  651  C   THR A 162    14581   9197  10850   4898   5346   3502       C  
ATOM    652  O   THR A 162      55.893  58.832-180.208  1.00 84.91           O  
ANISOU  652  O   THR A 162    14057   8198  10008   4967   5535   3500       O  
ATOM    653  CB  THR A 162      53.901  55.925-180.734  1.00 94.96           C  
ANISOU  653  CB  THR A 162    14463  10160  11459   5050   5160   3757       C  
ATOM    654  OG1 THR A 162      54.835  54.880-181.050  1.00 84.86           O  
ANISOU  654  OG1 THR A 162    13090   8959  10192   4832   4922   3613       O  
ATOM    655  CG2 THR A 162      53.473  56.639-182.017  1.00 97.60           C  
ANISOU  655  CG2 THR A 162    14713  10558  11811   5214   5155   3927       C  
ATOM    656  N   TYR A 163      56.622  56.869-181.025  1.00 90.21           N  
ANISOU  656  N   TYR A 163    14364   9158  10752   4723   5115   3403       N  
ATOM    657  CA  TYR A 163      57.746  57.492-181.709  1.00 89.89           C  
ANISOU  657  CA  TYR A 163    14505   8971  10677   4615   5073   3309       C  
ATOM    658  C   TYR A 163      58.209  56.581-182.835  1.00 82.23           C  
ANISOU  658  C   TYR A 163    13308   8183   9752   4508   4807   3306       C  
ATOM    659  O   TYR A 163      57.906  55.385-182.862  1.00 81.61           O  
ANISOU  659  O   TYR A 163    12977   8310   9720   4465   4649   3320       O  
ATOM    660  CB  TYR A 163      58.902  57.808-180.747  1.00 84.97           C  
ANISOU  660  CB  TYR A 163    14195   8103   9986   4416   5138   3086       C  
ATOM    661  CG  TYR A 163      59.704  56.609-180.280  1.00 83.37           C  
ANISOU  661  CG  TYR A 163    13925   7957   9795   4185   4953   2917       C  
ATOM    662  CD1 TYR A 163      59.218  55.771-179.281  1.00 76.53           C  
ANISOU  662  CD1 TYR A 163    12965   7171   8942   4170   4954   2894       C  
ATOM    663  CD2 TYR A 163      60.962  56.330-180.815  1.00 76.00           C  
ANISOU  663  CD2 TYR A 163    13030   6986   8859   3979   4785   2786       C  
ATOM    664  CE1 TYR A 163      59.943  54.686-178.844  1.00 70.86           C  
ANISOU  664  CE1 TYR A 163    12192   6497   8235   3967   4788   2745       C  
ATOM    665  CE2 TYR A 163      61.701  55.235-180.379  1.00 73.72           C  
ANISOU  665  CE2 TYR A 163    12680   6745   8585   3773   4618   2640       C  
ATOM    666  CZ  TYR A 163      61.181  54.418-179.391  1.00 74.30           C  
ANISOU  666  CZ  TYR A 163    12662   6899   8672   3771   4620   2619       C  
ATOM    667  OH  TYR A 163      61.890  53.330-178.936  1.00 67.52           O  
ANISOU  667  OH  TYR A 163    11746   6082   7826   3575   4458   2479       O  
ATOM    668  N   GLN A 164      58.943  57.174-183.769  1.00 82.54           N  
ANISOU  668  N   GLN A 164    13450   8139   9771   4464   4764   3292       N  
ATOM    669  CA  GLN A 164      59.501  56.471-184.911  1.00 78.75           C  
ANISOU  669  CA  GLN A 164    12805   7800   9318   4354   4528   3290       C  
ATOM    670  C   GLN A 164      61.002  56.301-184.718  1.00 76.77           C  
ANISOU  670  C   GLN A 164    12729   7403   9039   4096   4445   3081       C  
ATOM    671  O   GLN A 164      61.691  57.238-184.301  1.00 74.01           O  
ANISOU  671  O   GLN A 164    12666   6816   8638   4033   4575   2983       O  
ATOM    672  CB  GLN A 164      59.220  57.232-186.214  1.00 77.11           C  
ANISOU  672  CB  GLN A 164    12572   7620   9106   4490   4530   3448       C  
ATOM    673  CG  GLN A 164      57.762  57.612-186.411  1.00 89.00           C  
ANISOU  673  CG  GLN A 164    13934   9245  10637   4756   4633   3667       C  
ATOM    674  CD  GLN A 164      56.840  56.406-186.411  1.00 91.51           C  
ANISOU  674  CD  GLN A 164    13915   9844  11009   4796   4499   3757       C  
ATOM    675  OE1 GLN A 164      57.094  55.417-187.100  1.00 84.95           O  
ANISOU  675  OE1 GLN A 164    12888   9189  10199   4687   4278   3746       O  
ATOM    676  NE2 GLN A 164      55.762  56.482-185.632  1.00 94.37           N  
ANISOU  676  NE2 GLN A 164    14216  10249  11393   4948   4638   3848       N  
ATOM    677  N   LEU A 165      61.500  55.099-185.007  1.00 70.08           N  
ANISOU  677  N   LEU A 165    11707   6699   8221   3941   4228   3015       N  
ATOM    678  CA  LEU A 165      62.933  54.845-184.985  1.00 68.07           C  
ANISOU  678  CA  LEU A 165    11580   6337   7948   3693   4125   2839       C  
ATOM    679  C   LEU A 165      63.599  55.377-186.252  1.00 71.46           C  
ANISOU  679  C   LEU A 165    12065   6729   8358   3651   4066   2875       C  
ATOM    680  O   LEU A 165      63.061  55.244-187.356  1.00 69.09           O  
ANISOU  680  O   LEU A 165    11590   6589   8074   3757   3985   3023       O  
ATOM    681  CB  LEU A 165      63.214  53.348-184.873  1.00 65.08           C  
ANISOU  681  CB  LEU A 165    10993   6126   7606   3551   3920   2769       C  
ATOM    682  CG  LEU A 165      62.937  52.658-183.538  1.00 65.75           C  
ANISOU  682  CG  LEU A 165    11054   6223   7705   3516   3945   2685       C  
ATOM    683  CD1 LEU A 165      62.979  51.148-183.706  1.00 65.40           C  
ANISOU  683  CD1 LEU A 165    10757   6386   7705   3420   3732   2666       C  
ATOM    684  CD2 LEU A 165      63.945  53.138-182.502  1.00 63.77           C  
ANISOU  684  CD2 LEU A 165    11091   5730   7407   3354   4031   2499       C  
ATOM    685  N   ARG A 166      64.780  55.974-186.087  1.00 68.50           N  
ANISOU  685  N   ARG A 166    11936   6146   7943   3486   4103   2741       N  
ATOM    686  CA  ARG A 166      65.646  56.214-187.233  1.00 71.18           C  
ANISOU  686  CA  ARG A 166    12315   6463   8267   3383   4013   2747       C  
ATOM    687  C   ARG A 166      66.050  54.884-187.864  1.00 68.38           C  
ANISOU  687  C   ARG A 166    11732   6308   7943   3254   3781   2731       C  
ATOM    688  O   ARG A 166      66.059  53.838-187.212  1.00 66.21           O  
ANISOU  688  O   ARG A 166    11336   6125   7696   3177   3691   2657       O  
ATOM    689  CB  ARG A 166      66.897  56.990-186.817  1.00 68.63           C  
ANISOU  689  CB  ARG A 166    12287   5891   7899   3196   4088   2594       C  
ATOM    690  CG  ARG A 166      66.619  58.383-186.271  1.00 73.87           C  
ANISOU  690  CG  ARG A 166    13214   6337   8517   3303   4323   2602       C  
ATOM    691  CD  ARG A 166      67.901  59.066-185.810  1.00 71.81           C  
ANISOU  691  CD  ARG A 166    13239   5840   8204   3085   4379   2439       C  
ATOM    692  NE  ARG A 166      67.664  60.460-185.454  1.00 78.13           N  
ANISOU  692  NE  ARG A 166    14306   6429   8950   3185   4603   2456       N  
ATOM    693  CZ  ARG A 166      68.575  61.275-184.931  1.00 75.62           C  
ANISOU  693  CZ  ARG A 166    14273   5885   8573   3027   4696   2328       C  
ATOM    694  NH1 ARG A 166      69.806  60.836-184.686  1.00 73.82           N  
ANISOU  694  NH1 ARG A 166    14090   5620   8338   2756   4579   2175       N  
ATOM    695  NH2 ARG A 166      68.248  62.536-184.654  1.00 78.52           N  
ANISOU  695  NH2 ARG A 166    14881   6067   8886   3138   4908   2358       N  
ATOM    696  N   GLU A 167      66.400  54.936-189.152  1.00 68.89           N  
ANISOU  696  N   GLU A 167    11749   6434   7993   3228   3688   2803       N  
ATOM    697  CA  GLU A 167      66.748  53.715-189.874  1.00 67.44           C  
ANISOU  697  CA  GLU A 167    11357   6445   7822   3114   3477   2803       C  
ATOM    698  C   GLU A 167      67.944  53.016-189.240  1.00 66.84           C  
ANISOU  698  C   GLU A 167    11332   6311   7753   2866   3397   2621       C  
ATOM    699  O   GLU A 167      67.948  51.789-189.093  1.00 64.08           O  
ANISOU  699  O   GLU A 167    10803   6114   7430   2796   3259   2587       O  
ATOM    700  CB  GLU A 167      67.032  54.035-191.344  1.00 72.36           C  
ANISOU  700  CB  GLU A 167    11969   7114   8409   3112   3415   2904       C  
ATOM    701  CG  GLU A 167      66.971  52.835-192.280  1.00 83.19           C  
ANISOU  701  CG  GLU A 167    13097   8733   9780   3064   3210   2959       C  
ATOM    702  CD  GLU A 167      66.923  53.252-193.747  1.00102.63           C  
ANISOU  702  CD  GLU A 167    15543  11260  12193   3114   3167   3094       C  
ATOM    703  OE1 GLU A 167      67.564  52.585-194.588  1.00110.99           O  
ANISOU  703  OE1 GLU A 167    16531  12422  13221   2980   3029   3084       O  
ATOM    704  OE2 GLU A 167      66.248  54.258-194.058  1.00107.67           O  
ANISOU  704  OE2 GLU A 167    16247  11845  12819   3289   3275   3214       O  
ATOM    705  N   SER A 168      68.968  53.779-188.853  1.00 61.63           N  
ANISOU  705  N   SER A 168    10915   5435   7068   2724   3482   2506       N  
ATOM    706  CA  SER A 168      70.144  53.175-188.231  1.00 59.65           C  
ANISOU  706  CA  SER A 168    10713   5128   6822   2479   3406   2338       C  
ATOM    707  C   SER A 168      69.814  52.566-186.877  1.00 59.49           C  
ANISOU  707  C   SER A 168    10663   5112   6829   2472   3413   2249       C  
ATOM    708  O   SER A 168      70.432  51.570-186.479  1.00 61.20           O  
ANISOU  708  O   SER A 168    10805   5384   7064   2311   3295   2150       O  
ATOM    709  CB  SER A 168      71.243  54.220-188.080  1.00 67.17           C  
ANISOU  709  CB  SER A 168    11933   5851   7737   2328   3502   2243       C  
ATOM    710  OG  SER A 168      70.795  55.313-187.293  1.00 68.70           O  
ANISOU  710  OG  SER A 168    12326   5870   7907   2431   3686   2231       O  
ATOM    711  N   GLU A 169      68.859  53.154-186.152  1.00 62.39           N  
ANISOU  711  N   GLU A 169    11094   5420   7192   2642   3558   2286       N  
ATOM    712  CA  GLU A 169      68.426  52.556-184.893  1.00 59.21           C  
ANISOU  712  CA  GLU A 169    10655   5034   6807   2651   3573   2217       C  
ATOM    713  C   GLU A 169      67.656  51.268-185.138  1.00 57.64           C  
ANISOU  713  C   GLU A 169    10162   5083   6656   2724   3436   2294       C  
ATOM    714  O   GLU A 169      67.797  50.304-184.380  1.00 62.28           O  
ANISOU  714  O   GLU A 169    10676   5724   7266   2632   3356   2210       O  
ATOM    715  CB  GLU A 169      67.569  53.545-184.103  1.00 61.48           C  
ANISOU  715  CB  GLU A 169    11090   5200   7069   2820   3783   2250       C  
ATOM    716  CG  GLU A 169      68.256  54.866-183.797  1.00 63.99           C  
ANISOU  716  CG  GLU A 169    11719   5266   7330   2752   3933   2174       C  
ATOM    717  CD  GLU A 169      67.289  55.926-183.289  1.00 71.04           C  
ANISOU  717  CD  GLU A 169    12751   6052   8190   2955   4154   2244       C  
ATOM    718  OE1 GLU A 169      66.061  55.737-183.432  1.00 74.41           O  
ANISOU  718  OE1 GLU A 169    13012   6614   8645   3168   4190   2381       O  
ATOM    719  OE2 GLU A 169      67.762  56.951-182.753  1.00 68.80           O  
ANISOU  719  OE2 GLU A 169    12742   5553   7847   2898   4294   2165       O  
ATOM    720  N   LEU A 170      66.823  51.238-186.184  1.00 62.13           N  
ANISOU  720  N   LEU A 170    10565   5807   7236   2884   3403   2456       N  
ATOM    721  CA  LEU A 170      66.110  50.008-186.502  1.00 59.57           C  
ANISOU  721  CA  LEU A 170     9956   5729   6947   2936   3260   2531       C  
ATOM    722  C   LEU A 170      67.090  48.897-186.834  1.00 56.75           C  
ANISOU  722  C   LEU A 170     9512   5454   6597   2730   3074   2445       C  
ATOM    723  O   LEU A 170      66.925  47.752-186.393  1.00 58.87           O  
ANISOU  723  O   LEU A 170     9631   5844   6893   2685   2971   2411       O  
ATOM    724  CB  LEU A 170      65.144  50.238-187.659  1.00 66.53           C  
ANISOU  724  CB  LEU A 170    10686   6765   7828   3120   3244   2720       C  
ATOM    725  CG  LEU A 170      64.436  48.996-188.205  1.00 70.23           C  
ANISOU  725  CG  LEU A 170    10856   7507   8320   3155   3076   2809       C  
ATOM    726  CD1 LEU A 170      63.429  48.420-187.200  1.00 71.23           C  
ANISOU  726  CD1 LEU A 170    10854   7724   8487   3247   3107   2827       C  
ATOM    727  CD2 LEU A 170      63.767  49.341-189.528  1.00 75.92           C  
ANISOU  727  CD2 LEU A 170    11464   8362   9020   3290   3040   2985       C  
ATOM    728  N   VAL A 171      68.147  49.235-187.572  1.00 57.40           N  
ANISOU  728  N   VAL A 171     9696   5462   6650   2600   3040   2408       N  
ATOM    729  CA  VAL A 171      69.183  48.265-187.910  1.00 56.88           C  
ANISOU  729  CA  VAL A 171     9566   5462   6584   2397   2887   2328       C  
ATOM    730  C   VAL A 171      69.894  47.778-186.656  1.00 57.77           C  
ANISOU  730  C   VAL A 171     9754   5481   6715   2236   2875   2167       C  
ATOM    731  O   VAL A 171      70.045  46.572-186.434  1.00 52.70           O  
ANISOU  731  O   VAL A 171     8972   4957   6095   2153   2750   2125       O  
ATOM    732  CB  VAL A 171      70.171  48.888-188.899  1.00 56.23           C  
ANISOU  732  CB  VAL A 171     9599   5303   6464   2292   2887   2326       C  
ATOM    733  CG1 VAL A 171      71.411  48.038-188.990  1.00 55.36           C  
ANISOU  733  CG1 VAL A 171     9467   5216   6352   2060   2771   2219       C  
ATOM    734  CG2 VAL A 171      69.494  49.041-190.234  1.00 54.59           C  
ANISOU  734  CG2 VAL A 171     9277   5234   6230   2429   2851   2488       C  
ATOM    735  N   PHE A 172      70.370  48.712-185.837  1.00 56.38           N  
ANISOU  735  N   PHE A 172     9807   5090   6523   2182   3002   2075       N  
ATOM    736  CA  PHE A 172      71.078  48.333-184.625  1.00 58.93           C  
ANISOU  736  CA  PHE A 172    10220   5319   6852   2017   2988   1922       C  
ATOM    737  C   PHE A 172      70.181  47.510-183.705  1.00 58.32           C  
ANISOU  737  C   PHE A 172    10022   5333   6804   2102   2968   1921       C  
ATOM    738  O   PHE A 172      70.632  46.536-183.092  1.00 58.98           O  
ANISOU  738  O   PHE A 172    10051   5454   6904   1972   2869   1833       O  
ATOM    739  CB  PHE A 172      71.588  49.591-183.923  1.00 60.62           C  
ANISOU  739  CB  PHE A 172    10711   5293   7027   1958   3136   1836       C  
ATOM    740  CG  PHE A 172      71.946  49.381-182.484  1.00 58.25           C  
ANISOU  740  CG  PHE A 172    10520   4893   6718   1840   3152   1696       C  
ATOM    741  CD1 PHE A 172      73.206  48.934-182.126  1.00 56.33           C  
ANISOU  741  CD1 PHE A 172    10324   4606   6473   1596   3058   1570       C  
ATOM    742  CD2 PHE A 172      71.021  49.648-181.489  1.00 59.67           C  
ANISOU  742  CD2 PHE A 172    10758   5027   6886   1972   3266   1697       C  
ATOM    743  CE1 PHE A 172      73.531  48.746-180.793  1.00 59.03           C  
ANISOU  743  CE1 PHE A 172    10770   4862   6798   1481   3062   1445       C  
ATOM    744  CE2 PHE A 172      71.341  49.462-180.161  1.00 63.76           C  
ANISOU  744  CE2 PHE A 172    11391   5454   7381   1859   3281   1570       C  
ATOM    745  CZ  PHE A 172      72.599  49.016-179.815  1.00 58.67           C  
ANISOU  745  CZ  PHE A 172    10795   4767   6731   1612   3172   1443       C  
ATOM    746  N   GLY A 173      68.898  47.865-183.629  1.00 61.23           N  
ANISOU  746  N   GLY A 173    10339   5747   7178   2320   3063   2028       N  
ATOM    747  CA  GLY A 173      67.993  47.157-182.741  1.00 59.33           C  
ANISOU  747  CA  GLY A 173     9987   5592   6963   2405   3065   2037       C  
ATOM    748  C   GLY A 173      67.688  45.749-183.210  1.00 60.40           C  
ANISOU  748  C   GLY A 173     9857   5956   7136   2396   2891   2086       C  
ATOM    749  O   GLY A 173      67.499  44.840-182.394  1.00 54.38           O  
ANISOU  749  O   GLY A 173     9018   5249   6395   2359   2839   2038       O  
ATOM    750  N   ALA A 174      67.623  45.549-184.527  1.00 54.65           N  
ANISOU  750  N   ALA A 174     8993   5364   6407   2426   2801   2184       N  
ATOM    751  CA  ALA A 174      67.377  44.214-185.065  1.00 50.44           C  
ANISOU  751  CA  ALA A 174     8219   5054   5893   2404   2631   2230       C  
ATOM    752  C   ALA A 174      68.539  43.285-184.758  1.00 47.88           C  
ANISOU  752  C   ALA A 174     7907   4716   5572   2186   2514   2100       C  
ATOM    753  O   ALA A 174      68.342  42.155-184.297  1.00 48.22           O  
ANISOU  753  O   ALA A 174     7820   4864   5636   2148   2421   2075       O  
ATOM    754  CB  ALA A 174      67.139  44.292-186.574  1.00 54.06           C  
ANISOU  754  CB  ALA A 174     8561   5651   6329   2467   2564   2356       C  
ATOM    755  N   LYS A 175      69.768  43.752-185.000  1.00 50.21           N  
ANISOU  755  N   LYS A 175     8353   4880   5843   2036   2521   2019       N  
ATOM    756  CA  LYS A 175      70.941  42.968-184.631  1.00 47.65           C  
ANISOU  756  CA  LYS A 175     8052   4531   5523   1822   2428   1896       C  
ATOM    757  C   LYS A 175      70.992  42.714-183.129  1.00 47.28           C  
ANISOU  757  C   LYS A 175     8082   4387   5493   1766   2455   1789       C  
ATOM    758  O   LYS A 175      71.462  41.656-182.701  1.00 46.32           O  
ANISOU  758  O   LYS A 175     7895   4317   5386   1644   2352   1721       O  
ATOM    759  CB  LYS A 175      72.218  43.671-185.096  1.00 47.82           C  
ANISOU  759  CB  LYS A 175     8229   4422   5519   1671   2455   1836       C  
ATOM    760  CG  LYS A 175      72.330  43.813-186.618  1.00 46.60           C  
ANISOU  760  CG  LYS A 175     8005   4365   5337   1697   2418   1932       C  
ATOM    761  CD  LYS A 175      73.511  44.696-187.000  1.00 48.57           C  
ANISOU  761  CD  LYS A 175     8427   4466   5561   1559   2476   1879       C  
ATOM    762  CE  LYS A 175      73.636  44.821-188.514  1.00 61.26           C  
ANISOU  762  CE  LYS A 175     9973   6169   7132   1580   2445   1975       C  
ATOM    763  NZ  LYS A 175      74.818  45.643-188.890  1.00 67.81           N  
ANISOU  763  NZ  LYS A 175    10965   6859   7940   1434   2504   1925       N  
ATOM    764  N   GLN A 176      70.524  43.666-182.315  1.00 48.71           N  
ANISOU  764  N   GLN A 176     8412   4430   5665   1851   2598   1773       N  
ATOM    765  CA  GLN A 176      70.585  43.474-180.866  1.00 44.57           C  
ANISOU  765  CA  GLN A 176     7985   3810   5141   1791   2630   1667       C  
ATOM    766  C   GLN A 176      69.609  42.401-180.408  1.00 48.10           C  
ANISOU  766  C   GLN A 176     8252   4405   5619   1881   2576   1711       C  
ATOM    767  O   GLN A 176      69.953  41.560-179.568  1.00 52.60           O  
ANISOU  767  O   GLN A 176     8814   4975   6198   1770   2506   1626       O  
ATOM    768  CB  GLN A 176      70.306  44.789-180.138  1.00 54.42           C  
ANISOU  768  CB  GLN A 176     9450   4873   6353   1861   2811   1641       C  
ATOM    769  CG  GLN A 176      71.514  45.694-179.991  1.00 65.73           C  
ANISOU  769  CG  GLN A 176    11112   6117   7745   1695   2856   1536       C  
ATOM    770  CD  GLN A 176      72.654  45.042-179.238  1.00 66.00           C  
ANISOU  770  CD  GLN A 176    11199   6104   7776   1458   2754   1397       C  
ATOM    771  OE1 GLN A 176      73.614  44.572-179.838  1.00 73.36           O  
ANISOU  771  OE1 GLN A 176    12072   7078   8722   1311   2644   1371       O  
ATOM    772  NE2 GLN A 176      72.556  45.020-177.912  1.00 70.16           N  
ANISOU  772  NE2 GLN A 176    11837   6545   8277   1420   2795   1310       N  
ATOM    773  N   ALA A 177      68.375  42.440-180.918  1.00 49.85           N  
ANISOU  773  N   ALA A 177     8329   4755   5857   2079   2609   1847       N  
ATOM    774  CA  ALA A 177      67.403  41.410-180.574  1.00 57.64           C  
ANISOU  774  CA  ALA A 177     9123   5901   6875   2160   2555   1902       C  
ATOM    775  C   ALA A 177      67.901  40.031-180.980  1.00 55.26           C  
ANISOU  775  C   ALA A 177     8664   5744   6590   2034   2368   1882       C  
ATOM    776  O   ALA A 177      67.718  39.064-180.240  1.00 46.69           O  
ANISOU  776  O   ALA A 177     7506   4711   5521   1995   2308   1847       O  
ATOM    777  CB  ALA A 177      66.054  41.706-181.226  1.00 54.12           C  
ANISOU  777  CB  ALA A 177     8527   5592   6443   2377   2609   2066       C  
ATOM    778  N   TRP A 178      68.549  39.917-182.147  1.00 47.19           N  
ANISOU  778  N   TRP A 178     7594   4782   5554   1967   2281   1903       N  
ATOM    779  CA  TRP A 178      69.153  38.637-182.514  1.00 43.31           C  
ANISOU  779  CA  TRP A 178     6979   4413   5065   1834   2121   1873       C  
ATOM    780  C   TRP A 178      70.256  38.254-181.530  1.00 55.27           C  
ANISOU  780  C   TRP A 178     8617   5802   6582   1648   2094   1728       C  
ATOM    781  O   TRP A 178      70.284  37.130-181.012  1.00 48.77           O  
ANISOU  781  O   TRP A 178     7708   5049   5773   1585   2005   1693       O  
ATOM    782  CB  TRP A 178      69.693  38.689-183.953  1.00 43.52           C  
ANISOU  782  CB  TRP A 178     6956   4516   5062   1795   2059   1921       C  
ATOM    783  CG  TRP A 178      70.321  37.393-184.442  1.00 47.24           C  
ANISOU  783  CG  TRP A 178     7305   5122   5522   1666   1911   1895       C  
ATOM    784  CD1 TRP A 178      70.263  36.157-183.837  1.00 48.03           C  
ANISOU  784  CD1 TRP A 178     7307   5305   5639   1608   1821   1857       C  
ATOM    785  CD2 TRP A 178      71.099  37.216-185.637  1.00 42.39           C  
ANISOU  785  CD2 TRP A 178     6662   4573   4869   1581   1852   1906       C  
ATOM    786  NE1 TRP A 178      70.959  35.229-184.591  1.00 49.67           N  
ANISOU  786  NE1 TRP A 178     7393   5643   5836   1475   1684   1789       N  
ATOM    787  CE2 TRP A 178      71.478  35.859-185.697  1.00 48.35           C  
ANISOU  787  CE2 TRP A 178     7279   5464   5629   1466   1715   1836       C  
ATOM    788  CE3 TRP A 178      71.507  38.079-186.669  1.00 44.44           C  
ANISOU  788  CE3 TRP A 178     6990   4800   5096   1583   1896   1944       C  
ATOM    789  CZ2 TRP A 178      72.254  35.347-186.739  1.00 46.96           C  
ANISOU  789  CZ2 TRP A 178     7024   5390   5427   1353   1624   1787       C  
ATOM    790  CZ3 TRP A 178      72.278  37.573-187.691  1.00 48.18           C  
ANISOU  790  CZ3 TRP A 178     7415   5362   5528   1482   1828   1942       C  
ATOM    791  CH2 TRP A 178      72.639  36.215-187.725  1.00 48.37           C  
ANISOU  791  CH2 TRP A 178     7293   5526   5559   1369   1694   1857       C  
ATOM    792  N   ARG A 179      71.175  39.186-181.265  1.00 51.87           N  
ANISOU  792  N   ARG A 179     8387   5188   6135   1553   2167   1645       N  
ATOM    793  CA  ARG A 179      72.259  38.962-180.307  1.00 44.72           C  
ANISOU  793  CA  ARG A 179     7608   4156   5226   1364   2141   1508       C  
ATOM    794  C   ARG A 179      71.740  38.547-178.936  1.00 47.51           C  
ANISOU  794  C   ARG A 179     7989   4475   5587   1379   2155   1458       C  
ATOM    795  O   ARG A 179      72.393  37.768-178.228  1.00 45.27           O  
ANISOU  795  O   ARG A 179     7720   4172   5307   1237   2076   1371       O  
ATOM    796  CB  ARG A 179      73.075  40.251-180.191  1.00 42.93           C  
ANISOU  796  CB  ARG A 179     7599   3739   4973   1282   2238   1441       C  
ATOM    797  CG  ARG A 179      74.282  40.201-179.272  1.00 49.43           C  
ANISOU  797  CG  ARG A 179     8564   4431   5787   1066   2208   1302       C  
ATOM    798  CD  ARG A 179      74.855  41.616-179.126  1.00 51.24           C  
ANISOU  798  CD  ARG A 179     9012   4477   5982   1007   2318   1249       C  
ATOM    799  NE  ARG A 179      76.203  41.619-178.570  1.00 51.87           N  
ANISOU  799  NE  ARG A 179     9202   4454   6050    769   2270   1127       N  
ATOM    800  CZ  ARG A 179      76.897  42.715-178.283  1.00 55.27           C  
ANISOU  800  CZ  ARG A 179     9826   4727   6445    663   2341   1059       C  
ATOM    801  NH1 ARG A 179      76.378  43.922-178.510  1.00 58.88           N  
ANISOU  801  NH1 ARG A 179    10404   5097   6872    782   2475   1099       N  
ATOM    802  NH2 ARG A 179      78.117  42.603-177.780  1.00 56.35           N  
ANISOU  802  NH2 ARG A 179    10035   4800   6578    434   2276    954       N  
ATOM    803  N   ASN A 180      70.579  39.056-178.546  1.00 43.75           N  
ANISOU  803  N   ASN A 180     7522   3991   5110   1550   2261   1515       N  
ATOM    804  CA  ASN A 180      70.030  38.795-177.226  1.00 47.57           C  
ANISOU  804  CA  ASN A 180     8053   4431   5592   1575   2304   1472       C  
ATOM    805  C   ASN A 180      69.197  37.520-177.154  1.00 43.80           C  
ANISOU  805  C   ASN A 180     7365   4130   5147   1639   2218   1536       C  
ATOM    806  O   ASN A 180      68.731  37.190-176.067  1.00 47.64           O  
ANISOU  806  O   ASN A 180     7879   4590   5632   1654   2250   1506       O  
ATOM    807  CB  ASN A 180      69.180  39.990-176.768  1.00 45.60           C  
ANISOU  807  CB  ASN A 180     7926   4079   5320   1730   2488   1504       C  
ATOM    808  CG  ASN A 180      70.022  41.211-176.439  1.00 46.14           C  
ANISOU  808  CG  ASN A 180     8247   3942   5340   1639   2582   1412       C  
ATOM    809  OD1 ASN A 180      71.221  41.096-176.178  1.00 49.51           O  
ANISOU  809  OD1 ASN A 180     8772   4289   5751   1442   2510   1304       O  
ATOM    810  ND2 ASN A 180      69.392  42.386-176.433  1.00 46.13           N  
ANISOU  810  ND2 ASN A 180     8353   3859   5315   1780   2747   1458       N  
ATOM    811  N   ALA A 181      68.978  36.825-178.268  1.00 44.45           N  
ANISOU  811  N   ALA A 181     7247   4391   5250   1671   2116   1624       N  
ATOM    812  CA  ALA A 181      68.106  35.652-178.299  1.00 44.98           C  
ANISOU  812  CA  ALA A 181     7104   4643   5342   1732   2033   1696       C  
ATOM    813  C   ALA A 181      68.751  34.474-177.570  1.00 40.99           C  
ANISOU  813  C   ALA A 181     6578   4154   4843   1567   1912   1585       C  
ATOM    814  O   ALA A 181      69.678  33.859-178.115  1.00 41.90           O  
ANISOU  814  O   ALA A 181     6621   4337   4963   1421   1776   1501       O  
ATOM    815  CB  ALA A 181      67.797  35.261-179.744  1.00 47.41           C  
ANISOU  815  CB  ALA A 181     7217   5143   5653   1786   1942   1805       C  
ATOM    816  N   PRO A 182      68.292  34.110-176.373  1.00 43.61           N  
ANISOU  816  N   PRO A 182     6940   4451   5178   1573   1940   1550       N  
ATOM    817  CA  PRO A 182      69.018  33.088-175.593  1.00 41.40           C  
ANISOU  817  CA  PRO A 182     6645   4183   4902   1391   1810   1402       C  
ATOM    818  C   PRO A 182      69.018  31.710-176.236  1.00 44.10           C  
ANISOU  818  C   PRO A 182     6743   4739   5275   1322   1626   1379       C  
ATOM    819  O   PRO A 182      69.933  30.910-175.992  1.00 41.77           O  
ANISOU  819  O   PRO A 182     6426   4456   4987   1161   1499   1258       O  
ATOM    820  CB  PRO A 182      68.274  33.077-174.245  1.00 41.06           C  
ANISOU  820  CB  PRO A 182     6688   4066   4847   1449   1905   1401       C  
ATOM    821  CG  PRO A 182      67.514  34.359-174.194  1.00 44.20           C  
ANISOU  821  CG  PRO A 182     7212   4352   5231   1630   2107   1507       C  
ATOM    822  CD  PRO A 182      67.150  34.668-175.629  1.00 45.46           C  
ANISOU  822  CD  PRO A 182     7224   4635   5413   1735   2094   1619       C  
ATOM    823  N   ARG A 183      68.022  31.395-177.046  1.00 39.17           N  
ANISOU  823  N   ARG A 183     5935   4282   4665   1437   1607   1495       N  
ATOM    824  CA  ARG A 183      67.931  30.052-177.579  1.00 43.45           C  
ANISOU  824  CA  ARG A 183     6265   5018   5228   1363   1440   1469       C  
ATOM    825  C   ARG A 183      68.621  29.888-178.926  1.00 36.92           C  
ANISOU  825  C   ARG A 183     5358   4275   4393   1302   1345   1457       C  
ATOM    826  O   ARG A 183      68.572  28.792-179.490  1.00 40.44           O  
ANISOU  826  O   ARG A 183     5642   4877   4848   1239   1211   1432       O  
ATOM    827  CB  ARG A 183      66.462  29.637-177.676  1.00 44.09           C  
ANISOU  827  CB  ARG A 183     6174   5254   5324   1489   1450   1592       C  
ATOM    828  CG  ARG A 183      65.809  29.520-176.306  1.00 45.26           C  
ANISOU  828  CG  ARG A 183     6374   5340   5481   1527   1531   1588       C  
ATOM    829  CD  ARG A 183      64.311  29.311-176.372  1.00 45.52           C  
ANISOU  829  CD  ARG A 183     6240   5519   5537   1669   1573   1729       C  
ATOM    830  NE  ARG A 183      63.832  28.908-175.058  1.00 43.42           N  
ANISOU  830  NE  ARG A 183     6007   5212   5279   1663   1625   1700       N  
ATOM    831  CZ  ARG A 183      62.555  28.760-174.722  1.00 46.12           C  
ANISOU  831  CZ  ARG A 183     6233   5646   5643   1778   1695   1808       C  
ATOM    832  NH1 ARG A 183      61.591  28.984-175.604  1.00 40.55           N  
ANISOU  832  NH1 ARG A 183     5357   5091   4959   1912   1713   1960       N  
ATOM    833  NH2 ARG A 183      62.246  28.365-173.495  1.00 48.36           N  
ANISOU  833  NH2 ARG A 183     6567   5880   5926   1753   1746   1767       N  
ATOM    834  N   CYS A 184      69.273  30.928-179.452  1.00 39.20           N  
ANISOU  834  N   CYS A 184     5769   4461   4662   1311   1416   1469       N  
ATOM    835  CA  CYS A 184      69.843  30.868-180.794  1.00 35.02           C  
ANISOU  835  CA  CYS A 184     5172   4015   4117   1268   1348   1474       C  
ATOM    836  C   CYS A 184      71.325  30.508-180.727  1.00 41.24           C  
ANISOU  836  C   CYS A 184     6010   4742   4916   1087   1272   1324       C  
ATOM    837  O   CYS A 184      72.128  31.250-180.147  1.00 40.01           O  
ANISOU  837  O   CYS A 184     6021   4420   4759   1028   1339   1267       O  
ATOM    838  CB  CYS A 184      69.652  32.196-181.534  1.00 38.05           C  
ANISOU  838  CB  CYS A 184     5648   4336   4472   1387   1472   1593       C  
ATOM    839  SG  CYS A 184      70.299  32.236-183.284  1.00 40.96           S  
ANISOU  839  SG  CYS A 184     5951   4808   4804   1343   1407   1617       S  
ATOM    840  N   VAL A 185      71.688  29.388-181.360  1.00 41.23           N  
ANISOU  840  N   VAL A 185     5865   4877   4924    999   1136   1265       N  
ATOM    841  CA  VAL A 185      73.077  28.941-181.393  1.00 40.58           C  
ANISOU  841  CA  VAL A 185     5797   4760   4861    843   1061   1133       C  
ATOM    842  C   VAL A 185      73.884  29.583-182.518  1.00 44.40           C  
ANISOU  842  C   VAL A 185     6314   5232   5325    813   1093   1142       C  
ATOM    843  O   VAL A 185      75.114  29.403-182.569  1.00 40.62           O  
ANISOU  843  O   VAL A 185     5852   4714   4868    688   1055   1042       O  
ATOM    844  CB  VAL A 185      73.105  27.404-181.506  1.00 38.05           C  
ANISOU  844  CB  VAL A 185     5319   4575   4562    771    916   1062       C  
ATOM    845  CG1 VAL A 185      72.736  26.975-182.926  1.00 35.24           C  
ANISOU  845  CG1 VAL A 185     4835   4380   4175    800    864   1115       C  
ATOM    846  CG2 VAL A 185      74.459  26.852-181.096  1.00 34.05           C  
ANISOU  846  CG2 VAL A 185     4831   4013   4094    626    844    925       C  
ATOM    847  N   GLY A 186      73.248  30.345-183.409  1.00 40.53           N  
ANISOU  847  N   GLY A 186     5831   4774   4794    926   1165   1265       N  
ATOM    848  CA  GLY A 186      73.957  30.931-184.540  1.00 38.16           C  
ANISOU  848  CA  GLY A 186     5566   4469   4464    899   1198   1283       C  
ATOM    849  C   GLY A 186      74.408  32.367-184.352  1.00 40.91           C  
ANISOU  849  C   GLY A 186     6104   4638   4802    911   1336   1314       C  
ATOM    850  O   GLY A 186      74.716  33.053-185.333  1.00 41.41           O  
ANISOU  850  O   GLY A 186     6211   4691   4830    923   1391   1369       O  
ATOM    851  N   ARG A 187      74.478  32.833-183.098  1.00 39.12           N  
ANISOU  851  N   ARG A 187     6006   4261   4598    898   1396   1277       N  
ATOM    852  CA  ARG A 187      74.672  34.255-182.838  1.00 42.34           C  
ANISOU  852  CA  ARG A 187     6619   4483   4986    925   1542   1319       C  
ATOM    853  C   ARG A 187      76.096  34.730-183.089  1.00 46.87           C  
ANISOU  853  C   ARG A 187     7283   4962   5563    770   1558   1240       C  
ATOM    854  O   ARG A 187      76.356  35.930-182.948  1.00 44.47           O  
ANISOU  854  O   ARG A 187     7162   4494   5239    769   1680   1268       O  
ATOM    855  CB  ARG A 187      74.262  34.586-181.399  1.00 40.94           C  
ANISOU  855  CB  ARG A 187     6567   4169   4817    954   1607   1299       C  
ATOM    856  CG  ARG A 187      72.758  34.606-181.183  1.00 43.19           C  
ANISOU  856  CG  ARG A 187     6810   4505   5096   1142   1659   1416       C  
ATOM    857  CD  ARG A 187      72.405  34.924-179.736  1.00 43.27           C  
ANISOU  857  CD  ARG A 187     6958   4373   5109   1165   1739   1387       C  
ATOM    858  NE  ARG A 187      72.541  33.753-178.863  1.00 42.03           N  
ANISOU  858  NE  ARG A 187     6715   4276   4977   1069   1621   1282       N  
ATOM    859  CZ  ARG A 187      72.535  33.808-177.534  1.00 42.95           C  
ANISOU  859  CZ  ARG A 187     6953   4278   5089   1034   1655   1221       C  
ATOM    860  NH1 ARG A 187      72.409  34.976-176.920  1.00 43.89           N  
ANISOU  860  NH1 ARG A 187     7290   4208   5177   1083   1809   1244       N  
ATOM    861  NH2 ARG A 187      72.650  32.697-176.820  1.00 40.49           N  
ANISOU  861  NH2 ARG A 187     6557   4032   4797    949   1540   1136       N  
ATOM    862  N   ILE A 188      77.026  33.842-183.446  1.00 44.37           N  
ANISOU  862  N   ILE A 188     6845   4739   5274    639   1447   1143       N  
ATOM    863  CA  ILE A 188      78.322  34.305-183.920  1.00 43.96           C  
ANISOU  863  CA  ILE A 188     6846   4628   5228    505   1471   1091       C  
ATOM    864  C   ILE A 188      78.136  35.241-185.115  1.00 43.25           C  
ANISOU  864  C   ILE A 188     6818   4527   5088    580   1574   1203       C  
ATOM    865  O   ILE A 188      78.967  36.125-185.356  1.00 42.10           O  
ANISOU  865  O   ILE A 188     6792   4270   4934    497   1654   1196       O  
ATOM    866  CB  ILE A 188      79.223  33.092-184.272  1.00 43.58           C  
ANISOU  866  CB  ILE A 188     6627   4710   5221    387   1342    986       C  
ATOM    867  CG1 ILE A 188      80.689  33.504-184.429  1.00 45.05           C  
ANISOU  867  CG1 ILE A 188     6855   4829   5434    225   1363    914       C  
ATOM    868  CG2 ILE A 188      78.775  32.451-185.589  1.00 42.27           C  
ANISOU  868  CG2 ILE A 188     6319   4715   5024    458   1301   1039       C  
ATOM    869  CD1 ILE A 188      81.366  33.922-183.167  1.00 47.65           C  
ANISOU  869  CD1 ILE A 188     7297   5016   5792    107   1366    839       C  
ATOM    870  N   GLN A 189      77.023  35.098-185.835  1.00 43.38           N  
ANISOU  870  N   GLN A 189     6762   4654   5067    733   1573   1315       N  
ATOM    871  CA  GLN A 189      76.718  35.845-187.054  1.00 45.15           C  
ANISOU  871  CA  GLN A 189     7024   4898   5233    821   1649   1440       C  
ATOM    872  C   GLN A 189      75.955  37.142-186.796  1.00 49.36           C  
ANISOU  872  C   GLN A 189     7729   5286   5739    961   1792   1563       C  
ATOM    873  O   GLN A 189      75.525  37.785-187.756  1.00 48.28           O  
ANISOU  873  O   GLN A 189     7627   5166   5553   1064   1855   1690       O  
ATOM    874  CB  GLN A 189      75.887  34.973-187.993  1.00 46.70           C  
ANISOU  874  CB  GLN A 189     7043   5305   5395    910   1557   1504       C  
ATOM    875  CG  GLN A 189      76.623  33.805-188.610  1.00 43.96           C  
ANISOU  875  CG  GLN A 189     6549   5098   5054    791   1442   1402       C  
ATOM    876  CD  GLN A 189      77.548  34.251-189.718  1.00 47.55           C  
ANISOU  876  CD  GLN A 189     7045   5548   5472    718   1492   1405       C  
ATOM    877  OE1 GLN A 189      77.302  35.263-190.373  1.00 50.84           O  
ANISOU  877  OE1 GLN A 189     7564   5917   5836    790   1587   1518       O  
ATOM    878  NE2 GLN A 189      78.623  33.507-189.928  1.00 46.71           N  
ANISOU  878  NE2 GLN A 189     6862   5490   5396    581   1436   1285       N  
ATOM    879  N   TRP A 190      75.760  37.535-185.531  1.00 46.82           N  
ANISOU  879  N   TRP A 190     7525   4821   5445    972   1848   1533       N  
ATOM    880  CA  TRP A 190      74.762  38.561-185.231  1.00 50.61           C  
ANISOU  880  CA  TRP A 190     8129   5193   5906   1141   1972   1642       C  
ATOM    881  C   TRP A 190      75.065  39.911-185.873  1.00 46.26           C  
ANISOU  881  C   TRP A 190     7712   4533   5334   1153   2069   1667       C  
ATOM    882  O   TRP A 190      74.137  40.698-186.079  1.00 51.91           O  
ANISOU  882  O   TRP A 190     8451   5233   6040   1313   2134   1746       O  
ATOM    883  CB  TRP A 190      74.605  38.728-183.724  1.00 51.48           C  
ANISOU  883  CB  TRP A 190     8342   5171   6047   1128   2008   1563       C  
ATOM    884  CG  TRP A 190      75.744  39.415-183.040  1.00 53.94           C  
ANISOU  884  CG  TRP A 190     8840   5292   6362    961   2059   1450       C  
ATOM    885  CD1 TRP A 190      76.836  38.828-182.467  1.00 56.13           C  
ANISOU  885  CD1 TRP A 190     9127   5539   6660    767   1992   1336       C  
ATOM    886  CD2 TRP A 190      75.882  40.817-182.820  1.00 52.43           C  
ANISOU  886  CD2 TRP A 190     8835   4931   6153    965   2174   1427       C  
ATOM    887  NE1 TRP A 190      77.650  39.782-181.914  1.00 57.31           N  
ANISOU  887  NE1 TRP A 190     9473   5503   6801    643   2063   1265       N  
ATOM    888  CE2 TRP A 190      77.087  41.014-182.119  1.00 53.81           C  
ANISOU  888  CE2 TRP A 190     9139   4975   6331    759   2171   1308       C  
ATOM    889  CE3 TRP A 190      75.104  41.928-183.147  1.00 52.53           C  
ANISOU  889  CE3 TRP A 190     8920   4891   6146   1122   2280   1499       C  
ATOM    890  CZ2 TRP A 190      77.532  42.276-181.744  1.00 53.53           C  
ANISOU  890  CZ2 TRP A 190     9304   4763   6273    697   2266   1254       C  
ATOM    891  CZ3 TRP A 190      75.553  43.182-182.788  1.00 57.56           C  
ANISOU  891  CZ3 TRP A 190     9764   5342   6762   1071   2386   1446       C  
ATOM    892  CH2 TRP A 190      76.755  43.346-182.092  1.00 60.47           C  
ANISOU  892  CH2 TRP A 190    10262   5587   7127    856   2377   1322       C  
ATOM    893  N   GLY A 191      76.328  40.198-186.202  1.00 52.01           N  
ANISOU  893  N   GLY A 191     8522   5187   6054    988   2088   1608       N  
ATOM    894  CA  GLY A 191      76.667  41.476-186.802  1.00 54.32           C  
ANISOU  894  CA  GLY A 191     8948   5369   6323    984   2181   1630       C  
ATOM    895  C   GLY A 191      76.384  41.571-188.286  1.00 50.00           C  
ANISOU  895  C   GLY A 191     8320   4943   5733   1066   2171   1740       C  
ATOM    896  O   GLY A 191      76.310  42.683-188.822  1.00 53.00           O  
ANISOU  896  O   GLY A 191     8804   5243   6090   1118   2252   1788       O  
ATOM    897  N   LYS A 192      76.219  40.431-188.953  1.00 49.40           N  
ANISOU  897  N   LYS A 192     8072   5059   5638   1076   2074   1779       N  
ATOM    898  CA  LYS A 192      75.920  40.362-190.379  1.00 50.38           C  
ANISOU  898  CA  LYS A 192     8112   5324   5705   1143   2045   1879       C  
ATOM    899  C   LYS A 192      74.430  40.073-190.532  1.00 56.89           C  
ANISOU  899  C   LYS A 192     8812   6284   6520   1337   1993   1985       C  
ATOM    900  O   LYS A 192      74.004  38.914-190.535  1.00 50.88           O  
ANISOU  900  O   LYS A 192     7897   5682   5753   1353   1893   1996       O  
ATOM    901  CB  LYS A 192      76.781  39.299-191.053  1.00 52.59           C  
ANISOU  901  CB  LYS A 192     8293   5733   5957   1009   1981   1842       C  
ATOM    902  CG  LYS A 192      76.844  39.412-192.582  1.00 69.80           C  
ANISOU  902  CG  LYS A 192    10438   8023   8060   1026   1973   1920       C  
ATOM    903  CD  LYS A 192      75.628  38.798-193.273  1.00 81.46           C  
ANISOU  903  CD  LYS A 192    11767   9698   9485   1172   1879   2025       C  
ATOM    904  CE  LYS A 192      74.643  39.836-193.830  1.00 85.52           C  
ANISOU  904  CE  LYS A 192    12319  10201   9975   1336   1910   2147       C  
ATOM    905  NZ  LYS A 192      73.368  39.221-194.326  1.00 77.03           N  
ANISOU  905  NZ  LYS A 192    11082   9325   8861   1472   1806   2250       N  
ATOM    906  N   LEU A 193      73.637  41.134-190.667  1.00 56.35           N  
ANISOU  906  N   LEU A 193     8806   6156   6449   1483   2063   2065       N  
ATOM    907  CA  LEU A 193      72.192  41.005-190.799  1.00 56.46           C  
ANISOU  907  CA  LEU A 193     8695   6295   6463   1673   2028   2176       C  
ATOM    908  C   LEU A 193      71.697  42.083-191.748  1.00 51.07           C  
ANISOU  908  C   LEU A 193     8060   5602   5743   1795   2086   2290       C  
ATOM    909  O   LEU A 193      71.964  43.268-191.528  1.00 51.98           O  
ANISOU  909  O   LEU A 193     8344   5538   5869   1810   2205   2278       O  
ATOM    910  CB  LEU A 193      71.492  41.130-189.435  1.00 48.88           C  
ANISOU  910  CB  LEU A 193     7753   5255   5562   1755   2078   2147       C  
ATOM    911  CG  LEU A 193      69.961  41.069-189.435  1.00 49.00           C  
ANISOU  911  CG  LEU A 193     7633   5395   5590   1953   2066   2263       C  
ATOM    912  CD1 LEU A 193      69.477  39.687-189.879  1.00 48.38           C  
ANISOU  912  CD1 LEU A 193     7335   5554   5494   1948   1915   2304       C  
ATOM    913  CD2 LEU A 193      69.398  41.423-188.054  1.00 52.04           C  
ANISOU  913  CD2 LEU A 193     8079   5667   6029   2029   2160   2226       C  
ATOM    914  N   GLN A 194      70.980  41.672-192.793  1.00 55.76           N  
ANISOU  914  N   GLN A 194     8510   6387   6289   1876   2000   2401       N  
ATOM    915  CA  GLN A 194      70.394  42.599-193.756  1.00 54.07           C  
ANISOU  915  CA  GLN A 194     8320   6191   6035   2003   2037   2527       C  
ATOM    916  C   GLN A 194      68.981  42.965-193.307  1.00 61.19           C  
ANISOU  916  C   GLN A 194     9147   7127   6974   2204   2071   2623       C  
ATOM    917  O   GLN A 194      68.103  42.096-193.232  1.00 51.53           O  
ANISOU  917  O   GLN A 194     7740   6079   5759   2263   1977   2670       O  
ATOM    918  CB  GLN A 194      70.367  41.983-195.156  1.00 60.22           C  
ANISOU  918  CB  GLN A 194     8988   7165   6727   1974   1921   2599       C  
ATOM    919  CG  GLN A 194      69.514  42.752-196.143  1.00 70.99           C  
ANISOU  919  CG  GLN A 194    10336   8591   8045   2121   1927   2750       C  
ATOM    920  CD  GLN A 194      70.107  44.104-196.481  1.00 81.12           C  
ANISOU  920  CD  GLN A 194    11820   9685   9314   2121   2055   2763       C  
ATOM    921  OE1 GLN A 194      71.293  44.345-196.249  1.00 75.82           O  
ANISOU  921  OE1 GLN A 194    11288   8870   8652   1978   2116   2658       O  
ATOM    922  NE2 GLN A 194      69.285  44.996-197.027  1.00 88.89           N  
ANISOU  922  NE2 GLN A 194    12820  10674  10280   2279   2095   2894       N  
ATOM    923  N   VAL A 195      68.757  44.250-193.036  1.00 57.84           N  
ANISOU  923  N   VAL A 195     8864   6541   6570   2306   2210   2655       N  
ATOM    924  CA  VAL A 195      67.501  44.748-192.480  1.00 59.60           C  
ANISOU  924  CA  VAL A 195     9043   6767   6834   2500   2284   2737       C  
ATOM    925  C   VAL A 195      66.740  45.487-193.580  1.00 62.58           C  
ANISOU  925  C   VAL A 195     9390   7218   7171   2649   2297   2898       C  
ATOM    926  O   VAL A 195      67.165  46.560-194.028  1.00 66.70           O  
ANISOU  926  O   VAL A 195    10075   7601   7667   2661   2388   2919       O  
ATOM    927  CB  VAL A 195      67.746  45.659-191.268  1.00 59.21           C  
ANISOU  927  CB  VAL A 195     9187   6480   6830   2514   2447   2652       C  
ATOM    928  CG1 VAL A 195      66.436  46.273-190.784  1.00 64.33           C  
ANISOU  928  CG1 VAL A 195     9803   7131   7509   2728   2552   2749       C  
ATOM    929  CG2 VAL A 195      68.442  44.887-190.151  1.00 52.55           C  
ANISOU  929  CG2 VAL A 195     8369   5577   6022   2364   2420   2499       C  
ATOM    930  N   PHE A 196      65.607  44.924-194.010  1.00 63.09           N  
ANISOU  930  N   PHE A 196     9243   7500   7229   2757   2204   3015       N  
ATOM    931  CA  PHE A 196      64.731  45.573-194.986  1.00 61.46           C  
ANISOU  931  CA  PHE A 196     8981   7385   6987   2910   2206   3182       C  
ATOM    932  C   PHE A 196      63.646  46.345-194.249  1.00 60.79           C  
ANISOU  932  C   PHE A 196     8889   7251   6958   3107   2341   3260       C  
ATOM    933  O   PHE A 196      62.850  45.756-193.511  1.00 60.77           O  
ANISOU  933  O   PHE A 196     8742   7344   7002   3163   2327   3269       O  
ATOM    934  CB  PHE A 196      64.080  44.561-195.932  1.00 68.36           C  
ANISOU  934  CB  PHE A 196     9626   8537   7812   2906   2023   3274       C  
ATOM    935  CG  PHE A 196      65.051  43.833-196.814  1.00 74.78           C  
ANISOU  935  CG  PHE A 196    10449   9416   8549   2727   1899   3215       C  
ATOM    936  CD1 PHE A 196      65.816  44.523-197.742  1.00 74.22           C  
ANISOU  936  CD1 PHE A 196    10526   9261   8413   2678   1928   3230       C  
ATOM    937  CD2 PHE A 196      65.181  42.455-196.731  1.00 70.48           C  
ANISOU  937  CD2 PHE A 196     9766   9021   7992   2608   1762   3149       C  
ATOM    938  CE1 PHE A 196      66.703  43.854-198.560  1.00 69.96           C  
ANISOU  938  CE1 PHE A 196     9998   8788   7796   2514   1832   3178       C  
ATOM    939  CE2 PHE A 196      66.064  41.778-197.544  1.00 70.29           C  
ANISOU  939  CE2 PHE A 196     9756   9061   7889   2449   1664   3095       C  
ATOM    940  CZ  PHE A 196      66.828  42.480-198.464  1.00 73.70           C  
ANISOU  940  CZ  PHE A 196    10336   9412   8255   2402   1704   3109       C  
ATOM    941  N   ASP A 197      63.600  47.654-194.459  1.00 58.85           N  
ANISOU  941  N   ASP A 197     8798   6858   6703   3212   2477   3320       N  
ATOM    942  CA  ASP A 197      62.673  48.514-193.732  1.00 63.05           C  
ANISOU  942  CA  ASP A 197     9361   7314   7281   3401   2637   3388       C  
ATOM    943  C   ASP A 197      61.355  48.579-194.501  1.00 77.08           C  
ANISOU  943  C   ASP A 197    10944   9296   9047   3575   2589   3584       C  
ATOM    944  O   ASP A 197      61.258  49.254-195.532  1.00 70.87           O  
ANISOU  944  O   ASP A 197    10195   8519   8214   3640   2585   3694       O  
ATOM    945  CB  ASP A 197      63.292  49.894-193.532  1.00 68.84           C  
ANISOU  945  CB  ASP A 197    10370   7780   8005   3423   2814   3351       C  
ATOM    946  CG  ASP A 197      62.366  50.860-192.840  1.00 73.78           C  
ANISOU  946  CG  ASP A 197    11053   8316   8664   3623   2998   3424       C  
ATOM    947  OD1 ASP A 197      61.254  50.459-192.435  1.00 72.86           O  
ANISOU  947  OD1 ASP A 197    10758   8341   8583   3743   2997   3502       O  
ATOM    948  OD2 ASP A 197      62.761  52.035-192.700  1.00 71.69           O  
ANISOU  948  OD2 ASP A 197    11018   7837   8386   3655   3150   3405       O  
ATOM    949  N   ALA A 198      60.337  47.883-193.992  1.00 70.59           N  
ANISOU  949  N   ALA A 198     9916   8638   8267   3645   2552   3633       N  
ATOM    950  CA  ALA A 198      59.013  47.859-194.601  1.00 69.92           C  
ANISOU  950  CA  ALA A 198     9620   8766   8180   3799   2500   3821       C  
ATOM    951  C   ALA A 198      57.990  48.634-193.774  1.00 71.18           C  
ANISOU  951  C   ALA A 198     9778   8874   8395   3998   2682   3908       C  
ATOM    952  O   ALA A 198      56.795  48.330-193.806  1.00 72.48           O  
ANISOU  952  O   ALA A 198     9728   9229   8584   4108   2649   4038       O  
ATOM    953  CB  ALA A 198      58.550  46.418-194.810  1.00 64.60           C  
ANISOU  953  CB  ALA A 198     8685   8355   7504   3714   2303   3832       C  
ATOM    954  N   ARG A 199      58.443  49.653-193.042  1.00 67.13           N  
ANISOU  954  N   ARG A 199     9506   8103   7896   4041   2878   3839       N  
ATOM    955  CA  ARG A 199      57.545  50.379-192.155  1.00 73.84           C  
ANISOU  955  CA  ARG A 199    10383   8885   8788   4222   3072   3907       C  
ATOM    956  C   ARG A 199      56.543  51.257-192.904  1.00 86.65           C  
ANISOU  956  C   ARG A 199    11945  10575  10402   4432   3129   4116       C  
ATOM    957  O   ARG A 199      55.544  51.674-192.308  1.00 95.70           O  
ANISOU  957  O   ARG A 199    13042  11734  11585   4599   3264   4213       O  
ATOM    958  CB  ARG A 199      58.365  51.209-191.170  1.00 69.85           C  
ANISOU  958  CB  ARG A 199    10175   8081   8286   4189   3261   3763       C  
ATOM    959  CG  ARG A 199      59.090  50.352-190.136  1.00 73.62           C  
ANISOU  959  CG  ARG A 199    10690   8499   8782   4013   3229   3574       C  
ATOM    960  CD  ARG A 199      59.994  51.190-189.263  1.00 79.29           C  
ANISOU  960  CD  ARG A 199    11714   8925   9489   3953   3394   3427       C  
ATOM    961  NE  ARG A 199      61.047  51.837-190.042  1.00 78.86           N  
ANISOU  961  NE  ARG A 199    11840   8732   9392   3864   3382   3382       N  
ATOM    962  CZ  ARG A 199      61.861  52.766-189.555  1.00 74.49           C  
ANISOU  962  CZ  ARG A 199    11565   7921   8816   3810   3522   3276       C  
ATOM    963  NH1 ARG A 199      61.739  53.162-188.295  1.00 73.11           N  
ANISOU  963  NH1 ARG A 199    11528   7600   8651   3839   3682   3201       N  
ATOM    964  NH2 ARG A 199      62.796  53.296-190.323  1.00 71.56           N  
ANISOU  964  NH2 ARG A 199    11339   7442   8407   3719   3501   3246       N  
ATOM    965  N   ASP A 200      56.769  51.541-194.186  1.00 86.14           N  
ANISOU  965  N   ASP A 200    11885  10557  10288   4429   3033   4194       N  
ATOM    966  CA  ASP A 200      55.800  52.278-194.988  1.00 94.56           C  
ANISOU  966  CA  ASP A 200    12874  11712  11343   4624   3058   4404       C  
ATOM    967  C   ASP A 200      54.846  51.357-195.748  1.00100.83           C  
ANISOU  967  C   ASP A 200    13353  12826  12132   4640   2859   4541       C  
ATOM    968  O   ASP A 200      54.211  51.794-196.714  1.00107.67           O  
ANISOU  968  O   ASP A 200    14140  13800  12971   4756   2814   4713       O  
ATOM    969  CB  ASP A 200      56.519  53.220-195.959  1.00 95.84           C  
ANISOU  969  CB  ASP A 200    13235  11734  11445   4623   3076   4429       C  
ATOM    970  CG  ASP A 200      57.617  52.528-196.737  1.00105.77           C  
ANISOU  970  CG  ASP A 200    14519  13023  12647   4406   2898   4327       C  
ATOM    971  OD1 ASP A 200      57.981  51.391-196.359  1.00107.13           O  
ANISOU  971  OD1 ASP A 200    14596  13277  12830   4250   2786   4207       O  
ATOM    972  OD2 ASP A 200      58.113  53.117-197.725  1.00107.41           O  
ANISOU  972  OD2 ASP A 200    14845  13171  12796   4392   2875   4370       O  
ATOM    973  N   CYS A 201      54.742  50.097-195.333  1.00 99.37           N  
ANISOU  973  N   CYS A 201    12994  12792  11969   4519   2736   4468       N  
ATOM    974  CA  CYS A 201      53.796  49.156-195.917  1.00 97.05           C  
ANISOU  974  CA  CYS A 201    12399  12803  11671   4515   2550   4585       C  
ATOM    975  C   CYS A 201      52.373  49.502-195.484  1.00100.73           C  
ANISOU  975  C   CYS A 201    12707  13372  12194   4716   2650   4753       C  
ATOM    976  O   CYS A 201      52.151  50.049-194.398  1.00 97.52           O  
ANISOU  976  O   CYS A 201    12396  12821  11838   4816   2852   4733       O  
ATOM    977  CB  CYS A 201      54.151  47.730-195.477  1.00 89.53           C  
ANISOU  977  CB  CYS A 201    11333  11957  10728   4320   2409   4445       C  
ATOM    978  SG  CYS A 201      53.277  46.385-196.309  1.00 83.93           S  
ANISOU  978  SG  CYS A 201    10283  11616   9993   4240   2141   4543       S  
ATOM    979  N   ARG A 202      51.398  49.175-196.339  1.00107.42           N  
ANISOU  979  N   ARG A 202    13313  14474  13026   4770   2507   4922       N  
ATOM    980  CA  ARG A 202      50.004  49.374-195.946  1.00116.92           C  
ANISOU  980  CA  ARG A 202    14332  15806  14288   4947   2584   5090       C  
ATOM    981  C   ARG A 202      48.991  48.579-196.765  1.00111.96           C  
ANISOU  981  C   ARG A 202    13391  15503  13646   4932   2373   5238       C  
ATOM    982  O   ARG A 202      47.902  49.083-197.053  1.00121.01           O  
ANISOU  982  O   ARG A 202    14403  16761  14813   5104   2404   5434       O  
ATOM    983  CB  ARG A 202      49.647  50.862-196.006  1.00132.63           C  
ANISOU  983  CB  ARG A 202    16462  17644  16288   5175   2784   5220       C  
ATOM    984  CG  ARG A 202      49.304  51.452-194.643  1.00139.46           C  
ANISOU  984  CG  ARG A 202    17427  18344  17217   5304   3041   5204       C  
ATOM    985  CD  ARG A 202      49.189  52.970-194.692  1.00147.30           C  
ANISOU  985  CD  ARG A 202    18619  19141  18209   5510   3253   5300       C  
ATOM    986  NE  ARG A 202      50.305  53.586-195.407  1.00150.85           N  
ANISOU  986  NE  ARG A 202    19305  19415  18598   5449   3242   5225       N  
ATOM    987  CZ  ARG A 202      51.541  53.694-194.926  1.00148.79           C  
ANISOU  987  CZ  ARG A 202    19291  18926  18317   5314   3305   5023       C  
ATOM    988  NH1 ARG A 202      51.837  53.219-193.722  1.00147.65           N  
ANISOU  988  NH1 ARG A 202    19194  18700  18205   5226   3378   4871       N  
ATOM    989  NH2 ARG A 202      52.486  54.273-195.655  1.00145.99           N  
ANISOU  989  NH2 ARG A 202    19135  18427  17907   5260   3290   4976       N  
ATOM    990  N   SER A 203      49.319  47.341-197.126  1.00102.66           N  
ANISOU  990  N   SER A 203    12096  14477  12431   4727   2160   5149       N  
ATOM    991  CA  SER A 203      48.326  46.412-197.653  1.00 96.02           C  
ANISOU  991  CA  SER A 203    10953  13948  11583   4680   1963   5260       C  
ATOM    992  C   SER A 203      48.924  45.014-197.651  1.00 93.21           C  
ANISOU  992  C   SER A 203    10535  13686  11196   4433   1781   5099       C  
ATOM    993  O   SER A 203      50.144  44.852-197.739  1.00 87.44           O  
ANISOU  993  O   SER A 203     9986  12813  10423   4304   1759   4939       O  
ATOM    994  CB  SER A 203      47.863  46.792-199.070  1.00 87.57           C  
ANISOU  994  CB  SER A 203     9799  13026  10447   4741   1830   5432       C  
ATOM    995  OG  SER A 203      48.844  46.501-200.052  1.00 82.55           O  
ANISOU  995  OG  SER A 203     9271  12379   9716   4586   1678   5346       O  
ATOM    996  N   ALA A 204      48.051  44.008-197.545  1.00104.11           N  
ANISOU  996  N   ALA A 204    11657  15304  12594   4366   1654   5147       N  
ATOM    997  CA  ALA A 204      48.497  42.624-197.671  1.00110.98           C  
ANISOU  997  CA  ALA A 204    12448  16292  13426   4130   1462   5013       C  
ATOM    998  C   ALA A 204      49.126  42.353-199.032  1.00109.96           C  
ANISOU  998  C   ALA A 204    12362  16233  13187   4004   1269   4991       C  
ATOM    999  O   ALA A 204      49.864  41.372-199.183  1.00114.11           O  
ANISOU  999  O   ALA A 204    12908  16784  13665   3806   1139   4846       O  
ATOM   1000  CB  ALA A 204      47.327  41.666-197.430  1.00111.14           C  
ANISOU 1000  CB  ALA A 204    12179  16569  13481   4084   1355   5090       C  
ATOM   1001  N   GLN A 205      48.851  43.202-200.023  1.00 97.78           N  
ANISOU 1001  N   GLN A 205    10839  14717  11597   4116   1252   5134       N  
ATOM   1002  CA  GLN A 205      49.521  43.078-201.308  1.00 90.45           C  
ANISOU 1002  CA  GLN A 205     9991  13824  10552   4005   1092   5115       C  
ATOM   1003  C   GLN A 205      50.967  43.553-201.221  1.00 85.81           C  
ANISOU 1003  C   GLN A 205     9698  12968   9938   3962   1192   4964       C  
ATOM   1004  O   GLN A 205      51.874  42.890-201.736  1.00 80.20           O  
ANISOU 1004  O   GLN A 205     9065  12258   9150   3782   1070   4844       O  
ATOM   1005  CB  GLN A 205      48.755  43.863-202.369  1.00 90.89           C  
ANISOU 1005  CB  GLN A 205     9982  13988  10563   4142   1044   5325       C  
ATOM   1006  CG  GLN A 205      49.250  43.622-203.775  1.00102.45           C  
ANISOU 1006  CG  GLN A 205    11500  15534  11891   4018    852   5328       C  
ATOM   1007  CD  GLN A 205      49.284  42.149-204.126  1.00106.56           C  
ANISOU 1007  CD  GLN A 205    11886  16256  12346   3784    629   5238       C  
ATOM   1008  OE1 GLN A 205      50.348  41.590-204.401  1.00104.35           O  
ANISOU 1008  OE1 GLN A 205    11739  15913  11995   3615    562   5084       O  
ATOM   1009  NE2 GLN A 205      48.117  41.510-204.118  1.00109.86           N  
ANISOU 1009  NE2 GLN A 205    12041  16915  12785   3767    517   5333       N  
ATOM   1010  N   GLU A 206      51.200  44.698-200.569  1.00 85.81           N  
ANISOU 1010  N   GLU A 206     9869  12735   9999   4118   1417   4969       N  
ATOM   1011  CA  GLU A 206      52.565  45.184-200.377  1.00 84.38           C  
ANISOU 1011  CA  GLU A 206     9970  12288   9802   4068   1524   4821       C  
ATOM   1012  C   GLU A 206      53.388  44.197-199.559  1.00 82.39           C  
ANISOU 1012  C   GLU A 206     9756  11977   9572   3892   1505   4617       C  
ATOM   1013  O   GLU A 206      54.561  43.943-199.865  1.00 73.67           O  
ANISOU 1013  O   GLU A 206     8804  10774   8413   3749   1461   4486       O  
ATOM   1014  CB  GLU A 206      52.551  46.547-199.686  1.00 89.51           C  
ANISOU 1014  CB  GLU A 206    10790  12703  10518   4261   1776   4857       C  
ATOM   1015  CG  GLU A 206      51.914  47.672-200.479  1.00109.43           C  
ANISOU 1015  CG  GLU A 206    13325  15237  13019   4447   1821   5053       C  
ATOM   1016  CD  GLU A 206      52.324  49.038-199.960  1.00115.10           C  
ANISOU 1016  CD  GLU A 206    14292  15668  13773   4591   2066   5044       C  
ATOM   1017  OE1 GLU A 206      53.387  49.127-199.308  1.00115.74           O  
ANISOU 1017  OE1 GLU A 206    14576  15535  13867   4503   2163   4871       O  
ATOM   1018  OE2 GLU A 206      51.590  50.018-200.201  1.00120.67           O  
ANISOU 1018  OE2 GLU A 206    14995  16362  14493   4788   2159   5210       O  
ATOM   1019  N   MET A 207      52.793  43.657-198.491  1.00 85.20           N  
ANISOU 1019  N   MET A 207     9980  12385  10009   3903   1547   4592       N  
ATOM   1020  CA  MET A 207      53.460  42.638-197.687  1.00 81.65           C  
ANISOU 1020  CA  MET A 207     9543  11898   9582   3740   1516   4412       C  
ATOM   1021  C   MET A 207      54.030  41.544-198.574  1.00 78.84           C  
ANISOU 1021  C   MET A 207     9142  11678   9136   3535   1295   4337       C  
ATOM   1022  O   MET A 207      55.214  41.205-198.487  1.00 82.74           O  
ANISOU 1022  O   MET A 207     9786  12049   9602   3402   1283   4183       O  
ATOM   1023  CB  MET A 207      52.480  42.031-196.682  1.00 92.60           C  
ANISOU 1023  CB  MET A 207    10738  13399  11049   3769   1539   4437       C  
ATOM   1024  CG  MET A 207      52.159  42.883-195.477  1.00103.74           C  
ANISOU 1024  CG  MET A 207    12232  14639  12547   3931   1779   4452       C  
ATOM   1025  SD  MET A 207      51.296  41.882-194.244  1.00112.32           S  
ANISOU 1025  SD  MET A 207    13118  15847  13710   3901   1786   4438       S  
ATOM   1026  CE  MET A 207      52.491  40.578-193.988  1.00105.23           C  
ANISOU 1026  CE  MET A 207    12275  14920  12786   3651   1651   4216       C  
ATOM   1027  N   PHE A 208      53.190  40.995-199.456  1.00 73.10           N  
ANISOU 1027  N   PHE A 208     8213  11205   8356   3504   1120   4448       N  
ATOM   1028  CA  PHE A 208      53.605  39.849-200.255  1.00 76.56           C  
ANISOU 1028  CA  PHE A 208     8598  11791   8700   3299    907   4375       C  
ATOM   1029  C   PHE A 208      54.801  40.194-201.129  1.00 80.30           C  
ANISOU 1029  C   PHE A 208     9289  12144   9080   3227    888   4312       C  
ATOM   1030  O   PHE A 208      55.713  39.374-201.296  1.00 76.42           O  
ANISOU 1030  O   PHE A 208     8862  11641   8531   3053    803   4174       O  
ATOM   1031  CB  PHE A 208      52.431  39.350-201.096  1.00 79.97           C  
ANISOU 1031  CB  PHE A 208     8793  12509   9084   3283    730   4516       C  
ATOM   1032  CG  PHE A 208      52.766  38.183-201.976  1.00 80.23           C  
ANISOU 1032  CG  PHE A 208     8779  12702   9005   3068    509   4445       C  
ATOM   1033  CD1 PHE A 208      52.964  36.923-201.436  1.00 81.97           C  
ANISOU 1033  CD1 PHE A 208     8926  12984   9235   2903    427   4312       C  
ATOM   1034  CD2 PHE A 208      52.866  38.345-203.348  1.00 83.97           C  
ANISOU 1034  CD2 PHE A 208     9291  13260   9355   3028    385   4511       C  
ATOM   1035  CE1 PHE A 208      53.265  35.843-202.249  1.00 83.13           C  
ANISOU 1035  CE1 PHE A 208     9043  13272   9271   2703    232   4241       C  
ATOM   1036  CE2 PHE A 208      53.169  37.272-204.166  1.00 87.89           C  
ANISOU 1036  CE2 PHE A 208     9762  13898   9733   2826    190   4439       C  
ATOM   1037  CZ  PHE A 208      53.369  36.017-203.614  1.00 86.21           C  
ANISOU 1037  CZ  PHE A 208     9480  13744   9533   2662    116   4301       C  
ATOM   1038  N   THR A 209      54.826  41.415-201.678  1.00 83.32           N  
ANISOU 1038  N   THR A 209     9789  12426   9440   3360    975   4414       N  
ATOM   1039  CA  THR A 209      55.988  41.866-202.437  1.00 72.84           C  
ANISOU 1039  CA  THR A 209     8688  10960   8029   3298    985   4359       C  
ATOM   1040  C   THR A 209      57.219  41.989-201.541  1.00 76.39           C  
ANISOU 1040  C   THR A 209     9337  11160   8527   3239   1124   4185       C  
ATOM   1041  O   THR A 209      58.323  41.593-201.934  1.00 70.93           O  
ANISOU 1041  O   THR A 209     8771  10413   7767   3087   1077   4071       O  
ATOM   1042  CB  THR A 209      55.671  43.195-203.126  1.00 79.99           C  
ANISOU 1042  CB  THR A 209     9677  11804   8911   3463   1061   4514       C  
ATOM   1043  OG1 THR A 209      54.512  43.031-203.952  1.00 75.83           O  
ANISOU 1043  OG1 THR A 209     8954  11521   8339   3512    919   4680       O  
ATOM   1044  CG2 THR A 209      56.835  43.645-203.996  1.00 73.58           C  
ANISOU 1044  CG2 THR A 209     9096  10861   8002   3386   1066   4468       C  
ATOM   1045  N   TYR A 210      57.047  42.518-200.327  1.00 77.68           N  
ANISOU 1045  N   TYR A 210     9536  11177   8803   3350   1296   4162       N  
ATOM   1046  CA  TYR A 210      58.153  42.571-199.374  1.00 76.35           C  
ANISOU 1046  CA  TYR A 210     9547  10781   8683   3282   1417   3993       C  
ATOM   1047  C   TYR A 210      58.645  41.175-199.022  1.00 62.94           C  
ANISOU 1047  C   TYR A 210     7779   9160   6976   3097   1299   3852       C  
ATOM   1048  O   TYR A 210      59.848  40.895-199.075  1.00 61.64           O  
ANISOU 1048  O   TYR A 210     7756   8889   6777   2960   1292   3721       O  
ATOM   1049  CB  TYR A 210      57.725  43.307-198.107  1.00 75.88           C  
ANISOU 1049  CB  TYR A 210     9526  10573   8733   3430   1612   3998       C  
ATOM   1050  CG  TYR A 210      57.873  44.797-198.201  1.00 73.20           C  
ANISOU 1050  CG  TYR A 210     9375  10036   8402   3572   1783   4059       C  
ATOM   1051  CD1 TYR A 210      59.128  45.378-198.316  1.00 71.73           C  
ANISOU 1051  CD1 TYR A 210     9435   9631   8188   3499   1860   3959       C  
ATOM   1052  CD2 TYR A 210      56.759  45.627-198.171  1.00 75.72           C  
ANISOU 1052  CD2 TYR A 210     9627  10386   8756   3773   1873   4219       C  
ATOM   1053  CE1 TYR A 210      59.269  46.750-198.407  1.00 73.38           C  
ANISOU 1053  CE1 TYR A 210     9828   9654   8401   3618   2017   4012       C  
ATOM   1054  CE2 TYR A 210      56.891  46.997-198.252  1.00 75.26           C  
ANISOU 1054  CE2 TYR A 210     9752  10140   8702   3906   2036   4275       C  
ATOM   1055  CZ  TYR A 210      58.149  47.550-198.371  1.00 74.15           C  
ANISOU 1055  CZ  TYR A 210     9864   9780   8531   3824   2105   4168       C  
ATOM   1056  OH  TYR A 210      58.295  48.910-198.450  1.00 77.65           O  
ANISOU 1056  OH  TYR A 210    10499  10029   8974   3944   2267   4219       O  
ATOM   1057  N   ILE A 211      57.726  40.291-198.641  1.00 67.48           N  
ANISOU 1057  N   ILE A 211     8136   9920   7585   3089   1211   3879       N  
ATOM   1058  CA  ILE A 211      58.108  38.928-198.287  1.00 66.19           C  
ANISOU 1058  CA  ILE A 211     7899   9837   7414   2918   1096   3751       C  
ATOM   1059  C   ILE A 211      58.808  38.263-199.462  1.00 64.38           C  
ANISOU 1059  C   ILE A 211     7699   9700   7061   2756    939   3707       C  
ATOM   1060  O   ILE A 211      59.797  37.544-199.289  1.00 57.05           O  
ANISOU 1060  O   ILE A 211     6847   8720   6109   2609    906   3567       O  
ATOM   1061  CB  ILE A 211      56.867  38.142-197.825  1.00 64.70           C  
ANISOU 1061  CB  ILE A 211     7460   9850   7273   2935   1021   3811       C  
ATOM   1062  CG1 ILE A 211      56.330  38.756-196.534  1.00 66.55           C  
ANISOU 1062  CG1 ILE A 211     7694   9967   7622   3082   1203   3833       C  
ATOM   1063  CG2 ILE A 211      57.179  36.659-197.661  1.00 65.24           C  
ANISOU 1063  CG2 ILE A 211     7442  10030   7317   2747    875   3693       C  
ATOM   1064  CD1 ILE A 211      55.012  38.176-196.070  1.00 73.79           C  
ANISOU 1064  CD1 ILE A 211     8369  11077   8592   3121   1161   3918       C  
ATOM   1065  N   CYS A 212      58.349  38.551-200.682  1.00 74.55           N  
ANISOU 1065  N   CYS A 212     8946  11117   8264   2784    851   3828       N  
ATOM   1066  CA  CYS A 212      58.982  37.981-201.864  1.00 72.37           C  
ANISOU 1066  CA  CYS A 212     8716  10928   7853   2632    711   3792       C  
ATOM   1067  C   CYS A 212      60.381  38.545-202.077  1.00 66.92           C  
ANISOU 1067  C   CYS A 212     8276  10026   7125   2581    811   3704       C  
ATOM   1068  O   CYS A 212      61.296  37.804-202.448  1.00 63.31           O  
ANISOU 1068  O   CYS A 212     7884   9578   6592   2420    746   3594       O  
ATOM   1069  CB  CYS A 212      58.106  38.217-203.094  1.00 76.27           C  
ANISOU 1069  CB  CYS A 212     9116  11605   8260   2677    595   3950       C  
ATOM   1070  SG  CYS A 212      56.674  37.112-203.177  1.00 79.13           S  
ANISOU 1070  SG  CYS A 212     9175  12273   8619   2635    409   4023       S  
ATOM   1071  N   ASN A 213      60.566  39.853-201.865  1.00 70.50           N  
ANISOU 1071  N   ASN A 213     8871  10289   7627   2711    973   3749       N  
ATOM   1072  CA  ASN A 213      61.903  40.436-201.951  1.00 65.96           C  
ANISOU 1072  CA  ASN A 213     8533   9498   7029   2652   1082   3660       C  
ATOM   1073  C   ASN A 213      62.852  39.754-200.979  1.00 58.61           C  
ANISOU 1073  C   ASN A 213     7660   8459   6150   2529   1122   3485       C  
ATOM   1074  O   ASN A 213      63.979  39.391-201.337  1.00 55.70           O  
ANISOU 1074  O   ASN A 213     7403   8042   5720   2385   1109   3384       O  
ATOM   1075  CB  ASN A 213      61.850  41.935-201.663  1.00 66.22           C  
ANISOU 1075  CB  ASN A 213     8704   9332   7123   2810   1260   3727       C  
ATOM   1076  CG  ASN A 213      61.354  42.746-202.850  1.00 78.59           C  
ANISOU 1076  CG  ASN A 213    10290  10958   8614   2904   1235   3887       C  
ATOM   1077  OD1 ASN A 213      61.253  42.237-203.969  1.00 78.17           O  
ANISOU 1077  OD1 ASN A 213    10181  11072   8447   2828   1088   3934       O  
ATOM   1078  ND2 ASN A 213      61.050  44.019-202.610  1.00 76.60           N  
ANISOU 1078  ND2 ASN A 213    10127  10562   8416   3067   1382   3971       N  
ATOM   1079  N   HIS A 214      62.403  39.588-199.732  1.00 62.57           N  
ANISOU 1079  N   HIS A 214     8087   8923   6763   2587   1177   3452       N  
ATOM   1080  CA  HIS A 214      63.191  38.953-198.682  1.00 58.55           C  
ANISOU 1080  CA  HIS A 214     7625   8311   6311   2485   1213   3296       C  
ATOM   1081  C   HIS A 214      63.609  37.541-199.078  1.00 55.75           C  
ANISOU 1081  C   HIS A 214     7190   8108   5883   2311   1058   3214       C  
ATOM   1082  O   HIS A 214      64.797  37.197-199.064  1.00 50.24           O  
ANISOU 1082  O   HIS A 214     6608   7325   5157   2180   1073   3095       O  
ATOM   1083  CB  HIS A 214      62.354  38.951-197.400  1.00 58.61           C  
ANISOU 1083  CB  HIS A 214     7537   8299   6434   2589   1278   3304       C  
ATOM   1084  CG  HIS A 214      63.041  38.373-196.201  1.00 56.96           C  
ANISOU 1084  CG  HIS A 214     7379   7976   6289   2501   1320   3156       C  
ATOM   1085  ND1 HIS A 214      63.089  39.033-194.992  1.00 59.93           N  
ANISOU 1085  ND1 HIS A 214     7851   8162   6757   2574   1474   3113       N  
ATOM   1086  CD2 HIS A 214      63.659  37.185-196.003  1.00 55.18           C  
ANISOU 1086  CD2 HIS A 214     7119   7802   6043   2347   1226   3044       C  
ATOM   1087  CE1 HIS A 214      63.727  38.286-194.107  1.00 55.86           C  
ANISOU 1087  CE1 HIS A 214     7362   7586   6277   2465   1467   2983       C  
ATOM   1088  NE2 HIS A 214      64.084  37.159-194.696  1.00 56.98           N  
ANISOU 1088  NE2 HIS A 214     7423   7873   6356   2331   1320   2942       N  
ATOM   1089  N   ILE A 215      62.628  36.711-199.440  1.00 55.56           N  
ANISOU 1089  N   ILE A 215     6968   8317   5827   2304    910   3275       N  
ATOM   1090  CA  ILE A 215      62.899  35.322-199.794  1.00 58.78           C  
ANISOU 1090  CA  ILE A 215     7295   8880   6159   2139    758   3196       C  
ATOM   1091  C   ILE A 215      63.893  35.233-200.944  1.00 58.11           C  
ANISOU 1091  C   ILE A 215     7338   8796   5945   2022    723   3155       C  
ATOM   1092  O   ILE A 215      64.814  34.411-200.917  1.00 55.12           O  
ANISOU 1092  O   ILE A 215     7008   8409   5525   1880    698   3033       O  
ATOM   1093  CB  ILE A 215      61.585  34.591-200.123  1.00 60.90           C  
ANISOU 1093  CB  ILE A 215     7336   9398   6405   2145    603   3282       C  
ATOM   1094  CG1 ILE A 215      60.732  34.448-198.860  1.00 59.23           C  
ANISOU 1094  CG1 ILE A 215     6993   9191   6322   2229    645   3296       C  
ATOM   1095  CG2 ILE A 215      61.878  33.232-200.739  1.00 56.20           C  
ANISOU 1095  CG2 ILE A 215     6685   8966   5703   1961    438   3201       C  
ATOM   1096  CD1 ILE A 215      59.356  33.861-199.111  1.00 62.42           C  
ANISOU 1096  CD1 ILE A 215     7162   9836   6720   2240    513   3394       C  
ATOM   1097  N   LYS A 216      63.735  36.073-201.975  1.00 57.50           N  
ANISOU 1097  N   LYS A 216     7321   8729   5799   2079    730   3258       N  
ATOM   1098  CA  LYS A 216      64.706  36.012-203.060  1.00 52.69           C  
ANISOU 1098  CA  LYS A 216     6845   8114   5060   1963    713   3218       C  
ATOM   1099  C   LYS A 216      66.083  36.481-202.589  1.00 59.91           C  
ANISOU 1099  C   LYS A 216     7951   8798   6013   1913    868   3110       C  
ATOM   1100  O   LYS A 216      67.100  35.858-202.920  1.00 56.81           O  
ANISOU 1100  O   LYS A 216     7629   8403   5552   1769    861   3005       O  
ATOM   1101  CB  LYS A 216      64.222  36.821-204.275  1.00 56.67           C  
ANISOU 1101  CB  LYS A 216     7379   8677   5475   2033    684   3359       C  
ATOM   1102  CG  LYS A 216      64.870  38.184-204.447  1.00 69.09           C  
ANISOU 1102  CG  LYS A 216     9146  10042   7063   2101    841   3392       C  
ATOM   1103  CD  LYS A 216      64.883  38.638-205.897  1.00 77.94           C  
ANISOU 1103  CD  LYS A 216    10343  11227   8045   2090    795   3486       C  
ATOM   1104  CE  LYS A 216      65.617  39.967-206.029  1.00 84.89           C  
ANISOU 1104  CE  LYS A 216    11425  11888   8941   2141    958   3509       C  
ATOM   1105  NZ  LYS A 216      65.720  40.449-207.432  1.00 85.99           N  
ANISOU 1105  NZ  LYS A 216    11660  12072   8941   2123    925   3599       N  
ATOM   1106  N   TYR A 217      66.138  37.555-201.793  1.00 56.69           N  
ANISOU 1106  N   TYR A 217     7627   8196   5716   2022   1014   3127       N  
ATOM   1107  CA  TYR A 217      67.424  38.048-201.308  1.00 52.02           C  
ANISOU 1107  CA  TYR A 217     7217   7383   5166   1959   1157   3022       C  
ATOM   1108  C   TYR A 217      68.074  37.036-200.375  1.00 56.27           C  
ANISOU 1108  C   TYR A 217     7729   7898   5753   1846   1150   2878       C  
ATOM   1109  O   TYR A 217      69.267  36.734-200.494  1.00 56.34           O  
ANISOU 1109  O   TYR A 217     7832   7844   5730   1714   1189   2773       O  
ATOM   1110  CB  TYR A 217      67.255  39.389-200.578  1.00 53.51           C  
ANISOU 1110  CB  TYR A 217     7505   7368   5458   2093   1308   3062       C  
ATOM   1111  CG  TYR A 217      68.536  39.846-199.886  1.00 51.72           C  
ANISOU 1111  CG  TYR A 217     7455   6908   5287   2009   1447   2940       C  
ATOM   1112  CD1 TYR A 217      69.385  40.760-200.499  1.00 61.39           C  
ANISOU 1112  CD1 TYR A 217     8854   7999   6472   1968   1541   2940       C  
ATOM   1113  CD2 TYR A 217      68.914  39.333-198.637  1.00 58.96           C  
ANISOU 1113  CD2 TYR A 217     8365   7746   6291   1955   1478   2823       C  
ATOM   1114  CE1 TYR A 217      70.559  41.164-199.892  1.00 59.36           C  
ANISOU 1114  CE1 TYR A 217     8747   7542   6266   1871   1659   2827       C  
ATOM   1115  CE2 TYR A 217      70.090  39.728-198.029  1.00 55.63           C  
ANISOU 1115  CE2 TYR A 217     8098   7123   5915   1861   1591   2711       C  
ATOM   1116  CZ  TYR A 217      70.907  40.649-198.665  1.00 66.48           C  
ANISOU 1116  CZ  TYR A 217     9633   8374   7253   1815   1681   2713       C  
ATOM   1117  OH  TYR A 217      72.079  41.065-198.084  1.00 75.55           O  
ANISOU 1117  OH  TYR A 217    10927   9331   8448   1705   1788   2603       O  
ATOM   1118  N   ALA A 218      67.313  36.548-199.397  1.00 48.11           N  
ANISOU 1118  N   ALA A 218     6569   6909   4802   1901   1114   2873       N  
ATOM   1119  CA  ALA A 218      67.882  35.630-198.416  1.00 48.67           C  
ANISOU 1119  CA  ALA A 218     6620   6946   4924   1804   1110   2745       C  
ATOM   1120  C   ALA A 218      68.286  34.312-199.060  1.00 53.77           C  
ANISOU 1120  C   ALA A 218     7200   7760   5470   1660    988   2680       C  
ATOM   1121  O   ALA A 218      69.295  33.713-198.671  1.00 55.32           O  
ANISOU 1121  O   ALA A 218     7446   7900   5671   1545   1016   2561       O  
ATOM   1122  CB  ALA A 218      66.891  35.390-197.275  1.00 46.04           C  
ANISOU 1122  CB  ALA A 218     6165   6635   4694   1896   1096   2764       C  
ATOM   1123  N   THR A 219      67.510  33.833-200.033  1.00 53.29           N  
ANISOU 1123  N   THR A 219     7028   7905   5314   1660    854   2754       N  
ATOM   1124  CA  THR A 219      67.838  32.552-200.654  1.00 59.66           C  
ANISOU 1124  CA  THR A 219     7782   8873   6011   1517    737   2683       C  
ATOM   1125  C   THR A 219      69.090  32.672-201.515  1.00 57.88           C  
ANISOU 1125  C   THR A 219     7707   8595   5691   1413    801   2620       C  
ATOM   1126  O   THR A 219      70.038  31.894-201.351  1.00 58.82           O  
ANISOU 1126  O   THR A 219     7846   8684   5819   1277    809   2457       O  
ATOM   1127  CB  THR A 219      66.645  32.022-201.458  1.00 60.37           C  
ANISOU 1127  CB  THR A 219     7722   9196   6019   1525    570   2770       C  
ATOM   1128  OG1 THR A 219      65.547  31.744-200.564  1.00 52.91           O  
ANISOU 1128  OG1 THR A 219     6619   8312   5173   1599    517   2812       O  
ATOM   1129  CG2 THR A 219      67.025  30.742-202.187  1.00 61.34           C  
ANISOU 1129  CG2 THR A 219     7822   9475   6010   1363    453   2684       C  
ATOM   1130  N   ASN A 220      69.122  33.653-202.426  1.00 52.34           N  
ANISOU 1130  N   ASN A 220     7097   7856   4934   1457    845   2702       N  
ATOM   1131  CA  ASN A 220      70.354  34.012-203.130  1.00 52.03           C  
ANISOU 1131  CA  ASN A 220     7216   7727   4825   1369    943   2648       C  
ATOM   1132  C   ASN A 220      70.949  32.795-203.840  1.00 52.71           C  
ANISOU 1132  C   ASN A 220     7290   7953   4786   1221    878   2552       C  
ATOM   1133  O   ASN A 220      72.159  32.565-203.826  1.00 51.45           O  
ANISOU 1133  O   ASN A 220     7203   7701   4645   1107    959   2408       O  
ATOM   1134  CB  ASN A 220      71.347  34.655-202.155  1.00 51.90           C  
ANISOU 1134  CB  ASN A 220     7312   7478   4929   1359   1105   2572       C  
ATOM   1135  CG  ASN A 220      72.617  35.160-202.818  1.00 58.20           C  
ANISOU 1135  CG  ASN A 220     8265   8171   5678   1266   1222   2522       C  
ATOM   1136  OD1 ASN A 220      72.614  35.591-203.975  1.00 57.99           O  
ANISOU 1136  OD1 ASN A 220     8299   8187   5547   1262   1218   2586       O  
ATOM   1137  ND2 ASN A 220      73.722  35.111-202.071  1.00 59.70           N  
ANISOU 1137  ND2 ASN A 220     8516   8222   5945   1183   1329   2407       N  
ATOM   1138  N   ARG A 221      70.071  31.991-204.447  1.00 53.66           N  
ANISOU 1138  N   ARG A 221     7300   8280   4811   1201    718   2588       N  
ATOM   1139  CA  ARG A 221      70.448  30.823-205.246  1.00 67.21           C  
ANISOU 1139  CA  ARG A 221     9004  10129   6405   1050    633   2473       C  
ATOM   1140  C   ARG A 221      71.126  29.748-204.404  1.00 59.79           C  
ANISOU 1140  C   ARG A 221     8011   9126   5581    931    628   2249       C  
ATOM   1141  O   ARG A 221      71.908  28.944-204.917  1.00 54.60           O  
ANISOU 1141  O   ARG A 221     7387   8487   4872    798    625   2101       O  
ATOM   1142  CB  ARG A 221      71.343  31.210-206.429  1.00 60.68           C  
ANISOU 1142  CB  ARG A 221     8331   9280   5446    987    715   2468       C  
ATOM   1143  CG  ARG A 221      70.754  32.287-207.328  1.00 74.19           C  
ANISOU 1143  CG  ARG A 221    10100  11003   7085   1073    705   2628       C  
ATOM   1144  CD  ARG A 221      71.667  32.587-208.503  1.00 78.33           C  
ANISOU 1144  CD  ARG A 221    10780  11503   7478    991    784   2606       C  
ATOM   1145  NE  ARG A 221      71.125  32.084-209.763  1.00 93.30           N  
ANISOU 1145  NE  ARG A 221    12676  13582   9192    932    651   2642       N  
ATOM   1146  CZ  ARG A 221      71.551  32.464-210.966  1.00101.89           C  
ANISOU 1146  CZ  ARG A 221    13896  14675  10140    882    688   2666       C  
ATOM   1147  NH1 ARG A 221      72.528  33.356-211.078  1.00101.94           N  
ANISOU 1147  NH1 ARG A 221    14036  14519  10177    880    856   2659       N  
ATOM   1148  NH2 ARG A 221      70.999  31.955-212.060  1.00104.27           N  
ANISOU 1148  NH2 ARG A 221    14204  15144  10271    822    556   2694       N  
ATOM   1149  N   GLY A 222      70.832  29.722-203.111  1.00 53.73           N  
ANISOU 1149  N   GLY A 222     7165   8281   4968    983    634   2226       N  
ATOM   1150  CA  GLY A 222      71.417  28.753-202.217  1.00 53.68           C  
ANISOU 1150  CA  GLY A 222     7108   8210   5076    885    625   2031       C  
ATOM   1151  C   GLY A 222      72.557  29.283-201.375  1.00 52.96           C  
ANISOU 1151  C   GLY A 222     7095   7909   5117    872    768   1937       C  
ATOM   1152  O   GLY A 222      72.987  28.594-200.446  1.00 53.08           O  
ANISOU 1152  O   GLY A 222     7062   7859   5245    811    760   1796       O  
ATOM   1153  N   ASN A 223      73.072  30.476-201.682  1.00 52.01           N  
ANISOU 1153  N   ASN A 223     7098   7681   4982    918    896   2013       N  
ATOM   1154  CA  ASN A 223      74.099  31.103-200.850  1.00 51.13           C  
ANISOU 1154  CA  ASN A 223     7066   7369   4994    897   1030   1939       C  
ATOM   1155  C   ASN A 223      73.391  32.014-199.850  1.00 47.64           C  
ANISOU 1155  C   ASN A 223     6635   6828   4638   1031   1073   2051       C  
ATOM   1156  O   ASN A 223      73.322  33.235-200.003  1.00 51.15           O  
ANISOU 1156  O   ASN A 223     7187   7182   5066   1119   1173   2177       O  
ATOM   1157  CB  ASN A 223      75.109  31.855-201.710  1.00 57.17           C  
ANISOU 1157  CB  ASN A 223     7965   8060   5695    851   1153   1948       C  
ATOM   1158  CG  ASN A 223      76.256  32.414-200.892  1.00 65.72           C  
ANISOU 1158  CG  ASN A 223     9118   8949   6902    797   1281   1859       C  
ATOM   1159  OD1 ASN A 223      76.548  31.924-199.797  1.00 66.35           O  
ANISOU 1159  OD1 ASN A 223     9138   8967   7105    757   1261   1744       O  
ATOM   1160  ND2 ASN A 223      76.904  33.447-201.408  1.00 61.94           N  
ANISOU 1160  ND2 ASN A 223     8770   8375   6389    789   1408   1915       N  
ATOM   1161  N   LEU A 224      72.858  31.391-198.800  1.00 44.77           N  
ANISOU 1161  N   LEU A 224     6169   6476   4366   1046   1005   2002       N  
ATOM   1162  CA  LEU A 224      71.888  32.061-197.939  1.00 52.91           C  
ANISOU 1162  CA  LEU A 224     7185   7458   5459   1188   1028   2121       C  
ATOM   1163  C   LEU A 224      72.498  33.256-197.202  1.00 46.98           C  
ANISOU 1163  C   LEU A 224     6577   6485   4788   1226   1184   2131       C  
ATOM   1164  O   LEU A 224      73.663  33.249-196.803  1.00 46.55           O  
ANISOU 1164  O   LEU A 224     6587   6309   4792   1115   1244   1997       O  
ATOM   1165  CB  LEU A 224      71.303  31.058-196.935  1.00 46.48           C  
ANISOU 1165  CB  LEU A 224     6236   6697   4726   1175    932   2048       C  
ATOM   1166  CG  LEU A 224      70.014  30.335-197.356  1.00 51.34           C  
ANISOU 1166  CG  LEU A 224     6704   7524   5278   1216    791   2134       C  
ATOM   1167  CD1 LEU A 224      70.089  29.771-198.767  1.00 52.31           C  
ANISOU 1167  CD1 LEU A 224     6810   7805   5262   1138    704   2133       C  
ATOM   1168  CD2 LEU A 224      69.695  29.217-196.371  1.00 47.01           C  
ANISOU 1168  CD2 LEU A 224     6039   7010   4813   1161    706   2027       C  
ATOM   1169  N   ARG A 225      71.683  34.290-197.010  1.00 48.42           N  
ANISOU 1169  N   ARG A 225     6811   6615   4971   1384   1249   2295       N  
ATOM   1170  CA  ARG A 225      72.101  35.517-196.344  1.00 46.46           C  
ANISOU 1170  CA  ARG A 225     6723   6145   4783   1433   1404   2322       C  
ATOM   1171  C   ARG A 225      71.081  35.887-195.283  1.00 49.99           C  
ANISOU 1171  C   ARG A 225     7136   6538   5319   1565   1419   2372       C  
ATOM   1172  O   ARG A 225      69.889  35.994-195.585  1.00 53.37           O  
ANISOU 1172  O   ARG A 225     7465   7078   5735   1686   1363   2479       O  
ATOM   1173  CB  ARG A 225      72.245  36.681-197.347  1.00 48.10           C  
ANISOU 1173  CB  ARG A 225     7043   6295   4938   1471   1473   2402       C  
ATOM   1174  CG  ARG A 225      73.351  36.492-198.371  1.00 48.72           C  
ANISOU 1174  CG  ARG A 225     7183   6399   4929   1339   1494   2355       C  
ATOM   1175  CD  ARG A 225      73.449  37.695-199.306  1.00 53.80           C  
ANISOU 1175  CD  ARG A 225     7943   6974   5525   1376   1561   2435       C  
ATOM   1176  NE  ARG A 225      72.389  37.715-200.309  1.00 54.82           N  
ANISOU 1176  NE  ARG A 225     7998   7264   5567   1474   1467   2561       N  
ATOM   1177  CZ  ARG A 225      72.434  38.464-201.408  1.00 59.57           C  
ANISOU 1177  CZ  ARG A 225     8679   7866   6090   1492   1492   2640       C  
ATOM   1178  NH1 ARG A 225      73.482  39.245-201.626  1.00 58.71           N  
ANISOU 1178  NH1 ARG A 225     8722   7604   5983   1418   1611   2601       N  
ATOM   1179  NH2 ARG A 225      71.440  38.437-202.288  1.00 53.27           N  
ANISOU 1179  NH2 ARG A 225     7808   7222   5211   1575   1394   2757       N  
ATOM   1180  N   SER A 226      71.552  36.081-194.048  1.00 43.32           N  
ANISOU 1180  N   SER A 226     6371   5527   4563   1533   1497   2287       N  
ATOM   1181  CA  SER A 226      70.669  36.450-192.950  1.00 53.81           C  
ANISOU 1181  CA  SER A 226     7686   6786   5974   1648   1531   2310       C  
ATOM   1182  C   SER A 226      69.935  37.744-193.265  1.00 54.49           C  
ANISOU 1182  C   SER A 226     7825   6811   6066   1797   1607   2414       C  
ATOM   1183  O   SER A 226      70.526  38.708-193.757  1.00 48.82           O  
ANISOU 1183  O   SER A 226     7245   5976   5328   1782   1690   2420       O  
ATOM   1184  CB  SER A 226      71.462  36.624-191.662  1.00 51.82           C  
ANISOU 1184  CB  SER A 226     7554   6338   5796   1570   1615   2193       C  
ATOM   1185  OG  SER A 226      72.197  35.459-191.358  1.00 56.37           O  
ANISOU 1185  OG  SER A 226     8054   6969   6396   1413   1524   2044       O  
ATOM   1186  N   ALA A 227      68.642  37.769-192.961  1.00 51.81           N  
ANISOU 1186  N   ALA A 227     7375   6552   5758   1940   1587   2499       N  
ATOM   1187  CA  ALA A 227      67.825  38.907-193.351  1.00 50.64           C  
ANISOU 1187  CA  ALA A 227     7250   6380   5611   2097   1656   2616       C  
ATOM   1188  C   ALA A 227      66.595  38.984-192.460  1.00 57.59           C  
ANISOU 1188  C   ALA A 227     8036   7287   6560   2241   1687   2670       C  
ATOM   1189  O   ALA A 227      66.117  37.966-191.948  1.00 51.12           O  
ANISOU 1189  O   ALA A 227     7075   6584   5763   2225   1607   2654       O  
ATOM   1190  CB  ALA A 227      67.410  38.814-194.824  1.00 44.65           C  
ANISOU 1190  CB  ALA A 227     6400   5800   4764   2125   1562   2727       C  
ATOM   1191  N   ILE A 228      66.103  40.206-192.276  1.00 58.24           N  
ANISOU 1191  N   ILE A 228     8201   7258   6670   2379   1815   2733       N  
ATOM   1192  CA  ILE A 228      64.847  40.464-191.585  1.00 56.50           C  
ANISOU 1192  CA  ILE A 228     7892   7069   6504   2540   1874   2808       C  
ATOM   1193  C   ILE A 228      64.141  41.607-192.304  1.00 60.87           C  
ANISOU 1193  C   ILE A 228     8463   7624   7040   2699   1947   2946       C  
ATOM   1194  O   ILE A 228      64.788  42.545-192.781  1.00 59.47           O  
ANISOU 1194  O   ILE A 228     8452   7310   6834   2692   2021   2942       O  
ATOM   1195  CB  ILE A 228      65.069  40.793-190.093  1.00 52.87           C  
ANISOU 1195  CB  ILE A 228     7561   6415   6111   2541   2003   2707       C  
ATOM   1196  CG1 ILE A 228      63.725  40.972-189.381  1.00 53.79           C  
ANISOU 1196  CG1 ILE A 228     7577   6585   6277   2707   2075   2789       C  
ATOM   1197  CG2 ILE A 228      65.943  42.032-189.941  1.00 50.85           C  
ANISOU 1197  CG2 ILE A 228     7555   5915   5851   2519   2142   2647       C  
ATOM   1198  CD1 ILE A 228      63.842  41.364-187.910  1.00 58.30           C  
ANISOU 1198  CD1 ILE A 228     8290   6966   6898   2720   2217   2696       C  
ATOM   1199  N   THR A 229      62.817  41.513-192.403  1.00 54.96           N  
ANISOU 1199  N   THR A 229     7537   7037   6307   2837   1926   3072       N  
ATOM   1200  CA  THR A 229      61.974  42.559-192.975  1.00 59.39           C  
ANISOU 1200  CA  THR A 229     8090   7617   6860   3009   2000   3220       C  
ATOM   1201  C   THR A 229      61.041  43.055-191.880  1.00 66.00           C  
ANISOU 1201  C   THR A 229     8911   8400   7765   3160   2144   3260       C  
ATOM   1202  O   THR A 229      60.408  42.247-191.190  1.00 64.76           O  
ANISOU 1202  O   THR A 229     8607   8353   7648   3163   2108   3257       O  
ATOM   1203  CB  THR A 229      61.177  42.037-194.175  1.00 56.21           C  
ANISOU 1203  CB  THR A 229     7479   7475   6404   3035   1843   3354       C  
ATOM   1204  OG1 THR A 229      62.084  41.572-195.181  1.00 62.31           O  
ANISOU 1204  OG1 THR A 229     8288   8290   7097   2888   1721   3310       O  
ATOM   1205  CG2 THR A 229      60.285  43.145-194.781  1.00 57.19           C  
ANISOU 1205  CG2 THR A 229     7591   7621   6519   3220   1916   3521       C  
ATOM   1206  N   VAL A 230      60.981  44.369-191.698  1.00 65.79           N  
ANISOU 1206  N   VAL A 230     9046   8203   7749   3278   2315   3295       N  
ATOM   1207  CA  VAL A 230      60.319  44.974-190.545  1.00 70.19           C  
ANISOU 1207  CA  VAL A 230     9653   8657   8359   3408   2490   3306       C  
ATOM   1208  C   VAL A 230      59.116  45.764-191.049  1.00 77.96           C  
ANISOU 1208  C   VAL A 230    10550   9727   9343   3613   2560   3494       C  
ATOM   1209  O   VAL A 230      59.264  46.868-191.591  1.00 74.29           O  
ANISOU 1209  O   VAL A 230    10222   9153   8853   3693   2647   3550       O  
ATOM   1210  CB  VAL A 230      61.270  45.865-189.740  1.00 63.07           C  
ANISOU 1210  CB  VAL A 230     9037   7465   7463   3367   2651   3176       C  
ATOM   1211  CG1 VAL A 230      60.550  46.464-188.553  1.00 63.65           C  
ANISOU 1211  CG1 VAL A 230     9172   7438   7574   3499   2837   3188       C  
ATOM   1212  CG2 VAL A 230      62.492  45.079-189.315  1.00 64.75           C  
ANISOU 1212  CG2 VAL A 230     9325   7604   7674   3155   2568   3000       C  
ATOM   1213  N   PHE A 231      57.925  45.207-190.855  1.00 68.71           N  
ANISOU 1213  N   PHE A 231     9153   8752   8203   3696   2524   3597       N  
ATOM   1214  CA  PHE A 231      56.674  45.869-191.186  1.00 68.18           C  
ANISOU 1214  CA  PHE A 231     8976   8784   8146   3894   2593   3785       C  
ATOM   1215  C   PHE A 231      56.343  46.904-190.106  1.00 72.26           C  
ANISOU 1215  C   PHE A 231     9649   9110   8698   4035   2839   3790       C  
ATOM   1216  O   PHE A 231      57.052  47.003-189.102  1.00 63.13           O  
ANISOU 1216  O   PHE A 231     8673   7762   7553   3964   2936   3641       O  
ATOM   1217  CB  PHE A 231      55.598  44.798-191.365  1.00 71.72           C  
ANISOU 1217  CB  PHE A 231     9121   9519   8612   3897   2451   3884       C  
ATOM   1218  CG  PHE A 231      55.801  43.956-192.585  1.00 77.14           C  
ANISOU 1218  CG  PHE A 231     9668  10397   9246   3777   2219   3902       C  
ATOM   1219  CD1 PHE A 231      55.555  44.482-193.847  1.00 77.74           C  
ANISOU 1219  CD1 PHE A 231     9713  10553   9270   3841   2159   4030       C  
ATOM   1220  CD2 PHE A 231      56.260  42.647-192.479  1.00 72.02           C  
ANISOU 1220  CD2 PHE A 231     8934   9842   8588   3597   2063   3792       C  
ATOM   1221  CE1 PHE A 231      55.749  43.725-194.981  1.00 78.87           C  
ANISOU 1221  CE1 PHE A 231     9749  10870   9348   3722   1950   4044       C  
ATOM   1222  CE2 PHE A 231      56.455  41.879-193.619  1.00 76.73           C  
ANISOU 1222  CE2 PHE A 231     9421  10611   9121   3481   1857   3805       C  
ATOM   1223  CZ  PHE A 231      56.197  42.425-194.874  1.00 76.88           C  
ANISOU 1223  CZ  PHE A 231     9418  10712   9083   3541   1801   3930       C  
ATOM   1224  N   PRO A 232      55.285  47.716-190.294  1.00 71.17           N  
ANISOU 1224  N   PRO A 232     9457   9014   8570   4233   2946   3960       N  
ATOM   1225  CA  PRO A 232      55.062  48.865-189.397  1.00 69.34           C  
ANISOU 1225  CA  PRO A 232     9417   8575   8355   4374   3198   3968       C  
ATOM   1226  C   PRO A 232      54.839  48.491-187.937  1.00 72.94           C  
ANISOU 1226  C   PRO A 232     9895   8972   8847   4359   3305   3888       C  
ATOM   1227  O   PRO A 232      54.293  47.433-187.618  1.00 71.54           O  
ANISOU 1227  O   PRO A 232     9512   8971   8699   4315   3209   3903       O  
ATOM   1228  CB  PRO A 232      53.806  49.524-189.978  1.00 79.67           C  
ANISOU 1228  CB  PRO A 232    10593  10006   9673   4588   3253   4193       C  
ATOM   1229  CG  PRO A 232      53.818  49.151-191.406  1.00 76.62           C  
ANISOU 1229  CG  PRO A 232    10058   9801   9252   4545   3046   4274       C  
ATOM   1230  CD  PRO A 232      54.356  47.756-191.443  1.00 73.55           C  
ANISOU 1230  CD  PRO A 232     9554   9533   8858   4337   2846   4153       C  
ATOM   1231  N   GLN A 233      55.231  49.413-187.051  1.00 79.51           N  
ANISOU 1231  N   GLN A 233    10989   9551   9669   4396   3511   3808       N  
ATOM   1232  CA  GLN A 233      55.101  49.204-185.613  1.00 78.13           C  
ANISOU 1232  CA  GLN A 233    10888   9285   9512   4380   3635   3724       C  
ATOM   1233  C   GLN A 233      53.646  49.325-185.175  1.00 79.94           C  
ANISOU 1233  C   GLN A 233    10967   9631   9775   4562   3747   3895       C  
ATOM   1234  O   GLN A 233      52.912  50.197-185.643  1.00 82.26           O  
ANISOU 1234  O   GLN A 233    11244   9942  10069   4741   3844   4054       O  
ATOM   1235  CB  GLN A 233      55.957  50.212-184.843  1.00 77.62           C  
ANISOU 1235  CB  GLN A 233    11166   8914   9412   4355   3820   3588       C  
ATOM   1236  CG  GLN A 233      55.682  51.668-185.208  1.00 82.04           C  
ANISOU 1236  CG  GLN A 233    11882   9343   9947   4525   3996   3690       C  
ATOM   1237  CD  GLN A 233      56.317  52.660-184.252  1.00 84.27           C  
ANISOU 1237  CD  GLN A 233    12503   9329  10189   4508   4205   3565       C  
ATOM   1238  OE1 GLN A 233      55.752  52.977-183.209  1.00 92.05           O  
ANISOU 1238  OE1 GLN A 233    13567  10238  11169   4592   4381   3579       O  
ATOM   1239  NE2 GLN A 233      57.493  53.163-184.611  1.00 86.81           N  
ANISOU 1239  NE2 GLN A 233    13031   9481  10473   4392   4188   3447       N  
ATOM   1240  N   ARG A 234      53.240  48.444-184.263  1.00 78.06           N  
ANISOU 1240  N   ARG A 234    10624   9469   9565   4516   3735   3867       N  
ATOM   1241  CA  ARG A 234      51.909  48.502-183.674  1.00 82.99           C  
ANISOU 1241  CA  ARG A 234    11122  10188  10223   4670   3853   4020       C  
ATOM   1242  C   ARG A 234      51.632  49.881-183.082  1.00 88.07           C  
ANISOU 1242  C   ARG A 234    11995  10621  10845   4836   4125   4067       C  
ATOM   1243  O   ARG A 234      52.510  50.507-182.483  1.00 90.41           O  
ANISOU 1243  O   ARG A 234    12581  10670  11101   4781   4246   3923       O  
ATOM   1244  CB  ARG A 234      51.789  47.420-182.597  1.00 78.63           C  
ANISOU 1244  CB  ARG A 234    10501   9682   9694   4565   3821   3941       C  
ATOM   1245  CG  ARG A 234      50.639  47.588-181.615  1.00 76.21           C  
ANISOU 1245  CG  ARG A 234    10155   9387   9413   4701   3992   4057       C  
ATOM   1246  CD  ARG A 234      50.724  46.543-180.531  1.00 74.50           C  
ANISOU 1246  CD  ARG A 234     9916   9179   9211   4575   3958   3955       C  
ATOM   1247  NE  ARG A 234      50.546  45.197-181.068  1.00 70.17           N  
ANISOU 1247  NE  ARG A 234     9086   8879   8696   4461   3715   3968       N  
ATOM   1248  CZ  ARG A 234      50.875  44.084-180.419  1.00 74.74           C  
ANISOU 1248  CZ  ARG A 234     9625   9486   9286   4311   3618   3856       C  
ATOM   1249  NH1 ARG A 234      51.418  44.145-179.207  1.00 67.76           N  
ANISOU 1249  NH1 ARG A 234     8964   8401   8382   4253   3736   3721       N  
ATOM   1250  NH2 ARG A 234      50.664  42.904-180.984  1.00 75.27           N  
ANISOU 1250  NH2 ARG A 234     9437   9782   9379   4213   3401   3878       N  
ATOM   1251  N   CYS A 235      50.406  50.358-183.262  1.00 90.77           N  
ANISOU 1251  N   CYS A 235    12210  11063  11214   5034   4218   4272       N  
ATOM   1252  CA  CYS A 235      49.986  51.632-182.700  1.00102.12           C  
ANISOU 1252  CA  CYS A 235    13847  12318  12636   5213   4485   4343       C  
ATOM   1253  C   CYS A 235      48.564  51.496-182.179  1.00102.30           C  
ANISOU 1253  C   CYS A 235    13689  12474  12707   5369   4578   4523       C  
ATOM   1254  O   CYS A 235      47.775  50.713-182.721  1.00 97.90           O  
ANISOU 1254  O   CYS A 235    12823  12179  12196   5383   4424   4647       O  
ATOM   1255  CB  CYS A 235      50.055  52.767-183.734  1.00110.56           C  
ANISOU 1255  CB  CYS A 235    14996  13326  13684   5340   4533   4433       C  
ATOM   1256  SG  CYS A 235      48.576  52.939-184.753  1.00121.49           S  
ANISOU 1256  SG  CYS A 235    16070  14971  15118   5560   4492   4726       S  
ATOM   1257  N   PRO A 236      48.214  52.236-181.125  1.00104.48           N  
ANISOU 1257  N   PRO A 236    14154  12575  12970   5479   4826   4542       N  
ATOM   1258  CA  PRO A 236      46.863  52.119-180.559  1.00105.70           C  
ANISOU 1258  CA  PRO A 236    14146  12841  13175   5630   4927   4717       C  
ATOM   1259  C   PRO A 236      45.795  52.561-181.547  1.00108.86           C  
ANISOU 1259  C   PRO A 236    14326  13418  13617   5830   4917   4956       C  
ATOM   1260  O   PRO A 236      46.020  53.424-182.399  1.00102.55           O  
ANISOU 1260  O   PRO A 236    13603  12564  12797   5914   4940   5002       O  
ATOM   1261  CB  PRO A 236      46.904  53.047-179.338  1.00104.05           C  
ANISOU 1261  CB  PRO A 236    14252  12357  12926   5709   5213   4674       C  
ATOM   1262  CG  PRO A 236      48.354  53.247-179.041  1.00103.92           C  
ANISOU 1262  CG  PRO A 236    14533  12114  12838   5531   5215   4434       C  
ATOM   1263  CD  PRO A 236      49.064  53.157-180.353  1.00103.54           C  
ANISOU 1263  CD  PRO A 236    14412  12142  12786   5453   5021   4395       C  
ATOM   1264  N   GLY A 237      44.617  51.948-181.426  1.00123.93           N  
ANISOU 1264  N   GLY A 237    15956  15543  15589   5902   4877   5113       N  
ATOM   1265  CA  GLY A 237      43.465  52.313-182.217  1.00135.74           C  
ANISOU 1265  CA  GLY A 237    17221  17222  17132   6098   4873   5355       C  
ATOM   1266  C   GLY A 237      43.290  51.545-183.510  1.00133.94           C  
ANISOU 1266  C   GLY A 237    16690  17277  16924   6026   4592   5423       C  
ATOM   1267  O   GLY A 237      42.159  51.440-184.000  1.00138.47           O  
ANISOU 1267  O   GLY A 237    16995  18069  17548   6147   4543   5626       O  
ATOM   1268  N   ARG A 238      44.367  51.008-184.079  1.00123.68           N  
ANISOU 1268  N   ARG A 238    15427  15980  15586   5831   4406   5262       N  
ATOM   1269  CA  ARG A 238      44.306  50.269-185.331  1.00121.75           C  
ANISOU 1269  CA  ARG A 238    14927  15987  15347   5744   4135   5309       C  
ATOM   1270  C   ARG A 238      44.803  48.842-185.130  1.00115.97           C  
ANISOU 1270  C   ARG A 238    14087  15362  14613   5502   3931   5159       C  
ATOM   1271  O   ARG A 238      45.557  48.546-184.200  1.00107.50           O  
ANISOU 1271  O   ARG A 238    13192  14128  13524   5383   3984   4982       O  
ATOM   1272  CB  ARG A 238      45.146  50.942-186.428  1.00127.32           C  
ANISOU 1272  CB  ARG A 238    15764  16609  16002   5737   4078   5271       C  
ATOM   1273  CG  ARG A 238      46.614  50.556-186.378  1.00128.01           C  
ANISOU 1273  CG  ARG A 238    16043  16553  16041   5521   3991   5028       C  
ATOM   1274  CD  ARG A 238      47.356  50.840-187.681  1.00130.24           C  
ANISOU 1274  CD  ARG A 238    16368  16837  16282   5474   3854   5006       C  
ATOM   1275  NE  ARG A 238      48.121  49.680-188.139  1.00132.92           N  
ANISOU 1275  NE  ARG A 238    16620  17283  16602   5245   3609   4872       N  
ATOM   1276  CZ  ARG A 238      49.214  49.209-187.541  1.00137.09           C  
ANISOU 1276  CZ  ARG A 238    17305  17672  17110   5068   3589   4658       C  
ATOM   1277  NH1 ARG A 238      49.686  49.784-186.441  1.00137.39           N  
ANISOU 1277  NH1 ARG A 238    17602  17461  17141   5080   3791   4546       N  
ATOM   1278  NH2 ARG A 238      49.834  48.148-188.038  1.00138.36           N  
ANISOU 1278  NH2 ARG A 238    17369  17945  17256   4876   3365   4557       N  
ATOM   1279  N   GLY A 239      44.387  47.962-186.034  1.00115.47           N  
ANISOU 1279  N   GLY A 239    13738  15572  14563   5427   3694   5232       N  
ATOM   1280  CA  GLY A 239      44.825  46.584-186.024  1.00107.52           C  
ANISOU 1280  CA  GLY A 239    12613  14687  13552   5199   3482   5103       C  
ATOM   1281  C   GLY A 239      46.314  46.476-186.326  1.00103.68           C  
ANISOU 1281  C   GLY A 239    12330  14053  13011   5036   3401   4895       C  
ATOM   1282  O   GLY A 239      47.032  47.461-186.506  1.00105.49           O  
ANISOU 1282  O   GLY A 239    12796  14079  13207   5088   3508   4842       O  
ATOM   1283  N   ASP A 240      46.781  45.232-186.387  1.00 97.43           N  
ANISOU 1283  N   ASP A 240    11439  13366  12212   4832   3205   4777       N  
ATOM   1284  CA  ASP A 240      48.201  44.952-186.557  1.00 87.28           C  
ANISOU 1284  CA  ASP A 240    10328  11950  10884   4662   3119   4573       C  
ATOM   1285  C   ASP A 240      48.474  44.231-187.868  1.00 81.41           C  
ANISOU 1285  C   ASP A 240     9425  11397  10110   4537   2859   4574       C  
ATOM   1286  O   ASP A 240      47.649  43.450-188.353  1.00 79.19           O  
ANISOU 1286  O   ASP A 240     8877  11371   9841   4505   2704   4677       O  
ATOM   1287  CB  ASP A 240      48.743  44.111-185.394  1.00 90.24           C  
ANISOU 1287  CB  ASP A 240    10778  12238  11270   4518   3126   4404       C  
ATOM   1288  CG  ASP A 240      49.328  44.963-184.295  1.00 94.18           C  
ANISOU 1288  CG  ASP A 240    11583  12441  11759   4565   3359   4298       C  
ATOM   1289  OD1 ASP A 240      49.769  46.090-184.600  1.00103.19           O  
ANISOU 1289  OD1 ASP A 240    12920  13417  12872   4649   3472   4293       O  
ATOM   1290  OD2 ASP A 240      49.348  44.508-183.134  1.00 94.12           O  
ANISOU 1290  OD2 ASP A 240    11630  12365  11768   4513   3425   4220       O  
ATOM   1291  N   PHE A 241      49.642  44.520-188.444  1.00 83.65           N  
ANISOU 1291  N   PHE A 241     9886  11550  10348   4461   2814   4458       N  
ATOM   1292  CA  PHE A 241      50.215  43.652-189.464  1.00 79.98           C  
ANISOU 1292  CA  PHE A 241     9327  11220   9843   4294   2570   4400       C  
ATOM   1293  C   PHE A 241      50.647  42.345-188.816  1.00 77.46           C  
ANISOU 1293  C   PHE A 241     8957  10940   9534   4107   2462   4254       C  
ATOM   1294  O   PHE A 241      51.306  42.355-187.771  1.00 69.59           O  
ANISOU 1294  O   PHE A 241     8136   9753   8553   4064   2571   4115       O  
ATOM   1295  CB  PHE A 241      51.419  44.315-190.126  1.00 75.99           C  
ANISOU 1295  CB  PHE A 241     9047  10540   9287   4257   2569   4308       C  
ATOM   1296  CG  PHE A 241      51.067  45.387-191.113  1.00 82.10           C  
ANISOU 1296  CG  PHE A 241     9839  11319  10035   4406   2606   4456       C  
ATOM   1297  CD1 PHE A 241      50.993  46.711-190.717  1.00 86.92           C  
ANISOU 1297  CD1 PHE A 241    10637  11731  10657   4575   2833   4500       C  
ATOM   1298  CD2 PHE A 241      50.830  45.072-192.439  1.00 83.90           C  
ANISOU 1298  CD2 PHE A 241     9911  11747  10221   4374   2413   4550       C  
ATOM   1299  CE1 PHE A 241      50.675  47.704-191.625  1.00 91.98           C  
ANISOU 1299  CE1 PHE A 241    11301  12370  11275   4718   2868   4641       C  
ATOM   1300  CE2 PHE A 241      50.510  46.062-193.356  1.00 88.69           C  
ANISOU 1300  CE2 PHE A 241    10540  12356  10800   4513   2441   4693       C  
ATOM   1301  CZ  PHE A 241      50.435  47.379-192.948  1.00 87.29           C  
ANISOU 1301  CZ  PHE A 241    10544  11978  10643   4690   2669   4741       C  
ATOM   1302  N   ARG A 242      50.279  41.222-189.435  1.00 86.01           N  
ANISOU 1302  N   ARG A 242     9807  12266  10605   3991   2247   4284       N  
ATOM   1303  CA  ARG A 242      50.640  39.902-188.933  1.00 87.32           C  
ANISOU 1303  CA  ARG A 242     9908  12489  10778   3809   2125   4156       C  
ATOM   1304  C   ARG A 242      50.709  38.912-190.087  1.00 84.19           C  
ANISOU 1304  C   ARG A 242     9344  12312  10334   3659   1868   4157       C  
ATOM   1305  O   ARG A 242      49.883  38.955-191.004  1.00 87.37           O  
ANISOU 1305  O   ARG A 242     9574  12907  10716   3701   1775   4302       O  
ATOM   1306  CB  ARG A 242      49.637  39.391-187.887  1.00 86.62           C  
ANISOU 1306  CB  ARG A 242     9678  12485  10747   3839   2185   4211       C  
ATOM   1307  CG  ARG A 242      49.616  40.168-186.578  1.00 90.00           C  
ANISOU 1307  CG  ARG A 242    10288  12693  11214   3958   2436   4186       C  
ATOM   1308  CD  ARG A 242      49.513  39.241-185.398  1.00 98.93           C  
ANISOU 1308  CD  ARG A 242    11387  13822  12381   3871   2445   4108       C  
ATOM   1309  NE  ARG A 242      50.508  38.177-185.473  1.00 97.05           N  
ANISOU 1309  NE  ARG A 242    11167  13585  12121   3670   2280   3943       N  
ATOM   1310  CZ  ARG A 242      50.558  37.153-184.632  1.00 93.90           C  
ANISOU 1310  CZ  ARG A 242    10723  13207  11747   3561   2235   3861       C  
ATOM   1311  NH1 ARG A 242      49.668  37.062-183.655  1.00 87.43           N  
ANISOU 1311  NH1 ARG A 242     9842  12406  10972   3628   2343   3928       N  
ATOM   1312  NH2 ARG A 242      51.494  36.221-184.771  1.00 93.65           N  
ANISOU 1312  NH2 ARG A 242    10714  13175  11695   3387   2085   3717       N  
ATOM   1313  N   ILE A 243      51.701  38.025-190.034  1.00 70.63           N  
ANISOU 1313  N   ILE A 243     7686  10560   8593   3481   1755   3995       N  
ATOM   1314  CA  ILE A 243      51.764  36.844-190.892  1.00 72.93           C  
ANISOU 1314  CA  ILE A 243     7821  11054   8834   3310   1514   3971       C  
ATOM   1315  C   ILE A 243      51.196  35.668-190.109  1.00 77.78           C  
ANISOU 1315  C   ILE A 243     8271  11793   9487   3215   1451   3947       C  
ATOM   1316  O   ILE A 243      51.651  35.378-188.996  1.00 72.29           O  
ANISOU 1316  O   ILE A 243     7673  10963   8832   3182   1531   3836       O  
ATOM   1317  CB  ILE A 243      53.205  36.551-191.348  1.00 71.49           C  
ANISOU 1317  CB  ILE A 243     7805  10762   8596   3171   1428   3814       C  
ATOM   1318  CG1 ILE A 243      53.768  37.705-192.185  1.00 76.02           C  
ANISOU 1318  CG1 ILE A 243     8542  11214   9126   3252   1485   3843       C  
ATOM   1319  CG2 ILE A 243      53.263  35.240-192.117  1.00 69.58           C  
ANISOU 1319  CG2 ILE A 243     7415  10724   8297   2985   1190   3777       C  
ATOM   1320  CD1 ILE A 243      54.755  38.581-191.439  1.00 75.03           C  
ANISOU 1320  CD1 ILE A 243     8687  10796   9027   3300   1667   3737       C  
ATOM   1321  N   TRP A 244      50.206  34.981-190.686  1.00 78.40           N  
ANISOU 1321  N   TRP A 244     8108  12128   9552   3164   1304   4049       N  
ATOM   1322  CA  TRP A 244      49.531  33.906-189.966  1.00 75.45           C  
ANISOU 1322  CA  TRP A 244     7567  11882   9218   3076   1249   4044       C  
ATOM   1323  C   TRP A 244      50.324  32.606-189.946  1.00 69.50           C  
ANISOU 1323  C   TRP A 244     6820  11154   8434   2861   1089   3883       C  
ATOM   1324  O   TRP A 244      50.116  31.784-189.047  1.00 71.82           O  
ANISOU 1324  O   TRP A 244     7052  11468   8768   2789   1084   3833       O  
ATOM   1325  CB  TRP A 244      48.146  33.660-190.566  1.00 77.75           C  
ANISOU 1325  CB  TRP A 244     7597  12437   9507   3089   1151   4214       C  
ATOM   1326  CG  TRP A 244      47.134  34.651-190.092  1.00 83.73           C  
ANISOU 1326  CG  TRP A 244     8308  13182  10323   3297   1330   4375       C  
ATOM   1327  CD1 TRP A 244      47.347  35.971-189.820  1.00 82.29           C  
ANISOU 1327  CD1 TRP A 244     8297  12808  10162   3484   1530   4412       C  
ATOM   1328  CD2 TRP A 244      45.756  34.398-189.797  1.00 87.54           C  
ANISOU 1328  CD2 TRP A 244     8566  13844  10852   3340   1331   4521       C  
ATOM   1329  NE1 TRP A 244      46.183  36.559-189.387  1.00 83.34           N  
ANISOU 1329  NE1 TRP A 244     8328  12990  10348   3647   1660   4574       N  
ATOM   1330  CE2 TRP A 244      45.192  35.613-189.363  1.00 88.38           C  
ANISOU 1330  CE2 TRP A 244     8718  13858  11005   3565   1540   4647       C  
ATOM   1331  CE3 TRP A 244      44.943  33.261-189.862  1.00 88.24           C  
ANISOU 1331  CE3 TRP A 244     8423  14159  10944   3204   1177   4557       C  
ATOM   1332  CZ2 TRP A 244      43.854  35.725-188.997  1.00 90.95           C  
ANISOU 1332  CZ2 TRP A 244     8858  14315  11385   3667   1601   4813       C  
ATOM   1333  CZ3 TRP A 244      43.615  33.374-189.501  1.00 85.70           C  
ANISOU 1333  CZ3 TRP A 244     7915  13969  10676   3296   1233   4720       C  
ATOM   1334  CH2 TRP A 244      43.084  34.596-189.072  1.00 88.90           C  
ANISOU 1334  CH2 TRP A 244     8364  14283  11133   3531   1443   4850       C  
ATOM   1335  N   ASN A 245      51.218  32.400-190.905  1.00 70.28           N  
ANISOU 1335  N   ASN A 245     6995  11249   8458   2760    965   3806       N  
ATOM   1336  CA  ASN A 245      52.082  31.233-190.897  1.00 65.20           C  
ANISOU 1336  CA  ASN A 245     6384  10608   7780   2566    828   3650       C  
ATOM   1337  C   ASN A 245      53.218  31.429-189.902  1.00 62.62           C  
ANISOU 1337  C   ASN A 245     6275  10028   7490   2577    952   3510       C  
ATOM   1338  O   ASN A 245      53.718  32.541-189.707  1.00 59.12           O  
ANISOU 1338  O   ASN A 245     6008   9394   7062   2699   1104   3506       O  
ATOM   1339  CB  ASN A 245      52.655  30.982-192.295  1.00 67.87           C  
ANISOU 1339  CB  ASN A 245     6745  11026   8017   2457    662   3622       C  
ATOM   1340  CG  ASN A 245      51.645  31.245-193.394  1.00 72.83           C  
ANISOU 1340  CG  ASN A 245     7216  11857   8601   2491    575   3777       C  
ATOM   1341  OD1 ASN A 245      51.280  32.394-193.652  1.00 75.57           O  
ANISOU 1341  OD1 ASN A 245     7588  12165   8961   2657    679   3894       O  
ATOM   1342  ND2 ASN A 245      51.190  30.182-194.050  1.00 68.10           N  
ANISOU 1342  ND2 ASN A 245     6461  11470   7945   2330    380   3780       N  
ATOM   1343  N   SER A 246      53.626  30.328-189.266  1.00 59.56           N  
ANISOU 1343  N   SER A 246     5879   9636   7115   2442    883   3393       N  
ATOM   1344  CA  SER A 246      54.749  30.381-188.338  1.00 56.98           C  
ANISOU 1344  CA  SER A 246     5754   9079   6817   2431    975   3255       C  
ATOM   1345  C   SER A 246      56.065  30.621-189.065  1.00 59.46           C  
ANISOU 1345  C   SER A 246     6245   9278   7068   2375    936   3163       C  
ATOM   1346  O   SER A 246      56.967  31.266-188.521  1.00 56.67           O  
ANISOU 1346  O   SER A 246     6096   8700   6734   2417   1058   3087       O  
ATOM   1347  CB  SER A 246      54.824  29.080-187.548  1.00 51.65           C  
ANISOU 1347  CB  SER A 246     5012   8444   6167   2298    894   3164       C  
ATOM   1348  OG  SER A 246      55.167  28.007-188.413  1.00 56.23           O  
ANISOU 1348  OG  SER A 246     5523   9164   6679   2123    689   3105       O  
ATOM   1349  N   GLN A 247      56.199  30.100-190.280  1.00 64.07           N  
ANISOU 1349  N   GLN A 247     6763  10009   7571   2268    769   3166       N  
ATOM   1350  CA  GLN A 247      57.343  30.370-191.134  1.00 61.08           C  
ANISOU 1350  CA  GLN A 247     6542   9547   7120   2218    734   3102       C  
ATOM   1351  C   GLN A 247      56.845  30.732-192.523  1.00 56.17           C  
ANISOU 1351  C   GLN A 247     5843   9076   6424   2238    652   3211       C  
ATOM   1352  O   GLN A 247      55.672  30.534-192.856  1.00 55.01           O  
ANISOU 1352  O   GLN A 247     5506   9118   6276   2254    587   3319       O  
ATOM   1353  CB  GLN A 247      58.296  29.176-191.214  1.00 53.96           C  
ANISOU 1353  CB  GLN A 247     5679   8656   6169   2035    604   2964       C  
ATOM   1354  CG  GLN A 247      59.045  28.912-189.932  1.00 51.88           C  
ANISOU 1354  CG  GLN A 247     5533   8214   5967   2013    683   2851       C  
ATOM   1355  CD  GLN A 247      59.973  27.728-190.055  1.00 52.55           C  
ANISOU 1355  CD  GLN A 247     5651   8318   5998   1839    555   2727       C  
ATOM   1356  OE1 GLN A 247      60.495  27.433-191.137  1.00 58.35           O  
ANISOU 1356  OE1 GLN A 247     6409   9118   6643   1741    456   2690       O  
ATOM   1357  NE2 GLN A 247      60.184  27.037-188.948  1.00 55.34           N  
ANISOU 1357  NE2 GLN A 247     6019   8592   6418   1757    569   2599       N  
ATOM   1358  N   LEU A 248      57.751  31.267-193.342  1.00 50.92           N  
ANISOU 1358  N   LEU A 248     5330   8324   5693   2229    656   3184       N  
ATOM   1359  CA  LEU A 248      57.354  31.641-194.696  1.00 59.27           C  
ANISOU 1359  CA  LEU A 248     6337   9513   6670   2246    577   3286       C  
ATOM   1360  C   LEU A 248      57.190  30.401-195.564  1.00 60.94           C  
ANISOU 1360  C   LEU A 248     6426   9939   6788   2071    366   3259       C  
ATOM   1361  O   LEU A 248      56.254  30.316-196.368  1.00 61.18           O  
ANISOU 1361  O   LEU A 248     6312  10157   6775   2067    266   3364       O  
ATOM   1362  CB  LEU A 248      58.373  32.613-195.292  1.00 57.26           C  
ANISOU 1362  CB  LEU A 248     6293   9093   6369   2286    656   3267       C  
ATOM   1363  CG  LEU A 248      58.524  33.918-194.497  1.00 57.69           C  
ANISOU 1363  CG  LEU A 248     6489   8925   6507   2448    869   3288       C  
ATOM   1364  CD1 LEU A 248      59.547  34.843-195.127  1.00 56.51           C  
ANISOU 1364  CD1 LEU A 248     6549   8612   6309   2463    939   3265       C  
ATOM   1365  CD2 LEU A 248      57.190  34.629-194.356  1.00 60.01           C  
ANISOU 1365  CD2 LEU A 248     6657   9291   6853   2613    939   3442       C  
ATOM   1366  N   VAL A 249      58.062  29.412-195.381  1.00 56.28           N  
ANISOU 1366  N   VAL A 249     5893   9324   6165   1921    296   3120       N  
ATOM   1367  CA  VAL A 249      57.964  28.122-196.054  1.00 59.97           C  
ANISOU 1367  CA  VAL A 249     6266   9977   6544   1738    105   3067       C  
ATOM   1368  C   VAL A 249      57.553  27.072-195.021  1.00 60.76           C  
ANISOU 1368  C   VAL A 249     6249  10126   6711   1662     64   3009       C  
ATOM   1369  O   VAL A 249      58.256  26.862-194.022  1.00 59.53           O  
ANISOU 1369  O   VAL A 249     6181   9825   6613   1656    135   2915       O  
ATOM   1370  CB  VAL A 249      59.284  27.739-196.741  1.00 56.30           C  
ANISOU 1370  CB  VAL A 249     5962   9456   5973   1616     56   2952       C  
ATOM   1371  CG1 VAL A 249      59.059  26.577-197.688  1.00 64.45           C  
ANISOU 1371  CG1 VAL A 249     6911  10688   6888   1436   -137   2913       C  
ATOM   1372  CG2 VAL A 249      59.874  28.931-197.485  1.00 57.73           C  
ANISOU 1372  CG2 VAL A 249     6297   9528   6109   1706    146   2999       C  
ATOM   1373  N   ARG A 250      56.408  26.425-195.257  1.00 59.90           N  
ANISOU 1373  N   ARG A 250     5945  10220   6594   1598    -51   3069       N  
ATOM   1374  CA  ARG A 250      55.905  25.330-194.437  1.00 55.64           C  
ANISOU 1374  CA  ARG A 250     5280   9756   6105   1498   -111   3020       C  
ATOM   1375  C   ARG A 250      55.246  24.301-195.346  1.00 68.18           C  
ANISOU 1375  C   ARG A 250     6735  11568   7605   1322   -304   3020       C  
ATOM   1376  O   ARG A 250      54.750  24.640-196.424  1.00 72.47           O  
ANISOU 1376  O   ARG A 250     7230  12229   8077   1326   -371   3108       O  
ATOM   1377  CB  ARG A 250      54.877  25.806-193.406  1.00 60.81           C  
ANISOU 1377  CB  ARG A 250     5818  10406   6880   1634      6   3121       C  
ATOM   1378  CG  ARG A 250      55.383  26.818-192.399  1.00 67.60           C  
ANISOU 1378  CG  ARG A 250     6817  11040   7829   1804    209   3119       C  
ATOM   1379  CD  ARG A 250      55.686  26.146-191.061  1.00 72.88           C  
ANISOU 1379  CD  ARG A 250     7507  11613   8572   1763    252   3021       C  
ATOM   1380  NE  ARG A 250      56.881  25.315-191.140  1.00 81.62           N  
ANISOU 1380  NE  ARG A 250     8728  12659   9627   1621    167   2872       N  
ATOM   1381  CZ  ARG A 250      57.321  24.537-190.159  1.00 81.99           C  
ANISOU 1381  CZ  ARG A 250     8802  12633   9715   1552    164   2772       C  
ATOM   1382  NH1 ARG A 250      56.660  24.471-189.010  1.00 79.35           N  
ANISOU 1382  NH1 ARG A 250     8394  12279   9476   1609    242   2801       N  
ATOM   1383  NH2 ARG A 250      58.426  23.823-190.332  1.00 83.95           N  
ANISOU 1383  NH2 ARG A 250     9173  12803   9922   1397    104   2596       N  
ATOM   1384  N   TYR A 251      55.232  23.045-194.902  1.00 60.30           N  
ANISOU 1384  N   TYR A 251     5684  10620   6608   1162   -395   2920       N  
ATOM   1385  CA  TYR A 251      54.592  21.969-195.650  1.00 58.08           C  
ANISOU 1385  CA  TYR A 251     5290  10534   6245    969   -575   2901       C  
ATOM   1386  C   TYR A 251      53.209  21.656-195.086  1.00 59.44           C  
ANISOU 1386  C   TYR A 251     5255  10836   6493    960   -589   2992       C  
ATOM   1387  O   TYR A 251      52.991  21.687-193.872  1.00 57.85           O  
ANISOU 1387  O   TYR A 251     5014  10565   6402   1030   -488   3000       O  
ATOM   1388  CB  TYR A 251      55.443  20.701-195.631  1.00 54.85           C  
ANISOU 1388  CB  TYR A 251     4967  10099   5775    773   -673   2724       C  
ATOM   1389  CG  TYR A 251      56.711  20.770-196.447  1.00 54.36           C  
ANISOU 1389  CG  TYR A 251     5093   9959   5602    735   -690   2632       C  
ATOM   1390  CD1 TYR A 251      56.689  21.174-197.779  1.00 52.19           C  
ANISOU 1390  CD1 TYR A 251     4856   9762   5214    724   -747   2681       C  
ATOM   1391  CD2 TYR A 251      57.930  20.428-195.888  1.00 48.78           C  
ANISOU 1391  CD2 TYR A 251     4528   9105   4900    708   -646   2502       C  
ATOM   1392  CE1 TYR A 251      57.854  21.232-198.534  1.00 49.98           C  
ANISOU 1392  CE1 TYR A 251     4754   9413   4825    685   -749   2598       C  
ATOM   1393  CE2 TYR A 251      59.096  20.483-196.624  1.00 54.29           C  
ANISOU 1393  CE2 TYR A 251     5404   9716   5507    663   -635   2402       C  
ATOM   1394  CZ  TYR A 251      59.054  20.883-197.952  1.00 55.53           C  
ANISOU 1394  CZ  TYR A 251     5591   9973   5534    658   -694   2470       C  
ATOM   1395  OH  TYR A 251      60.215  20.936-198.693  1.00 54.34           O  
ANISOU 1395  OH  TYR A 251     5620   9738   5289    611   -669   2370       O  
ATOM   1396  N   ALA A 252      52.282  21.317-195.982  1.00 55.02           N  
ANISOU 1396  N   ALA A 252     4571  10468   5868    863   -717   3061       N  
ATOM   1397  CA  ALA A 252      50.913  21.048-195.563  1.00 56.93           C  
ANISOU 1397  CA  ALA A 252     4608  10852   6172    848   -734   3164       C  
ATOM   1398  C   ALA A 252      50.832  19.779-194.709  1.00 53.99           C  
ANISOU 1398  C   ALA A 252     4194  10484   5837    685   -780   3056       C  
ATOM   1399  O   ALA A 252      51.683  18.892-194.786  1.00 54.32           O  
ANISOU 1399  O   ALA A 252     4346  10469   5824    535   -853   2899       O  
ATOM   1400  CB  ALA A 252      50.000  20.912-196.779  1.00 58.90           C  
ANISOU 1400  CB  ALA A 252     4741  11307   6331    760   -877   3257       C  
ATOM   1401  N   GLY A 253      49.776  19.702-193.896  1.00 61.26           N  
ANISOU 1401  N   GLY A 253     4957  11472   6849    718   -733   3146       N  
ATOM   1402  CA  GLY A 253      49.433  18.496-193.159  1.00 60.05           C  
ANISOU 1402  CA  GLY A 253     4734  11353   6728    554   -785   3072       C  
ATOM   1403  C   GLY A 253      47.947  18.196-193.226  1.00 66.89           C  
ANISOU 1403  C   GLY A 253     5390  12415   7612    495   -840   3198       C  
ATOM   1404  O   GLY A 253      47.134  19.024-192.805  1.00 62.04           O  
ANISOU 1404  O   GLY A 253     4662  11837   7073    663   -733   3350       O  
ATOM   1405  N   TYR A 254      47.576  17.023-193.750  1.00 88.23           N  
ANISOU 1405  N   TYR A 254     8044  15237  10241    256  -1000   3138       N  
ATOM   1406  CA  TYR A 254      46.191  16.678-194.065  1.00 95.11           C  
ANISOU 1406  CA  TYR A 254     8721  16313  11104    168  -1084   3256       C  
ATOM   1407  C   TYR A 254      45.723  15.483-193.239  1.00 99.79           C  
ANISOU 1407  C   TYR A 254     9245  16932  11736     -4  -1118   3195       C  
ATOM   1408  O   TYR A 254      46.494  14.554-192.992  1.00105.71           O  
ANISOU 1408  O   TYR A 254    10117  17585  12461   -152  -1161   3028       O  
ATOM   1409  CB  TYR A 254      46.025  16.333-195.558  1.00 96.07           C  
ANISOU 1409  CB  TYR A 254     8845  16571  11088     15  -1259   3251       C  
ATOM   1410  CG  TYR A 254      46.637  17.301-196.559  1.00 99.99           C  
ANISOU 1410  CG  TYR A 254     9441  17038  11514    135  -1258   3281       C  
ATOM   1411  CD1 TYR A 254      46.197  18.618-196.653  1.00103.26           C  
ANISOU 1411  CD1 TYR A 254     9782  17478  11975    365  -1162   3450       C  
ATOM   1412  CD2 TYR A 254      47.622  16.878-197.447  1.00101.03           C  
ANISOU 1412  CD2 TYR A 254     9744  17117  11524     13  -1351   3141       C  
ATOM   1413  CE1 TYR A 254      46.743  19.497-197.587  1.00100.01           C  
ANISOU 1413  CE1 TYR A 254     9468  17036  11496    469  -1161   3480       C  
ATOM   1414  CE2 TYR A 254      48.173  17.747-198.382  1.00101.46           C  
ANISOU 1414  CE2 TYR A 254     9894  17148  11508    116  -1349   3172       C  
ATOM   1415  CZ  TYR A 254      47.728  19.054-198.449  1.00 97.78           C  
ANISOU 1415  CZ  TYR A 254     9353  16705  11093    341  -1257   3342       C  
ATOM   1416  OH  TYR A 254      48.272  19.919-199.376  1.00 91.15           O  
ANISOU 1416  OH  TYR A 254     8617  15834  10181    440  -1253   3374       O  
ATOM   1417  N   ARG A 255      44.443  15.482-192.855  1.00102.25           N  
ANISOU 1417  N   ARG A 255     9364  17381  12107      9  -1102   3333       N  
ATOM   1418  CA  ARG A 255      43.860  14.408-192.057  1.00100.71           C  
ANISOU 1418  CA  ARG A 255     9089  17224  11954   -149  -1126   3298       C  
ATOM   1419  C   ARG A 255      43.182  13.366-192.957  1.00112.49           C  
ANISOU 1419  C   ARG A 255    10511  18881  13348   -408  -1313   3282       C  
ATOM   1420  O   ARG A 255      43.233  13.449-194.188  1.00117.89           O  
ANISOU 1420  O   ARG A 255    11220  19644  13928   -468  -1426   3287       O  
ATOM   1421  CB  ARG A 255      42.864  14.983-191.054  1.00 99.06           C  
ANISOU 1421  CB  ARG A 255     8715  17061  11864     13   -990   3456       C  
ATOM   1422  CG  ARG A 255      43.301  16.271-190.387  1.00101.04           C  
ANISOU 1422  CG  ARG A 255     9022  17171  12198    297   -799   3514       C  
ATOM   1423  CD  ARG A 255      42.118  16.914-189.677  1.00109.56           C  
ANISOU 1423  CD  ARG A 255     9926  18329  13374    459   -676   3697       C  
ATOM   1424  NE  ARG A 255      42.531  17.769-188.569  1.00113.41           N  
ANISOU 1424  NE  ARG A 255    10492  18642  13956    684   -471   3710       N  
ATOM   1425  CZ  ARG A 255      42.818  17.319-187.351  1.00116.89           C  
ANISOU 1425  CZ  ARG A 255    10984  18966  14465    671   -384   3630       C  
ATOM   1426  NH1 ARG A 255      42.744  16.021-187.086  1.00118.93           N  
ANISOU 1426  NH1 ARG A 255    11219  19260  14709    443   -483   3531       N  
ATOM   1427  NH2 ARG A 255      43.185  18.165-186.398  1.00115.11           N  
ANISOU 1427  NH2 ARG A 255    10841  18578  14315    880   -195   3645       N  
ATOM   1428  N   GLN A 256      42.526  12.381-192.348  1.00115.98           N  
ANISOU 1428  N   GLN A 256    10871  19376  13820   -567  -1346   3263       N  
ATOM   1429  CA  GLN A 256      41.790  11.340-193.077  1.00118.85           C  
ANISOU 1429  CA  GLN A 256    11168  19893  14098   -826  -1514   3251       C  
ATOM   1430  C   GLN A 256      40.544  10.961-192.278  1.00117.61           C  
ANISOU 1430  C   GLN A 256    10814  19852  14020   -869  -1489   3358       C  
ATOM   1431  O   GLN A 256      40.060  11.743-191.453  1.00121.62           O  
ANISOU 1431  O   GLN A 256    11206  20367  14636   -669  -1352   3486       O  
ATOM   1432  CB  GLN A 256      42.689  10.117-193.348  1.00117.45           C  
ANISOU 1432  CB  GLN A 256    11185  19605  13834  -1063  -1611   3033       C  
ATOM   1433  CG  GLN A 256      43.442  10.159-194.667  1.00119.75           C  
ANISOU 1433  CG  GLN A 256    11624  19882  13995  -1122  -1714   2950       C  
ATOM   1434  CD  GLN A 256      44.767  10.891-194.561  1.00112.53           C  
ANISOU 1434  CD  GLN A 256    10873  18790  13092   -950  -1620   2873       C  
ATOM   1435  OE1 GLN A 256      45.319  11.035-193.470  1.00109.42           O  
ANISOU 1435  OE1 GLN A 256    10528  18255  12792   -846  -1500   2828       O  
ATOM   1436  NE2 GLN A 256      45.281  11.364-195.697  1.00 98.88           N  
ANISOU 1436  NE2 GLN A 256     9233  17071  11267   -921  -1676   2861       N  
ATOM   1437  N   GLN A 257      40.021   9.753-192.530  1.00108.07           N  
ANISOU 1437  N   GLN A 257     9576  18731  12755  -1134  -1618   3305       N  
ATOM   1438  CA  GLN A 257      39.019   9.156-191.651  1.00108.19           C  
ANISOU 1438  CA  GLN A 257     9440  18824  12843  -1216  -1595   3366       C  
ATOM   1439  C   GLN A 257      39.551   8.969-190.235  1.00117.81           C  
ANISOU 1439  C   GLN A 257    10732  19867  14163  -1152  -1454   3285       C  
ATOM   1440  O   GLN A 257      38.761   8.761-189.305  1.00122.14           O  
ANISOU 1440  O   GLN A 257    11150  20461  14796  -1149  -1387   3357       O  
ATOM   1441  CB  GLN A 257      38.535   7.810-192.243  1.00101.05           C  
ANISOU 1441  CB  GLN A 257     8535  18015  11844  -1536  -1764   3294       C  
ATOM   1442  CG  GLN A 257      38.402   6.619-191.256  1.00 97.28           C  
ANISOU 1442  CG  GLN A 257     8085  17469  11408  -1716  -1749   3197       C  
ATOM   1443  CD  GLN A 257      37.011   5.980-191.255  1.00 98.72           C  
ANISOU 1443  CD  GLN A 257     8072  17846  11592  -1883  -1826   3300       C  
ATOM   1444  OE1 GLN A 257      36.292   6.034-192.254  1.00102.50           O  
ANISOU 1444  OE1 GLN A 257     8443  18504  12000  -1959  -1945   3391       O  
ATOM   1445  NE2 GLN A 257      36.630   5.374-190.129  1.00 74.20           N  
ANISOU 1445  NE2 GLN A 257     4917  14707   8567  -1943  -1758   3288       N  
ATOM   1446  N   ASP A 258      40.864   9.111-190.048  1.00125.30           N  
ANISOU 1446  N   ASP A 258    11880  20621  15107  -1088  -1401   3149       N  
ATOM   1447  CA  ASP A 258      41.570   8.685-188.849  1.00122.73           C  
ANISOU 1447  CA  ASP A 258    11664  20115  14851  -1087  -1304   3032       C  
ATOM   1448  C   ASP A 258      42.455   9.788-188.280  1.00122.95           C  
ANISOU 1448  C   ASP A 258    11775  19995  14947   -823  -1153   3035       C  
ATOM   1449  O   ASP A 258      43.437   9.499-187.591  1.00121.94           O  
ANISOU 1449  O   ASP A 258    11793  19693  14847   -825  -1099   2904       O  
ATOM   1450  CB  ASP A 258      42.408   7.445-189.157  1.00112.40           C  
ANISOU 1450  CB  ASP A 258    10548  18700  13460  -1330  -1411   2825       C  
ATOM   1451  CG  ASP A 258      42.851   7.394-190.614  1.00104.05           C  
ANISOU 1451  CG  ASP A 258     9590  17674  12272  -1415  -1543   2765       C  
ATOM   1452  OD1 ASP A 258      41.975   7.439-191.509  1.00101.05           O  
ANISOU 1452  OD1 ASP A 258     9093  17470  11830  -1481  -1640   2863       O  
ATOM   1453  OD2 ASP A 258      44.072   7.330-190.871  1.00 95.62           O  
ANISOU 1453  OD2 ASP A 258     8713  16458  11159  -1414  -1549   2624       O  
ATOM   1454  N   GLY A 259      42.150  11.050-188.579  1.00125.26           N  
ANISOU 1454  N   GLY A 259    11985  20346  15263   -600  -1086   3180       N  
ATOM   1455  CA  GLY A 259      42.901  12.165-188.027  1.00123.43           C  
ANISOU 1455  CA  GLY A 259    11834  19969  15096   -344   -930   3195       C  
ATOM   1456  C   GLY A 259      44.367  12.223-188.417  1.00117.89           C  
ANISOU 1456  C   GLY A 259    11344  19108  14339   -340   -952   3042       C  
ATOM   1457  O   GLY A 259      44.868  13.291-188.790  1.00116.85           O  
ANISOU 1457  O   GLY A 259    11268  18926  14202   -156   -893   3082       O  
ATOM   1458  N   SER A 260      45.060  11.080-188.324  1.00109.66           N  
ANISOU 1458  N   SER A 260    10427  17982  13258   -542  -1031   2870       N  
ATOM   1459  CA  SER A 260      46.470  10.932-188.682  1.00102.11           C  
ANISOU 1459  CA  SER A 260     9673  16877  12245   -570  -1065   2709       C  
ATOM   1460  C   SER A 260      46.796  11.617-190.004  1.00 94.89           C  
ANISOU 1460  C   SER A 260     8806  16007  11240   -513  -1126   2733       C  
ATOM   1461  O   SER A 260      45.927  11.749-190.873  1.00 93.23           O  
ANISOU 1461  O   SER A 260     8486  15959  10977   -550  -1203   2834       O  
ATOM   1462  CB  SER A 260      46.845   9.452-188.755  1.00102.35           C  
ANISOU 1462  CB  SER A 260     9808  16862  12218   -842  -1180   2539       C  
ATOM   1463  OG  SER A 260      46.197   8.823-189.845  1.00106.38           O  
ANISOU 1463  OG  SER A 260    10279  17512  12628  -1030  -1326   2543       O  
ATOM   1464  N   VAL A 261      48.047  12.036-190.174  1.00 88.05           N  
ANISOU 1464  N   VAL A 261     8102  15000  10352   -428  -1096   2642       N  
ATOM   1465  CA  VAL A 261      48.391  13.116-191.091  1.00 83.93           C  
ANISOU 1465  CA  VAL A 261     7619  14489   9782   -280  -1084   2702       C  
ATOM   1466  C   VAL A 261      49.276  12.609-192.221  1.00 86.84           C  
ANISOU 1466  C   VAL A 261     8142  14830  10022   -421  -1208   2565       C  
ATOM   1467  O   VAL A 261      50.246  11.878-191.985  1.00 83.47           O  
ANISOU 1467  O   VAL A 261     7860  14279   9575   -522  -1231   2403       O  
ATOM   1468  CB  VAL A 261      49.080  14.273-190.347  1.00 75.56           C  
ANISOU 1468  CB  VAL A 261     6622  13283   8806    -25   -918   2735       C  
ATOM   1469  CG1 VAL A 261      49.228  15.470-191.267  1.00 76.25           C  
ANISOU 1469  CG1 VAL A 261     6732  13390   8850    136   -893   2825       C  
ATOM   1470  CG2 VAL A 261      48.298  14.639-189.099  1.00 69.01           C  
ANISOU 1470  CG2 VAL A 261     5670  12451   8099    102   -782   2843       C  
ATOM   1471  N   ARG A 262      48.930  13.003-193.448  1.00 89.19           N  
ANISOU 1471  N   ARG A 262     8411  15244  10231   -426  -1284   2634       N  
ATOM   1472  CA  ARG A 262      49.843  12.983-194.582  1.00 85.12           C  
ANISOU 1472  CA  ARG A 262     8053  14695   9594   -480  -1360   2539       C  
ATOM   1473  C   ARG A 262      50.423  14.390-194.708  1.00 76.15           C  
ANISOU 1473  C   ARG A 262     6965  13489   8481   -234  -1251   2614       C  
ATOM   1474  O   ARG A 262      49.674  15.366-194.832  1.00 79.69           O  
ANISOU 1474  O   ARG A 262     7295  14017   8966    -80  -1199   2779       O  
ATOM   1475  CB  ARG A 262      49.110  12.560-195.859  1.00 90.71           C  
ANISOU 1475  CB  ARG A 262     8712  15570  10183   -642  -1509   2570       C  
ATOM   1476  CG  ARG A 262      49.977  12.356-197.114  1.00 90.76           C  
ANISOU 1476  CG  ARG A 262     8892  15550  10042   -735  -1599   2460       C  
ATOM   1477  CD  ARG A 262      49.245  11.487-198.153  1.00 92.94           C  
ANISOU 1477  CD  ARG A 262     9143  15970  10198   -965  -1759   2445       C  
ATOM   1478  NE  ARG A 262      49.888  11.456-199.470  1.00 87.47           N  
ANISOU 1478  NE  ARG A 262     8603  15279   9355  -1036  -1840   2372       N  
ATOM   1479  CZ  ARG A 262      50.783  10.549-199.859  1.00 87.29           C  
ANISOU 1479  CZ  ARG A 262     8774  15157   9236  -1195  -1888   2185       C  
ATOM   1480  NH1 ARG A 262      51.165   9.585-199.034  1.00 93.56           N  
ANISOU 1480  NH1 ARG A 262     9635  15838  10074  -1301  -1868   2050       N  
ATOM   1481  NH2 ARG A 262      51.303  10.607-201.077  1.00 87.09           N  
ANISOU 1481  NH2 ARG A 262     8883  15140   9067  -1246  -1949   2132       N  
ATOM   1482  N   GLY A 263      51.741  14.500-194.637  1.00 66.78           N  
ANISOU 1482  N   GLY A 263     5952  12146   7274   -194  -1211   2498       N  
ATOM   1483  CA  GLY A 263      52.410  15.791-194.554  1.00 60.54           C  
ANISOU 1483  CA  GLY A 263     5230  11253   6517     36  -1088   2555       C  
ATOM   1484  C   GLY A 263      52.965  16.068-193.163  1.00 66.68           C  
ANISOU 1484  C   GLY A 263     6047  11871   7416    165   -950   2527       C  
ATOM   1485  O   GLY A 263      53.241  15.162-192.366  1.00 61.87           O  
ANISOU 1485  O   GLY A 263     5461  11201   6844     61   -963   2421       O  
ATOM   1486  N   ASP A 264      53.128  17.370-192.873  1.00 60.50           N  
ANISOU 1486  N   ASP A 264     5282  11012   6694    395   -812   2625       N  
ATOM   1487  CA  ASP A 264      53.721  17.810-191.614  1.00 52.01           C  
ANISOU 1487  CA  ASP A 264     4270   9767   5725    537   -667   2605       C  
ATOM   1488  C   ASP A 264      52.634  17.987-190.563  1.00 58.18           C  
ANISOU 1488  C   ASP A 264     4901  10583   6620    618   -577   2710       C  
ATOM   1489  O   ASP A 264      51.781  18.870-190.718  1.00 64.21           O  
ANISOU 1489  O   ASP A 264     5570  11413   7412    752   -511   2859       O  
ATOM   1490  CB  ASP A 264      54.474  19.121-191.810  1.00 46.52           C  
ANISOU 1490  CB  ASP A 264     3699   8946   5032    735   -551   2647       C  
ATOM   1491  CG  ASP A 264      55.361  19.474-190.620  1.00 52.94           C  
ANISOU 1491  CG  ASP A 264     4629   9557   5930    849   -417   2592       C  
ATOM   1492  OD1 ASP A 264      55.170  18.883-189.532  1.00 49.00           O  
ANISOU 1492  OD1 ASP A 264     4101   9007   5511    805   -382   2537       O  
ATOM   1493  OD2 ASP A 264      56.265  20.345-190.775  1.00 49.95           O  
ANISOU 1493  OD2 ASP A 264     4408   9026   5543    957   -324   2568       O  
ATOM   1494  N   PRO A 265      52.636  17.198-189.482  1.00 57.52           N  
ANISOU 1494  N   PRO A 265     4798  10455   6603    547   -563   2643       N  
ATOM   1495  CA  PRO A 265      51.625  17.385-188.426  1.00 56.72           C  
ANISOU 1495  CA  PRO A 265     4564  10380   6607    630   -459   2745       C  
ATOM   1496  C   PRO A 265      51.729  18.716-187.705  1.00 56.63           C  
ANISOU 1496  C   PRO A 265     4600  10240   6677    885   -264   2831       C  
ATOM   1497  O   PRO A 265      50.725  19.177-187.145  1.00 60.58           O  
ANISOU 1497  O   PRO A 265     4988  10785   7244    990   -165   2953       O  
ATOM   1498  CB  PRO A 265      51.894  16.217-187.467  1.00 50.80           C  
ANISOU 1498  CB  PRO A 265     3825   9580   5897    487   -488   2626       C  
ATOM   1499  CG  PRO A 265      52.656  15.215-188.291  1.00 61.33           C  
ANISOU 1499  CG  PRO A 265     5251  10923   7129    281   -649   2479       C  
ATOM   1500  CD  PRO A 265      53.464  16.001-189.259  1.00 58.25           C  
ANISOU 1500  CD  PRO A 265     4979  10487   6666    367   -653   2473       C  
ATOM   1501  N   ALA A 266      52.905  19.343-187.689  1.00 58.88           N  
ANISOU 1501  N   ALA A 266     5059  10360   6955    984   -201   2771       N  
ATOM   1502  CA  ALA A 266      53.038  20.650-187.055  1.00 60.90           C  
ANISOU 1502  CA  ALA A 266     5392  10470   7278   1218     -9   2843       C  
ATOM   1503  C   ALA A 266      52.124  21.688-187.699  1.00 67.94           C  
ANISOU 1503  C   ALA A 266     6203  11449   8163   1350     46   3002       C  
ATOM   1504  O   ALA A 266      51.691  22.633-187.031  1.00 65.01           O  
ANISOU 1504  O   ALA A 266     5835  11007   7860   1530    212   3095       O  
ATOM   1505  CB  ALA A 266      54.490  21.126-187.133  1.00 58.46           C  
ANISOU 1505  CB  ALA A 266     5300   9969   6944   1271     32   2746       C  
ATOM   1506  N   ASN A 267      51.815  21.530-188.987  1.00 62.84           N  
ANISOU 1506  N   ASN A 267     5491  10955   7431   1264    -88   3037       N  
ATOM   1507  CA  ASN A 267      51.097  22.540-189.755  1.00 62.01           C  
ANISOU 1507  CA  ASN A 267     5323  10931   7308   1389    -53   3186       C  
ATOM   1508  C   ASN A 267      49.688  22.089-190.140  1.00 68.18           C  
ANISOU 1508  C   ASN A 267     5885  11939   8080   1312   -144   3298       C  
ATOM   1509  O   ASN A 267      49.163  22.496-191.179  1.00 72.22           O  
ANISOU 1509  O   ASN A 267     6328  12575   8538   1329   -205   3395       O  
ATOM   1510  CB  ASN A 267      51.904  22.913-190.996  1.00 60.45           C  
ANISOU 1510  CB  ASN A 267     5239  10716   7013   1375   -123   3153       C  
ATOM   1511  CG  ASN A 267      53.341  23.281-190.668  1.00 58.72           C  
ANISOU 1511  CG  ASN A 267     5238  10279   6796   1429    -45   3040       C  
ATOM   1512  OD1 ASN A 267      53.607  23.989-189.698  1.00 56.27           O  
ANISOU 1512  OD1 ASN A 267     5012   9804   6564   1573    118   3047       O  
ATOM   1513  ND2 ASN A 267      54.278  22.796-191.480  1.00 59.32           N  
ANISOU 1513  ND2 ASN A 267     5414  10347   6779   1306   -158   2935       N  
ATOM   1514  N   VAL A 268      49.065  21.244-189.314  1.00 66.04           N  
ANISOU 1514  N   VAL A 268     5506  11726   7860   1223   -156   3288       N  
ATOM   1515  CA  VAL A 268      47.685  20.839-189.571  1.00 70.71           C  
ANISOU 1515  CA  VAL A 268     5889  12527   8451   1151   -230   3402       C  
ATOM   1516  C   VAL A 268      46.742  22.017-189.373  1.00 81.81           C  
ANISOU 1516  C   VAL A 268     7203  13963   9916   1369    -90   3587       C  
ATOM   1517  O   VAL A 268      45.762  22.182-190.111  1.00 83.10           O  
ANISOU 1517  O   VAL A 268     7218  14302  10054   1368   -154   3717       O  
ATOM   1518  CB  VAL A 268      47.301  19.651-188.669  1.00 66.36           C  
ANISOU 1518  CB  VAL A 268     5259  12013   7943   1000   -265   3342       C  
ATOM   1519  CG1 VAL A 268      45.795  19.378-188.740  1.00 69.76           C  
ANISOU 1519  CG1 VAL A 268     5470  12646   8391    955   -307   3481       C  
ATOM   1520  CG2 VAL A 268      48.089  18.413-189.062  1.00 68.00           C  
ANISOU 1520  CG2 VAL A 268     5543  12215   8077    764   -425   3170       C  
ATOM   1521  N   GLU A 269      47.035  22.861-188.382  1.00 81.39           N  
ANISOU 1521  N   GLU A 269     7247  13736   9940   1557    105   3601       N  
ATOM   1522  CA  GLU A 269      46.169  23.986-188.049  1.00 73.98           C  
ANISOU 1522  CA  GLU A 269     6247  12800   9062   1773    264   3768       C  
ATOM   1523  C   GLU A 269      46.144  25.022-189.165  1.00 77.05           C  
ANISOU 1523  C   GLU A 269     6654  13219   9403   1888    262   3863       C  
ATOM   1524  O   GLU A 269      45.072  25.455-189.603  1.00 81.31           O  
ANISOU 1524  O   GLU A 269     7043  13904   9948   1959    260   4024       O  
ATOM   1525  CB  GLU A 269      46.645  24.618-186.745  1.00 75.87           C  
ANISOU 1525  CB  GLU A 269     6632  12816   9379   1931    475   3733       C  
ATOM   1526  CG  GLU A 269      45.821  25.785-186.265  1.00 89.54           C  
ANISOU 1526  CG  GLU A 269     8335  14515  11172   2158    664   3890       C  
ATOM   1527  CD  GLU A 269      46.017  26.037-184.783  1.00102.58           C  
ANISOU 1527  CD  GLU A 269    10100  15979  12898   2261    856   3850       C  
ATOM   1528  OE1 GLU A 269      46.701  25.220-184.127  1.00106.82           O  
ANISOU 1528  OE1 GLU A 269    10708  16435  13445   2147    827   3709       O  
ATOM   1529  OE2 GLU A 269      45.487  27.044-184.270  1.00108.99           O  
ANISOU 1529  OE2 GLU A 269    10934  16721  13756   2455   1036   3958       O  
ATOM   1530  N   ILE A 270      47.320  25.448-189.626  1.00 58.46           N  
ANISOU 1530  N   ILE A 270     4482  10726   7003   1911    266   3772       N  
ATOM   1531  CA  ILE A 270      47.353  26.475-190.655  1.00 65.51           C  
ANISOU 1531  CA  ILE A 270     5410  11631   7851   2025    275   3860       C  
ATOM   1532  C   ILE A 270      46.891  25.901-191.987  1.00 70.15           C  
ANISOU 1532  C   ILE A 270     5867  12438   8348   1877     65   3900       C  
ATOM   1533  O   ILE A 270      46.288  26.615-192.800  1.00 76.06           O  
ANISOU 1533  O   ILE A 270     6543  13284   9071   1967     52   4037       O  
ATOM   1534  CB  ILE A 270      48.763  27.088-190.730  1.00 66.65           C  
ANISOU 1534  CB  ILE A 270     5796  11556   7972   2084    345   3749       C  
ATOM   1535  CG1 ILE A 270      48.817  28.221-191.759  1.00 72.55           C  
ANISOU 1535  CG1 ILE A 270     6594  12298   8675   2210    369   3843       C  
ATOM   1536  CG2 ILE A 270      49.816  26.001-190.949  1.00 61.04           C  
ANISOU 1536  CG2 ILE A 270     5171  10818   7203   1884    205   3571       C  
ATOM   1537  CD1 ILE A 270      48.084  29.476-191.314  1.00 71.15           C  
ANISOU 1537  CD1 ILE A 270     6400  12068   8566   2443    558   3993       C  
ATOM   1538  N   THR A 271      47.130  24.604-192.221  1.00 72.39           N  
ANISOU 1538  N   THR A 271     6125  12801   8580   1648   -101   3784       N  
ATOM   1539  CA  THR A 271      46.623  23.959-193.429  1.00 74.64           C  
ANISOU 1539  CA  THR A 271     6294  13294   8771   1484   -303   3812       C  
ATOM   1540  C   THR A 271      45.107  24.081-193.523  1.00 90.17           C  
ANISOU 1540  C   THR A 271     8033  15458  10770   1520   -320   3993       C  
ATOM   1541  O   THR A 271      44.566  24.373-194.597  1.00 91.43           O  
ANISOU 1541  O   THR A 271     8107  15762  10869   1521   -414   4099       O  
ATOM   1542  CB  THR A 271      47.032  22.484-193.466  1.00 73.16           C  
ANISOU 1542  CB  THR A 271     6122  13144   8531   1226   -456   3652       C  
ATOM   1543  OG1 THR A 271      48.455  22.371-193.362  1.00 67.79           O  
ANISOU 1543  OG1 THR A 271     5648  12284   7824   1200   -438   3491       O  
ATOM   1544  CG2 THR A 271      46.569  21.833-194.769  1.00 74.16           C  
ANISOU 1544  CG2 THR A 271     6163  13469   8547   1045   -662   3668       C  
ATOM   1545  N   GLU A 272      44.401  23.867-192.408  1.00 94.35           N  
ANISOU 1545  N   GLU A 272     8461  15998  11391   1553   -231   4037       N  
ATOM   1546  CA  GLU A 272      42.945  23.947-192.460  1.00 99.61           C  
ANISOU 1546  CA  GLU A 272     8900  16857  12091   1586   -245   4214       C  
ATOM   1547  C   GLU A 272      42.463  25.392-192.540  1.00100.90           C  
ANISOU 1547  C   GLU A 272     9039  17001  12298   1848   -100   4387       C  
ATOM   1548  O   GLU A 272      41.392  25.652-193.099  1.00103.50           O  
ANISOU 1548  O   GLU A 272     9192  17511  12624   1885   -150   4551       O  
ATOM   1549  CB  GLU A 272      42.333  23.220-191.260  1.00 96.06           C  
ANISOU 1549  CB  GLU A 272     8351  16427  11720   1531   -197   4208       C  
ATOM   1550  CG  GLU A 272      42.342  23.988-189.951  1.00103.26           C  
ANISOU 1550  CG  GLU A 272     9322  17173  12738   1740     37   4242       C  
ATOM   1551  CD  GLU A 272      41.998  23.108-188.759  1.00112.93           C  
ANISOU 1551  CD  GLU A 272    10489  18390  14027   1654     71   4194       C  
ATOM   1552  OE1 GLU A 272      42.515  21.972-188.690  1.00114.92           O  
ANISOU 1552  OE1 GLU A 272    10781  18638  14246   1447    -44   4046       O  
ATOM   1553  OE2 GLU A 272      41.206  23.550-187.897  1.00115.65           O  
ANISOU 1553  OE2 GLU A 272    10755  18733  14456   1794    215   4305       O  
ATOM   1554  N   LEU A 273      43.239  26.345-192.012  1.00 92.88           N  
ANISOU 1554  N   LEU A 273     8201  15766  11322   2028     77   4355       N  
ATOM   1555  CA  LEU A 273      42.901  27.754-192.198  1.00 85.14           C  
ANISOU 1555  CA  LEU A 273     7232  14745  10371   2271    216   4506       C  
ATOM   1556  C   LEU A 273      43.062  28.163-193.658  1.00 89.52           C  
ANISOU 1556  C   LEU A 273     7796  15383  10835   2265     94   4553       C  
ATOM   1557  O   LEU A 273      42.200  28.851-194.217  1.00 88.06           O  
ANISOU 1557  O   LEU A 273     7490  15317  10651   2381     96   4727       O  
ATOM   1558  CB  LEU A 273      43.765  28.633-191.292  1.00 76.00           C  
ANISOU 1558  CB  LEU A 273     6291  13318   9268   2441    433   4441       C  
ATOM   1559  CG  LEU A 273      43.516  28.495-189.790  1.00 77.00           C  
ANISOU 1559  CG  LEU A 273     6424  13346   9487   2497    589   4423       C  
ATOM   1560  CD1 LEU A 273      44.364  29.480-189.000  1.00 73.99           C  
ANISOU 1560  CD1 LEU A 273     6276  12692   9144   2666    803   4365       C  
ATOM   1561  CD2 LEU A 273      42.040  28.691-189.482  1.00 79.00           C  
ANISOU 1561  CD2 LEU A 273     6465  13751   9800   2590    642   4610       C  
ATOM   1562  N   CYS A 274      44.160  27.743-194.294  1.00 90.06           N  
ANISOU 1562  N   CYS A 274     8009  15391  10820   2132    -14   4404       N  
ATOM   1563  CA  CYS A 274      44.377  28.081-195.698  1.00 87.84           C  
ANISOU 1563  CA  CYS A 274     7756  15181  10440   2114   -134   4440       C  
ATOM   1564  C   CYS A 274      43.277  27.511-196.584  1.00 90.73           C  
ANISOU 1564  C   CYS A 274     7906  15817  10751   1993   -321   4549       C  
ATOM   1565  O   CYS A 274      42.792  28.190-197.499  1.00 90.71           O  
ANISOU 1565  O   CYS A 274     7841  15914  10709   2077   -364   4688       O  
ATOM   1566  CB  CYS A 274      45.741  27.574-196.161  1.00 84.57           C  
ANISOU 1566  CB  CYS A 274     7533  14658   9941   1971   -220   4251       C  
ATOM   1567  SG  CYS A 274      47.146  28.447-195.446  1.00 78.53           S  
ANISOU 1567  SG  CYS A 274     7040  13580   9220   2119    -20   4139       S  
ATOM   1568  N   ILE A 275      42.880  26.261-196.339  1.00 87.98           N  
ANISOU 1568  N   ILE A 275     7446  15586  10395   1790   -438   4489       N  
ATOM   1569  CA  ILE A 275      41.805  25.667-197.127  1.00 95.71           C  
ANISOU 1569  CA  ILE A 275     8221  16821  11322   1656   -617   4589       C  
ATOM   1570  C   ILE A 275      40.495  26.392-196.855  1.00102.57           C  
ANISOU 1570  C   ILE A 275     8891  17809  12272   1830   -534   4809       C  
ATOM   1571  O   ILE A 275      39.664  26.570-197.755  1.00106.37           O  
ANISOU 1571  O   ILE A 275     9225  18480  12711   1828   -644   4952       O  
ATOM   1572  CB  ILE A 275      41.705  24.160-196.834  1.00 89.07           C  
ANISOU 1572  CB  ILE A 275     7325  16057  10459   1393   -745   4465       C  
ATOM   1573  CG1 ILE A 275      42.997  23.460-197.253  1.00 83.10           C  
ANISOU 1573  CG1 ILE A 275     6769  15193   9611   1224   -836   4255       C  
ATOM   1574  CG2 ILE A 275      40.514  23.543-197.557  1.00 91.93           C  
ANISOU 1574  CG2 ILE A 275     7473  16683  10773   1247   -921   4572       C  
ATOM   1575  CD1 ILE A 275      43.032  21.990-196.922  1.00 80.74           C  
ANISOU 1575  CD1 ILE A 275     6452  14935   9290    971   -946   4116       C  
ATOM   1576  N   GLN A 276      40.310  26.854-195.621  1.00103.82           N  
ANISOU 1576  N   GLN A 276     9049  17853  12544   1990   -335   4842       N  
ATOM   1577  CA  GLN A 276      39.130  27.600-195.206  1.00109.98           C  
ANISOU 1577  CA  GLN A 276     9660  18715  13411   2180   -219   5046       C  
ATOM   1578  C   GLN A 276      39.274  29.069-195.602  1.00111.24           C  
ANISOU 1578  C   GLN A 276     9902  18784  13580   2431    -96   5159       C  
ATOM   1579  O   GLN A 276      38.678  29.963-194.992  1.00119.18           O  
ANISOU 1579  O   GLN A 276    10861  19751  14672   2649     79   5293       O  
ATOM   1580  CB  GLN A 276      38.936  27.428-193.701  1.00109.96           C  
ANISOU 1580  CB  GLN A 276     9651  18611  13516   2236    -53   5019       C  
ATOM   1581  CG  GLN A 276      37.638  27.931-193.123  1.00116.92           C  
ANISOU 1581  CG  GLN A 276    10343  19590  14490   2398     61   5217       C  
ATOM   1582  CD  GLN A 276      37.880  28.742-191.870  1.00118.07           C  
ANISOU 1582  CD  GLN A 276    10615  19516  14730   2611    321   5215       C  
ATOM   1583  OE1 GLN A 276      37.422  28.384-190.785  1.00117.75           O  
ANISOU 1583  OE1 GLN A 276    10515  19461  14763   2616    411   5219       O  
ATOM   1584  NE2 GLN A 276      38.614  29.842-192.012  1.00116.18           N  
ANISOU 1584  NE2 GLN A 276    10561  19097  14484   2783    446   5206       N  
ATOM   1585  N   HIS A 277      40.072  29.322-196.635  1.00 99.87           N  
ANISOU 1585  N   HIS A 277     8594  17306  12048   2400   -183   5103       N  
ATOM   1586  CA  HIS A 277      40.189  30.674-197.169  1.00 95.90           C  
ANISOU 1586  CA  HIS A 277     8168  16731  11540   2619    -90   5214       C  
ATOM   1587  C   HIS A 277      40.356  30.693-198.684  1.00 95.68           C  
ANISOU 1587  C   HIS A 277     8147  16817  11391   2538   -280   5240       C  
ATOM   1588  O   HIS A 277      40.725  31.742-199.228  1.00100.60           O  
ANISOU 1588  O   HIS A 277     8882  17352  11991   2692   -220   5297       O  
ATOM   1589  CB  HIS A 277      41.367  31.412-196.531  1.00 96.53           C  
ANISOU 1589  CB  HIS A 277     8508  16520  11652   2747    101   5099       C  
ATOM   1590  CG  HIS A 277      41.010  32.182-195.297  1.00 98.66           C  
ANISOU 1590  CG  HIS A 277     8792  16658  12036   2957    345   5166       C  
ATOM   1591  ND1 HIS A 277      40.752  31.578-194.084  1.00 99.84           N  
ANISOU 1591  ND1 HIS A 277     8896  16779  12259   2917    421   5116       N  
ATOM   1592  CD2 HIS A 277      40.881  33.513-195.088  1.00100.62           C  
ANISOU 1592  CD2 HIS A 277     9111  16786  12333   3207    535   5277       C  
ATOM   1593  CE1 HIS A 277      40.476  32.504-193.182  1.00100.01           C  
ANISOU 1593  CE1 HIS A 277     8963  16671  12365   3134    648   5192       C  
ATOM   1594  NE2 HIS A 277      40.548  33.687-193.766  1.00100.57           N  
ANISOU 1594  NE2 HIS A 277     9107  16682  12424   3312    724   5288       N  
ATOM   1595  N   GLY A 278      40.112  29.592-199.387  1.00 96.50           N  
ANISOU 1595  N   GLY A 278     8151  17104  11411   2300   -503   5199       N  
ATOM   1596  CA  GLY A 278      40.200  29.549-200.834  1.00100.68           C  
ANISOU 1596  CA  GLY A 278     8688  17753  11813   2209   -692   5226       C  
ATOM   1597  C   GLY A 278      41.176  28.529-201.383  1.00101.66           C  
ANISOU 1597  C   GLY A 278     8953  17850  11823   1961   -845   5024       C  
ATOM   1598  O   GLY A 278      41.014  28.101-202.537  1.00104.94           O  
ANISOU 1598  O   GLY A 278     9335  18417  12120   1816  -1042   5037       O  
ATOM   1599  N   TRP A 279      42.175  28.111-200.603  1.00 91.55           N  
ANISOU 1599  N   TRP A 279     7832  16385  10569   1906   -764   4839       N  
ATOM   1600  CA  TRP A 279      43.229  27.263-201.142  1.00 91.76           C  
ANISOU 1600  CA  TRP A 279     8017  16360  10486   1697   -889   4647       C  
ATOM   1601  C   TRP A 279      42.704  25.862-201.414  1.00 94.14           C  
ANISOU 1601  C   TRP A 279     8196  16844  10728   1430  -1081   4591       C  
ATOM   1602  O   TRP A 279      42.145  25.210-200.525  1.00 93.60           O  
ANISOU 1602  O   TRP A 279     8008  16820  10736   1368  -1059   4580       O  
ATOM   1603  CB  TRP A 279      44.419  27.195-200.188  1.00 91.40           C  
ANISOU 1603  CB  TRP A 279     8164  16071  10492   1717   -749   4474       C  
ATOM   1604  CG  TRP A 279      45.580  26.459-200.783  1.00 88.24           C  
ANISOU 1604  CG  TRP A 279     7941  15606   9980   1532   -859   4288       C  
ATOM   1605  CD1 TRP A 279      46.197  26.739-201.963  1.00 88.17           C  
ANISOU 1605  CD1 TRP A 279     8060  15589   9850   1506   -943   4269       C  
ATOM   1606  CD2 TRP A 279      46.259  25.321-200.235  1.00 88.41           C  
ANISOU 1606  CD2 TRP A 279     8036  15559   9995   1352   -894   4097       C  
ATOM   1607  NE1 TRP A 279      47.219  25.851-202.189  1.00 88.17           N  
ANISOU 1607  NE1 TRP A 279     8211  15523   9768   1322  -1021   4079       N  
ATOM   1608  CE2 TRP A 279      47.279  24.970-201.142  1.00 87.24           C  
ANISOU 1608  CE2 TRP A 279     8061  15367   9720   1227   -994   3971       C  
ATOM   1609  CE3 TRP A 279      46.108  24.568-199.065  1.00 90.90           C  
ANISOU 1609  CE3 TRP A 279     8295  15846  10397   1287   -847   4025       C  
ATOM   1610  CZ2 TRP A 279      48.143  23.900-200.920  1.00 88.68           C  
ANISOU 1610  CZ2 TRP A 279     8355  15478   9863   1045  -1046   3776       C  
ATOM   1611  CZ3 TRP A 279      46.969  23.504-198.845  1.00 91.98           C  
ANISOU 1611  CZ3 TRP A 279     8544  15909  10496   1104   -906   3832       C  
ATOM   1612  CH2 TRP A 279      47.974  23.182-199.768  1.00 90.40           C  
ANISOU 1612  CH2 TRP A 279     8510  15666  10171    988  -1003   3710       C  
ATOM   1613  N   THR A 280      42.892  25.400-202.642  1.00 99.23           N  
ANISOU 1613  N   THR A 280     8884  17588  11232   1267  -1266   4552       N  
ATOM   1614  CA  THR A 280      42.563  24.026-202.984  1.00108.03           C  
ANISOU 1614  CA  THR A 280     9931  18847  12269    989  -1451   4468       C  
ATOM   1615  C   THR A 280      43.696  23.119-202.515  1.00107.44           C  
ANISOU 1615  C   THR A 280    10032  18615  12174    839  -1441   4236       C  
ATOM   1616  O   THR A 280      44.836  23.289-202.964  1.00103.82           O  
ANISOU 1616  O   THR A 280     9779  18024  11644    837  -1433   4126       O  
ATOM   1617  CB  THR A 280      42.333  23.884-204.487  1.00109.48           C  
ANISOU 1617  CB  THR A 280    10112  19189  12297    869  -1648   4512       C  
ATOM   1618  OG1 THR A 280      43.578  24.013-205.186  1.00110.67           O  
ANISOU 1618  OG1 THR A 280    10503  19206  12339    842  -1666   4388       O  
ATOM   1619  CG2 THR A 280      41.377  24.968-204.976  1.00109.09           C  
ANISOU 1619  CG2 THR A 280     9913  19268  12268   1056  -1644   4750       C  
ATOM   1620  N   PRO A 281      43.437  22.173-201.612  1.00101.37           N  
ANISOU 1620  N   PRO A 281     9195  17854  11467    718  -1437   4160       N  
ATOM   1621  CA  PRO A 281      44.531  21.391-201.027  1.00 98.12           C  
ANISOU 1621  CA  PRO A 281     8951  17277  11054    605  -1408   3948       C  
ATOM   1622  C   PRO A 281      45.262  20.564-202.070  1.00 96.13           C  
ANISOU 1622  C   PRO A 281     8848  17033  10645    388  -1565   3798       C  
ATOM   1623  O   PRO A 281      44.708  20.190-203.106  1.00103.79           O  
ANISOU 1623  O   PRO A 281     9763  18167  11507    251  -1726   3838       O  
ATOM   1624  CB  PRO A 281      43.818  20.490-200.012  1.00 99.41           C  
ANISOU 1624  CB  PRO A 281     8976  17495  11301    500  -1403   3931       C  
ATOM   1625  CG  PRO A 281      42.415  20.395-200.518  1.00104.10           C  
ANISOU 1625  CG  PRO A 281     9347  18327  11878    450  -1512   4095       C  
ATOM   1626  CD  PRO A 281      42.121  21.739-201.115  1.00103.91           C  
ANISOU 1626  CD  PRO A 281     9283  18342  11857    670  -1466   4268       C  
ATOM   1627  N   GLY A 282      46.530  20.290-201.784  1.00 82.44           N  
ANISOU 1627  N   GLY A 282     7311  15117   8895    358  -1513   3626       N  
ATOM   1628  CA  GLY A 282      47.292  19.351-202.571  1.00 80.73           C  
ANISOU 1628  CA  GLY A 282     7251  14885   8539    142  -1640   3458       C  
ATOM   1629  C   GLY A 282      47.063  17.931-202.098  1.00 85.96           C  
ANISOU 1629  C   GLY A 282     7880  15579   9202    -88  -1717   3337       C  
ATOM   1630  O   GLY A 282      46.261  17.653-201.206  1.00 83.70           O  
ANISOU 1630  O   GLY A 282     7440  15342   9020    -90  -1684   3390       O  
ATOM   1631  N   ASN A 283      47.802  17.010-202.710  1.00 97.87           N  
ANISOU 1631  N   ASN A 283     9548  17049  10588   -286  -1815   3168       N  
ATOM   1632  CA  ASN A 283      47.688  15.600-202.368  1.00105.29           C  
ANISOU 1632  CA  ASN A 283    10494  17997  11512   -521  -1891   3033       C  
ATOM   1633  C   ASN A 283      48.888  15.062-201.602  1.00 96.82           C  
ANISOU 1633  C   ASN A 283     9588  16727  10471   -551  -1813   2847       C  
ATOM   1634  O   ASN A 283      48.797  13.969-201.031  1.00 99.41           O  
ANISOU 1634  O   ASN A 283     9916  17034  10821   -711  -1844   2743       O  
ATOM   1635  CB  ASN A 283      47.507  14.764-203.641  1.00114.01           C  
ANISOU 1635  CB  ASN A 283    11660  19211  12446   -758  -2069   2970       C  
ATOM   1636  CG  ASN A 283      48.717  14.837-204.559  1.00116.47           C  
ANISOU 1636  CG  ASN A 283    12207  19424  12622   -782  -2086   2850       C  
ATOM   1637  OD1 ASN A 283      49.490  15.798-204.515  1.00116.42           O  
ANISOU 1637  OD1 ASN A 283    12283  19313  12638   -594  -1981   2871       O  
ATOM   1638  ND2 ASN A 283      48.887  13.818-205.395  1.00115.72           N  
ANISOU 1638  ND2 ASN A 283    12230  19356  12382  -1015  -2210   2723       N  
ATOM   1639  N   GLY A 284      49.995  15.805-201.556  1.00 82.87           N  
ANISOU 1639  N   GLY A 284     7963  14815   8709   -401  -1713   2809       N  
ATOM   1640  CA  GLY A 284      51.284  15.227-201.249  1.00 73.99           C  
ANISOU 1640  CA  GLY A 284     7030  13522   7561   -463  -1677   2619       C  
ATOM   1641  C   GLY A 284      51.717  15.372-199.798  1.00 75.04           C  
ANISOU 1641  C   GLY A 284     7156  13513   7842   -345  -1539   2589       C  
ATOM   1642  O   GLY A 284      51.028  15.932-198.946  1.00 62.95           O  
ANISOU 1642  O   GLY A 284     5480  12000   6438   -208  -1455   2710       O  
ATOM   1643  N   ARG A 285      52.905  14.838-199.532  1.00 72.26           N  
ANISOU 1643  N   ARG A 285     6974  13015   7467   -403  -1514   2421       N  
ATOM   1644  CA  ARG A 285      53.532  14.893-198.221  1.00 70.74           C  
ANISOU 1644  CA  ARG A 285     6810  12672   7395   -308  -1396   2368       C  
ATOM   1645  C   ARG A 285      54.439  16.105-198.057  1.00 67.84           C  
ANISOU 1645  C   ARG A 285     6535  12181   7061    -89  -1265   2405       C  
ATOM   1646  O   ARG A 285      54.922  16.352-196.947  1.00 57.95           O  
ANISOU 1646  O   ARG A 285     5303  10801   5915     18  -1155   2385       O  
ATOM   1647  CB  ARG A 285      54.329  13.606-197.986  1.00 71.14           C  
ANISOU 1647  CB  ARG A 285     6994  12632   7404   -495  -1444   2166       C  
ATOM   1648  CG  ARG A 285      53.741  12.409-198.727  1.00 88.08           C  
ANISOU 1648  CG  ARG A 285     9138  14881   9448   -746  -1590   2095       C  
ATOM   1649  CD  ARG A 285      54.729  11.261-198.861  1.00 90.96           C  
ANISOU 1649  CD  ARG A 285     9693  15135   9733   -922  -1630   1882       C  
ATOM   1650  NE  ARG A 285      55.249  10.845-197.567  1.00 87.47           N  
ANISOU 1650  NE  ARG A 285     9273  14561   9401   -905  -1560   1800       N  
ATOM   1651  CZ  ARG A 285      56.539  10.821-197.250  1.00 88.39           C  
ANISOU 1651  CZ  ARG A 285     9540  14531   9515   -863  -1499   1684       C  
ATOM   1652  NH1 ARG A 285      57.450  11.173-198.147  1.00 95.00           N  
ANISOU 1652  NH1 ARG A 285    10521  15334  10240   -838  -1490   1635       N  
ATOM   1653  NH2 ARG A 285      56.916  10.434-196.037  1.00 78.77           N  
ANISOU 1653  NH2 ARG A 285     8335  13187   8409   -848  -1435   1614       N  
ATOM   1654  N   PHE A 286      54.668  16.866-199.128  1.00 61.72           N  
ANISOU 1654  N   PHE A 286     5823  11433   6196    -25  -1273   2461       N  
ATOM   1655  CA  PHE A 286      55.535  18.042-199.106  1.00 60.90           C  
ANISOU 1655  CA  PHE A 286     5825  11206   6109    170  -1148   2500       C  
ATOM   1656  C   PHE A 286      54.969  19.144-200.001  1.00 71.08           C  
ANISOU 1656  C   PHE A 286     7067  12578   7361    291  -1143   2659       C  
ATOM   1657  O   PHE A 286      55.656  19.679-200.873  1.00 71.20           O  
ANISOU 1657  O   PHE A 286     7213  12559   7282    327  -1133   2656       O  
ATOM   1658  CB  PHE A 286      56.957  17.693-199.546  1.00 56.83           C  
ANISOU 1658  CB  PHE A 286     5519  10584   5489     98  -1147   2347       C  
ATOM   1659  CG  PHE A 286      57.634  16.674-198.689  1.00 57.19           C  
ANISOU 1659  CG  PHE A 286     5626  10536   5568     -6  -1145   2190       C  
ATOM   1660  CD1 PHE A 286      58.203  17.037-197.479  1.00 51.20           C  
ANISOU 1660  CD1 PHE A 286     4893   9628   4934    119  -1020   2173       C  
ATOM   1661  CD2 PHE A 286      57.728  15.354-199.099  1.00 64.95           C  
ANISOU 1661  CD2 PHE A 286     6659  11559   6458   -233  -1262   2048       C  
ATOM   1662  CE1 PHE A 286      58.832  16.106-196.687  1.00 50.96           C  
ANISOU 1662  CE1 PHE A 286     4945   9441   4976     18   -983   1985       C  
ATOM   1663  CE2 PHE A 286      58.360  14.412-198.305  1.00 62.57           C  
ANISOU 1663  CE2 PHE A 286     6430  11141   6203   -326  -1245   1888       C  
ATOM   1664  CZ  PHE A 286      58.912  14.793-197.097  1.00 60.85           C  
ANISOU 1664  CZ  PHE A 286     6244  10728   6148   -197  -1094   1846       C  
ATOM   1665  N   ASP A 287      53.699  19.495-199.799  1.00 76.41           N  
ANISOU 1665  N   ASP A 287     7558  13366   8108    356  -1147   2805       N  
ATOM   1666  CA  ASP A 287      53.088  20.620-200.497  1.00 75.49           C  
ANISOU 1666  CA  ASP A 287     7382  13324   7978    498  -1130   2973       C  
ATOM   1667  C   ASP A 287      53.399  21.904-199.736  1.00 72.51           C  
ANISOU 1667  C   ASP A 287     7037  12800   7715    746   -945   3053       C  
ATOM   1668  O   ASP A 287      53.016  22.046-198.571  1.00 73.08           O  
ANISOU 1668  O   ASP A 287     7025  12824   7918    835   -848   3086       O  
ATOM   1669  CB  ASP A 287      51.574  20.444-200.632  1.00 74.49           C  
ANISOU 1669  CB  ASP A 287     7038  13389   7874    461  -1212   3102       C  
ATOM   1670  CG  ASP A 287      51.195  19.149-201.316  1.00 75.77           C  
ANISOU 1670  CG  ASP A 287     7173  13688   7928    202  -1392   3022       C  
ATOM   1671  OD1 ASP A 287      51.994  18.646-202.134  1.00 75.48           O  
ANISOU 1671  OD1 ASP A 287     7294  13626   7761     72  -1467   2900       O  
ATOM   1672  OD2 ASP A 287      50.094  18.636-201.028  1.00 75.02           O  
ANISOU 1672  OD2 ASP A 287     6908  13721   7875    125  -1450   3079       O  
ATOM   1673  N   VAL A 288      54.090  22.836-200.395  1.00 71.26           N  
ANISOU 1673  N   VAL A 288     7013  12561   7503    852   -889   3082       N  
ATOM   1674  CA  VAL A 288      54.373  24.128-199.780  1.00 64.54           C  
ANISOU 1674  CA  VAL A 288     6214  11559   6751   1081   -709   3159       C  
ATOM   1675  C   VAL A 288      53.075  24.885-199.565  1.00 65.93           C  
ANISOU 1675  C   VAL A 288     6217  11823   7011   1226   -663   3339       C  
ATOM   1676  O   VAL A 288      52.280  25.073-200.497  1.00 69.40           O  
ANISOU 1676  O   VAL A 288     6565  12416   7387   1217   -755   3448       O  
ATOM   1677  CB  VAL A 288      55.341  24.937-200.654  1.00 66.07           C  
ANISOU 1677  CB  VAL A 288     6593  11655   6856   1143   -667   3156       C  
ATOM   1678  CG1 VAL A 288      55.509  26.340-200.092  1.00 64.95           C  
ANISOU 1678  CG1 VAL A 288     6509  11354   6814   1374   -480   3245       C  
ATOM   1679  CG2 VAL A 288      56.671  24.236-200.746  1.00 62.08           C  
ANISOU 1679  CG2 VAL A 288     6259  11052   6275   1015   -683   2982       C  
ATOM   1680  N   LEU A 289      52.867  25.346-198.346  1.00 63.12           N  
ANISOU 1680  N   LEU A 289     5824  11367   6791   1365   -516   3373       N  
ATOM   1681  CA  LEU A 289      51.630  26.029-198.009  1.00 67.38           C  
ANISOU 1681  CA  LEU A 289     6202  11985   7416   1509   -450   3540       C  
ATOM   1682  C   LEU A 289      51.596  27.443-198.594  1.00 72.00           C  
ANISOU 1682  C   LEU A 289     6845  12520   7993   1699   -361   3668       C  
ATOM   1683  O   LEU A 289      52.640  28.045-198.858  1.00 68.45           O  
ANISOU 1683  O   LEU A 289     6582  11916   7510   1753   -295   3617       O  
ATOM   1684  CB  LEU A 289      51.455  26.090-196.494  1.00 72.13           C  
ANISOU 1684  CB  LEU A 289     6769  12481   8155   1598   -304   3530       C  
ATOM   1685  CG  LEU A 289      50.985  24.791-195.819  1.00 67.08           C  
ANISOU 1685  CG  LEU A 289     6007  11934   7546   1437   -385   3463       C  
ATOM   1686  CD1 LEU A 289      51.070  24.877-194.303  1.00 65.60           C  
ANISOU 1686  CD1 LEU A 289     5836  11607   7483   1525   -231   3432       C  
ATOM   1687  CD2 LEU A 289      49.560  24.453-196.253  1.00 69.49           C  
ANISOU 1687  CD2 LEU A 289     6091  12471   7839   1379   -490   3589       C  
ATOM   1688  N   PRO A 290      50.403  27.983-198.823  1.00 72.75           N  
ANISOU 1688  N   PRO A 290     6783  12744   8116   1799   -359   3838       N  
ATOM   1689  CA  PRO A 290      50.280  29.397-199.188  1.00 78.82           C  
ANISOU 1689  CA  PRO A 290     7602  13449   8898   2007   -249   3970       C  
ATOM   1690  C   PRO A 290      50.446  30.285-197.959  1.00 77.07           C  
ANISOU 1690  C   PRO A 290     7451  13030   8802   2198    -21   3983       C  
ATOM   1691  O   PRO A 290      50.443  29.827-196.820  1.00 77.92           O  
ANISOU 1691  O   PRO A 290     7536  13080   8990   2180     45   3916       O  
ATOM   1692  CB  PRO A 290      48.860  29.490-199.756  1.00 78.71           C  
ANISOU 1692  CB  PRO A 290     7371  13660   8874   2032   -336   4146       C  
ATOM   1693  CG  PRO A 290      48.108  28.412-199.029  1.00 76.87           C  
ANISOU 1693  CG  PRO A 290     6965  13548   8692   1912   -393   4123       C  
ATOM   1694  CD  PRO A 290      49.099  27.292-198.821  1.00 75.15           C  
ANISOU 1694  CD  PRO A 290     6856  13265   8433   1717   -465   3920       C  
ATOM   1695  N   LEU A 291      50.582  31.582-198.210  1.00 75.61           N  
ANISOU 1695  N   LEU A 291     7364  12737   8628   2379    100   4070       N  
ATOM   1696  CA  LEU A 291      50.726  32.568-197.147  1.00 68.87           C  
ANISOU 1696  CA  LEU A 291     6605  11682   7880   2566    326   4087       C  
ATOM   1697  C   LEU A 291      49.372  33.182-196.813  1.00 76.89           C  
ANISOU 1697  C   LEU A 291     7455  12791   8970   2727    409   4266       C  
ATOM   1698  O   LEU A 291      48.588  33.502-197.711  1.00 80.95           O  
ANISOU 1698  O   LEU A 291     7854  13459   9444   2771    333   4410       O  
ATOM   1699  CB  LEU A 291      51.711  33.664-197.556  1.00 65.11           C  
ANISOU 1699  CB  LEU A 291     6356  11009   7373   2666    428   4068       C  
ATOM   1700  CG  LEU A 291      53.068  33.714-196.858  1.00 72.27           C  
ANISOU 1700  CG  LEU A 291     7483  11674   8301   2637    531   3902       C  
ATOM   1701  CD1 LEU A 291      53.692  32.322-196.733  1.00 69.96           C  
ANISOU 1701  CD1 LEU A 291     7183  11427   7971   2424    397   3746       C  
ATOM   1702  CD2 LEU A 291      54.007  34.670-197.576  1.00 65.26           C  
ANISOU 1702  CD2 LEU A 291     6805  10634   7358   2691    587   3892       C  
ATOM   1703  N   LEU A 292      49.095  33.338-195.515  1.00 73.42           N  
ANISOU 1703  N   LEU A 292     7007  12257   8633   2815    567   4261       N  
ATOM   1704  CA  LEU A 292      47.913  34.060-195.038  1.00 80.18           C  
ANISOU 1704  CA  LEU A 292     7742  13159   9566   2994    693   4428       C  
ATOM   1705  C   LEU A 292      48.401  35.375-194.440  1.00 77.40           C  
ANISOU 1705  C   LEU A 292     7590  12555   9263   3190    927   4430       C  
ATOM   1706  O   LEU A 292      48.901  35.409-193.310  1.00 69.98           O  
ANISOU 1706  O   LEU A 292     6771  11439   8380   3208   1063   4328       O  
ATOM   1707  CB  LEU A 292      47.114  33.244-194.023  1.00 82.52           C  
ANISOU 1707  CB  LEU A 292     7877  13547   9932   2945    702   4433       C  
ATOM   1708  CG  LEU A 292      46.059  32.276-194.567  1.00 84.56           C  
ANISOU 1708  CG  LEU A 292     7879  14088  10161   2813    511   4513       C  
ATOM   1709  CD1 LEU A 292      45.329  31.559-193.432  1.00 84.08           C  
ANISOU 1709  CD1 LEU A 292     7684  14085  10178   2774    549   4516       C  
ATOM   1710  CD2 LEU A 292      45.072  33.003-195.471  1.00 86.26           C  
ANISOU 1710  CD2 LEU A 292     7960  14456  10357   2931    479   4714       C  
ATOM   1711  N   LEU A 293      48.241  36.456-195.199  1.00 77.14           N  
ANISOU 1711  N   LEU A 293     7601  12503   9205   3330    972   4547       N  
ATOM   1712  CA  LEU A 293      48.790  37.760-194.851  1.00 83.35           C  
ANISOU 1712  CA  LEU A 293     8605  13044  10020   3500   1180   4545       C  
ATOM   1713  C   LEU A 293      47.673  38.714-194.446  1.00 91.38           C  
ANISOU 1713  C   LEU A 293     9546  14071  11103   3719   1341   4721       C  
ATOM   1714  O   LEU A 293      46.674  38.856-195.163  1.00 87.55           O  
ANISOU 1714  O   LEU A 293     8883  13778  10606   3779   1266   4889       O  
ATOM   1715  CB  LEU A 293      49.590  38.332-196.021  1.00 79.59           C  
ANISOU 1715  CB  LEU A 293     8275  12506   9461   3496   1123   4536       C  
ATOM   1716  CG  LEU A 293      50.704  37.404-196.507  1.00 75.47           C  
ANISOU 1716  CG  LEU A 293     7833  11979   8864   3283    967   4371       C  
ATOM   1717  CD1 LEU A 293      51.540  38.086-197.571  1.00 68.54           C  
ANISOU 1717  CD1 LEU A 293     7128  11011   7904   3290    944   4366       C  
ATOM   1718  CD2 LEU A 293      51.581  36.932-195.338  1.00 62.16           C  
ANISOU 1718  CD2 LEU A 293     6273  10121   7226   3205   1048   4191       C  
ATOM   1719  N   GLN A 294      47.865  39.384-193.311  1.00 91.52           N  
ANISOU 1719  N   GLN A 294     9710  13879  11185   3836   1564   4683       N  
ATOM   1720  CA  GLN A 294      46.826  40.160-192.638  1.00 89.06           C  
ANISOU 1720  CA  GLN A 294     9342  13557  10942   4034   1745   4829       C  
ATOM   1721  C   GLN A 294      47.262  41.619-192.550  1.00 86.97           C  
ANISOU 1721  C   GLN A 294     9310  13053  10682   4212   1950   4848       C  
ATOM   1722  O   GLN A 294      48.132  41.968-191.745  1.00 78.70           O  
ANISOU 1722  O   GLN A 294     8489  11766   9648   4212   2092   4712       O  
ATOM   1723  CB  GLN A 294      46.551  39.577-191.252  1.00 91.83           C  
ANISOU 1723  CB  GLN A 294     9661  13873  11358   4006   1836   4769       C  
ATOM   1724  CG  GLN A 294      45.639  40.408-190.367  1.00 97.51           C  
ANISOU 1724  CG  GLN A 294    10373  14531  12144   4210   2058   4895       C  
ATOM   1725  CD  GLN A 294      45.601  39.893-188.936  1.00 99.34           C  
ANISOU 1725  CD  GLN A 294    10637  14680  12428   4173   2163   4809       C  
ATOM   1726  OE1 GLN A 294      45.283  38.729-188.689  1.00 99.77           O  
ANISOU 1726  OE1 GLN A 294    10530  14883  12496   4035   2036   4780       O  
ATOM   1727  NE2 GLN A 294      45.942  40.758-187.987  1.00 96.64           N  
ANISOU 1727  NE2 GLN A 294    10516  14093  12111   4289   2394   4764       N  
ATOM   1728  N   ALA A 295      46.661  42.469-193.381  1.00 89.75           N  
ANISOU 1728  N   ALA A 295     9612  13469  11019   4359   1962   5017       N  
ATOM   1729  CA  ALA A 295      46.790  43.903-193.212  1.00 94.10           C  
ANISOU 1729  CA  ALA A 295    10359  13810  11584   4556   2178   5070       C  
ATOM   1730  C   ALA A 295      45.894  44.353-192.058  1.00101.26           C  
ANISOU 1730  C   ALA A 295    11236  14670  12566   4717   2389   5156       C  
ATOM   1731  O   ALA A 295      44.950  43.649-191.692  1.00105.70           O  
ANISOU 1731  O   ALA A 295    11578  15414  13168   4701   2341   5231       O  
ATOM   1732  CB  ALA A 295      46.415  44.626-194.504  1.00 94.14           C  
ANISOU 1732  CB  ALA A 295    10316  13905  11547   4662   2114   5232       C  
ATOM   1733  N   PRO A 296      46.179  45.509-191.455  1.00100.83           N  
ANISOU 1733  N   PRO A 296    11412  14370  12529   4865   2625   5145       N  
ATOM   1734  CA  PRO A 296      45.401  45.942-190.286  1.00100.98           C  
ANISOU 1734  CA  PRO A 296    11437  14320  12610   5012   2842   5214       C  
ATOM   1735  C   PRO A 296      43.899  45.964-190.543  1.00102.18           C  
ANISOU 1735  C   PRO A 296    11316  14705  12804   5148   2825   5446       C  
ATOM   1736  O   PRO A 296      43.432  46.437-191.581  1.00102.97           O  
ANISOU 1736  O   PRO A 296    11319  14919  12887   5243   2760   5597       O  
ATOM   1737  CB  PRO A 296      45.946  47.346-190.009  1.00100.45           C  
ANISOU 1737  CB  PRO A 296    11667  13967  12531   5157   3073   5190       C  
ATOM   1738  CG  PRO A 296      47.351  47.284-190.477  1.00 96.65           C  
ANISOU 1738  CG  PRO A 296    11377  13351  11995   5007   2988   5012       C  
ATOM   1739  CD  PRO A 296      47.339  46.390-191.691  1.00 97.27           C  
ANISOU 1739  CD  PRO A 296    11251  13670  12037   4876   2710   5040       C  
ATOM   1740  N   ASP A 297      43.148  45.410-189.589  1.00103.01           N  
ANISOU 1740  N   ASP A 297    11293  14883  12963   5150   2876   5477       N  
ATOM   1741  CA  ASP A 297      41.688  45.503-189.549  1.00111.32           C  
ANISOU 1741  CA  ASP A 297    12103  16124  14070   5295   2908   5697       C  
ATOM   1742  C   ASP A 297      41.026  44.884-190.774  1.00119.11           C  
ANISOU 1742  C   ASP A 297    12799  17416  15039   5233   2656   5823       C  
ATOM   1743  O   ASP A 297      39.944  45.308-191.186  1.00128.77           O  
ANISOU 1743  O   ASP A 297    13846  18789  16292   5385   2666   6033       O  
ATOM   1744  CB  ASP A 297      41.238  46.955-189.379  1.00113.09           C  
ANISOU 1744  CB  ASP A 297    12447  16206  14317   5559   3150   5837       C  
ATOM   1745  CG  ASP A 297      41.613  47.520-188.031  1.00115.97           C  
ANISOU 1745  CG  ASP A 297    13072  16293  14700   5627   3413   5738       C  
ATOM   1746  OD1 ASP A 297      41.279  46.887-187.006  1.00119.14           O  
ANISOU 1746  OD1 ASP A 297    13423  16708  15138   5579   3458   5703       O  
ATOM   1747  OD2 ASP A 297      42.252  48.591-187.998  1.00115.35           O  
ANISOU 1747  OD2 ASP A 297    13257  15979  14593   5720   3570   5694       O  
ATOM   1748  N   GLU A 298      41.658  43.877-191.365  1.00116.40           N  
ANISOU 1748  N   GLU A 298    12408  17171  14646   5010   2428   5700       N  
ATOM   1749  CA  GLU A 298      41.087  43.176-192.501  1.00119.37           C  
ANISOU 1749  CA  GLU A 298    12526  17837  14992   4916   2174   5797       C  
ATOM   1750  C   GLU A 298      41.293  41.680-192.315  1.00117.67           C  
ANISOU 1750  C   GLU A 298    12196  17751  14764   4664   1989   5665       C  
ATOM   1751  O   GLU A 298      42.235  41.262-191.631  1.00109.33           O  
ANISOU 1751  O   GLU A 298    11304  16535  13701   4549   2022   5473       O  
ATOM   1752  CB  GLU A 298      41.721  43.630-193.828  1.00122.60           C  
ANISOU 1752  CB  GLU A 298    13019  18238  15325   4904   2058   5799       C  
ATOM   1753  CG  GLU A 298      41.703  45.150-194.073  1.00132.65           C  
ANISOU 1753  CG  GLU A 298    14448  19351  16602   5143   2240   5910       C  
ATOM   1754  CD  GLU A 298      40.336  45.704-194.480  1.00148.16           C  
ANISOU 1754  CD  GLU A 298    16201  21491  18604   5337   2260   6171       C  
ATOM   1755  OE1 GLU A 298      39.295  45.172-194.035  1.00153.26           O  
ANISOU 1755  OE1 GLU A 298    16616  22312  19304   5347   2244   6270       O  
ATOM   1756  OE2 GLU A 298      40.304  46.687-195.253  1.00157.59           O  
ANISOU 1756  OE2 GLU A 298    17459  22645  19773   5482   2292   6282       O  
ATOM   1757  N   PRO A 299      40.424  40.857-192.893  1.00125.27           N  
ANISOU 1757  N   PRO A 299    12881  18995  15721   4574   1794   5764       N  
ATOM   1758  CA  PRO A 299      40.657  39.414-192.868  1.00124.04           C  
ANISOU 1758  CA  PRO A 299    12625  18964  15539   4319   1599   5635       C  
ATOM   1759  C   PRO A 299      41.925  39.076-193.623  1.00119.07           C  
ANISOU 1759  C   PRO A 299    12149  18266  14825   4157   1459   5468       C  
ATOM   1760  O   PRO A 299      42.354  39.837-194.506  1.00127.64           O  
ANISOU 1760  O   PRO A 299    13340  19295  15861   4225   1447   5497       O  
ATOM   1761  CB  PRO A 299      39.417  38.842-193.573  1.00128.17           C  
ANISOU 1761  CB  PRO A 299    12831  19805  16061   4275   1419   5803       C  
ATOM   1762  CG  PRO A 299      38.950  39.958-194.455  1.00131.75           C  
ANISOU 1762  CG  PRO A 299    13257  20299  16502   4466   1446   5987       C  
ATOM   1763  CD  PRO A 299      39.215  41.203-193.659  1.00131.99           C  
ANISOU 1763  CD  PRO A 299    13501  20066  16583   4691   1731   5998       C  
ATOM   1764  N   PRO A 300      42.567  37.954-193.306  1.00104.03           N  
ANISOU 1764  N   PRO A 300    10268  16359  12901   3946   1354   5292       N  
ATOM   1765  CA  PRO A 300      43.769  37.563-194.047  1.00105.32           C  
ANISOU 1765  CA  PRO A 300    10569  16467  12982   3788   1216   5136       C  
ATOM   1766  C   PRO A 300      43.478  37.391-195.532  1.00109.23           C  
ANISOU 1766  C   PRO A 300    10939  17167  13396   3722   1001   5225       C  
ATOM   1767  O   PRO A 300      42.330  37.240-195.957  1.00116.01           O  
ANISOU 1767  O   PRO A 300    11569  18248  14260   3743    914   5386       O  
ATOM   1768  CB  PRO A 300      44.181  36.235-193.396  1.00102.71           C  
ANISOU 1768  CB  PRO A 300    10218  16151  12654   3577   1128   4969       C  
ATOM   1769  CG  PRO A 300      42.956  35.755-192.675  1.00 98.27           C  
ANISOU 1769  CG  PRO A 300     9440  15739  12160   3590   1148   5071       C  
ATOM   1770  CD  PRO A 300      42.234  36.991-192.243  1.00 97.64           C  
ANISOU 1770  CD  PRO A 300     9367  15590  12143   3846   1362   5232       C  
ATOM   1771  N   GLU A 301      44.543  37.437-196.330  1.00106.46           N  
ANISOU 1771  N   GLU A 301    10749  16736  12965   3641    918   5122       N  
ATOM   1772  CA  GLU A 301      44.453  37.206-197.766  1.00105.61           C  
ANISOU 1772  CA  GLU A 301    10566  16801  12761   3553    705   5178       C  
ATOM   1773  C   GLU A 301      45.441  36.117-198.157  1.00 90.64           C  
ANISOU 1773  C   GLU A 301     8745  14910  10784   3309    537   4991       C  
ATOM   1774  O   GLU A 301      46.616  36.181-197.786  1.00 86.20           O  
ANISOU 1774  O   GLU A 301     8393  14142  10217   3276    610   4834       O  
ATOM   1775  CB  GLU A 301      44.727  38.492-198.559  1.00113.64           C  
ANISOU 1775  CB  GLU A 301    11718  17718  13741   3717    770   5269       C  
ATOM   1776  CG  GLU A 301      43.710  39.602-198.318  1.00117.23           C  
ANISOU 1776  CG  GLU A 301    12097  18178  14266   3968    927   5471       C  
ATOM   1777  CD  GLU A 301      43.696  40.649-199.423  1.00116.14           C  
ANISOU 1777  CD  GLU A 301    12023  18032  14074   4100    915   5601       C  
ATOM   1778  OE1 GLU A 301      44.766  40.948-199.995  1.00111.40           O  
ANISOU 1778  OE1 GLU A 301    11629  17293  13405   4059    897   5508       O  
ATOM   1779  OE2 GLU A 301      42.602  41.169-199.726  1.00120.44           O  
ANISOU 1779  OE2 GLU A 301    12408  18710  14643   4245    923   5803       O  
ATOM   1780  N   LEU A 302      44.961  35.119-198.895  1.00 87.03           N  
ANISOU 1780  N   LEU A 302     8119  14686  10262   3136    315   5007       N  
ATOM   1781  CA  LEU A 302      45.828  34.061-199.396  1.00 86.85           C  
ANISOU 1781  CA  LEU A 302     8165  14685  10149   2901    146   4839       C  
ATOM   1782  C   LEU A 302      46.777  34.594-200.463  1.00 92.09           C  
ANISOU 1782  C   LEU A 302     9018  15259  10712   2900    102   4806       C  
ATOM   1783  O   LEU A 302      46.426  35.478-201.250  1.00 96.35           O  
ANISOU 1783  O   LEU A 302     9556  15834  11220   3025    102   4947       O  
ATOM   1784  CB  LEU A 302      44.999  32.923-199.993  1.00 91.05           C  
ANISOU 1784  CB  LEU A 302     8481  15490  10625   2714    -78   4874       C  
ATOM   1785  CG  LEU A 302      44.495  31.773-199.125  1.00 93.73           C  
ANISOU 1785  CG  LEU A 302     8672  15922  11017   2577   -117   4815       C  
ATOM   1786  CD1 LEU A 302      43.713  30.812-199.992  1.00 98.54           C  
ANISOU 1786  CD1 LEU A 302     9094  16797  11549   2390   -351   4862       C  
ATOM   1787  CD2 LEU A 302      45.647  31.050-198.448  1.00 87.95           C  
ANISOU 1787  CD2 LEU A 302     8100  15030  10288   2449    -94   4597       C  
ATOM   1788  N   PHE A 303      47.985  34.030-200.498  1.00 83.95           N  
ANISOU 1788  N   PHE A 303     8153  14116   9629   2756     63   4622       N  
ATOM   1789  CA  PHE A 303      48.951  34.353-201.547  1.00 81.37           C  
ANISOU 1789  CA  PHE A 303     8010  13716   9192   2719      6   4575       C  
ATOM   1790  C   PHE A 303      49.752  33.104-201.878  1.00 79.80           C  
ANISOU 1790  C   PHE A 303     7867  13551   8904   2475   -147   4401       C  
ATOM   1791  O   PHE A 303      50.363  32.504-200.990  1.00 78.49           O  
ANISOU 1791  O   PHE A 303     7757  13283   8785   2400    -98   4256       O  
ATOM   1792  CB  PHE A 303      49.886  35.489-201.125  1.00 80.36           C  
ANISOU 1792  CB  PHE A 303     8114  13314   9106   2870    209   4537       C  
ATOM   1793  CG  PHE A 303      49.193  36.807-200.935  1.00 88.35           C  
ANISOU 1793  CG  PHE A 303     9110  14272  10188   3113    366   4704       C  
ATOM   1794  CD1 PHE A 303      48.789  37.214-199.675  1.00 89.82           C  
ANISOU 1794  CD1 PHE A 303     9269  14361  10497   3248    551   4724       C  
ATOM   1795  CD2 PHE A 303      48.941  37.638-202.018  1.00 92.73           C  
ANISOU 1795  CD2 PHE A 303     9685  14870  10678   3208    331   4842       C  
ATOM   1796  CE1 PHE A 303      48.147  38.423-199.494  1.00 94.40           C  
ANISOU 1796  CE1 PHE A 303     9845  14886  11135   3474    706   4876       C  
ATOM   1797  CE2 PHE A 303      48.297  38.854-201.845  1.00 95.96           C  
ANISOU 1797  CE2 PHE A 303    10084  15226  11152   3439    479   5000       C  
ATOM   1798  CZ  PHE A 303      47.900  39.246-200.581  1.00 98.70           C  
ANISOU 1798  CZ  PHE A 303    10405  15474  11621   3573    670   5015       C  
ATOM   1799  N   LEU A 304      49.747  32.721-203.150  1.00 82.10           N  
ANISOU 1799  N   LEU A 304     8151  13982   9062   2353   -328   4417       N  
ATOM   1800  CA  LEU A 304      50.517  31.575-203.617  1.00 83.78           C  
ANISOU 1800  CA  LEU A 304     8437  14227   9168   2122   -471   4256       C  
ATOM   1801  C   LEU A 304      51.963  32.008-203.824  1.00 83.65           C  
ANISOU 1801  C   LEU A 304     8683  14000   9102   2128   -390   4146       C  
ATOM   1802  O   LEU A 304      52.229  32.944-204.583  1.00 90.87           O  
ANISOU 1802  O   LEU A 304     9710  14857   9960   2222   -358   4221       O  
ATOM   1803  CB  LEU A 304      49.910  31.040-204.915  1.00 93.60           C  
ANISOU 1803  CB  LEU A 304     9588  15699  10277   1988   -688   4318       C  
ATOM   1804  CG  LEU A 304      49.972  29.558-205.297  1.00 92.84           C  
ANISOU 1804  CG  LEU A 304     9452  15739  10085   1724   -875   4192       C  
ATOM   1805  CD1 LEU A 304      49.244  28.701-204.275  1.00 97.63           C  
ANISOU 1805  CD1 LEU A 304     9876  16426  10792   1656   -885   4165       C  
ATOM   1806  CD2 LEU A 304      49.370  29.361-206.692  1.00 92.98           C  
ANISOU 1806  CD2 LEU A 304     9413  15958   9958   1628  -1068   4279       C  
ATOM   1807  N   LEU A 305      52.896  31.356-203.137  1.00 72.87           N  
ANISOU 1807  N   LEU A 305     7414  12515   7757   2031   -352   3975       N  
ATOM   1808  CA  LEU A 305      54.300  31.692-203.325  1.00 74.41           C  
ANISOU 1808  CA  LEU A 305     7851  12518   7903   2019   -277   3868       C  
ATOM   1809  C   LEU A 305      54.777  31.173-204.681  1.00 85.68           C  
ANISOU 1809  C   LEU A 305     9363  14037   9155   1860   -432   3824       C  
ATOM   1810  O   LEU A 305      54.440  30.049-205.068  1.00 88.94           O  
ANISOU 1810  O   LEU A 305     9684  14615   9495   1687   -594   3774       O  
ATOM   1811  CB  LEU A 305      55.164  31.095-202.208  1.00 71.10           C  
ANISOU 1811  CB  LEU A 305     7506  11956   7553   1956   -200   3702       C  
ATOM   1812  CG  LEU A 305      55.136  31.730-200.818  1.00 70.02           C  
ANISOU 1812  CG  LEU A 305     7378  11654   7573   2109    -10   3706       C  
ATOM   1813  CD1 LEU A 305      55.933  30.871-199.845  1.00 66.48           C  
ANISOU 1813  CD1 LEU A 305     6985  11108   7168   2005     15   3539       C  
ATOM   1814  CD2 LEU A 305      55.690  33.143-200.844  1.00 69.64           C  
ANISOU 1814  CD2 LEU A 305     7504  11406   7549   2274    158   3753       C  
ATOM   1815  N   PRO A 306      55.543  31.963-205.428  1.00 89.84           N  
ANISOU 1815  N   PRO A 306    10074  14458   9605   1905   -381   3839       N  
ATOM   1816  CA  PRO A 306      56.077  31.479-206.707  1.00 93.28           C  
ANISOU 1816  CA  PRO A 306    10616  14966   9860   1751   -510   3789       C  
ATOM   1817  C   PRO A 306      56.972  30.272-206.489  1.00 87.89           C  
ANISOU 1817  C   PRO A 306    10002  14262   9128   1561   -553   3597       C  
ATOM   1818  O   PRO A 306      57.956  30.352-205.740  1.00 81.60           O  
ANISOU 1818  O   PRO A 306     9323  13289   8393   1576   -426   3493       O  
ATOM   1819  CB  PRO A 306      56.877  32.679-207.243  1.00 91.00           C  
ANISOU 1819  CB  PRO A 306    10533  14514   9529   1856   -392   3832       C  
ATOM   1820  CG  PRO A 306      56.335  33.863-206.509  1.00 88.66           C  
ANISOU 1820  CG  PRO A 306    10190  14117   9378   2079   -245   3954       C  
ATOM   1821  CD  PRO A 306      55.935  33.357-205.157  1.00 86.29           C  
ANISOU 1821  CD  PRO A 306     9753  13811   9222   2095   -197   3903       C  
ATOM   1822  N   PRO A 307      56.649  29.133-207.112  1.00 90.76           N  
ANISOU 1822  N   PRO A 307    10300  14800   9383   1378   -729   3543       N  
ATOM   1823  CA  PRO A 307      57.489  27.932-206.941  1.00 91.67           C  
ANISOU 1823  CA  PRO A 307    10490  14897   9444   1193   -769   3355       C  
ATOM   1824  C   PRO A 307      58.954  28.184-207.239  1.00 88.43           C  
ANISOU 1824  C   PRO A 307    10315  14323   8961   1171   -667   3256       C  
ATOM   1825  O   PRO A 307      59.838  27.647-206.558  1.00 88.48           O  
ANISOU 1825  O   PRO A 307    10391  14227   9000   1111   -604   3118       O  
ATOM   1826  CB  PRO A 307      56.874  26.936-207.934  1.00 93.29           C  
ANISOU 1826  CB  PRO A 307    10629  15309   9506   1009   -972   3338       C  
ATOM   1827  CG  PRO A 307      55.463  27.402-208.119  1.00 90.76           C  
ANISOU 1827  CG  PRO A 307    10119  15136   9228   1098  -1041   3516       C  
ATOM   1828  CD  PRO A 307      55.501  28.895-208.004  1.00 88.17           C  
ANISOU 1828  CD  PRO A 307     9836  14690   8974   1326   -897   3651       C  
ATOM   1829  N   GLU A 308      59.223  29.017-208.244  1.00 73.84           N  
ANISOU 1829  N   GLU A 308     8590  12450   7015   1221   -646   3331       N  
ATOM   1830  CA  GLU A 308      60.585  29.415-208.574  1.00 75.11           C  
ANISOU 1830  CA  GLU A 308     8977  12452   7110   1209   -528   3257       C  
ATOM   1831  C   GLU A 308      61.291  30.074-207.393  1.00 75.22           C  
ANISOU 1831  C   GLU A 308     9049  12253   7278   1328   -338   3225       C  
ATOM   1832  O   GLU A 308      62.526  30.050-207.311  1.00 66.62           O  
ANISOU 1832  O   GLU A 308     8118  11031   6165   1280   -237   3118       O  
ATOM   1833  CB  GLU A 308      60.557  30.362-209.778  1.00 76.06           C  
ANISOU 1833  CB  GLU A 308     9204  12579   7118   1266   -530   3374       C  
ATOM   1834  CG  GLU A 308      59.228  31.107-209.954  1.00 91.78           C  
ANISOU 1834  CG  GLU A 308    11047  14668   9157   1404   -586   3564       C  
ATOM   1835  CD  GLU A 308      58.155  30.264-210.637  1.00109.57           C  
ANISOU 1835  CD  GLU A 308    13152  17160  11318   1292   -795   3601       C  
ATOM   1836  OE1 GLU A 308      58.512  29.386-211.451  1.00117.75           O  
ANISOU 1836  OE1 GLU A 308    14266  18277  12196   1113   -900   3504       O  
ATOM   1837  OE2 GLU A 308      56.957  30.473-210.348  1.00116.24           O  
ANISOU 1837  OE2 GLU A 308    13806  18112  12250   1379   -846   3724       O  
ATOM   1838  N   LEU A 309      60.533  30.653-206.464  1.00 71.10           N  
ANISOU 1838  N   LEU A 309     8405  11696   6914   1478   -281   3313       N  
ATOM   1839  CA  LEU A 309      61.135  31.383-205.362  1.00 62.10           C  
ANISOU 1839  CA  LEU A 309     7338  10342   5915   1594    -98   3289       C  
ATOM   1840  C   LEU A 309      61.357  30.529-204.123  1.00 64.31           C  
ANISOU 1840  C   LEU A 309     7556  10584   6294   1542    -79   3170       C  
ATOM   1841  O   LEU A 309      62.035  30.987-203.201  1.00 62.85           O  
ANISOU 1841  O   LEU A 309     7456  10213   6210   1606     68   3121       O  
ATOM   1842  CB  LEU A 309      60.274  32.585-204.983  1.00 68.93           C  
ANISOU 1842  CB  LEU A 309     8139  11160   6892   1797    -14   3442       C  
ATOM   1843  CG  LEU A 309      61.054  33.881-204.779  1.00 82.68           C  
ANISOU 1843  CG  LEU A 309    10061  12669   8683   1916    173   3461       C  
ATOM   1844  CD1 LEU A 309      61.693  34.342-206.090  1.00 81.63           C  
ANISOU 1844  CD1 LEU A 309    10091  12521   8406   1873    166   3486       C  
ATOM   1845  CD2 LEU A 309      60.143  34.954-204.215  1.00 90.21           C  
ANISOU 1845  CD2 LEU A 309    10946  13572   9759   2117    266   3594       C  
ATOM   1846  N   VAL A 310      60.806  29.318-204.072  1.00 70.05           N  
ANISOU 1846  N   VAL A 310     8146  11475   6995   1421   -223   3121       N  
ATOM   1847  CA  VAL A 310      60.956  28.428-202.921  1.00 57.13           C  
ANISOU 1847  CA  VAL A 310     6448   9814   5447   1362   -219   3012       C  
ATOM   1848  C   VAL A 310      61.992  27.377-203.303  1.00 57.91           C  
ANISOU 1848  C   VAL A 310     6650   9923   5431   1180   -271   2855       C  
ATOM   1849  O   VAL A 310      61.692  26.412-204.010  1.00 61.70           O  
ANISOU 1849  O   VAL A 310     7083  10560   5799   1035   -418   2812       O  
ATOM   1850  CB  VAL A 310      59.621  27.801-202.509  1.00 51.91           C  
ANISOU 1850  CB  VAL A 310     5564   9315   4844   1347   -329   3063       C  
ATOM   1851  CG1 VAL A 310      59.780  26.971-201.211  1.00 52.79           C  
ANISOU 1851  CG1 VAL A 310     5622   9379   5057   1299   -309   2957       C  
ATOM   1852  CG2 VAL A 310      58.576  28.882-202.319  1.00 58.25           C  
ANISOU 1852  CG2 VAL A 310     6265  10129   5739   1530   -270   3230       C  
ATOM   1853  N   LEU A 311      63.224  27.573-202.848  1.00 55.65           N  
ANISOU 1853  N   LEU A 311     6511   9464   5168   1184   -141   2767       N  
ATOM   1854  CA  LEU A 311      64.293  26.631-203.136  1.00 56.59           C  
ANISOU 1854  CA  LEU A 311     6731   9583   5187   1027   -158   2617       C  
ATOM   1855  C   LEU A 311      64.176  25.426-202.212  1.00 60.23           C  
ANISOU 1855  C   LEU A 311     7097  10063   5724    928   -220   2488       C  
ATOM   1856  O   LEU A 311      64.086  25.576-200.987  1.00 50.91           O  
ANISOU 1856  O   LEU A 311     5869   8774   4698    998   -149   2471       O  
ATOM   1857  CB  LEU A 311      65.651  27.304-202.958  1.00 57.08           C  
ANISOU 1857  CB  LEU A 311     6971   9435   5281   1054     18   2546       C  
ATOM   1858  CG  LEU A 311      66.861  26.438-203.287  1.00 50.88           C  
ANISOU 1858  CG  LEU A 311     6290   8583   4460    882     37   2323       C  
ATOM   1859  CD1 LEU A 311      66.774  25.891-204.714  1.00 55.92           C  
ANISOU 1859  CD1 LEU A 311     6965   9386   4896    769    -72   2322       C  
ATOM   1860  CD2 LEU A 311      68.136  27.241-203.088  1.00 50.98           C  
ANISOU 1860  CD2 LEU A 311     6453   8383   4535    910    216   2258       C  
ATOM   1861  N   GLU A 312      64.168  24.228-202.788  1.00 56.62           N  
ANISOU 1861  N   GLU A 312     6625   9718   5169    754   -344   2376       N  
ATOM   1862  CA  GLU A 312      64.065  23.027-201.973  1.00 57.16           C  
ANISOU 1862  CA  GLU A 312     6619   9780   5319    642   -401   2230       C  
ATOM   1863  C   GLU A 312      65.169  22.052-202.339  1.00 55.28           C  
ANISOU 1863  C   GLU A 312     6505   9466   5033    477   -393   2008       C  
ATOM   1864  O   GLU A 312      65.763  22.122-203.415  1.00 51.43           O  
ANISOU 1864  O   GLU A 312     6135   8992   4416    424   -382   1977       O  
ATOM   1865  CB  GLU A 312      62.706  22.345-202.127  1.00 53.24           C  
ANISOU 1865  CB  GLU A 312     5951   9509   4770    586   -577   2321       C  
ATOM   1866  CG  GLU A 312      61.541  23.226-201.781  1.00 66.37           C  
ANISOU 1866  CG  GLU A 312     7468  11237   6512    746   -577   2520       C  
ATOM   1867  CD  GLU A 312      60.352  22.433-201.298  1.00 80.77           C  
ANISOU 1867  CD  GLU A 312     9102  13191   8397    683   -692   2535       C  
ATOM   1868  OE1 GLU A 312      59.515  23.016-200.588  1.00 87.62           O  
ANISOU 1868  OE1 GLU A 312     9846  14055   9391    811   -645   2644       O  
ATOM   1869  OE2 GLU A 312      60.258  21.227-201.609  1.00 85.77           O  
ANISOU 1869  OE2 GLU A 312     9717  13920   8950    500   -817   2433       O  
ATOM   1870  N   VAL A 313      65.416  21.122-201.427  1.00 49.81           N  
ANISOU 1870  N   VAL A 313     5786   8694   4446    400   -395   1857       N  
ATOM   1871  CA  VAL A 313      66.500  20.161-201.581  1.00 45.34           C  
ANISOU 1871  CA  VAL A 313     5330   8031   3868    265   -371   1642       C  
ATOM   1872  C   VAL A 313      65.937  18.750-201.476  1.00 53.53           C  
ANISOU 1872  C   VAL A 313     6303   9157   4878    118   -504   1551       C  
ATOM   1873  O   VAL A 313      65.482  18.346-200.394  1.00 59.81           O  
ANISOU 1873  O   VAL A 313     7003   9929   5794    122   -525   1537       O  
ATOM   1874  CB  VAL A 313      67.589  20.396-200.520  1.00 49.45           C  
ANISOU 1874  CB  VAL A 313     5908   8330   4552    315   -226   1532       C  
ATOM   1875  CG1 VAL A 313      68.748  19.441-200.740  1.00 44.88           C  
ANISOU 1875  CG1 VAL A 313     5431   7658   3965    194   -194   1325       C  
ATOM   1876  CG2 VAL A 313      68.046  21.857-200.545  1.00 46.37           C  
ANISOU 1876  CG2 VAL A 313     5581   7847   4192    453    -95   1633       C  
ATOM   1877  N   PRO A 314      65.937  17.971-202.551  1.00 44.18           N  
ANISOU 1877  N   PRO A 314     5180   8072   3536    -21   -591   1485       N  
ATOM   1878  CA  PRO A 314      65.588  16.555-202.416  1.00 44.13           C  
ANISOU 1878  CA  PRO A 314     5149   8109   3508   -180   -699   1367       C  
ATOM   1879  C   PRO A 314      66.669  15.843-201.635  1.00 47.96           C  
ANISOU 1879  C   PRO A 314     5710   8397   4115   -213   -606   1172       C  
ATOM   1880  O   PRO A 314      67.856  16.146-201.777  1.00 45.24           O  
ANISOU 1880  O   PRO A 314     5476   7918   3795   -177   -482   1089       O  
ATOM   1881  CB  PRO A 314      65.525  16.060-203.868  1.00 47.76           C  
ANISOU 1881  CB  PRO A 314     5702   8695   3752   -314   -786   1336       C  
ATOM   1882  CG  PRO A 314      65.433  17.294-204.682  1.00 51.28           C  
ANISOU 1882  CG  PRO A 314     6165   9215   4105   -210   -762   1496       C  
ATOM   1883  CD  PRO A 314      66.185  18.334-203.963  1.00 42.40           C  
ANISOU 1883  CD  PRO A 314     5058   7924   3128    -48   -598   1522       C  
ATOM   1884  N   LEU A 315      66.247  14.904-200.786  1.00 44.26           N  
ANISOU 1884  N   LEU A 315     5176   7913   3727   -281   -665   1108       N  
ATOM   1885  CA  LEU A 315      67.153  14.273-199.842  1.00 39.18           C  
ANISOU 1885  CA  LEU A 315     4583   7084   3221   -291   -586    950       C  
ATOM   1886  C   LEU A 315      67.662  12.956-200.411  1.00 42.47           C  
ANISOU 1886  C   LEU A 315     5113   7466   3557   -444   -616    773       C  
ATOM   1887  O   LEU A 315      66.871  12.101-200.838  1.00 47.71           O  
ANISOU 1887  O   LEU A 315     5765   8242   4120   -576   -739    759       O  
ATOM   1888  CB  LEU A 315      66.466  14.067-198.490  1.00 40.57           C  
ANISOU 1888  CB  LEU A 315     4637   7240   3537   -263   -614    987       C  
ATOM   1889  CG  LEU A 315      66.127  15.363-197.735  1.00 44.50           C  
ANISOU 1889  CG  LEU A 315     5047   7725   4137    -96   -548   1139       C  
ATOM   1890  CD1 LEU A 315      65.729  15.068-196.280  1.00 45.22           C  
ANISOU 1890  CD1 LEU A 315     5054   7751   4376    -71   -542   1137       C  
ATOM   1891  CD2 LEU A 315      67.276  16.365-197.785  1.00 41.66           C  
ANISOU 1891  CD2 LEU A 315     4782   7230   3819     12   -406   1126       C  
ATOM   1892  N   GLU A 316      68.987  12.829-200.457  1.00 44.22           N  
ANISOU 1892  N   GLU A 316     5448   7534   3819   -425   -499    641       N  
ATOM   1893  CA AGLU A 316      69.668  11.618-200.888  0.56 44.96           C  
ANISOU 1893  CA AGLU A 316     5664   7555   3864   -538   -488    462       C  
ATOM   1894  CA BGLU A 316      69.676  11.629-200.898  0.44 45.32           C  
ANISOU 1894  CA BGLU A 316     5711   7601   3909   -537   -487    462       C  
ATOM   1895  C   GLU A 316      70.789  11.321-199.903  1.00 43.58           C  
ANISOU 1895  C   GLU A 316     5515   7185   3860   -482   -381    346       C  
ATOM   1896  O   GLU A 316      71.212  12.184-199.133  1.00 42.46           O  
ANISOU 1896  O   GLU A 316     5321   6968   3843   -365   -306    397       O  
ATOM   1897  CB AGLU A 316      70.235  11.740-202.324  0.56 47.08           C  
ANISOU 1897  CB AGLU A 316     6063   7859   3966   -577   -445    422       C  
ATOM   1898  CB BGLU A 316      70.228  11.818-202.326  0.44 47.17           C  
ANISOU 1898  CB BGLU A 316     6071   7874   3979   -570   -443    430       C  
ATOM   1899  CG AGLU A 316      71.594  12.445-202.432  0.56 43.97           C  
ANISOU 1899  CG AGLU A 316     5733   7341   3633   -477   -281    381       C  
ATOM   1900  CG BGLU A 316      69.177  12.381-203.283  0.44 48.45           C  
ANISOU 1900  CG BGLU A 316     6201   8236   3973   -600   -547    578       C  
ATOM   1901  CD AGLU A 316      72.264  12.246-203.792  0.56 52.96           C  
ANISOU 1901  CD AGLU A 316     7019   8491   4612   -536   -221    302       C  
ATOM   1902  CD BGLU A 316      69.747  12.954-204.577  0.44 57.41           C  
ANISOU 1902  CD BGLU A 316     7452   9405   4956   -594   -484    588       C  
ATOM   1903  OE1AGLU A 316      71.539  12.060-204.793  0.56 53.55           O  
ANISOU 1903  OE1AGLU A 316     7140   8704   4502   -626   -312    337       O  
ATOM   1904  OE1BGLU A 316      70.604  12.300-205.204  0.44 53.46           O  
ANISOU 1904  OE1BGLU A 316     7092   8833   4389   -660   -416    441       O  
ATOM   1905  OE2AGLU A 316      73.515  12.269-203.860  0.56 52.72           O  
ANISOU 1905  OE2AGLU A 316     7056   8337   4637   -495    -82    206       O  
ATOM   1906  OE2BGLU A 316      69.322  14.063-204.969  0.44 57.47           O  
ANISOU 1906  OE2BGLU A 316     7416   9511   4911   -519   -496    748       O  
ATOM   1907  N   HIS A 317      71.258  10.079-199.918  1.00 45.02           N  
ANISOU 1907  N   HIS A 317     5781   7282   4042   -568   -379    191       N  
ATOM   1908  CA  HIS A 317      72.320   9.698-199.010  1.00 49.76           C  
ANISOU 1908  CA  HIS A 317     6400   7705   4801   -514   -290     85       C  
ATOM   1909  C   HIS A 317      73.571   9.349-199.806  1.00 53.17           C  
ANISOU 1909  C   HIS A 317     6955   8050   5195   -519   -180    -44       C  
ATOM   1910  O   HIS A 317      73.461   8.788-200.900  1.00 53.32           O  
ANISOU 1910  O   HIS A 317     7076   8122   5061   -610   -197   -103       O  
ATOM   1911  CB  HIS A 317      71.884   8.499-198.146  1.00 46.94           C  
ANISOU 1911  CB  HIS A 317     6031   7294   4510   -586   -364     18       C  
ATOM   1912  CG  HIS A 317      72.860   8.127-197.081  1.00 38.69           C  
ANISOU 1912  CG  HIS A 317     4990   6076   3633   -522   -291    -67       C  
ATOM   1913  ND1 HIS A 317      74.027   7.446-197.349  1.00 43.22           N  
ANISOU 1913  ND1 HIS A 317     5662   6528   4231   -519   -207   -204       N  
ATOM   1914  CD2 HIS A 317      72.839   8.325-195.735  1.00 42.44           C  
ANISOU 1914  CD2 HIS A 317     5385   6483   4257   -458   -294    -29       C  
ATOM   1915  CE1 HIS A 317      74.687   7.245-196.220  1.00 45.29           C  
ANISOU 1915  CE1 HIS A 317     5892   6662   4654   -454   -170   -241       C  
ATOM   1916  NE2 HIS A 317      73.988   7.769-195.228  1.00 38.24           N  
ANISOU 1916  NE2 HIS A 317     4900   5798   3833   -422   -224   -139       N  
ATOM   1917  N   PRO A 318      74.766   9.685-199.306  1.00 46.73           N  
ANISOU 1917  N   PRO A 318     6134   7109   4511   -425    -64    -87       N  
ATOM   1918  CA  PRO A 318      75.974   9.447-200.121  1.00 46.82           C  
ANISOU 1918  CA  PRO A 318     6246   7052   4490   -419     57   -196       C  
ATOM   1919  C   PRO A 318      76.208   7.991-200.479  1.00 49.34           C  
ANISOU 1919  C   PRO A 318     6676   7308   4764   -500     58   -346       C  
ATOM   1920  O   PRO A 318      76.723   7.712-201.566  1.00 52.12           O  
ANISOU 1920  O   PRO A 318     7139   7659   5005   -532    130   -423       O  
ATOM   1921  CB  PRO A 318      77.108  10.011-199.252  1.00 46.35           C  
ANISOU 1921  CB  PRO A 318     6124   6876   4610   -310    159   -202       C  
ATOM   1922  CG  PRO A 318      76.520  10.125-197.841  1.00 47.12           C  
ANISOU 1922  CG  PRO A 318     6120   6948   4836   -279     80   -138       C  
ATOM   1923  CD  PRO A 318      75.068  10.437-198.075  1.00 46.14           C  
ANISOU 1923  CD  PRO A 318     5962   6965   4605   -323    -32    -26       C  
ATOM   1924  N   THR A 319      75.838   7.046-199.620  1.00 48.92           N  
ANISOU 1924  N   THR A 319     6608   7194   4785   -536    -13   -392       N  
ATOM   1925  CA  THR A 319      76.099   5.641-199.900  1.00 54.69           C  
ANISOU 1925  CA  THR A 319     7461   7839   5482   -607     -1   -537       C  
ATOM   1926  C   THR A 319      74.867   4.755-199.863  1.00 55.82           C  
ANISOU 1926  C   THR A 319     7637   8034   5538   -740   -139   -544       C  
ATOM   1927  O   THR A 319      74.925   3.632-200.377  1.00 67.23           O  
ANISOU 1927  O   THR A 319     9216   9424   6904   -828   -135   -663       O  
ATOM   1928  CB  THR A 319      77.132   5.076-198.914  1.00 58.81           C  
ANISOU 1928  CB  THR A 319     7966   8191   6188   -525     70   -617       C  
ATOM   1929  OG1 THR A 319      76.580   5.058-197.589  1.00 58.99           O  
ANISOU 1929  OG1 THR A 319     7889   8193   6330   -509    -17   -555       O  
ATOM   1930  CG2 THR A 319      78.397   5.928-198.927  1.00 57.06           C  
ANISOU 1930  CG2 THR A 319     7696   7925   6059   -406    202   -609       C  
ATOM   1931  N   LEU A 320      73.765   5.214-199.278  1.00 48.47           N  
ANISOU 1931  N   LEU A 320     6591   7204   4620   -760   -252   -422       N  
ATOM   1932  CA  LEU A 320      72.532   4.431-199.197  1.00 44.43           C  
ANISOU 1932  CA  LEU A 320     6085   6761   4036   -897   -387   -414       C  
ATOM   1933  C   LEU A 320      71.677   4.804-200.402  1.00 48.32           C  
ANISOU 1933  C   LEU A 320     6596   7434   4329   -991   -464   -349       C  
ATOM   1934  O   LEU A 320      70.901   5.760-200.381  1.00 44.83           O  
ANISOU 1934  O   LEU A 320     6036   7132   3866   -965   -527   -202       O  
ATOM   1935  CB  LEU A 320      71.828   4.680-197.868  1.00 44.41           C  
ANISOU 1935  CB  LEU A 320     5940   6772   4164   -864   -458   -315       C  
ATOM   1936  CG  LEU A 320      72.623   4.161-196.665  1.00 46.68           C  
ANISOU 1936  CG  LEU A 320     6226   6881   4629   -791   -401   -382       C  
ATOM   1937  CD1 LEU A 320      72.032   4.661-195.350  1.00 42.57           C  
ANISOU 1937  CD1 LEU A 320     5568   6375   4231   -738   -449   -273       C  
ATOM   1938  CD2 LEU A 320      72.690   2.645-196.671  1.00 51.41           C  
ANISOU 1938  CD2 LEU A 320     6952   7373   5210   -890   -417   -515       C  
ATOM   1939  N   GLU A 321      71.836   4.031-201.477  1.00 51.53           N  
ANISOU 1939  N   GLU A 321     7162   7834   4583  -1098   -455   -460       N  
ATOM   1940  CA  GLU A 321      71.245   4.388-202.759  1.00 59.44           C  
ANISOU 1940  CA  GLU A 321     8210   8999   5375  -1187   -515   -412       C  
ATOM   1941  C   GLU A 321      69.731   4.521-202.672  1.00 55.95           C  
ANISOU 1941  C   GLU A 321     7656   8738   4866  -1287   -690   -285       C  
ATOM   1942  O   GLU A 321      69.144   5.352-203.372  1.00 57.09           O  
ANISOU 1942  O   GLU A 321     7747   9048   4895  -1293   -750   -165       O  
ATOM   1943  CB  GLU A 321      71.655   3.354-203.815  1.00 72.23           C  
ANISOU 1943  CB  GLU A 321    10045  10560   6839  -1304   -476   -573       C  
ATOM   1944  CG  GLU A 321      71.877   1.928-203.270  1.00 93.08           C  
ANISOU 1944  CG  GLU A 321    12788  13035   9544  -1369   -462   -721       C  
ATOM   1945  CD  GLU A 321      73.187   1.764-202.488  1.00 99.24           C  
ANISOU 1945  CD  GLU A 321    13571  13617  10519  -1215   -311   -798       C  
ATOM   1946  OE1 GLU A 321      74.223   2.308-202.930  1.00101.57           O  
ANISOU 1946  OE1 GLU A 321    13891  13870  10829  -1107   -178   -822       O  
ATOM   1947  OE2 GLU A 321      73.167   1.110-201.421  1.00 93.30           O  
ANISOU 1947  OE2 GLU A 321    12787  12757   9905  -1203   -329   -827       O  
ATOM   1948  N   TRP A 322      69.083   3.745-201.802  1.00 48.58           N  
ANISOU 1948  N   TRP A 322     6674   7778   4007  -1359   -770   -296       N  
ATOM   1949  CA  TRP A 322      67.625   3.754-201.700  1.00 48.01           C  
ANISOU 1949  CA  TRP A 322     6483   7883   3877  -1468   -933   -179       C  
ATOM   1950  C   TRP A 322      67.065   4.965-200.956  1.00 50.89           C  
ANISOU 1950  C   TRP A 322     6637   8347   4351  -1337   -956      7       C  
ATOM   1951  O   TRP A 322      65.846   5.173-200.996  1.00 47.86           O  
ANISOU 1951  O   TRP A 322     6130   8138   3915  -1403  -1083    132       O  
ATOM   1952  CB  TRP A 322      67.136   2.470-201.008  1.00 50.47           C  
ANISOU 1952  CB  TRP A 322     6821   8123   4231  -1600   -999   -257       C  
ATOM   1953  CG  TRP A 322      67.930   2.154-199.754  1.00 45.94           C  
ANISOU 1953  CG  TRP A 322     6244   7348   3863  -1487   -899   -320       C  
ATOM   1954  CD1 TRP A 322      68.911   1.214-199.631  1.00 49.92           C  
ANISOU 1954  CD1 TRP A 322     6903   7652   4411  -1484   -806   -482       C  
ATOM   1955  CD2 TRP A 322      67.837   2.806-198.476  1.00 49.09           C  
ANISOU 1955  CD2 TRP A 322     6483   7726   4443  -1355   -879   -219       C  
ATOM   1956  NE1 TRP A 322      69.423   1.228-198.352  1.00 50.38           N  
ANISOU 1956  NE1 TRP A 322     6898   7577   4666  -1362   -744   -480       N  
ATOM   1957  CE2 TRP A 322      68.785   2.201-197.628  1.00 45.66           C  
ANISOU 1957  CE2 TRP A 322     6115   7084   4149  -1288   -788   -325       C  
ATOM   1958  CE3 TRP A 322      67.039   3.832-197.963  1.00 52.30           C  
ANISOU 1958  CE3 TRP A 322     6703   8266   4902  -1284   -926    -48       C  
ATOM   1959  CZ2 TRP A 322      68.953   2.585-196.291  1.00 51.15           C  
ANISOU 1959  CZ2 TRP A 322     6704   7709   5024  -1169   -753   -268       C  
ATOM   1960  CZ3 TRP A 322      67.224   4.228-196.634  1.00 47.54           C  
ANISOU 1960  CZ3 TRP A 322     6003   7579   4480  -1158   -875      1       C  
ATOM   1961  CH2 TRP A 322      68.169   3.601-195.820  1.00 42.19           C  
ANISOU 1961  CH2 TRP A 322     5402   6701   3927  -1110   -795   -111       C  
ATOM   1962  N   PHE A 323      67.901   5.751-200.262  1.00 46.56           N  
ANISOU 1962  N   PHE A 323     6043   7693   3955  -1157   -836     29       N  
ATOM   1963  CA  PHE A 323      67.367   6.856-199.465  1.00 53.02           C  
ANISOU 1963  CA  PHE A 323     6684   8581   4881  -1034   -845    195       C  
ATOM   1964  C   PHE A 323      66.615   7.862-200.337  1.00 55.10           C  
ANISOU 1964  C   PHE A 323     6872   9044   5021  -1018   -908    350       C  
ATOM   1965  O   PHE A 323      65.544   8.347-199.951  1.00 49.17           O  
ANISOU 1965  O   PHE A 323     5965   8423   4292   -998   -987    499       O  
ATOM   1966  CB  PHE A 323      68.491   7.544-198.689  1.00 46.07           C  
ANISOU 1966  CB  PHE A 323     5797   7545   4161   -862   -704    179       C  
ATOM   1967  CG  PHE A 323      68.006   8.410-197.556  1.00 51.49           C  
ANISOU 1967  CG  PHE A 323     6333   8249   4983   -748   -700    313       C  
ATOM   1968  CD1 PHE A 323      67.510   9.681-197.798  1.00 42.17           C  
ANISOU 1968  CD1 PHE A 323     5059   7187   3778   -656   -702    472       C  
ATOM   1969  CD2 PHE A 323      68.064   7.957-196.245  1.00 48.46           C  
ANISOU 1969  CD2 PHE A 323     5912   7754   4746   -727   -686    280       C  
ATOM   1970  CE1 PHE A 323      67.067  10.481-196.758  1.00 44.50           C  
ANISOU 1970  CE1 PHE A 323     5231   7483   4193   -544   -681    590       C  
ATOM   1971  CE2 PHE A 323      67.618   8.760-195.195  1.00 41.81           C  
ANISOU 1971  CE2 PHE A 323     4948   6921   4018   -624   -671    397       C  
ATOM   1972  CZ  PHE A 323      67.125  10.021-195.453  1.00 38.81           C  
ANISOU 1972  CZ  PHE A 323     4480   6652   3612   -531   -664    548       C  
ATOM   1973  N   ALA A 324      67.161   8.188-201.515  1.00 51.17           N  
ANISOU 1973  N   ALA A 324     6481   8571   4390  -1020   -870    325       N  
ATOM   1974  CA  ALA A 324      66.467   9.070-202.448  1.00 49.87           C  
ANISOU 1974  CA  ALA A 324     6265   8596   4087  -1013   -939    473       C  
ATOM   1975  C   ALA A 324      65.062   8.561-202.752  1.00 55.23           C  
ANISOU 1975  C   ALA A 324     6862   9467   4656  -1163  -1119    548       C  
ATOM   1976  O   ALA A 324      64.114   9.347-202.851  1.00 50.91           O  
ANISOU 1976  O   ALA A 324     6171   9090   4083  -1121  -1199    727       O  
ATOM   1977  CB  ALA A 324      67.278   9.205-203.745  1.00 46.25           C  
ANISOU 1977  CB  ALA A 324     5970   8128   3475  -1033   -876    405       C  
ATOM   1978  N   ALA A 325      64.909   7.241-202.893  1.00 63.93           N  
ANISOU 1978  N   ALA A 325     8053  10543   5695  -1340  -1184    416       N  
ATOM   1979  CA  ALA A 325      63.611   6.660-203.223  1.00 64.94           C  
ANISOU 1979  CA  ALA A 325     8113  10853   5709  -1517  -1362    472       C  
ATOM   1980  C   ALA A 325      62.567   6.900-202.138  1.00 63.46           C  
ANISOU 1980  C   ALA A 325     7705  10752   5657  -1479  -1428    613       C  
ATOM   1981  O   ALA A 325      61.366   6.813-202.422  1.00 61.18           O  
ANISOU 1981  O   ALA A 325     7296  10663   5286  -1586  -1577    724       O  
ATOM   1982  CB  ALA A 325      63.764   5.161-203.487  1.00 60.68           C  
ANISOU 1982  CB  ALA A 325     7739  10229   5088  -1718  -1396    285       C  
ATOM   1983  N   LEU A 326      62.987   7.205-200.902  1.00 56.31           N  
ANISOU 1983  N   LEU A 326     6739   9704   4951  -1334  -1320    614       N  
ATOM   1984  CA  LEU A 326      62.016   7.570-199.876  1.00 52.17           C  
ANISOU 1984  CA  LEU A 326     6010   9261   4553  -1276  -1359    758       C  
ATOM   1985  C   LEU A 326      61.277   8.863-200.201  1.00 53.98           C  
ANISOU 1985  C   LEU A 326     6082   9674   4755  -1158  -1395    972       C  
ATOM   1986  O   LEU A 326      60.251   9.139-199.570  1.00 60.24           O  
ANISOU 1986  O   LEU A 326     6689  10581   5619  -1128  -1447   1112       O  
ATOM   1987  CB  LEU A 326      62.702   7.682-198.499  1.00 40.19           C  
ANISOU 1987  CB  LEU A 326     4487   7543   3240  -1142  -1228    710       C  
ATOM   1988  CG  LEU A 326      63.246   6.373-197.941  1.00 48.91           C  
ANISOU 1988  CG  LEU A 326     5712   8474   4399  -1245  -1204    529       C  
ATOM   1989  CD1 LEU A 326      63.986   6.595-196.619  1.00 48.99           C  
ANISOU 1989  CD1 LEU A 326     5718   8297   4600  -1101  -1081    497       C  
ATOM   1990  CD2 LEU A 326      62.113   5.379-197.745  1.00 51.93           C  
ANISOU 1990  CD2 LEU A 326     6030   8955   4746  -1429  -1334    539       C  
ATOM   1991  N   GLY A 327      61.751   9.647-201.174  1.00 59.47           N  
ANISOU 1991  N   GLY A 327     6848  10400   5349  -1088  -1363   1006       N  
ATOM   1992  CA  GLY A 327      61.026  10.831-201.610  1.00 54.38           C  
ANISOU 1992  CA  GLY A 327     6070   9932   4660   -980  -1406   1217       C  
ATOM   1993  C   GLY A 327      61.044  11.997-200.640  1.00 55.01           C  
ANISOU 1993  C   GLY A 327     6039   9952   4909   -756  -1294   1340       C  
ATOM   1994  O   GLY A 327      60.182  12.883-200.729  1.00 45.63           O  
ANISOU 1994  O   GLY A 327     4703   8916   3719   -659  -1334   1536       O  
ATOM   1995  N   LEU A 328      62.000  12.031-199.716  1.00 59.46           N  
ANISOU 1995  N   LEU A 328     6674  10299   5617   -669  -1154   1235       N  
ATOM   1996  CA  LEU A 328      62.055  13.106-198.738  1.00 58.12           C  
ANISOU 1996  CA  LEU A 328     6426  10056   5603   -472  -1042   1336       C  
ATOM   1997  C   LEU A 328      62.692  14.354-199.335  1.00 56.14           C  
ANISOU 1997  C   LEU A 328     6240   9772   5318   -328   -950   1404       C  
ATOM   1998  O   LEU A 328      63.605  14.281-200.162  1.00 54.62           O  
ANISOU 1998  O   LEU A 328     6195   9520   5037   -365   -913   1307       O  
ATOM   1999  CB  LEU A 328      62.839  12.663-197.501  1.00 49.10           C  
ANISOU 1999  CB  LEU A 328     5339   8699   4617   -448   -941   1201       C  
ATOM   2000  CG  LEU A 328      62.311  11.379-196.871  1.00 47.85           C  
ANISOU 2000  CG  LEU A 328     5142   8545   4494   -594  -1019   1124       C  
ATOM   2001  CD1 LEU A 328      63.233  10.878-195.771  1.00 41.91           C  
ANISOU 2001  CD1 LEU A 328     4475   7572   3878   -575   -923    981       C  
ATOM   2002  CD2 LEU A 328      60.902  11.607-196.342  1.00 54.82           C  
ANISOU 2002  CD2 LEU A 328     5824   9588   5418   -575  -1088   1292       C  
ATOM   2003  N   ARG A 329      62.197  15.512-198.900  1.00 50.81           N  
ANISOU 2003  N   ARG A 329     5460   9130   4715   -160   -901   1573       N  
ATOM   2004  CA  ARG A 329      62.748  16.803-199.287  1.00 56.57           C  
ANISOU 2004  CA  ARG A 329     6252   9807   5435     -8   -798   1653       C  
ATOM   2005  C   ARG A 329      62.659  17.740-198.087  1.00 53.88           C  
ANISOU 2005  C   ARG A 329     5850   9363   5258    168   -681   1739       C  
ATOM   2006  O   ARG A 329      61.935  17.468-197.129  1.00 53.02           O  
ANISOU 2006  O   ARG A 329     5625   9276   5245    180   -700   1774       O  
ATOM   2007  CB  ARG A 329      61.992  17.377-200.499  1.00 55.05           C  
ANISOU 2007  CB  ARG A 329     6009   9818   5089      8   -890   1820       C  
ATOM   2008  CG  ARG A 329      60.864  16.464-200.968  1.00 63.24           C  
ANISOU 2008  CG  ARG A 329     6933  11071   6026   -146  -1075   1858       C  
ATOM   2009  CD  ARG A 329      59.818  17.187-201.780  1.00 70.29           C  
ANISOU 2009  CD  ARG A 329     7710  12165   6830    -91  -1165   2065       C  
ATOM   2010  NE  ARG A 329      60.433  17.977-202.831  1.00 78.98           N  
ANISOU 2010  NE  ARG A 329     8940  13251   7819    -33  -1121   2098       N  
ATOM   2011  CZ  ARG A 329      59.818  18.952-203.484  1.00 84.63           C  
ANISOU 2011  CZ  ARG A 329     9606  14031   8518     71  -1124   2249       C  
ATOM   2012  NH1 ARG A 329      58.561  19.267-203.187  1.00 95.80           N  
ANISOU 2012  NH1 ARG A 329    10837  15538  10025    133  -1163   2383       N  
ATOM   2013  NH2 ARG A 329      60.470  19.624-204.415  1.00 71.91           N  
ANISOU 2013  NH2 ARG A 329     8131  12390   6801    114  -1078   2269       N  
ATOM   2014  N   TRP A 330      63.425  18.835-198.125  1.00 44.52           N  
ANISOU 2014  N   TRP A 330     4756   8058   4100    297   -553   1766       N  
ATOM   2015  CA  TRP A 330      63.200  19.951-197.212  1.00 39.73           C  
ANISOU 2015  CA  TRP A 330     4106   7374   3615    476   -444   1882       C  
ATOM   2016  C   TRP A 330      63.555  21.244-197.930  1.00 52.45           C  
ANISOU 2016  C   TRP A 330     5795   8960   5172    599   -363   1989       C  
ATOM   2017  O   TRP A 330      64.184  21.238-198.991  1.00 61.72           O  
ANISOU 2017  O   TRP A 330     7071  10146   6233    541   -373   1945       O  
ATOM   2018  CB  TRP A 330      63.984  19.829-195.884  1.00 43.87           C  
ANISOU 2018  CB  TRP A 330     4690   7688   4289    495   -335   1755       C  
ATOM   2019  CG  TRP A 330      63.293  20.582-194.788  1.00 47.02           C  
ANISOU 2019  CG  TRP A 330     5008   8055   4803    639   -264   1874       C  
ATOM   2020  CD1 TRP A 330      63.633  21.804-194.289  1.00 43.26           C  
ANISOU 2020  CD1 TRP A 330     4596   7447   4395    790   -126   1936       C  
ATOM   2021  CD2 TRP A 330      62.106  20.178-194.085  1.00 48.49           C  
ANISOU 2021  CD2 TRP A 330     5038   8343   5041    645   -320   1950       C  
ATOM   2022  NE1 TRP A 330      62.740  22.180-193.305  1.00 43.45           N  
ANISOU 2022  NE1 TRP A 330     4525   7477   4509    897    -84   2041       N  
ATOM   2023  CE2 TRP A 330      61.789  21.204-193.171  1.00 42.18           C  
ANISOU 2023  CE2 TRP A 330     4219   7466   4342    815   -200   2056       C  
ATOM   2024  CE3 TRP A 330      61.284  19.046-194.137  1.00 43.72           C  
ANISOU 2024  CE3 TRP A 330     4316   7888   4409    517   -452   1938       C  
ATOM   2025  CZ2 TRP A 330      60.690  21.132-192.317  1.00 43.47           C  
ANISOU 2025  CZ2 TRP A 330     4240   7697   4578    870   -200   2151       C  
ATOM   2026  CZ3 TRP A 330      60.193  18.981-193.295  1.00 49.37           C  
ANISOU 2026  CZ3 TRP A 330     4881   8678   5200    561   -461   2037       C  
ATOM   2027  CH2 TRP A 330      59.907  20.018-192.391  1.00 43.25           C  
ANISOU 2027  CH2 TRP A 330     4082   7825   4526    742   -331   2143       C  
ATOM   2028  N   TYR A 331      63.124  22.365-197.360  1.00 49.24           N  
ANISOU 2028  N   TYR A 331     5349   8515   4843    772   -276   2133       N  
ATOM   2029  CA  TYR A 331      63.345  23.640-198.022  1.00 52.62           C  
ANISOU 2029  CA  TYR A 331     5854   8917   5221    899   -197   2256       C  
ATOM   2030  C   TYR A 331      64.626  24.301-197.527  1.00 51.34           C  
ANISOU 2030  C   TYR A 331     5853   8518   5136    940    -36   2159       C  
ATOM   2031  O   TYR A 331      65.191  23.945-196.485  1.00 46.09           O  
ANISOU 2031  O   TYR A 331     5220   7712   4581    907     20   2028       O  
ATOM   2032  CB  TYR A 331      62.146  24.578-197.838  1.00 52.47           C  
ANISOU 2032  CB  TYR A 331     5716   8991   5231   1076   -186   2486       C  
ATOM   2033  CG  TYR A 331      61.640  24.694-196.421  1.00 63.46           C  
ANISOU 2033  CG  TYR A 331     7028  10310   6774   1165   -117   2508       C  
ATOM   2034  CD1 TYR A 331      62.151  25.657-195.559  1.00 56.97           C  
ANISOU 2034  CD1 TYR A 331     6309   9283   6054   1291     51   2508       C  
ATOM   2035  CD2 TYR A 331      60.636  23.855-195.949  1.00 58.47           C  
ANISOU 2035  CD2 TYR A 331     6226   9815   6176   1115   -214   2531       C  
ATOM   2036  CE1 TYR A 331      61.691  25.772-194.273  1.00 56.30           C  
ANISOU 2036  CE1 TYR A 331     6170   9127   6093   1369    122   2525       C  
ATOM   2037  CE2 TYR A 331      60.171  23.966-194.647  1.00 55.63           C  
ANISOU 2037  CE2 TYR A 331     5800   9388   5949   1197   -138   2552       C  
ATOM   2038  CZ  TYR A 331      60.706  24.929-193.818  1.00 57.79           C  
ANISOU 2038  CZ  TYR A 331     6189   9454   6313   1327     32   2548       C  
ATOM   2039  OH  TYR A 331      60.261  25.059-192.519  1.00 61.14           O  
ANISOU 2039  OH  TYR A 331     6570   9805   6857   1406    117   2564       O  
ATOM   2040  N   ALA A 332      65.096  25.264-198.319  1.00 50.75           N  
ANISOU 2040  N   ALA A 332     5883   8405   4994   1004     33   2227       N  
ATOM   2041  CA  ALA A 332      66.382  25.905-198.066  1.00 47.82           C  
ANISOU 2041  CA  ALA A 332     5671   7825   4674   1017    179   2137       C  
ATOM   2042  C   ALA A 332      66.305  26.934-196.938  1.00 43.80           C  
ANISOU 2042  C   ALA A 332     5190   7162   4291   1161    310   2203       C  
ATOM   2043  O   ALA A 332      67.240  27.052-196.143  1.00 46.83           O  
ANISOU 2043  O   ALA A 332     5663   7366   4764   1134    404   2082       O  
ATOM   2044  CB  ALA A 332      66.880  26.571-199.360  1.00 49.11           C  
ANISOU 2044  CB  ALA A 332     5943   8006   4712   1024    211   2193       C  
ATOM   2045  N   LEU A 333      65.210  27.687-196.844  1.00 48.72           N  
ANISOU 2045  N   LEU A 333     5742   7849   4921   1314    321   2394       N  
ATOM   2046  CA  LEU A 333      65.212  28.909-196.042  1.00 46.87           C  
ANISOU 2046  CA  LEU A 333     5583   7451   4776   1469    473   2475       C  
ATOM   2047  C   LEU A 333      64.385  28.773-194.772  1.00 51.80           C  
ANISOU 2047  C   LEU A 333     6108   8063   5513   1542    491   2503       C  
ATOM   2048  O   LEU A 333      63.152  28.642-194.856  1.00 52.03           O  
ANISOU 2048  O   LEU A 333     5983   8255   5532   1616    421   2641       O  
ATOM   2049  CB  LEU A 333      64.687  30.075-196.886  1.00 50.65           C  
ANISOU 2049  CB  LEU A 333     6087   7970   5187   1616    513   2676       C  
ATOM   2050  CG  LEU A 333      64.712  31.474-196.265  1.00 48.26           C  
ANISOU 2050  CG  LEU A 333     5888   7466   4982   1761    683   2723       C  
ATOM   2051  CD1 LEU A 333      66.149  31.939-196.153  1.00 54.07           C  
ANISOU 2051  CD1 LEU A 333     6826   8003   5715   1707    801   2631       C  
ATOM   2052  CD2 LEU A 333      63.887  32.476-197.099  1.00 46.97           C  
ANISOU 2052  CD2 LEU A 333     5697   7354   4795   1882    694   2865       C  
ATOM   2053  N   PRO A 334      65.007  28.824-193.575  1.00 44.58           N  
ANISOU 2053  N   PRO A 334     5273   6962   4702   1524    585   2384       N  
ATOM   2054  CA  PRO A 334      64.238  28.921-192.329  1.00 44.17           C  
ANISOU 2054  CA  PRO A 334     5161   6873   4750   1616    636   2426       C  
ATOM   2055  C   PRO A 334      63.914  30.378-192.032  1.00 52.81           C  
ANISOU 2055  C   PRO A 334     6341   7849   5877   1811    790   2574       C  
ATOM   2056  O   PRO A 334      64.799  31.177-191.714  1.00 45.44           O  
ANISOU 2056  O   PRO A 334     5583   6714   4967   1824    914   2522       O  
ATOM   2057  CB  PRO A 334      65.193  28.313-191.288  1.00 40.21           C  
ANISOU 2057  CB  PRO A 334     4734   6220   4323   1492    660   2222       C  
ATOM   2058  CG  PRO A 334      66.558  28.736-191.790  1.00 48.41           C  
ANISOU 2058  CG  PRO A 334     5932   7130   5332   1422    713   2129       C  
ATOM   2059  CD  PRO A 334      66.460  28.776-193.326  1.00 48.12           C  
ANISOU 2059  CD  PRO A 334     5869   7238   5177   1412    645   2207       C  
ATOM   2060  N   ALA A 335      62.642  30.740-192.184  1.00 51.86           N  
ANISOU 2060  N   ALA A 335     6089   7841   5772   1933    784   2712       N  
ATOM   2061  CA  ALA A 335      62.225  32.134-192.061  1.00 56.20           C  
ANISOU 2061  CA  ALA A 335     6702   8280   6369   2093    929   2795       C  
ATOM   2062  C   ALA A 335      61.031  32.188-191.117  1.00 56.73           C  
ANISOU 2062  C   ALA A 335     6646   8386   6523   2200    980   2860       C  
ATOM   2063  O   ALA A 335      59.893  31.961-191.532  1.00 58.36           O  
ANISOU 2063  O   ALA A 335     6667   8782   6723   2240    909   2963       O  
ATOM   2064  CB  ALA A 335      61.894  32.733-193.423  1.00 49.14           C  
ANISOU 2064  CB  ALA A 335     5784   7485   5403   2139    891   2899       C  
ATOM   2065  N   VAL A 336      61.295  32.504-189.859  1.00 56.91           N  
ANISOU 2065  N   VAL A 336     6774   8227   6620   2239   1109   2799       N  
ATOM   2066  CA  VAL A 336      60.256  32.499-188.837  1.00 51.45           C  
ANISOU 2066  CA  VAL A 336     5986   7557   6006   2332   1177   2847       C  
ATOM   2067  C   VAL A 336      59.461  33.789-188.930  1.00 55.73           C  
ANISOU 2067  C   VAL A 336     6537   8064   6573   2509   1315   2965       C  
ATOM   2068  O   VAL A 336      60.032  34.886-188.981  1.00 57.70           O  
ANISOU 2068  O   VAL A 336     6968   8136   6821   2567   1435   2949       O  
ATOM   2069  CB  VAL A 336      60.872  32.313-187.446  1.00 55.42           C  
ANISOU 2069  CB  VAL A 336     6618   7875   6563   2296   1262   2731       C  
ATOM   2070  CG1 VAL A 336      59.878  32.721-186.364  1.00 57.98           C  
ANISOU 2070  CG1 VAL A 336     6904   8164   6959   2424   1394   2786       C  
ATOM   2071  CG2 VAL A 336      61.259  30.872-187.296  1.00 50.87           C  
ANISOU 2071  CG2 VAL A 336     5969   7389   5970   2142   1113   2651       C  
ATOM   2072  N   SER A 337      58.134  33.659-188.949  1.00 51.38           N  
ANISOU 2072  N   SER A 337     5790   7685   6045   2588   1299   3085       N  
ATOM   2073  CA  SER A 337      57.261  34.770-189.296  1.00 50.78           C  
ANISOU 2073  CA  SER A 337     5684   7631   5980   2753   1401   3224       C  
ATOM   2074  C   SER A 337      56.149  35.003-188.283  1.00 55.38           C  
ANISOU 2074  C   SER A 337     6183   8228   6633   2874   1526   3301       C  
ATOM   2075  O   SER A 337      55.241  35.794-188.555  1.00 65.57           O  
ANISOU 2075  O   SER A 337     7410   9571   7933   3015   1604   3438       O  
ATOM   2076  CB  SER A 337      56.661  34.545-190.690  1.00 62.73           C  
ANISOU 2076  CB  SER A 337     7032   9373   7431   2737   1251   3335       C  
ATOM   2077  OG  SER A 337      56.143  33.228-190.808  1.00 62.68           O  
ANISOU 2077  OG  SER A 337     6826   9579   7412   2618   1084   3334       O  
ATOM   2078  N   ASN A 338      56.190  34.356-187.120  1.00 66.13           N  
ANISOU 2078  N   ASN A 338     7547   9540   8039   2828   1555   3224       N  
ATOM   2079  CA  ASN A 338      55.147  34.557-186.122  1.00 68.37           C  
ANISOU 2079  CA  ASN A 338     7763   9833   8381   2938   1685   3299       C  
ATOM   2080  C   ASN A 338      55.658  35.214-184.846  1.00 65.19           C  
ANISOU 2080  C   ASN A 338     7585   9172   8014   2994   1880   3211       C  
ATOM   2081  O   ASN A 338      54.932  35.230-183.846  1.00 62.32           O  
ANISOU 2081  O   ASN A 338     7193   8794   7692   3063   1991   3247       O  
ATOM   2082  CB  ASN A 338      54.461  33.230-185.776  1.00 72.82           C  
ANISOU 2082  CB  ASN A 338     8115  10586   8967   2845   1564   3311       C  
ATOM   2083  CG  ASN A 338      55.417  32.215-185.185  1.00 67.30           C  
ANISOU 2083  CG  ASN A 338     7485   9815   8270   2694   1484   3153       C  
ATOM   2084  OD1 ASN A 338      56.602  32.488-184.999  1.00 69.24           O  
ANISOU 2084  OD1 ASN A 338     7936   9870   8502   2654   1518   3036       O  
ATOM   2085  ND2 ASN A 338      54.903  31.031-184.885  1.00 72.43           N  
ANISOU 2085  ND2 ASN A 338     7965  10619   8938   2602   1375   3152       N  
ATOM   2086  N   MET A 339      56.879  35.739-184.835  1.00 59.54           N  
ANISOU 2086  N   MET A 339     7097   8249   7275   2954   1922   3095       N  
ATOM   2087  CA  MET A 339      57.419  36.324-183.616  1.00 60.41           C  
ANISOU 2087  CA  MET A 339     7435   8111   7408   2977   2093   2994       C  
ATOM   2088  C   MET A 339      57.354  37.843-183.666  1.00 65.77           C  
ANISOU 2088  C   MET A 339     8277   8637   8077   3117   2276   3039       C  
ATOM   2089  O   MET A 339      57.299  38.462-184.735  1.00 64.10           O  
ANISOU 2089  O   MET A 339     8049   8468   7838   3171   2257   3115       O  
ATOM   2090  CB  MET A 339      58.858  35.867-183.365  1.00 61.22           C  
ANISOU 2090  CB  MET A 339     7700   8067   7494   2816   2024   2821       C  
ATOM   2091  CG  MET A 339      58.969  34.423-182.881  1.00 53.30           C  
ANISOU 2091  CG  MET A 339     6590   7155   6507   2689   1889   2758       C  
ATOM   2092  SD  MET A 339      60.640  33.966-182.374  1.00 58.12           S  
ANISOU 2092  SD  MET A 339     7412   7571   7099   2508   1836   2563       S  
ATOM   2093  CE  MET A 339      60.733  34.732-180.753  1.00 58.66           C  
ANISOU 2093  CE  MET A 339     7705   7388   7194   2561   2047   2485       C  
ATOM   2094  N   LEU A 340      57.349  38.437-182.478  1.00 65.73           N  
ANISOU 2094  N   LEU A 340     8437   8448   8087   3174   2458   2992       N  
ATOM   2095  CA  LEU A 340      57.165  39.872-182.306  1.00 62.94           C  
ANISOU 2095  CA  LEU A 340     8252   7941   7722   3312   2659   3034       C  
ATOM   2096  C   LEU A 340      58.510  40.501-181.977  1.00 60.39           C  
ANISOU 2096  C   LEU A 340     8215   7358   7370   3226   2719   2873       C  
ATOM   2097  O   LEU A 340      59.173  40.094-181.018  1.00 59.34           O  
ANISOU 2097  O   LEU A 340     8203   7104   7241   3119   2726   2736       O  
ATOM   2098  CB  LEU A 340      56.143  40.155-181.205  1.00 60.59           C  
ANISOU 2098  CB  LEU A 340     7954   7622   7448   3434   2834   3103       C  
ATOM   2099  CG  LEU A 340      55.714  41.607-180.980  1.00 68.92           C  
ANISOU 2099  CG  LEU A 340     9162   8537   8486   3599   3058   3175       C  
ATOM   2100  CD1 LEU A 340      54.252  41.657-180.559  1.00 65.35           C  
ANISOU 2100  CD1 LEU A 340     8561   8208   8063   3746   3159   3342       C  
ATOM   2101  CD2 LEU A 340      56.596  42.295-179.942  1.00 63.85           C  
ANISOU 2101  CD2 LEU A 340     8835   7612   7814   3556   3210   3021       C  
ATOM   2102  N   LEU A 341      58.905  41.490-182.771  1.00 56.55           N  
ANISOU 2102  N   LEU A 341     7838   6792   6856   3265   2759   2892       N  
ATOM   2103  CA  LEU A 341      60.144  42.221-182.554  1.00 63.03           C  
ANISOU 2103  CA  LEU A 341     8931   7369   7647   3180   2821   2753       C  
ATOM   2104  C   LEU A 341      59.872  43.441-181.688  1.00 63.51           C  
ANISOU 2104  C   LEU A 341     9198   7239   7694   3291   3056   2750       C  
ATOM   2105  O   LEU A 341      59.012  44.271-182.016  1.00 61.23           O  
ANISOU 2105  O   LEU A 341     8885   6978   7403   3458   3170   2885       O  
ATOM   2106  CB  LEU A 341      60.759  42.653-183.887  1.00 61.81           C  
ANISOU 2106  CB  LEU A 341     8799   7221   7465   3151   2743   2776       C  
ATOM   2107  CG  LEU A 341      61.948  43.617-183.825  1.00 56.44           C  
ANISOU 2107  CG  LEU A 341     8397   6296   6752   3075   2822   2662       C  
ATOM   2108  CD1 LEU A 341      63.142  42.982-183.122  1.00 55.07           C  
ANISOU 2108  CD1 LEU A 341     8338   6010   6577   2872   2753   2483       C  
ATOM   2109  CD2 LEU A 341      62.330  44.099-185.246  1.00 57.08           C  
ANISOU 2109  CD2 LEU A 341     8476   6406   6803   3076   2760   2724       C  
ATOM   2110  N   GLU A 342      60.619  43.565-180.597  1.00 61.77           N  
ANISOU 2110  N   GLU A 342     9189   6823   7457   3192   3126   2598       N  
ATOM   2111  CA  GLU A 342      60.435  44.662-179.654  1.00 65.71           C  
ANISOU 2111  CA  GLU A 342     9913   7129   7925   3271   3350   2574       C  
ATOM   2112  C   GLU A 342      61.726  45.462-179.576  1.00 56.52           C  
ANISOU 2112  C   GLU A 342     9024   5733   6717   3149   3386   2430       C  
ATOM   2113  O   GLU A 342      62.780  44.915-179.237  1.00 56.69           O  
ANISOU 2113  O   GLU A 342     9121   5686   6732   2964   3282   2284       O  
ATOM   2114  CB  GLU A 342      60.023  44.134-178.274  1.00 79.08           C  
ANISOU 2114  CB  GLU A 342    11627   8799   9622   3261   3419   2528       C  
ATOM   2115  CG  GLU A 342      59.677  45.220-177.263  1.00 93.18           C  
ANISOU 2115  CG  GLU A 342    13640  10402  11362   3352   3663   2521       C  
ATOM   2116  CD  GLU A 342      60.894  45.723-176.509  1.00 99.12           C  
ANISOU 2116  CD  GLU A 342    14695  10908  12057   3199   3710   2330       C  
ATOM   2117  OE1 GLU A 342      61.800  44.906-176.234  1.00 95.68           O  
ANISOU 2117  OE1 GLU A 342    14274  10455  11627   3020   3565   2195       O  
ATOM   2118  OE2 GLU A 342      60.947  46.933-176.200  1.00 99.68           O  
ANISOU 2118  OE2 GLU A 342    14992  10806  12075   3253   3887   2318       O  
ATOM   2119  N   ILE A 343      61.646  46.750-179.898  1.00 60.65           N  
ANISOU 2119  N   ILE A 343     9694   6141   7209   3247   3529   2478       N  
ATOM   2120  CA  ILE A 343      62.795  47.650-179.876  1.00 68.19           C  
ANISOU 2120  CA  ILE A 343    10916   6875   8118   3137   3578   2358       C  
ATOM   2121  C   ILE A 343      62.382  48.944-179.187  1.00 79.52           C  
ANISOU 2121  C   ILE A 343    12576   8135   9505   3253   3821   2373       C  
ATOM   2122  O   ILE A 343      61.469  49.636-179.657  1.00 76.05           O  
ANISOU 2122  O   ILE A 343    12091   7737   9068   3443   3932   2524       O  
ATOM   2123  CB  ILE A 343      63.327  47.967-181.284  1.00 67.82           C  
ANISOU 2123  CB  ILE A 343    10837   6859   8073   3115   3486   2402       C  
ATOM   2124  CG1 ILE A 343      63.705  46.702-182.057  1.00 61.64           C  
ANISOU 2124  CG1 ILE A 343     9838   6257   7324   3005   3253   2401       C  
ATOM   2125  CG2 ILE A 343      64.519  48.888-181.175  1.00 64.18           C  
ANISOU 2125  CG2 ILE A 343    10655   6167   7565   2986   3544   2279       C  
ATOM   2126  CD1 ILE A 343      64.064  46.987-183.507  1.00 55.46           C  
ANISOU 2126  CD1 ILE A 343     9009   5529   6533   3002   3171   2470       C  
ATOM   2127  N   GLY A 344      63.074  49.288-178.103  1.00 69.95           N  
ANISOU 2127  N   GLY A 344    11610   6727   8241   3133   3901   2222       N  
ATOM   2128  CA  GLY A 344      62.872  50.556-177.429  1.00 69.96           C  
ANISOU 2128  CA  GLY A 344    11869   6536   8177   3209   4131   2214       C  
ATOM   2129  C   GLY A 344      61.439  50.840-177.024  1.00 67.75           C  
ANISOU 2129  C   GLY A 344    11528   6315   7899   3432   4303   2364       C  
ATOM   2130  O   GLY A 344      61.007  51.994-177.033  1.00 69.27           O  
ANISOU 2130  O   GLY A 344    11863   6401   8055   3566   4490   2436       O  
ATOM   2131  N   GLY A 345      60.689  49.802-176.670  1.00 68.16           N  
ANISOU 2131  N   GLY A 345    11367   6535   7995   3472   4246   2419       N  
ATOM   2132  CA  GLY A 345      59.294  49.955-176.319  1.00 73.59           C  
ANISOU 2132  CA  GLY A 345    11962   7304   8694   3674   4394   2581       C  
ATOM   2133  C   GLY A 345      58.330  49.856-177.484  1.00 80.26           C  
ANISOU 2133  C   GLY A 345    12533   8360   9600   3843   4344   2782       C  
ATOM   2134  O   GLY A 345      57.114  49.797-177.257  1.00 81.24           O  
ANISOU 2134  O   GLY A 345    12526   8592   9748   4001   4433   2934       O  
ATOM   2135  N   LEU A 346      58.826  49.838-178.718  1.00 63.52           N  
ANISOU 2135  N   LEU A 346    10326   6304   7503   3809   4201   2796       N  
ATOM   2136  CA  LEU A 346      57.979  49.676-179.889  1.00 71.93           C  
ANISOU 2136  CA  LEU A 346    11130   7584   8617   3947   4124   2981       C  
ATOM   2137  C   LEU A 346      57.845  48.199-180.228  1.00 68.24           C  
ANISOU 2137  C   LEU A 346    10377   7348   8201   3865   3901   2991       C  
ATOM   2138  O   LEU A 346      58.738  47.397-179.946  1.00 65.83           O  
ANISOU 2138  O   LEU A 346    10092   7022   7897   3684   3771   2843       O  
ATOM   2139  CB  LEU A 346      58.553  50.441-181.081  1.00 67.71           C  
ANISOU 2139  CB  LEU A 346    10661   6998   8068   3953   4089   3000       C  
ATOM   2140  CG  LEU A 346      58.792  51.926-180.799  1.00 75.04           C  
ANISOU 2140  CG  LEU A 346    11890   7681   8940   4019   4304   2980       C  
ATOM   2141  CD1 LEU A 346      59.422  52.626-182.007  1.00 73.54           C  
ANISOU 2141  CD1 LEU A 346    11768   7438   8737   4009   4257   2997       C  
ATOM   2142  CD2 LEU A 346      57.492  52.616-180.383  1.00 76.58           C  
ANISOU 2142  CD2 LEU A 346    12082   7882   9133   4246   4513   3140       C  
ATOM   2143  N   GLU A 347      56.719  47.843-180.838  1.00 70.05           N  
ANISOU 2143  N   GLU A 347    10342   7802   8471   3994   3853   3171       N  
ATOM   2144  CA  GLU A 347      56.384  46.445-181.076  1.00 71.80           C  
ANISOU 2144  CA  GLU A 347    10286   8258   8737   3928   3658   3199       C  
ATOM   2145  C   GLU A 347      56.066  46.223-182.547  1.00 75.84           C  
ANISOU 2145  C   GLU A 347    10575   8974   9265   3967   3500   3325       C  
ATOM   2146  O   GLU A 347      55.222  46.921-183.121  1.00 71.52           O  
ANISOU 2146  O   GLU A 347     9959   8492   8722   4132   3571   3488       O  
ATOM   2147  CB  GLU A 347      55.210  46.009-180.194  1.00 71.31           C  
ANISOU 2147  CB  GLU A 347    10096   8295   8702   4017   3738   3294       C  
ATOM   2148  CG  GLU A 347      55.560  45.968-178.713  1.00 75.12           C  
ANISOU 2148  CG  GLU A 347    10784   8598   9161   3947   3860   3161       C  
ATOM   2149  CD  GLU A 347      54.389  45.556-177.838  1.00 88.67           C  
ANISOU 2149  CD  GLU A 347    12387  10403  10903   4035   3946   3266       C  
ATOM   2150  OE1 GLU A 347      53.231  45.764-178.262  1.00 87.71           O  
ANISOU 2150  OE1 GLU A 347    12089  10426  10811   4193   3986   3456       O  
ATOM   2151  OE2 GLU A 347      54.631  45.023-176.730  1.00 90.99           O  
ANISOU 2151  OE2 GLU A 347    12766  10620  11185   3944   3970   3162       O  
ATOM   2152  N   PHE A 348      56.746  45.248-183.151  1.00 59.23           N  
ANISOU 2152  N   PHE A 348     8366   6970   7167   3812   3286   3252       N  
ATOM   2153  CA  PHE A 348      56.554  44.887-184.552  1.00 68.83           C  
ANISOU 2153  CA  PHE A 348     9382   8386   8384   3813   3112   3353       C  
ATOM   2154  C   PHE A 348      56.062  43.445-184.610  1.00 64.96           C  
ANISOU 2154  C   PHE A 348     8624   8135   7923   3738   2934   3380       C  
ATOM   2155  O   PHE A 348      56.870  42.508-184.682  1.00 66.02           O  
ANISOU 2155  O   PHE A 348     8740   8292   8053   3571   2782   3262       O  
ATOM   2156  CB  PHE A 348      57.852  45.082-185.338  1.00 67.72           C  
ANISOU 2156  CB  PHE A 348     9378   8143   8209   3689   3021   3249       C  
ATOM   2157  CG  PHE A 348      58.445  46.473-185.199  1.00 68.53           C  
ANISOU 2157  CG  PHE A 348     9765   7992   8281   3733   3193   3203       C  
ATOM   2158  CD1 PHE A 348      59.271  46.794-184.124  1.00 59.60           C  
ANISOU 2158  CD1 PHE A 348     8879   6630   7137   3644   3300   3041       C  
ATOM   2159  CD2 PHE A 348      58.178  47.458-186.144  1.00 74.97           C  
ANISOU 2159  CD2 PHE A 348    10609   8800   9077   3855   3244   3322       C  
ATOM   2160  CE1 PHE A 348      59.814  48.070-183.990  1.00 61.31           C  
ANISOU 2160  CE1 PHE A 348     9363   6615   7318   3668   3454   2994       C  
ATOM   2161  CE2 PHE A 348      58.725  48.743-186.023  1.00 71.40           C  
ANISOU 2161  CE2 PHE A 348    10427   8109   8594   3890   3405   3280       C  
ATOM   2162  CZ  PHE A 348      59.535  49.054-184.944  1.00 61.91           C  
ANISOU 2162  CZ  PHE A 348     9466   6680   7376   3793   3512   3114       C  
ATOM   2163  N   PRO A 349      54.743  43.219-184.566  1.00 68.26           N  
ANISOU 2163  N   PRO A 349     8832   8734   8369   3852   2948   3535       N  
ATOM   2164  CA  PRO A 349      54.221  41.845-184.669  1.00 64.57           C  
ANISOU 2164  CA  PRO A 349     8104   8506   7926   3769   2771   3566       C  
ATOM   2165  C   PRO A 349      54.458  41.187-186.025  1.00 70.65           C  
ANISOU 2165  C   PRO A 349     8716   9457   8670   3675   2543   3589       C  
ATOM   2166  O   PRO A 349      54.245  39.972-186.150  1.00 64.95           O  
ANISOU 2166  O   PRO A 349     7806   8915   7956   3569   2378   3582       O  
ATOM   2167  CB  PRO A 349      52.718  42.015-184.389  1.00 67.78           C  
ANISOU 2167  CB  PRO A 349     8341   9048   8366   3925   2861   3747       C  
ATOM   2168  CG  PRO A 349      52.427  43.437-184.656  1.00 80.01           C  
ANISOU 2168  CG  PRO A 349    10011  10489   9902   4099   3031   3844       C  
ATOM   2169  CD  PRO A 349      53.674  44.208-184.346  1.00 80.32           C  
ANISOU 2169  CD  PRO A 349    10360  10249   9908   4055   3133   3688       C  
ATOM   2170  N   ALA A 350      54.886  41.940-187.035  1.00 66.68           N  
ANISOU 2170  N   ALA A 350     8295   8911   8131   3706   2530   3616       N  
ATOM   2171  CA  ALA A 350      55.215  41.399-188.351  1.00 66.48           C  
ANISOU 2171  CA  ALA A 350     8160   9035   8065   3611   2323   3631       C  
ATOM   2172  C   ALA A 350      56.645  41.824-188.673  1.00 62.23           C  
ANISOU 2172  C   ALA A 350     7856   8300   7488   3518   2323   3499       C  
ATOM   2173  O   ALA A 350      56.884  42.963-189.084  1.00 64.76           O  
ANISOU 2173  O   ALA A 350     8325   8492   7787   3602   2423   3532       O  
ATOM   2174  CB  ALA A 350      54.231  41.884-189.407  1.00 61.94           C  
ANISOU 2174  CB  ALA A 350     7435   8627   7474   3738   2292   3823       C  
ATOM   2175  N   ALA A 351      57.592  40.915-188.466  1.00 59.32           N  
ANISOU 2175  N   ALA A 351     7523   7904   7112   3343   2214   3353       N  
ATOM   2176  CA  ALA A 351      59.014  41.160-188.687  1.00 65.26           C  
ANISOU 2176  CA  ALA A 351     8486   8477   7831   3226   2204   3220       C  
ATOM   2177  C   ALA A 351      59.715  39.833-188.960  1.00 58.81           C  
ANISOU 2177  C   ALA A 351     7593   7759   6993   3039   2013   3125       C  
ATOM   2178  O   ALA A 351      60.438  39.319-188.096  1.00 53.64           O  
ANISOU 2178  O   ALA A 351     7024   6999   6358   2930   2014   2990       O  
ATOM   2179  CB  ALA A 351      59.640  41.871-187.483  1.00 57.71           C  
ANISOU 2179  CB  ALA A 351     7775   7253   6900   3227   2382   3101       C  
ATOM   2180  N   PRO A 352      59.511  39.238-190.137  1.00 54.56           N  
ANISOU 2180  N   PRO A 352     6900   7423   6409   2994   1846   3193       N  
ATOM   2181  CA  PRO A 352      60.074  37.906-190.398  1.00 55.03           C  
ANISOU 2181  CA  PRO A 352     6878   7592   6438   2819   1668   3110       C  
ATOM   2182  C   PRO A 352      61.584  37.979-190.578  1.00 57.49           C  
ANISOU 2182  C   PRO A 352     7389   7740   6715   2686   1662   2978       C  
ATOM   2183  O   PRO A 352      62.092  38.825-191.317  1.00 54.90           O  
ANISOU 2183  O   PRO A 352     7185   7327   6348   2701   1703   2996       O  
ATOM   2184  CB  PRO A 352      59.371  37.478-191.692  1.00 56.53           C  
ANISOU 2184  CB  PRO A 352     6874   8032   6571   2819   1512   3229       C  
ATOM   2185  CG  PRO A 352      59.107  38.783-192.397  1.00 57.63           C  
ANISOU 2185  CG  PRO A 352     7086   8120   6691   2955   1603   3339       C  
ATOM   2186  CD  PRO A 352      58.738  39.745-191.292  1.00 56.75           C  
ANISOU 2186  CD  PRO A 352     7074   7840   6650   3097   1811   3351       C  
ATOM   2187  N   PHE A 353      62.301  37.076-189.911  1.00 53.89           N  
ANISOU 2187  N   PHE A 353     6961   7245   6272   2551   1611   2852       N  
ATOM   2188  CA  PHE A 353      63.751  36.992-190.021  1.00 55.11           C  
ANISOU 2188  CA  PHE A 353     7281   7263   6395   2406   1599   2727       C  
ATOM   2189  C   PHE A 353      64.174  35.605-190.494  1.00 55.02           C  
ANISOU 2189  C   PHE A 353     7162   7405   6337   2255   1426   2678       C  
ATOM   2190  O   PHE A 353      63.481  34.610-190.262  1.00 51.16           O  
ANISOU 2190  O   PHE A 353     6503   7076   5859   2241   1329   2697       O  
ATOM   2191  CB  PHE A 353      64.431  37.326-188.693  1.00 51.55           C  
ANISOU 2191  CB  PHE A 353     7007   6581   5997   2370   1721   2605       C  
ATOM   2192  CG  PHE A 353      63.930  36.509-187.524  1.00 58.58           C  
ANISOU 2192  CG  PHE A 353     7813   7505   6940   2365   1709   2569       C  
ATOM   2193  CD1 PHE A 353      64.479  35.264-187.239  1.00 52.16           C  
ANISOU 2193  CD1 PHE A 353     6953   6745   6122   2222   1594   2483       C  
ATOM   2194  CD2 PHE A 353      62.917  36.988-186.710  1.00 64.79           C  
ANISOU 2194  CD2 PHE A 353     8575   8268   7776   2505   1823   2625       C  
ATOM   2195  CE1 PHE A 353      64.026  34.510-186.156  1.00 57.34           C  
ANISOU 2195  CE1 PHE A 353     7539   7424   6822   2215   1583   2453       C  
ATOM   2196  CE2 PHE A 353      62.460  36.238-185.630  1.00 65.19           C  
ANISOU 2196  CE2 PHE A 353     8554   8347   7869   2497   1820   2595       C  
ATOM   2197  CZ  PHE A 353      63.017  34.999-185.355  1.00 54.35           C  
ANISOU 2197  CZ  PHE A 353     7137   7021   6492   2351   1695   2509       C  
ATOM   2198  N   SER A 354      65.315  35.544-191.178  1.00 52.05           N  
ANISOU 2198  N   SER A 354     6889   6984   5904   2138   1395   2616       N  
ATOM   2199  CA  SER A 354      65.778  34.289-191.738  1.00 45.42           C  
ANISOU 2199  CA  SER A 354     5967   6289   5003   1998   1248   2569       C  
ATOM   2200  C   SER A 354      67.291  34.190-191.622  1.00 48.28           C  
ANISOU 2200  C   SER A 354     6488   6509   5349   1856   1283   2444       C  
ATOM   2201  O   SER A 354      67.998  35.197-191.552  1.00 47.31           O  
ANISOU 2201  O   SER A 354     6533   6203   5239   1855   1399   2413       O  
ATOM   2202  CB  SER A 354      65.341  34.135-193.193  1.00 50.03           C  
ANISOU 2202  CB  SER A 354     6447   7066   5497   2004   1140   2663       C  
ATOM   2203  OG  SER A 354      65.886  35.174-193.987  1.00 54.04           O  
ANISOU 2203  OG  SER A 354     7092   7477   5964   2025   1213   2690       O  
ATOM   2204  N   GLY A 355      67.770  32.954-191.569  1.00 50.71           N  
ANISOU 2204  N   GLY A 355     6721   6900   5648   1709   1173   2325       N  
ATOM   2205  CA  GLY A 355      69.187  32.660-191.571  1.00 48.53           C  
ANISOU 2205  CA  GLY A 355     6533   6528   5378   1539   1173   2151       C  
ATOM   2206  C   GLY A 355      69.447  31.477-192.470  1.00 50.35           C  
ANISOU 2206  C   GLY A 355     6649   6929   5552   1412   1030   2074       C  
ATOM   2207  O   GLY A 355      69.000  31.460-193.622  1.00 45.34           O  
ANISOU 2207  O   GLY A 355     5963   6437   4829   1444    975   2172       O  
ATOM   2208  N   TRP A 356      70.176  30.487-191.964  1.00 42.59           N  
ANISOU 2208  N   TRP A 356     5637   5930   4614   1270    971   1901       N  
ATOM   2209  CA  TRP A 356      70.302  29.205-192.636  1.00 45.92           C  
ANISOU 2209  CA  TRP A 356     5950   6505   4992   1157    838   1817       C  
ATOM   2210  C   TRP A 356      70.159  28.118-191.583  1.00 45.33           C  
ANISOU 2210  C   TRP A 356     5793   6439   4992   1092    766   1707       C  
ATOM   2211  O   TRP A 356      70.268  28.375-190.380  1.00 39.20           O  
ANISOU 2211  O   TRP A 356     5064   5536   4297   1111    824   1671       O  
ATOM   2212  CB  TRP A 356      71.627  29.064-193.410  1.00 43.75           C  
ANISOU 2212  CB  TRP A 356     5745   6196   4682   1036    851   1709       C  
ATOM   2213  CG  TRP A 356      72.853  29.386-192.628  1.00 44.68           C  
ANISOU 2213  CG  TRP A 356     5963   6132   4880    964    934   1591       C  
ATOM   2214  CD1 TRP A 356      73.508  28.565-191.747  1.00 44.70           C  
ANISOU 2214  CD1 TRP A 356     5939   6083   4962    865    896   1442       C  
ATOM   2215  CD2 TRP A 356      73.586  30.616-192.653  1.00 43.20           C  
ANISOU 2215  CD2 TRP A 356     5920   5794   4700    976   1064   1618       C  
ATOM   2216  NE1 TRP A 356      74.601  29.217-191.219  1.00 42.15           N  
ANISOU 2216  NE1 TRP A 356     5722   5597   4694    813    985   1376       N  
ATOM   2217  CE2 TRP A 356      74.674  30.474-191.766  1.00 43.39           C  
ANISOU 2217  CE2 TRP A 356     5988   5690   4809    871   1091   1478       C  
ATOM   2218  CE3 TRP A 356      73.428  31.823-193.337  1.00 44.65           C  
ANISOU 2218  CE3 TRP A 356     6203   5936   4826   1061   1158   1751       C  
ATOM   2219  CZ2 TRP A 356      75.594  31.497-191.542  1.00 44.39           C  
ANISOU 2219  CZ2 TRP A 356     6250   5655   4962    835   1204   1463       C  
ATOM   2220  CZ3 TRP A 356      74.352  32.838-193.126  1.00 50.08           C  
ANISOU 2220  CZ3 TRP A 356     7038   6450   5540   1029   1282   1733       C  
ATOM   2221  CH2 TRP A 356      75.416  32.669-192.232  1.00 47.07           C  
ANISOU 2221  CH2 TRP A 356     6693   5948   5242    910   1302   1588       C  
ATOM   2222  N   TYR A 357      69.884  26.900-192.048  1.00 42.18           N  
ANISOU 2222  N   TYR A 357     5282   6188   4556   1013    639   1657       N  
ATOM   2223  CA  TYR A 357      69.581  25.801-191.142  1.00 42.62           C  
ANISOU 2223  CA  TYR A 357     5253   6269   4671    956    563   1572       C  
ATOM   2224  C   TYR A 357      70.838  25.248-190.486  1.00 40.33           C  
ANISOU 2224  C   TYR A 357     5019   5855   4448    843    569   1396       C  
ATOM   2225  O   TYR A 357      71.925  25.237-191.069  1.00 37.73           O  
ANISOU 2225  O   TYR A 357     4747   5486   4103    772    588   1317       O  
ATOM   2226  CB  TYR A 357      68.879  24.662-191.883  1.00 45.20           C  
ANISOU 2226  CB  TYR A 357     5455   6787   4931    895    425   1573       C  
ATOM   2227  CG  TYR A 357      67.362  24.700-191.864  1.00 48.25           C  
ANISOU 2227  CG  TYR A 357     5720   7315   5298    983    376   1723       C  
ATOM   2228  CD1 TYR A 357      66.656  24.456-190.696  1.00 44.41           C  
ANISOU 2228  CD1 TYR A 357     5170   6814   4889   1018    379   1738       C  
ATOM   2229  CD2 TYR A 357      66.633  24.958-193.032  1.00 43.15           C  
ANISOU 2229  CD2 TYR A 357     5017   6827   4552   1026    325   1856       C  
ATOM   2230  CE1 TYR A 357      65.272  24.469-190.674  1.00 40.12           C  
ANISOU 2230  CE1 TYR A 357     4496   6411   4337   1097    340   1880       C  
ATOM   2231  CE2 TYR A 357      65.247  24.968-193.013  1.00 47.18           C  
ANISOU 2231  CE2 TYR A 357     5391   7483   5051   1104    271   2002       C  
ATOM   2232  CZ  TYR A 357      64.575  24.717-191.828  1.00 45.34           C  
ANISOU 2232  CZ  TYR A 357     5085   7236   4909   1140    283   2013       C  
ATOM   2233  OH  TYR A 357      63.203  24.716-191.784  1.00 44.65           O  
ANISOU 2233  OH  TYR A 357     4844   7301   4819   1217    238   2163       O  
ATOM   2234  N   MET A 358      70.675  24.789-189.246  1.00 37.59           N  
ANISOU 2234  N   MET A 358     4652   5452   4178    829    554   1342       N  
ATOM   2235  CA  MET A 358      71.559  23.788-188.668  1.00 37.07           C  
ANISOU 2235  CA  MET A 358     4588   5329   4167    714    505   1184       C  
ATOM   2236  C   MET A 358      70.967  22.414-188.968  1.00 40.09           C  
ANISOU 2236  C   MET A 358     4862   5848   4523    651    382   1147       C  
ATOM   2237  O   MET A 358      69.753  22.216-188.852  1.00 40.04           O  
ANISOU 2237  O   MET A 358     4773   5942   4500    694    340   1234       O  
ATOM   2238  CB  MET A 358      71.705  23.992-187.157  1.00 36.03           C  
ANISOU 2238  CB  MET A 358     4507   5062   4120    724    548   1147       C  
ATOM   2239  CG  MET A 358      72.733  23.059-186.541  1.00 36.45           C  
ANISOU 2239  CG  MET A 358     4569   5048   4231    613    497    994       C  
ATOM   2240  SD  MET A 358      73.130  23.483-184.831  1.00 43.88           S  
ANISOU 2240  SD  MET A 358     5601   5818   5252    610    548    951       S  
ATOM   2241  CE  MET A 358      71.562  23.173-184.024  1.00 39.27           C  
ANISOU 2241  CE  MET A 358     4957   5294   4670    683    532   1034       C  
ATOM   2242  N   SER A 359      71.818  21.474-189.386  1.00 34.22           N  
ANISOU 2242  N   SER A 359     4118   5109   3775    547    330   1022       N  
ATOM   2243  CA  SER A 359      71.300  20.240-189.977  1.00 37.58           C  
ANISOU 2243  CA  SER A 359     4467   5663   4149    478    221    988       C  
ATOM   2244  C   SER A 359      70.437  19.425-189.014  1.00 37.93           C  
ANISOU 2244  C   SER A 359     4442   5734   4236    461    155    986       C  
ATOM   2245  O   SER A 359      69.494  18.755-189.458  1.00 36.82           O  
ANISOU 2245  O   SER A 359     4222   5726   4043    430     73   1023       O  
ATOM   2246  CB  SER A 359      72.442  19.384-190.521  1.00 39.00           C  
ANISOU 2246  CB  SER A 359     4679   5817   4324    381    198    847       C  
ATOM   2247  OG  SER A 359      73.453  19.172-189.568  1.00 37.21           O  
ANISOU 2247  OG  SER A 359     4489   5455   4194    353    225    746       O  
ATOM   2248  N   THR A 360      70.715  19.462-187.702  1.00 34.03           N  
ANISOU 2248  N   THR A 360     3979   5121   3831    471    187    947       N  
ATOM   2249  CA  THR A 360      69.871  18.689-186.792  1.00 32.50           C  
ANISOU 2249  CA  THR A 360     3725   4952   3670    452    133    950       C  
ATOM   2250  C   THR A 360      68.431  19.177-186.787  1.00 35.95           C  
ANISOU 2250  C   THR A 360     4082   5498   4079    532    140   1100       C  
ATOM   2251  O   THR A 360      67.521  18.389-186.514  1.00 34.67           O  
ANISOU 2251  O   THR A 360     3835   5421   3916    498     74   1121       O  
ATOM   2252  CB  THR A 360      70.411  18.726-185.350  1.00 34.20           C  
ANISOU 2252  CB  THR A 360     4003   5019   3972    452    171    890       C  
ATOM   2253  OG1 THR A 360      70.636  20.085-184.947  1.00 38.18           O  
ANISOU 2253  OG1 THR A 360     4580   5432   4496    536    276    948       O  
ATOM   2254  CG2 THR A 360      71.692  17.940-185.251  1.00 33.11           C  
ANISOU 2254  CG2 THR A 360     3909   4799   3872    366    136    748       C  
ATOM   2255  N   GLU A 361      68.201  20.470-187.043  1.00 41.97           N  
ANISOU 2255  N   GLU A 361     4868   6255   4825    642    224   1211       N  
ATOM   2256  CA  GLU A 361      66.826  20.961-187.076  1.00 42.59           C  
ANISOU 2256  CA  GLU A 361     4855   6443   4883    738    236   1368       C  
ATOM   2257  C   GLU A 361      65.999  20.177-188.081  1.00 41.31           C  
ANISOU 2257  C   GLU A 361     4573   6476   4648    682    120   1411       C  
ATOM   2258  O   GLU A 361      64.843  19.828-187.810  1.00 42.20           O  
ANISOU 2258  O   GLU A 361     4570   6698   4764    692     78   1491       O  
ATOM   2259  CB  GLU A 361      66.774  22.446-187.434  1.00 45.78           C  
ANISOU 2259  CB  GLU A 361     5312   6812   5269    870    341   1485       C  
ATOM   2260  CG  GLU A 361      67.476  23.396-186.500  1.00 44.62           C  
ANISOU 2260  CG  GLU A 361     5298   6474   5181    926    465   1459       C  
ATOM   2261  CD  GLU A 361      67.298  24.841-186.964  1.00 53.11           C  
ANISOU 2261  CD  GLU A 361     6431   7517   6230   1057    571   1587       C  
ATOM   2262  OE1 GLU A 361      66.213  25.407-186.725  1.00 54.14           O  
ANISOU 2262  OE1 GLU A 361     6513   7692   6367   1181    620   1724       O  
ATOM   2263  OE2 GLU A 361      68.235  25.392-187.588  1.00 50.85           O  
ANISOU 2263  OE2 GLU A 361     6239   7165   5918   1039    608   1556       O  
ATOM   2264  N   ILE A 362      66.579  19.899-189.248  1.00 42.40           N  
ANISOU 2264  N   ILE A 362     4737   6659   4714    615     70   1360       N  
ATOM   2265  CA  ILE A 362      65.875  19.160-190.287  1.00 38.80           C  
ANISOU 2265  CA  ILE A 362     4191   6384   4168    542    -46   1390       C  
ATOM   2266  C   ILE A 362      65.926  17.670-190.007  1.00 35.77           C  
ANISOU 2266  C   ILE A 362     3786   6010   3795    399   -139   1265       C  
ATOM   2267  O   ILE A 362      64.892  16.998-189.939  1.00 43.35           O  
ANISOU 2267  O   ILE A 362     4641   7091   4738    349   -220   1309       O  
ATOM   2268  CB  ILE A 362      66.477  19.470-191.671  1.00 39.23           C  
ANISOU 2268  CB  ILE A 362     4305   6476   4126    524    -53   1384       C  
ATOM   2269  CG1 ILE A 362      66.637  20.976-191.872  1.00 42.60           C  
ANISOU 2269  CG1 ILE A 362     4785   6851   4550    661     55   1495       C  
ATOM   2270  CG2 ILE A 362      65.614  18.848-192.754  1.00 38.83           C  
ANISOU 2270  CG2 ILE A 362     4166   6623   3962    452   -177   1436       C  
ATOM   2271  CD1 ILE A 362      67.455  21.365-193.108  1.00 42.55           C  
ANISOU 2271  CD1 ILE A 362     4865   6845   4457    642     75   1475       C  
ATOM   2272  N   GLY A 363      67.138  17.136-189.857  1.00 39.67           N  
ANISOU 2272  N   GLY A 363     4378   6377   4317    332   -125   1112       N  
ATOM   2273  CA  GLY A 363      67.309  15.694-189.829  1.00 42.58           C  
ANISOU 2273  CA  GLY A 363     4750   6747   4681    200   -210    988       C  
ATOM   2274  C   GLY A 363      66.835  15.071-188.534  1.00 43.12           C  
ANISOU 2274  C   GLY A 363     4781   6773   4830    177   -226    972       C  
ATOM   2275  O   GLY A 363      66.310  13.957-188.528  1.00 45.36           O  
ANISOU 2275  O   GLY A 363     5023   7117   5095     75   -312    935       O  
ATOM   2276  N   THR A 364      67.014  15.770-187.422  1.00 35.66           N  
ANISOU 2276  N   THR A 364     3863   5720   3968    263   -143    997       N  
ATOM   2277  CA  THR A 364      66.620  15.160-186.160  1.00 34.96           C  
ANISOU 2277  CA  THR A 364     3754   5582   3947    238   -153    977       C  
ATOM   2278  C   THR A 364      65.213  15.572-185.729  1.00 36.51           C  
ANISOU 2278  C   THR A 364     3841   5883   4150    300   -139   1122       C  
ATOM   2279  O   THR A 364      64.379  14.714-185.435  1.00 42.26           O  
ANISOU 2279  O   THR A 364     4492   6688   4879    229   -201   1135       O  
ATOM   2280  CB  THR A 364      67.633  15.502-185.068  1.00 37.05           C  
ANISOU 2280  CB  THR A 364     4120   5665   4292    275    -79    907       C  
ATOM   2281  OG1 THR A 364      68.950  15.140-185.506  1.00 33.05           O  
ANISOU 2281  OG1 THR A 364     3692   5077   3789    225    -90    784       O  
ATOM   2282  CG2 THR A 364      67.292  14.735-183.812  1.00 34.61           C  
ANISOU 2282  CG2 THR A 364     3806   5305   4038    235    -98    878       C  
ATOM   2283  N   ARG A 365      64.918  16.872-185.718  1.00 34.03           N  
ANISOU 2283  N   ARG A 365     3516   5574   3840    432    -52   1237       N  
ATOM   2284  CA  ARG A 365      63.629  17.328-185.204  1.00 41.24           C  
ANISOU 2284  CA  ARG A 365     4325   6572   4774    517    -16   1380       C  
ATOM   2285  C   ARG A 365      62.514  17.216-186.249  1.00 42.11           C  
ANISOU 2285  C   ARG A 365     4287   6897   4816    507    -95   1498       C  
ATOM   2286  O   ARG A 365      61.492  16.562-186.011  1.00 42.14           O  
ANISOU 2286  O   ARG A 365     4170   7016   4825    456   -152   1549       O  
ATOM   2287  CB  ARG A 365      63.759  18.763-184.690  1.00 42.46           C  
ANISOU 2287  CB  ARG A 365     4542   6625   4964    673    122   1456       C  
ATOM   2288  CG  ARG A 365      64.831  18.963-183.604  1.00 33.12           C  
ANISOU 2288  CG  ARG A 365     3509   5236   3840    672    196   1347       C  
ATOM   2289  CD  ARG A 365      64.637  18.039-182.347  1.00 34.16           C  
ANISOU 2289  CD  ARG A 365     3641   5315   4021    605    178   1285       C  
ATOM   2290  NE  ARG A 365      63.260  18.106-181.850  1.00 34.70           N  
ANISOU 2290  NE  ARG A 365     3599   5481   4105    661    209   1407       N  
ATOM   2291  CZ  ARG A 365      62.769  19.127-181.152  1.00 40.02           C  
ANISOU 2291  CZ  ARG A 365     4290   6108   4807    794    334   1501       C  
ATOM   2292  NH1 ARG A 365      63.554  20.148-180.834  1.00 38.04           N  
ANISOU 2292  NH1 ARG A 365     4179   5706   4567    868    431   1479       N  
ATOM   2293  NH2 ARG A 365      61.500  19.124-180.770  1.00 45.72           N  
ANISOU 2293  NH2 ARG A 365     4891   6933   5546    848    366   1616       N  
ATOM   2294  N   ASN A 366      62.685  17.846-187.420  1.00 39.01           N  
ANISOU 2294  N   ASN A 366     3900   6566   4356    547   -106   1548       N  
ATOM   2295  CA  ASN A 366      61.583  17.890-188.380  1.00 40.05           C  
ANISOU 2295  CA  ASN A 366     3889   6911   4417    552   -185   1683       C  
ATOM   2296  C   ASN A 366      61.281  16.504-188.937  1.00 42.31           C  
ANISOU 2296  C   ASN A 366     4116   7315   4643    370   -331   1614       C  
ATOM   2297  O   ASN A 366      60.114  16.141-189.109  1.00 46.59           O  
ANISOU 2297  O   ASN A 366     4509   8031   5164    332   -408   1711       O  
ATOM   2298  CB  ASN A 366      61.896  18.882-189.507  1.00 45.88           C  
ANISOU 2298  CB  ASN A 366     4668   7680   5086    634   -164   1754       C  
ATOM   2299  CG  ASN A 366      62.148  20.296-188.990  1.00 43.38           C  
ANISOU 2299  CG  ASN A 366     4422   7237   4824    809    -13   1829       C  
ATOM   2300  OD1 ASN A 366      61.821  20.618-187.846  1.00 45.34           O  
ANISOU 2300  OD1 ASN A 366     4664   7409   5154    887     73   1860       O  
ATOM   2301  ND2 ASN A 366      62.739  21.137-189.825  1.00 40.63           N  
ANISOU 2301  ND2 ASN A 366     4156   6856   4425    867     26   1855       N  
ATOM   2302  N   LEU A 367      62.308  15.693-189.174  1.00 39.42           N  
ANISOU 2302  N   LEU A 367     3867   6856   4256    254   -367   1447       N  
ATOM   2303  CA  LEU A 367      62.068  14.403-189.808  1.00 48.92           C  
ANISOU 2303  CA  LEU A 367     5044   8154   5388     80   -497   1374       C  
ATOM   2304  C   LEU A 367      61.894  13.254-188.820  1.00 43.63           C  
ANISOU 2304  C   LEU A 367     4368   7430   4778    -25   -527   1289       C  
ATOM   2305  O   LEU A 367      61.212  12.275-189.153  1.00 40.29           O  
ANISOU 2305  O   LEU A 367     3881   7121   4308   -163   -633   1280       O  
ATOM   2306  CB  LEU A 367      63.203  14.076-190.788  1.00 43.62           C  
ANISOU 2306  CB  LEU A 367     4505   7424   4644     11   -519   1245       C  
ATOM   2307  CG  LEU A 367      63.278  14.983-192.023  1.00 45.07           C  
ANISOU 2307  CG  LEU A 367     4697   7693   4733     72   -516   1326       C  
ATOM   2308  CD1 LEU A 367      64.513  14.668-192.848  1.00 43.99           C  
ANISOU 2308  CD1 LEU A 367     4703   7474   4536     10   -508   1187       C  
ATOM   2309  CD2 LEU A 367      62.016  14.857-192.881  1.00 43.58           C  
ANISOU 2309  CD2 LEU A 367     4376   7738   4447     23   -634   1453       C  
ATOM   2310  N   CYS A 368      62.463  13.338-187.606  1.00 38.88           N  
ANISOU 2310  N   CYS A 368     3838   6660   4275     27   -440   1231       N  
ATOM   2311  CA  CYS A 368      62.435  12.204-186.684  1.00 39.00           C  
ANISOU 2311  CA  CYS A 368     3872   6605   4340    -75   -467   1143       C  
ATOM   2312  C   CYS A 368      61.605  12.400-185.419  1.00 38.02           C  
ANISOU 2312  C   CYS A 368     3672   6480   4294    -21   -411   1228       C  
ATOM   2313  O   CYS A 368      61.403  11.417-184.689  1.00 38.90           O  
ANISOU 2313  O   CYS A 368     3787   6555   4436   -117   -441   1174       O  
ATOM   2314  CB  CYS A 368      63.858  11.820-186.251  1.00 44.49           C  
ANISOU 2314  CB  CYS A 368     4726   7099   5078    -92   -431    985       C  
ATOM   2315  SG  CYS A 368      64.938  11.308-187.585  1.00 46.14           S  
ANISOU 2315  SG  CYS A 368     5038   7285   5210   -170   -480    856       S  
ATOM   2316  N   ASP A 369      61.140  13.608-185.112  1.00 41.09           N  
ANISOU 2316  N   ASP A 369     4004   6895   4712    130   -322   1357       N  
ATOM   2317  CA  ASP A 369      60.256  13.747-183.956  1.00 38.89           C  
ANISOU 2317  CA  ASP A 369     3648   6627   4500    182   -259   1442       C  
ATOM   2318  C   ASP A 369      59.027  12.862-184.147  1.00 43.77           C  
ANISOU 2318  C   ASP A 369     4109   7425   5096     66   -353   1505       C  
ATOM   2319  O   ASP A 369      58.485  12.780-185.262  1.00 40.48           O  
ANISOU 2319  O   ASP A 369     3593   7177   4610     19   -444   1566       O  
ATOM   2320  CB  ASP A 369      59.789  15.189-183.756  1.00 38.48           C  
ANISOU 2320  CB  ASP A 369     3548   6595   4475    371   -144   1588       C  
ATOM   2321  CG  ASP A 369      60.742  16.027-182.913  1.00 44.46           C  
ANISOU 2321  CG  ASP A 369     4463   7147   5282    477    -19   1536       C  
ATOM   2322  OD1 ASP A 369      61.820  15.532-182.509  1.00 45.81           O  
ANISOU 2322  OD1 ASP A 369     4768   7170   5469    409    -29   1392       O  
ATOM   2323  OD2 ASP A 369      60.396  17.203-182.654  1.00 42.91           O  
ANISOU 2323  OD2 ASP A 369     4257   6938   5109    631     91   1645       O  
ATOM   2324  N   PRO A 370      58.553  12.205-183.090  1.00 41.37           N  
ANISOU 2324  N   PRO A 370     3780   7096   4844     10   -336   1497       N  
ATOM   2325  CA  PRO A 370      57.377  11.335-183.230  1.00 35.85           C  
ANISOU 2325  CA  PRO A 370     2927   6568   4128   -119   -423   1557       C  
ATOM   2326  C   PRO A 370      56.143  12.087-183.655  1.00 41.71           C  
ANISOU 2326  C   PRO A 370     3465   7519   4864    -34   -417   1747       C  
ATOM   2327  O   PRO A 370      55.231  11.490-184.238  1.00 45.28           O  
ANISOU 2327  O   PRO A 370     3770   8158   5276   -150   -524   1808       O  
ATOM   2328  CB  PRO A 370      57.210  10.724-181.820  1.00 36.69           C  
ANISOU 2328  CB  PRO A 370     3066   6574   4301   -160   -366   1521       C  
ATOM   2329  CG  PRO A 370      58.452  11.067-181.071  1.00 43.12           C  
ANISOU 2329  CG  PRO A 370     4071   7160   5152    -82   -283   1415       C  
ATOM   2330  CD  PRO A 370      59.033  12.290-181.700  1.00 39.29           C  
ANISOU 2330  CD  PRO A 370     3626   6651   4651     61   -234   1442       C  
ATOM   2331  N   HIS A 371      56.084  13.386-183.377  1.00 38.21           N  
ANISOU 2331  N   HIS A 371     3011   7049   4459    166   -297   1847       N  
ATOM   2332  CA  HIS A 371      54.946  14.215-183.733  1.00 44.31           C  
ANISOU 2332  CA  HIS A 371     3591   8007   5238    285   -273   2044       C  
ATOM   2333  C   HIS A 371      55.230  15.101-184.940  1.00 41.07           C  
ANISOU 2333  C   HIS A 371     3185   7653   4765    377   -300   2101       C  
ATOM   2334  O   HIS A 371      54.454  16.017-185.219  1.00 47.15           O  
ANISOU 2334  O   HIS A 371     3824   8545   5546    521   -260   2272       O  
ATOM   2335  CB  HIS A 371      54.521  15.070-182.537  1.00 45.19           C  
ANISOU 2335  CB  HIS A 371     3682   8051   5436    459    -99   2135       C  
ATOM   2336  CG  HIS A 371      55.618  15.921-181.977  1.00 48.23           C  
ANISOU 2336  CG  HIS A 371     4274   8204   5845    585     26   2059       C  
ATOM   2337  ND1 HIS A 371      56.745  15.394-181.381  1.00 48.47           N  
ANISOU 2337  ND1 HIS A 371     4496   8039   5881    504     29   1885       N  
ATOM   2338  CD2 HIS A 371      55.744  17.266-181.896  1.00 49.93           C  
ANISOU 2338  CD2 HIS A 371     4537   8354   6082    782    152   2139       C  
ATOM   2339  CE1 HIS A 371      57.525  16.377-180.970  1.00 45.22           C  
ANISOU 2339  CE1 HIS A 371     4232   7461   5490    633    143   1859       C  
ATOM   2340  NE2 HIS A 371      56.940  17.524-181.270  1.00 46.45           N  
ANISOU 2340  NE2 HIS A 371     4313   7683   5653    799    223   2006       N  
ATOM   2341  N   ARG A 372      56.331  14.866-185.636  1.00 45.90           N  
ANISOU 2341  N   ARG A 372     3949   8175   5318    307   -358   1968       N  
ATOM   2342  CA  ARG A 372      56.615  15.513-186.914  1.00 50.80           C  
ANISOU 2342  CA  ARG A 372     4582   8861   5859    356   -402   2010       C  
ATOM   2343  C   ARG A 372      56.543  14.444-188.008  1.00 47.05           C  
ANISOU 2343  C   ARG A 372     4080   8514   5283    157   -574   1948       C  
ATOM   2344  O   ARG A 372      55.592  13.657-187.992  1.00 43.50           O  
ANISOU 2344  O   ARG A 372     3490   8213   4824     37   -663   1991       O  
ATOM   2345  CB  ARG A 372      57.934  16.270-186.828  1.00 46.70           C  
ANISOU 2345  CB  ARG A 372     4263   8132   5351    452   -303   1920       C  
ATOM   2346  CG  ARG A 372      57.946  17.372-185.779  1.00 44.85           C  
ANISOU 2346  CG  ARG A 372     4068   7770   5201    638   -134   1984       C  
ATOM   2347  CD  ARG A 372      56.923  18.467-186.040  1.00 47.26           C  
ANISOU 2347  CD  ARG A 372     4236   8205   5516    812    -78   2194       C  
ATOM   2348  NE  ARG A 372      57.195  19.193-187.283  1.00 45.54           N  
ANISOU 2348  NE  ARG A 372     4039   8041   5224    872   -109   2253       N  
ATOM   2349  CZ  ARG A 372      58.201  20.049-187.447  1.00 49.21           C  
ANISOU 2349  CZ  ARG A 372     4669   8348   5680    956    -25   2209       C  
ATOM   2350  NH1 ARG A 372      59.052  20.285-186.459  1.00 44.36           N  
ANISOU 2350  NH1 ARG A 372     4211   7518   5126    983     85   2102       N  
ATOM   2351  NH2 ARG A 372      58.379  20.659-188.616  1.00 50.78           N  
ANISOU 2351  NH2 ARG A 372     4883   8607   5804   1001    -56   2272       N  
ATOM   2352  N   TYR A 373      57.499  14.368-188.938  1.00 47.53           N  
ANISOU 2352  N   TYR A 373     4274   8521   5265    107   -619   1847       N  
ATOM   2353  CA  TYR A 373      57.374  13.384-190.008  1.00 49.96           C  
ANISOU 2353  CA  TYR A 373     4570   8951   5462    -81   -774   1790       C  
ATOM   2354  C   TYR A 373      57.614  11.961-189.523  1.00 48.79           C  
ANISOU 2354  C   TYR A 373     4487   8724   5325   -267   -826   1633       C  
ATOM   2355  O   TYR A 373      57.205  11.020-190.210  1.00 47.61           O  
ANISOU 2355  O   TYR A 373     4306   8690   5094   -444   -955   1601       O  
ATOM   2356  CB  TYR A 373      58.321  13.731-191.154  1.00 47.07           C  
ANISOU 2356  CB  TYR A 373     4336   8546   5001    -74   -790   1729       C  
ATOM   2357  CG  TYR A 373      57.755  14.767-192.080  1.00 51.85           C  
ANISOU 2357  CG  TYR A 373     4847   9311   5541     35   -812   1902       C  
ATOM   2358  CD1 TYR A 373      57.831  16.117-191.774  1.00 50.48           C  
ANISOU 2358  CD1 TYR A 373     4673   9081   5426    248   -687   2013       C  
ATOM   2359  CD2 TYR A 373      57.121  14.393-193.264  1.00 57.16           C  
ANISOU 2359  CD2 TYR A 373     5440  10190   6087    -79   -961   1959       C  
ATOM   2360  CE1 TYR A 373      57.301  17.070-192.636  1.00 51.54           C  
ANISOU 2360  CE1 TYR A 373     4727   9356   5500    358   -705   2183       C  
ATOM   2361  CE2 TYR A 373      56.595  15.328-194.120  1.00 52.74           C  
ANISOU 2361  CE2 TYR A 373     4793   9784   5461     23   -992   2128       C  
ATOM   2362  CZ  TYR A 373      56.686  16.663-193.805  1.00 53.60           C  
ANISOU 2362  CZ  TYR A 373     4900   9829   5636    248   -862   2243       C  
ATOM   2363  OH  TYR A 373      56.150  17.587-194.673  1.00 54.59           O  
ANISOU 2363  OH  TYR A 373     4967  10062   5713    348   -868   2391       O  
ATOM   2364  N   ASN A 374      58.243  11.781-188.350  1.00 43.68           N  
ANISOU 2364  N   ASN A 374     3939   7884   4774   -235   -731   1540       N  
ATOM   2365  CA  ASN A 374      58.340  10.481-187.685  1.00 44.11           C  
ANISOU 2365  CA  ASN A 374     4045   7858   4857   -388   -766   1418       C  
ATOM   2366  C   ASN A 374      58.839   9.371-188.622  1.00 49.41           C  
ANISOU 2366  C   ASN A 374     4818   8522   5432   -569   -876   1278       C  
ATOM   2367  O   ASN A 374      58.248   8.290-188.713  1.00 51.33           O  
ANISOU 2367  O   ASN A 374     5026   8835   5641   -742   -970   1248       O  
ATOM   2368  CB  ASN A 374      56.987  10.109-187.061  1.00 47.09           C  
ANISOU 2368  CB  ASN A 374     4248   8373   5273   -443   -794   1528       C  
ATOM   2369  CG  ASN A 374      57.056   8.845-186.215  1.00 44.76           C  
ANISOU 2369  CG  ASN A 374     4014   7977   5015   -589   -811   1415       C  
ATOM   2370  OD1 ASN A 374      58.118   8.473-185.715  1.00 38.41           O  
ANISOU 2370  OD1 ASN A 374     3379   6973   4244   -592   -767   1277       O  
ATOM   2371  ND2 ASN A 374      55.925   8.164-186.078  1.00 44.15           N  
ANISOU 2371  ND2 ASN A 374     3799   8043   4934   -717   -879   1480       N  
ATOM   2372  N   ILE A 375      59.963   9.630-189.307  1.00 49.53           N  
ANISOU 2372  N   ILE A 375     4973   8442   5405   -533   -853   1187       N  
ATOM   2373  CA  ILE A 375      60.450   8.711-190.338  1.00 50.07           C  
ANISOU 2373  CA  ILE A 375     5147   8507   5369   -684   -939   1060       C  
ATOM   2374  C   ILE A 375      61.447   7.692-189.809  1.00 46.23           C  
ANISOU 2374  C   ILE A 375     4822   7818   4926   -754   -913    881       C  
ATOM   2375  O   ILE A 375      61.913   6.837-190.574  1.00 35.38           O  
ANISOU 2375  O   ILE A 375     3556   6412   3474   -874   -966    762       O  
ATOM   2376  CB  ILE A 375      61.118   9.456-191.519  1.00 42.78           C  
ANISOU 2376  CB  ILE A 375     4290   7604   4361   -619   -927   1058       C  
ATOM   2377  CG1 ILE A 375      62.521   9.921-191.124  1.00 45.80           C  
ANISOU 2377  CG1 ILE A 375     4811   7780   4813   -502   -807    963       C  
ATOM   2378  CG2 ILE A 375      60.304  10.646-191.935  1.00 47.58           C  
ANISOU 2378  CG2 ILE A 375     4757   8379   4942   -505   -931   1245       C  
ATOM   2379  CD1 ILE A 375      63.263  10.637-192.228  1.00 53.08           C  
ANISOU 2379  CD1 ILE A 375     5806   8705   5658   -443   -778    954       C  
ATOM   2380  N   LEU A 376      61.772   7.731-188.517  1.00 37.52           N  
ANISOU 2380  N   LEU A 376     3742   6574   3939   -682   -833    861       N  
ATOM   2381  CA  LEU A 376      62.937   7.006-188.031  1.00 37.24           C  
ANISOU 2381  CA  LEU A 376     3863   6334   3953   -702   -796    705       C  
ATOM   2382  C   LEU A 376      62.804   5.499-188.237  1.00 38.42           C  
ANISOU 2382  C   LEU A 376     4081   6460   4058   -888   -878    598       C  
ATOM   2383  O   LEU A 376      63.766   4.830-188.627  1.00 35.94           O  
ANISOU 2383  O   LEU A 376     3908   6026   3723   -929   -875    462       O  
ATOM   2384  CB  LEU A 376      63.135   7.328-186.548  1.00 37.78           C  
ANISOU 2384  CB  LEU A 376     3933   6279   4141   -603   -711    724       C  
ATOM   2385  CG  LEU A 376      64.449   7.089-185.834  1.00 46.85           C  
ANISOU 2385  CG  LEU A 376     5220   7217   5364   -556   -651    605       C  
ATOM   2386  CD1 LEU A 376      65.534   8.001-186.381  1.00 41.30           C  
ANISOU 2386  CD1 LEU A 376     4575   6459   4659   -446   -590    578       C  
ATOM   2387  CD2 LEU A 376      64.211   7.337-184.327  1.00 39.70           C  
ANISOU 2387  CD2 LEU A 376     4293   6238   4552   -492   -593    654       C  
ATOM   2388  N   GLU A 377      61.637   4.934-187.948  1.00 33.49           N  
ANISOU 2388  N   GLU A 377     3363   5940   3424  -1001   -943    658       N  
ATOM   2389  CA  GLU A 377      61.507   3.496-188.141  1.00 44.79           C  
ANISOU 2389  CA  GLU A 377     4876   7335   4809  -1191  -1018    554       C  
ATOM   2390  C   GLU A 377      61.542   3.124-189.630  1.00 43.82           C  
ANISOU 2390  C   GLU A 377     4808   7295   4546  -1306  -1098    497       C  
ATOM   2391  O   GLU A 377      62.114   2.093-190.002  1.00 43.43           O  
ANISOU 2391  O   GLU A 377     4912   7136   4454  -1411  -1117    357       O  
ATOM   2392  CB  GLU A 377      60.222   2.992-187.489  1.00 49.26           C  
ANISOU 2392  CB  GLU A 377     5323   8000   5394  -1303  -1068    637       C  
ATOM   2393  CG  GLU A 377      60.120   1.488-187.437  1.00 64.83           C  
ANISOU 2393  CG  GLU A 377     7398   9897   7336  -1501  -1130    528       C  
ATOM   2394  CD  GLU A 377      59.025   1.024-186.502  1.00 82.24           C  
ANISOU 2394  CD  GLU A 377     9499  12159   9589  -1594  -1149    606       C  
ATOM   2395  OE1 GLU A 377      58.935  -0.197-186.255  1.00 87.33           O  
ANISOU 2395  OE1 GLU A 377    10237  12719  10225  -1751  -1185    524       O  
ATOM   2396  OE2 GLU A 377      58.262   1.888-186.015  1.00 88.68           O  
ANISOU 2396  OE2 GLU A 377    10145  13098  10453  -1505  -1119    751       O  
ATOM   2397  N   ASP A 378      60.962   3.944-190.497  1.00 42.64           N  
ANISOU 2397  N   ASP A 378     4550   7332   4321  -1283  -1140    604       N  
ATOM   2398  CA  ASP A 378      61.007   3.615-191.921  1.00 39.00           C  
ANISOU 2398  CA  ASP A 378     4156   6953   3711  -1397  -1218    551       C  
ATOM   2399  C   ASP A 378      62.444   3.542-192.420  1.00 44.18           C  
ANISOU 2399  C   ASP A 378     4996   7442   4349  -1337  -1145    409       C  
ATOM   2400  O   ASP A 378      62.801   2.630-193.173  1.00 50.78           O  
ANISOU 2400  O   ASP A 378     5972   8230   5094  -1464  -1179    284       O  
ATOM   2401  CB  ASP A 378      60.188   4.628-192.703  1.00 41.74           C  
ANISOU 2401  CB  ASP A 378     4350   7527   3983  -1357  -1273    709       C  
ATOM   2402  CG  ASP A 378      58.722   4.518-192.398  1.00 55.75           C  
ANISOU 2402  CG  ASP A 378     5932   9489   5760  -1445  -1360    845       C  
ATOM   2403  OD1 ASP A 378      58.173   3.401-192.533  1.00 63.78           O  
ANISOU 2403  OD1 ASP A 378     6966  10544   6723  -1650  -1452    794       O  
ATOM   2404  OD2 ASP A 378      58.120   5.535-192.004  1.00 66.25           O  
ANISOU 2404  OD2 ASP A 378     7097  10925   7150  -1311  -1330   1004       O  
ATOM   2405  N   VAL A 379      63.299   4.455-191.959  1.00 42.65           N  
ANISOU 2405  N   VAL A 379     4809   7150   4245  -1151  -1038    421       N  
ATOM   2406  CA  VAL A 379      64.693   4.442-192.390  1.00 40.58           C  
ANISOU 2406  CA  VAL A 379     4698   6739   3980  -1088   -960    297       C  
ATOM   2407  C   VAL A 379      65.418   3.236-191.821  1.00 43.51           C  
ANISOU 2407  C   VAL A 379     5205   6917   4410  -1142   -934    148       C  
ATOM   2408  O   VAL A 379      66.262   2.627-192.493  1.00 38.03           O  
ANISOU 2408  O   VAL A 379     4654   6128   3666  -1177   -909     20       O  
ATOM   2409  CB  VAL A 379      65.377   5.766-192.003  1.00 40.37           C  
ANISOU 2409  CB  VAL A 379     4633   6667   4038   -889   -857    358       C  
ATOM   2410  CG1 VAL A 379      66.894   5.682-192.200  1.00 42.16           C  
ANISOU 2410  CG1 VAL A 379     4999   6726   4295   -824   -768    229       C  
ATOM   2411  CG2 VAL A 379      64.790   6.899-192.823  1.00 41.33           C  
ANISOU 2411  CG2 VAL A 379     4658   6964   4081   -835   -878    493       C  
ATOM   2412  N   ALA A 380      65.095   2.860-190.578  1.00 39.64           N  
ANISOU 2412  N   ALA A 380     4677   6362   4022  -1145   -932    168       N  
ATOM   2413  CA  ALA A 380      65.757   1.719-189.961  1.00 41.41           C  
ANISOU 2413  CA  ALA A 380     5031   6397   4306  -1186   -909     42       C  
ATOM   2414  C   ALA A 380      65.387   0.419-190.668  1.00 39.84           C  
ANISOU 2414  C   ALA A 380     4936   6197   4004  -1380   -982    -51       C  
ATOM   2415  O   ALA A 380      66.242  -0.453-190.842  1.00 40.96           O  
ANISOU 2415  O   ALA A 380     5235   6182   4145  -1403   -948   -186       O  
ATOM   2416  CB  ALA A 380      65.410   1.662-188.468  1.00 37.17           C  
ANISOU 2416  CB  ALA A 380     4433   5801   3888  -1151   -895     99       C  
ATOM   2417  N   VAL A 381      64.125   0.270-191.087  1.00 38.65           N  
ANISOU 2417  N   VAL A 381     4701   6219   3764  -1521  -1081     20       N  
ATOM   2418  CA  VAL A 381      63.735  -0.902-191.869  1.00 48.49           C  
ANISOU 2418  CA  VAL A 381     6056   7477   4891  -1729  -1159    -69       C  
ATOM   2419  C   VAL A 381      64.576  -0.982-193.136  1.00 51.94           C  
ANISOU 2419  C   VAL A 381     6636   7879   5220  -1731  -1132   -177       C  
ATOM   2420  O   VAL A 381      65.125  -2.037-193.474  1.00 46.90           O  
ANISOU 2420  O   VAL A 381     6179   7100   4542  -1813  -1114   -320       O  
ATOM   2421  CB  VAL A 381      62.226  -0.858-192.189  1.00 45.01           C  
ANISOU 2421  CB  VAL A 381     5471   7265   4367  -1880  -1280     45       C  
ATOM   2422  CG1 VAL A 381      61.842  -1.962-193.167  1.00 43.81           C  
ANISOU 2422  CG1 VAL A 381     5440   7141   4065  -2114  -1371    -49       C  
ATOM   2423  CG2 VAL A 381      61.419  -0.975-190.904  1.00 46.10           C  
ANISOU 2423  CG2 VAL A 381     5485   7419   4613  -1894  -1290    136       C  
ATOM   2424  N   CYS A 382      64.729   0.149-193.829  1.00 50.38           N  
ANISOU 2424  N   CYS A 382     6369   7795   4977  -1631  -1116   -109       N  
ATOM   2425  CA  CYS A 382      65.537   0.181-195.042  1.00 53.58           C  
ANISOU 2425  CA  CYS A 382     6907   8176   5276  -1625  -1078   -201       C  
ATOM   2426  C   CYS A 382      66.991  -0.173-194.767  1.00 54.89           C  
ANISOU 2426  C   CYS A 382     7213   8116   5529  -1514   -953   -332       C  
ATOM   2427  O   CYS A 382      67.661  -0.752-195.628  1.00 55.34           O  
ANISOU 2427  O   CYS A 382     7430   8093   5503  -1555   -914   -457       O  
ATOM   2428  CB  CYS A 382      65.440   1.555-195.703  1.00 49.32           C  
ANISOU 2428  CB  CYS A 382     6260   7794   4686  -1522  -1074    -86       C  
ATOM   2429  SG  CYS A 382      63.802   1.988-196.311  1.00 51.29           S  
ANISOU 2429  SG  CYS A 382     6347   8332   4810  -1644  -1227     75       S  
ATOM   2430  N   MET A 383      67.502   0.160-193.588  1.00 50.06           N  
ANISOU 2430  N   MET A 383     6542   7398   5079  -1373   -888   -304       N  
ATOM   2431  CA  MET A 383      68.884  -0.172-193.283  1.00 42.18           C  
ANISOU 2431  CA  MET A 383     5654   6200   4173  -1265   -781   -414       C  
ATOM   2432  C   MET A 383      69.035  -1.578-192.738  1.00 44.23           C  
ANISOU 2432  C   MET A 383     6039   6294   4473  -1343   -784   -519       C  
ATOM   2433  O   MET A 383      70.151  -1.957-192.371  1.00 49.92           O  
ANISOU 2433  O   MET A 383     6842   6842   5283  -1247   -701   -602       O  
ATOM   2434  CB  MET A 383      69.472   0.820-192.270  1.00 35.08           C  
ANISOU 2434  CB  MET A 383     4648   5256   3423  -1083   -716   -341       C  
ATOM   2435  CG  MET A 383      69.487   2.259-192.744  1.00 39.76           C  
ANISOU 2435  CG  MET A 383     5139   5977   3990   -986   -690   -241       C  
ATOM   2436  SD  MET A 383      69.893   3.384-191.379  1.00 42.45           S  
ANISOU 2436  SD  MET A 383     5362   6268   4498   -810   -630   -146       S  
ATOM   2437  CE  MET A 383      71.605   2.937-191.104  1.00 36.72           C  
ANISOU 2437  CE  MET A 383     4743   5335   3873   -717   -530   -276       C  
ATOM   2438  N   ASP A 384      67.940  -2.336-192.667  1.00 43.24           N  
ANISOU 2438  N   ASP A 384     5923   6219   4287  -1514   -878   -510       N  
ATOM   2439  CA  ASP A 384      67.934  -3.710-192.181  1.00 47.45           C  
ANISOU 2439  CA  ASP A 384     6587   6596   4845  -1613   -887   -602       C  
ATOM   2440  C   ASP A 384      68.325  -3.797-190.709  1.00 46.37           C  
ANISOU 2440  C   ASP A 384     6415   6328   4877  -1503   -848   -574       C  
ATOM   2441  O   ASP A 384      68.930  -4.782-190.283  1.00 50.59           O  
ANISOU 2441  O   ASP A 384     7081   6675   5466  -1498   -810   -664       O  
ATOM   2442  CB  ASP A 384      68.839  -4.604-193.036  1.00 52.16           C  
ANISOU 2442  CB  ASP A 384     7395   7044   5378  -1638   -822   -763       C  
ATOM   2443  CG  ASP A 384      68.350  -4.721-194.479  1.00 67.93           C  
ANISOU 2443  CG  ASP A 384     9466   9162   7183  -1787   -871   -805       C  
ATOM   2444  OD1 ASP A 384      67.140  -4.951-194.680  1.00 71.44           O  
ANISOU 2444  OD1 ASP A 384     9870   9738   7534  -1963   -984   -757       O  
ATOM   2445  OD2 ASP A 384      69.168  -4.562-195.409  1.00 72.17           O  
ANISOU 2445  OD2 ASP A 384    10095   9669   7657  -1731   -797   -880       O  
ATOM   2446  N   LEU A 385      67.977  -2.779-189.921  1.00 43.57           N  
ANISOU 2446  N   LEU A 385     5892   6065   4599  -1412   -856   -446       N  
ATOM   2447  CA  LEU A 385      68.343  -2.758-188.508  1.00 47.95           C  
ANISOU 2447  CA  LEU A 385     6417   6505   5299  -1308   -822   -413       C  
ATOM   2448  C   LEU A 385      67.370  -3.582-187.671  1.00 52.56           C  
ANISOU 2448  C   LEU A 385     7001   7072   5898  -1437   -883   -383       C  
ATOM   2449  O   LEU A 385      66.199  -3.751-188.020  1.00 52.56           O  
ANISOU 2449  O   LEU A 385     6948   7207   5814  -1587   -957   -337       O  
ATOM   2450  CB  LEU A 385      68.379  -1.325-187.977  1.00 41.46           C  
ANISOU 2450  CB  LEU A 385     5437   5772   4543  -1164   -795   -296       C  
ATOM   2451  CG  LEU A 385      69.337  -0.347-188.649  1.00 44.69           C  
ANISOU 2451  CG  LEU A 385     5830   6198   4952  -1031   -728   -307       C  
ATOM   2452  CD1 LEU A 385      69.137   1.035-188.081  1.00 39.76           C  
ANISOU 2452  CD1 LEU A 385     5062   5663   4382   -918   -709   -182       C  
ATOM   2453  CD2 LEU A 385      70.780  -0.791-188.515  1.00 45.83           C  
ANISOU 2453  CD2 LEU A 385     6082   6160   5172   -936   -653   -413       C  
ATOM   2454  N   ASP A 386      67.863  -4.076-186.540  1.00 59.98           N  
ANISOU 2454  N   ASP A 386     7995   7851   6945  -1379   -851   -400       N  
ATOM   2455  CA  ASP A 386      67.034  -4.866-185.627  1.00 61.92           C  
ANISOU 2455  CA  ASP A 386     8254   8060   7213  -1491   -894   -369       C  
ATOM   2456  C   ASP A 386      66.213  -3.901-184.784  1.00 58.24           C  
ANISOU 2456  C   ASP A 386     7611   7728   6790  -1453   -908   -225       C  
ATOM   2457  O   ASP A 386      66.660  -3.413-183.747  1.00 59.82           O  
ANISOU 2457  O   ASP A 386     7779   7865   7086  -1325   -865   -182       O  
ATOM   2458  CB  ASP A 386      67.895  -5.769-184.752  1.00 66.17           C  
ANISOU 2458  CB  ASP A 386     8929   8371   7842  -1437   -856   -435       C  
ATOM   2459  CG  ASP A 386      67.084  -6.528-183.706  1.00 77.59           C  
ANISOU 2459  CG  ASP A 386    10396   9769   9315  -1545   -891   -392       C  
ATOM   2460  OD1 ASP A 386      67.703  -7.080-182.772  1.00 83.42           O  
ANISOU 2460  OD1 ASP A 386    11223  10337  10137  -1481   -863   -413       O  
ATOM   2461  OD2 ASP A 386      65.838  -6.586-183.819  1.00 75.86           O  
ANISOU 2461  OD2 ASP A 386    10103   9686   9036  -1694   -946   -334       O  
ATOM   2462  N   THR A 387      64.986  -3.634-185.220  1.00 50.26           N  
ANISOU 2462  N   THR A 387     6486   6905   5705  -1567   -966   -149       N  
ATOM   2463  CA  THR A 387      64.110  -2.739-184.478  1.00 54.04           C  
ANISOU 2463  CA  THR A 387     6791   7518   6223  -1527   -967     -7       C  
ATOM   2464  C   THR A 387      63.360  -3.431-183.355  1.00 53.79           C  
ANISOU 2464  C   THR A 387     6755   7449   6234  -1619   -980     36       C  
ATOM   2465  O   THR A 387      62.460  -2.816-182.775  1.00 55.09           O  
ANISOU 2465  O   THR A 387     6774   7737   6422  -1610   -976    157       O  
ATOM   2466  CB  THR A 387      63.093  -2.089-185.405  1.00 48.65           C  
ANISOU 2466  CB  THR A 387     5964   7069   5452  -1591  -1021     78       C  
ATOM   2467  OG1 THR A 387      62.162  -3.087-185.825  1.00 54.94           O  
ANISOU 2467  OG1 THR A 387     6777   7929   6170  -1808  -1103     61       O  
ATOM   2468  CG2 THR A 387      63.786  -1.480-186.612  1.00 54.32           C  
ANISOU 2468  CG2 THR A 387     6705   7827   6107  -1520  -1011     35       C  
ATOM   2469  N   ARG A 388      63.694  -4.683-183.045  1.00 49.67           N  
ANISOU 2469  N   ARG A 388     6392   6757   5723  -1703   -986    -54       N  
ATOM   2470  CA  ARG A 388      62.948  -5.434-182.048  1.00 53.08           C  
ANISOU 2470  CA  ARG A 388     6835   7148   6184  -1813   -999    -15       C  
ATOM   2471  C   ARG A 388      63.462  -5.216-180.629  1.00 52.73           C  
ANISOU 2471  C   ARG A 388     6813   6978   6243  -1678   -938     20       C  
ATOM   2472  O   ARG A 388      62.744  -5.534-179.679  1.00 52.51           O  
ANISOU 2472  O   ARG A 388     6763   6948   6241  -1744   -934     84       O  
ATOM   2473  CB  ARG A 388      62.966  -6.932-182.386  1.00 62.46           C  
ANISOU 2473  CB  ARG A 388     8201   8207   7325  -1984  -1035   -123       C  
ATOM   2474  CG  ARG A 388      62.144  -7.295-183.637  1.00 70.70           C  
ANISOU 2474  CG  ARG A 388     9226   9390   8248  -2178  -1111   -148       C  
ATOM   2475  CD  ARG A 388      62.039  -8.804-183.838  1.00 76.41           C  
ANISOU 2475  CD  ARG A 388    10139   9972   8920  -2371  -1141   -251       C  
ATOM   2476  NE  ARG A 388      60.970  -9.161-184.773  1.00 79.36           N  
ANISOU 2476  NE  ARG A 388    10473  10503   9177  -2600  -1229   -248       N  
ATOM   2477  CZ  ARG A 388      60.664 -10.408-185.118  1.00 85.50           C  
ANISOU 2477  CZ  ARG A 388    11407  11194   9885  -2812  -1269   -334       C  
ATOM   2478  NH1 ARG A 388      61.352 -11.423-184.609  1.00 90.66           N  
ANISOU 2478  NH1 ARG A 388    12272  11595  10580  -2808  -1220   -425       N  
ATOM   2479  NH2 ARG A 388      59.672 -10.643-185.971  1.00 82.42           N  
ANISOU 2479  NH2 ARG A 388    10966  10968   9381  -3030  -1360   -324       N  
ATOM   2480  N   THR A 389      64.668  -4.674-180.460  1.00 49.78           N  
ANISOU 2480  N   THR A 389     6482   6508   5923  -1501   -892    -15       N  
ATOM   2481  CA  THR A 389      65.205  -4.360-179.141  1.00 52.39           C  
ANISOU 2481  CA  THR A 389     6831   6733   6340  -1375   -846     22       C  
ATOM   2482  C   THR A 389      65.816  -2.964-179.141  1.00 56.66           C  
ANISOU 2482  C   THR A 389     7285   7327   6914  -1200   -803     59       C  
ATOM   2483  O   THR A 389      66.519  -2.584-180.081  1.00 51.00           O  
ANISOU 2483  O   THR A 389     6573   6625   6181  -1138   -797      7       O  
ATOM   2484  CB  THR A 389      66.258  -5.384-178.709  1.00 57.30           C  
ANISOU 2484  CB  THR A 389     7632   7131   7008  -1348   -841    -69       C  
ATOM   2485  OG1 THR A 389      66.848  -4.963-177.474  1.00 71.19           O  
ANISOU 2485  OG1 THR A 389     9403   8805   8842  -1220   -809    -27       O  
ATOM   2486  CG2 THR A 389      67.345  -5.515-179.765  1.00 59.49           C  
ANISOU 2486  CG2 THR A 389     7982   7346   7277  -1286   -834   -175       C  
ATOM   2487  N   THR A 390      65.569  -2.202-178.068  1.00 46.85           N  
ANISOU 2487  N   THR A 390     5979   6106   5715  -1123   -765    148       N  
ATOM   2488  CA  THR A 390      66.115  -0.848-178.016  1.00 48.55           C  
ANISOU 2488  CA  THR A 390     6128   6361   5958   -968   -719    184       C  
ATOM   2489  C   THR A 390      67.635  -0.857-177.944  1.00 39.47           C  
ANISOU 2489  C   THR A 390     5074   5065   4858   -860   -708    103       C  
ATOM   2490  O   THR A 390      68.273   0.107-178.373  1.00 37.76           O  
ANISOU 2490  O   THR A 390     4817   4880   4651   -757   -680    100       O  
ATOM   2491  CB  THR A 390      65.557  -0.076-176.820  1.00 45.41           C  
ANISOU 2491  CB  THR A 390     5669   5995   5589   -912   -671    288       C  
ATOM   2492  OG1 THR A 390      65.878  -0.775-175.605  1.00 46.82           O  
ANISOU 2492  OG1 THR A 390     5956   6027   5807   -921   -669    274       O  
ATOM   2493  CG2 THR A 390      64.045   0.086-176.944  1.00 48.22           C  
ANISOU 2493  CG2 THR A 390     5896   6520   5907   -997   -668    384       C  
ATOM   2494  N   SER A 391      68.231  -1.925-177.405  1.00 34.12           N  
ANISOU 2494  N   SER A 391     4520   4228   4214   -879   -728     43       N  
ATOM   2495  CA  SER A 391      69.659  -1.910-177.113  1.00 36.70           C  
ANISOU 2495  CA  SER A 391     4918   4422   4603   -764   -719    -12       C  
ATOM   2496  C   SER A 391      70.523  -2.161-178.339  1.00 35.09           C  
ANISOU 2496  C   SER A 391     4745   4194   4394   -738   -717   -105       C  
ATOM   2497  O   SER A 391      71.750  -2.069-178.241  1.00 36.67           O  
ANISOU 2497  O   SER A 391     4978   4304   4651   -635   -704   -147       O  
ATOM   2498  CB  SER A 391      69.989  -2.935-176.020  1.00 42.77           C  
ANISOU 2498  CB  SER A 391     5805   5031   5414   -778   -742    -24       C  
ATOM   2499  OG  SER A 391      69.588  -4.236-176.409  1.00 47.37           O  
ANISOU 2499  OG  SER A 391     6473   5557   5969   -895   -769    -74       O  
ATOM   2500  N   SER A 392      69.925  -2.481-179.490  1.00 37.97           N  
ANISOU 2500  N   SER A 392     5099   4639   4687   -832   -730   -137       N  
ATOM   2501  CA  SER A 392      70.696  -2.437-180.726  1.00 41.51           C  
ANISOU 2501  CA  SER A 392     5567   5090   5115   -797   -711   -217       C  
ATOM   2502  C   SER A 392      71.070  -1.018-181.118  1.00 44.61           C  
ANISOU 2502  C   SER A 392     5856   5583   5511   -694   -674   -179       C  
ATOM   2503  O   SER A 392      71.925  -0.846-181.998  1.00 38.81           O  
ANISOU 2503  O   SER A 392     5135   4838   4773   -641   -645   -240       O  
ATOM   2504  CB  SER A 392      69.907  -3.074-181.866  1.00 37.11           C  
ANISOU 2504  CB  SER A 392     5035   4603   4461   -937   -739   -258       C  
ATOM   2505  OG  SER A 392      68.760  -2.293-182.160  1.00 40.94           O  
ANISOU 2505  OG  SER A 392     5396   5272   4886   -992   -759   -172       O  
ATOM   2506  N   LEU A 393      70.450  -0.016-180.472  1.00 32.12           N  
ANISOU 2506  N   LEU A 393     4180   4089   3935   -665   -666    -80       N  
ATOM   2507  CA  LEU A 393      70.608   1.405-180.798  1.00 26.81           C  
ANISOU 2507  CA  LEU A 393     3416   3512   3257   -577   -626    -29       C  
ATOM   2508  C   LEU A 393      70.235   1.683-182.254  1.00 31.17           C  
ANISOU 2508  C   LEU A 393     3924   4191   3727   -616   -627    -38       C  
ATOM   2509  O   LEU A 393      70.857   2.512-182.925  1.00 34.32           O  
ANISOU 2509  O   LEU A 393     4297   4625   4120   -542   -589    -44       O  
ATOM   2510  CB  LEU A 393      72.018   1.902-180.508  1.00 28.77           C  
ANISOU 2510  CB  LEU A 393     3687   3668   3577   -459   -591    -63       C  
ATOM   2511  CG  LEU A 393      72.415   1.754-179.019  1.00 34.17           C  
ANISOU 2511  CG  LEU A 393     4411   4238   4332   -419   -601    -43       C  
ATOM   2512  CD1 LEU A 393      73.670   2.565-178.746  1.00 32.22           C  
ANISOU 2512  CD1 LEU A 393     4154   3942   4147   -311   -574    -53       C  
ATOM   2513  CD2 LEU A 393      71.259   2.167-178.109  1.00 30.24           C  
ANISOU 2513  CD2 LEU A 393     3875   3797   3816   -448   -600     52       C  
ATOM   2514  N   TRP A 394      69.194   1.004-182.738  1.00 33.60           N  
ANISOU 2514  N   TRP A 394     4227   4573   3964   -741   -673    -33       N  
ATOM   2515  CA  TRP A 394      68.769   1.245-184.113  1.00 37.28           C  
ANISOU 2515  CA  TRP A 394     4655   5172   4336   -792   -690    -34       C  
ATOM   2516  C   TRP A 394      68.262   2.664-184.313  1.00 40.15           C  
ANISOU 2516  C   TRP A 394     4895   5680   4680   -722   -667     76       C  
ATOM   2517  O   TRP A 394      68.432   3.228-185.401  1.00 34.75           O  
ANISOU 2517  O   TRP A 394     4190   5076   3937   -701   -656     74       O  
ATOM   2518  CB  TRP A 394      67.704   0.246-184.532  1.00 33.83           C  
ANISOU 2518  CB  TRP A 394     4234   4797   3824   -959   -757    -44       C  
ATOM   2519  CG  TRP A 394      66.439   0.271-183.747  1.00 29.42           C  
ANISOU 2519  CG  TRP A 394     3585   4323   3271  -1023   -788     57       C  
ATOM   2520  CD1 TRP A 394      66.156  -0.466-182.626  1.00 37.80           C  
ANISOU 2520  CD1 TRP A 394     4684   5296   4383  -1070   -796     63       C  
ATOM   2521  CD2 TRP A 394      65.264   1.033-184.035  1.00 38.55           C  
ANISOU 2521  CD2 TRP A 394     4595   5672   4380  -1046   -809    174       C  
ATOM   2522  NE1 TRP A 394      64.880  -0.201-182.203  1.00 36.79           N  
ANISOU 2522  NE1 TRP A 394     4440   5296   4243  -1126   -813    172       N  
ATOM   2523  CE2 TRP A 394      64.309   0.714-183.049  1.00 37.77           C  
ANISOU 2523  CE2 TRP A 394     4442   5596   4312  -1108   -822    244       C  
ATOM   2524  CE3 TRP A 394      64.925   1.957-185.036  1.00 40.52           C  
ANISOU 2524  CE3 TRP A 394     4752   6079   4565  -1017   -817    234       C  
ATOM   2525  CZ2 TRP A 394      63.043   1.287-183.025  1.00 38.79           C  
ANISOU 2525  CZ2 TRP A 394     4416   5905   4419  -1133   -837    371       C  
ATOM   2526  CZ3 TRP A 394      63.672   2.530-185.008  1.00 41.91           C  
ANISOU 2526  CZ3 TRP A 394     4777   6430   4718  -1037   -841    364       C  
ATOM   2527  CH2 TRP A 394      62.747   2.195-184.006  1.00 42.40           C  
ANISOU 2527  CH2 TRP A 394     4775   6515   4820  -1091   -848    432       C  
ATOM   2528  N   LYS A 395      67.618   3.248-183.299  1.00 32.68           N  
ANISOU 2528  N   LYS A 395     3874   4766   3776   -684   -652    174       N  
ATOM   2529  CA  LYS A 395      67.165   4.635-183.417  1.00 33.86           C  
ANISOU 2529  CA  LYS A 395     3917   5033   3915   -597   -614    282       C  
ATOM   2530  C   LYS A 395      68.340   5.579-183.613  1.00 31.44           C  
ANISOU 2530  C   LYS A 395     3640   4665   3639   -474   -552    258       C  
ATOM   2531  O   LYS A 395      68.299   6.467-184.477  1.00 34.34           O  
ANISOU 2531  O   LYS A 395     3962   5124   3961   -429   -531    300       O  
ATOM   2532  CB  LYS A 395      66.359   5.053-182.184  1.00 34.68           C  
ANISOU 2532  CB  LYS A 395     3958   5154   4065   -565   -588    382       C  
ATOM   2533  CG  LYS A 395      64.969   4.443-182.102  1.00 41.38           C  
ANISOU 2533  CG  LYS A 395     4729   6114   4879   -680   -637    444       C  
ATOM   2534  CD  LYS A 395      64.212   4.966-180.879  1.00 48.12           C  
ANISOU 2534  CD  LYS A 395     5516   6986   5780   -630   -587    548       C  
ATOM   2535  CE  LYS A 395      62.748   4.554-180.917  1.00 52.59           C  
ANISOU 2535  CE  LYS A 395     5967   7701   6315   -734   -625    634       C  
ATOM   2536  NZ  LYS A 395      62.049   4.884-179.645  1.00 56.42           N  
ANISOU 2536  NZ  LYS A 395     6401   8187   6851   -693   -562    724       N  
ATOM   2537  N   ASP A 396      69.386   5.422-182.788  1.00 33.99           N  
ANISOU 2537  N   ASP A 396     4036   4839   4039   -423   -525    199       N  
ATOM   2538  CA  ASP A 396      70.555   6.283-182.904  1.00 32.65           C  
ANISOU 2538  CA  ASP A 396     3887   4610   3906   -323   -470    176       C  
ATOM   2539  C   ASP A 396      71.214   6.150-184.276  1.00 35.17           C  
ANISOU 2539  C   ASP A 396     4232   4952   4178   -333   -464    106       C  
ATOM   2540  O   ASP A 396      71.594   7.153-184.884  1.00 33.62           O  
ANISOU 2540  O   ASP A 396     4012   4798   3965   -271   -418    131       O  
ATOM   2541  CB  ASP A 396      71.549   5.949-181.805  1.00 29.75           C  
ANISOU 2541  CB  ASP A 396     3586   4090   3626   -286   -463    123       C  
ATOM   2542  CG  ASP A 396      70.865   5.770-180.448  1.00 41.59           C  
ANISOU 2542  CG  ASP A 396     5089   5557   5156   -301   -476    177       C  
ATOM   2543  OD1 ASP A 396      70.075   4.810-180.309  1.00 36.67           O  
ANISOU 2543  OD1 ASP A 396     4471   4949   4510   -387   -520    176       O  
ATOM   2544  OD2 ASP A 396      71.106   6.593-179.535  1.00 47.03           O  
ANISOU 2544  OD2 ASP A 396     5782   6204   5883   -234   -439    218       O  
ATOM   2545  N   LYS A 397      71.363   4.917-184.766  1.00 35.27           N  
ANISOU 2545  N   LYS A 397     4306   4929   4166   -412   -502     18       N  
ATOM   2546  CA  LYS A 397      72.017   4.669-186.054  1.00 34.08           C  
ANISOU 2546  CA  LYS A 397     4201   4785   3963   -426   -485    -61       C  
ATOM   2547  C   LYS A 397      71.235   5.279-187.208  1.00 37.40           C  
ANISOU 2547  C   LYS A 397     4570   5364   4274   -457   -495     -4       C  
ATOM   2548  O   LYS A 397      71.816   5.922-188.089  1.00 34.78           O  
ANISOU 2548  O   LYS A 397     4245   5063   3909   -413   -450    -14       O  
ATOM   2549  CB  LYS A 397      72.183   3.168-186.277  1.00 39.06           C  
ANISOU 2549  CB  LYS A 397     4926   5334   4580   -510   -518   -165       C  
ATOM   2550  CG  LYS A 397      73.137   2.499-185.309  1.00 45.28           C  
ANISOU 2550  CG  LYS A 397     5773   5957   5473   -463   -505   -224       C  
ATOM   2551  CD  LYS A 397      73.009   1.005-185.398  1.00 59.74           C  
ANISOU 2551  CD  LYS A 397     7704   7707   7289   -551   -540   -306       C  
ATOM   2552  CE  LYS A 397      74.363   0.374-185.351  1.00 71.48           C  
ANISOU 2552  CE  LYS A 397     9266   9045   8847   -482   -497   -398       C  
ATOM   2553  NZ  LYS A 397      74.328  -0.990-185.937  1.00 77.05           N  
ANISOU 2553  NZ  LYS A 397    10092   9675   9508   -561   -505   -494       N  
ATOM   2554  N   ALA A 398      69.917   5.069-187.228  1.00 33.66           N  
ANISOU 2554  N   ALA A 398     4046   5000   3745   -538   -557     61       N  
ATOM   2555  CA  ALA A 398      69.094   5.618-188.302  1.00 41.89           C  
ANISOU 2555  CA  ALA A 398     5027   6209   4680   -570   -585    131       C  
ATOM   2556  C   ALA A 398      69.088   7.135-188.264  1.00 39.64           C  
ANISOU 2556  C   ALA A 398     4667   5983   4411   -451   -530    237       C  
ATOM   2557  O   ALA A 398      69.168   7.791-189.306  1.00 38.40           O  
ANISOU 2557  O   ALA A 398     4502   5907   4181   -428   -514    264       O  
ATOM   2558  CB  ALA A 398      67.669   5.082-188.198  1.00 42.67           C  
ANISOU 2558  CB  ALA A 398     5062   6420   4730   -683   -668    192       C  
ATOM   2559  N   ALA A 399      68.993   7.713-187.066  1.00 32.93           N  
ANISOU 2559  N   ALA A 399     3778   5086   3649   -375   -495    298       N  
ATOM   2560  CA  ALA A 399      69.025   9.164-186.927  1.00 30.02           C  
ANISOU 2560  CA  ALA A 399     3361   4745   3299   -258   -430    393       C  
ATOM   2561  C   ALA A 399      70.313   9.736-187.479  1.00 33.76           C  
ANISOU 2561  C   ALA A 399     3895   5152   3782   -197   -366    338       C  
ATOM   2562  O   ALA A 399      70.297  10.757-188.174  1.00 38.37           O  
ANISOU 2562  O   ALA A 399     4457   5801   4323   -142   -328    402       O  
ATOM   2563  CB  ALA A 399      68.869   9.555-185.437  1.00 27.71           C  
ANISOU 2563  CB  ALA A 399     3051   4378   3098   -197   -394    441       C  
ATOM   2564  N   VAL A 400      71.449   9.105-187.175  1.00 29.33           N  
ANISOU 2564  N   VAL A 400     3405   4460   3280   -204   -350    226       N  
ATOM   2565  CA  VAL A 400      72.710   9.670-187.652  1.00 32.17           C  
ANISOU 2565  CA  VAL A 400     3802   4761   3659   -147   -282    179       C  
ATOM   2566  C   VAL A 400      72.746   9.672-189.180  1.00 32.70           C  
ANISOU 2566  C   VAL A 400     3889   4916   3621   -179   -277    161       C  
ATOM   2567  O   VAL A 400      73.203  10.640-189.801  1.00 36.58           O  
ANISOU 2567  O   VAL A 400     4380   5430   4088   -127   -216    191       O  
ATOM   2568  CB  VAL A 400      73.909   8.916-187.055  1.00 36.04           C  
ANISOU 2568  CB  VAL A 400     4347   5109   4239   -144   -271     72       C  
ATOM   2569  CG1 VAL A 400      75.202   9.317-187.769  1.00 41.52           C  
ANISOU 2569  CG1 VAL A 400     5065   5764   4946   -103   -200     16       C  
ATOM   2570  CG2 VAL A 400      74.040   9.229-185.565  1.00 33.43           C  
ANISOU 2570  CG2 VAL A 400     4005   4693   4002   -101   -268    103       C  
ATOM   2571  N   GLU A 401      72.240   8.610-189.811  1.00 37.19           N  
ANISOU 2571  N   GLU A 401     4482   5534   4116   -275   -338    112       N  
ATOM   2572  CA  GLU A 401      72.292   8.558-191.276  1.00 35.40           C  
ANISOU 2572  CA  GLU A 401     4293   5386   3770   -317   -336     86       C  
ATOM   2573  C   GLU A 401      71.340   9.562-191.918  1.00 41.40           C  
ANISOU 2573  C   GLU A 401     4989   6300   4440   -301   -354    215       C  
ATOM   2574  O   GLU A 401      71.630  10.083-193.002  1.00 40.52           O  
ANISOU 2574  O   GLU A 401     4905   6243   4247   -289   -322    225       O  
ATOM   2575  CB  GLU A 401      72.006   7.139-191.768  1.00 43.21           C  
ANISOU 2575  CB  GLU A 401     5348   6377   4693   -436   -397     -7       C  
ATOM   2576  CG  GLU A 401      73.078   6.123-191.402  1.00 42.78           C  
ANISOU 2576  CG  GLU A 401     5375   6164   4715   -437   -363   -139       C  
ATOM   2577  CD  GLU A 401      74.507   6.604-191.657  1.00 55.98           C  
ANISOU 2577  CD  GLU A 401     7074   7756   6441   -347   -261   -190       C  
ATOM   2578  OE1 GLU A 401      74.769   7.327-192.656  1.00 42.29           O  
ANISOU 2578  OE1 GLU A 401     5346   6087   4635   -327   -212   -172       O  
ATOM   2579  OE2 GLU A 401      75.375   6.257-190.827  1.00 58.76           O  
ANISOU 2579  OE2 GLU A 401     7435   7983   6908   -299   -232   -242       O  
ATOM   2580  N   ILE A 402      70.205   9.850-191.275  1.00 38.78           N  
ANISOU 2580  N   ILE A 402     4572   6041   4123   -295   -402    322       N  
ATOM   2581  CA  ILE A 402      69.322  10.900-191.777  1.00 38.72           C  
ANISOU 2581  CA  ILE A 402     4489   6174   4049   -251   -412    463       C  
ATOM   2582  C   ILE A 402      70.032  12.247-191.737  1.00 40.09           C  
ANISOU 2582  C   ILE A 402     4673   6297   4262   -128   -312    513       C  
ATOM   2583  O   ILE A 402      69.975  13.026-192.697  1.00 41.04           O  
ANISOU 2583  O   ILE A 402     4795   6495   4301    -96   -291    577       O  
ATOM   2584  CB  ILE A 402      68.007  10.909-190.977  1.00 34.71           C  
ANISOU 2584  CB  ILE A 402     3875   5745   3568   -255   -467    569       C  
ATOM   2585  CG1 ILE A 402      67.240   9.611-191.232  1.00 40.36           C  
ANISOU 2585  CG1 ILE A 402     4579   6532   4223   -401   -572    527       C  
ATOM   2586  CG2 ILE A 402      67.146  12.125-191.312  1.00 34.89           C  
ANISOU 2586  CG2 ILE A 402     3808   5899   3550   -172   -459    733       C  
ATOM   2587  CD1 ILE A 402      66.092   9.339-190.232  1.00 35.55           C  
ANISOU 2587  CD1 ILE A 402     3869   5973   3665   -426   -618    604       C  
ATOM   2588  N   ASN A 403      70.736  12.535-190.633  1.00 31.05           N  
ANISOU 2588  N   ASN A 403     3546   5018   3235    -67   -251    485       N  
ATOM   2589  CA  ASN A 403      71.489  13.781-190.554  1.00 32.26           C  
ANISOU 2589  CA  ASN A 403     3723   5108   3427     28   -155    521       C  
ATOM   2590  C   ASN A 403      72.606  13.830-191.597  1.00 34.13           C  
ANISOU 2590  C   ASN A 403     4027   5319   3622     15   -105    445       C  
ATOM   2591  O   ASN A 403      72.860  14.881-192.199  1.00 33.90           O  
ANISOU 2591  O   ASN A 403     4014   5311   3557     68    -43    504       O  
ATOM   2592  CB  ASN A 403      72.035  13.959-189.123  1.00 29.48           C  
ANISOU 2592  CB  ASN A 403     3383   4618   3199     71   -115    494       C  
ATOM   2593  CG  ASN A 403      70.968  14.466-188.165  1.00 36.39           C  
ANISOU 2593  CG  ASN A 403     4205   5517   4106    121   -119    602       C  
ATOM   2594  OD1 ASN A 403      70.843  15.671-187.949  1.00 42.13           O  
ANISOU 2594  OD1 ASN A 403     4932   6232   4844    207    -52    690       O  
ATOM   2595  ND2 ASN A 403      70.179  13.551-187.610  1.00 40.07           N  
ANISOU 2595  ND2 ASN A 403     4630   6014   4582     68   -187    598       N  
ATOM   2596  N   VAL A 404      73.288  12.709-191.826  1.00 32.80           N  
ANISOU 2596  N   VAL A 404     3903   5100   3458    -52   -121    317       N  
ATOM   2597  CA  VAL A 404      74.285  12.667-192.895  1.00 30.66           C  
ANISOU 2597  CA  VAL A 404     3694   4815   3140    -65    -63    244       C  
ATOM   2598  C   VAL A 404      73.632  13.002-194.233  1.00 36.09           C  
ANISOU 2598  C   VAL A 404     4394   5641   3678    -90    -82    307       C  
ATOM   2599  O   VAL A 404      74.168  13.787-195.024  1.00 36.56           O  
ANISOU 2599  O   VAL A 404     4486   5713   3690    -58    -11    329       O  
ATOM   2600  CB  VAL A 404      74.976  11.289-192.935  1.00 34.33           C  
ANISOU 2600  CB  VAL A 404     4209   5206   3630   -126    -74    100       C  
ATOM   2601  CG1 VAL A 404      75.737  11.105-194.232  1.00 35.31           C  
ANISOU 2601  CG1 VAL A 404     4401   5342   3673   -149    -15     28       C  
ATOM   2602  CG2 VAL A 404      75.922  11.115-191.705  1.00 31.41           C  
ANISOU 2602  CG2 VAL A 404     3828   4694   3411    -84    -44     44       C  
ATOM   2603  N   ALA A 405      72.443  12.450-194.484  1.00 39.88           N  
ANISOU 2603  N   ALA A 405     4844   6231   4079   -153   -181    345       N  
ATOM   2604  CA  ALA A 405      71.771  12.693-195.758  1.00 43.62           C  
ANISOU 2604  CA  ALA A 405     5325   6850   4398   -189   -221    409       C  
ATOM   2605  C   ALA A 405      71.385  14.158-195.908  1.00 44.41           C  
ANISOU 2605  C   ALA A 405     5381   7012   4481    -91   -185    562       C  
ATOM   2606  O   ALA A 405      71.461  14.716-197.011  1.00 41.84           O  
ANISOU 2606  O   ALA A 405     5093   6756   4047    -84   -163    606       O  
ATOM   2607  CB  ALA A 405      70.541  11.794-195.891  1.00 43.86           C  
ANISOU 2607  CB  ALA A 405     5316   6993   4355   -289   -347    426       C  
ATOM   2608  N   VAL A 406      70.971  14.805-194.813  1.00 37.90           N  
ANISOU 2608  N   VAL A 406     4489   6155   3756    -12   -172    646       N  
ATOM   2609  CA  VAL A 406      70.637  16.227-194.887  1.00 39.48           C  
ANISOU 2609  CA  VAL A 406     4662   6389   3948     95   -121    791       C  
ATOM   2610  C   VAL A 406      71.866  17.034-195.284  1.00 44.65           C  
ANISOU 2610  C   VAL A 406     5400   6952   4614    139     -6    762       C  
ATOM   2611  O   VAL A 406      71.833  17.835-196.226  1.00 38.38           O  
ANISOU 2611  O   VAL A 406     4635   6217   3731    172     26    841       O  
ATOM   2612  CB  VAL A 406      70.058  16.726-193.551  1.00 36.24           C  
ANISOU 2612  CB  VAL A 406     4186   5935   3648    174   -106    869       C  
ATOM   2613  CG1 VAL A 406      70.062  18.259-193.520  1.00 33.06           C  
ANISOU 2613  CG1 VAL A 406     3796   5507   3258    297    -16    992       C  
ATOM   2614  CG2 VAL A 406      68.645  16.192-193.352  1.00 40.90           C  
ANISOU 2614  CG2 VAL A 406     4674   6655   4211    143   -210    943       C  
ATOM   2615  N   LEU A 407      72.967  16.845-194.555  1.00 40.47           N  
ANISOU 2615  N   LEU A 407     4904   6279   4193    138     55    657       N  
ATOM   2616  CA  LEU A 407      74.187  17.592-194.845  1.00 38.94           C  
ANISOU 2616  CA  LEU A 407     4773   5998   4024    167    166    627       C  
ATOM   2617  C   LEU A 407      74.672  17.334-196.268  1.00 35.52           C  
ANISOU 2617  C   LEU A 407     4399   5621   3475    116    188    581       C  
ATOM   2618  O   LEU A 407      75.037  18.273-196.988  1.00 39.19           O  
ANISOU 2618  O   LEU A 407     4909   6095   3888    149    263    636       O  
ATOM   2619  CB  LEU A 407      75.269  17.222-193.838  1.00 35.34           C  
ANISOU 2619  CB  LEU A 407     4323   5401   3703    156    205    517       C  
ATOM   2620  CG  LEU A 407      75.047  17.817-192.444  1.00 36.37           C  
ANISOU 2620  CG  LEU A 407     4427   5452   3940    212    215    567       C  
ATOM   2621  CD1 LEU A 407      75.813  17.032-191.385  1.00 33.73           C  
ANISOU 2621  CD1 LEU A 407     4086   5010   3721    180    200    456       C  
ATOM   2622  CD2 LEU A 407      75.508  19.259-192.464  1.00 34.53           C  
ANISOU 2622  CD2 LEU A 407     4236   5162   3722    272    315    638       C  
ATOM   2623  N   HIS A 408      74.714  16.059-196.678  1.00 35.08           N  
ANISOU 2623  N   HIS A 408     4360   5595   3375     33    134    475       N  
ATOM   2624  CA  HIS A 408      75.199  15.713-198.010  1.00 37.64           C  
ANISOU 2624  CA  HIS A 408     4759   5963   3581    -21    164    415       C  
ATOM   2625  C   HIS A 408      74.328  16.342-199.087  1.00 40.50           C  
ANISOU 2625  C   HIS A 408     5137   6466   3786    -19    128    536       C  
ATOM   2626  O   HIS A 408      74.838  16.919-200.061  1.00 45.53           O  
ANISOU 2626  O   HIS A 408     5840   7121   4339    -13    201    553       O  
ATOM   2627  CB  HIS A 408      75.240  14.192-198.169  1.00 37.11           C  
ANISOU 2627  CB  HIS A 408     4719   5891   3488   -110    108    282       C  
ATOM   2628  CG  HIS A 408      75.286  13.736-199.596  1.00 51.44           C  
ANISOU 2628  CG  HIS A 408     6623   7782   5140   -181    110    236       C  
ATOM   2629  ND1 HIS A 408      76.453  13.692-200.327  1.00 50.30           N  
ANISOU 2629  ND1 HIS A 408     6555   7584   4971   -185    223    150       N  
ATOM   2630  CD2 HIS A 408      74.306  13.302-200.426  1.00 51.06           C  
ANISOU 2630  CD2 HIS A 408     6601   7862   4936   -258     14    262       C  
ATOM   2631  CE1 HIS A 408      76.192  13.248-201.544  1.00 54.70           C  
ANISOU 2631  CE1 HIS A 408     7198   8226   5360   -257    204    121       C  
ATOM   2632  NE2 HIS A 408      74.896  13.005-201.630  1.00 55.62           N  
ANISOU 2632  NE2 HIS A 408     7289   8455   5391   -308     70    188       N  
ATOM   2633  N   SER A 409      73.007  16.263-198.910  1.00 42.47           N  
ANISOU 2633  N   SER A 409     5321   6821   3996    -23     18    629       N  
ATOM   2634  CA  SER A 409      72.079  16.771-199.915  1.00 49.12           C  
ANISOU 2634  CA  SER A 409     6161   7818   4687    -23    -40    756       C  
ATOM   2635  C   SER A 409      72.188  18.283-200.069  1.00 49.00           C  
ANISOU 2635  C   SER A 409     6154   7791   4673     87     42    891       C  
ATOM   2636  O   SER A 409      72.211  18.801-201.198  1.00 44.42           O  
ANISOU 2636  O   SER A 409     5633   7282   3963     88     61    951       O  
ATOM   2637  CB  SER A 409      70.656  16.368-199.539  1.00 40.41           C  
ANISOU 2637  CB  SER A 409     4956   6831   3567    -46   -176    836       C  
ATOM   2638  OG  SER A 409      70.520  14.956-199.522  1.00 44.63           O  
ANISOU 2638  OG  SER A 409     5501   7376   4080   -166   -254    714       O  
ATOM   2639  N   TYR A 410      72.249  19.007-198.948  1.00 45.55           N  
ANISOU 2639  N   TYR A 410     5673   7260   4374    176     95    940       N  
ATOM   2640  CA  TYR A 410      72.337  20.462-199.003  1.00 40.65           C  
ANISOU 2640  CA  TYR A 410     5078   6606   3763    281    183   1066       C  
ATOM   2641  C   TYR A 410      73.659  20.914-199.606  1.00 46.31           C  
ANISOU 2641  C   TYR A 410     5895   7236   4465    268    305   1004       C  
ATOM   2642  O   TYR A 410      73.700  21.886-200.374  1.00 41.53           O  
ANISOU 2642  O   TYR A 410     5345   6653   3780    312    361   1103       O  
ATOM   2643  CB  TYR A 410      72.147  21.060-197.605  1.00 37.36           C  
ANISOU 2643  CB  TYR A 410     4614   6090   3494    366    219   1112       C  
ATOM   2644  CG  TYR A 410      70.698  21.282-197.244  1.00 41.08           C  
ANISOU 2644  CG  TYR A 410     4990   6661   3956    431    142   1253       C  
ATOM   2645  CD1 TYR A 410      70.206  22.560-197.039  1.00 37.69           C  
ANISOU 2645  CD1 TYR A 410     4558   6219   3544    557    199   1407       C  
ATOM   2646  CD2 TYR A 410      69.817  20.213-197.127  1.00 39.73           C  
ANISOU 2646  CD2 TYR A 410     4733   6599   3764    367     19   1235       C  
ATOM   2647  CE1 TYR A 410      68.886  22.775-196.729  1.00 35.90           C  
ANISOU 2647  CE1 TYR A 410     4233   6090   3318    632    141   1545       C  
ATOM   2648  CE2 TYR A 410      68.490  20.421-196.818  1.00 39.49           C  
ANISOU 2648  CE2 TYR A 410     4597   6675   3731    425    -47   1372       C  
ATOM   2649  CZ  TYR A 410      68.030  21.711-196.630  1.00 38.45           C  
ANISOU 2649  CZ  TYR A 410     4452   6536   3622    565     16   1530       C  
ATOM   2650  OH  TYR A 410      66.710  21.950-196.341  1.00 43.20           O  
ANISOU 2650  OH  TYR A 410     4936   7248   4229    639    -37   1677       O  
ATOM   2651  N   GLN A 411      74.748  20.221-199.273  1.00 41.84           N  
ANISOU 2651  N   GLN A 411     5349   6571   3977    210    351    849       N  
ATOM   2652  CA  GLN A 411      76.036  20.568-199.860  1.00 43.01           C  
ANISOU 2652  CA  GLN A 411     5574   6648   4119    191    472    788       C  
ATOM   2653  C   GLN A 411      76.035  20.293-201.359  1.00 48.54           C  
ANISOU 2653  C   GLN A 411     6345   7453   4646    137    470    782       C  
ATOM   2654  O   GLN A 411      76.548  21.101-202.141  1.00 49.00           O  
ANISOU 2654  O   GLN A 411     6475   7505   4639    151    563    827       O  
ATOM   2655  CB  GLN A 411      77.161  19.805-199.151  1.00 47.26           C  
ANISOU 2655  CB  GLN A 411     6096   7073   4787    149    514    631       C  
ATOM   2656  CG  GLN A 411      77.322  20.197-197.666  1.00 50.56           C  
ANISOU 2656  CG  GLN A 411     6463   7380   5368    193    524    637       C  
ATOM   2657  CD  GLN A 411      78.214  19.236-196.891  1.00 57.55           C  
ANISOU 2657  CD  GLN A 411     7314   8177   6374    152    524    494       C  
ATOM   2658  OE1 GLN A 411      78.570  18.169-197.387  1.00 68.69           O  
ANISOU 2658  OE1 GLN A 411     8735   9609   7756     99    510    390       O  
ATOM   2659  NE2 GLN A 411      78.579  19.617-195.668  1.00 53.01           N  
ANISOU 2659  NE2 GLN A 411     6709   7500   5931    177    541    490       N  
ATOM   2660  N   LEU A 412      75.417  19.184-201.779  1.00 43.16           N  
ANISOU 2660  N   LEU A 412     5656   6866   3877     69    365    731       N  
ATOM   2661  CA  LEU A 412      75.349  18.863-203.202  1.00 48.01           C  
ANISOU 2661  CA  LEU A 412     6353   7582   4305      4    353    719       C  
ATOM   2662  C   LEU A 412      74.507  19.889-203.952  1.00 50.38           C  
ANISOU 2662  C   LEU A 412     6671   7994   4475     51    321    897       C  
ATOM   2663  O   LEU A 412      74.852  20.295-205.069  1.00 47.85           O  
ANISOU 2663  O   LEU A 412     6444   7712   4025     35    378    924       O  
ATOM   2664  CB  LEU A 412      74.786  17.452-203.382  1.00 49.57           C  
ANISOU 2664  CB  LEU A 412     6548   7850   4438    -92    236    626       C  
ATOM   2665  CG  LEU A 412      74.750  16.834-204.782  1.00 58.66           C  
ANISOU 2665  CG  LEU A 412     7805   9094   5389   -187    215    575       C  
ATOM   2666  CD1 LEU A 412      76.149  16.794-205.363  1.00 59.14           C  
ANISOU 2666  CD1 LEU A 412     7963   9064   5443   -199    371    464       C  
ATOM   2667  CD2 LEU A 412      74.143  15.434-204.733  1.00 60.28           C  
ANISOU 2667  CD2 LEU A 412     8007   9345   5551   -289     95    479       C  
ATOM   2668  N   ALA A 413      73.407  20.334-203.349  1.00 52.78           N  
ANISOU 2668  N   ALA A 413     6887   8353   4815    116    237   1027       N  
ATOM   2669  CA  ALA A 413      72.585  21.399-203.910  1.00 54.94           C  
ANISOU 2669  CA  ALA A 413     7160   8722   4991    190    211   1218       C  
ATOM   2670  C   ALA A 413      73.195  22.786-203.736  1.00 54.89           C  
ANISOU 2670  C   ALA A 413     7202   8605   5047    289    349   1301       C  
ATOM   2671  O   ALA A 413      72.581  23.767-204.172  1.00 53.13           O  
ANISOU 2671  O   ALA A 413     6993   8441   4754    368    345   1468       O  
ATOM   2672  CB  ALA A 413      71.192  21.370-203.273  1.00 49.48           C  
ANISOU 2672  CB  ALA A 413     6343   8126   4332    237     84   1332       C  
ATOM   2673  N   LYS A 414      74.378  22.892-203.126  1.00 49.25           N  
ANISOU 2673  N   LYS A 414     6516   7736   4462    283    468   1194       N  
ATOM   2674  CA  LYS A 414      75.025  24.178-202.855  1.00 47.20           C  
ANISOU 2674  CA  LYS A 414     6307   7355   4271    354    601   1258       C  
ATOM   2675  C   LYS A 414      74.071  25.128-202.138  1.00 50.01           C  
ANISOU 2675  C   LYS A 414     6619   7701   4682    473    581   1417       C  
ATOM   2676  O   LYS A 414      73.882  26.281-202.534  1.00 45.86           O  
ANISOU 2676  O   LYS A 414     6150   7165   4109    550    639   1557       O  
ATOM   2677  CB  LYS A 414      75.560  24.814-204.143  1.00 59.25           C  
ANISOU 2677  CB  LYS A 414     7947   8902   5662    340    688   1303       C  
ATOM   2678  CG  LYS A 414      76.073  23.814-205.161  1.00 65.97           C  
ANISOU 2678  CG  LYS A 414     8850   9820   6397    232    684   1181       C  
ATOM   2679  CD  LYS A 414      77.588  23.765-205.224  1.00 73.21           C  
ANISOU 2679  CD  LYS A 414     9818  10621   7379    181    832   1052       C  
ATOM   2680  CE  LYS A 414      78.046  23.673-206.676  1.00 82.15           C  
ANISOU 2680  CE  LYS A 414    11061  11816   8337    122    894   1033       C  
ATOM   2681  NZ  LYS A 414      79.476  23.280-206.802  1.00 90.58           N  
ANISOU 2681  NZ  LYS A 414    12157  12796   9464     62   1031    884       N  
ATOM   2682  N   VAL A 415      73.445  24.619-201.079  1.00 42.24           N  
ANISOU 2682  N   VAL A 415     5536   6716   3797    490    505   1397       N  
ATOM   2683  CA  VAL A 415      72.605  25.411-200.199  1.00 42.29           C  
ANISOU 2683  CA  VAL A 415     5495   6694   3879    606    504   1525       C  
ATOM   2684  C   VAL A 415      73.293  25.443-198.846  1.00 45.14           C  
ANISOU 2684  C   VAL A 415     5853   6891   4409    604    569   1429       C  
ATOM   2685  O   VAL A 415      73.641  24.388-198.297  1.00 42.56           O  
ANISOU 2685  O   VAL A 415     5479   6545   4146    529    525   1290       O  
ATOM   2686  CB  VAL A 415      71.190  24.825-200.085  1.00 44.73           C  
ANISOU 2686  CB  VAL A 415     5687   7154   4154    627    361   1601       C  
ATOM   2687  CG1 VAL A 415      70.380  25.626-199.084  1.00 42.07           C  
ANISOU 2687  CG1 VAL A 415     5298   6776   3912    757    383   1726       C  
ATOM   2688  CG2 VAL A 415      70.509  24.802-201.467  1.00 47.42           C  
ANISOU 2688  CG2 VAL A 415     6031   7672   4315    616    278   1704       C  
ATOM   2689  N   THR A 416      73.513  26.648-198.332  1.00 43.16           N  
ANISOU 2689  N   THR A 416     5661   6517   4220    683    674   1501       N  
ATOM   2690  CA  THR A 416      74.184  26.827-197.051  1.00 43.13           C  
ANISOU 2690  CA  THR A 416     5671   6354   4361    675    738   1419       C  
ATOM   2691  C   THR A 416      73.528  25.991-195.948  1.00 44.39           C  
ANISOU 2691  C   THR A 416     5733   6530   4602    676    650   1374       C  
ATOM   2692  O   THR A 416      72.308  26.004-195.765  1.00 39.08           O  
ANISOU 2692  O   THR A 416     4995   5941   3911    749    590   1478       O  
ATOM   2693  CB  THR A 416      74.170  28.312-196.678  1.00 43.21           C  
ANISOU 2693  CB  THR A 416     5772   6242   4405    770    853   1532       C  
ATOM   2694  OG1 THR A 416      74.710  29.077-197.761  1.00 42.81           O  
ANISOU 2694  OG1 THR A 416     5816   6180   4268    765    934   1585       O  
ATOM   2695  CG2 THR A 416      75.002  28.570-195.426  1.00 37.79           C  
ANISOU 2695  CG2 THR A 416     5124   5383   3850    736    922   1439       C  
ATOM   2696  N   ILE A 417      74.354  25.241-195.222  1.00 40.22           N  
ANISOU 2696  N   ILE A 417     5190   5927   4163    594    643   1224       N  
ATOM   2697  CA  ILE A 417      73.911  24.506-194.044  1.00 37.34           C  
ANISOU 2697  CA  ILE A 417     4755   5548   3885    589    576   1174       C  
ATOM   2698  C   ILE A 417      75.108  24.400-193.114  1.00 34.74           C  
ANISOU 2698  C   ILE A 417     4459   5074   3668    530    623   1048       C  
ATOM   2699  O   ILE A 417      76.263  24.472-193.545  1.00 35.85           O  
ANISOU 2699  O   ILE A 417     4640   5166   3815    471    677    976       O  
ATOM   2700  CB  ILE A 417      73.360  23.109-194.414  1.00 35.26           C  
ANISOU 2700  CB  ILE A 417     4405   5418   3574    526    451   1119       C  
ATOM   2701  CG1 ILE A 417      72.597  22.496-193.240  1.00 44.24           C  
ANISOU 2701  CG1 ILE A 417     5467   6555   4785    536    384   1109       C  
ATOM   2702  CG2 ILE A 417      74.511  22.195-194.890  1.00 37.39           C  
ANISOU 2702  CG2 ILE A 417     4694   5670   3842    420    448    964       C  
ATOM   2703  CD1 ILE A 417      71.421  21.655-193.641  1.00 46.22           C  
ANISOU 2703  CD1 ILE A 417     5627   6965   4968    517    267   1150       C  
ATOM   2704  N   VAL A 418      74.837  24.226-191.823  1.00 41.56           N  
ANISOU 2704  N   VAL A 418     5300   5874   4618    544    601   1027       N  
ATOM   2705  CA  VAL A 418      75.906  24.037-190.852  1.00 37.34           C  
ANISOU 2705  CA  VAL A 418     4788   5215   4185    483    622    913       C  
ATOM   2706  C   VAL A 418      75.563  22.848-189.960  1.00 33.33           C  
ANISOU 2706  C   VAL A 418     4211   4722   3730    452    527    842       C  
ATOM   2707  O   VAL A 418      74.419  22.692-189.522  1.00 33.19           O  
ANISOU 2707  O   VAL A 418     4153   4753   3704    501    484    906       O  
ATOM   2708  CB  VAL A 418      76.163  25.323-190.030  1.00 40.97           C  
ANISOU 2708  CB  VAL A 418     5338   5534   4694    522    718    960       C  
ATOM   2709  CG1 VAL A 418      74.921  25.759-189.238  1.00 45.07           C  
ANISOU 2709  CG1 VAL A 418     5862   6044   5218    619    722   1060       C  
ATOM   2710  CG2 VAL A 418      77.376  25.142-189.116  1.00 40.94           C  
ANISOU 2710  CG2 VAL A 418     5356   5415   4784    438    726    842       C  
ATOM   2711  N   ASP A 419      76.544  21.984-189.730  1.00 34.72           N  
ANISOU 2711  N   ASP A 419     4369   4863   3962    373    496    715       N  
ATOM   2712  CA  ASP A 419      76.332  20.845-188.852  1.00 32.58           C  
ANISOU 2712  CA  ASP A 419     4047   4588   3744    341    410    646       C  
ATOM   2713  C   ASP A 419      76.451  21.291-187.394  1.00 32.49           C  
ANISOU 2713  C   ASP A 419     4072   4462   3812    354    428    645       C  
ATOM   2714  O   ASP A 419      76.956  22.376-187.088  1.00 33.86           O  
ANISOU 2714  O   ASP A 419     4314   4546   4007    366    505    670       O  
ATOM   2715  CB  ASP A 419      77.313  19.703-189.176  1.00 37.01           C  
ANISOU 2715  CB  ASP A 419     4578   5150   4333    267    373    519       C  
ATOM   2716  CG  ASP A 419      78.763  20.020-188.809  1.00 48.42           C  
ANISOU 2716  CG  ASP A 419     6045   6494   5859    230    425    449       C  
ATOM   2717  OD1 ASP A 419      79.088  20.076-187.597  1.00 39.66           O  
ANISOU 2717  OD1 ASP A 419     4943   5297   4827    218    409    423       O  
ATOM   2718  OD2 ASP A 419      79.588  20.172-189.737  1.00 45.85           O  
ANISOU 2718  OD2 ASP A 419     5725   6182   5515    206    479    420       O  
ATOM   2719  N   HIS A 420      75.938  20.448-186.495  1.00 31.67           N  
ANISOU 2719  N   HIS A 420     3934   4358   3743    344    357    618       N  
ATOM   2720  CA  HIS A 420      75.867  20.823-185.079  1.00 34.72           C  
ANISOU 2720  CA  HIS A 420     4365   4643   4185    357    371    625       C  
ATOM   2721  C   HIS A 420      77.239  20.898-184.414  1.00 34.01           C  
ANISOU 2721  C   HIS A 420     4314   4442   4165    295    378    537       C  
ATOM   2722  O   HIS A 420      77.389  21.617-183.419  1.00 38.39           O  
ANISOU 2722  O   HIS A 420     4938   4900   4748    297    413    549       O  
ATOM   2723  CB  HIS A 420      74.933  19.863-184.316  1.00 33.34           C  
ANISOU 2723  CB  HIS A 420     4145   4504   4020    357    297    624       C  
ATOM   2724  CG  HIS A 420      75.239  18.403-184.503  1.00 37.74           C  
ANISOU 2724  CG  HIS A 420     4646   5099   4594    290    206    531       C  
ATOM   2725  ND1 HIS A 420      75.077  17.751-185.710  1.00 35.48           N  
ANISOU 2725  ND1 HIS A 420     4313   4913   4254    268    172    515       N  
ATOM   2726  CD2 HIS A 420      75.634  17.456-183.617  1.00 37.10           C  
ANISOU 2726  CD2 HIS A 420     4562   4964   4570    243    145    454       C  
ATOM   2727  CE1 HIS A 420      75.405  16.480-185.574  1.00 35.84           C  
ANISOU 2727  CE1 HIS A 420     4336   4954   4329    211    104    425       C  
ATOM   2728  NE2 HIS A 420      75.744  16.272-184.310  1.00 38.36           N  
ANISOU 2728  NE2 HIS A 420     4676   5180   4718    200     85    391       N  
ATOM   2729  N   HIS A 421      78.256  20.211-184.944  1.00 30.26           N  
ANISOU 2729  N   HIS A 421     3798   3981   3718    239    350    452       N  
ATOM   2730  CA  HIS A 421      79.595  20.347-184.367  1.00 36.44           C  
ANISOU 2730  CA  HIS A 421     4596   4675   4574    182    355    382       C  
ATOM   2731  C   HIS A 421      80.190  21.706-184.706  1.00 36.14           C  
ANISOU 2731  C   HIS A 421     4617   4587   4527    174    450    418       C  
ATOM   2732  O   HIS A 421      80.722  22.396-183.836  1.00 33.45           O  
ANISOU 2732  O   HIS A 421     4334   4151   4223    140    471    412       O  
ATOM   2733  CB  HIS A 421      80.509  19.217-184.856  1.00 33.84           C  
ANISOU 2733  CB  HIS A 421     4194   4377   4286    140    309    290       C  
ATOM   2734  CG  HIS A 421      79.987  17.858-184.519  1.00 35.97           C  
ANISOU 2734  CG  HIS A 421     4424   4677   4565    140    220    251       C  
ATOM   2735  ND1 HIS A 421      79.952  17.383-183.225  1.00 34.37           N  
ANISOU 2735  ND1 HIS A 421     4231   4415   4413    126    156    229       N  
ATOM   2736  CD2 HIS A 421      79.446  16.888-185.294  1.00 36.01           C  
ANISOU 2736  CD2 HIS A 421     4393   4760   4528    145    185    232       C  
ATOM   2737  CE1 HIS A 421      79.418  16.176-183.218  1.00 33.24           C  
ANISOU 2737  CE1 HIS A 421     4057   4307   4264    125     91    201       C  
ATOM   2738  NE2 HIS A 421      79.105  15.851-184.461  1.00 33.75           N  
ANISOU 2738  NE2 HIS A 421     4096   4454   4274    132    106    199       N  
ATOM   2739  N   ALA A 422      80.101  22.108-185.974  1.00 33.87           N  
ANISOU 2739  N   ALA A 422     4327   4360   4183    197    508    457       N  
ATOM   2740  CA  ALA A 422      80.606  23.416-186.381  1.00 33.94           C  
ANISOU 2740  CA  ALA A 422     4402   4317   4174    189    608    500       C  
ATOM   2741  C   ALA A 422      79.837  24.532-185.691  1.00 35.62           C  
ANISOU 2741  C   ALA A 422     4714   4456   4364    240    660    585       C  
ATOM   2742  O   ALA A 422      80.427  25.523-185.247  1.00 33.94           O  
ANISOU 2742  O   ALA A 422     4584   4141   4170    205    722    591       O  
ATOM   2743  CB  ALA A 422      80.505  23.568-187.907  1.00 29.23           C  
ANISOU 2743  CB  ALA A 422     3793   3807   3505    213    657    537       C  
ATOM   2744  N   ALA A 423      78.512  24.393-185.600  1.00 36.93           N  
ANISOU 2744  N   ALA A 423     4874   4671   4486    320    641    654       N  
ATOM   2745  CA  ALA A 423      77.703  25.467-185.046  1.00 34.68           C  
ANISOU 2745  CA  ALA A 423     4681   4319   4177    392    710    745       C  
ATOM   2746  C   ALA A 423      78.005  25.681-183.569  1.00 31.27           C  
ANISOU 2746  C   ALA A 423     4321   3765   3795    353    709    703       C  
ATOM   2747  O   ALA A 423      78.148  26.829-183.123  1.00 32.99           O  
ANISOU 2747  O   ALA A 423     4657   3871   4007    358    793    735       O  
ATOM   2748  CB  ALA A 423      76.221  25.170-185.255  1.00 40.97           C  
ANISOU 2748  CB  ALA A 423     5426   5213   4926    488    687    832       C  
ATOM   2749  N   THR A 424      78.147  24.591-182.804  1.00 31.93           N  
ANISOU 2749  N   THR A 424     4348   3862   3922    309    614    628       N  
ATOM   2750  CA  THR A 424      78.390  24.737-181.371  1.00 31.47           C  
ANISOU 2750  CA  THR A 424     4364   3695   3897    268    601    591       C  
ATOM   2751  C   THR A 424      79.803  25.229-181.099  1.00 32.55           C  
ANISOU 2751  C   THR A 424     4549   3745   4073    165    611    527       C  
ATOM   2752  O   THR A 424      80.031  25.976-180.135  1.00 32.63           O  
ANISOU 2752  O   THR A 424     4673   3642   4084    128    643    521       O  
ATOM   2753  CB  THR A 424      78.150  23.414-180.615  1.00 32.56           C  
ANISOU 2753  CB  THR A 424     4435   3870   4065    249    494    538       C  
ATOM   2754  OG1 THR A 424      78.902  22.349-181.213  1.00 33.63           O  
ANISOU 2754  OG1 THR A 424     4466   4074   4237    198    417    466       O  
ATOM   2755  CG2 THR A 424      76.684  23.039-180.593  1.00 32.79           C  
ANISOU 2755  CG2 THR A 424     4430   3971   4059    334    490    607       C  
ATOM   2756  N   ALA A 425      80.769  24.782-181.908  1.00 33.13           N  
ANISOU 2756  N   ALA A 425     4537   3874   4179    111    582    476       N  
ATOM   2757  CA  ALA A 425      82.118  25.325-181.802  1.00 34.85           C  
ANISOU 2757  CA  ALA A 425     4777   4027   4438     10    600    428       C  
ATOM   2758  C   ALA A 425      82.111  26.835-182.032  1.00 41.67           C  
ANISOU 2758  C   ALA A 425     5767   4805   5259      9    719    488       C  
ATOM   2759  O   ALA A 425      82.798  27.586-181.327  1.00 35.88           O  
ANISOU 2759  O   ALA A 425     5123   3968   4542    -74    742    466       O  
ATOM   2760  CB  ALA A 425      83.056  24.621-182.791  1.00 32.01           C  
ANISOU 2760  CB  ALA A 425     4293   3752   4117    -28    575    377       C  
ATOM   2761  N   SER A 426      81.328  27.304-183.007  1.00 34.25           N  
ANISOU 2761  N   SER A 426     4846   3904   4263     99    794    569       N  
ATOM   2762  CA ASER A 426      81.257  28.741-183.254  0.55 40.88           C  
ANISOU 2762  CA ASER A 426     5820   4652   5062    113    915    637       C  
ATOM   2763  CA BSER A 426      81.270  28.743-183.242  0.45 40.45           C  
ANISOU 2763  CA BSER A 426     5765   4595   5008    112    914    636       C  
ATOM   2764  C   SER A 426      80.563  29.460-182.100  1.00 39.69           C  
ANISOU 2764  C   SER A 426     5810   4382   4890    150    959    672       C  
ATOM   2765  O   SER A 426      80.910  30.605-181.776  1.00 35.78           O  
ANISOU 2765  O   SER A 426     5457   3758   4379    109   1044    685       O  
ATOM   2766  CB ASER A 426      80.545  29.022-184.583  0.55 37.64           C  
ANISOU 2766  CB ASER A 426     5392   4319   4591    212    975    728       C  
ATOM   2767  CB BSER A 426      80.580  29.042-184.572  0.45 37.89           C  
ANISOU 2767  CB BSER A 426     5426   4347   4624    209    976    727       C  
ATOM   2768  OG ASER A 426      79.128  28.945-184.455  0.55 41.82           O  
ANISOU 2768  OG ASER A 426     5925   4885   5081    337    976    807       O  
ATOM   2769  OG BSER A 426      81.361  28.577-185.653  0.45 36.31           O  
ANISOU 2769  OG BSER A 426     5131   4233   4431    160    962    691       O  
ATOM   2770  N   PHE A 427      79.582  28.808-181.475  1.00 36.10           N  
ANISOU 2770  N   PHE A 427     5326   3963   4429    223    911    684       N  
ATOM   2771  CA  PHE A 427      78.894  29.454-180.367  1.00 33.54           C  
ANISOU 2771  CA  PHE A 427     5137   3526   4081    266    967    716       C  
ATOM   2772  C   PHE A 427      79.832  29.638-179.186  1.00 34.21           C  
ANISOU 2772  C   PHE A 427     5314   3497   4189    136    937    630       C  
ATOM   2773  O   PHE A 427      79.745  30.638-178.471  1.00 37.39           O  
ANISOU 2773  O   PHE A 427     5886   3761   4561    126   1020    643       O  
ATOM   2774  CB  PHE A 427      77.658  28.660-179.957  1.00 38.50           C  
ANISOU 2774  CB  PHE A 427     5700   4229   4701    364    926    750       C  
ATOM   2775  CG  PHE A 427      76.842  29.346-178.901  1.00 38.07           C  
ANISOU 2775  CG  PHE A 427     5783   4066   4617    429   1008    793       C  
ATOM   2776  CD1 PHE A 427      76.040  30.435-179.227  1.00 39.89           C  
ANISOU 2776  CD1 PHE A 427     6104   4244   4809    548   1140    899       C  
ATOM   2777  CD2 PHE A 427      76.899  28.925-177.580  1.00 37.67           C  
ANISOU 2777  CD2 PHE A 427     5780   3958   4575    376    962    732       C  
ATOM   2778  CE1 PHE A 427      75.300  31.089-178.257  1.00 40.25           C  
ANISOU 2778  CE1 PHE A 427     6285   4179   4829    620   1235    938       C  
ATOM   2779  CE2 PHE A 427      76.158  29.569-176.600  1.00 37.59           C  
ANISOU 2779  CE2 PHE A 427     5911   3841   4529    436   1053    767       C  
ATOM   2780  CZ  PHE A 427      75.357  30.650-176.934  1.00 38.69           C  
ANISOU 2780  CZ  PHE A 427     6140   3925   4635    561   1195    868       C  
ATOM   2781  N   MET A 428      80.734  28.678-178.966  1.00 36.14           N  
ANISOU 2781  N   MET A 428     5452   3795   4484     37    819    543       N  
ATOM   2782  CA  MET A 428      81.719  28.841-177.897  1.00 37.76           C  
ANISOU 2782  CA  MET A 428     5728   3909   4710    -99    772    468       C  
ATOM   2783  C   MET A 428      82.627  30.034-178.168  1.00 41.37           C  
ANISOU 2783  C   MET A 428     6284   4273   5161   -194    848    464       C  
ATOM   2784  O   MET A 428      83.035  30.748-177.242  1.00 40.57           O  
ANISOU 2784  O   MET A 428     6326   4048   5040   -287    865    434       O  
ATOM   2785  CB  MET A 428      82.551  27.574-177.747  1.00 34.28           C  
ANISOU 2785  CB  MET A 428     5134   3558   4334   -171    630    392       C  
ATOM   2786  CG  MET A 428      81.752  26.345-177.335  1.00 36.50           C  
ANISOU 2786  CG  MET A 428     5335   3912   4621   -101    548    387       C  
ATOM   2787  SD  MET A 428      81.055  26.456-175.673  1.00 42.39           S  
ANISOU 2787  SD  MET A 428     6227   4557   5323   -100    539    385       S  
ATOM   2788  CE  MET A 428      82.527  26.736-174.669  1.00 40.84           C  
ANISOU 2788  CE  MET A 428     6097   4274   5145   -277    462    305       C  
ATOM   2789  N   LYS A 429      82.982  30.246-179.436  1.00 34.33           N  
ANISOU 2789  N   LYS A 429     5324   3438   4282   -186    893    490       N  
ATOM   2790  CA  LYS A 429      83.736  31.434-179.790  1.00 35.10           C  
ANISOU 2790  CA  LYS A 429     5524   3445   4369   -273    983    500       C  
ATOM   2791  C   LYS A 429      82.884  32.669-179.549  1.00 39.37           C  
ANISOU 2791  C   LYS A 429     6270   3849   4842   -201   1116    570       C  
ATOM   2792  O   LYS A 429      83.369  33.676-179.013  1.00 39.51           O  
ANISOU 2792  O   LYS A 429     6450   3725   4838   -298   1176    554       O  
ATOM   2793  CB  LYS A 429      84.202  31.323-181.249  1.00 40.66           C  
ANISOU 2793  CB  LYS A 429     6110   4247   5091   -266   1011    520       C  
ATOM   2794  CG  LYS A 429      84.778  32.590-181.836  1.00 56.04           C  
ANISOU 2794  CG  LYS A 429     8166   6108   7018   -333   1128    552       C  
ATOM   2795  CD  LYS A 429      86.083  32.990-181.178  1.00 61.58           C  
ANISOU 2795  CD  LYS A 429     8902   6736   7759   -522   1101    482       C  
ATOM   2796  CE  LYS A 429      86.696  34.169-181.927  1.00 75.59           C  
ANISOU 2796  CE  LYS A 429    10767   8437   9516   -600   1221    516       C  
ATOM   2797  NZ  LYS A 429      87.756  34.848-181.139  1.00 83.75           N  
ANISOU 2797  NZ  LYS A 429    11887   9367  10568   -794   1212    461       N  
ATOM   2798  N   HIS A 430      81.586  32.580-179.866  1.00 38.53           N  
ANISOU 2798  N   HIS A 430     6159   3780   4700    -34   1161    649       N  
ATOM   2799  CA  HIS A 430      80.678  33.686-179.572  1.00 43.89           C  
ANISOU 2799  CA  HIS A 430     7023   4330   5322     64   1294    726       C  
ATOM   2800  C   HIS A 430      80.642  33.987-178.080  1.00 36.26           C  
ANISOU 2800  C   HIS A 430     6213   3229   4336      9   1300    677       C  
ATOM   2801  O   HIS A 430      80.704  35.158-177.674  1.00 42.95           O  
ANISOU 2801  O   HIS A 430     7266   3910   5142    -19   1410    689       O  
ATOM   2802  CB  HIS A 430      79.265  33.376-180.069  1.00 40.70           C  
ANISOU 2802  CB  HIS A 430     6551   4018   4897    256   1322    824       C  
ATOM   2803  CG  HIS A 430      78.270  34.447-179.740  1.00 40.53           C  
ANISOU 2803  CG  HIS A 430     6700   3873   4827    383   1463    914       C  
ATOM   2804  ND1 HIS A 430      78.330  35.710-180.291  1.00 44.19           N  
ANISOU 2804  ND1 HIS A 430     7307   4224   5257    413   1597    982       N  
ATOM   2805  CD2 HIS A 430      77.206  34.455-178.902  1.00 46.26           C  
ANISOU 2805  CD2 HIS A 430     7481   4561   5534    492   1504    950       C  
ATOM   2806  CE1 HIS A 430      77.334  36.442-179.824  1.00 47.19           C  
ANISOU 2806  CE1 HIS A 430     7824   4502   5604    547   1714   1058       C  
ATOM   2807  NE2 HIS A 430      76.643  35.708-178.970  1.00 46.19           N  
ANISOU 2807  NE2 HIS A 430     7643   4421   5485    596   1663   1039       N  
ATOM   2808  N   LEU A 431      80.515  32.945-177.249  1.00 34.96           N  
ANISOU 2808  N   LEU A 431     5968   3125   4191     -8   1187    621       N  
ATOM   2809  CA  LEU A 431      80.513  33.169-175.807  1.00 35.91           C  
ANISOU 2809  CA  LEU A 431     6241   3122   4279    -70   1184    571       C  
ATOM   2810  C   LEU A 431      81.758  33.926-175.371  1.00 41.77           C  
ANISOU 2810  C   LEU A 431     7112   3746   5013   -259   1182    502       C  
ATOM   2811  O   LEU A 431      81.676  34.850-174.560  1.00 40.51           O  
ANISOU 2811  O   LEU A 431     7173   3422   4796   -298   1265    491       O  
ATOM   2812  CB  LEU A 431      80.416  31.837-175.060  1.00 39.95           C  
ANISOU 2812  CB  LEU A 431     6633   3730   4817    -86   1044    518       C  
ATOM   2813  CG  LEU A 431      79.039  31.179-175.096  1.00 40.32           C  
ANISOU 2813  CG  LEU A 431     6602   3861   4857     80   1056    581       C  
ATOM   2814  CD1 LEU A 431      79.053  29.831-174.381  1.00 41.33           C  
ANISOU 2814  CD1 LEU A 431     6618   4074   5010     45    916    525       C  
ATOM   2815  CD2 LEU A 431      78.021  32.115-174.475  1.00 39.10           C  
ANISOU 2815  CD2 LEU A 431     6633   3579   4643    183   1203    640       C  
ATOM   2816  N   GLU A 432      82.918  33.555-175.917  1.00 44.00           N  
ANISOU 2816  N   GLU A 432     7260   4108   5349   -380   1094    456       N  
ATOM   2817  CA  GLU A 432      84.173  34.197-175.545  1.00 52.68           C  
ANISOU 2817  CA  GLU A 432     8445   5120   6450   -578   1075    394       C  
ATOM   2818  C   GLU A 432      84.208  35.653-175.999  1.00 55.24           C  
ANISOU 2818  C   GLU A 432     8957   5300   6732   -595   1234    438       C  
ATOM   2819  O   GLU A 432      84.649  36.530-175.243  1.00 51.16           O  
ANISOU 2819  O   GLU A 432     8636   4631   6170   -723   1273    400       O  
ATOM   2820  CB  GLU A 432      85.338  33.406-176.143  1.00 57.44           C  
ANISOU 2820  CB  GLU A 432     8826   5863   7134   -679    957    350       C  
ATOM   2821  CG  GLU A 432      86.696  33.665-175.506  1.00 75.38           C  
ANISOU 2821  CG  GLU A 432    11120   8094   9426   -898    879    277       C  
ATOM   2822  CD  GLU A 432      87.741  32.643-175.939  1.00 89.16           C  
ANISOU 2822  CD  GLU A 432    12614   9998  11265   -965    750    239       C  
ATOM   2823  OE1 GLU A 432      87.353  31.498-176.263  1.00 91.26           O  
ANISOU 2823  OE1 GLU A 432    12717  10388  11570   -851    687    245       O  
ATOM   2824  OE2 GLU A 432      88.945  32.985-175.964  1.00 93.46           O  
ANISOU 2824  OE2 GLU A 432    13124  10541  11845  -1132    718    205       O  
ATOM   2825  N   ASN A 433      83.738  35.926-177.226  1.00 45.25           N  
ANISOU 2825  N   ASN A 433     7646   4076   5470   -471   1326    519       N  
ATOM   2826  CA  ASN A 433      83.642  37.301-177.724  1.00 45.77           C  
ANISOU 2826  CA  ASN A 433     7899   4000   5493   -459   1488    579       C  
ATOM   2827  C   ASN A 433      82.730  38.142-176.836  1.00 49.37           C  
ANISOU 2827  C   ASN A 433     8602   4279   5878   -381   1605    607       C  
ATOM   2828  O   ASN A 433      83.040  39.295-176.511  1.00 51.09           O  
ANISOU 2828  O   ASN A 433     9046   4314   6050   -466   1707    598       O  
ATOM   2829  CB  ASN A 433      83.102  37.317-179.156  1.00 50.35           C  
ANISOU 2829  CB  ASN A 433     8379   4671   6079   -309   1554    676       C  
ATOM   2830  CG  ASN A 433      84.063  36.726-180.169  1.00 50.24           C  
ANISOU 2830  CG  ASN A 433     8166   4803   6121   -391   1482    652       C  
ATOM   2831  OD1 ASN A 433      85.251  36.549-179.899  1.00 51.26           O  
ANISOU 2831  OD1 ASN A 433     8242   4944   6291   -568   1408    573       O  
ATOM   2832  ND2 ASN A 433      83.550  36.441-181.360  1.00 51.10           N  
ANISOU 2832  ND2 ASN A 433     8163   5024   6228   -261   1507    725       N  
ATOM   2833  N   GLU A 434      81.578  37.584-176.460  1.00 45.00           N  
ANISOU 2833  N   GLU A 434     8013   3772   5314   -216   1602    642       N  
ATOM   2834  CA  GLU A 434      80.598  38.349-175.704  1.00 46.11           C  
ANISOU 2834  CA  GLU A 434     8372   3755   5392   -108   1735    682       C  
ATOM   2835  C   GLU A 434      81.060  38.600-174.277  1.00 49.03           C  
ANISOU 2835  C   GLU A 434     8927   3986   5716   -259   1714    584       C  
ATOM   2836  O   GLU A 434      80.708  39.632-173.691  1.00 52.62           O  
ANISOU 2836  O   GLU A 434     9597   4291   6106   -235   1830    574       O  
ATOM   2837  CB  GLU A 434      79.257  37.619-175.708  1.00 47.03           C  
ANISOU 2837  CB  GLU A 434     8372   3982   5517    102   1735    751       C  
ATOM   2838  CG  GLU A 434      78.547  37.690-177.035  1.00 51.79           C  
ANISOU 2838  CG  GLU A 434     8858   4682   6137    273   1792    869       C  
ATOM   2839  CD  GLU A 434      78.101  39.095-177.369  1.00 53.95           C  
ANISOU 2839  CD  GLU A 434     9331   4800   6369    373   1976    955       C  
ATOM   2840  OE1 GLU A 434      76.940  39.434-177.069  1.00 55.25           O  
ANISOU 2840  OE1 GLU A 434     9519   4959   6513    548   2052   1000       O  
ATOM   2841  OE2 GLU A 434      78.916  39.865-177.916  1.00 56.94           O  
ANISOU 2841  OE2 GLU A 434     9780   5115   6741    276   2010    938       O  
ATOM   2842  N   GLN A 435      81.841  37.674-173.711  1.00 47.19           N  
ANISOU 2842  N   GLN A 435     8574   3845   5511   -405   1543    493       N  
ATOM   2843  CA  GLN A 435      82.399  37.877-172.375  1.00 51.17           C  
ANISOU 2843  CA  GLN A 435     9246   4233   5962   -575   1497    400       C  
ATOM   2844  C   GLN A 435      83.223  39.155-172.318  1.00 60.13           C  
ANISOU 2844  C   GLN A 435    10599   5192   7054   -740   1577    369       C  
ATOM   2845  O   GLN A 435      83.071  39.973-171.402  1.00 53.35           O  
ANISOU 2845  O   GLN A 435     9932   4229   6112   -767   1629    315       O  
ATOM   2846  CB  GLN A 435      83.257  36.673-171.972  1.00 52.31           C  
ANISOU 2846  CB  GLN A 435     9195   4526   6155   -708   1286    323       C  
ATOM   2847  CG  GLN A 435      83.734  36.691-170.518  1.00 49.59           C  
ANISOU 2847  CG  GLN A 435     9002   4091   5748   -873   1208    235       C  
ATOM   2848  CD  GLN A 435      82.585  36.588-169.536  1.00 53.73           C  
ANISOU 2848  CD  GLN A 435     9666   4545   6202   -753   1270    244       C  
ATOM   2849  OE1 GLN A 435      81.549  35.993-169.843  1.00 49.70           O  
ANISOU 2849  OE1 GLN A 435     9043   4121   5718   -560   1302    306       O  
ATOM   2850  NE2 GLN A 435      82.753  37.180-168.351  1.00 53.91           N  
ANISOU 2850  NE2 GLN A 435     9941   4410   6131   -872   1294    183       N  
ATOM   2851  N   LYS A 436      84.099  39.352-173.298  1.00 58.41           N  
ANISOU 2851  N   LYS A 436    10278   5027   6887   -831   1557    376       N  
ATOM   2852  CA  LYS A 436      84.953  40.527-173.263  1.00 59.60           C  
ANISOU 2852  CA  LYS A 436    10587   5057   7001   -998   1607    334       C  
ATOM   2853  C   LYS A 436      84.216  41.776-173.723  1.00 57.88           C  
ANISOU 2853  C   LYS A 436    10510   4752   6731   -845   1781    384       C  
ATOM   2854  O   LYS A 436      84.523  42.878-173.254  1.00 60.68           O  
ANISOU 2854  O   LYS A 436    11047   4993   7017   -930   1838    331       O  
ATOM   2855  CB  LYS A 436      86.206  40.273-174.101  1.00 66.20           C  
ANISOU 2855  CB  LYS A 436    11262   5976   7913  -1166   1531    325       C  
ATOM   2856  CG  LYS A 436      85.928  39.723-175.477  1.00 73.73           C  
ANISOU 2856  CG  LYS A 436    11985   7093   8936  -1012   1541    401       C  
ATOM   2857  CD  LYS A 436      86.547  40.622-176.545  1.00 83.89           C  
ANISOU 2857  CD  LYS A 436    13308   8332  10233  -1082   1641    440       C  
ATOM   2858  CE  LYS A 436      86.129  40.217-177.952  1.00 87.86           C  
ANISOU 2858  CE  LYS A 436    13627   8976  10779   -913   1675    526       C  
ATOM   2859  NZ  LYS A 436      84.753  40.677-178.298  1.00 88.65           N  
ANISOU 2859  NZ  LYS A 436    13840   9010  10831   -678   1812    628       N  
ATOM   2860  N   ALA A 437      83.221  41.634-174.603  1.00 53.80           N  
ANISOU 2860  N   ALA A 437     9914   4288   6241   -619   1864    486       N  
ATOM   2861  CA  ALA A 437      82.510  42.809-175.101  1.00 61.26           C  
ANISOU 2861  CA  ALA A 437    10975   5158   7145   -464   2022    541       C  
ATOM   2862  C   ALA A 437      81.458  43.303-174.108  1.00 64.49           C  
ANISOU 2862  C   ALA A 437    11540   5484   7481   -329   2111    525       C  
ATOM   2863  O   ALA A 437      81.382  44.505-173.828  1.00 58.90           O  
ANISOU 2863  O   ALA A 437    11024   4649   6705   -327   2223    498       O  
ATOM   2864  CB  ALA A 437      81.872  42.503-176.457  1.00 54.94           C  
ANISOU 2864  CB  ALA A 437    10019   4462   6395   -280   2065    664       C  
ATOM   2865  N   ARG A 438      80.636  42.394-173.566  1.00 58.99           N  
ANISOU 2865  N   ARG A 438    10766   4854   6794   -216   2075    541       N  
ATOM   2866  CA  ARG A 438      79.505  42.772-172.719  1.00 60.31           C  
ANISOU 2866  CA  ARG A 438    11053   4962   6899    -62   2179    541       C  
ATOM   2867  C   ARG A 438      79.508  42.137-171.333  1.00 60.38           C  
ANISOU 2867  C   ARG A 438    11115   4959   6866   -144   2104    460       C  
ATOM   2868  O   ARG A 438      78.608  42.432-170.535  1.00 58.59           O  
ANISOU 2868  O   ARG A 438    11000   4681   6579    -30   2199    454       O  
ATOM   2869  CB  ARG A 438      78.174  42.420-173.401  1.00 61.19           C  
ANISOU 2869  CB  ARG A 438    11025   5169   7054    203   2244    661       C  
ATOM   2870  CG  ARG A 438      77.765  43.349-174.516  1.00 62.63           C  
ANISOU 2870  CG  ARG A 438    11213   5337   7245    343   2362    749       C  
ATOM   2871  CD  ARG A 438      76.250  43.369-174.670  1.00 58.99           C  
ANISOU 2871  CD  ARG A 438    10691   4930   6794    612   2462    849       C  
ATOM   2872  NE  ARG A 438      75.701  42.050-174.965  1.00 55.98           N  
ANISOU 2872  NE  ARG A 438    10082   4716   6472    696   2365    914       N  
ATOM   2873  CZ  ARG A 438      74.444  41.847-175.346  1.00 60.57           C  
ANISOU 2873  CZ  ARG A 438    10542   5392   7078    916   2416   1020       C  
ATOM   2874  NH1 ARG A 438      73.621  42.878-175.469  1.00 58.23           N  
ANISOU 2874  NH1 ARG A 438    10328   5038   6758   1080   2568   1076       N  
ATOM   2875  NH2 ARG A 438      74.010  40.622-175.607  1.00 58.98           N  
ANISOU 2875  NH2 ARG A 438    10136   5348   6925    969   2318   1076       N  
ATOM   2876  N   GLY A 439      80.465  41.268-171.024  1.00 59.51           N  
ANISOU 2876  N   GLY A 439    10930   4900   6784   -333   1941    403       N  
ATOM   2877  CA  GLY A 439      80.500  40.659-169.711  1.00 54.03           C  
ANISOU 2877  CA  GLY A 439    10290   4197   6042   -416   1858    329       C  
ATOM   2878  C   GLY A 439      79.601  39.461-169.528  1.00 53.94           C  
ANISOU 2878  C   GLY A 439    10139   4285   6070   -277   1818    378       C  
ATOM   2879  O   GLY A 439      79.243  39.141-168.395  1.00 54.63           O  
ANISOU 2879  O   GLY A 439    10305   4351   6102   -283   1802    333       O  
ATOM   2880  N   GLY A 440      79.224  38.780-170.594  1.00 52.73           N  
ANISOU 2880  N   GLY A 440     9789   4245   6003   -157   1802    470       N  
ATOM   2881  CA  GLY A 440      78.403  37.591-170.472  1.00 47.24           C  
ANISOU 2881  CA  GLY A 440     8951   3654   5345    -38   1755    522       C  
ATOM   2882  C   GLY A 440      77.477  37.470-171.667  1.00 53.06           C  
ANISOU 2882  C   GLY A 440     9532   4492   6136    174   1825    648       C  
ATOM   2883  O   GLY A 440      77.521  38.251-172.601  1.00 52.28           O  
ANISOU 2883  O   GLY A 440     9433   4382   6048    224   1899    694       O  
ATOM   2884  N   CYS A 441      76.622  36.468-171.602  1.00 50.21           N  
ANISOU 2884  N   CYS A 441     9011   4262   5805    292   1781    691       N  
ATOM   2885  CA  CYS A 441      75.787  36.164-172.750  1.00 50.16           C  
ANISOU 2885  CA  CYS A 441     8809   4402   5849    470   1801    802       C  
ATOM   2886  C   CYS A 441      74.587  35.352-172.284  1.00 47.56           C  
ANISOU 2886  C   CYS A 441     8373   4170   5527    608   1799    848       C  
ATOM   2887  O   CYS A 441      74.762  34.273-171.710  1.00 46.57           O  
ANISOU 2887  O   CYS A 441     8147   4134   5415    530   1666    783       O  
ATOM   2888  CB  CYS A 441      76.600  35.398-173.806  1.00 46.96           C  
ANISOU 2888  CB  CYS A 441     8177   4162   5505    386   1649    780       C  
ATOM   2889  SG  CYS A 441      75.647  34.877-175.258  1.00 49.98           S  
ANISOU 2889  SG  CYS A 441     8313   4744   5933    573   1642    905       S  
ATOM   2890  N   PRO A 442      73.363  35.832-172.500  1.00 46.60           N  
ANISOU 2890  N   PRO A 442     8267   4038   5401    812   1944    963       N  
ATOM   2891  CA  PRO A 442      72.183  35.030-172.145  1.00 43.97           C  
ANISOU 2891  CA  PRO A 442     7801   3822   5085    940   1942   1018       C  
ATOM   2892  C   PRO A 442      72.099  33.805-173.038  1.00 44.55           C  
ANISOU 2892  C   PRO A 442     7581   4127   5216    938   1780   1037       C  
ATOM   2893  O   PRO A 442      72.072  33.908-174.269  1.00 41.01           O  
ANISOU 2893  O   PRO A 442     7016   3770   4796    991   1765   1102       O  
ATOM   2894  CB  PRO A 442      71.014  35.989-172.384  1.00 45.21           C  
ANISOU 2894  CB  PRO A 442     7985   3957   5235   1150   2116   1117       C  
ATOM   2895  CG  PRO A 442      71.524  36.940-173.403  1.00 48.69           C  
ANISOU 2895  CG  PRO A 442     8460   4361   5679   1150   2151   1134       C  
ATOM   2896  CD  PRO A 442      73.000  37.100-173.151  1.00 50.06           C  
ANISOU 2896  CD  PRO A 442     8768   4423   5829    927   2080   1017       C  
ATOM   2897  N   ALA A 443      72.066  32.641-172.419  1.00 44.00           N  
ANISOU 2897  N   ALA A 443     7409   4149   5159    872   1661    979       N  
ATOM   2898  CA  ALA A 443      72.060  31.423-173.200  1.00 38.61           C  
ANISOU 2898  CA  ALA A 443     6475   3669   4528    851   1507    981       C  
ATOM   2899  C   ALA A 443      71.173  30.410-172.502  1.00 39.73           C  
ANISOU 2899  C   ALA A 443     6517   3901   4677    889   1468    992       C  
ATOM   2900  O   ALA A 443      71.185  30.301-171.273  1.00 39.58           O  
ANISOU 2900  O   ALA A 443     6620   3795   4626    841   1485    937       O  
ATOM   2901  CB  ALA A 443      73.481  30.887-173.402  1.00 40.34           C  
ANISOU 2901  CB  ALA A 443     6654   3907   4767    667   1354    869       C  
ATOM   2902  N   ASP A 444      70.388  29.701-173.291  1.00 42.41           N  
ANISOU 2902  N   ASP A 444     6646   4415   5052    969   1420   1065       N  
ATOM   2903  CA  ASP A 444      69.414  28.742-172.795  1.00 37.85           C  
ANISOU 2903  CA  ASP A 444     5951   3943   4487   1010   1390   1094       C  
ATOM   2904  C   ASP A 444      69.981  27.354-173.096  1.00 37.53           C  
ANISOU 2904  C   ASP A 444     5755   4026   4477    884   1199   1018       C  
ATOM   2905  O   ASP A 444      69.853  26.847-174.217  1.00 35.41           O  
ANISOU 2905  O   ASP A 444     5319   3898   4236    897   1124   1050       O  
ATOM   2906  CB  ASP A 444      68.052  29.003-173.436  1.00 42.07           C  
ANISOU 2906  CB  ASP A 444     6364   4584   5037   1189   1479   1242       C  
ATOM   2907  CG  ASP A 444      66.942  28.147-172.862  1.00 48.69           C  
ANISOU 2907  CG  ASP A 444     7084   5527   5889   1235   1474   1286       C  
ATOM   2908  OD1 ASP A 444      67.225  27.046-172.343  1.00 51.50           O  
ANISOU 2908  OD1 ASP A 444     7394   5922   6250   1118   1358   1205       O  
ATOM   2909  OD2 ASP A 444      65.771  28.573-172.949  1.00 47.03           O  
ANISOU 2909  OD2 ASP A 444     6819   5362   5687   1391   1590   1409       O  
ATOM   2910  N   TRP A 445      70.576  26.732-172.066  1.00 36.85           N  
ANISOU 2910  N   TRP A 445     5736   3884   4382    766   1125    920       N  
ATOM   2911  CA  TRP A 445      71.343  25.497-172.253  1.00 31.72           C  
ANISOU 2911  CA  TRP A 445     4974   3313   3763    643    951    837       C  
ATOM   2912  C   TRP A 445      70.551  24.448-173.015  1.00 33.33           C  
ANISOU 2912  C   TRP A 445     4970   3694   4000    680    879    885       C  
ATOM   2913  O   TRP A 445      71.072  23.816-173.938  1.00 34.65           O  
ANISOU 2913  O   TRP A 445     5022   3948   4194    629    774    853       O  
ATOM   2914  CB  TRP A 445      71.780  24.948-170.879  1.00 31.56           C  
ANISOU 2914  CB  TRP A 445     5054   3213   3722    541    894    754       C  
ATOM   2915  CG  TRP A 445      72.798  23.818-170.923  1.00 33.36           C  
ANISOU 2915  CG  TRP A 445     5204   3487   3984    414    721    664       C  
ATOM   2916  CD1 TRP A 445      74.160  23.936-170.816  1.00 37.54           C  
ANISOU 2916  CD1 TRP A 445     5790   3953   4522    302    645    582       C  
ATOM   2917  CD2 TRP A 445      72.531  22.419-171.039  1.00 29.18           C  
ANISOU 2917  CD2 TRP A 445     4531   3070   3486    389    609    653       C  
ATOM   2918  NE1 TRP A 445      74.746  22.703-170.871  1.00 33.94           N  
ANISOU 2918  NE1 TRP A 445     5227   3564   4106    227    498    526       N  
ATOM   2919  CE2 TRP A 445      73.772  21.752-171.009  1.00 30.14           C  
ANISOU 2919  CE2 TRP A 445     4633   3182   3637    277    476    565       C  
ATOM   2920  CE3 TRP A 445      71.364  21.664-171.196  1.00 31.12           C  
ANISOU 2920  CE3 TRP A 445     4660   3424   3742    446    610    712       C  
ATOM   2921  CZ2 TRP A 445      73.882  20.365-171.120  1.00 27.71           C  
ANISOU 2921  CZ2 TRP A 445     4211   2953   3365    234    353    532       C  
ATOM   2922  CZ3 TRP A 445      71.474  20.286-171.302  1.00 28.84           C  
ANISOU 2922  CZ3 TRP A 445     4262   3214   3482    383    483    674       C  
ATOM   2923  CH2 TRP A 445      72.724  19.652-171.252  1.00 31.52           C  
ANISOU 2923  CH2 TRP A 445     4603   3525   3848    283    360    583       C  
ATOM   2924  N   ALA A 446      69.278  24.268-172.648  1.00 33.16           N  
ANISOU 2924  N   ALA A 446     4901   3728   3972    767    942    963       N  
ATOM   2925  CA  ALA A 446      68.467  23.205-173.229  1.00 36.13           C  
ANISOU 2925  CA  ALA A 446     5083   4272   4373    779    866   1007       C  
ATOM   2926  C   ALA A 446      68.217  23.412-174.717  1.00 30.14           C  
ANISOU 2926  C   ALA A 446     4195   3633   3625    836    851   1074       C  
ATOM   2927  O   ALA A 446      67.918  22.448-175.427  1.00 40.91           O  
ANISOU 2927  O   ALA A 446     5407   5136   5003    802    751   1079       O  
ATOM   2928  CB  ALA A 446      67.132  23.102-172.491  1.00 39.93           C  
ANISOU 2928  CB  ALA A 446     5537   4789   4848    859    953   1089       C  
ATOM   2929  N   TRP A 447      68.306  24.647-175.200  1.00 36.80           N  
ANISOU 2929  N   TRP A 447     5106   4422   4454    917    950   1127       N  
ATOM   2930  CA  TRP A 447      68.127  24.911-176.625  1.00 31.42           C  
ANISOU 2930  CA  TRP A 447     4319   3849   3771    971    936   1195       C  
ATOM   2931  C   TRP A 447      69.439  25.025-177.385  1.00 36.90           C  
ANISOU 2931  C   TRP A 447     5048   4507   4464    885    875   1116       C  
ATOM   2932  O   TRP A 447      69.450  24.791-178.600  1.00 41.54           O  
ANISOU 2932  O   TRP A 447     5531   5207   5045    885    820   1140       O  
ATOM   2933  CB  TRP A 447      67.306  26.191-176.830  1.00 38.25           C  
ANISOU 2933  CB  TRP A 447     5222   4689   4622   1133   1087   1326       C  
ATOM   2934  CG  TRP A 447      65.824  25.989-176.641  1.00 43.92           C  
ANISOU 2934  CG  TRP A 447     5819   5520   5350   1242   1133   1444       C  
ATOM   2935  CD1 TRP A 447      65.188  25.561-175.508  1.00 49.91           C  
ANISOU 2935  CD1 TRP A 447     6580   6264   6118   1248   1169   1443       C  
ATOM   2936  CD2 TRP A 447      64.799  26.209-177.619  1.00 53.77           C  
ANISOU 2936  CD2 TRP A 447     6916   6919   6598   1358   1147   1586       C  
ATOM   2937  NE1 TRP A 447      63.830  25.502-175.724  1.00 48.28           N  
ANISOU 2937  NE1 TRP A 447     6223   6195   5926   1359   1211   1576       N  
ATOM   2938  CE2 TRP A 447      63.567  25.894-177.010  1.00 52.29           C  
ANISOU 2938  CE2 TRP A 447     6629   6809   6429   1429   1192   1667       C  
ATOM   2939  CE3 TRP A 447      64.801  26.656-178.951  1.00 63.27           C  
ANISOU 2939  CE3 TRP A 447     8056   8202   7781   1408   1126   1658       C  
ATOM   2940  CZ2 TRP A 447      62.347  26.009-177.685  1.00 64.40           C  
ANISOU 2940  CZ2 TRP A 447     7989   8508   7972   1548   1208   1822       C  
ATOM   2941  CZ3 TRP A 447      63.584  26.766-179.622  1.00 64.43           C  
ANISOU 2941  CZ3 TRP A 447     8042   8510   7927   1527   1135   1812       C  
ATOM   2942  CH2 TRP A 447      62.376  26.442-178.986  1.00 66.12           C  
ANISOU 2942  CH2 TRP A 447     8145   8808   8169   1595   1173   1894       C  
ATOM   2943  N   ILE A 448      70.535  25.358-176.707  1.00 34.52           N  
ANISOU 2943  N   ILE A 448     4888   4061   4165    805    884   1023       N  
ATOM   2944  CA  ILE A 448      71.830  25.476-177.373  1.00 38.42           C  
ANISOU 2944  CA  ILE A 448     5405   4526   4668    717    834    949       C  
ATOM   2945  C   ILE A 448      72.433  24.102-177.647  1.00 36.63           C  
ANISOU 2945  C   ILE A 448     5066   4383   4469    611    686    860       C  
ATOM   2946  O   ILE A 448      72.957  23.843-178.741  1.00 32.46           O  
ANISOU 2946  O   ILE A 448     4464   3923   3945    580    636    840       O  
ATOM   2947  CB  ILE A 448      72.766  26.350-176.526  1.00 33.20           C  
ANISOU 2947  CB  ILE A 448     4927   3688   4000    660    892    889       C  
ATOM   2948  CG1 ILE A 448      72.243  27.799-176.469  1.00 35.57           C  
ANISOU 2948  CG1 ILE A 448     5358   3888   4268    770   1054    977       C  
ATOM   2949  CG2 ILE A 448      74.193  26.282-177.054  1.00 35.03           C  
ANISOU 2949  CG2 ILE A 448     5158   3901   4253    545    824    803       C  
ATOM   2950  CD1 ILE A 448      72.196  28.508-177.820  1.00 36.00           C  
ANISOU 2950  CD1 ILE A 448     5379   3987   4311    838   1103   1054       C  
ATOM   2951  N   VAL A 449      72.367  23.204-176.669  1.00 33.25           N  
ANISOU 2951  N   VAL A 449     4633   3945   4057    559    622    808       N  
ATOM   2952  CA  VAL A 449      72.829  21.833-176.828  1.00 28.58           C  
ANISOU 2952  CA  VAL A 449     3945   3420   3494    472    490    731       C  
ATOM   2953  C   VAL A 449      71.968  21.130-177.874  1.00 37.71           C  
ANISOU 2953  C   VAL A 449     4956   4732   4641    506    448    781       C  
ATOM   2954  O   VAL A 449      70.731  21.103-177.765  1.00 33.21           O  
ANISOU 2954  O   VAL A 449     4336   4228   4055    572    481    864       O  
ATOM   2955  CB  VAL A 449      72.801  21.087-175.483  1.00 35.63           C  
ANISOU 2955  CB  VAL A 449     4880   4259   4397    420    441    683       C  
ATOM   2956  CG1 VAL A 449      73.227  19.617-175.669  1.00 27.47           C  
ANISOU 2956  CG1 VAL A 449     3754   3287   3397    343    309    611       C  
ATOM   2957  CG2 VAL A 449      73.722  21.787-174.523  1.00 33.20           C  
ANISOU 2957  CG2 VAL A 449     4721   3807   4086    370    467    631       C  
ATOM   2958  N   PRO A 450      72.580  20.568-178.902  1.00 30.94           N  
ANISOU 2958  N   PRO A 450     4028   3939   3791    458    379    734       N  
ATOM   2959  CA  PRO A 450      71.815  19.999-180.020  1.00 32.36           C  
ANISOU 2959  CA  PRO A 450     4087   4265   3942    477    338    779       C  
ATOM   2960  C   PRO A 450      71.081  18.728-179.619  1.00 31.96           C  
ANISOU 2960  C   PRO A 450     3964   4281   3900    438    259    766       C  
ATOM   2961  O   PRO A 450      71.404  18.095-178.589  1.00 34.03           O  
ANISOU 2961  O   PRO A 450     4266   4473   4193    386    221    705       O  
ATOM   2962  CB  PRO A 450      72.893  19.732-181.086  1.00 37.93           C  
ANISOU 2962  CB  PRO A 450     4771   4990   4649    422    296    709       C  
ATOM   2963  CG  PRO A 450      74.189  19.721-180.342  1.00 47.24           C  
ANISOU 2963  CG  PRO A 450     6024   6049   5878    359    283    616       C  
ATOM   2964  CD  PRO A 450      74.025  20.638-179.159  1.00 32.11           C  
ANISOU 2964  CD  PRO A 450     4211   4025   3964    390    353    648       C  
ATOM   2965  N   PRO A 451      70.059  18.340-180.394  1.00 38.29           N  
ANISOU 2965  N   PRO A 451     4660   5220   4668    456    231    831       N  
ATOM   2966  CA  PRO A 451      69.185  17.224-180.008  1.00 35.94           C  
ANISOU 2966  CA  PRO A 451     4290   4991   4372    413    167    836       C  
ATOM   2967  C   PRO A 451      69.756  15.844-180.278  1.00 38.39           C  
ANISOU 2967  C   PRO A 451     4582   5312   4694    307     60    730       C  
ATOM   2968  O   PRO A 451      69.121  14.850-179.907  1.00 41.53           O  
ANISOU 2968  O   PRO A 451     4938   5748   5095    255      6    724       O  
ATOM   2969  CB  PRO A 451      67.931  17.472-180.860  1.00 35.28           C  
ANISOU 2969  CB  PRO A 451     4096   5062   4246    466    175    953       C  
ATOM   2970  CG  PRO A 451      68.494  18.091-182.125  1.00 38.29           C  
ANISOU 2970  CG  PRO A 451     4484   5474   4593    488    184    959       C  
ATOM   2971  CD  PRO A 451      69.574  19.017-181.621  1.00 32.96           C  
ANISOU 2971  CD  PRO A 451     3931   4646   3946    517    261    918       C  
ATOM   2972  N   ILE A 452      70.905  15.752-180.936  1.00 33.17           N  
ANISOU 2972  N   ILE A 452     3950   4614   4038    275     38    651       N  
ATOM   2973  CA  ILE A 452      71.674  14.519-180.999  1.00 30.23           C  
ANISOU 2973  CA  ILE A 452     3585   4211   3691    193    -42    542       C  
ATOM   2974  C   ILE A 452      73.091  14.842-180.558  1.00 32.29           C  
ANISOU 2974  C   ILE A 452     3917   4350   4002    189    -25    469       C  
ATOM   2975  O   ILE A 452      73.564  15.974-180.703  1.00 36.69           O  
ANISOU 2975  O   ILE A 452     4510   4872   4558    230     41    492       O  
ATOM   2976  CB  ILE A 452      71.705  13.852-182.401  1.00 34.41           C  
ANISOU 2976  CB  ILE A 452     4064   4833   4176    149    -90    508       C  
ATOM   2977  CG1 ILE A 452      72.187  14.829-183.469  1.00 40.43           C  
ANISOU 2977  CG1 ILE A 452     4831   5625   4906    192    -36    530       C  
ATOM   2978  CG2 ILE A 452      70.358  13.232-182.751  1.00 41.17           C  
ANISOU 2978  CG2 ILE A 452     4845   5814   4984    117   -139    564       C  
ATOM   2979  CD1 ILE A 452      72.664  14.117-184.731  1.00 43.84           C  
ANISOU 2979  CD1 ILE A 452     5249   6109   5299    140    -75    462       C  
ATOM   2980  N   SER A 453      73.755  13.839-179.985  1.00 33.00           N  
ANISOU 2980  N   SER A 453     4028   4375   4136    136    -87    388       N  
ATOM   2981  CA  SER A 453      75.175  13.923-179.642  1.00 34.34           C  
ANISOU 2981  CA  SER A 453     4240   4448   4359    122    -94    317       C  
ATOM   2982  C   SER A 453      75.499  15.109-178.729  1.00 32.03           C  
ANISOU 2982  C   SER A 453     4014   4075   4080    148    -40    348       C  
ATOM   2983  O   SER A 453      76.577  15.694-178.822  1.00 33.73           O  
ANISOU 2983  O   SER A 453     4252   4241   4323    141    -20    316       O  
ATOM   2984  CB  SER A 453      76.031  13.970-180.904  1.00 36.24           C  
ANISOU 2984  CB  SER A 453     4450   4720   4600    119    -80    272       C  
ATOM   2985  OG  SER A 453      75.816  12.802-181.682  1.00 39.94           O  
ANISOU 2985  OG  SER A 453     4882   5244   5050     86   -129    228       O  
ATOM   2986  N   GLY A 454      74.585  15.454-177.831  1.00 34.00           N  
ANISOU 2986  N   GLY A 454     4301   4310   4309    171    -12    407       N  
ATOM   2987  CA  GLY A 454      74.790  16.586-176.943  1.00 36.86           C  
ANISOU 2987  CA  GLY A 454     4752   4585   4668    192     50    433       C  
ATOM   2988  C   GLY A 454      76.168  16.680-176.310  1.00 31.02           C  
ANISOU 2988  C   GLY A 454     4067   3748   3970    142     14    364       C  
ATOM   2989  O   GLY A 454      76.853  17.694-176.481  1.00 34.27           O  
ANISOU 2989  O   GLY A 454     4518   4120   4385    141     63    363       O  
ATOM   2990  N   SER A 455      76.598  15.640-175.592  1.00 32.21           N  
ANISOU 2990  N   SER A 455     4221   3865   4155     97    -72    313       N  
ATOM   2991  CA  SER A 455      77.858  15.758-174.867  1.00 29.73           C  
ANISOU 2991  CA  SER A 455     3950   3468   3878     49   -118    262       C  
ATOM   2992  C   SER A 455      79.072  15.651-175.771  1.00 30.53           C  
ANISOU 2992  C   SER A 455     3982   3588   4030     31   -139    211       C  
ATOM   2993  O   SER A 455      80.192  15.834-175.295  1.00 29.92           O  
ANISOU 2993  O   SER A 455     3918   3459   3992    -10   -176    176       O  
ATOM   2994  CB  SER A 455      77.950  14.696-173.754  1.00 26.66           C  
ANISOU 2994  CB  SER A 455     3589   3033   3506     15   -208    237       C  
ATOM   2995  OG  SER A 455      78.140  13.393-174.283  1.00 29.09           O  
ANISOU 2995  OG  SER A 455     3822   3379   3853     10   -275    198       O  
ATOM   2996  N   LEU A 456      78.884  15.326-177.057  1.00 32.86           N  
ANISOU 2996  N   LEU A 456     4202   3961   4323     57   -119    206       N  
ATOM   2997  CA  LEU A 456      79.985  15.394-178.003  1.00 25.52           C  
ANISOU 2997  CA  LEU A 456     3213   3050   3432     47   -109    163       C  
ATOM   2998  C   LEU A 456      80.284  16.824-178.458  1.00 30.62           C  
ANISOU 2998  C   LEU A 456     3887   3690   4058     50    -22    194       C  
ATOM   2999  O   LEU A 456      81.283  17.046-179.159  1.00 34.36           O  
ANISOU 2999  O   LEU A 456     4317   4174   4565     32     -2    163       O  
ATOM   3000  CB  LEU A 456      79.673  14.522-179.237  1.00 27.62           C  
ANISOU 3000  CB  LEU A 456     3412   3397   3687     68   -111    142       C  
ATOM   3001  CG  LEU A 456      79.288  13.067-178.929  1.00 28.72           C  
ANISOU 3001  CG  LEU A 456     3538   3536   3839     59   -187    110       C  
ATOM   3002  CD1 LEU A 456      79.225  12.244-180.228  1.00 30.63           C  
ANISOU 3002  CD1 LEU A 456     3729   3841   4066     64   -184     72       C  
ATOM   3003  CD2 LEU A 456      80.247  12.438-177.923  1.00 33.62           C  
ANISOU 3003  CD2 LEU A 456     4165   4079   4528     38   -260     68       C  
ATOM   3004  N   THR A 457      79.441  17.785-178.099  1.00 31.22           N  
ANISOU 3004  N   THR A 457     4035   3745   4082     75     39    256       N  
ATOM   3005  CA  THR A 457      79.684  19.165-178.475  1.00 32.86           C  
ANISOU 3005  CA  THR A 457     4292   3927   4267     79    129    290       C  
ATOM   3006  C   THR A 457      80.193  19.949-177.271  1.00 33.68           C  
ANISOU 3006  C   THR A 457     4495   3926   4377     31    134    284       C  
ATOM   3007  O   THR A 457      79.927  19.575-176.131  1.00 34.89           O  
ANISOU 3007  O   THR A 457     4695   4034   4526     16     85    277       O  
ATOM   3008  CB  THR A 457      78.404  19.823-179.030  1.00 36.82           C  
ANISOU 3008  CB  THR A 457     4815   4472   4704    153    210    374       C  
ATOM   3009  OG1 THR A 457      77.401  19.904-178.003  1.00 37.31           O  
ANISOU 3009  OG1 THR A 457     4936   4502   4739    184    219    417       O  
ATOM   3010  CG2 THR A 457      77.855  19.007-180.193  1.00 37.60           C  
ANISOU 3010  CG2 THR A 457     4820   4684   4782    183    188    381       C  
ATOM   3011  N   PRO A 458      80.959  21.020-177.496  1.00 34.27           N  
ANISOU 3011  N   PRO A 458     4611   3956   4455     -6    189    283       N  
ATOM   3012  CA  PRO A 458      81.544  21.743-176.354  1.00 31.14           C  
ANISOU 3012  CA  PRO A 458     4319   3456   4057    -77    183    267       C  
ATOM   3013  C   PRO A 458      80.508  22.447-175.487  1.00 31.44           C  
ANISOU 3013  C   PRO A 458     4493   3422   4030    -41    246    315       C  
ATOM   3014  O   PRO A 458      80.725  22.584-174.272  1.00 38.36           O  
ANISOU 3014  O   PRO A 458     5463   4220   4893    -96    213    293       O  
ATOM   3015  CB  PRO A 458      82.516  22.736-177.019  1.00 34.09           C  
ANISOU 3015  CB  PRO A 458     4699   3807   4446   -130    242    261       C  
ATOM   3016  CG  PRO A 458      82.065  22.832-178.479  1.00 33.22           C  
ANISOU 3016  CG  PRO A 458     4528   3776   4319    -58    314    299       C  
ATOM   3017  CD  PRO A 458      81.477  21.485-178.800  1.00 33.42           C  
ANISOU 3017  CD  PRO A 458     4453   3890   4353     -4    249    288       C  
ATOM   3018  N   VAL A 459      79.374  22.864-176.059  1.00 31.73           N  
ANISOU 3018  N   VAL A 459     4543   3487   4024     52    335    384       N  
ATOM   3019  CA  VAL A 459      78.386  23.601-175.277  1.00 34.77           C  
ANISOU 3019  CA  VAL A 459     5054   3801   4354    104    417    437       C  
ATOM   3020  C   VAL A 459      77.788  22.750-174.149  1.00 35.30           C  
ANISOU 3020  C   VAL A 459     5137   3863   4412    106    359    426       C  
ATOM   3021  O   VAL A 459      77.308  23.296-173.153  1.00 35.89           O  
ANISOU 3021  O   VAL A 459     5340   3853   4443    116    414    445       O  
ATOM   3022  CB  VAL A 459      77.274  24.138-176.188  1.00 29.93           C  
ANISOU 3022  CB  VAL A 459     4424   3240   3709    220    518    526       C  
ATOM   3023  CG1 VAL A 459      77.820  25.249-177.138  1.00 33.62           C  
ANISOU 3023  CG1 VAL A 459     4926   3680   4168    219    599    549       C  
ATOM   3024  CG2 VAL A 459      76.633  23.010-176.993  1.00 31.55           C  
ANISOU 3024  CG2 VAL A 459     4477   3585   3927    266    458    543       C  
ATOM   3025  N   PHE A 460      77.792  21.424-174.286  1.00 32.87           N  
ANISOU 3025  N   PHE A 460     4714   3636   4139     97    258    398       N  
ATOM   3026  CA  PHE A 460      77.258  20.567-173.224  1.00 31.97           C  
ANISOU 3026  CA  PHE A 460     4619   3512   4015     90    203    391       C  
ATOM   3027  C   PHE A 460      77.983  20.805-171.902  1.00 34.09           C  
ANISOU 3027  C   PHE A 460     5010   3674   4269      8    163    347       C  
ATOM   3028  O   PHE A 460      77.366  20.792-170.824  1.00 33.49           O  
ANISOU 3028  O   PHE A 460     5030   3547   4148     13    181    362       O  
ATOM   3029  CB  PHE A 460      77.359  19.090-173.653  1.00 26.47           C  
ANISOU 3029  CB  PHE A 460     3791   2902   3363     79     97    358       C  
ATOM   3030  CG  PHE A 460      76.737  18.117-172.683  1.00 29.71           C  
ANISOU 3030  CG  PHE A 460     4216   3308   3764     72     43    358       C  
ATOM   3031  CD1 PHE A 460      77.462  17.643-171.590  1.00 31.11           C  
ANISOU 3031  CD1 PHE A 460     4450   3421   3951      5    -43    313       C  
ATOM   3032  CD2 PHE A 460      75.431  17.667-172.857  1.00 29.72           C  
ANISOU 3032  CD2 PHE A 460     4173   3376   3744    127     73    411       C  
ATOM   3033  CE1 PHE A 460      76.892  16.725-170.686  1.00 34.20           C  
ANISOU 3033  CE1 PHE A 460     4866   3802   4327     -4    -90    318       C  
ATOM   3034  CE2 PHE A 460      74.858  16.762-171.961  1.00 30.06           C  
ANISOU 3034  CE2 PHE A 460     4231   3412   3776    110     30    413       C  
ATOM   3035  CZ  PHE A 460      75.580  16.291-170.872  1.00 29.19           C  
ANISOU 3035  CZ  PHE A 460     4192   3227   3672     47    -47    367       C  
ATOM   3036  N   HIS A 461      79.295  21.007-171.957  1.00 35.43           N  
ANISOU 3036  N   HIS A 461     5175   3816   4471    -73    108    296       N  
ATOM   3037  CA  HIS A 461      80.102  21.125-170.750  1.00 35.68           C  
ANISOU 3037  CA  HIS A 461     5304   3766   4488   -169     40    254       C  
ATOM   3038  C   HIS A 461      80.224  22.553-170.259  1.00 37.73           C  
ANISOU 3038  C   HIS A 461     5729   3917   4689   -209    129    259       C  
ATOM   3039  O   HIS A 461      80.934  22.796-169.272  1.00 36.18           O  
ANISOU 3039  O   HIS A 461     5632   3649   4467   -309     73    221       O  
ATOM   3040  CB  HIS A 461      81.477  20.520-171.010  1.00 33.79           C  
ANISOU 3040  CB  HIS A 461     4954   3563   4320   -241    -78    202       C  
ATOM   3041  CG  HIS A 461      81.398  19.191-171.682  1.00 34.00           C  
ANISOU 3041  CG  HIS A 461     4830   3682   4406   -192   -141    193       C  
ATOM   3042  ND1 HIS A 461      81.151  18.027-170.991  1.00 31.98           N  
ANISOU 3042  ND1 HIS A 461     4560   3433   4156   -188   -229    185       N  
ATOM   3043  CD2 HIS A 461      81.460  18.846-172.993  1.00 35.96           C  
ANISOU 3043  CD2 HIS A 461     4955   4011   4699   -146   -121    191       C  
ATOM   3044  CE1 HIS A 461      81.096  17.015-171.841  1.00 37.89           C  
ANISOU 3044  CE1 HIS A 461     5185   4256   4955   -144   -260    175       C  
ATOM   3045  NE2 HIS A 461      81.277  17.486-173.063  1.00 31.95           N  
ANISOU 3045  NE2 HIS A 461     4365   3551   4223   -119   -196    176       N  
ATOM   3046  N   GLN A 462      79.522  23.487-170.899  1.00 34.12           N  
ANISOU 3046  N   GLN A 462     5314   3445   4206   -135    264    307       N  
ATOM   3047  CA  GLN A 462      79.562  24.901-170.545  1.00 32.75           C  
ANISOU 3047  CA  GLN A 462     5315   3153   3976   -160    372    316       C  
ATOM   3048  C   GLN A 462      78.324  25.275-169.739  1.00 37.04           C  
ANISOU 3048  C   GLN A 462     5994   3629   4448    -83    477    359       C  
ATOM   3049  O   GLN A 462      77.204  25.221-170.253  1.00 40.68           O  
ANISOU 3049  O   GLN A 462     6403   4144   4911     40    557    425       O  
ATOM   3050  CB  GLN A 462      79.642  25.751-171.817  1.00 34.55           C  
ANISOU 3050  CB  GLN A 462     5511   3395   4223   -118    466    351       C  
ATOM   3051  CG  GLN A 462      79.647  27.230-171.553  1.00 36.86           C  
ANISOU 3051  CG  GLN A 462     5993   3553   4458   -136    592    366       C  
ATOM   3052  CD  GLN A 462      80.877  27.671-170.810  1.00 37.97           C  
ANISOU 3052  CD  GLN A 462     6236   3606   4585   -299    532    296       C  
ATOM   3053  OE1 GLN A 462      81.992  27.465-171.275  1.00 37.67           O  
ANISOU 3053  OE1 GLN A 462     6095   3615   4601   -388    449    259       O  
ATOM   3054  NE2 GLN A 462      80.686  28.265-169.635  1.00 34.78           N  
ANISOU 3054  NE2 GLN A 462     6032   3076   4105   -343    573    279       N  
ATOM   3055  N   GLU A 463      78.521  25.679-168.488  1.00 33.50           N  
ANISOU 3055  N   GLU A 463     5722   3070   3937   -157    480    326       N  
ATOM   3056  CA  GLU A 463      77.425  26.278-167.741  1.00 37.93           C  
ANISOU 3056  CA  GLU A 463     6444   3544   4423    -82    615    365       C  
ATOM   3057  C   GLU A 463      77.010  27.604-168.382  1.00 40.71           C  
ANISOU 3057  C   GLU A 463     6883   3828   4758     -3    782    415       C  
ATOM   3058  O   GLU A 463      77.833  28.338-168.938  1.00 39.44           O  
ANISOU 3058  O   GLU A 463     6749   3627   4610    -63    792    396       O  
ATOM   3059  CB  GLU A 463      77.830  26.491-166.277  1.00 33.31           C  
ANISOU 3059  CB  GLU A 463     6056   2842   3758   -194    586    309       C  
ATOM   3060  CG  GLU A 463      78.138  25.184-165.549  1.00 37.72           C  
ANISOU 3060  CG  GLU A 463     6546   3461   4325   -259    425    275       C  
ATOM   3061  CD  GLU A 463      78.616  25.401-164.122  1.00 44.68           C  
ANISOU 3061  CD  GLU A 463     7627   4236   5115   -381    379    223       C  
ATOM   3062  OE1 GLU A 463      79.034  26.541-163.806  1.00 45.20           O  
ANISOU 3062  OE1 GLU A 463     7868   4185   5121   -453    441    195       O  
ATOM   3063  OE2 GLU A 463      78.575  24.432-163.327  1.00 45.19           O  
ANISOU 3063  OE2 GLU A 463     7681   4328   5160   -411    280    212       O  
ATOM   3064  N   MET A 464      75.712  27.908-168.297  1.00 42.55           N  
ANISOU 3064  N   MET A 464     7157   4048   4963    137    919    486       N  
ATOM   3065  CA  MET A 464      75.109  29.037-168.997  1.00 38.21           C  
ANISOU 3065  CA  MET A 464     6661   3451   4406    254   1082    558       C  
ATOM   3066  C   MET A 464      74.099  29.728-168.093  1.00 43.70           C  
ANISOU 3066  C   MET A 464     7537   4032   5034    346   1247    598       C  
ATOM   3067  O   MET A 464      73.525  29.110-167.192  1.00 44.14           O  
ANISOU 3067  O   MET A 464     7610   4099   5062    359   1240    594       O  
ATOM   3068  CB  MET A 464      74.422  28.581-170.291  1.00 36.85           C  
ANISOU 3068  CB  MET A 464     6272   3434   4296    375   1080    638       C  
ATOM   3069  CG  MET A 464      75.392  28.070-171.348  1.00 40.33           C  
ANISOU 3069  CG  MET A 464     6554   3973   4796    301    955    603       C  
ATOM   3070  SD  MET A 464      74.503  27.465-172.790  1.00 43.93           S  
ANISOU 3070  SD  MET A 464     6779   4612   5300    430    946    691       S  
ATOM   3071  CE  MET A 464      75.766  26.499-173.608  1.00 38.15           C  
ANISOU 3071  CE  MET A 464     5888   3980   4626    312    780    613       C  
ATOM   3072  N   VAL A 465      73.903  31.023-168.332  1.00 43.77           N  
ANISOU 3072  N   VAL A 465     7693   3925   5015    412   1404    637       N  
ATOM   3073  CA  VAL A 465      72.979  31.850-167.564  1.00 47.60           C  
ANISOU 3073  CA  VAL A 465     8370   4279   5437    519   1592    679       C  
ATOM   3074  C   VAL A 465      71.920  32.387-168.513  1.00 48.36           C  
ANISOU 3074  C   VAL A 465     8386   4419   5570    721   1731    805       C  
ATOM   3075  O   VAL A 465      72.252  32.976-169.549  1.00 42.94           O  
ANISOU 3075  O   VAL A 465     7669   3734   4911    743   1750    839       O  
ATOM   3076  CB  VAL A 465      73.705  33.011-166.859  1.00 50.20           C  
ANISOU 3076  CB  VAL A 465     8992   4395   5688    415   1672    612       C  
ATOM   3077  CG1 VAL A 465      72.751  33.758-165.921  1.00 45.63           C  
ANISOU 3077  CG1 VAL A 465     8635   3668   5033    523   1874    641       C  
ATOM   3078  CG2 VAL A 465      74.918  32.495-166.116  1.00 46.36           C  
ANISOU 3078  CG2 VAL A 465     8552   3892   5171    197   1501    495       C  
ATOM   3079  N   ASN A 466      70.654  32.189-168.161  1.00 47.00           N  
ANISOU 3079  N   ASN A 466     8175   4286   5396    868   1829    881       N  
ATOM   3080  CA  ASN A 466      69.532  32.582-169.002  1.00 44.06           C  
ANISOU 3080  CA  ASN A 466     7693   3984   5064   1072   1949   1018       C  
ATOM   3081  C   ASN A 466      68.779  33.759-168.387  1.00 51.52           C  
ANISOU 3081  C   ASN A 466     8845   4769   5963   1211   2180   1068       C  
ATOM   3082  O   ASN A 466      68.402  33.717-167.207  1.00 50.10           O  
ANISOU 3082  O   ASN A 466     8783   4520   5732   1209   2249   1028       O  
ATOM   3083  CB  ASN A 466      68.585  31.401-169.214  1.00 40.24           C  
ANISOU 3083  CB  ASN A 466     6957   3704   4630   1142   1878   1081       C  
ATOM   3084  CG  ASN A 466      67.606  31.659-170.321  1.00 56.15           C  
ANISOU 3084  CG  ASN A 466     8804   5837   6694   1321   1944   1223       C  
ATOM   3085  OD1 ASN A 466      67.773  32.603-171.098  1.00 51.17           O  
ANISOU 3085  OD1 ASN A 466     8223   5152   6066   1385   2013   1272       O  
ATOM   3086  ND2 ASN A 466      66.577  30.830-170.408  1.00 62.35           N  
ANISOU 3086  ND2 ASN A 466     9391   6786   7515   1398   1920   1296       N  
ATOM   3087  N   TYR A 467      68.549  34.801-169.193  1.00 44.26           N  
ANISOU 3087  N   TYR A 467     7925   3833   5059   1321   2277   1119       N  
ATOM   3088  CA  TYR A 467      67.846  35.997-168.741  1.00 50.42           C  
ANISOU 3088  CA  TYR A 467     8848   4508   5801   1454   2480   1130       C  
ATOM   3089  C   TYR A 467      67.422  36.805-169.962  1.00 57.60           C  
ANISOU 3089  C   TYR A 467     9667   5466   6751   1602   2552   1232       C  
ATOM   3090  O   TYR A 467      67.877  36.558-171.081  1.00 55.00           O  
ANISOU 3090  O   TYR A 467     9209   5224   6463   1570   2441   1267       O  
ATOM   3091  CB  TYR A 467      68.716  36.845-167.808  1.00 45.11           C  
ANISOU 3091  CB  TYR A 467     8463   3640   5039   1316   2530    992       C  
ATOM   3092  CG  TYR A 467      70.113  37.108-168.344  1.00 51.16           C  
ANISOU 3092  CG  TYR A 467     9284   4355   5798   1138   2412    916       C  
ATOM   3093  CD1 TYR A 467      71.164  36.266-168.008  1.00 48.89           C  
ANISOU 3093  CD1 TYR A 467     9000   4070   5504    935   2239    833       C  
ATOM   3094  CD2 TYR A 467      70.381  38.200-169.177  1.00 51.05           C  
ANISOU 3094  CD2 TYR A 467     9319   4292   5787   1172   2479    935       C  
ATOM   3095  CE1 TYR A 467      72.443  36.486-168.476  1.00 47.81           C  
ANISOU 3095  CE1 TYR A 467     8902   3893   5370    771   2139    771       C  
ATOM   3096  CE2 TYR A 467      71.672  38.431-169.660  1.00 54.93           C  
ANISOU 3096  CE2 TYR A 467     9857   4737   6276   1002   2379    870       C  
ATOM   3097  CZ  TYR A 467      72.699  37.560-169.311  1.00 55.60           C  
ANISOU 3097  CZ  TYR A 467     9931   4832   6361    802   2211    791       C  
ATOM   3098  OH  TYR A 467      73.984  37.756-169.769  1.00 49.63           O  
ANISOU 3098  OH  TYR A 467     9207   4039   5610    630   2118    734       O  
ATOM   3099  N   PHE A 468      66.551  37.792-169.725  1.00 49.20           N  
ANISOU 3099  N   PHE A 468     8684   4345   5667   1766   2748   1281       N  
ATOM   3100  CA  PHE A 468      65.924  38.572-170.787  1.00 64.26           C  
ANISOU 3100  CA  PHE A 468    10499   6308   7607   1935   2836   1399       C  
ATOM   3101  C   PHE A 468      66.589  39.943-170.901  1.00 59.50           C  
ANISOU 3101  C   PHE A 468    10118   5541   6949   1899   2931   1338       C  
ATOM   3102  O   PHE A 468      66.629  40.702-169.924  1.00 57.03           O  
ANISOU 3102  O   PHE A 468    10034   5075   6561   1883   3066   1266       O  
ATOM   3103  CB  PHE A 468      64.424  38.720-170.522  1.00 74.31           C  
ANISOU 3103  CB  PHE A 468    11686   7650   8897   2155   2997   1523       C  
ATOM   3104  CG  PHE A 468      63.691  39.567-171.546  1.00 83.39           C  
ANISOU 3104  CG  PHE A 468    12743   8868  10074   2337   3096   1660       C  
ATOM   3105  CD1 PHE A 468      62.985  38.969-172.582  1.00 81.58           C  
ANISOU 3105  CD1 PHE A 468    12233   8849   9915   2438   3014   1800       C  
ATOM   3106  CD2 PHE A 468      63.693  40.958-171.459  1.00 81.93           C  
ANISOU 3106  CD2 PHE A 468    12755   8540   9834   2399   3269   1654       C  
ATOM   3107  CE1 PHE A 468      62.305  39.735-173.512  1.00 81.27           C  
ANISOU 3107  CE1 PHE A 468    12107   8881   9892   2596   3092   1932       C  
ATOM   3108  CE2 PHE A 468      63.019  41.732-172.388  1.00 80.39           C  
ANISOU 3108  CE2 PHE A 468    12479   8405   9660   2565   3357   1788       C  
ATOM   3109  CZ  PHE A 468      62.322  41.121-173.416  1.00 80.17           C  
ANISOU 3109  CZ  PHE A 468    12166   8592   9703   2664   3266   1928       C  
ATOM   3110  N   LEU A 469      67.085  40.264-172.097  1.00 59.37           N  
ANISOU 3110  N   LEU A 469    10039   5558   6960   1884   2866   1370       N  
ATOM   3111  CA  LEU A 469      67.537  41.610-172.436  1.00 61.01           C  
ANISOU 3111  CA  LEU A 469    10424   5632   7126   1882   2968   1347       C  
ATOM   3112  C   LEU A 469      66.720  42.164-173.599  1.00 59.37           C  
ANISOU 3112  C   LEU A 469    10085   5515   6956   2077   3038   1496       C  
ATOM   3113  O   LEU A 469      66.197  41.415-174.429  1.00 59.15           O  
ANISOU 3113  O   LEU A 469     9813   5670   6990   2153   2946   1601       O  
ATOM   3114  CB  LEU A 469      69.031  41.641-172.814  1.00 55.82           C  
ANISOU 3114  CB  LEU A 469     9843   4909   6457   1665   2837   1246       C  
ATOM   3115  CG  LEU A 469      70.058  41.091-171.820  1.00 54.83           C  
ANISOU 3115  CG  LEU A 469     9834   4707   6294   1439   2733   1102       C  
ATOM   3116  CD1 LEU A 469      71.458  41.167-172.423  1.00 59.05           C  
ANISOU 3116  CD1 LEU A 469    10399   5206   6831   1245   2613   1036       C  
ATOM   3117  CD2 LEU A 469      69.996  41.866-170.529  1.00 52.55           C  
ANISOU 3117  CD2 LEU A 469     9799   4253   5915   1414   2871   1015       C  
ATOM   3118  N   SER A 470      66.623  43.492-173.654  1.00 66.89           N  
ANISOU 3118  N   SER A 470    11207   6344   7865   2149   3200   1508       N  
ATOM   3119  CA  SER A 470      65.979  44.208-174.742  1.00 67.75           C  
ANISOU 3119  CA  SER A 470    11234   6511   7997   2321   3275   1645       C  
ATOM   3120  C   SER A 470      67.014  45.016-175.521  1.00 58.58           C  
ANISOU 3120  C   SER A 470    10194   5248   6815   2224   3252   1601       C  
ATOM   3121  O   SER A 470      67.955  45.542-174.919  1.00 58.06           O  
ANISOU 3121  O   SER A 470    10352   5014   6693   2070   3276   1474       O  
ATOM   3122  CB  SER A 470      64.890  45.146-174.201  1.00 80.73           C  
ANISOU 3122  CB  SER A 470    12974   8094   9605   2510   3506   1721       C  
ATOM   3123  OG  SER A 470      63.997  45.547-175.222  1.00 84.58           O  
ANISOU 3123  OG  SER A 470    13313   8695  10130   2702   3559   1887       O  
ATOM   3124  N   PRO A 471      66.893  45.128-176.859  1.00 52.91           N  
ANISOU 3124  N   PRO A 471     9336   4632   6134   2297   3201   1706       N  
ATOM   3125  CA  PRO A 471      65.883  44.592-177.784  1.00 51.64           C  
ANISOU 3125  CA  PRO A 471     8908   4683   6028   2457   3151   1864       C  
ATOM   3126  C   PRO A 471      65.748  43.076-177.786  1.00 50.01           C  
ANISOU 3126  C   PRO A 471     8478   4654   5869   2404   2980   1871       C  
ATOM   3127  O   PRO A 471      66.698  42.361-177.470  1.00 50.90           O  
ANISOU 3127  O   PRO A 471     8617   4741   5980   2221   2858   1759       O  
ATOM   3128  CB  PRO A 471      66.386  45.062-179.163  1.00 53.45           C  
ANISOU 3128  CB  PRO A 471     9115   4932   6261   2447   3097   1914       C  
ATOM   3129  CG  PRO A 471      67.185  46.276-178.872  1.00 57.79           C  
ANISOU 3129  CG  PRO A 471     9942   5258   6757   2371   3210   1825       C  
ATOM   3130  CD  PRO A 471      67.863  45.990-177.555  1.00 55.86           C  
ANISOU 3130  CD  PRO A 471     9848   4893   6483   2206   3203   1668       C  
ATOM   3131  N   ALA A 472      64.576  42.582-178.180  1.00 53.91           N  
ANISOU 3131  N   ALA A 472     8747   5335   6400   2557   2967   2009       N  
ATOM   3132  CA  ALA A 472      64.332  41.151-178.095  1.00 54.77           C  
ANISOU 3132  CA  ALA A 472     8650   5613   6549   2512   2818   2020       C  
ATOM   3133  C   ALA A 472      63.313  40.708-179.135  1.00 55.59           C  
ANISOU 3133  C   ALA A 472     8483   5952   6687   2645   2752   2186       C  
ATOM   3134  O   ALA A 472      62.444  41.479-179.562  1.00 56.28           O  
ANISOU 3134  O   ALA A 472     8530   6080   6774   2810   2858   2308       O  
ATOM   3135  CB  ALA A 472      63.834  40.765-176.695  1.00 57.25           C  
ANISOU 3135  CB  ALA A 472     9004   5887   6861   2526   2892   1977       C  
ATOM   3136  N   PHE A 473      63.434  39.446-179.525  1.00 48.81           N  
ANISOU 3136  N   PHE A 473     7442   5251   5851   2561   2573   2190       N  
ATOM   3137  CA  PHE A 473      62.357  38.722-180.182  1.00 59.28           C  
ANISOU 3137  CA  PHE A 473     8494   6822   7206   2656   2492   2331       C  
ATOM   3138  C   PHE A 473      61.521  38.021-179.119  1.00 57.70           C  
ANISOU 3138  C   PHE A 473     8208   6680   7034   2697   2525   2347       C  
ATOM   3139  O   PHE A 473      62.062  37.304-178.270  1.00 57.40           O  
ANISOU 3139  O   PHE A 473     8231   6579   6998   2577   2477   2238       O  
ATOM   3140  CB  PHE A 473      62.914  37.713-181.188  1.00 54.11           C  
ANISOU 3140  CB  PHE A 473     7698   6314   6547   2536   2283   2327       C  
ATOM   3141  CG  PHE A 473      63.599  38.356-182.368  1.00 51.65           C  
ANISOU 3141  CG  PHE A 473     7445   5976   6203   2510   2253   2337       C  
ATOM   3142  CD1 PHE A 473      62.856  38.906-183.404  1.00 58.25           C  
ANISOU 3142  CD1 PHE A 473     8178   6925   7031   2641   2268   2475       C  
ATOM   3143  CD2 PHE A 473      64.978  38.414-182.438  1.00 53.79           C  
ANISOU 3143  CD2 PHE A 473     7872   6113   6451   2350   2213   2215       C  
ATOM   3144  CE1 PHE A 473      63.480  39.508-184.497  1.00 52.84           C  
ANISOU 3144  CE1 PHE A 473     7557   6211   6310   2617   2245   2489       C  
ATOM   3145  CE2 PHE A 473      65.607  39.008-183.526  1.00 52.98           C  
ANISOU 3145  CE2 PHE A 473     7825   5987   6317   2322   2196   2231       C  
ATOM   3146  CZ  PHE A 473      64.854  39.554-184.554  1.00 53.54           C  
ANISOU 3146  CZ  PHE A 473     7804   6163   6376   2459   2213   2367       C  
ATOM   3147  N   ARG A 474      60.210  38.249-179.157  1.00 55.83           N  
ANISOU 3147  N   ARG A 474     7834   6563   6817   2861   2610   2490       N  
ATOM   3148  CA  ARG A 474      59.275  37.682-178.199  1.00 62.75           C  
ANISOU 3148  CA  ARG A 474     8616   7505   7719   2915   2664   2534       C  
ATOM   3149  C   ARG A 474      58.258  36.801-178.912  1.00 68.09           C  
ANISOU 3149  C   ARG A 474     8983   8460   8429   2958   2541   2676       C  
ATOM   3150  O   ARG A 474      57.913  37.035-180.073  1.00 63.82           O  
ANISOU 3150  O   ARG A 474     8315   8052   7882   3010   2481   2778       O  
ATOM   3151  CB  ARG A 474      58.529  38.781-177.435  1.00 68.34           C  
ANISOU 3151  CB  ARG A 474     9448   8104   8415   3065   2902   2590       C  
ATOM   3152  CG  ARG A 474      59.408  39.683-176.587  1.00 73.08           C  
ANISOU 3152  CG  ARG A 474    10367   8429   8970   3018   3038   2448       C  
ATOM   3153  CD  ARG A 474      58.587  40.836-176.023  1.00 82.66           C  
ANISOU 3153  CD  ARG A 474    11698   9551  10158   3178   3277   2527       C  
ATOM   3154  NE  ARG A 474      57.152  40.586-176.157  1.00 87.26           N  
ANISOU 3154  NE  ARG A 474    12052  10326  10775   3323   3314   2714       N  
ATOM   3155  CZ  ARG A 474      56.213  41.523-176.072  1.00 90.20           C  
ANISOU 3155  CZ  ARG A 474    12445  10687  11139   3490   3490   2847       C  
ATOM   3156  NH1 ARG A 474      56.549  42.789-175.854  1.00 89.10           N  
ANISOU 3156  NH1 ARG A 474    12554  10349  10951   3540   3657   2810       N  
ATOM   3157  NH2 ARG A 474      54.935  41.194-176.213  1.00 91.13           N  
ANISOU 3157  NH2 ARG A 474    12335  10993  11295   3602   3496   3021       N  
ATOM   3158  N   TYR A 475      57.768  35.792-178.199  1.00 59.07           N  
ANISOU 3158  N   TYR A 475     7724   7404   7314   2928   2502   2681       N  
ATOM   3159  CA  TYR A 475      56.610  35.047-178.663  1.00 62.91           C  
ANISOU 3159  CA  TYR A 475     7920   8152   7831   2972   2414   2824       C  
ATOM   3160  C   TYR A 475      55.349  35.882-178.482  1.00 62.55           C  
ANISOU 3160  C   TYR A 475     7823   8147   7796   3146   2581   2978       C  
ATOM   3161  O   TYR A 475      55.289  36.775-177.633  1.00 58.95           O  
ANISOU 3161  O   TYR A 475     7559   7513   7328   3227   2778   2963       O  
ATOM   3162  CB  TYR A 475      56.481  33.722-177.912  1.00 63.98           C  
ANISOU 3162  CB  TYR A 475     7955   8360   7997   2880   2327   2782       C  
ATOM   3163  CG  TYR A 475      57.726  32.878-178.004  1.00 68.18           C  
ANISOU 3163  CG  TYR A 475     8552   8839   8515   2710   2168   2639       C  
ATOM   3164  CD1 TYR A 475      58.079  32.254-179.197  1.00 66.77           C  
ANISOU 3164  CD1 TYR A 475     8242   8808   8320   2620   1973   2647       C  
ATOM   3165  CD2 TYR A 475      58.557  32.714-176.902  1.00 74.45           C  
ANISOU 3165  CD2 TYR A 475     9553   9435   9302   2628   2211   2501       C  
ATOM   3166  CE1 TYR A 475      59.225  31.483-179.288  1.00 68.38           C  
ANISOU 3166  CE1 TYR A 475     8515   8963   8502   2459   1835   2528       C  
ATOM   3167  CE2 TYR A 475      59.702  31.948-176.980  1.00 76.44           C  
ANISOU 3167  CE2 TYR A 475     9871   9639   9532   2458   2063   2385       C  
ATOM   3168  CZ  TYR A 475      60.030  31.334-178.174  1.00 79.04           C  
ANISOU 3168  CZ  TYR A 475    10060  10124   9847   2366   1879   2388       C  
ATOM   3169  OH  TYR A 475      61.168  30.568-178.255  1.00 87.37           O  
ANISOU 3169  OH  TYR A 475    11165  11156  10877   2153   1733   2219       O  
ATOM   3170  N   GLN A 476      54.340  35.591-179.300  1.00 65.34           N  
ANISOU 3170  N   GLN A 476     7922   8737   8165   3195   2498   3128       N  
ATOM   3171  CA  GLN A 476      53.081  36.318-179.248  1.00 65.14           C  
ANISOU 3171  CA  GLN A 476     7819   8776   8154   3359   2633   3297       C  
ATOM   3172  C   GLN A 476      51.949  35.357-179.571  1.00 61.16           C  
ANISOU 3172  C   GLN A 476     7008   8546   7684   3344   2505   3422       C  
ATOM   3173  O   GLN A 476      52.177  34.339-180.235  1.00 68.02           O  
ANISOU 3173  O   GLN A 476     7725   9568   8550   3215   2301   3390       O  
ATOM   3174  CB  GLN A 476      53.077  37.501-180.231  1.00 63.74           C  
ANISOU 3174  CB  GLN A 476     7691   8577   7951   3465   2686   3372       C  
ATOM   3175  CG  GLN A 476      53.172  37.088-181.683  1.00 61.82           C  
ANISOU 3175  CG  GLN A 476     7275   8522   7693   3405   2483   3412       C  
ATOM   3176  CD  GLN A 476      53.043  38.265-182.649  1.00 61.71           C  
ANISOU 3176  CD  GLN A 476     7299   8493   7654   3525   2540   3506       C  
ATOM   3177  OE1 GLN A 476      52.221  39.165-182.460  1.00 67.05           O  
ANISOU 3177  OE1 GLN A 476     7987   9149   8341   3684   2697   3627       O  
ATOM   3178  NE2 GLN A 476      53.860  38.255-183.696  1.00 63.02           N  
ANISOU 3178  NE2 GLN A 476     7491   8668   7785   3449   2413   3455       N  
ATOM   3179  N   PRO A 477      50.725  35.654-179.140  1.00 62.84           N  
ANISOU 3179  N   PRO A 477     7127   8824   7926   3466   2617   3565       N  
ATOM   3180  CA  PRO A 477      49.612  34.739-179.415  1.00 74.50           C  
ANISOU 3180  CA  PRO A 477     8307  10563   9437   3438   2493   3683       C  
ATOM   3181  C   PRO A 477      49.283  34.685-180.900  1.00 79.61           C  
ANISOU 3181  C   PRO A 477     8761  11422  10066   3425   2334   3777       C  
ATOM   3182  O   PRO A 477      49.572  35.614-181.656  1.00 80.70           O  
ANISOU 3182  O   PRO A 477     8980  11507  10174   3500   2369   3806       O  
ATOM   3183  CB  PRO A 477      48.454  35.335-178.603  1.00 71.23           C  
ANISOU 3183  CB  PRO A 477     7877  10129   9059   3596   2681   3818       C  
ATOM   3184  CG  PRO A 477      48.803  36.780-178.465  1.00 71.26           C  
ANISOU 3184  CG  PRO A 477     8126   9916   9034   3734   2881   3820       C  
ATOM   3185  CD  PRO A 477      50.299  36.813-178.336  1.00 68.25           C  
ANISOU 3185  CD  PRO A 477     7979   9340   8612   3627   2864   3623       C  
ATOM   3186  N   ASP A 478      48.691  33.567-181.317  1.00 88.29           N  
ANISOU 3186  N   ASP A 478     9610  12758  11177   3319   2152   3820       N  
ATOM   3187  CA  ASP A 478      48.225  33.438-182.688  1.00 94.01           C  
ANISOU 3187  CA  ASP A 478    10139  13703  11876   3294   1993   3920       C  
ATOM   3188  C   ASP A 478      47.113  34.455-182.944  1.00 95.60           C  
ANISOU 3188  C   ASP A 478    10263  13964  12095   3481   2113   4111       C  
ATOM   3189  O   ASP A 478      46.345  34.786-182.038  1.00 94.43           O  
ANISOU 3189  O   ASP A 478    10111  13777  11991   3593   2268   4190       O  
ATOM   3190  CB  ASP A 478      47.712  32.024-182.962  1.00100.42           C  
ANISOU 3190  CB  ASP A 478    10708  14753  12694   3130   1787   3926       C  
ATOM   3191  CG  ASP A 478      48.832  31.014-183.109  1.00103.64           C  
ANISOU 3191  CG  ASP A 478    11168  15139  13071   2940   1630   3752       C  
ATOM   3192  OD1 ASP A 478      49.827  31.336-183.788  1.00102.01           O  
ANISOU 3192  OD1 ASP A 478    11090  14849  12821   2915   1586   3675       O  
ATOM   3193  OD2 ASP A 478      48.717  29.903-182.543  1.00107.61           O  
ANISOU 3193  OD2 ASP A 478    11585  15707  13596   2817   1552   3696       O  
ATOM   3194  N   PRO A 479      47.004  34.976-184.165  1.00 93.65           N  
ANISOU 3194  N   PRO A 479     9958  13809  11815   3524   2046   4193       N  
ATOM   3195  CA  PRO A 479      46.009  36.033-184.411  1.00 95.33           C  
ANISOU 3195  CA  PRO A 479    10111  14063  12047   3720   2170   4379       C  
ATOM   3196  C   PRO A 479      44.585  35.517-184.598  1.00 97.51           C  
ANISOU 3196  C   PRO A 479    10093  14598  12357   3730   2093   4545       C  
ATOM   3197  O   PRO A 479      43.890  35.961-185.517  1.00 98.35           O  
ANISOU 3197  O   PRO A 479    10063  14850  12455   3809   2051   4693       O  
ATOM   3198  CB  PRO A 479      46.535  36.713-185.683  1.00 90.40           C  
ANISOU 3198  CB  PRO A 479     9543  13435  11371   3747   2110   4392       C  
ATOM   3199  CG  PRO A 479      47.280  35.638-186.392  1.00 87.68           C  
ANISOU 3199  CG  PRO A 479     9149  13184  10981   3538   1880   4272       C  
ATOM   3200  CD  PRO A 479      47.880  34.752-185.329  1.00 87.22           C  
ANISOU 3200  CD  PRO A 479     9166  13031  10942   3414   1878   4116       C  
ATOM   3201  N   TRP A 480      44.129  34.612-183.736  1.00108.95           N  
ANISOU 3201  N   TRP A 480    11444  16106  13845   3653   2076   4527       N  
ATOM   3202  CA  TRP A 480      42.727  34.190-183.737  1.00117.94           C  
ANISOU 3202  CA  TRP A 480    12314  17471  15026   3671   2032   4686       C  
ATOM   3203  C   TRP A 480      42.372  33.476-182.432  1.00120.38           C  
ANISOU 3203  C   TRP A 480    12598  17753  15388   3628   2093   4648       C  
ATOM   3204  O   TRP A 480      43.164  33.469-181.488  1.00118.77           O  
ANISOU 3204  O   TRP A 480    12601  17338  15187   3614   2194   4512       O  
ATOM   3205  CB  TRP A 480      42.413  33.292-184.946  1.00122.35           C  
ANISOU 3205  CB  TRP A 480    12642  18298  15549   3511   1770   4718       C  
ATOM   3206  CG  TRP A 480      43.104  31.952-184.964  1.00126.69           C  
ANISOU 3206  CG  TRP A 480    13178  18890  16068   3271   1588   4553       C  
ATOM   3207  CD1 TRP A 480      42.626  30.774-184.462  1.00130.17           C  
ANISOU 3207  CD1 TRP A 480    13471  19452  16534   3130   1496   4528       C  
ATOM   3208  CD2 TRP A 480      44.383  31.652-185.537  1.00124.61           C  
ANISOU 3208  CD2 TRP A 480    13052  18550  15744   3145   1476   4393       C  
ATOM   3209  NE1 TRP A 480      43.534  29.765-184.676  1.00126.40           N  
ANISOU 3209  NE1 TRP A 480    13038  18974  16015   2926   1338   4362       N  
ATOM   3210  CE2 TRP A 480      44.621  30.278-185.333  1.00123.15           C  
ANISOU 3210  CE2 TRP A 480    12798  18444  15551   2935   1322   4279       C  
ATOM   3211  CE3 TRP A 480      45.354  32.412-186.196  1.00123.07           C  
ANISOU 3211  CE3 TRP A 480    13035  18225  15503   3190   1493   4337       C  
ATOM   3212  CZ2 TRP A 480      45.789  29.651-185.762  1.00119.42           C  
ANISOU 3212  CZ2 TRP A 480    12426  17923  15025   2778   1190   4115       C  
ATOM   3213  CZ3 TRP A 480      46.513  31.786-186.622  1.00118.80           C  
ANISOU 3213  CZ3 TRP A 480    12590  17640  14911   3031   1360   4175       C  
ATOM   3214  CH2 TRP A 480      46.721  30.420-186.403  1.00117.32           C  
ANISOU 3214  CH2 TRP A 480    12328  17532  14716   2831   1211   4067       C  
ATOM   3215  OXT TRP A 480      41.286  32.913-182.274  1.00123.62           O  
ANISOU 3215  OXT TRP A 480    12786  18344  15838   3608   2047   4752       O  
TER    3216      TRP A 480                                                      
ATOM   3217  N   PHE B  68      50.505  27.244-159.469  1.00 74.49           N  
ANISOU 3217  N   PHE B  68     8857  10252   9194   2936   2434   2645       N  
ATOM   3218  CA  PHE B  68      51.126  25.954-159.757  1.00 67.81           C  
ANISOU 3218  CA  PHE B  68     7853   9501   8411   2710   2262   2537       C  
ATOM   3219  C   PHE B  68      51.540  25.849-161.222  1.00 61.05           C  
ANISOU 3219  C   PHE B  68     6882   8734   7582   2635   2134   2548       C  
ATOM   3220  O   PHE B  68      50.713  26.023-162.118  1.00 59.63           O  
ANISOU 3220  O   PHE B  68     6542   8738   7376   2693   2093   2693       O  
ATOM   3221  CB  PHE B  68      50.176  24.817-159.390  1.00 71.14           C  
ANISOU 3221  CB  PHE B  68     8023  10162   8845   2622   2179   2602       C  
ATOM   3222  CG  PHE B  68      49.751  24.836-157.949  1.00 79.81           C  
ANISOU 3222  CG  PHE B  68     9221  11189   9917   2691   2301   2596       C  
ATOM   3223  CD1 PHE B  68      48.428  24.628-157.596  1.00 78.84           C  
ANISOU 3223  CD1 PHE B  68     8934  11248   9773   2763   2325   2744       C  
ATOM   3224  CD2 PHE B  68      50.677  25.073-156.949  1.00 81.78           C  
ANISOU 3224  CD2 PHE B  68     9733  11187  10152   2683   2393   2442       C  
ATOM   3225  CE1 PHE B  68      48.041  24.656-156.268  1.00 75.35           C  
ANISOU 3225  CE1 PHE B  68     8587  10738   9303   2835   2443   2742       C  
ATOM   3226  CE2 PHE B  68      50.295  25.100-155.622  1.00 76.55           C  
ANISOU 3226  CE2 PHE B  68     9178  10458   9451   2747   2504   2433       C  
ATOM   3227  CZ  PHE B  68      48.977  24.893-155.282  1.00 71.19           C  
ANISOU 3227  CZ  PHE B  68     8332   9961   8758   2829   2532   2585       C  
ATOM   3228  N   PRO B  69      52.816  25.540-161.457  1.00 56.92           N  
ANISOU 3228  N   PRO B  69     6438   8085   7103   2505   2071   2395       N  
ATOM   3229  CA  PRO B  69      53.345  25.528-162.833  1.00 52.99           C  
ANISOU 3229  CA  PRO B  69     5866   7638   6629   2445   1960   2395       C  
ATOM   3230  C   PRO B  69      52.637  24.507-163.715  1.00 57.14           C  
ANISOU 3230  C   PRO B  69     6084   8466   7160   2326   1782   2477       C  
ATOM   3231  O   PRO B  69      52.426  23.359-163.319  1.00 61.60           O  
ANISOU 3231  O   PRO B  69     6504   9154   7748   2175   1689   2442       O  
ATOM   3232  CB  PRO B  69      54.825  25.164-162.640  1.00 54.94           C  
ANISOU 3232  CB  PRO B  69     6267   7689   6918   2275   1900   2195       C  
ATOM   3233  CG  PRO B  69      55.114  25.422-161.182  1.00 51.14           C  
ANISOU 3233  CG  PRO B  69     6014   7002   6416   2291   2018   2095       C  
ATOM   3234  CD  PRO B  69      53.831  25.171-160.457  1.00 48.84           C  
ANISOU 3234  CD  PRO B  69     5580   6877   6102   2405   2104   2219       C  
ATOM   3235  N   ARG B  70      52.267  24.935-164.922  1.00 52.55           N  
ANISOU 3235  N   ARG B  70     5420   8000   6548   2381   1738   2583       N  
ATOM   3236  CA  ARG B  70      51.728  24.017-165.916  1.00 55.41           C  
ANISOU 3236  CA  ARG B  70     5522   8631   6899   2248   1557   2639       C  
ATOM   3237  C   ARG B  70      52.868  23.398-166.710  1.00 54.78           C  
ANISOU 3237  C   ARG B  70     5429   8525   6860   2083   1417   2518       C  
ATOM   3238  O   ARG B  70      53.828  24.079-167.084  1.00 57.70           O  
ANISOU 3238  O   ARG B  70     5959   8719   7246   2135   1461   2464       O  
ATOM   3239  CB  ARG B  70      50.751  24.705-166.869  1.00 58.84           C  
ANISOU 3239  CB  ARG B  70     5866   9227   7263   2375   1572   2810       C  
ATOM   3240  CG  ARG B  70      50.314  23.791-168.009  1.00 63.73           C  
ANISOU 3240  CG  ARG B  70     6247  10108   7859   2221   1378   2847       C  
ATOM   3241  CD  ARG B  70      49.049  24.270-168.702  1.00 75.66           C  
ANISOU 3241  CD  ARG B  70     7624  11832   9293   2333   1395   3029       C  
ATOM   3242  NE  ARG B  70      49.121  25.663-169.128  1.00 86.38           N  
ANISOU 3242  NE  ARG B  70     9125  13087  10608   2542   1540   3109       N  
ATOM   3243  CZ  ARG B  70      49.831  26.097-170.166  1.00 87.79           C  
ANISOU 3243  CZ  ARG B  70     9369  13212  10774   2549   1516   3083       C  
ATOM   3244  NH1 ARG B  70      50.559  25.249-170.884  1.00 77.52           N  
ANISOU 3244  NH1 ARG B  70     8007  11950   9497   2366   1348   2979       N  
ATOM   3245  NH2 ARG B  70      49.823  27.388-170.480  1.00 92.38           N  
ANISOU 3245  NH2 ARG B  70    10087  13696  11317   2739   1665   3160       N  
ATOM   3246  N   VAL B  71      52.748  22.098-166.966  1.00 56.97           N  
ANISOU 3246  N   VAL B  71     5524   8972   7152   1879   1248   2478       N  
ATOM   3247  CA  VAL B  71      53.810  21.291-167.548  1.00 54.54           C  
ANISOU 3247  CA  VAL B  71     5200   8644   6881   1694   1106   2351       C  
ATOM   3248  C   VAL B  71      53.245  20.592-168.774  1.00 50.89           C  
ANISOU 3248  C   VAL B  71     4543   8422   6372   1573    928   2404       C  
ATOM   3249  O   VAL B  71      52.254  19.861-168.670  1.00 59.03           O  
ANISOU 3249  O   VAL B  71     5418   9634   7379   1483    856   2454       O  
ATOM   3250  CB  VAL B  71      54.340  20.262-166.539  1.00 51.07           C  
ANISOU 3250  CB  VAL B  71     4832   8099   6472   1486   1047   2192       C  
ATOM   3251  CG1 VAL B  71      55.639  19.733-166.994  1.00 49.84           C  
ANISOU 3251  CG1 VAL B  71     4805   7803   6329   1293    918   2020       C  
ATOM   3252  CG2 VAL B  71      54.459  20.881-165.155  1.00 52.21           C  
ANISOU 3252  CG2 VAL B  71     5159   8050   6629   1596   1218   2160       C  
ATOM   3253  N   LYS B  72      53.869  20.801-169.927  1.00 47.85           N  
ANISOU 3253  N   LYS B  72     4181   8032   5969   1562    858   2387       N  
ATOM   3254  CA  LYS B  72      53.383  20.225-171.171  1.00 47.70           C  
ANISOU 3254  CA  LYS B  72     4013   8226   5886   1451    697   2424       C  
ATOM   3255  C   LYS B  72      54.334  19.142-171.664  1.00 46.20           C  
ANISOU 3255  C   LYS B  72     3810   8028   5715   1236    532   2286       C  
ATOM   3256  O   LYS B  72      55.557  19.277-171.563  1.00 44.74           O  
ANISOU 3256  O   LYS B  72     3829   7614   5557   1188    546   2150       O  
ATOM   3257  CB  LYS B  72      53.214  21.297-172.256  1.00 51.54           C  
ANISOU 3257  CB  LYS B  72     4530   8743   6309   1609    742   2528       C  
ATOM   3258  CG  LYS B  72      52.643  20.761-173.562  1.00 54.66           C  
ANISOU 3258  CG  LYS B  72     4775   9369   6625   1504    589   2569       C  
ATOM   3259  CD  LYS B  72      52.332  21.879-174.565  1.00 55.03           C  
ANISOU 3259  CD  LYS B  72     4841   9465   6603   1676    656   2689       C  
ATOM   3260  CE  LYS B  72      51.574  21.346-175.769  1.00 57.61           C  
ANISOU 3260  CE  LYS B  72     5003  10045   6841   1579    513   2740       C  
ATOM   3261  NZ  LYS B  72      51.262  22.428-176.762  1.00 65.34           N  
ANISOU 3261  NZ  LYS B  72     5991  11084   7750   1749    583   2861       N  
ATOM   3262  N   ASN B  73      53.765  18.071-172.204  1.00 48.17           N  
ANISOU 3262  N   ASN B  73     3922   8459   5921   1052    374   2273       N  
ATOM   3263  CA  ASN B  73      54.515  17.105-172.993  1.00 44.91           C  
ANISOU 3263  CA  ASN B  73     3509   8063   5493    855    207   2156       C  
ATOM   3264  C   ASN B  73      54.250  17.413-174.460  1.00 45.16           C  
ANISOU 3264  C   ASN B  73     3502   8223   5433    883    137   2216       C  
ATOM   3265  O   ASN B  73      53.096  17.401-174.898  1.00 51.99           O  
ANISOU 3265  O   ASN B  73     4247   9270   6235    887    110   2311       O  
ATOM   3266  CB  ASN B  73      54.110  15.669-172.666  1.00 45.98           C  
ANISOU 3266  CB  ASN B  73     3558   8283   5629    616     82   2082       C  
ATOM   3267  CG  ASN B  73      54.817  14.661-173.551  1.00 54.88           C  
ANISOU 3267  CG  ASN B  73     4711   9418   6723    413    -87   1959       C  
ATOM   3268  OD1 ASN B  73      54.515  14.535-174.746  1.00 52.57           O  
ANISOU 3268  OD1 ASN B  73     4379   9248   6349    372   -181   1977       O  
ATOM   3269  ND2 ASN B  73      55.769  13.949-172.978  1.00 49.08           N  
ANISOU 3269  ND2 ASN B  73     4121   8494   6032    277   -108   1799       N  
ATOM   3270  N   TRP B  74      55.304  17.682-175.214  1.00 41.80           N  
ANISOU 3270  N   TRP B  74     3176   7710   4998    902    110   2164       N  
ATOM   3271  CA  TRP B  74      55.107  18.170-176.574  1.00 44.07           C  
ANISOU 3271  CA  TRP B  74     3448   8101   5194    964     75   2232       C  
ATOM   3272  C   TRP B  74      54.952  17.060-177.602  1.00 50.08           C  
ANISOU 3272  C   TRP B  74     4142   9012   5876    760   -110   2166       C  
ATOM   3273  O   TRP B  74      54.446  17.321-178.701  1.00 50.56           O  
ANISOU 3273  O   TRP B  74     4151   9210   5849    792   -149   2233       O  
ATOM   3274  CB  TRP B  74      56.258  19.099-176.966  1.00 43.18           C  
ANISOU 3274  CB  TRP B  74     3490   7819   5097   1100    151   2227       C  
ATOM   3275  CG  TRP B  74      56.162  20.397-176.246  1.00 53.38           C  
ANISOU 3275  CG  TRP B  74     4866   8977   6438   1323    347   2316       C  
ATOM   3276  CD1 TRP B  74      56.682  20.690-175.021  1.00 54.23           C  
ANISOU 3276  CD1 TRP B  74     5123   8855   6626   1339    465   2237       C  
ATOM   3277  CD2 TRP B  74      55.474  21.573-176.684  1.00 58.48           C  
ANISOU 3277  CD2 TRP B  74     5519   9664   7037   1515    464   2455       C  
ATOM   3278  NE1 TRP B  74      56.365  21.979-174.670  1.00 53.86           N  
ANISOU 3278  NE1 TRP B  74     5134   8735   6595   1573    639   2356       N  
ATOM   3279  CE2 TRP B  74      55.629  22.545-175.677  1.00 56.39           C  
ANISOU 3279  CE2 TRP B  74     5379   9209   6837   1679    646   2485       C  
ATOM   3280  CE3 TRP B  74      54.749  21.901-177.835  1.00 59.86           C  
ANISOU 3280  CE3 TRP B  74     5613  10014   7118   1564    436   2552       C  
ATOM   3281  CZ2 TRP B  74      55.085  23.820-175.781  1.00 55.62           C  
ANISOU 3281  CZ2 TRP B  74     5337   9085   6710   1884    802   2608       C  
ATOM   3282  CZ3 TRP B  74      54.209  23.170-177.937  1.00 62.16           C  
ANISOU 3282  CZ3 TRP B  74     5939  10293   7386   1776    591   2683       C  
ATOM   3283  CH2 TRP B  74      54.381  24.114-176.916  1.00 62.17           C  
ANISOU 3283  CH2 TRP B  74     6075  10097   7452   1933    773   2709       C  
ATOM   3284  N   GLU B  75      55.377  15.840-177.287  1.00 45.99           N  
ANISOU 3284  N   GLU B  75     3635   8460   5381    552   -219   2033       N  
ATOM   3285  CA  GLU B  75      55.164  14.731-178.208  1.00 49.95           C  
ANISOU 3285  CA  GLU B  75     4098   9079   5801    348   -387   1959       C  
ATOM   3286  C   GLU B  75      53.687  14.363-178.303  1.00 58.00           C  
ANISOU 3286  C   GLU B  75     4967  10294   6777    285   -428   2036       C  
ATOM   3287  O   GLU B  75      53.161  14.160-179.405  1.00 58.32           O  
ANISOU 3287  O   GLU B  75     4951  10484   6725    233   -518   2059       O  
ATOM   3288  CB  GLU B  75      56.002  13.529-177.771  1.00 48.11           C  
ANISOU 3288  CB  GLU B  75     3942   8733   5605    147   -474   1795       C  
ATOM   3289  CG  GLU B  75      55.652  12.238-178.487  1.00 55.23           C  
ANISOU 3289  CG  GLU B  75     4827   9725   6431    -82   -632   1705       C  
ATOM   3290  CD  GLU B  75      56.566  11.090-178.105  1.00 58.04           C  
ANISOU 3290  CD  GLU B  75     5294   9941   6818   -267   -704   1540       C  
ATOM   3291  OE1 GLU B  75      57.579  11.331-177.412  1.00 56.81           O  
ANISOU 3291  OE1 GLU B  75     5263   9587   6736   -217   -621   1474       O  
ATOM   3292  OE2 GLU B  75      56.269   9.944-178.500  1.00 61.91           O  
ANISOU 3292  OE2 GLU B  75     5798  10467   7258   -461   -817   1456       O  
ATOM   3293  N   VAL B  76      52.993  14.317-177.166  1.00 56.41           N  
ANISOU 3293  N   VAL B  76     4698  10099   6637    298   -360   2084       N  
ATOM   3294  CA  VAL B  76      51.644  13.761-177.080  1.00 61.00           C  
ANISOU 3294  CA  VAL B  76     5136  10855   7188    205   -408   2147       C  
ATOM   3295  C   VAL B  76      50.605  14.871-176.972  1.00 68.66           C  
ANISOU 3295  C   VAL B  76     6000  11945   8142    412   -291   2330       C  
ATOM   3296  O   VAL B  76      49.489  14.746-177.491  1.00 77.52           O  
ANISOU 3296  O   VAL B  76     6989  13265   9201    382   -340   2419       O  
ATOM   3297  CB  VAL B  76      51.544  12.789-175.885  1.00 68.94           C  
ANISOU 3297  CB  VAL B  76     6139  11792   8264     56   -418   2076       C  
ATOM   3298  CG1 VAL B  76      50.092  12.469-175.539  1.00 69.64           C  
ANISOU 3298  CG1 VAL B  76     6073  12050   8338     10   -424   2176       C  
ATOM   3299  CG2 VAL B  76      52.306  11.505-176.184  1.00 68.39           C  
ANISOU 3299  CG2 VAL B  76     6161  11638   8185   -178   -553   1903       C  
ATOM   3300  N   GLY B  77      50.962  15.966-176.300  1.00 67.13           N  
ANISOU 3300  N   GLY B  77     5874  11629   8002    624   -133   2388       N  
ATOM   3301  CA  GLY B  77      50.033  17.041-176.003  1.00 62.26           C  
ANISOU 3301  CA  GLY B  77     5191  11088   7376    836      4   2556       C  
ATOM   3302  C   GLY B  77      49.546  17.075-174.564  1.00 69.53           C  
ANISOU 3302  C   GLY B  77     6091  11963   8365    886    111   2596       C  
ATOM   3303  O   GLY B  77      48.740  17.950-174.224  1.00 75.77           O  
ANISOU 3303  O   GLY B  77     6836  12808   9144   1069    235   2738       O  
ATOM   3304  N   SER B  78      50.011  16.160-173.713  1.00 66.05           N  
ANISOU 3304  N   SER B  78     5688  11419   7987    735     72   2478       N  
ATOM   3305  CA  SER B  78      49.584  16.105-172.317  1.00 73.68           C  
ANISOU 3305  CA  SER B  78     6641  12339   9015    771    171   2507       C  
ATOM   3306  C   SER B  78      49.885  17.411-171.591  1.00 73.51           C  
ANISOU 3306  C   SER B  78     6729  12169   9031   1026    365   2567       C  
ATOM   3307  O   SER B  78      50.868  18.097-171.877  1.00 74.38           O  
ANISOU 3307  O   SER B  78     6969  12134   9156   1122    414   2525       O  
ATOM   3308  CB  SER B  78      50.289  14.958-171.585  1.00 75.67           C  
ANISOU 3308  CB  SER B  78     6948  12474   9329    571    105   2354       C  
ATOM   3309  OG  SER B  78      50.113  13.718-172.242  1.00 78.77           O  
ANISOU 3309  OG  SER B  78     7282  12962   9686    327    -67   2280       O  
ATOM   3310  N   ILE B  79      49.043  17.729-170.611  1.00 68.69           N  
ANISOU 3310  N   ILE B  79     6078  11583   8436   1132    479   2661       N  
ATOM   3311  CA  ILE B  79      49.201  18.910-169.768  1.00 60.01           C  
ANISOU 3311  CA  ILE B  79     5104  10331   7366   1370    675   2714       C  
ATOM   3312  C   ILE B  79      48.913  18.511-168.321  1.00 59.88           C  
ANISOU 3312  C   ILE B  79     5092  10259   7401   1353    747   2698       C  
ATOM   3313  O   ILE B  79      47.878  17.901-168.036  1.00 64.62           O  
ANISOU 3313  O   ILE B  79     5549  11017   7986   1280    709   2764       O  
ATOM   3314  CB  ILE B  79      48.267  20.052-170.225  1.00 61.53           C  
ANISOU 3314  CB  ILE B  79     5256  10628   7493   1587    776   2891       C  
ATOM   3315  CG1 ILE B  79      48.903  20.854-171.367  1.00 59.95           C  
ANISOU 3315  CG1 ILE B  79     5138  10381   7257   1676    780   2895       C  
ATOM   3316  CG2 ILE B  79      47.883  20.960-169.068  1.00 58.27           C  
ANISOU 3316  CG2 ILE B  79     4930  10110   7098   1800    974   2971       C  
ATOM   3317  CD1 ILE B  79      48.014  21.991-171.860  1.00 67.61           C  
ANISOU 3317  CD1 ILE B  79     6077  11453   8159   1889    887   3071       C  
ATOM   3318  N   THR B  80      49.837  18.837-167.412  1.00 53.90           N  
ANISOU 3318  N   THR B  80     4500   9279   6700   1414    853   2609       N  
ATOM   3319  CA  THR B  80      49.665  18.605-165.981  1.00 58.03           C  
ANISOU 3319  CA  THR B  80     5062   9725   7263   1425    949   2589       C  
ATOM   3320  C   THR B  80      50.110  19.848-165.221  1.00 58.60           C  
ANISOU 3320  C   THR B  80     5335   9584   7347   1653   1148   2593       C  
ATOM   3321  O   THR B  80      50.692  20.776-165.789  1.00 53.86           O  
ANISOU 3321  O   THR B  80     4852   8878   6737   1772   1201   2592       O  
ATOM   3322  CB  THR B  80      50.461  17.383-165.485  1.00 60.19           C  
ANISOU 3322  CB  THR B  80     5351   9929   7590   1198    858   2435       C  
ATOM   3323  OG1 THR B  80      51.865  17.635-165.618  1.00 56.07           O  
ANISOU 3323  OG1 THR B  80     4981   9222   7102   1193    872   2314       O  
ATOM   3324  CG2 THR B  80      50.105  16.138-166.279  1.00 63.47           C  
ANISOU 3324  CG2 THR B  80     5611  10518   7988    957    660   2412       C  
ATOM   3325  N   TYR B  81      49.836  19.856-163.917  1.00 54.37           N  
ANISOU 3325  N   TYR B  81     4855   8977   6827   1707   1262   2592       N  
ATOM   3326  CA  TYR B  81      50.202  20.951-163.025  1.00 52.36           C  
ANISOU 3326  CA  TYR B  81     4819   8503   6571   1906   1457   2579       C  
ATOM   3327  C   TYR B  81      50.981  20.384-161.854  1.00 58.37           C  
ANISOU 3327  C   TYR B  81     5695   9112   7371   1810   1497   2438       C  
ATOM   3328  O   TYR B  81      50.499  19.473-161.175  1.00 59.67           O  
ANISOU 3328  O   TYR B  81     5762   9363   7545   1699   1463   2437       O  
ATOM   3329  CB  TYR B  81      48.960  21.703-162.519  1.00 58.04           C  
ANISOU 3329  CB  TYR B  81     5522   9284   7245   2107   1589   2737       C  
ATOM   3330  CG  TYR B  81      48.223  22.409-163.633  1.00 60.02           C  
ANISOU 3330  CG  TYR B  81     5684   9676   7444   2224   1579   2887       C  
ATOM   3331  CD1 TYR B  81      47.283  21.736-164.404  1.00 66.93           C  
ANISOU 3331  CD1 TYR B  81     6317  10820   8294   2124   1445   2983       C  
ATOM   3332  CD2 TYR B  81      48.494  23.735-163.939  1.00 67.00           C  
ANISOU 3332  CD2 TYR B  81     6738  10421   8297   2420   1705   2928       C  
ATOM   3333  CE1 TYR B  81      46.623  22.373-165.447  1.00 77.35           C  
ANISOU 3333  CE1 TYR B  81     7555  12281   9554   2227   1440   3121       C  
ATOM   3334  CE2 TYR B  81      47.834  24.382-164.976  1.00 71.99           C  
ANISOU 3334  CE2 TYR B  81     7293  11188   8873   2525   1705   3070       C  
ATOM   3335  CZ  TYR B  81      46.901  23.694-165.724  1.00 71.53           C  
ANISOU 3335  CZ  TYR B  81     6982  11411   8786   2432   1573   3167       C  
ATOM   3336  OH  TYR B  81      46.245  24.326-166.751  1.00 76.37           O  
ANISOU 3336  OH  TYR B  81     7515  12169   9334   2535   1578   3307       O  
ATOM   3337  N   ASP B  82      52.180  20.913-161.618  1.00 57.43           N  
ANISOU 3337  N   ASP B  82     5787   8766   7266   1844   1573   2322       N  
ATOM   3338  CA  ASP B  82      53.038  20.386-160.555  1.00 52.86           C  
ANISOU 3338  CA  ASP B  82     5368   8016   6698   1717   1583   2164       C  
ATOM   3339  C   ASP B  82      52.670  21.092-159.254  1.00 58.98           C  
ANISOU 3339  C   ASP B  82     6287   8683   7441   1898   1790   2194       C  
ATOM   3340  O   ASP B  82      53.207  22.147-158.913  1.00 64.85           O  
ANISOU 3340  O   ASP B  82     7275   9207   8159   2024   1908   2141       O  
ATOM   3341  CB  ASP B  82      54.509  20.555-160.915  1.00 55.78           C  
ANISOU 3341  CB  ASP B  82     5958   8159   7078   1600   1496   1989       C  
ATOM   3342  CG  ASP B  82      55.428  19.808-159.966  1.00 57.16           C  
ANISOU 3342  CG  ASP B  82     6285   8175   7257   1416   1433   1816       C  
ATOM   3343  OD1 ASP B  82      55.332  20.043-158.748  1.00 63.96           O  
ANISOU 3343  OD1 ASP B  82     7274   8936   8091   1481   1551   1794       O  
ATOM   3344  OD2 ASP B  82      56.241  18.983-160.436  1.00 56.14           O  
ANISOU 3344  OD2 ASP B  82     6154   8026   7152   1215   1270   1706       O  
ATOM   3345  N   THR B  83      51.733  20.495-158.515  1.00 58.99           N  
ANISOU 3345  N   THR B  83     6174   8806   7433   1880   1800   2258       N  
ATOM   3346  CA  THR B  83      51.348  21.026-157.214  1.00 56.23           C  
ANISOU 3346  CA  THR B  83     5977   8345   7041   2023   1964   2271       C  
ATOM   3347  C   THR B  83      52.358  20.681-156.128  1.00 58.38           C  
ANISOU 3347  C   THR B  83     6450   8435   7295   1931   2016   2114       C  
ATOM   3348  O   THR B  83      52.390  21.353-155.094  1.00 66.35           O  
ANISOU 3348  O   THR B  83     7671   9285   8254   2056   2162   2082       O  
ATOM   3349  CB  THR B  83      49.961  20.507-156.824  1.00 55.27           C  
ANISOU 3349  CB  THR B  83     5660   8425   6915   2036   1955   2404       C  
ATOM   3350  OG1 THR B  83      49.972  19.072-156.782  1.00 58.66           O  
ANISOU 3350  OG1 THR B  83     5925   8984   7380   1799   1819   2364       O  
ATOM   3351  CG2 THR B  83      48.907  20.981-157.832  1.00 58.45           C  
ANISOU 3351  CG2 THR B  83     5889   9007   7310   2144   1921   2573       C  
ATOM   3352  N   LEU B  84      53.192  19.664-156.347  1.00 55.33           N  
ANISOU 3352  N   LEU B  84     6060   8024   6940   1677   1830   1984       N  
ATOM   3353  CA  LEU B  84      54.162  19.263-155.335  1.00 50.93           C  
ANISOU 3353  CA  LEU B  84     5720   7271   6358   1546   1798   1815       C  
ATOM   3354  C   LEU B  84      55.264  20.304-155.160  1.00 49.57           C  
ANISOU 3354  C   LEU B  84     5847   6830   6156   1595   1841   1686       C  
ATOM   3355  O   LEU B  84      55.859  20.398-154.079  1.00 51.68           O  
ANISOU 3355  O   LEU B  84     6332   6926   6377   1568   1882   1574       O  
ATOM   3356  CB  LEU B  84      54.763  17.901-155.700  1.00 46.38           C  
ANISOU 3356  CB  LEU B  84     5057   6740   5824   1277   1587   1721       C  
ATOM   3357  CG  LEU B  84      55.775  17.252-154.751  1.00 46.77           C  
ANISOU 3357  CG  LEU B  84     5291   6625   5853   1120   1521   1559       C  
ATOM   3358  CD1 LEU B  84      55.147  16.942-153.396  1.00 44.40           C  
ANISOU 3358  CD1 LEU B  84     5016   6346   5509   1164   1635   1598       C  
ATOM   3359  CD2 LEU B  84      56.366  15.989-155.370  1.00 48.35           C  
ANISOU 3359  CD2 LEU B  84     5400   6872   6101    883   1318   1483       C  
ATOM   3360  N   SER B  85      55.559  21.084-156.204  1.00 49.30           N  
ANISOU 3360  N   SER B  85     5831   6758   6144   1656   1830   1700       N  
ATOM   3361  CA  SER B  85      56.644  22.055-156.100  1.00 46.52           C  
ANISOU 3361  CA  SER B  85     5758   6147   5769   1675   1863   1578       C  
ATOM   3362  C   SER B  85      56.350  23.122-155.051  1.00 58.03           C  
ANISOU 3362  C   SER B  85     7437   7454   7160   1871   2074   1589       C  
ATOM   3363  O   SER B  85      57.280  23.708-154.490  1.00 56.67           O  
ANISOU 3363  O   SER B  85     7535   7048   6951   1840   2099   1455       O  
ATOM   3364  CB  SER B  85      56.906  22.712-157.460  1.00 53.62           C  
ANISOU 3364  CB  SER B  85     6626   7044   6704   1716   1829   1615       C  
ATOM   3365  OG  SER B  85      55.837  23.550-157.850  1.00 60.13           O  
ANISOU 3365  OG  SER B  85     7368   7962   7517   1956   1975   1787       O  
ATOM   3366  N   ALA B  86      55.071  23.395-154.777  1.00 66.08           N  
ANISOU 3366  N   ALA B  86     8347   8604   8156   2073   2229   1748       N  
ATOM   3367  CA  ALA B  86      54.725  24.363-153.742  1.00 74.37           C  
ANISOU 3367  CA  ALA B  86     9614   9512   9132   2277   2446   1763       C  
ATOM   3368  C   ALA B  86      55.242  23.951-152.371  1.00 71.97           C  
ANISOU 3368  C   ALA B  86     9500   9079   8768   2173   2448   1626       C  
ATOM   3369  O   ALA B  86      55.416  24.814-151.506  1.00 75.46           O  
ANISOU 3369  O   ALA B  86    10213   9325   9132   2285   2593   1568       O  
ATOM   3370  CB  ALA B  86      53.210  24.570-153.693  1.00 68.65           C  
ANISOU 3370  CB  ALA B  86     8714   8967   8402   2473   2548   1962       C  
ATOM   3371  N   GLN B  87      55.503  22.662-152.160  1.00 65.29           N  
ANISOU 3371  N   GLN B  87     8532   8330   7947   1962   2292   1570       N  
ATOM   3372  CA  GLN B  87      56.044  22.163-150.905  1.00 65.03           C  
ANISOU 3372  CA  GLN B  87     8664   8191   7854   1852   2272   1445       C  
ATOM   3373  C   GLN B  87      57.566  22.207-150.852  1.00 62.04           C  
ANISOU 3373  C   GLN B  87     8494   7609   7469   1668   2135   1251       C  
ATOM   3374  O   GLN B  87      58.148  21.674-149.904  1.00 56.80           O  
ANISOU 3374  O   GLN B  87     7948   6874   6758   1548   2081   1142       O  
ATOM   3375  CB  GLN B  87      55.580  20.725-150.661  1.00 75.59           C  
ANISOU 3375  CB  GLN B  87     9776   9726   9220   1719   2179   1491       C  
ATOM   3376  CG  GLN B  87      54.096  20.496-150.884  1.00 84.65           C  
ANISOU 3376  CG  GLN B  87    10652  11118  10392   1851   2276   1693       C  
ATOM   3377  CD  GLN B  87      53.571  19.329-150.076  1.00 88.66           C  
ANISOU 3377  CD  GLN B  87    11039  11758  10890   1759   2263   1731       C  
ATOM   3378  OE1 GLN B  87      53.879  18.171-150.357  1.00 96.26           O  
ANISOU 3378  OE1 GLN B  87    11877  12797  11902   1547   2093   1693       O  
ATOM   3379  NE2 GLN B  87      52.780  19.631-149.057  1.00 90.19           N  
ANISOU 3379  NE2 GLN B  87    11279  11970  11017   1923   2452   1810       N  
ATOM   3380  N   ALA B  88      58.220  22.826-151.841  1.00 55.84           N  
ANISOU 3380  N   ALA B  88     7749   6741   6728   1645   2080   1214       N  
ATOM   3381  CA  ALA B  88      59.678  22.839-151.941  1.00 58.63           C  
ANISOU 3381  CA  ALA B  88     8257   6930   7090   1459   1940   1046       C  
ATOM   3382  C   ALA B  88      60.334  23.285-150.642  1.00 62.86           C  
ANISOU 3382  C   ALA B  88     9091   7261   7531   1435   1991    912       C  
ATOM   3383  O   ALA B  88      60.183  24.437-150.220  1.00 68.06           O  
ANISOU 3383  O   ALA B  88     9965   7768   8127   1579   2148    905       O  
ATOM   3384  CB  ALA B  88      60.133  23.742-153.092  1.00 60.81           C  
ANISOU 3384  CB  ALA B  88     8568   7125   7411   1487   1934   1049       C  
ATOM   3385  N   GLN B  89      61.089  22.371-150.027  1.00 74.98           N  
ANISOU 3385  N   GLN B  89    10648   8790   9049   1251   1854    805       N  
ATOM   3386  CA  GLN B  89      61.617  22.590-148.683  1.00 83.79           C  
ANISOU 3386  CA  GLN B  89    12021   9754  10060   1218   1884    686       C  
ATOM   3387  C   GLN B  89      62.693  23.672-148.669  1.00 89.56           C  
ANISOU 3387  C   GLN B  89    13011  10257  10759   1167   1877    557       C  
ATOM   3388  O   GLN B  89      62.711  24.527-147.775  1.00 93.21           O  
ANISOU 3388  O   GLN B  89    13733  10559  11122   1242   1996    499       O  
ATOM   3389  CB  GLN B  89      62.166  21.273-148.122  1.00 78.16           C  
ANISOU 3389  CB  GLN B  89    11243   9112   9341   1036   1726    620       C  
ATOM   3390  CG  GLN B  89      61.317  20.657-147.008  1.00 83.96           C  
ANISOU 3390  CG  GLN B  89    11963   9931  10005   1101   1810    675       C  
ATOM   3391  CD  GLN B  89      60.680  19.321-147.390  1.00 84.91           C  
ANISOU 3391  CD  GLN B  89    11796  10267  10199   1044   1737    777       C  
ATOM   3392  OE1 GLN B  89      60.801  18.856-148.525  1.00 72.50           O  
ANISOU 3392  OE1 GLN B  89    10035   8786   8725    965   1626    807       O  
ATOM   3393  NE2 GLN B  89      59.996  18.698-146.431  1.00 86.99           N  
ANISOU 3393  NE2 GLN B  89    12038  10608  10408   1078   1803    829       N  
ATOM   3394  N   GLN B  90      63.601  23.652-149.642  1.00 80.23           N  
ANISOU 3394  N   GLN B  90    11771   9057   9657   1033   1741    510       N  
ATOM   3395  CA  GLN B  90      64.719  24.587-149.689  1.00 80.75           C  
ANISOU 3395  CA  GLN B  90    12056   8918   9705    946   1714    389       C  
ATOM   3396  C   GLN B  90      64.705  25.351-151.015  1.00 80.16           C  
ANISOU 3396  C   GLN B  90    11929   8817   9711   1005   1749    453       C  
ATOM   3397  O   GLN B  90      63.834  25.154-151.867  1.00 82.06           O  
ANISOU 3397  O   GLN B  90    11965   9203  10011   1117   1787    587       O  
ATOM   3398  CB  GLN B  90      66.048  23.854-149.475  1.00 83.77           C  
ANISOU 3398  CB  GLN B  90    12439   9292  10097    709   1511    262       C  
ATOM   3399  CG  GLN B  90      67.183  24.736-148.969  1.00 92.62           C  
ANISOU 3399  CG  GLN B  90    13827  10205  11159    597   1485    118       C  
ATOM   3400  CD  GLN B  90      68.258  23.955-148.246  1.00 97.93           C  
ANISOU 3400  CD  GLN B  90    14522  10891  11797    400   1312      2       C  
ATOM   3401  OE1 GLN B  90      67.982  22.932-147.617  1.00101.62           O  
ANISOU 3401  OE1 GLN B  90    14903  11473  12234    390   1266     17       O  
ATOM   3402  NE2 GLN B  90      69.494  24.437-148.326  1.00 96.33           N  
ANISOU 3402  NE2 GLN B  90    14431  10573  11595    242   1218   -106       N  
ATOM   3403  N   ASP B  91      65.677  26.244-151.176  1.00 68.00           N  
ANISOU 3403  N   ASP B  91    10578   7092   8167    923   1735    359       N  
ATOM   3404  CA  ASP B  91      65.721  27.163-152.301  1.00 66.07           C  
ANISOU 3404  CA  ASP B  91    10344   6778   7981    985   1795    413       C  
ATOM   3405  C   ASP B  91      66.866  26.801-153.241  1.00 65.46           C  
ANISOU 3405  C   ASP B  91    10157   6726   7989    793   1622    363       C  
ATOM   3406  O   ASP B  91      67.958  26.429-152.798  1.00 61.18           O  
ANISOU 3406  O   ASP B  91     9666   6142   7437    601   1489    242       O  
ATOM   3407  CB  ASP B  91      65.870  28.608-151.821  1.00 65.55           C  
ANISOU 3407  CB  ASP B  91    10604   6457   7846   1055   1946    359       C  
ATOM   3408  CG  ASP B  91      64.575  29.178-151.256  1.00 72.68           C  
ANISOU 3408  CG  ASP B  91    11602   7334   8677   1311   2162    450       C  
ATOM   3409  OD1 ASP B  91      63.588  28.422-151.114  1.00 80.81           O  
ANISOU 3409  OD1 ASP B  91    12439   8554   9709   1419   2189    551       O  
ATOM   3410  OD2 ASP B  91      64.544  30.387-150.955  1.00 77.38           O  
ANISOU 3410  OD2 ASP B  91    12469   7717   9214   1405   2313    423       O  
ATOM   3411  N   GLY B  92      66.607  26.911-154.541  1.00 63.62           N  
ANISOU 3411  N   GLY B  92     9768   6572   7834    853   1627    464       N  
ATOM   3412  CA  GLY B  92      67.617  26.665-155.542  1.00 47.57           C  
ANISOU 3412  CA  GLY B  92     7635   4561   5878    700   1491    432       C  
ATOM   3413  C   GLY B  92      68.312  27.947-155.967  1.00 49.64           C  
ANISOU 3413  C   GLY B  92     8089   4623   6151    676   1554    399       C  
ATOM   3414  O   GLY B  92      68.203  28.992-155.316  1.00 47.09           O  
ANISOU 3414  O   GLY B  92     8014   4111   5766    740   1684    367       O  
ATOM   3415  N   PRO B  93      69.036  27.889-157.083  1.00 45.58           N  
ANISOU 3415  N   PRO B  93     7471   4138   5711    582   1470    409       N  
ATOM   3416  CA  PRO B  93      69.859  29.030-157.514  1.00 44.27           C  
ANISOU 3416  CA  PRO B  93     7477   3781   5563    521   1514    374       C  
ATOM   3417  C   PRO B  93      69.178  30.035-158.433  1.00 44.51           C  
ANISOU 3417  C   PRO B  93     7546   3754   5611    703   1667    498       C  
ATOM   3418  O   PRO B  93      69.787  31.068-158.734  1.00 47.25           O  
ANISOU 3418  O   PRO B  93     8066   3919   5969    662   1727    476       O  
ATOM   3419  CB  PRO B  93      71.011  28.330-158.245  1.00 52.61           C  
ANISOU 3419  CB  PRO B  93     8378   4922   6689    328   1344    330       C  
ATOM   3420  CG  PRO B  93      70.368  27.116-158.839  1.00 46.80           C  
ANISOU 3420  CG  PRO B  93     7371   4426   5986    385   1268    410       C  
ATOM   3421  CD  PRO B  93      69.325  26.664-157.853  1.00 43.66           C  
ANISOU 3421  CD  PRO B  93     6967   4093   5530    491   1313    428       C  
ATOM   3422  N   CYS B  94      67.948  29.790-158.874  1.00 44.36           N  
ANISOU 3422  N   CYS B  94     7376   3886   5593    899   1732    634       N  
ATOM   3423  CA  CYS B  94      67.298  30.658-159.846  1.00 46.15           C  
ANISOU 3423  CA  CYS B  94     7606   4093   5837   1084   1863    771       C  
ATOM   3424  C   CYS B  94      66.534  31.793-159.174  1.00 57.85           C  
ANISOU 3424  C   CYS B  94     9321   5404   7254   1280   2071    810       C  
ATOM   3425  O   CYS B  94      66.075  31.679-158.036  1.00 50.84           O  
ANISOU 3425  O   CYS B  94     8519   4492   6305   1328   2122    770       O  
ATOM   3426  CB  CYS B  94      66.339  29.858-160.727  1.00 43.61           C  
ANISOU 3426  CB  CYS B  94     6992   4036   5542   1201   1824    909       C  
ATOM   3427  SG  CYS B  94      67.099  28.562-161.733  1.00 43.46           S  
ANISOU 3427  SG  CYS B  94     6711   4214   5590   1008   1603    881       S  
ATOM   3428  N   THR B  95      66.385  32.888-159.905  1.00 57.24           N  
ANISOU 3428  N   THR B  95     9352   5209   7187   1404   2200    896       N  
ATOM   3429  CA  THR B  95      65.548  34.015-159.519  1.00 60.75           C  
ANISOU 3429  CA  THR B  95     9955   5570   7556   1597   2388    946       C  
ATOM   3430  C   THR B  95      64.703  34.412-160.715  1.00 60.02           C  
ANISOU 3430  C   THR B  95     9714   5611   7480   1794   2464   1123       C  
ATOM   3431  O   THR B  95      64.914  33.921-161.828  1.00 58.14           O  
ANISOU 3431  O   THR B  95     9295   5484   7310   1767   2374   1192       O  
ATOM   3432  CB  THR B  95      66.393  35.214-159.052  1.00 58.22           C  
ANISOU 3432  CB  THR B  95     9919   5021   7182   1472   2436    818       C  
ATOM   3433  OG1 THR B  95      67.037  35.801-160.182  1.00 52.80           O  
ANISOU 3433  OG1 THR B  95     9225   4292   6546   1408   2419    842       O  
ATOM   3434  CG2 THR B  95      67.441  34.795-158.025  1.00 55.35           C  
ANISOU 3434  CG2 THR B  95     9676   4550   6803   1231   2319    637       C  
ATOM   3435  N   PRO B  96      63.714  35.293-160.523  1.00 56.02           N  
ANISOU 3435  N   PRO B  96     9277   5108   6901   1996   2630   1208       N  
ATOM   3436  CA  PRO B  96      62.991  35.828-161.686  1.00 59.09           C  
ANISOU 3436  CA  PRO B  96     9545   5614   7293   2171   2705   1372       C  
ATOM   3437  C   PRO B  96      63.887  36.581-162.649  1.00 59.86           C  
ANISOU 3437  C   PRO B  96     9724   5597   7422   2078   2692   1348       C  
ATOM   3438  O   PRO B  96      63.502  36.773-163.808  1.00 65.82           O  
ANISOU 3438  O   PRO B  96    10343   6471   8195   2185   2708   1477       O  
ATOM   3439  CB  PRO B  96      61.942  36.757-161.059  1.00 63.91           C  
ANISOU 3439  CB  PRO B  96    10280   6200   7805   2374   2897   1443       C  
ATOM   3440  CG  PRO B  96      61.730  36.213-159.698  1.00 52.21           C  
ANISOU 3440  CG  PRO B  96     8858   4698   6283   2352   2899   1368       C  
ATOM   3441  CD  PRO B  96      63.061  35.669-159.254  1.00 55.90           C  
ANISOU 3441  CD  PRO B  96     9416   5032   6792   2092   2753   1183       C  
ATOM   3442  N   ARG B  97      65.070  37.013-162.210  1.00 58.71           N  
ANISOU 3442  N   ARG B  97     9788   5239   7278   1876   2659   1192       N  
ATOM   3443  CA  ARG B  97      65.976  37.732-163.097  1.00 64.57           C  
ANISOU 3443  CA  ARG B  97    10604   5875   8056   1771   2647   1171       C  
ATOM   3444  C   ARG B  97      66.748  36.785-164.007  1.00 60.28           C  
ANISOU 3444  C   ARG B  97     9871   5427   7604   1627   2481   1173       C  
ATOM   3445  O   ARG B  97      66.983  37.101-165.175  1.00 62.66           O  
ANISOU 3445  O   ARG B  97    10109   5759   7938   1640   2479   1244       O  
ATOM   3446  CB  ARG B  97      66.962  38.562-162.282  1.00 72.22           C  
ANISOU 3446  CB  ARG B  97    11851   6599   8989   1592   2665   1010       C  
ATOM   3447  CG  ARG B  97      66.398  39.127-160.997  1.00 90.82           C  
ANISOU 3447  CG  ARG B  97    14410   8853  11244   1670   2784    963       C  
ATOM   3448  CD  ARG B  97      67.301  40.216-160.436  1.00 95.37           C  
ANISOU 3448  CD  ARG B  97    15273   9190  11774   1513   2820    831       C  
ATOM   3449  NE  ARG B  97      67.316  41.408-161.281  1.00 89.85           N  
ANISOU 3449  NE  ARG B  97    14670   8401  11068   1583   2934    899       N  
ATOM   3450  CZ  ARG B  97      68.228  41.653-162.215  1.00 89.43           C  
ANISOU 3450  CZ  ARG B  97    14591   8305  11083   1452   2872    889       C  
ATOM   3451  NH1 ARG B  97      69.208  40.784-162.429  1.00 90.63           N  
ANISOU 3451  NH1 ARG B  97    14618   8502  11314   1242   2697    818       N  
ATOM   3452  NH2 ARG B  97      68.161  42.766-162.938  1.00 89.22           N  
ANISOU 3452  NH2 ARG B  97    14664   8193  11044   1533   2991    957       N  
ATOM   3453  N   ARG B  98      67.150  35.628-163.490  1.00 51.38           N  
ANISOU 3453  N   ARG B  98     8661   4349   6514   1493   2348   1099       N  
ATOM   3454  CA  ARG B  98      68.126  34.798-164.182  1.00 53.18           C  
ANISOU 3454  CA  ARG B  98     8760   4626   6819   1312   2194   1073       C  
ATOM   3455  C   ARG B  98      67.964  33.352-163.748  1.00 46.97           C  
ANISOU 3455  C   ARG B  98     7802   3989   6055   1262   2068   1055       C  
ATOM   3456  O   ARG B  98      67.841  33.066-162.556  1.00 46.71           O  
ANISOU 3456  O   ARG B  98     7838   3924   5986   1228   2061    966       O  
ATOM   3457  CB  ARG B  98      69.543  35.275-163.871  1.00 49.52           C  
ANISOU 3457  CB  ARG B  98     8466   3977   6372   1063   2143    922       C  
ATOM   3458  CG  ARG B  98      69.662  35.726-162.406  1.00 61.16           C  
ANISOU 3458  CG  ARG B  98    10158   5300   7780    999   2181    787       C  
ATOM   3459  CD  ARG B  98      71.084  35.570-161.947  1.00 65.52           C  
ANISOU 3459  CD  ARG B  98    10784   5754   8358    712   2056    632       C  
ATOM   3460  NE  ARG B  98      71.235  35.421-160.504  1.00 54.11           N  
ANISOU 3460  NE  ARG B  98     9472   4236   6851    623   2026    500       N  
ATOM   3461  CZ  ARG B  98      70.842  34.356-159.805  1.00 47.98           C  
ANISOU 3461  CZ  ARG B  98     8617   3548   6065    641   1969    480       C  
ATOM   3462  NH1 ARG B  98      70.201  33.354-160.387  1.00 50.98           N  
ANISOU 3462  NH1 ARG B  98     8786   4090   6494    752   1941    589       N  
ATOM   3463  NH2 ARG B  98      71.064  34.311-158.505  1.00 71.04           N  
ANISOU 3463  NH2 ARG B  98    11675   6397   8919    551   1941    356       N  
ATOM   3464  N   CYS B  99      67.985  32.447-164.718  1.00 42.53           N  
ANISOU 3464  N   CYS B  99     6980   3651   5528   1225   1942   1105       N  
ATOM   3465  CA  CYS B  99      67.953  31.016-164.464  1.00 45.81           C  
ANISOU 3465  CA  CYS B  99     7178   4276   5950   1121   1777   1050       C  
ATOM   3466  C   CYS B  99      69.381  30.482-164.429  1.00 47.75           C  
ANISOU 3466  C   CYS B  99     7417   4489   6236    861   1632    912       C  
ATOM   3467  O   CYS B  99      70.171  30.741-165.344  1.00 44.76           O  
ANISOU 3467  O   CYS B  99     7030   4080   5896    783   1608    921       O  
ATOM   3468  CB  CYS B  99      67.116  30.308-165.535  1.00 38.69           C  
ANISOU 3468  CB  CYS B  99     6010   3637   5054   1229   1722   1180       C  
ATOM   3469  SG  CYS B  99      67.106  28.523-165.553  1.00 41.12           S  
ANISOU 3469  SG  CYS B  99     6049   4200   5375   1091   1518   1126       S  
ATOM   3470  N   LEU B 100      69.721  29.776-163.346  1.00 40.61           N  
ANISOU 3470  N   LEU B 100     6520   3591   5321    735   1545    792       N  
ATOM   3471  CA  LEU B 100      70.995  29.074-163.228  1.00 40.50           C  
ANISOU 3471  CA  LEU B 100     6460   3589   5341    503   1393    673       C  
ATOM   3472  C   LEU B 100      70.793  27.558-163.198  1.00 42.52           C  
ANISOU 3472  C   LEU B 100     6488   4065   5602    457   1250    657       C  
ATOM   3473  O   LEU B 100      71.579  26.815-162.596  1.00 40.13           O  
ANISOU 3473  O   LEU B 100     6163   3777   5306    299   1134    551       O  
ATOM   3474  CB  LEU B 100      71.759  29.550-161.994  1.00 45.88           C  
ANISOU 3474  CB  LEU B 100     7357   4078   5998    370   1399    540       C  
ATOM   3475  CG  LEU B 100      72.216  31.005-162.007  1.00 51.65           C  
ANISOU 3475  CG  LEU B 100     8337   4562   6726    355   1522    528       C  
ATOM   3476  CD1 LEU B 100      72.739  31.410-160.637  1.00 45.66           C  
ANISOU 3476  CD1 LEU B 100     7802   3627   5920    234   1525    392       C  
ATOM   3477  CD2 LEU B 100      73.287  31.212-163.071  1.00 48.44           C  
ANISOU 3477  CD2 LEU B 100     7883   4139   6384    227   1474    535       C  
ATOM   3478  N   GLY B 101      69.741  27.084-163.863  1.00 42.19           N  
ANISOU 3478  N   GLY B 101     6279   4198   5555    592   1255    766       N  
ATOM   3479  CA  GLY B 101      69.454  25.663-163.893  1.00 39.61           C  
ANISOU 3479  CA  GLY B 101     5749   4070   5230    546   1127    757       C  
ATOM   3480  C   GLY B 101      70.580  24.797-164.428  1.00 37.84           C  
ANISOU 3480  C   GLY B 101     5426   3905   5045    376    983    687       C  
ATOM   3481  O   GLY B 101      70.670  23.629-164.047  1.00 36.53           O  
ANISOU 3481  O   GLY B 101     5160   3839   4880    296    875    634       O  
ATOM   3482  N   SER B 102      71.447  25.333-165.294  1.00 37.40           N  
ANISOU 3482  N   SER B 102     5401   3787   5021    325    987    690       N  
ATOM   3483  CA  SER B 102      72.515  24.516-165.877  1.00 35.38           C  
ANISOU 3483  CA  SER B 102     5043   3600   4802    183    865    636       C  
ATOM   3484  C   SER B 102      73.747  24.380-164.982  1.00 37.98           C  
ANISOU 3484  C   SER B 102     5449   3831   5149     13    799    512       C  
ATOM   3485  O   SER B 102      74.686  23.669-165.350  1.00 36.70           O  
ANISOU 3485  O   SER B 102     5199   3728   5018    -98    701    469       O  
ATOM   3486  CB  SER B 102      72.953  25.093-167.229  1.00 35.96           C  
ANISOU 3486  CB  SER B 102     5099   3667   4898    200    899    701       C  
ATOM   3487  OG  SER B 102      73.723  26.273-167.066  1.00 41.12           O  
ANISOU 3487  OG  SER B 102     5919   4133   5573    149    978    679       O  
ATOM   3488  N   LEU B 103      73.798  25.054-163.840  1.00 38.87           N  
ANISOU 3488  N   LEU B 103     5728   3802   5241     -8    852    458       N  
ATOM   3489  CA  LEU B 103      74.985  24.955-162.999  1.00 34.35           C  
ANISOU 3489  CA  LEU B 103     5224   3151   4677   -179    777    344       C  
ATOM   3490  C   LEU B 103      75.067  23.567-162.359  1.00 33.57           C  
ANISOU 3490  C   LEU B 103     5013   3176   4567   -236    653    288       C  
ATOM   3491  O   LEU B 103      74.063  23.011-161.902  1.00 36.15           O  
ANISOU 3491  O   LEU B 103     5303   3574   4860   -150    659    310       O  
ATOM   3492  CB  LEU B 103      74.973  26.060-161.930  1.00 44.21           C  
ANISOU 3492  CB  LEU B 103     6701   4209   5888   -191    863    293       C  
ATOM   3493  CG  LEU B 103      75.681  27.369-162.322  1.00 49.52           C  
ANISOU 3493  CG  LEU B 103     7521   4709   6584   -251    941    292       C  
ATOM   3494  CD1 LEU B 103      75.294  27.845-163.721  1.00 45.34           C  
ANISOU 3494  CD1 LEU B 103     6937   4204   6087   -137   1023    410       C  
ATOM   3495  CD2 LEU B 103      75.406  28.461-161.310  1.00 58.65           C  
ANISOU 3495  CD2 LEU B 103     8927   5667   7689   -233   1046    248       C  
ATOM   3496  N   VAL B 104      76.270  22.984-162.364  1.00 30.15           N  
ANISOU 3496  N   VAL B 104     4518   2774   4163   -376    544    226       N  
ATOM   3497  CA  VAL B 104      76.446  21.648-161.800  1.00 33.01           C  
ANISOU 3497  CA  VAL B 104     4781   3245   4516   -424    429    180       C  
ATOM   3498  C   VAL B 104      76.211  21.681-160.290  1.00 38.28           C  
ANISOU 3498  C   VAL B 104     5566   3849   5128   -443    426    117       C  
ATOM   3499  O   VAL B 104      75.489  20.846-159.737  1.00 38.16           O  
ANISOU 3499  O   VAL B 104     5509   3907   5081   -394    403    121       O  
ATOM   3500  CB  VAL B 104      77.844  21.103-162.160  1.00 36.54           C  
ANISOU 3500  CB  VAL B 104     5139   3738   5006   -551    327    140       C  
ATOM   3501  CG1 VAL B 104      78.151  19.808-161.410  1.00 34.59           C  
ANISOU 3501  CG1 VAL B 104     4820   3578   4744   -599    214     90       C  
ATOM   3502  CG2 VAL B 104      77.952  20.851-163.679  1.00 33.68           C  
ANISOU 3502  CG2 VAL B 104     4651   3460   4684   -511    333    206       C  
ATOM   3503  N   PHE B 105      76.767  22.671-159.612  1.00 35.37           N  
ANISOU 3503  N   PHE B 105     5358   3341   4741   -517    455     60       N  
ATOM   3504  CA  PHE B 105      76.539  22.820-158.178  1.00 46.80           C  
ANISOU 3504  CA  PHE B 105     6946   4716   6118   -533    461     -4       C  
ATOM   3505  C   PHE B 105      75.619  24.005-157.915  1.00 46.20           C  
ANISOU 3505  C   PHE B 105     7045   4508   6002   -424    612     21       C  
ATOM   3506  O   PHE B 105      76.066  25.159-157.963  1.00 44.08           O  
ANISOU 3506  O   PHE B 105     6922   4092   5733   -471    671     -3       O  
ATOM   3507  CB  PHE B 105      77.872  22.989-157.454  1.00 43.15           C  
ANISOU 3507  CB  PHE B 105     6552   4198   5644   -709    369   -100       C  
ATOM   3508  CG  PHE B 105      78.729  21.771-157.528  1.00 49.55           C  
ANISOU 3508  CG  PHE B 105     7196   5146   6485   -791    227   -118       C  
ATOM   3509  CD1 PHE B 105      78.271  20.563-157.027  1.00 52.18           C  
ANISOU 3509  CD1 PHE B 105     7450   5584   6790   -743    171   -114       C  
ATOM   3510  CD2 PHE B 105      79.972  21.814-158.120  1.00 52.80           C  
ANISOU 3510  CD2 PHE B 105     7529   5581   6952   -908    161   -128       C  
ATOM   3511  CE1 PHE B 105      79.048  19.429-157.099  1.00 54.41           C  
ANISOU 3511  CE1 PHE B 105     7596   5981   7098   -801     52   -124       C  
ATOM   3512  CE2 PHE B 105      80.750  20.688-158.197  1.00 51.19           C  
ANISOU 3512  CE2 PHE B 105     7172   5505   6773   -959     44   -135       C  
ATOM   3513  CZ  PHE B 105      80.296  19.497-157.680  1.00 57.48           C  
ANISOU 3513  CZ  PHE B 105     7909   6393   7540   -902    -10   -135       C  
ATOM   3514  N   PRO B 106      74.322  23.778-157.663  1.00 53.17           N  
ANISOU 3514  N   PRO B 106     7917   5435   6848   -274    684     76       N  
ATOM   3515  CA  PRO B 106      73.297  24.811-157.476  1.00 60.20           C  
ANISOU 3515  CA  PRO B 106     8950   6222   7700   -128    844    123       C  
ATOM   3516  C   PRO B 106      73.290  25.409-156.063  1.00 65.01           C  
ANISOU 3516  C   PRO B 106     9787   6689   8225   -147    893     41       C  
ATOM   3517  O   PRO B 106      73.778  24.764-155.130  1.00 63.18           O  
ANISOU 3517  O   PRO B 106     9567   6485   7954   -247    796    -38       O  
ATOM   3518  CB  PRO B 106      71.986  24.059-157.754  1.00 63.79           C  
ANISOU 3518  CB  PRO B 106     9252   6831   8154     24    876    222       C  
ATOM   3519  CG  PRO B 106      72.309  22.573-157.602  1.00 59.96           C  
ANISOU 3519  CG  PRO B 106     8604   6495   7684    -66    730    192       C  
ATOM   3520  CD  PRO B 106      73.796  22.418-157.429  1.00 59.35           C  
ANISOU 3520  CD  PRO B 106     8550   6376   7624   -242    614     97       C  
ATOM   3521  N   ALA B 119      71.043  25.073-133.595  1.00 93.39           N  
ANISOU 3521  N   ALA B 119    16282   9703   9501    -43   1148   -956       N  
ATOM   3522  CA  ALA B 119      69.783  25.455-134.223  1.00 91.01           C  
ANISOU 3522  CA  ALA B 119    15961   9352   9267    176   1383   -857       C  
ATOM   3523  C   ALA B 119      68.684  24.410-133.992  1.00 92.36           C  
ANISOU 3523  C   ALA B 119    16024   9654   9416    357   1505   -749       C  
ATOM   3524  O   ALA B 119      68.259  23.738-134.936  1.00 90.20           O  
ANISOU 3524  O   ALA B 119    15544   9475   9252    421   1542   -670       O  
ATOM   3525  CB  ALA B 119      69.994  25.676-135.714  1.00 83.38           C  
ANISOU 3525  CB  ALA B 119    14843   8364   8472    144   1371   -836       C  
ATOM   3526  N   PRO B 120      68.216  24.281-132.744  1.00 93.16           N  
ANISOU 3526  N   PRO B 120    16250   9768   9378    436   1569   -735       N  
ATOM   3527  CA  PRO B 120      67.229  23.226-132.446  1.00 92.11           C  
ANISOU 3527  CA  PRO B 120    15996   9780   9223    588   1676   -620       C  
ATOM   3528  C   PRO B 120      65.849  23.485-133.031  1.00 96.53           C  
ANISOU 3528  C   PRO B 120    16457  10352   9867    820   1915   -481       C  
ATOM   3529  O   PRO B 120      65.143  22.521-133.351  1.00101.37           O  
ANISOU 3529  O   PRO B 120    16866  11119  10530    909   1981   -366       O  
ATOM   3530  CB  PRO B 120      67.189  23.202-130.910  1.00 88.71           C  
ANISOU 3530  CB  PRO B 120    15745   9338   8622    600   1677   -649       C  
ATOM   3531  CG  PRO B 120      68.424  23.934-130.468  1.00 89.15           C  
ANISOU 3531  CG  PRO B 120    15977   9286   8609    404   1506   -795       C  
ATOM   3532  CD  PRO B 120      68.674  24.960-131.521  1.00 91.81           C  
ANISOU 3532  CD  PRO B 120    16321   9502   9060    365   1524   -825       C  
ATOM   3533  N   GLU B 121      65.439  24.748-133.178  1.00 89.60           N  
ANISOU 3533  N   GLU B 121    15706   9330   9009    916   2045   -474       N  
ATOM   3534  CA  GLU B 121      64.095  25.039-133.673  1.00 88.19           C  
ANISOU 3534  CA  GLU B 121    15423   9177   8911   1151   2267   -325       C  
ATOM   3535  C   GLU B 121      63.902  24.550-135.102  1.00 81.26           C  
ANISOU 3535  C   GLU B 121    14277   8405   8192   1171   2270   -248       C  
ATOM   3536  O   GLU B 121      62.803  24.117-135.469  1.00 81.66           O  
ANISOU 3536  O   GLU B 121    14129   8585   8313   1333   2405    -97       O  
ATOM   3537  CB  GLU B 121      63.813  26.543-133.600  1.00 98.35           C  
ANISOU 3537  CB  GLU B 121    16913  10276  10179   1241   2390   -332       C  
ATOM   3538  CG  GLU B 121      64.415  27.249-132.392  1.00108.33           C  
ANISOU 3538  CG  GLU B 121    18478  11397  11285   1149   2340   -452       C  
ATOM   3539  CD  GLU B 121      65.845  27.711-132.631  1.00112.63           C  
ANISOU 3539  CD  GLU B 121    19124  11845  11826    900   2143   -602       C  
ATOM   3540  OE1 GLU B 121      66.092  28.406-133.640  1.00111.02           O  
ANISOU 3540  OE1 GLU B 121    18896  11564  11722    869   2146   -606       O  
ATOM   3541  OE2 GLU B 121      66.724  27.370-131.813  1.00114.80           O  
ANISOU 3541  OE2 GLU B 121    19485  12133  12000    734   1981   -707       O  
ATOM   3542  N   GLN B 122      64.950  24.613-135.916  1.00 73.48           N  
ANISOU 3542  N   GLN B 122    13272   7375   7272   1002   2118   -343       N  
ATOM   3543  CA  GLN B 122      64.858  24.239-137.318  1.00 79.45           C  
ANISOU 3543  CA  GLN B 122    13718   8237   8233    985   2061   -247       C  
ATOM   3544  C   GLN B 122      65.158  22.765-137.531  1.00 72.04           C  
ANISOU 3544  C   GLN B 122    12491   7498   7383    857   1878   -195       C  
ATOM   3545  O   GLN B 122      64.609  22.162-138.456  1.00 76.08           O  
ANISOU 3545  O   GLN B 122    12714   8149   8044    895   1877    -69       O  
ATOM   3546  CB  GLN B 122      65.796  25.108-138.169  1.00 86.80           C  
ANISOU 3546  CB  GLN B 122    14719   9028   9235    861   1972   -341       C  
ATOM   3547  CG  GLN B 122      66.825  25.932-137.381  1.00 98.53           C  
ANISOU 3547  CG  GLN B 122    16531  10324  10581    719   1900   -519       C  
ATOM   3548  CD  GLN B 122      66.211  27.050-136.533  1.00107.52           C  
ANISOU 3548  CD  GLN B 122    17895  11337  11622    842   2054   -500       C  
ATOM   3549  OE1 GLN B 122      65.062  27.449-136.737  1.00113.60           O  
ANISOU 3549  OE1 GLN B 122    18636  12106  12421   1059   2250   -379       O  
ATOM   3550  NE2 GLN B 122      66.972  27.533-135.557  1.00107.39           N  
ANISOU 3550  NE2 GLN B 122    18094  11224  11484    705   1961   -613       N  
ATOM   3551  N   LEU B 123      66.007  22.175-136.689  1.00 67.16           N  
ANISOU 3551  N   LEU B 123    11953   6894   6669    709   1726   -287       N  
ATOM   3552  CA  LEU B 123      66.066  20.721-136.606  1.00 62.29           C  
ANISOU 3552  CA  LEU B 123    11107   6458   6101    637   1603   -219       C  
ATOM   3553  C   LEU B 123      64.697  20.151-136.260  1.00 59.40           C  
ANISOU 3553  C   LEU B 123    10633   6211   5727    810   1773    -71       C  
ATOM   3554  O   LEU B 123      64.238  19.187-136.879  1.00 58.77           O  
ANISOU 3554  O   LEU B 123    10272   6283   5774    808   1743     47       O  
ATOM   3555  CB  LEU B 123      67.109  20.292-135.568  1.00 55.88           C  
ANISOU 3555  CB  LEU B 123    10441   5635   5155    487   1441   -332       C  
ATOM   3556  CG  LEU B 123      67.227  18.796-135.249  1.00 53.36           C  
ANISOU 3556  CG  LEU B 123     9942   5482   4853    425   1323   -268       C  
ATOM   3557  CD1 LEU B 123      67.358  17.980-136.526  1.00 54.33           C  
ANISOU 3557  CD1 LEU B 123     9746   5717   5181    358   1216   -188       C  
ATOM   3558  CD2 LEU B 123      68.422  18.542-134.364  1.00 55.94           C  
ANISOU 3558  CD2 LEU B 123    10414   5791   5051    273   1144   -385       C  
ATOM   3559  N   LEU B 124      64.026  20.742-135.268  1.00 54.17           N  
ANISOU 3559  N   LEU B 124    10193   5479   4911    959   1958    -74       N  
ATOM   3560  CA  LEU B 124      62.700  20.263-134.887  1.00 61.90           C  
ANISOU 3560  CA  LEU B 124    11069   6576   5876   1131   2139     77       C  
ATOM   3561  C   LEU B 124      61.708  20.410-136.031  1.00 58.05           C  
ANISOU 3561  C   LEU B 124    10335   6170   5549   1255   2252    221       C  
ATOM   3562  O   LEU B 124      60.895  19.509-136.280  1.00 48.56           O  
ANISOU 3562  O   LEU B 124     8879   5139   4431   1293   2285    364       O  
ATOM   3563  CB  LEU B 124      62.202  21.018-133.660  1.00 66.79           C  
ANISOU 3563  CB  LEU B 124    11994   7090   6292   1285   2334     42       C  
ATOM   3564  CG  LEU B 124      62.795  20.575-132.331  1.00 73.29           C  
ANISOU 3564  CG  LEU B 124    12999   7897   6950   1195   2241    -45       C  
ATOM   3565  CD1 LEU B 124      62.318  21.498-131.220  1.00 76.89           C  
ANISOU 3565  CD1 LEU B 124    13680   8231   7302   1315   2360    -66       C  
ATOM   3566  CD2 LEU B 124      62.396  19.139-132.059  1.00 78.83           C  
ANISOU 3566  CD2 LEU B 124    13496   8786   7667   1180   2219     72       C  
ATOM   3567  N   SER B 125      61.760  21.543-136.737  1.00 59.51           N  
ANISOU 3567  N   SER B 125    10596   6238   5777   1313   2311    189       N  
ATOM   3568  CA  SER B 125      60.839  21.776-137.842  1.00 60.24           C  
ANISOU 3568  CA  SER B 125    10466   6410   6011   1442   2417    329       C  
ATOM   3569  C   SER B 125      61.043  20.757-138.957  1.00 54.41           C  
ANISOU 3569  C   SER B 125     9394   5828   5450   1304   2241    392       C  
ATOM   3570  O   SER B 125      60.070  20.238-139.519  1.00 56.89           O  
ANISOU 3570  O   SER B 125     9448   6304   5862   1378   2300    544       O  
ATOM   3571  CB  SER B 125      61.009  23.203-138.368  1.00 64.86           C  
ANISOU 3571  CB  SER B 125    11226   6818   6598   1521   2501    274       C  
ATOM   3572  OG  SER B 125      60.486  23.326-139.674  1.00 71.09           O  
ANISOU 3572  OG  SER B 125    11773   7692   7546   1586   2525    390       O  
ATOM   3573  N   GLN B 126      62.299  20.449-139.288  1.00 52.44           N  
ANISOU 3573  N   GLN B 126     9148   5537   5241   1099   2024    279       N  
ATOM   3574  CA  GLN B 126      62.565  19.423-140.292  1.00 56.47           C  
ANISOU 3574  CA  GLN B 126     9368   6183   5904    968   1857    327       C  
ATOM   3575  C   GLN B 126      62.140  18.048-139.789  1.00 53.33           C  
ANISOU 3575  C   GLN B 126     8817   5939   5506    929   1824    407       C  
ATOM   3576  O   GLN B 126      61.527  17.269-140.526  1.00 44.35           O  
ANISOU 3576  O   GLN B 126     7417   4950   4486    921   1806    521       O  
ATOM   3577  CB  GLN B 126      64.047  19.419-140.671  1.00 56.11           C  
ANISOU 3577  CB  GLN B 126     9373   6057   5889    772   1647    191       C  
ATOM   3578  CG  GLN B 126      64.552  20.717-141.267  1.00 59.66           C  
ANISOU 3578  CG  GLN B 126     9959   6353   6355    777   1666    115       C  
ATOM   3579  CD  GLN B 126      66.068  20.775-141.331  1.00 65.74           C  
ANISOU 3579  CD  GLN B 126    10817   7038   7123    576   1471    -28       C  
ATOM   3580  OE1 GLN B 126      66.670  20.420-142.341  1.00 68.47           O  
ANISOU 3580  OE1 GLN B 126    10994   7432   7591    468   1337    -28       O  
ATOM   3581  NE2 GLN B 126      66.691  21.221-140.243  1.00 70.71           N  
ANISOU 3581  NE2 GLN B 126    11710   7549   7606    523   1453   -149       N  
ATOM   3582  N   ALA B 127      62.462  17.726-138.533  1.00 47.46           N  
ANISOU 3582  N   ALA B 127     8244   5161   4626    899   1812    348       N  
ATOM   3583  CA  ALA B 127      62.108  16.409-138.009  1.00 48.14           C  
ANISOU 3583  CA  ALA B 127     8205   5380   4706    859   1784    426       C  
ATOM   3584  C   ALA B 127      60.597  16.213-138.007  1.00 48.61           C  
ANISOU 3584  C   ALA B 127     8112   5565   4794   1010   1973    594       C  
ATOM   3585  O   ALA B 127      60.095  15.147-138.387  1.00 43.70           O  
ANISOU 3585  O   ALA B 127     7252   5087   4266    960   1938    700       O  
ATOM   3586  CB  ALA B 127      62.684  16.227-136.603  1.00 47.58           C  
ANISOU 3586  CB  ALA B 127     8370   5247   4463    822   1755    339       C  
ATOM   3587  N   ARG B 128      59.860  17.248-137.605  1.00 47.63           N  
ANISOU 3587  N   ARG B 128     8119   5387   4590   1195   2176    622       N  
ATOM   3588  CA  ARG B 128      58.403  17.186-137.574  1.00 52.99           C  
ANISOU 3588  CA  ARG B 128     8648   6195   5291   1362   2375    793       C  
ATOM   3589  C   ARG B 128      57.850  16.899-138.964  1.00 52.30           C  
ANISOU 3589  C   ARG B 128     8246   6244   5384   1347   2339    906       C  
ATOM   3590  O   ARG B 128      56.949  16.070-139.137  1.00 51.88           O  
ANISOU 3590  O   ARG B 128     7955   6361   5397   1351   2376   1047       O  
ATOM   3591  CB  ARG B 128      57.848  18.512-137.033  1.00 49.39           C  
ANISOU 3591  CB  ARG B 128     8411   5635   4721   1581   2600    792       C  
ATOM   3592  CG  ARG B 128      56.719  18.400-136.051  1.00 75.70           C  
ANISOU 3592  CG  ARG B 128    11743   9040   7980   1737   2785    903       C  
ATOM   3593  CD  ARG B 128      57.207  18.682-134.635  1.00 87.39           C  
ANISOU 3593  CD  ARG B 128    13538  10380   9287   1742   2795    782       C  
ATOM   3594  NE  ARG B 128      57.367  20.108-134.357  1.00 98.57           N  
ANISOU 3594  NE  ARG B 128    15215  11602  10635   1851   2867    688       N  
ATOM   3595  CZ  ARG B 128      58.230  20.601-133.472  1.00106.82           C  
ANISOU 3595  CZ  ARG B 128    16574  12478  11535   1797   2819    531       C  
ATOM   3596  NH1 ARG B 128      59.025  19.782-132.798  1.00109.02           N  
ANISOU 3596  NH1 ARG B 128    16934  12771  11716   1648   2694    450       N  
ATOM   3597  NH2 ARG B 128      58.310  21.910-133.268  1.00108.20           N  
ANISOU 3597  NH2 ARG B 128    16980  12470  11659   1883   2886    460       N  
ATOM   3598  N   ASP B 129      58.383  17.582-139.971  1.00 45.81           N  
ANISOU 3598  N   ASP B 129     7420   5349   4636   1323   2265    847       N  
ATOM   3599  CA  ASP B 129      57.909  17.350-141.331  1.00 50.87           C  
ANISOU 3599  CA  ASP B 129     7775   6119   5434   1308   2221    947       C  
ATOM   3600  C   ASP B 129      58.207  15.930-141.784  1.00 43.36           C  
ANISOU 3600  C   ASP B 129     6616   5282   4577   1111   2037    962       C  
ATOM   3601  O   ASP B 129      57.370  15.289-142.427  1.00 49.05           O  
ANISOU 3601  O   ASP B 129     7077   6168   5392   1101   2041   1090       O  
ATOM   3602  CB  ASP B 129      58.535  18.341-142.304  1.00 52.71           C  
ANISOU 3602  CB  ASP B 129     8066   6241   5720   1311   2172    875       C  
ATOM   3603  CG  ASP B 129      58.257  17.964-143.744  1.00 64.32           C  
ANISOU 3603  CG  ASP B 129     9252   7846   7343   1261   2085    959       C  
ATOM   3604  OD1 ASP B 129      57.076  18.041-144.148  1.00 65.76           O  
ANISOU 3604  OD1 ASP B 129     9249   8168   7570   1388   2201   1111       O  
ATOM   3605  OD2 ASP B 129      59.201  17.546-144.451  1.00 65.21           O  
ANISOU 3605  OD2 ASP B 129     9318   7936   7525   1096   1899    879       O  
ATOM   3606  N   PHE B 130      59.394  15.412-141.461  1.00 45.49           N  
ANISOU 3606  N   PHE B 130     6998   5468   4819    952   1873    835       N  
ATOM   3607  CA  PHE B 130      59.705  14.046-141.864  1.00 45.23           C  
ANISOU 3607  CA  PHE B 130     6792   5525   4869    779   1709    848       C  
ATOM   3608  C   PHE B 130      58.813  13.036-141.149  1.00 43.30           C  
ANISOU 3608  C   PHE B 130     6448   5402   4602    781   1780    962       C  
ATOM   3609  O   PHE B 130      58.342  12.074-141.766  1.00 44.14           O  
ANISOU 3609  O   PHE B 130     6329   5635   4806    695   1726   1049       O  
ATOM   3610  CB  PHE B 130      61.172  13.723-141.608  1.00 37.58           C  
ANISOU 3610  CB  PHE B 130     5964   4446   3867    632   1531    700       C  
ATOM   3611  CG  PHE B 130      61.492  12.266-141.794  1.00 37.82           C  
ANISOU 3611  CG  PHE B 130     5859   4551   3959    478   1386    717       C  
ATOM   3612  CD1 PHE B 130      61.512  11.707-143.067  1.00 38.07           C  
ANISOU 3612  CD1 PHE B 130     5685   4655   4125    390   1283    748       C  
ATOM   3613  CD2 PHE B 130      61.717  11.441-140.692  1.00 41.80           C  
ANISOU 3613  CD2 PHE B 130     6451   5051   4379    432   1364    709       C  
ATOM   3614  CE1 PHE B 130      61.778  10.355-143.246  1.00 40.47           C  
ANISOU 3614  CE1 PHE B 130     5886   5011   4481    254   1163    762       C  
ATOM   3615  CE2 PHE B 130      61.984  10.092-140.861  1.00 40.54           C  
ANISOU 3615  CE2 PHE B 130     6182   4946   4276    302   1245    732       C  
ATOM   3616  CZ  PHE B 130      62.013   9.542-142.133  1.00 42.04           C  
ANISOU 3616  CZ  PHE B 130     6178   5194   4602    212   1147    756       C  
ATOM   3617  N   ILE B 131      58.591  13.220-139.843  1.00 40.49           N  
ANISOU 3617  N   ILE B 131     6266   5005   4112    867   1900    962       N  
ATOM   3618  CA  ILE B 131      57.708  12.316-139.112  1.00 44.22           C  
ANISOU 3618  CA  ILE B 131     6651   5592   4558    877   1989   1082       C  
ATOM   3619  C   ILE B 131      56.307  12.347-139.709  1.00 44.50           C  
ANISOU 3619  C   ILE B 131     6439   5791   4679    967   2120   1251       C  
ATOM   3620  O   ILE B 131      55.644  11.309-139.822  1.00 42.10           O  
ANISOU 3620  O   ILE B 131     5937   5622   4437    890   2114   1362       O  
ATOM   3621  CB  ILE B 131      57.687  12.673-137.609  1.00 54.03           C  
ANISOU 3621  CB  ILE B 131     8144   6759   5625    980   2116   1052       C  
ATOM   3622  CG1 ILE B 131      59.076  12.509-136.986  1.00 50.09           C  
ANISOU 3622  CG1 ILE B 131     7867   6128   5035    871   1963    894       C  
ATOM   3623  CG2 ILE B 131      56.649  11.826-136.859  1.00 48.90           C  
ANISOU 3623  CG2 ILE B 131     7396   6237   4946   1012   2241   1198       C  
ATOM   3624  CD1 ILE B 131      59.693  11.154-137.212  1.00 55.36           C  
ANISOU 3624  CD1 ILE B 131     8428   6837   5771    689   1780    888       C  
ATOM   3625  N   ASN B 132      55.833  13.534-140.100  1.00 46.71           N  
ANISOU 3625  N   ASN B 132     6726   6062   4961   1129   2241   1279       N  
ATOM   3626  CA  ASN B 132      54.537  13.620-140.767  1.00 47.91           C  
ANISOU 3626  CA  ASN B 132     6619   6387   5197   1222   2353   1449       C  
ATOM   3627  C   ASN B 132      54.552  12.836-142.077  1.00 45.42           C  
ANISOU 3627  C   ASN B 132     6046   6182   5030   1060   2185   1482       C  
ATOM   3628  O   ASN B 132      53.602  12.106-142.385  1.00 47.08           O  
ANISOU 3628  O   ASN B 132     6011   6568   5310   1019   2206   1620       O  
ATOM   3629  CB  ASN B 132      54.160  15.086-141.007  1.00 50.16           C  
ANISOU 3629  CB  ASN B 132     6980   6625   5454   1438   2504   1467       C  
ATOM   3630  CG  ASN B 132      53.939  15.853-139.710  1.00 55.43           C  
ANISOU 3630  CG  ASN B 132     7898   7191   5974   1613   2688   1446       C  
ATOM   3631  OD1 ASN B 132      53.697  15.266-138.656  1.00 55.39           O  
ANISOU 3631  OD1 ASN B 132     7938   7203   5904   1597   2720   1461       O  
ATOM   3632  ND2 ASN B 132      54.002  17.175-139.793  1.00 53.39           N  
ANISOU 3632  ND2 ASN B 132     7799   6806   5682   1766   2768   1396       N  
ATOM   3633  N   GLN B 133      55.643  12.944-142.837  1.00 44.66           N  
ANISOU 3633  N   GLN B 133     6006   5984   4979    956   2016   1354       N  
ATOM   3634  CA  GLN B 133      55.785  12.152-144.058  1.00 47.49           C  
ANISOU 3634  CA  GLN B 133     6154   6427   5462    795   1849   1366       C  
ATOM   3635  C   GLN B 133      55.707  10.663-143.755  1.00 48.77           C  
ANISOU 3635  C   GLN B 133     6223   6657   5649    627   1767   1397       C  
ATOM   3636  O   GLN B 133      55.027   9.902-144.456  1.00 44.49           O  
ANISOU 3636  O   GLN B 133     5449   6259   5195    536   1725   1493       O  
ATOM   3637  CB  GLN B 133      57.114  12.461-144.737  1.00 42.68           C  
ANISOU 3637  CB  GLN B 133     5657   5680   4878    713   1689   1214       C  
ATOM   3638  CG  GLN B 133      57.195  13.798-145.449  1.00 41.54           C  
ANISOU 3638  CG  GLN B 133     5554   5481   4747    837   1738   1194       C  
ATOM   3639  CD  GLN B 133      58.419  13.866-146.326  1.00 44.71           C  
ANISOU 3639  CD  GLN B 133     6001   5787   5200    721   1566   1070       C  
ATOM   3640  OE1 GLN B 133      58.616  13.019-147.205  1.00 43.97           O  
ANISOU 3640  OE1 GLN B 133     5753   5764   5190    585   1427   1072       O  
ATOM   3641  NE2 GLN B 133      59.269  14.855-146.080  1.00 46.24           N  
ANISOU 3641  NE2 GLN B 133     6414   5817   5339    766   1575    958       N  
ATOM   3642  N   TYR B 134      56.422  10.224-142.721  1.00 44.53           N  
ANISOU 3642  N   TYR B 134     5875   6014   5031    576   1738   1317       N  
ATOM   3643  CA  TYR B 134      56.465   8.799-142.413  1.00 43.46           C  
ANISOU 3643  CA  TYR B 134     5681   5915   4915    419   1659   1342       C  
ATOM   3644  C   TYR B 134      55.095   8.285-141.993  1.00 45.95           C  
ANISOU 3644  C   TYR B 134     5834   6386   5237    443   1797   1511       C  
ATOM   3645  O   TYR B 134      54.631   7.251-142.485  1.00 44.94           O  
ANISOU 3645  O   TYR B 134     5521   6361   5192    304   1737   1585       O  
ATOM   3646  CB  TYR B 134      57.504   8.519-141.331  1.00 46.01           C  
ANISOU 3646  CB  TYR B 134     6247   6100   5136    386   1609   1233       C  
ATOM   3647  CG  TYR B 134      57.512   7.071-140.899  1.00 43.74           C  
ANISOU 3647  CG  TYR B 134     5924   5839   4857    248   1551   1273       C  
ATOM   3648  CD1 TYR B 134      58.064   6.092-141.709  1.00 49.02           C  
ANISOU 3648  CD1 TYR B 134     6510   6500   5615     83   1384   1238       C  
ATOM   3649  CD2 TYR B 134      56.938   6.684-139.698  1.00 42.67           C  
ANISOU 3649  CD2 TYR B 134     5844   5732   4637    288   1674   1352       C  
ATOM   3650  CE1 TYR B 134      58.066   4.773-141.324  1.00 50.77           C  
ANISOU 3650  CE1 TYR B 134     6719   6728   5844    -38   1341   1277       C  
ATOM   3651  CE2 TYR B 134      56.930   5.362-139.308  1.00 50.70           C  
ANISOU 3651  CE2 TYR B 134     6838   6764   5662    163   1630   1397       C  
ATOM   3652  CZ  TYR B 134      57.500   4.414-140.130  1.00 52.58           C  
ANISOU 3652  CZ  TYR B 134     7004   6981   5993     -1   1462   1358       C  
ATOM   3653  OH  TYR B 134      57.499   3.090-139.757  1.00 55.48           O  
ANISOU 3653  OH  TYR B 134     7367   7344   6369   -123   1425   1404       O  
ATOM   3654  N   TYR B 135      54.427   8.992-141.084  1.00 43.36           N  
ANISOU 3654  N   TYR B 135     5576   6077   4821    614   1988   1575       N  
ATOM   3655  CA  TYR B 135      53.119   8.515-140.653  1.00 44.53           C  
ANISOU 3655  CA  TYR B 135     5557   6387   4976    642   2132   1748       C  
ATOM   3656  C   TYR B 135      52.053   8.659-141.738  1.00 51.84           C  
ANISOU 3656  C   TYR B 135     6188   7497   6012    656   2160   1880       C  
ATOM   3657  O   TYR B 135      51.079   7.903-141.720  1.00 51.84           O  
ANISOU 3657  O   TYR B 135     5991   7641   6067    584   2179   1997       O  
ATOM   3658  CB  TYR B 135      52.719   9.204-139.343  1.00 48.41           C  
ANISOU 3658  CB  TYR B 135     6213   6849   5332    833   2339   1783       C  
ATOM   3659  CG  TYR B 135      53.413   8.530-138.179  1.00 50.86           C  
ANISOU 3659  CG  TYR B 135     6733   7051   5539    767   2310   1714       C  
ATOM   3660  CD1 TYR B 135      52.845   7.416-137.566  1.00 52.99           C  
ANISOU 3660  CD1 TYR B 135     6923   7404   5806    683   2353   1821       C  
ATOM   3661  CD2 TYR B 135      54.662   8.953-137.742  1.00 44.15           C  
ANISOU 3661  CD2 TYR B 135     6153   6023   4600    773   2225   1546       C  
ATOM   3662  CE1 TYR B 135      53.482   6.765-136.529  1.00 53.49           C  
ANISOU 3662  CE1 TYR B 135     7177   7372   5773    629   2325   1770       C  
ATOM   3663  CE2 TYR B 135      55.309   8.300-136.678  1.00 43.57           C  
ANISOU 3663  CE2 TYR B 135     6263   5868   4425    714   2186   1491       C  
ATOM   3664  CZ  TYR B 135      54.714   7.206-136.094  1.00 47.87           C  
ANISOU 3664  CZ  TYR B 135     6729   6496   4966    649   2237   1605       C  
ATOM   3665  OH  TYR B 135      55.333   6.542-135.049  1.00 48.46           O  
ANISOU 3665  OH  TYR B 135     6985   6494   4935    601   2202   1565       O  
ATOM   3666  N   SER B 136      52.224   9.577-142.697  1.00 51.12           N  
ANISOU 3666  N   SER B 136     6066   7395   5961    730   2126   1843       N  
ATOM   3667  CA  SER B 136      51.379   9.547-143.890  1.00 55.76           C  
ANISOU 3667  CA  SER B 136     6367   8164   6657    706   2101   1956       C  
ATOM   3668  C   SER B 136      51.583   8.257-144.674  1.00 52.14           C  
ANISOU 3668  C   SER B 136     5765   7754   6290    453   1910   1940       C  
ATOM   3669  O   SER B 136      50.612   7.622-145.105  1.00 56.58           O  
ANISOU 3669  O   SER B 136     6088   8486   6923    364   1893   2055       O  
ATOM   3670  CB  SER B 136      51.672  10.753-144.796  1.00 55.63           C  
ANISOU 3670  CB  SER B 136     6372   8105   6659    829   2086   1908       C  
ATOM   3671  OG  SER B 136      50.948  11.894-144.376  1.00 64.60           O  
ANISOU 3671  OG  SER B 136     7543   9252   7751   1065   2252   1966       O  
ATOM   3672  N   SER B 137      52.842   7.855-144.856  1.00 46.27           N  
ANISOU 3672  N   SER B 137     5181   6851   5549    332   1749   1783       N  
ATOM   3673  CA  SER B 137      53.155   6.693-145.682  1.00 52.89           C  
ANISOU 3673  CA  SER B 137     5920   7708   6469    108   1569   1750       C  
ATOM   3674  C   SER B 137      52.571   5.401-145.117  1.00 52.55           C  
ANISOU 3674  C   SER B 137     5796   7733   6439    -37   1582   1837       C  
ATOM   3675  O   SER B 137      52.258   4.482-145.883  1.00 57.21           O  
ANISOU 3675  O   SER B 137     6226   8404   7106   -214   1480   1872       O  
ATOM   3676  CB  SER B 137      54.670   6.554-145.829  1.00 47.72           C  
ANISOU 3676  CB  SER B 137     5470   6862   5801     38   1419   1572       C  
ATOM   3677  OG  SER B 137      55.261   6.148-144.599  1.00 47.48           O  
ANISOU 3677  OG  SER B 137     5638   6712   5691     30   1440   1518       O  
ATOM   3678  N   ILE B 138      52.435   5.296-143.794  1.00 55.80           N  
ANISOU 3678  N   ILE B 138     6326   8105   6770     27   1706   1869       N  
ATOM   3679  CA  ILE B 138      51.873   4.099-143.176  1.00 53.52           C  
ANISOU 3679  CA  ILE B 138     5975   7873   6488   -104   1738   1962       C  
ATOM   3680  C   ILE B 138      50.418   4.302-142.764  1.00 62.16           C  
ANISOU 3680  C   ILE B 138     6898   9133   7587    -21   1884   2108       C  
ATOM   3681  O   ILE B 138      49.886   3.516-141.971  1.00 60.82           O  
ANISOU 3681  O   ILE B 138     6718   8985   7405    -86   1929   2163       O  
ATOM   3682  CB  ILE B 138      52.716   3.634-141.975  1.00 48.55           C  
ANISOU 3682  CB  ILE B 138     5599   7081   5767   -111   1742   1885       C  
ATOM   3683  CG1 ILE B 138      52.670   4.671-140.849  1.00 53.08           C  
ANISOU 3683  CG1 ILE B 138     6334   7614   6220    107   1909   1887       C  
ATOM   3684  CG2 ILE B 138      54.153   3.356-142.409  1.00 48.65           C  
ANISOU 3684  CG2 ILE B 138     5772   6927   5787   -196   1556   1715       C  
ATOM   3685  CD1 ILE B 138      53.191   4.157-139.487  1.00 53.84           C  
ANISOU 3685  CD1 ILE B 138     6652   7598   6207    108   1945   1855       C  
ATOM   3686  N   LYS B 139      49.770   5.354-143.272  1.00 61.82           N  
ANISOU 3686  N   LYS B 139     6739   9183   7564    129   1932   2144       N  
ATOM   3687  CA  LYS B 139      48.352   5.631-143.026  1.00 69.16           C  
ANISOU 3687  CA  LYS B 139     7501  10263   8514    225   2027   2258       C  
ATOM   3688  C   LYS B 139      48.042   5.737-141.534  1.00 70.81           C  
ANISOU 3688  C   LYS B 139     7842  10430   8632    343   2184   2288       C  
ATOM   3689  O   LYS B 139      47.065   5.170-141.034  1.00 75.18           O  
ANISOU 3689  O   LYS B 139     8282  11081   9203    305   2236   2381       O  
ATOM   3690  CB  LYS B 139      47.472   4.581-143.707  1.00 72.64           C  
ANISOU 3690  CB  LYS B 139     7699  10850   9052     26   1925   2330       C  
ATOM   3691  CG  LYS B 139      47.549   4.677-145.217  1.00 73.81           C  
ANISOU 3691  CG  LYS B 139     7702  11066   9277    -54   1778   2309       C  
ATOM   3692  CD  LYS B 139      47.446   3.329-145.897  1.00 78.44           C  
ANISOU 3692  CD  LYS B 139     8179  11689   9934   -327   1623   2299       C  
ATOM   3693  CE  LYS B 139      47.710   3.477-147.392  1.00 83.13           C  
ANISOU 3693  CE  LYS B 139     8674  12328  10584   -397   1470   2254       C  
ATOM   3694  NZ  LYS B 139      47.471   2.212-148.134  1.00 85.09           N  
ANISOU 3694  NZ  LYS B 139     8821  12616  10894   -657   1315   2238       N  
ATOM   3695  N   ARG B 140      48.883   6.494-140.821  1.00 65.93           N  
ANISOU 3695  N   ARG B 140     7475   9664   7912    487   2260   2206       N  
ATOM   3696  CA  ARG B 140      48.705   6.743-139.392  1.00 69.43           C  
ANISOU 3696  CA  ARG B 140     8084  10050   8248    620   2406   2214       C  
ATOM   3697  C   ARG B 140      48.762   8.232-139.060  1.00 74.80           C  
ANISOU 3697  C   ARG B 140     8909  10659   8850    874   2524   2175       C  
ATOM   3698  O   ARG B 140      49.060   8.589-137.915  1.00 67.99           O  
ANISOU 3698  O   ARG B 140     8271   9690   7872    983   2621   2128       O  
ATOM   3699  CB  ARG B 140      49.759   5.985-138.573  1.00 61.78           C  
ANISOU 3699  CB  ARG B 140     7340   8939   7196    519   2374   2136       C  
ATOM   3700  CG  ARG B 140      49.232   4.768-137.836  1.00 74.26           C  
ANISOU 3700  CG  ARG B 140     8872  10565   8779    392   2391   2210       C  
ATOM   3701  CD  ARG B 140      48.660   3.756-138.806  1.00 78.73           C  
ANISOU 3701  CD  ARG B 140     9187  11248   9479    182   2281   2276       C  
ATOM   3702  NE  ARG B 140      48.119   2.567-138.145  1.00 76.96           N  
ANISOU 3702  NE  ARG B 140     8921  11057   9264     45   2300   2347       N  
ATOM   3703  CZ  ARG B 140      47.240   1.755-138.719  1.00 69.81           C  
ANISOU 3703  CZ  ARG B 140     7793  10272   8461   -115   2248   2424       C  
ATOM   3704  NH1 ARG B 140      46.798   2.020-139.945  1.00 70.17           N  
ANISOU 3704  NH1 ARG B 140     7636  10425   8601   -150   2166   2441       N  
ATOM   3705  NH2 ARG B 140      46.803   0.690-138.075  1.00 70.29           N  
ANISOU 3705  NH2 ARG B 140     7840  10342   8523   -241   2275   2482       N  
ATOM   3706  N   SER B 141      48.497   9.102-140.041  1.00 65.89           N  
ANISOU 3706  N   SER B 141     7674   9581   7781    966   2512   2191       N  
ATOM   3707  CA ASER B 141      48.531  10.538-139.804  0.37 62.53           C  
ANISOU 3707  CA ASER B 141     7397   9071   7290   1206   2625   2157       C  
ATOM   3708  CA BSER B 141      48.526  10.541-139.807  0.63 62.67           C  
ANISOU 3708  CA BSER B 141     7414   9090   7308   1207   2625   2157       C  
ATOM   3709  C   SER B 141      47.558  10.920-138.697  1.00 62.99           C  
ANISOU 3709  C   SER B 141     7483   9159   7290   1377   2788   2235       C  
ATOM   3710  O   SER B 141      46.425  10.419-138.645  1.00 69.78           O  
ANISOU 3710  O   SER B 141     8127  10178   8208   1357   2817   2365       O  
ATOM   3711  CB ASER B 141      48.197  11.290-141.096  0.37 61.07           C  
ANISOU 3711  CB ASER B 141     7053   8961   7191   1275   2585   2195       C  
ATOM   3712  CB BSER B 141      48.174  11.296-141.095  0.63 61.01           C  
ANISOU 3712  CB BSER B 141     7042   8956   7184   1277   2587   2198       C  
ATOM   3713  OG ASER B 141      48.212  12.690-140.898  0.37 59.73           O  
ANISOU 3713  OG ASER B 141     7039   8692   6962   1508   2699   2169       O  
ATOM   3714  OG BSER B 141      49.055  10.947-142.142  0.63 59.03           O  
ANISOU 3714  OG BSER B 141     6761   8682   6986   1122   2439   2129       O  
ATOM   3715  N   GLY B 142      48.009  11.809-137.809  1.00 58.25           N  
ANISOU 3715  N   GLY B 142     7158   8403   6573   1540   2893   2154       N  
ATOM   3716  CA  GLY B 142      47.168  12.254-136.718  1.00 58.94           C  
ANISOU 3716  CA  GLY B 142     7307   8496   6593   1717   3055   2219       C  
ATOM   3717  C   GLY B 142      46.850  11.218-135.663  1.00 68.84           C  
ANISOU 3717  C   GLY B 142     8556   9794   7806   1631   3090   2262       C  
ATOM   3718  O   GLY B 142      46.055  11.507-134.762  1.00 67.96           O  
ANISOU 3718  O   GLY B 142     8470   9707   7643   1774   3230   2332       O  
ATOM   3719  N   SER B 143      47.441  10.025-135.730  1.00 66.40           N  
ANISOU 3719  N   SER B 143     8225   9490   7514   1407   2974   2229       N  
ATOM   3720  CA  SER B 143      47.118   8.998-134.747  1.00 70.03           C  
ANISOU 3720  CA  SER B 143     8683   9989   7938   1319   3008   2280       C  
ATOM   3721  C   SER B 143      47.901   9.205-133.452  1.00 72.65           C  
ANISOU 3721  C   SER B 143     9338  10157   8108   1388   3067   2177       C  
ATOM   3722  O   SER B 143      48.802  10.047-133.356  1.00 66.11           O  
ANISOU 3722  O   SER B 143     8742   9179   7196   1470   3059   2052       O  
ATOM   3723  CB  SER B 143      47.375   7.597-135.304  1.00 66.32           C  
ANISOU 3723  CB  SER B 143     8072   9578   7550   1054   2865   2298       C  
ATOM   3724  OG  SER B 143      48.735   7.416-135.681  1.00 64.46           O  
ANISOU 3724  OG  SER B 143     7989   9214   7290    948   2741   2173       O  
ATOM   3725  N   GLN B 144      47.521   8.418-132.436  1.00 76.38           N  
ANISOU 3725  N   GLN B 144     9827  10663   8533   1349   3124   2233       N  
ATOM   3726  CA  GLN B 144      48.241   8.422-131.167  1.00 66.12           C  
ANISOU 3726  CA  GLN B 144     8823   9227   7074   1390   3161   2144       C  
ATOM   3727  C   GLN B 144      49.722   8.145-131.367  1.00 59.75           C  
ANISOU 3727  C   GLN B 144     8200   8288   6215   1265   3015   2006       C  
ATOM   3728  O   GLN B 144      50.572   8.869-130.834  1.00 64.34           O  
ANISOU 3728  O   GLN B 144     9051   8724   6670   1349   3017   1881       O  
ATOM   3729  CB  GLN B 144      47.634   7.381-130.227  1.00 73.27           C  
ANISOU 3729  CB  GLN B 144     9679  10204   7955   1324   3219   2240       C  
ATOM   3730  CG  GLN B 144      46.209   7.661-129.826  1.00 82.00           C  
ANISOU 3730  CG  GLN B 144    10633  11435   9089   1459   3377   2378       C  
ATOM   3731  CD  GLN B 144      46.122   8.602-128.649  1.00 89.04           C  
ANISOU 3731  CD  GLN B 144    11759  12235   9835   1682   3524   2342       C  
ATOM   3732  OE1 GLN B 144      46.860   9.588-128.571  1.00 88.84           O  
ANISOU 3732  OE1 GLN B 144    11958  12070   9729   1792   3521   2219       O  
ATOM   3733  NE2 GLN B 144      45.230   8.295-127.712  1.00 89.98           N  
ANISOU 3733  NE2 GLN B 144    11843  12427   9920   1744   3653   2446       N  
ATOM   3734  N   ALA B 145      50.048   7.087-132.124  1.00 57.48           N  
ANISOU 3734  N   ALA B 145     7775   8044   6020   1059   2883   2027       N  
ATOM   3735  CA  ALA B 145      51.450   6.761-132.373  1.00 54.44           C  
ANISOU 3735  CA  ALA B 145     7551   7540   5595    943   2740   1912       C  
ATOM   3736  C   ALA B 145      52.178   7.923-133.035  1.00 58.90           C  
ANISOU 3736  C   ALA B 145     8224   8011   6143   1025   2704   1798       C  
ATOM   3737  O   ALA B 145      53.337   8.205-132.716  1.00 54.42           O  
ANISOU 3737  O   ALA B 145     7902   7307   5469   1022   2642   1671       O  
ATOM   3738  CB  ALA B 145      51.550   5.498-133.220  1.00 51.67           C  
ANISOU 3738  CB  ALA B 145     7016   7250   5367    721   2615   1967       C  
ATOM   3739  N   HIS B 146      51.503   8.619-133.950  1.00 56.77           N  
ANISOU 3739  N   HIS B 146     7779   7815   5975   1098   2740   1844       N  
ATOM   3740  CA  HIS B 146      52.087   9.778-134.623  1.00 52.40           C  
ANISOU 3740  CA  HIS B 146     7321   7174   5415   1185   2721   1749       C  
ATOM   3741  C   HIS B 146      52.415  10.890-133.632  1.00 54.26           C  
ANISOU 3741  C   HIS B 146     7850   7267   5498   1357   2815   1648       C  
ATOM   3742  O   HIS B 146      53.559  11.355-133.570  1.00 52.75           O  
ANISOU 3742  O   HIS B 146     7891   6933   5221   1343   2750   1510       O  
ATOM   3743  CB  HIS B 146      51.127  10.266-135.730  1.00 48.45           C  
ANISOU 3743  CB  HIS B 146     6558   6798   5053   1246   2751   1843       C  
ATOM   3744  CG  HIS B 146      51.666  11.363-136.581  1.00 55.29           C  
ANISOU 3744  CG  HIS B 146     7491   7585   5933   1322   2727   1764       C  
ATOM   3745  ND1 HIS B 146      50.899  11.995-137.524  1.00 54.77           N  
ANISOU 3745  ND1 HIS B 146     7232   7609   5969   1410   2756   1839       N  
ATOM   3746  CD2 HIS B 146      52.891  11.935-136.655  1.00 55.35           C  
ANISOU 3746  CD2 HIS B 146     7735   7432   5865   1318   2673   1621       C  
ATOM   3747  CE1 HIS B 146      51.625  12.912-138.142  1.00 57.69           C  
ANISOU 3747  CE1 HIS B 146     7720   7871   6328   1462   2730   1747       C  
ATOM   3748  NE2 HIS B 146      52.839  12.904-137.630  1.00 59.31           N  
ANISOU 3748  NE2 HIS B 146     8188   7921   6427   1403   2682   1611       N  
ATOM   3749  N   GLU B 147      51.431  11.336-132.845  1.00 62.60           N  
ANISOU 3749  N   GLU B 147     8910   8357   6519   1515   2965   1714       N  
ATOM   3750  CA  GLU B 147      51.733  12.390-131.881  1.00 68.47           C  
ANISOU 3750  CA  GLU B 147     9950   8951   7114   1673   3053   1615       C  
ATOM   3751  C   GLU B 147      52.726  11.908-130.827  1.00 67.47           C  
ANISOU 3751  C   GLU B 147    10078   8720   6837   1591   2991   1509       C  
ATOM   3752  O   GLU B 147      53.571  12.689-130.367  1.00 70.53           O  
ANISOU 3752  O   GLU B 147    10745   8953   7100   1636   2974   1368       O  
ATOM   3753  CB  GLU B 147      50.454  12.907-131.230  1.00 82.10           C  
ANISOU 3753  CB  GLU B 147    11630  10732   8831   1863   3230   1720       C  
ATOM   3754  CG  GLU B 147      50.658  14.130-130.326  1.00 99.35           C  
ANISOU 3754  CG  GLU B 147    14127  12751  10873   2042   3334   1624       C  
ATOM   3755  CD  GLU B 147      51.193  15.350-131.074  1.00104.42           C  
ANISOU 3755  CD  GLU B 147    14890  13262  11522   2112   3316   1528       C  
ATOM   3756  OE1 GLU B 147      50.752  15.600-132.218  1.00103.79           O  
ANISOU 3756  OE1 GLU B 147    14601  13261  11575   2135   3309   1600       O  
ATOM   3757  OE2 GLU B 147      52.055  16.063-130.516  1.00105.83           O  
ANISOU 3757  OE2 GLU B 147    15378  13262  11572   2138   3305   1380       O  
ATOM   3758  N   GLN B 148      52.656  10.630-130.452  1.00 68.58           N  
ANISOU 3758  N   GLN B 148    10129   8941   6985   1464   2947   1574       N  
ATOM   3759  CA  GLN B 148      53.646  10.063-129.539  1.00 71.80           C  
ANISOU 3759  CA  GLN B 148    10760   9264   7257   1379   2865   1487       C  
ATOM   3760  C   GLN B 148      55.055  10.237-130.093  1.00 61.65           C  
ANISOU 3760  C   GLN B 148     9621   7866   5936   1279   2707   1346       C  
ATOM   3761  O   GLN B 148      55.972  10.654-129.376  1.00 56.61           O  
ANISOU 3761  O   GLN B 148     9256   7104   5149   1289   2658   1215       O  
ATOM   3762  CB  GLN B 148      53.337   8.583-129.286  1.00 74.54           C  
ANISOU 3762  CB  GLN B 148    10958   9715   7647   1245   2833   1597       C  
ATOM   3763  CG  GLN B 148      54.407   7.797-128.513  1.00 77.63           C  
ANISOU 3763  CG  GLN B 148    11545  10032   7918   1140   2723   1528       C  
ATOM   3764  CD  GLN B 148      55.403   7.068-129.421  1.00 86.94           C  
ANISOU 3764  CD  GLN B 148    12685  11188   9161    965   2547   1493       C  
ATOM   3765  OE1 GLN B 148      56.513   6.743-129.001  1.00 90.65           O  
ANISOU 3765  OE1 GLN B 148    13342  11574   9528    900   2431   1407       O  
ATOM   3766  NE2 GLN B 148      55.004   6.806-130.666  1.00 87.30           N  
ANISOU 3766  NE2 GLN B 148    12486  11311   9374    892   2520   1563       N  
ATOM   3767  N   ARG B 149      55.242   9.951-131.383  1.00 53.41           N  
ANISOU 3767  N   ARG B 149     8398   6867   5027   1178   2621   1371       N  
ATOM   3768  CA  ARG B 149      56.568  10.094-131.971  1.00 49.03           C  
ANISOU 3768  CA  ARG B 149     7970   6212   4445   1081   2473   1247       C  
ATOM   3769  C   ARG B 149      56.990  11.559-132.026  1.00 54.46           C  
ANISOU 3769  C   ARG B 149     8855   6774   5063   1190   2502   1119       C  
ATOM   3770  O   ARG B 149      58.137  11.893-131.706  1.00 54.35           O  
ANISOU 3770  O   ARG B 149     9062   6636   4953   1136   2383    967       O  
ATOM   3771  CB  ARG B 149      56.587   9.458-133.364  1.00 50.85           C  
ANISOU 3771  CB  ARG B 149     7928   6513   4878    940   2338   1287       C  
ATOM   3772  CG  ARG B 149      57.958   9.404-134.012  1.00 55.21           C  
ANISOU 3772  CG  ARG B 149     8532   6966   5481    803   2100   1135       C  
ATOM   3773  CD  ARG B 149      58.981   8.658-133.155  1.00 51.10           C  
ANISOU 3773  CD  ARG B 149     8179   6379   4859    707   1971   1060       C  
ATOM   3774  NE  ARG B 149      60.233   8.504-133.895  1.00 51.84           N  
ANISOU 3774  NE  ARG B 149     8270   6405   5022    575   1747    939       N  
ATOM   3775  CZ  ARG B 149      61.447   8.548-133.353  1.00 49.79           C  
ANISOU 3775  CZ  ARG B 149     8199   6056   4664    524   1613    816       C  
ATOM   3776  NH1 ARG B 149      61.588   8.760-132.051  1.00 51.54           N  
ANISOU 3776  NH1 ARG B 149     8643   6239   4700    589   1672    786       N  
ATOM   3777  NH2 ARG B 149      62.525   8.402-134.120  1.00 44.00           N  
ANISOU 3777  NH2 ARG B 149     7428   5281   4010    411   1421    725       N  
ATOM   3778  N   LEU B 150      56.071  12.449-132.413  1.00 55.39           N  
ANISOU 3778  N   LEU B 150     8878   6917   5249   1331   2629   1169       N  
ATOM   3779  CA  LEU B 150      56.374  13.877-132.428  1.00 59.45           C  
ANISOU 3779  CA  LEU B 150     9593   7294   5703   1446   2676   1057       C  
ATOM   3780  C   LEU B 150      56.818  14.361-131.051  1.00 63.24           C  
ANISOU 3780  C   LEU B 150    10387   7645   5997   1499   2699    943       C  
ATOM   3781  O   LEU B 150      57.833  15.052-130.923  1.00 62.05           O  
ANISOU 3781  O   LEU B 150    10477   7350   5750   1465   2624    789       O  
ATOM   3782  CB  LEU B 150      55.154  14.666-132.911  1.00 58.21           C  
ANISOU 3782  CB  LEU B 150     9280   7191   5645   1614   2823   1159       C  
ATOM   3783  CG  LEU B 150      54.848  14.523-134.405  1.00 55.45           C  
ANISOU 3783  CG  LEU B 150     8652   6948   5469   1571   2783   1242       C  
ATOM   3784  CD1 LEU B 150      53.557  15.238-134.791  1.00 59.97           C  
ANISOU 3784  CD1 LEU B 150     9056   7597   6132   1747   2919   1362       C  
ATOM   3785  CD2 LEU B 150      56.018  15.057-135.186  1.00 55.02           C  
ANISOU 3785  CD2 LEU B 150     8723   6775   5405   1499   2679   1114       C  
ATOM   3786  N   GLN B 151      56.070  13.997-130.007  1.00 67.60           N  
ANISOU 3786  N   GLN B 151    10940   8250   6496   1571   2796   1017       N  
ATOM   3787  CA  GLN B 151      56.435  14.411-128.654  1.00 72.52           C  
ANISOU 3787  CA  GLN B 151    11856   8760   6938   1622   2818    919       C  
ATOM   3788  C   GLN B 151      57.809  13.879-128.271  1.00 65.64           C  
ANISOU 3788  C   GLN B 151    11157   7829   5955   1459   2636    795       C  
ATOM   3789  O   GLN B 151      58.637  14.599-127.703  1.00 72.71           O  
ANISOU 3789  O   GLN B 151    12321   8589   6717   1449   2579    646       O  
ATOM   3790  CB  GLN B 151      55.386  13.925-127.654  1.00 81.78           C  
ANISOU 3790  CB  GLN B 151    12970  10021   8081   1714   2950   1038       C  
ATOM   3791  CG  GLN B 151      54.207  14.856-127.454  1.00 88.49           C  
ANISOU 3791  CG  GLN B 151    13801  10868   8954   1922   3142   1111       C  
ATOM   3792  CD  GLN B 151      53.237  14.320-126.414  1.00 97.18           C  
ANISOU 3792  CD  GLN B 151    14851  12059  10015   2003   3266   1227       C  
ATOM   3793  OE1 GLN B 151      52.266  13.644-126.750  1.00105.23           O  
ANISOU 3793  OE1 GLN B 151    15594  13236  11154   2006   3324   1382       O  
ATOM   3794  NE2 GLN B 151      53.504  14.612-125.144  1.00 96.42           N  
ANISOU 3794  NE2 GLN B 151    15021  11866   9749   2057   3301   1151       N  
ATOM   3795  N   GLU B 152      58.063  12.612-128.583  1.00 59.20           N  
ANISOU 3795  N   GLU B 152    10186   7114   5194   1325   2535    859       N  
ATOM   3796  CA  GLU B 152      59.327  11.979-128.231  1.00 63.54           C  
ANISOU 3796  CA  GLU B 152    10873   7625   5645   1178   2354    767       C  
ATOM   3797  C   GLU B 152      60.511  12.655-128.921  1.00 65.06           C  
ANISOU 3797  C   GLU B 152    11191   7711   5817   1094   2215    617       C  
ATOM   3798  O   GLU B 152      61.559  12.880-128.301  1.00 58.80           O  
ANISOU 3798  O   GLU B 152    10619   6833   4887   1027   2091    482       O  
ATOM   3799  CB  GLU B 152      59.230  10.501-128.589  1.00 64.66           C  
ANISOU 3799  CB  GLU B 152    10803   7886   5879   1065   2291    889       C  
ATOM   3800  CG  GLU B 152      60.513   9.736-128.700  1.00 74.46           C  
ANISOU 3800  CG  GLU B 152    12085   9101   7106    901   2066    816       C  
ATOM   3801  CD  GLU B 152      60.250   8.351-129.248  1.00 88.66           C  
ANISOU 3801  CD  GLU B 152    13630  10997   9058    794   2004    939       C  
ATOM   3802  OE1 GLU B 152      59.209   8.187-129.921  1.00 92.47           O  
ANISOU 3802  OE1 GLU B 152    13896  11564   9676    820   2113   1059       O  
ATOM   3803  OE2 GLU B 152      61.057   7.431-128.998  1.00 94.23           O  
ANISOU 3803  OE2 GLU B 152    14357  11697   9747    685   1850    920       O  
ATOM   3804  N   VAL B 153      60.367  12.990-130.203  1.00 61.67           N  
ANISOU 3804  N   VAL B 153    10584   7291   5558   1078   2199    632       N  
ATOM   3805  CA  VAL B 153      61.445  13.686-130.896  1.00 53.80           C  
ANISOU 3805  CA  VAL B 153     9649   6188   4606    985   2036    484       C  
ATOM   3806  C   VAL B 153      61.675  15.064-130.278  1.00 55.71           C  
ANISOU 3806  C   VAL B 153    10202   6284   4683   1075   2121    358       C  
ATOM   3807  O   VAL B 153      62.819  15.458-130.025  1.00 56.67           O  
ANISOU 3807  O   VAL B 153    10505   6306   4722    972   1972    207       O  
ATOM   3808  CB  VAL B 153      61.146  13.760-132.405  1.00 50.58           C  
ANISOU 3808  CB  VAL B 153     8976   5824   4417    961   2010    538       C  
ATOM   3809  CG1 VAL B 153      62.132  14.686-133.108  1.00 51.38           C  
ANISOU 3809  CG1 VAL B 153     9161   5806   4555    894   1888    395       C  
ATOM   3810  CG2 VAL B 153      61.219  12.367-133.035  1.00 54.03           C  
ANISOU 3810  CG2 VAL B 153     9150   6377   5002    829   1878    620       C  
ATOM   3811  N   GLU B 154      60.597  15.808-130.005  1.00 59.85           N  
ANISOU 3811  N   GLU B 154    10762   6789   5188   1255   2335    418       N  
ATOM   3812  CA  GLU B 154      60.724  17.071-129.278  1.00 74.23           C  
ANISOU 3812  CA  GLU B 154    12852   8452   6899   1334   2388    303       C  
ATOM   3813  C   GLU B 154      61.543  16.892-128.003  1.00 72.32           C  
ANISOU 3813  C   GLU B 154    12842   8156   6480   1254   2278    194       C  
ATOM   3814  O   GLU B 154      62.504  17.629-127.755  1.00 78.43           O  
ANISOU 3814  O   GLU B 154    13832   8801   7166   1173   2171     39       O  
ATOM   3815  CB  GLU B 154      59.342  17.632-128.922  1.00 90.59           C  
ANISOU 3815  CB  GLU B 154    14889  10532   8999   1543   2609    412       C  
ATOM   3816  CG  GLU B 154      58.440  18.022-130.083  1.00105.64           C  
ANISOU 3816  CG  GLU B 154    16575  12489  11072   1651   2724    525       C  
ATOM   3817  CD  GLU B 154      57.074  18.511-129.603  1.00123.51           C  
ANISOU 3817  CD  GLU B 154    18801  14775  13352   1861   2929    644       C  
ATOM   3818  OE1 GLU B 154      56.805  19.730-129.692  1.00129.72           O  
ANISOU 3818  OE1 GLU B 154    19714  15439  14133   1986   3025    620       O  
ATOM   3819  OE2 GLU B 154      56.277  17.677-129.117  1.00129.19           O  
ANISOU 3819  OE2 GLU B 154    19371  15630  14086   1901   2994    766       O  
ATOM   3820  N   ALA B 155      61.175  15.901-127.187  1.00 67.01           N  
ANISOU 3820  N   ALA B 155    12115   7587   5758   1266   2296    279       N  
ATOM   3821  CA  ALA B 155      61.853  15.686-125.912  1.00 68.60           C  
ANISOU 3821  CA  ALA B 155    12523   7756   5787   1209   2201    195       C  
ATOM   3822  C   ALA B 155      63.318  15.318-126.108  1.00 64.59           C  
ANISOU 3822  C   ALA B 155    12073   7236   5234   1015   1957     79       C  
ATOM   3823  O   ALA B 155      64.180  15.745-125.331  1.00 66.07           O  
ANISOU 3823  O   ALA B 155    12472   7344   5286    944   1842    -51       O  
ATOM   3824  CB  ALA B 155      61.136  14.594-125.121  1.00 67.82           C  
ANISOU 3824  CB  ALA B 155    12324   7781   5662   1259   2273    328       C  
ATOM   3825  N   GLU B 156      63.620  14.515-127.129  1.00 56.32           N  
ANISOU 3825  N   GLU B 156    10831   6271   4296    923   1867    130       N  
ATOM   3826  CA  GLU B 156      64.999  14.077-127.320  1.00 57.94           C  
ANISOU 3826  CA  GLU B 156    11070   6478   4465    746   1628     36       C  
ATOM   3827  C   GLU B 156      65.880  15.219-127.811  1.00 60.89           C  
ANISOU 3827  C   GLU B 156    11562   6727   4845    664   1525   -124       C  
ATOM   3828  O   GLU B 156      67.045  15.326-127.408  1.00 65.02           O  
ANISOU 3828  O   GLU B 156    12215   7216   5273    534   1339   -246       O  
ATOM   3829  CB  GLU B 156      65.059  12.900-128.294  1.00 60.49           C  
ANISOU 3829  CB  GLU B 156    11066   6911   5006    659   1517    140       C  
ATOM   3830  CG  GLU B 156      66.266  12.001-128.052  1.00 74.02           C  
ANISOU 3830  CG  GLU B 156    12762   8667   6695    512   1279    101       C  
ATOM   3831  CD  GLU B 156      66.317  10.814-128.990  1.00 87.22           C  
ANISOU 3831  CD  GLU B 156    14140  10428   8571    437   1185    201       C  
ATOM   3832  OE1 GLU B 156      67.429  10.298-129.230  1.00 93.44           O  
ANISOU 3832  OE1 GLU B 156    14875  11234   9395    316    979    155       O  
ATOM   3833  OE2 GLU B 156      65.248  10.404-129.488  1.00 87.65           O  
ANISOU 3833  OE2 GLU B 156    14020  10539   8746    499   1317    326       O  
ATOM   3834  N   VAL B 157      65.352  16.078-128.685  1.00 56.46           N  
ANISOU 3834  N   VAL B 157    10952   6104   4399    732   1639   -120       N  
ATOM   3835  CA  VAL B 157      66.134  17.223-129.136  1.00 55.42           C  
ANISOU 3835  CA  VAL B 157    10951   5835   4269    656   1563   -266       C  
ATOM   3836  C   VAL B 157      66.386  18.176-127.969  1.00 65.40           C  
ANISOU 3836  C   VAL B 157    12493   6976   5381    666   1570   -377       C  
ATOM   3837  O   VAL B 157      67.465  18.767-127.853  1.00 61.04           O  
ANISOU 3837  O   VAL B 157    12067   6340   4785    525   1413   -513       O  
ATOM   3838  CB  VAL B 157      65.432  17.910-130.324  1.00 60.12           C  
ANISOU 3838  CB  VAL B 157    11415   6393   5037    744   1690   -214       C  
ATOM   3839  CG1 VAL B 157      66.106  19.237-130.673  1.00 65.65           C  
ANISOU 3839  CG1 VAL B 157    12303   6925   5718    689   1658   -360       C  
ATOM   3840  CG2 VAL B 157      65.452  16.996-131.548  1.00 55.72           C  
ANISOU 3840  CG2 VAL B 157    10502   5955   4713    672   1586   -114       C  
ATOM   3841  N   ALA B 158      65.417  18.296-127.059  1.00 68.85           N  
ANISOU 3841  N   ALA B 158    13001   7409   5748    818   1739   -310       N  
ATOM   3842  CA  ALA B 158      65.596  19.150-125.886  1.00 81.49           C  
ANISOU 3842  CA  ALA B 158    14863   8895   7204    831   1749   -403       C  
ATOM   3843  C   ALA B 158      66.620  18.569-124.918  1.00 82.48           C  
ANISOU 3843  C   ALA B 158    15077   9068   7192    691   1551   -478       C  
ATOM   3844  O   ALA B 158      67.376  19.313-124.283  1.00 84.27           O  
ANISOU 3844  O   ALA B 158    15499   9203   7317    601   1453   -602       O  
ATOM   3845  CB  ALA B 158      64.259  19.362-125.176  1.00 82.34           C  
ANISOU 3845  CB  ALA B 158    15015   8997   7274   1040   1985   -303       C  
ATOM   3846  N   ALA B 159      66.657  17.244-124.788  1.00 74.40           N  
ANISOU 3846  N   ALA B 159    13908   8193   6166    670   1489   -394       N  
ATOM   3847  CA  ALA B 159      67.563  16.615-123.838  1.00 73.48           C  
ANISOU 3847  CA  ALA B 159    13860   8139   5921    561   1308   -440       C  
ATOM   3848  C   ALA B 159      68.972  16.453-124.391  1.00 74.61           C  
ANISOU 3848  C   ALA B 159    13951   8304   6095    362   1052   -532       C  
ATOM   3849  O   ALA B 159      69.943  16.527-123.629  1.00 72.01           O  
ANISOU 3849  O   ALA B 159    13724   7981   5656    250    883   -619       O  
ATOM   3850  CB  ALA B 159      67.012  15.250-123.421  1.00 76.21           C  
ANISOU 3850  CB  ALA B 159    14077   8627   6252    628   1353   -298       C  
ATOM   3851  N   THR B 160      69.110  16.220-125.699  1.00 70.18           N  
ANISOU 3851  N   THR B 160    13218   7765   5681    317   1018   -507       N  
ATOM   3852  CA  THR B 160      70.387  15.832-126.277  1.00 63.87           C  
ANISOU 3852  CA  THR B 160    12325   7016   4927    140    777   -565       C  
ATOM   3853  C   THR B 160      70.831  16.685-127.459  1.00 63.52           C  
ANISOU 3853  C   THR B 160    12243   6885   5008     56    735   -645       C  
ATOM   3854  O   THR B 160      71.933  16.458-127.974  1.00 65.29           O  
ANISOU 3854  O   THR B 160    12377   7147   5283    -97    532   -696       O  
ATOM   3855  CB  THR B 160      70.343  14.360-126.731  1.00 68.82           C  
ANISOU 3855  CB  THR B 160    12750   7784   5614    139    727   -442       C  
ATOM   3856  OG1 THR B 160      69.538  14.234-127.912  1.00 62.61           O  
ANISOU 3856  OG1 THR B 160    11730   7004   5053    203    841   -344       O  
ATOM   3857  CG2 THR B 160      69.764  13.466-125.631  1.00 71.17           C  
ANISOU 3857  CG2 THR B 160    13070   8163   5808    234    798   -339       C  
ATOM   3858  N   GLY B 161      70.022  17.640-127.912  1.00 61.57           N  
ANISOU 3858  N   GLY B 161    12048   6527   4817    156    919   -646       N  
ATOM   3859  CA  GLY B 161      70.358  18.408-129.096  1.00 69.83           C  
ANISOU 3859  CA  GLY B 161    13051   7490   5993     91    897   -704       C  
ATOM   3860  C   GLY B 161      70.172  17.678-130.410  1.00 66.58           C  
ANISOU 3860  C   GLY B 161    12326   7167   5804     92    878   -599       C  
ATOM   3861  O   GLY B 161      70.486  18.243-131.468  1.00 71.23           O  
ANISOU 3861  O   GLY B 161    12828   7702   6535     36    845   -629       O  
ATOM   3862  N   THR B 162      69.677  16.447-130.385  1.00 59.76           N  
ANISOU 3862  N   THR B 162    11270   6437   4999    147    890   -467       N  
ATOM   3863  CA  THR B 162      69.474  15.683-131.608  1.00 57.06           C  
ANISOU 3863  CA  THR B 162    10611   6183   4887    138    860   -360       C  
ATOM   3864  C   THR B 162      68.472  14.574-131.299  1.00 50.36           C  
ANISOU 3864  C   THR B 162     9636   5444   4053    243    965   -210       C  
ATOM   3865  O   THR B 162      67.834  14.573-130.244  1.00 56.31           O  
ANISOU 3865  O   THR B 162    10544   6197   4654    342   1092   -184       O  
ATOM   3866  CB  THR B 162      70.815  15.161-132.143  1.00 52.02           C  
ANISOU 3866  CB  THR B 162     9835   5596   4332    -33    614   -403       C  
ATOM   3867  OG1 THR B 162      70.631  14.620-133.456  1.00 50.31           O  
ANISOU 3867  OG1 THR B 162     9342   5438   4336    -40    598   -319       O  
ATOM   3868  CG2 THR B 162      71.384  14.082-131.219  1.00 49.57           C  
ANISOU 3868  CG2 THR B 162     9535   5384   3916    -81    484   -384       C  
ATOM   3869  N   TYR B 163      68.306  13.641-132.232  1.00 49.41           N  
ANISOU 3869  N   TYR B 163     9243   5416   4116    218    921   -110       N  
ATOM   3870  CA  TYR B 163      67.430  12.501-131.999  1.00 49.94           C  
ANISOU 3870  CA  TYR B 163     9180   5585   4211    284   1003     32       C  
ATOM   3871  C   TYR B 163      67.869  11.361-132.903  1.00 50.03           C  
ANISOU 3871  C   TYR B 163     8942   5676   4390    187    859     90       C  
ATOM   3872  O   TYR B 163      68.723  11.528-133.775  1.00 48.54           O  
ANISOU 3872  O   TYR B 163     8670   5471   4303     93    723     29       O  
ATOM   3873  CB  TYR B 163      65.961  12.867-132.235  1.00 47.23           C  
ANISOU 3873  CB  TYR B 163     8781   5251   3913    431   1236    132       C  
ATOM   3874  CG  TYR B 163      65.600  13.068-133.694  1.00 48.99           C  
ANISOU 3874  CG  TYR B 163     8783   5490   4340    430   1251    176       C  
ATOM   3875  CD1 TYR B 163      65.978  14.222-134.366  1.00 43.34           C  
ANISOU 3875  CD1 TYR B 163     8123   4681   3664    421   1240     86       C  
ATOM   3876  CD2 TYR B 163      64.859  12.121-134.384  1.00 42.51           C  
ANISOU 3876  CD2 TYR B 163     7711   4776   3663    434   1280    308       C  
ATOM   3877  CE1 TYR B 163      65.641  14.425-135.690  1.00 45.29           C  
ANISOU 3877  CE1 TYR B 163     8176   4947   4084    429   1257    133       C  
ATOM   3878  CE2 TYR B 163      64.517  12.311-135.714  1.00 43.82           C  
ANISOU 3878  CE2 TYR B 163     7682   4968   4000    430   1287    347       C  
ATOM   3879  CZ  TYR B 163      64.911  13.471-136.361  1.00 44.43           C  
ANISOU 3879  CZ  TYR B 163     7817   4957   4109    436   1277    262       C  
ATOM   3880  OH  TYR B 163      64.593  13.683-137.690  1.00 46.00           O  
ANISOU 3880  OH  TYR B 163     7828   5184   4466    439   1282    304       O  
ATOM   3881  N   GLN B 164      67.267  10.195-132.690  1.00 48.71           N  
ANISOU 3881  N   GLN B 164     8664   5593   4249    211    900    210       N  
ATOM   3882  CA  GLN B 164      67.615   8.978-133.416  1.00 41.77           C  
ANISOU 3882  CA  GLN B 164     7581   4779   3511    126    779    271       C  
ATOM   3883  C   GLN B 164      66.409   8.474-134.195  1.00 42.56           C  
ANISOU 3883  C   GLN B 164     7478   4936   3755    163    899    396       C  
ATOM   3884  O   GLN B 164      65.283   8.464-133.674  1.00 42.58           O  
ANISOU 3884  O   GLN B 164     7496   4971   3713    255   1070    483       O  
ATOM   3885  CB  GLN B 164      68.092   7.859-132.462  1.00 48.18           C  
ANISOU 3885  CB  GLN B 164     8449   5632   4224     97    697    307       C  
ATOM   3886  CG  GLN B 164      69.165   8.263-131.450  1.00 57.65           C  
ANISOU 3886  CG  GLN B 164     9859   6802   5243     68    584    201       C  
ATOM   3887  CD  GLN B 164      70.418   8.820-132.099  1.00 62.52           C  
ANISOU 3887  CD  GLN B 164    10458   7388   5909    -32    409     85       C  
ATOM   3888  OE1 GLN B 164      71.030   8.186-132.962  1.00 62.29           O  
ANISOU 3888  OE1 GLN B 164    10263   7391   6015   -101    289    100       O  
ATOM   3889  NE2 GLN B 164      70.803  10.024-131.686  1.00 69.05           N  
ANISOU 3889  NE2 GLN B 164    11463   8149   6624    -43    401    -31       N  
ATOM   3890  N   LEU B 165      66.653   8.042-135.434  1.00 41.62           N  
ANISOU 3890  N   LEU B 165     7169   4841   3805     90    809    408       N  
ATOM   3891  CA  LEU B 165      65.607   7.442-136.251  1.00 39.71           C  
ANISOU 3891  CA  LEU B 165     6723   4665   3701     94    889    522       C  
ATOM   3892  C   LEU B 165      65.339   6.004-135.835  1.00 42.08           C  
ANISOU 3892  C   LEU B 165     6968   5016   4005     55    882    621       C  
ATOM   3893  O   LEU B 165      66.260   5.250-135.507  1.00 38.14           O  
ANISOU 3893  O   LEU B 165     6516   4501   3473     -4    755    596       O  
ATOM   3894  CB  LEU B 165      65.988   7.466-137.733  1.00 31.19           C  
ANISOU 3894  CB  LEU B 165     5478   3588   2785     24    790    494       C  
ATOM   3895  CG  LEU B 165      66.191   8.847-138.355  1.00 38.11           C  
ANISOU 3895  CG  LEU B 165     6384   4412   3685     55    804    414       C  
ATOM   3896  CD1 LEU B 165      66.640   8.717-139.805  1.00 40.95           C  
ANISOU 3896  CD1 LEU B 165     6579   4781   4197    -19    698    394       C  
ATOM   3897  CD2 LEU B 165      64.909   9.670-138.251  1.00 40.72           C  
ANISOU 3897  CD2 LEU B 165     6719   4758   3997    178    999    475       C  
ATOM   3898  N   ARG B 166      64.068   5.621-135.865  1.00 44.65           N  
ANISOU 3898  N   ARG B 166     7187   5404   4372     88   1022    741       N  
ATOM   3899  CA  ARG B 166      63.741   4.211-135.795  1.00 45.93           C  
ANISOU 3899  CA  ARG B 166     7262   5608   4581     21   1013    841       C  
ATOM   3900  C   ARG B 166      64.128   3.545-137.108  1.00 46.82           C  
ANISOU 3900  C   ARG B 166     7214   5724   4853    -86    886    831       C  
ATOM   3901  O   ARG B 166      64.202   4.192-138.155  1.00 42.63           O  
ANISOU 3901  O   ARG B 166     6591   5194   4411    -95    854    784       O  
ATOM   3902  CB  ARG B 166      62.257   4.021-135.502  1.00 41.94           C  
ANISOU 3902  CB  ARG B 166     6673   5180   4082     69   1198    977       C  
ATOM   3903  CG  ARG B 166      61.872   4.461-134.094  1.00 46.12           C  
ANISOU 3903  CG  ARG B 166     7376   5708   4440    181   1335   1001       C  
ATOM   3904  CD  ARG B 166      60.378   4.458-133.905  1.00 49.94           C  
ANISOU 3904  CD  ARG B 166     7756   6281   4938    246   1535   1140       C  
ATOM   3905  NE  ARG B 166      59.981   4.912-132.575  1.00 54.71           N  
ANISOU 3905  NE  ARG B 166     8533   6884   5371    369   1686   1165       N  
ATOM   3906  CZ  ARG B 166      58.722   5.154-132.233  1.00 55.75           C  
ANISOU 3906  CZ  ARG B 166     8605   7093   5484    464   1887   1281       C  
ATOM   3907  NH1 ARG B 166      57.762   4.981-133.138  1.00 54.35           N  
ANISOU 3907  NH1 ARG B 166     8186   7010   5453    437   1946   1382       N  
ATOM   3908  NH2 ARG B 166      58.421   5.547-130.992  1.00 50.19           N  
ANISOU 3908  NH2 ARG B 166     8079   6382   4610    584   2028   1300       N  
ATOM   3909  N   GLU B 167      64.379   2.233-137.039  1.00 45.99           N  
ANISOU 3909  N   GLU B 167     7087   5612   4775   -163    821    878       N  
ATOM   3910  CA  GLU B 167      64.819   1.490-138.221  1.00 48.12           C  
ANISOU 3910  CA  GLU B 167     7235   5869   5179   -262    702    863       C  
ATOM   3911  C   GLU B 167      63.864   1.676-139.398  1.00 46.01           C  
ANISOU 3911  C   GLU B 167     6780   5659   5040   -297    752    904       C  
ATOM   3912  O   GLU B 167      64.300   1.923-140.526  1.00 41.80           O  
ANISOU 3912  O   GLU B 167     6166   5118   4597   -333    666    844       O  
ATOM   3913  CB  GLU B 167      64.971   0.005-137.879  1.00 53.61           C  
ANISOU 3913  CB  GLU B 167     7952   6540   5878   -327    666    929       C  
ATOM   3914  CG  GLU B 167      65.950  -0.743-138.777  1.00 74.23           C  
ANISOU 3914  CG  GLU B 167    10526   9102   8577   -400    517    881       C  
ATOM   3915  CD  GLU B 167      66.591  -1.938-138.077  1.00103.19           C  
ANISOU 3915  CD  GLU B 167    14298  12718  12192   -414    463    917       C  
ATOM   3916  OE1 GLU B 167      65.876  -2.681-137.366  1.00113.25           O  
ANISOU 3916  OE1 GLU B 167    15606  13994  13431   -426    552   1016       O  
ATOM   3917  OE2 GLU B 167      67.818  -2.126-138.227  1.00111.74           O  
ANISOU 3917  OE2 GLU B 167    15426  13761  13268   -408    336    854       O  
ATOM   3918  N   SER B 168      62.553   1.551-139.169  1.00 46.11           N  
ANISOU 3918  N   SER B 168     6714   5744   5062   -286    891   1014       N  
ATOM   3919  CA ASER B 168      61.623   1.714-140.287  0.47 40.09           C  
ANISOU 3919  CA ASER B 168     5756   5060   4417   -322    929   1063       C  
ATOM   3920  CA BSER B 168      61.613   1.716-140.278  0.53 40.11           C  
ANISOU 3920  CA BSER B 168     5758   5062   4418   -321    930   1064       C  
ATOM   3921  C   SER B 168      61.624   3.140-140.823  1.00 37.40           C  
ANISOU 3921  C   SER B 168     5391   4734   4084   -233    951   1004       C  
ATOM   3922  O   SER B 168      61.409   3.349-142.028  1.00 38.68           O  
ANISOU 3922  O   SER B 168     5413   4936   4347   -268    913   1000       O  
ATOM   3923  CB ASER B 168      60.210   1.315-139.873  0.47 44.42           C  
ANISOU 3923  CB ASER B 168     6207   5701   4970   -329   1076   1205       C  
ATOM   3924  CB BSER B 168      60.202   1.334-139.835  0.53 44.41           C  
ANISOU 3924  CB BSER B 168     6209   5700   4965   -325   1079   1206       C  
ATOM   3925  OG ASER B 168      60.115  -0.083-139.671  0.47 53.85           O  
ANISOU 3925  OG ASER B 168     7395   6878   6187   -443   1050   1267       O  
ATOM   3926  OG BSER B 168      59.813   2.051-138.672  0.53 47.83           O  
ANISOU 3926  OG BSER B 168     6747   6148   5280   -197   1217   1236       O  
ATOM   3927  N   GLU B 169      61.860   4.130-139.961  1.00 35.67           N  
ANISOU 3927  N   GLU B 169     5320   4478   3755   -120   1012    959       N  
ATOM   3928  CA  GLU B 169      61.943   5.512-140.432  1.00 33.78           C  
ANISOU 3928  CA  GLU B 169     5092   4226   3519    -36   1038    897       C  
ATOM   3929  C   GLU B 169      63.164   5.712-141.316  1.00 41.38           C  
ANISOU 3929  C   GLU B 169     6064   5122   4535    -95    878    783       C  
ATOM   3930  O   GLU B 169      63.115   6.465-142.305  1.00 35.90           O  
ANISOU 3930  O   GLU B 169     5292   4439   3910    -77    869    757       O  
ATOM   3931  CB  GLU B 169      61.994   6.471-139.235  1.00 36.38           C  
ANISOU 3931  CB  GLU B 169     5613   4506   3701     86   1138    863       C  
ATOM   3932  CG  GLU B 169      60.740   6.502-138.383  1.00 35.61           C  
ANISOU 3932  CG  GLU B 169     5511   4478   3541    177   1326    979       C  
ATOM   3933  CD  GLU B 169      60.954   7.228-137.056  1.00 46.10           C  
ANISOU 3933  CD  GLU B 169     7075   5742   4700    286   1410    931       C  
ATOM   3934  OE1 GLU B 169      62.116   7.570-136.735  1.00 45.83           O  
ANISOU 3934  OE1 GLU B 169     7206   5614   4594    266   1303    808       O  
ATOM   3935  OE2 GLU B 169      59.960   7.453-136.335  1.00 46.91           O  
ANISOU 3935  OE2 GLU B 169     7196   5893   4735    389   1584   1019       O  
ATOM   3936  N   LEU B 170      64.274   5.063-140.957  1.00 38.08           N  
ANISOU 3936  N   LEU B 170     5741   4643   4084   -156    756    721       N  
ATOM   3937  CA  LEU B 170      65.491   5.161-141.755  1.00 36.77           C  
ANISOU 3937  CA  LEU B 170     5574   4427   3970   -211    607    622       C  
ATOM   3938  C   LEU B 170      65.282   4.564-143.143  1.00 37.40           C  
ANISOU 3938  C   LEU B 170     5477   4546   4186   -288    551    649       C  
ATOM   3939  O   LEU B 170      65.696   5.140-144.160  1.00 35.23           O  
ANISOU 3939  O   LEU B 170     5148   4263   3976   -297    496    595       O  
ATOM   3940  CB  LEU B 170      66.640   4.454-141.036  1.00 33.35           C  
ANISOU 3940  CB  LEU B 170     5257   3943   3472   -250    495    575       C  
ATOM   3941  CG  LEU B 170      67.942   4.396-141.848  1.00 30.03           C  
ANISOU 3941  CG  LEU B 170     4815   3486   3109   -307    341    490       C  
ATOM   3942  CD1 LEU B 170      68.496   5.796-142.077  1.00 37.28           C  
ANISOU 3942  CD1 LEU B 170     5784   4370   4009   -277    325    399       C  
ATOM   3943  CD2 LEU B 170      68.957   3.522-141.110  1.00 36.16           C  
ANISOU 3943  CD2 LEU B 170     5681   4234   3824   -333    240    474       C  
ATOM   3944  N   VAL B 171      64.643   3.396-143.204  1.00 36.02           N  
ANISOU 3944  N   VAL B 171     5223   4412   4053   -352    564    731       N  
ATOM   3945  CA  VAL B 171      64.386   2.764-144.498  1.00 33.30           C  
ANISOU 3945  CA  VAL B 171     4727   4102   3824   -439    509    752       C  
ATOM   3946  C   VAL B 171      63.490   3.652-145.352  1.00 34.91           C  
ANISOU 3946  C   VAL B 171     4798   4383   4082   -403    575    785       C  
ATOM   3947  O   VAL B 171      63.729   3.839-146.549  1.00 35.12           O  
ANISOU 3947  O   VAL B 171     4741   4422   4182   -435    508    750       O  
ATOM   3948  CB  VAL B 171      63.759   1.373-144.298  1.00 34.57           C  
ANISOU 3948  CB  VAL B 171     4845   4283   4007   -527    524    838       C  
ATOM   3949  CG1 VAL B 171      63.382   0.761-145.651  1.00 36.08           C  
ANISOU 3949  CG1 VAL B 171     4889   4512   4307   -631    470    855       C  
ATOM   3950  CG2 VAL B 171      64.729   0.461-143.547  1.00 39.15           C  
ANISOU 3950  CG2 VAL B 171     5561   4778   4535   -550    454    811       C  
ATOM   3951  N   PHE B 172      62.418   4.172-144.757  1.00 35.89           N  
ANISOU 3951  N   PHE B 172     4899   4569   4168   -329    713    862       N  
ATOM   3952  CA  PHE B 172      61.516   5.054-145.487  1.00 35.94           C  
ANISOU 3952  CA  PHE B 172     4776   4660   4218   -269    788    911       C  
ATOM   3953  C   PHE B 172      62.242   6.309-145.969  1.00 41.35           C  
ANISOU 3953  C   PHE B 172     5523   5289   4900   -195    762    822       C  
ATOM   3954  O   PHE B 172      62.056   6.754-147.119  1.00 33.31           O  
ANISOU 3954  O   PHE B 172     4393   4313   3950   -193    741    826       O  
ATOM   3955  CB  PHE B 172      60.334   5.422-144.589  1.00 36.50           C  
ANISOU 3955  CB  PHE B 172     4832   4803   4235   -176    956   1015       C  
ATOM   3956  CG  PHE B 172      59.538   6.582-145.096  1.00 39.19           C  
ANISOU 3956  CG  PHE B 172     5081   5216   4595    -63   1055   1063       C  
ATOM   3957  CD1 PHE B 172      58.610   6.403-146.118  1.00 41.23           C  
ANISOU 3957  CD1 PHE B 172     5124   5603   4940    -99   1060   1152       C  
ATOM   3958  CD2 PHE B 172      59.739   7.858-144.583  1.00 34.64           C  
ANISOU 3958  CD2 PHE B 172     4640   4575   3944     78   1140   1020       C  
ATOM   3959  CE1 PHE B 172      57.890   7.474-146.609  1.00 43.31           C  
ANISOU 3959  CE1 PHE B 172     5295   5942   5218     21   1150   1208       C  
ATOM   3960  CE2 PHE B 172      59.014   8.938-145.063  1.00 41.79           C  
ANISOU 3960  CE2 PHE B 172     5475   5536   4867    200   1242   1072       C  
ATOM   3961  CZ  PHE B 172      58.087   8.746-146.082  1.00 48.56           C  
ANISOU 3961  CZ  PHE B 172     6103   6534   5814    179   1248   1172       C  
ATOM   3962  N   GLY B 173      63.079   6.889-145.104  1.00 31.67           N  
ANISOU 3962  N   GLY B 173     4477   3966   3588   -143    761    742       N  
ATOM   3963  CA  GLY B 173      63.768   8.126-145.454  1.00 38.07           C  
ANISOU 3963  CA  GLY B 173     5365   4710   4390    -86    745    657       C  
ATOM   3964  C   GLY B 173      64.792   7.961-146.568  1.00 37.78           C  
ANISOU 3964  C   GLY B 173     5285   4642   4428   -168    602    583       C  
ATOM   3965  O   GLY B 173      64.984   8.867-147.385  1.00 32.33           O  
ANISOU 3965  O   GLY B 173     4572   3937   3775   -136    599    553       O  
ATOM   3966  N   ALA B 174      65.484   6.819-146.597  1.00 33.60           N  
ANISOU 3966  N   ALA B 174     4753   4096   3918   -264    491    557       N  
ATOM   3967  CA  ALA B 174      66.475   6.572-147.641  1.00 36.85           C  
ANISOU 3967  CA  ALA B 174     5123   4482   4397   -332    364    494       C  
ATOM   3968  C   ALA B 174      65.808   6.404-149.005  1.00 34.50           C  
ANISOU 3968  C   ALA B 174     4660   4259   4191   -362    359    540       C  
ATOM   3969  O   ALA B 174      66.277   6.960-150.003  1.00 30.14           O  
ANISOU 3969  O   ALA B 174     4071   3697   3684   -361    315    499       O  
ATOM   3970  CB  ALA B 174      67.297   5.331-147.290  1.00 29.87           C  
ANISOU 3970  CB  ALA B 174     4282   3564   3505   -406    264    469       C  
ATOM   3971  N   LYS B 175      64.715   5.636-149.055  1.00 34.27           N  
ANISOU 3971  N   LYS B 175     4529   4307   4184   -396    401    628       N  
ATOM   3972  CA  LYS B 175      63.920   5.511-150.272  1.00 34.41           C  
ANISOU 3972  CA  LYS B 175     4383   4417   4274   -430    396    681       C  
ATOM   3973  C   LYS B 175      63.370   6.859-150.726  1.00 34.84           C  
ANISOU 3973  C   LYS B 175     4386   4517   4334   -326    476    710       C  
ATOM   3974  O   LYS B 175      63.322   7.141-151.925  1.00 34.16           O  
ANISOU 3974  O   LYS B 175     4207   4474   4300   -334    438    711       O  
ATOM   3975  CB  LYS B 175      62.767   4.531-150.041  1.00 28.84           C  
ANISOU 3975  CB  LYS B 175     3583   3796   3581   -494    437    779       C  
ATOM   3976  CG  LYS B 175      63.205   3.067-149.912  1.00 31.59           C  
ANISOU 3976  CG  LYS B 175     3968   4094   3940   -612    355    761       C  
ATOM   3977  CD  LYS B 175      62.083   2.199-149.366  1.00 39.96           C  
ANISOU 3977  CD  LYS B 175     4967   5217   4998   -675    418    862       C  
ATOM   3978  CE  LYS B 175      62.438   0.734-149.507  1.00 50.63           C  
ANISOU 3978  CE  LYS B 175     6353   6511   6374   -805    336    847       C  
ATOM   3979  NZ  LYS B 175      61.500  -0.150-148.761  1.00 58.12           N  
ANISOU 3979  NZ  LYS B 175     7278   7493   7312   -874    402    942       N  
ATOM   3980  N   GLN B 176      62.890   7.684-149.789  1.00 31.65           N  
ANISOU 3980  N   GLN B 176     4047   4108   3872   -219    595    742       N  
ATOM   3981  CA  GLN B 176      62.376   8.994-150.173  1.00 34.10           C  
ANISOU 3981  CA  GLN B 176     4330   4445   4183   -100    686    775       C  
ATOM   3982  C   GLN B 176      63.475   9.874-150.729  1.00 30.38           C  
ANISOU 3982  C   GLN B 176     3945   3878   3720    -81    633    679       C  
ATOM   3983  O   GLN B 176      63.220  10.677-151.631  1.00 33.16           O  
ANISOU 3983  O   GLN B 176     4236   4259   4106    -24    659    703       O  
ATOM   3984  CB  GLN B 176      61.712   9.702-148.985  1.00 37.19           C  
ANISOU 3984  CB  GLN B 176     4805   4827   4498     23    837    820       C  
ATOM   3985  CG  GLN B 176      60.357   9.164-148.639  1.00 42.54           C  
ANISOU 3985  CG  GLN B 176     5353   5633   5178     38    929    949       C  
ATOM   3986  CD  GLN B 176      59.346   9.354-149.746  1.00 39.33           C  
ANISOU 3986  CD  GLN B 176     4738   5368   4837     61    953   1049       C  
ATOM   3987  OE1 GLN B 176      58.946   8.398-150.391  1.00 53.59           O  
ANISOU 3987  OE1 GLN B 176     6394   7269   6698    -53    881   1093       O  
ATOM   3988  NE2 GLN B 176      58.924  10.583-149.958  1.00 53.54           N  
ANISOU 3988  NE2 GLN B 176     6534   7182   6625    208   1054   1088       N  
ATOM   3989  N   ALA B 177      64.699   9.736-150.214  1.00 27.75           N  
ANISOU 3989  N   ALA B 177     3749   3438   3356   -130    557    579       N  
ATOM   3990  CA  ALA B 177      65.796  10.549-150.720  1.00 31.78           C  
ANISOU 3990  CA  ALA B 177     4333   3864   3878   -131    504    492       C  
ATOM   3991  C   ALA B 177      66.077  10.214-152.178  1.00 27.80           C  
ANISOU 3991  C   ALA B 177     3704   3403   3454   -190    416    490       C  
ATOM   3992  O   ALA B 177      66.321  11.108-152.998  1.00 30.44           O  
ANISOU 3992  O   ALA B 177     4030   3719   3816   -154    423    476       O  
ATOM   3993  CB  ALA B 177      67.053  10.335-149.883  1.00 27.41           C  
ANISOU 3993  CB  ALA B 177     3922   3216   3276   -187    426    397       C  
ATOM   3994  N   TRP B 178      66.089   8.927-152.505  1.00 28.13           N  
ANISOU 3994  N   TRP B 178     3666   3492   3528   -281    336    500       N  
ATOM   3995  CA  TRP B 178      66.216   8.518-153.905  1.00 26.43           C  
ANISOU 3995  CA  TRP B 178     3339   3326   3378   -336    259    500       C  
ATOM   3996  C   TRP B 178      65.041   9.035-154.718  1.00 30.08           C  
ANISOU 3996  C   TRP B 178     3673   3892   3864   -283    322    587       C  
ATOM   3997  O   TRP B 178      65.218   9.650-155.783  1.00 28.45           O  
ANISOU 3997  O   TRP B 178     3423   3701   3687   -258    307    583       O  
ATOM   3998  CB  TRP B 178      66.298   6.993-153.970  1.00 26.89           C  
ANISOU 3998  CB  TRP B 178     3361   3403   3453   -442    179    498       C  
ATOM   3999  CG  TRP B 178      66.536   6.423-155.350  1.00 28.19           C  
ANISOU 3999  CG  TRP B 178     3442   3601   3668   -508     94    482       C  
ATOM   4000  CD1 TRP B 178      66.816   7.110-156.500  1.00 27.54           C  
ANISOU 4000  CD1 TRP B 178     3316   3536   3614   -483     75    466       C  
ATOM   4001  CD2 TRP B 178      66.499   5.040-155.698  1.00 31.48           C  
ANISOU 4001  CD2 TRP B 178     3827   4030   4102   -608     25    480       C  
ATOM   4002  NE1 TRP B 178      66.968   6.224-157.550  1.00 29.54           N  
ANISOU 4002  NE1 TRP B 178     3511   3819   3895   -560     -5    451       N  
ATOM   4003  CE2 TRP B 178      66.765   4.946-157.081  1.00 29.24           C  
ANISOU 4003  CE2 TRP B 178     3485   3773   3852   -639    -36    455       C  
ATOM   4004  CE3 TRP B 178      66.246   3.868-154.976  1.00 28.14           C  
ANISOU 4004  CE3 TRP B 178     3432   3592   3667   -675     15    498       C  
ATOM   4005  CZ2 TRP B 178      66.804   3.714-157.748  1.00 26.35           C  
ANISOU 4005  CZ2 TRP B 178     3100   3411   3501   -736   -108    439       C  
ATOM   4006  CZ3 TRP B 178      66.290   2.651-155.634  1.00 30.65           C  
ANISOU 4006  CZ3 TRP B 178     3731   3906   4008   -773    -55    485       C  
ATOM   4007  CH2 TRP B 178      66.566   2.581-157.007  1.00 31.15           C  
ANISOU 4007  CH2 TRP B 178     3748   3990   4099   -804   -116    452       C  
ATOM   4008  N   ARG B 179      63.824   8.782-154.224  1.00 32.02           N  
ANISOU 4008  N   ARG B 179     3849   4222   4097   -262    395    675       N  
ATOM   4009  CA  ARG B 179      62.613   9.250-154.892  1.00 35.23           C  
ANISOU 4009  CA  ARG B 179     4111   4753   4521   -202    458    777       C  
ATOM   4010  C   ARG B 179      62.666  10.751-155.213  1.00 39.05           C  
ANISOU 4010  C   ARG B 179     4633   5206   4997    -69    534    785       C  
ATOM   4011  O   ARG B 179      62.155  11.189-156.252  1.00 34.95           O  
ANISOU 4011  O   ARG B 179     4004   4772   4504    -28    541    843       O  
ATOM   4012  CB  ARG B 179      61.419   8.922-154.001  1.00 34.84           C  
ANISOU 4012  CB  ARG B 179     4003   4787   4449   -179    549    873       C  
ATOM   4013  CG  ARG B 179      60.068   9.201-154.594  1.00 36.75           C  
ANISOU 4013  CG  ARG B 179     4062   5191   4711   -128    609    999       C  
ATOM   4014  CD  ARG B 179      59.002   9.164-153.513  1.00 36.75           C  
ANISOU 4014  CD  ARG B 179     4025   5258   4680    -69    732   1096       C  
ATOM   4015  NE  ARG B 179      57.669   9.180-154.093  1.00 39.51           N  
ANISOU 4015  NE  ARG B 179     4161   5795   5056    -47    773   1231       N  
ATOM   4016  CZ  ARG B 179      56.552   8.966-153.412  1.00 42.60           C  
ANISOU 4016  CZ  ARG B 179     4453   6297   5436    -19    870   1345       C  
ATOM   4017  NH1 ARG B 179      56.598   8.713-152.106  1.00 47.58           N  
ANISOU 4017  NH1 ARG B 179     5195   6859   6025     -5    943   1337       N  
ATOM   4018  NH2 ARG B 179      55.389   8.989-154.043  1.00 43.34           N  
ANISOU 4018  NH2 ARG B 179     4330   6582   5557     -6    892   1473       N  
ATOM   4019  N   ASN B 180      63.277  11.551-154.330  1.00 31.35           N  
ANISOU 4019  N   ASN B 180     3823   4107   3981     -5    591    728       N  
ATOM   4020  CA  ASN B 180      63.334  13.008-154.435  1.00 33.19           C  
ANISOU 4020  CA  ASN B 180     4135   4278   4198    119    681    730       C  
ATOM   4021  C   ASN B 180      64.482  13.537-155.301  1.00 29.71           C  
ANISOU 4021  C   ASN B 180     3750   3753   3786     88    611    652       C  
ATOM   4022  O   ASN B 180      64.548  14.752-155.519  1.00 32.99           O  
ANISOU 4022  O   ASN B 180     4233   4107   4194    181    685    657       O  
ATOM   4023  CB  ASN B 180      63.436  13.613-153.015  1.00 33.81           C  
ANISOU 4023  CB  ASN B 180     4390   4251   4206    188    778    697       C  
ATOM   4024  CG  ASN B 180      62.127  13.536-152.256  1.00 34.67           C  
ANISOU 4024  CG  ASN B 180     4448   4445   4280    276    900    800       C  
ATOM   4025  OD1 ASN B 180      61.072  13.372-152.863  1.00 36.15           O  
ANISOU 4025  OD1 ASN B 180     4461   4772   4500    313    933    909       O  
ATOM   4026  ND2 ASN B 180      62.183  13.658-150.907  1.00 31.61           N  
ANISOU 4026  ND2 ASN B 180     4207   3983   3819    311    969    770       N  
ATOM   4027  N   ALA B 181      65.395  12.672-155.781  1.00 30.30           N  
ANISOU 4027  N   ALA B 181     3804   3817   3891    -34    482    584       N  
ATOM   4028  CA  ALA B 181      66.639  13.095-156.419  1.00 25.59           C  
ANISOU 4028  CA  ALA B 181     3268   3136   3317    -72    418    506       C  
ATOM   4029  C   ALA B 181      66.351  13.598-157.839  1.00 26.40           C  
ANISOU 4029  C   ALA B 181     3272   3300   3457    -31    423    557       C  
ATOM   4030  O   ALA B 181      66.046  12.790-158.718  1.00 30.27           O  
ANISOU 4030  O   ALA B 181     3636   3892   3974    -81    357    587       O  
ATOM   4031  CB  ALA B 181      67.646  11.945-156.457  1.00 27.09           C  
ANISOU 4031  CB  ALA B 181     3458   3310   3524   -194    292    433       C  
ATOM   4032  N   PRO B 182      66.419  14.909-158.092  1.00 30.39           N  
ANISOU 4032  N   PRO B 182     3842   3745   3959     59    502    571       N  
ATOM   4033  CA  PRO B 182      65.953  15.434-159.398  1.00 30.03           C  
ANISOU 4033  CA  PRO B 182     3700   3771   3939    122    523    644       C  
ATOM   4034  C   PRO B 182      66.766  14.970-160.591  1.00 34.56           C  
ANISOU 4034  C   PRO B 182     4217   4367   4547     38    417    606       C  
ATOM   4035  O   PRO B 182      66.246  14.995-161.718  1.00 30.37           O  
ANISOU 4035  O   PRO B 182     3576   3937   4027     68    406    671       O  
ATOM   4036  CB  PRO B 182      66.067  16.957-159.237  1.00 30.09           C  
ANISOU 4036  CB  PRO B 182     3836   3665   3931    232    638    653       C  
ATOM   4037  CG  PRO B 182      66.244  17.190-157.731  1.00 35.88           C  
ANISOU 4037  CG  PRO B 182     4722   4289   4620    237    692    596       C  
ATOM   4038  CD  PRO B 182      66.931  15.979-157.223  1.00 29.93           C  
ANISOU 4038  CD  PRO B 182     3961   3542   3868    102    575    520       C  
ATOM   4039  N   ARG B 183      68.026  14.596-160.403  1.00 32.28           N  
ANISOU 4039  N   ARG B 183     3999   3995   4270    -57    342    509       N  
ATOM   4040  CA  ARG B 183      68.895  14.271-161.524  1.00 33.43           C  
ANISOU 4040  CA  ARG B 183     4105   4151   4445   -119    260    474       C  
ATOM   4041  C   ARG B 183      68.968  12.779-161.815  1.00 35.05           C  
ANISOU 4041  C   ARG B 183     4230   4429   4657   -210    157    450       C  
ATOM   4042  O   ARG B 183      69.711  12.376-162.723  1.00 29.81           O  
ANISOU 4042  O   ARG B 183     3543   3774   4011   -258     92    417       O  
ATOM   4043  CB  ARG B 183      70.297  14.832-161.281  1.00 33.22           C  
ANISOU 4043  CB  ARG B 183     4191   3999   4433   -161    247    394       C  
ATOM   4044  CG  ARG B 183      70.338  16.381-161.307  1.00 32.02           C  
ANISOU 4044  CG  ARG B 183     4132   3757   4278    -86    347    414       C  
ATOM   4045  CD  ARG B 183      71.651  16.944-160.798  1.00 31.67           C  
ANISOU 4045  CD  ARG B 183     4209   3583   4240   -154    333    330       C  
ATOM   4046  NE  ARG B 183      71.773  18.359-161.134  1.00 34.55           N  
ANISOU 4046  NE  ARG B 183     4661   3856   4610   -102    423    351       N  
ATOM   4047  CZ  ARG B 183      72.820  19.126-160.844  1.00 41.75           C  
ANISOU 4047  CZ  ARG B 183     5686   4647   5530   -165    428    291       C  
ATOM   4048  NH1 ARG B 183      73.866  18.627-160.196  1.00 38.70           N  
ANISOU 4048  NH1 ARG B 183     5325   4235   5145   -277    341    209       N  
ATOM   4049  NH2 ARG B 183      72.822  20.400-161.210  1.00 40.51           N  
ANISOU 4049  NH2 ARG B 183     5617   4397   5378   -117    520    318       N  
ATOM   4050  N   CYS B 184      68.200  11.951-161.099  1.00 28.74           N  
ANISOU 4050  N   CYS B 184     3398   3679   3843   -234    150    470       N  
ATOM   4051  CA  CYS B 184      68.247  10.508-161.277  1.00 24.99           C  
ANISOU 4051  CA  CYS B 184     2873   3249   3371   -329     60    446       C  
ATOM   4052  C   CYS B 184      67.155  10.049-162.232  1.00 26.58           C  
ANISOU 4052  C   CYS B 184     2947   3584   3569   -341     40    513       C  
ATOM   4053  O   CYS B 184      65.965  10.165-161.916  1.00 29.86           O  
ANISOU 4053  O   CYS B 184     3295   4079   3973   -307     89    590       O  
ATOM   4054  CB  CYS B 184      68.070   9.788-159.931  1.00 24.55           C  
ANISOU 4054  CB  CYS B 184     2863   3165   3299   -365     61    431       C  
ATOM   4055  SG  CYS B 184      68.169   7.988-160.125  1.00 28.70           S  
ANISOU 4055  SG  CYS B 184     3356   3718   3830   -481    -39    403       S  
ATOM   4056  N   VAL B 185      67.561   9.467-163.369  1.00 27.85           N  
ANISOU 4056  N   VAL B 185     3073   3774   3733   -395    -35    485       N  
ATOM   4057  CA  VAL B 185      66.610   8.912-164.337  1.00 28.11           C  
ANISOU 4057  CA  VAL B 185     2995   3937   3750   -432    -78    535       C  
ATOM   4058  C   VAL B 185      66.143   7.510-163.971  1.00 35.68           C  
ANISOU 4058  C   VAL B 185     3931   4923   4702   -542   -135    523       C  
ATOM   4059  O   VAL B 185      65.156   7.025-164.538  1.00 32.70           O  
ANISOU 4059  O   VAL B 185     3455   4661   4308   -594   -169    572       O  
ATOM   4060  CB  VAL B 185      67.271   8.926-165.736  1.00 28.84           C  
ANISOU 4060  CB  VAL B 185     3083   4041   3834   -441   -129    505       C  
ATOM   4061  CG1 VAL B 185      68.350   7.847-165.808  1.00 28.45           C  
ANISOU 4061  CG1 VAL B 185     3108   3914   3790   -521   -197    412       C  
ATOM   4062  CG2 VAL B 185      66.227   8.785-166.857  1.00 31.48           C  
ANISOU 4062  CG2 VAL B 185     3302   4525   4135   -454   -164    569       C  
ATOM   4063  N   GLY B 186      66.815   6.838-163.028  1.00 32.57           N  
ANISOU 4063  N   GLY B 186     3627   4429   4317   -584   -148    464       N  
ATOM   4064  CA  GLY B 186      66.428   5.485-162.630  1.00 32.56           C  
ANISOU 4064  CA  GLY B 186     3628   4433   4312   -688   -192    456       C  
ATOM   4065  C   GLY B 186      65.388   5.338-161.528  1.00 34.82           C  
ANISOU 4065  C   GLY B 186     3876   4758   4595   -698   -140    520       C  
ATOM   4066  O   GLY B 186      65.240   4.253-160.939  1.00 32.43           O  
ANISOU 4066  O   GLY B 186     3603   4428   4291   -782   -164    511       O  
ATOM   4067  N   ARG B 187      64.624   6.395-161.262  1.00 32.51           N  
ANISOU 4067  N   ARG B 187     3522   4531   4300   -609    -62    594       N  
ATOM   4068  CA  ARG B 187      63.783   6.414-160.066  1.00 32.03           C  
ANISOU 4068  CA  ARG B 187     3443   4495   4233   -588     12    656       C  
ATOM   4069  C   ARG B 187      62.526   5.552-160.160  1.00 38.52           C  
ANISOU 4069  C   ARG B 187     4142   5439   5054   -681     -5    730       C  
ATOM   4070  O   ARG B 187      61.860   5.376-159.134  1.00 38.59           O  
ANISOU 4070  O   ARG B 187     4135   5469   5059   -680     57    784       O  
ATOM   4071  CB  ARG B 187      63.387   7.854-159.719  1.00 29.61           C  
ANISOU 4071  CB  ARG B 187     3124   4207   3918   -445    118    714       C  
ATOM   4072  CG  ARG B 187      64.495   8.666-159.027  1.00 28.75           C  
ANISOU 4072  CG  ARG B 187     3166   3956   3802   -373    156    644       C  
ATOM   4073  CD  ARG B 187      63.995  10.055-158.721  1.00 28.31           C  
ANISOU 4073  CD  ARG B 187     3118   3906   3732   -235    270    701       C  
ATOM   4074  NE  ARG B 187      64.046  10.926-159.911  1.00 28.61           N  
ANISOU 4074  NE  ARG B 187     3112   3975   3782   -174    274    724       N  
ATOM   4075  CZ  ARG B 187      63.506  12.137-159.963  1.00 35.50           C  
ANISOU 4075  CZ  ARG B 187     3977   4866   4646    -44    374    790       C  
ATOM   4076  NH1 ARG B 187      62.843  12.614-158.905  1.00 30.59           N  
ANISOU 4076  NH1 ARG B 187     3386   4236   4000     42    482    839       N  
ATOM   4077  NH2 ARG B 187      63.631  12.877-161.072  1.00 31.28           N  
ANISOU 4077  NH2 ARG B 187     3413   4352   4120     10    374    813       N  
ATOM   4078  N   ILE B 188      62.182   4.982-161.324  1.00 30.94           N  
ANISOU 4078  N   ILE B 188     3099   4563   4093   -771    -86    735       N  
ATOM   4079  CA  ILE B 188      61.079   4.021-161.327  1.00 32.12           C  
ANISOU 4079  CA  ILE B 188     3144   4816   4242   -896   -115    794       C  
ATOM   4080  C   ILE B 188      61.341   2.917-160.298  1.00 35.61           C  
ANISOU 4080  C   ILE B 188     3686   5155   4691   -985   -117    758       C  
ATOM   4081  O   ILE B 188      60.405   2.321-159.757  1.00 38.94           O  
ANISOU 4081  O   ILE B 188     4040   5641   5116  -1062    -95    825       O  
ATOM   4082  CB  ILE B 188      60.860   3.437-162.744  1.00 36.67           C  
ANISOU 4082  CB  ILE B 188     3655   5474   4804  -1007   -222    777       C  
ATOM   4083  CG1 ILE B 188      59.542   2.665-162.819  1.00 37.19           C  
ANISOU 4083  CG1 ILE B 188     3583   5682   4867  -1143   -253    855       C  
ATOM   4084  CG2 ILE B 188      61.985   2.503-163.118  1.00 30.97           C  
ANISOU 4084  CG2 ILE B 188     3078   4613   4076  -1087   -299    658       C  
ATOM   4085  CD1 ILE B 188      58.323   3.535-162.968  1.00 42.25           C  
ANISOU 4085  CD1 ILE B 188     4032   6516   5505  -1071   -204    987       C  
ATOM   4086  N   GLN B 189      62.615   2.661-159.986  1.00 36.45           N  
ANISOU 4086  N   GLN B 189     3946   5106   4797   -968   -137    663       N  
ATOM   4087  CA  GLN B 189      63.062   1.632-159.051  1.00 35.89           C  
ANISOU 4087  CA  GLN B 189     3989   4922   4724  -1031   -143    627       C  
ATOM   4088  C   GLN B 189      63.035   2.058-157.578  1.00 32.80           C  
ANISOU 4088  C   GLN B 189     3649   4491   4324   -949    -52    660       C  
ATOM   4089  O   GLN B 189      63.438   1.252-156.728  1.00 32.80           O  
ANISOU 4089  O   GLN B 189     3749   4399   4315   -986    -54    638       O  
ATOM   4090  CB  GLN B 189      64.495   1.215-159.416  1.00 34.87           C  
ANISOU 4090  CB  GLN B 189     3993   4661   4595  -1029   -206    521       C  
ATOM   4091  CG  GLN B 189      64.618   0.418-160.715  1.00 37.13           C  
ANISOU 4091  CG  GLN B 189     4278   4951   4878  -1127   -292    474       C  
ATOM   4092  CD  GLN B 189      64.076  -0.988-160.564  1.00 48.57           C  
ANISOU 4092  CD  GLN B 189     5755   6377   6324  -1277   -324    480       C  
ATOM   4093  OE1 GLN B 189      64.179  -1.594-159.496  1.00 42.26           O  
ANISOU 4093  OE1 GLN B 189     5031   5500   5528  -1295   -294    490       O  
ATOM   4094  NE2 GLN B 189      63.490  -1.515-161.633  1.00 44.98           N  
ANISOU 4094  NE2 GLN B 189     5248   5987   5858  -1391   -387    476       N  
ATOM   4095  N   TRP B 190      62.556   3.265-157.243  1.00 32.04           N  
ANISOU 4095  N   TRP B 190     3498   4458   4220   -834     30    715       N  
ATOM   4096  CA  TRP B 190      62.872   3.850-155.927  1.00 33.79           C  
ANISOU 4096  CA  TRP B 190     3815   4609   4415   -735    111    714       C  
ATOM   4097  C   TRP B 190      62.370   3.005-154.754  1.00 34.89           C  
ANISOU 4097  C   TRP B 190     3983   4737   4537   -787    154    759       C  
ATOM   4098  O   TRP B 190      62.996   3.003-153.692  1.00 38.67           O  
ANISOU 4098  O   TRP B 190     4586   5123   4984   -744    179    727       O  
ATOM   4099  CB  TRP B 190      62.331   5.288-155.820  1.00 31.85           C  
ANISOU 4099  CB  TRP B 190     3519   4424   4158   -599    207    769       C  
ATOM   4100  CG  TRP B 190      60.830   5.408-155.691  1.00 32.28           C  
ANISOU 4100  CG  TRP B 190     3426   4624   4214   -584    284    892       C  
ATOM   4101  CD1 TRP B 190      59.930   5.557-156.712  1.00 37.40           C  
ANISOU 4101  CD1 TRP B 190     3909   5418   4884   -600    269    964       C  
ATOM   4102  CD2 TRP B 190      60.068   5.404-154.479  1.00 31.76           C  
ANISOU 4102  CD2 TRP B 190     3357   4587   4123   -545    389    966       C  
ATOM   4103  NE1 TRP B 190      58.651   5.629-156.205  1.00 36.24           N  
ANISOU 4103  NE1 TRP B 190     3640   5396   4733   -575    357   1083       N  
ATOM   4104  CE2 TRP B 190      58.709   5.540-154.837  1.00 34.51           C  
ANISOU 4104  CE2 TRP B 190     3520   5105   4487   -539    438   1087       C  
ATOM   4105  CE3 TRP B 190      60.400   5.287-153.119  1.00 35.42           C  
ANISOU 4105  CE3 TRP B 190     3953   4958   4546   -513    446    947       C  
ATOM   4106  CZ2 TRP B 190      57.686   5.577-153.895  1.00 39.43           C  
ANISOU 4106  CZ2 TRP B 190     4082   5808   5093   -496    553   1192       C  
ATOM   4107  CZ3 TRP B 190      59.370   5.314-152.171  1.00 45.29           C  
ANISOU 4107  CZ3 TRP B 190     5159   6279   5772   -471    561   1046       C  
ATOM   4108  CH2 TRP B 190      58.034   5.456-152.560  1.00 43.68           C  
ANISOU 4108  CH2 TRP B 190     4763   6242   5589   -461    619   1169       C  
ATOM   4109  N   GLY B 191      61.263   2.272-154.915  1.00 36.89           N  
ANISOU 4109  N   GLY B 191     4123   5086   4806   -884    158    836       N  
ATOM   4110  CA  GLY B 191      60.736   1.472-153.821  1.00 41.07           C  
ANISOU 4110  CA  GLY B 191     4675   5608   5322   -939    209    891       C  
ATOM   4111  C   GLY B 191      61.496   0.194-153.544  1.00 42.00           C  
ANISOU 4111  C   GLY B 191     4919   5601   5437  -1038    144    832       C  
ATOM   4112  O   GLY B 191      61.314  -0.402-152.478  1.00 41.83           O  
ANISOU 4112  O   GLY B 191     4958   5541   5394  -1061    191    869       O  
ATOM   4113  N   LYS B 192      62.352  -0.230-154.469  1.00 36.21           N  
ANISOU 4113  N   LYS B 192     4235   4801   4721  -1085     45    747       N  
ATOM   4114  CA  LYS B 192      63.142  -1.458-154.344  1.00 44.04           C  
ANISOU 4114  CA  LYS B 192     5355   5665   5711  -1161    -14    691       C  
ATOM   4115  C   LYS B 192      64.566  -1.040-153.994  1.00 46.92           C  
ANISOU 4115  C   LYS B 192     5845   5925   6055  -1052    -37    612       C  
ATOM   4116  O   LYS B 192      65.415  -0.838-154.865  1.00 40.47           O  
ANISOU 4116  O   LYS B 192     5047   5077   5252  -1030    -99    541       O  
ATOM   4117  CB  LYS B 192      63.099  -2.273-155.637  1.00 47.14           C  
ANISOU 4117  CB  LYS B 192     5724   6057   6130  -1285   -101    654       C  
ATOM   4118  CG  LYS B 192      61.778  -2.996-155.891  1.00 63.63           C  
ANISOU 4118  CG  LYS B 192     7709   8234   8235  -1438    -99    727       C  
ATOM   4119  CD  LYS B 192      61.434  -3.058-157.386  1.00 75.73           C  
ANISOU 4119  CD  LYS B 192     9151   9844   9778  -1525   -179    702       C  
ATOM   4120  CE  LYS B 192      60.515  -1.903-157.799  1.00 78.96           C  
ANISOU 4120  CE  LYS B 192     9375  10433  10193  -1470   -150    774       C  
ATOM   4121  NZ  LYS B 192      60.220  -1.873-159.265  1.00 79.57           N  
ANISOU 4121  NZ  LYS B 192     9363  10601  10270  -1540   -234    754       N  
ATOM   4122  N   LEU B 193      64.825  -0.884-152.703  1.00 36.23           N  
ANISOU 4122  N   LEU B 193     4574   4528   4663   -986     14    627       N  
ATOM   4123  CA  LEU B 193      66.125  -0.411-152.243  1.00 33.11           C  
ANISOU 4123  CA  LEU B 193     4285   4054   4240   -891    -11    560       C  
ATOM   4124  C   LEU B 193      66.444  -1.198-150.991  1.00 30.90           C  
ANISOU 4124  C   LEU B 193     4122   3701   3917   -890      3    578       C  
ATOM   4125  O   LEU B 193      65.627  -1.231-150.075  1.00 36.62           O  
ANISOU 4125  O   LEU B 193     4846   4457   4612   -890     79    646       O  
ATOM   4126  CB  LEU B 193      66.119   1.100-151.956  1.00 31.79           C  
ANISOU 4126  CB  LEU B 193     4099   3930   4052   -784     40    555       C  
ATOM   4127  CG  LEU B 193      67.388   1.727-151.367  1.00 31.25           C  
ANISOU 4127  CG  LEU B 193     4137   3791   3946   -704     14    487       C  
ATOM   4128  CD1 LEU B 193      68.564   1.562-152.328  1.00 27.73           C  
ANISOU 4128  CD1 LEU B 193     3701   3302   3535   -715    -79    413       C  
ATOM   4129  CD2 LEU B 193      67.188   3.228-150.986  1.00 32.39           C  
ANISOU 4129  CD2 LEU B 193     4285   3963   4060   -612     82    485       C  
ATOM   4130  N   GLN B 194      67.580  -1.874-150.985  1.00 28.15           N  
ANISOU 4130  N   GLN B 194     3868   3263   3563   -885    -63    528       N  
ATOM   4131  CA  GLN B 194      68.028  -2.605-149.808  1.00 32.06           C  
ANISOU 4131  CA  GLN B 194     4481   3689   4010   -866    -58    549       C  
ATOM   4132  C   GLN B 194      68.783  -1.632-148.919  1.00 35.77           C  
ANISOU 4132  C   GLN B 194     5007   4161   4422   -763    -58    519       C  
ATOM   4133  O   GLN B 194      69.765  -1.036-149.361  1.00 33.31           O  
ANISOU 4133  O   GLN B 194     4695   3842   4120   -719   -115    454       O  
ATOM   4134  CB  GLN B 194      68.922  -3.778-150.201  1.00 31.47           C  
ANISOU 4134  CB  GLN B 194     4484   3521   3952   -890   -125    518       C  
ATOM   4135  CG  GLN B 194      69.424  -4.562-148.993  1.00 38.52           C  
ANISOU 4135  CG  GLN B 194     5502   4343   4791   -855   -120    551       C  
ATOM   4136  CD  GLN B 194      68.286  -5.119-148.145  1.00 49.72           C  
ANISOU 4136  CD  GLN B 194     6941   5765   6186   -912    -40    638       C  
ATOM   4137  OE1 GLN B 194      67.284  -5.605-148.669  1.00 53.07           O  
ANISOU 4137  OE1 GLN B 194     7310   6204   6652  -1016    -10    673       O  
ATOM   4138  NE2 GLN B 194      68.436  -5.036-146.831  1.00 48.60           N  
ANISOU 4138  NE2 GLN B 194     6876   5616   5972   -850     -6    675       N  
ATOM   4139  N   VAL B 195      68.333  -1.473-147.670  1.00 31.63           N  
ANISOU 4139  N   VAL B 195     4535   3648   3834   -731      8    566       N  
ATOM   4140  CA  VAL B 195      68.914  -0.500-146.751  1.00 30.71           C  
ANISOU 4140  CA  VAL B 195     4487   3535   3645   -645     12    535       C  
ATOM   4141  C   VAL B 195      69.705  -1.279-145.710  1.00 34.40           C  
ANISOU 4141  C   VAL B 195     5075   3949   4047   -621    -25    545       C  
ATOM   4142  O   VAL B 195      69.132  -2.054-144.932  1.00 36.00           O  
ANISOU 4142  O   VAL B 195     5327   4136   4213   -637     26    614       O  
ATOM   4143  CB  VAL B 195      67.840   0.395-146.109  1.00 34.86           C  
ANISOU 4143  CB  VAL B 195     4998   4118   4130   -608    121    577       C  
ATOM   4144  CG1 VAL B 195      68.465   1.362-145.108  1.00 36.04           C  
ANISOU 4144  CG1 VAL B 195     5253   4252   4188   -529    125    533       C  
ATOM   4145  CG2 VAL B 195      67.067   1.187-147.205  1.00 32.46           C  
ANISOU 4145  CG2 VAL B 195     4563   3877   3892   -616    157    580       C  
ATOM   4146  N   PHE B 196      71.020  -1.089-145.688  1.00 32.03           N  
ANISOU 4146  N   PHE B 196     4815   3626   3727   -581   -114    485       N  
ATOM   4147  CA  PHE B 196      71.861  -1.690-144.656  1.00 32.02           C  
ANISOU 4147  CA  PHE B 196     4920   3595   3651   -541   -160    499       C  
ATOM   4148  C   PHE B 196      72.116  -0.663-143.554  1.00 36.15           C  
ANISOU 4148  C   PHE B 196     5514   4148   4073   -490   -155    473       C  
ATOM   4149  O   PHE B 196      72.659   0.419-143.808  1.00 33.30           O  
ANISOU 4149  O   PHE B 196     5135   3808   3711   -478   -192    405       O  
ATOM   4150  CB  PHE B 196      73.177  -2.200-145.243  1.00 29.97           C  
ANISOU 4150  CB  PHE B 196     4653   3307   3425   -524   -263    463       C  
ATOM   4151  CG  PHE B 196      73.002  -3.338-146.229  1.00 35.26           C  
ANISOU 4151  CG  PHE B 196     5294   3926   4175   -567   -264    484       C  
ATOM   4152  CD1 PHE B 196      72.619  -4.606-145.794  1.00 39.58           C  
ANISOU 4152  CD1 PHE B 196     5914   4415   4710   -585   -232    551       C  
ATOM   4153  CD2 PHE B 196      73.241  -3.142-147.584  1.00 36.48           C  
ANISOU 4153  CD2 PHE B 196     5366   4084   4411   -591   -295    434       C  
ATOM   4154  CE1 PHE B 196      72.473  -5.658-146.697  1.00 38.85           C  
ANISOU 4154  CE1 PHE B 196     5820   4257   4684   -634   -232    561       C  
ATOM   4155  CE2 PHE B 196      73.092  -4.192-148.490  1.00 35.18           C  
ANISOU 4155  CE2 PHE B 196     5196   3865   4304   -633   -296    443       C  
ATOM   4156  CZ  PHE B 196      72.711  -5.429-148.058  1.00 38.52           C  
ANISOU 4156  CZ  PHE B 196     5700   4221   4715   -659   -266    501       C  
ATOM   4157  N   ASP B 197      71.756  -1.020-142.328  1.00 34.86           N  
ANISOU 4157  N   ASP B 197     5445   3982   3818   -465   -110    527       N  
ATOM   4158  CA  ASP B 197      71.862  -0.105-141.194  1.00 31.67           C  
ANISOU 4158  CA  ASP B 197     5134   3602   3297   -419    -93    503       C  
ATOM   4159  C   ASP B 197      73.212  -0.348-140.534  1.00 33.61           C  
ANISOU 4159  C   ASP B 197     5454   3850   3467   -389   -209    479       C  
ATOM   4160  O   ASP B 197      73.387  -1.315-139.790  1.00 35.83           O  
ANISOU 4160  O   ASP B 197     5803   4119   3691   -364   -220    539       O  
ATOM   4161  CB  ASP B 197      70.697  -0.339-140.239  1.00 37.67           C  
ANISOU 4161  CB  ASP B 197     5954   4369   3990   -403     27    580       C  
ATOM   4162  CG  ASP B 197      70.681   0.636-139.069  1.00 45.68           C  
ANISOU 4162  CG  ASP B 197     7084   5403   4870   -348     63    552       C  
ATOM   4163  OD1 ASP B 197      71.575   1.513-138.992  1.00 39.46           O  
ANISOU 4163  OD1 ASP B 197     6335   4618   4040   -338    -14    467       O  
ATOM   4164  OD2 ASP B 197      69.765   0.513-138.232  1.00 45.78           O  
ANISOU 4164  OD2 ASP B 197     7154   5425   4814   -321    172    616       O  
ATOM   4165  N   ALA B 198      74.173   0.528-140.816  1.00 34.53           N  
ANISOU 4165  N   ALA B 198     5550   3987   3582   -392   -294    398       N  
ATOM   4166  CA  ALA B 198      75.487   0.500-140.187  1.00 36.48           C  
ANISOU 4166  CA  ALA B 198     5846   4263   3752   -372   -415    372       C  
ATOM   4167  C   ALA B 198      75.665   1.640-139.180  1.00 35.99           C  
ANISOU 4167  C   ALA B 198     5887   4225   3562   -370   -427    315       C  
ATOM   4168  O   ALA B 198      76.781   2.112-138.953  1.00 34.12           O  
ANISOU 4168  O   ALA B 198     5662   4024   3278   -386   -539    261       O  
ATOM   4169  CB  ALA B 198      76.598   0.531-141.235  1.00 31.92           C  
ANISOU 4169  CB  ALA B 198     5163   3700   3265   -391   -516    330       C  
ATOM   4170  N   ARG B 199      74.574   2.105-138.579  1.00 34.00           N  
ANISOU 4170  N   ARG B 199     5712   3956   3249   -354   -311    326       N  
ATOM   4171  CA  ARG B 199      74.695   3.232-137.655  1.00 36.22           C  
ANISOU 4171  CA  ARG B 199     6118   4244   3400   -350   -310    261       C  
ATOM   4172  C   ARG B 199      75.370   2.859-136.345  1.00 39.49           C  
ANISOU 4172  C   ARG B 199     6652   4694   3659   -327   -388    274       C  
ATOM   4173  O   ARG B 199      75.589   3.757-135.518  1.00 36.99           O  
ANISOU 4173  O   ARG B 199     6457   4384   3214   -334   -406    210       O  
ATOM   4174  CB  ARG B 199      73.325   3.839-137.357  1.00 35.46           C  
ANISOU 4174  CB  ARG B 199     6079   4121   3273   -316   -149    276       C  
ATOM   4175  CG  ARG B 199      72.681   4.529-138.562  1.00 33.37           C  
ANISOU 4175  CG  ARG B 199     5709   3835   3137   -330    -76    256       C  
ATOM   4176  CD  ARG B 199      71.286   4.971-138.197  1.00 36.65           C  
ANISOU 4176  CD  ARG B 199     6165   4241   3519   -277     91    297       C  
ATOM   4177  NE  ARG B 199      70.412   3.827-137.979  1.00 36.20           N  
ANISOU 4177  NE  ARG B 199     6067   4205   3480   -261    166    406       N  
ATOM   4178  CZ  ARG B 199      69.279   3.876-137.293  1.00 39.11           C  
ANISOU 4178  CZ  ARG B 199     6484   4586   3790   -210    308    470       C  
ATOM   4179  NH1 ARG B 199      68.883   5.012-136.738  1.00 45.88           N  
ANISOU 4179  NH1 ARG B 199     7444   5431   4559   -153    396    432       N  
ATOM   4180  NH2 ARG B 199      68.540   2.785-137.157  1.00 38.65           N  
ANISOU 4180  NH2 ARG B 199     6376   4549   3759   -216    370    574       N  
ATOM   4181  N   ASP B 200      75.694   1.583-136.144  1.00 40.33           N  
ANISOU 4181  N   ASP B 200     6738   4818   3767   -300   -432    353       N  
ATOM   4182  CA  ASP B 200      76.470   1.130-134.993  1.00 50.19           C  
ANISOU 4182  CA  ASP B 200     8082   6115   4873   -269   -524    378       C  
ATOM   4183  C   ASP B 200      77.953   1.019-135.303  1.00 49.66           C  
ANISOU 4183  C   ASP B 200     7940   6105   4825   -288   -693    350       C  
ATOM   4184  O   ASP B 200      78.726   0.602-134.441  1.00 46.77           O  
ANISOU 4184  O   ASP B 200     7626   5798   4346   -259   -790    380       O  
ATOM   4185  CB  ASP B 200      75.958  -0.228-134.499  1.00 50.82           C  
ANISOU 4185  CB  ASP B 200     8198   6179   4932   -213   -463    498       C  
ATOM   4186  CG  ASP B 200      74.833  -0.095-133.492  1.00 73.62           C  
ANISOU 4186  CG  ASP B 200    11213   9051   7709   -181   -330    536       C  
ATOM   4187  OD1 ASP B 200      74.766   0.949-132.806  1.00 81.96           O  
ANISOU 4187  OD1 ASP B 200    12372  10122   8646   -181   -318    469       O  
ATOM   4188  OD2 ASP B 200      74.027  -1.043-133.377  1.00 85.62           O  
ANISOU 4188  OD2 ASP B 200    12736  10540   9254   -157   -232    634       O  
ATOM   4189  N   CYS B 201      78.363   1.367-136.516  1.00 41.93           N  
ANISOU 4189  N   CYS B 201     6830   5119   3982   -331   -728    304       N  
ATOM   4190  CA  CYS B 201      79.761   1.247-136.901  1.00 34.44           C  
ANISOU 4190  CA  CYS B 201     5786   4235   3066   -346   -876    289       C  
ATOM   4191  C   CYS B 201      80.651   2.056-135.972  1.00 46.54           C  
ANISOU 4191  C   CYS B 201     7386   5842   4456   -387   -996    229       C  
ATOM   4192  O   CYS B 201      80.308   3.169-135.562  1.00 42.71           O  
ANISOU 4192  O   CYS B 201     6996   5334   3898   -438   -968    150       O  
ATOM   4193  CB  CYS B 201      79.943   1.713-138.361  1.00 34.21           C  
ANISOU 4193  CB  CYS B 201     5617   4183   3197   -393   -873    240       C  
ATOM   4194  SG  CYS B 201      81.566   1.396-139.028  1.00 44.08           S  
ANISOU 4194  SG  CYS B 201     6721   5515   4515   -395  -1024    245       S  
ATOM   4195  N   ARG B 202      81.802   1.478-135.628  1.00 49.66           N  
ANISOU 4195  N   ARG B 202     7737   6326   4806   -363  -1132    269       N  
ATOM   4196  CA  ARG B 202      82.659   2.014-134.583  1.00 58.69           C  
ANISOU 4196  CA  ARG B 202     8945   7562   5790   -402  -1265    232       C  
ATOM   4197  C   ARG B 202      84.021   2.476-135.064  1.00 52.23           C  
ANISOU 4197  C   ARG B 202     7993   6839   5013   -469  -1417    192       C  
ATOM   4198  O   ARG B 202      84.653   3.293-134.381  1.00 53.47           O  
ANISOU 4198  O   ARG B 202     8200   7064   5053   -550  -1526    128       O  
ATOM   4199  CB  ARG B 202      82.881   0.960-133.483  1.00 64.64           C  
ANISOU 4199  CB  ARG B 202     9771   8376   6415   -312  -1310    331       C  
ATOM   4200  CG  ARG B 202      83.296   1.543-132.166  1.00 84.40           C  
ANISOU 4200  CG  ARG B 202    12401  10957   8709   -348  -1409    292       C  
ATOM   4201  CD  ARG B 202      82.076   1.903-131.346  1.00 96.45           C  
ANISOU 4201  CD  ARG B 202    14118  12404  10122   -337  -1278    268       C  
ATOM   4202  NE  ARG B 202      81.849   0.939-130.271  1.00104.94           N  
ANISOU 4202  NE  ARG B 202    15299  13508  11065   -242  -1263    369       N  
ATOM   4203  CZ  ARG B 202      81.285  -0.255-130.430  1.00101.77           C  
ANISOU 4203  CZ  ARG B 202    14881  13058  10730   -150  -1167    482       C  
ATOM   4204  NH1 ARG B 202      80.882  -0.660-131.626  1.00 97.76           N  
ANISOU 4204  NH1 ARG B 202    14255  12474  10415   -145  -1084    503       N  
ATOM   4205  NH2 ARG B 202      81.124  -1.051-129.382  1.00103.75           N  
ANISOU 4205  NH2 ARG B 202    15242  13332  10846    -70  -1154    575       N  
ATOM   4206  N   SER B 203      84.500   1.973-136.192  1.00 42.09           N  
ANISOU 4206  N   SER B 203     6544   5564   3883   -444  -1427    230       N  
ATOM   4207  CA  SER B 203      85.879   2.179-136.598  1.00 38.18           C  
ANISOU 4207  CA  SER B 203     5899   5182   3426   -485  -1570    224       C  
ATOM   4208  C   SER B 203      85.936   2.213-138.110  1.00 38.84           C  
ANISOU 4208  C   SER B 203     5839   5220   3699   -492  -1515    215       C  
ATOM   4209  O   SER B 203      84.974   1.847-138.799  1.00 43.01           O  
ANISOU 4209  O   SER B 203     6380   5641   4320   -451  -1382    227       O  
ATOM   4210  CB  SER B 203      86.778   1.057-136.092  1.00 44.29           C  
ANISOU 4210  CB  SER B 203     6613   6068   4146   -386  -1672    334       C  
ATOM   4211  OG  SER B 203      86.435  -0.131-136.783  1.00 39.19           O  
ANISOU 4211  OG  SER B 203     5923   5357   3610   -271  -1580    420       O  
ATOM   4212  N   ALA B 204      87.093   2.627-138.634  1.00 36.18           N  
ANISOU 4212  N   ALA B 204     5357   4976   3414   -547  -1620    198       N  
ATOM   4213  CA  ALA B 204      87.274   2.520-140.081  1.00 38.19           C  
ANISOU 4213  CA  ALA B 204     5469   5202   3840   -534  -1570    205       C  
ATOM   4214  C   ALA B 204      87.371   1.059-140.508  1.00 39.58           C  
ANISOU 4214  C   ALA B 204     5584   5374   4080   -391  -1534    311       C  
ATOM   4215  O   ALA B 204      86.994   0.710-141.628  1.00 38.65           O  
ANISOU 4215  O   ALA B 204     5417   5181   4088   -356  -1442    318       O  
ATOM   4216  CB  ALA B 204      88.519   3.295-140.511  1.00 46.08           C  
ANISOU 4216  CB  ALA B 204     6321   6309   4877   -627  -1683    173       C  
ATOM   4217  N   GLN B 205      87.873   0.185-139.629  1.00 42.31           N  
ANISOU 4217  N   GLN B 205     5946   5795   4334   -304  -1605    395       N  
ATOM   4218  CA  GLN B 205      87.993  -1.225-140.004  1.00 31.76           C  
ANISOU 4218  CA  GLN B 205     4575   4437   3054   -158  -1562    499       C  
ATOM   4219  C   GLN B 205      86.621  -1.873-140.145  1.00 37.50           C  
ANISOU 4219  C   GLN B 205     5431   5008   3810   -118  -1414    510       C  
ATOM   4220  O   GLN B 205      86.379  -2.625-141.094  1.00 39.28           O  
ANISOU 4220  O   GLN B 205     5626   5156   4143    -59  -1333    541       O  
ATOM   4221  CB  GLN B 205      88.854  -1.972-138.975  1.00 36.88           C  
ANISOU 4221  CB  GLN B 205     5218   5205   3588    -65  -1671    597       C  
ATOM   4222  CG  GLN B 205      90.333  -1.640-139.081  1.00 40.69           C  
ANISOU 4222  CG  GLN B 205     5522   5864   4073    -78  -1816    619       C  
ATOM   4223  CD  GLN B 205      91.140  -2.141-137.897  1.00 51.97           C  
ANISOU 4223  CD  GLN B 205     6946   7440   5361     -7  -1945    709       C  
ATOM   4224  OE1 GLN B 205      90.654  -2.176-136.759  1.00 54.19           O  
ANISOU 4224  OE1 GLN B 205     7373   7712   5503    -12  -1962    711       O  
ATOM   4225  NE2 GLN B 205      92.392  -2.520-138.156  1.00 48.49           N  
ANISOU 4225  NE2 GLN B 205     6329   7145   4949     67  -2036    792       N  
ATOM   4226  N   GLU B 206      85.709  -1.593-139.213  1.00 40.77           N  
ANISOU 4226  N   GLU B 206     5990   5376   4124   -155  -1375    487       N  
ATOM   4227  CA  GLU B 206      84.347  -2.089-139.360  1.00 41.00           C  
ANISOU 4227  CA  GLU B 206     6121   5269   4186   -139  -1230    499       C  
ATOM   4228  C   GLU B 206      83.672  -1.464-140.580  1.00 41.99           C  
ANISOU 4228  C   GLU B 206     6196   5318   4439   -209  -1144    426       C  
ATOM   4229  O   GLU B 206      82.945  -2.143-141.320  1.00 38.56           O  
ANISOU 4229  O   GLU B 206     5765   4792   4092   -184  -1046    450       O  
ATOM   4230  CB  GLU B 206      83.553  -1.798-138.092  1.00 45.91           C  
ANISOU 4230  CB  GLU B 206     6898   5877   4670   -161  -1201    491       C  
ATOM   4231  CG  GLU B 206      82.287  -2.620-137.896  1.00 60.25           C  
ANISOU 4231  CG  GLU B 206     8821   7583   6489   -122  -1065    546       C  
ATOM   4232  CD  GLU B 206      81.801  -2.586-136.442  1.00 74.44           C  
ANISOU 4232  CD  GLU B 206    10768   9393   8121   -109  -1052    572       C  
ATOM   4233  OE1 GLU B 206      81.879  -3.634-135.753  1.00 77.21           O  
ANISOU 4233  OE1 GLU B 206    11186   9743   8406    -25  -1052    669       O  
ATOM   4234  OE2 GLU B 206      81.362  -1.509-135.980  1.00 70.55           O  
ANISOU 4234  OE2 GLU B 206    10339   8908   7561   -175  -1036    498       O  
ATOM   4235  N   MET B 207      83.918  -0.172-140.814  1.00 39.32           N  
ANISOU 4235  N   MET B 207     5814   5016   4110   -301  -1181    339       N  
ATOM   4236  CA  MET B 207      83.381   0.483-142.008  1.00 36.60           C  
ANISOU 4236  CA  MET B 207     5413   4609   3883   -358  -1105    278       C  
ATOM   4237  C   MET B 207      83.766  -0.281-143.270  1.00 35.08           C  
ANISOU 4237  C   MET B 207     5110   4402   3818   -308  -1088    312       C  
ATOM   4238  O   MET B 207      82.918  -0.565-144.120  1.00 33.07           O  
ANISOU 4238  O   MET B 207     4855   4064   3645   -308   -992    308       O  
ATOM   4239  CB  MET B 207      83.877   1.932-142.057  1.00 38.76           C  
ANISOU 4239  CB  MET B 207     5655   4927   4143   -459  -1163    190       C  
ATOM   4240  CG  MET B 207      83.303   2.774-143.192  1.00 49.28           C  
ANISOU 4240  CG  MET B 207     6947   6196   5582   -515  -1082    130       C  
ATOM   4241  SD  MET B 207      83.887   4.488-143.045  1.00 52.57           S  
ANISOU 4241  SD  MET B 207     7367   6643   5964   -639  -1144     31       S  
ATOM   4242  CE  MET B 207      82.461   5.384-143.632  1.00 36.42           C  
ANISOU 4242  CE  MET B 207     5389   4481   3968   -665   -994    -20       C  
ATOM   4243  N   PHE B 208      85.040  -0.649-143.394  1.00 36.43           N  
ANISOU 4243  N   PHE B 208     5185   4657   3998   -261  -1180    349       N  
ATOM   4244  CA  PHE B 208      85.493  -1.425-144.547  1.00 36.80           C  
ANISOU 4244  CA  PHE B 208     5140   4690   4153   -193  -1157    386       C  
ATOM   4245  C   PHE B 208      84.693  -2.715-144.721  1.00 38.81           C  
ANISOU 4245  C   PHE B 208     5480   4836   4430   -119  -1065    440       C  
ATOM   4246  O   PHE B 208      84.314  -3.081-145.841  1.00 32.14           O  
ANISOU 4246  O   PHE B 208     4614   3920   3678   -112   -994    430       O  
ATOM   4247  CB  PHE B 208      86.985  -1.728-144.385  1.00 38.48           C  
ANISOU 4247  CB  PHE B 208     5245   5026   4349   -129  -1266    440       C  
ATOM   4248  CG  PHE B 208      87.539  -2.678-145.412  1.00 42.55           C  
ANISOU 4248  CG  PHE B 208     5684   5528   4956    -24  -1234    494       C  
ATOM   4249  CD1 PHE B 208      87.676  -2.294-146.738  1.00 46.44           C  
ANISOU 4249  CD1 PHE B 208     6084   6005   5555    -51  -1193    452       C  
ATOM   4250  CD2 PHE B 208      87.950  -3.947-145.040  1.00 51.95           C  
ANISOU 4250  CD2 PHE B 208     6903   6719   6115    110  -1240    589       C  
ATOM   4251  CE1 PHE B 208      88.202  -3.163-147.675  1.00 50.64           C  
ANISOU 4251  CE1 PHE B 208     6560   6523   6157     54  -1156    498       C  
ATOM   4252  CE2 PHE B 208      88.471  -4.817-145.974  1.00 49.58           C  
ANISOU 4252  CE2 PHE B 208     6552   6395   5890    219  -1199    636       C  
ATOM   4253  CZ  PHE B 208      88.605  -4.422-147.284  1.00 42.50           C  
ANISOU 4253  CZ  PHE B 208     5568   5485   5095    191  -1157    588       C  
ATOM   4254  N   THR B 209      84.446  -3.432-143.617  1.00 37.74           N  
ANISOU 4254  N   THR B 209     5448   4687   4203    -69  -1067    501       N  
ATOM   4255  CA  THR B 209      83.717  -4.696-143.689  1.00 31.71           C  
ANISOU 4255  CA  THR B 209     4779   3812   3456    -11   -979    560       C  
ATOM   4256  C   THR B 209      82.284  -4.484-144.161  1.00 28.55           C  
ANISOU 4256  C   THR B 209     4429   3315   3104    -95   -873    516       C  
ATOM   4257  O   THR B 209      81.781  -5.235-145.013  1.00 33.45           O  
ANISOU 4257  O   THR B 209     5066   3846   3799    -89   -802    526       O  
ATOM   4258  CB  THR B 209      83.751  -5.383-142.315  1.00 35.11           C  
ANISOU 4258  CB  THR B 209     5316   4254   3770     54  -1002    639       C  
ATOM   4259  OG1 THR B 209      85.113  -5.469-141.879  1.00 37.38           O  
ANISOU 4259  OG1 THR B 209     5535   4660   4007    130  -1116    684       O  
ATOM   4260  CG2 THR B 209      83.143  -6.794-142.394  1.00 31.52           C  
ANISOU 4260  CG2 THR B 209     4966   3675   3336    116   -912    713       C  
ATOM   4261  N   TYR B 210      81.637  -3.427-143.665  1.00 30.33           N  
ANISOU 4261  N   TYR B 210     4677   3562   3286   -174   -861    465       N  
ATOM   4262  CA  TYR B 210      80.301  -3.067-144.133  1.00 32.11           C  
ANISOU 4262  CA  TYR B 210     4922   3721   3558   -246   -761    430       C  
ATOM   4263  C   TYR B 210      80.299  -2.743-145.619  1.00 31.22           C  
ANISOU 4263  C   TYR B 210     4711   3592   3560   -280   -741    380       C  
ATOM   4264  O   TYR B 210      79.354  -3.092-146.336  1.00 31.57           O  
ANISOU 4264  O   TYR B 210     4760   3572   3664   -313   -665    380       O  
ATOM   4265  CB  TYR B 210      79.792  -1.851-143.375  1.00 29.37           C  
ANISOU 4265  CB  TYR B 210     4612   3408   3141   -302   -752    384       C  
ATOM   4266  CG  TYR B 210      79.119  -2.148-142.051  1.00 30.33           C  
ANISOU 4266  CG  TYR B 210     4856   3516   3152   -287   -713    430       C  
ATOM   4267  CD1 TYR B 210      77.929  -2.874-142.006  1.00 33.97           C  
ANISOU 4267  CD1 TYR B 210     5371   3908   3630   -293   -609    480       C  
ATOM   4268  CD2 TYR B 210      79.645  -1.669-140.875  1.00 35.03           C  
ANISOU 4268  CD2 TYR B 210     5512   4174   3625   -275   -779    423       C  
ATOM   4269  CE1 TYR B 210      77.291  -3.123-140.820  1.00 40.39           C  
ANISOU 4269  CE1 TYR B 210     6291   4711   4343   -279   -560    530       C  
ATOM   4270  CE2 TYR B 210      79.014  -1.915-139.658  1.00 38.14           C  
ANISOU 4270  CE2 TYR B 210     6027   4558   3907   -254   -735    466       C  
ATOM   4271  CZ  TYR B 210      77.840  -2.643-139.644  1.00 39.96           C  
ANISOU 4271  CZ  TYR B 210     6305   4718   4161   -251   -620    523       C  
ATOM   4272  OH  TYR B 210      77.197  -2.893-138.458  1.00 49.85           O  
ANISOU 4272  OH  TYR B 210     7674   5963   5304   -229   -565    575       O  
ATOM   4273  N   ILE B 211      81.336  -2.044-146.084  1.00 28.67           N  
ANISOU 4273  N   ILE B 211     4295   3335   3263   -281   -811    341       N  
ATOM   4274  CA  ILE B 211      81.395  -1.646-147.500  1.00 28.20           C  
ANISOU 4274  CA  ILE B 211     4142   3267   3304   -309   -790    296       C  
ATOM   4275  C   ILE B 211      81.606  -2.866-148.382  1.00 35.22           C  
ANISOU 4275  C   ILE B 211     5022   4104   4254   -251   -766    330       C  
ATOM   4276  O   ILE B 211      80.958  -3.017-149.427  1.00 33.97           O  
ANISOU 4276  O   ILE B 211     4852   3894   4161   -281   -708    308       O  
ATOM   4277  CB  ILE B 211      82.496  -0.588-147.692  1.00 26.48           C  
ANISOU 4277  CB  ILE B 211     3832   3134   3096   -331   -865    254       C  
ATOM   4278  CG1 ILE B 211      82.022   0.750-147.113  1.00 33.66           C  
ANISOU 4278  CG1 ILE B 211     4774   4058   3958   -409   -861    199       C  
ATOM   4279  CG2 ILE B 211      82.880  -0.419-149.197  1.00 29.86           C  
ANISOU 4279  CG2 ILE B 211     4157   3564   3626   -333   -849    228       C  
ATOM   4280  CD1 ILE B 211      83.114   1.837-147.022  1.00 36.17           C  
ANISOU 4280  CD1 ILE B 211     5027   4451   4263   -457   -945    156       C  
ATOM   4281  N   CYS B 212      82.488  -3.774-147.960  1.00 32.68           N  
ANISOU 4281  N   CYS B 212     4718   3794   3904   -163   -809    387       N  
ATOM   4282  CA  CYS B 212      82.699  -5.010-148.712  1.00 32.52           C  
ANISOU 4282  CA  CYS B 212     4722   3705   3930    -91   -774    422       C  
ATOM   4283  C   CYS B 212      81.407  -5.799-148.852  1.00 34.06           C  
ANISOU 4283  C   CYS B 212     5021   3784   4136   -133   -690    433       C  
ATOM   4284  O   CYS B 212      81.111  -6.333-149.928  1.00 35.81           O  
ANISOU 4284  O   CYS B 212     5254   3937   4417   -143   -643    415       O  
ATOM   4285  CB  CYS B 212      83.784  -5.854-148.041  1.00 38.28           C  
ANISOU 4285  CB  CYS B 212     5468   4464   4614     28   -825    498       C  
ATOM   4286  SG  CYS B 212      85.427  -5.170-148.334  1.00 44.67           S  
ANISOU 4286  SG  CYS B 212     6113   5418   5440     80   -918    497       S  
ATOM   4287  N   ASN B 213      80.621  -5.889-147.776  1.00 34.55           N  
ANISOU 4287  N   ASN B 213     5164   3827   4138   -164   -668    462       N  
ATOM   4288  CA AASN B 213      79.385  -6.645-147.901  0.53 32.10           C  
ANISOU 4288  CA AASN B 213     4938   3417   3842   -219   -587    481       C  
ATOM   4289  CA BASN B 213      79.344  -6.602-147.823  0.47 32.98           C  
ANISOU 4289  CA BASN B 213     5052   3531   3950   -222   -587    481       C  
ATOM   4290  C   ASN B 213      78.357  -5.903-148.748  1.00 34.46           C  
ANISOU 4290  C   ASN B 213     5180   3719   4195   -323   -543    423       C  
ATOM   4291  O   ASN B 213      77.599  -6.555-149.484  1.00 32.65           O  
ANISOU 4291  O   ASN B 213     4979   3418   4009   -375   -493    421       O  
ATOM   4292  CB AASN B 213      78.862  -7.013-146.515  0.53 36.81           C  
ANISOU 4292  CB AASN B 213     5633   3997   4358   -216   -565    542       C  
ATOM   4293  CB BASN B 213      78.750  -6.715-146.414  0.47 34.26           C  
ANISOU 4293  CB BASN B 213     5298   3692   4028   -231   -567    533       C  
ATOM   4294  CG AASN B 213      79.591  -8.218-145.949  0.53 40.54           C  
ANISOU 4294  CG AASN B 213     6193   4422   4790   -112   -580    619       C  
ATOM   4295  CG BASN B 213      77.264  -7.038-146.438  0.47 36.32           C  
ANISOU 4295  CG BASN B 213     5608   3887   4304   -322   -478    548       C  
ATOM   4296  OD1AASN B 213      80.550  -8.081-145.177  0.53 36.60           O  
ANISOU 4296  OD1AASN B 213     5683   3995   4228    -31   -648    650       O  
ATOM   4297  OD1BASN B 213      76.875  -8.200-146.516  0.47 32.35           O  
ANISOU 4297  OD1BASN B 213     5188   3289   3814   -331   -433    593       O  
ATOM   4298  ND2AASN B 213      79.189  -9.408-146.393  0.53 42.63           N  
ANISOU 4298  ND2AASN B 213     6545   4565   5088   -113   -520    651       N  
ATOM   4299  ND2BASN B 213      76.429  -6.005-146.393  0.47 41.38           N  
ANISOU 4299  ND2BASN B 213     6197   4579   4946   -391   -450    515       N  
ATOM   4300  N   HIS B 214      78.339  -4.565-148.705  1.00 30.66           N  
ANISOU 4300  N   HIS B 214     4622   3319   3711   -355   -564    378       N  
ATOM   4301  CA  HIS B 214      77.518  -3.813-149.650  1.00 32.83           C  
ANISOU 4301  CA  HIS B 214     4829   3604   4039   -429   -525    331       C  
ATOM   4302  C   HIS B 214      77.871  -4.185-151.091  1.00 35.49           C  
ANISOU 4302  C   HIS B 214     5123   3915   4446   -425   -529    300       C  
ATOM   4303  O   HIS B 214      76.988  -4.513-151.886  1.00 28.05           O  
ANISOU 4303  O   HIS B 214     4182   2936   3541   -485   -487    291       O  
ATOM   4304  CB  HIS B 214      77.698  -2.306-149.441  1.00 30.81           C  
ANISOU 4304  CB  HIS B 214     4512   3425   3769   -444   -547    287       C  
ATOM   4305  CG  HIS B 214      76.890  -1.452-150.375  1.00 34.33           C  
ANISOU 4305  CG  HIS B 214     4891   3886   4265   -500   -503    250       C  
ATOM   4306  ND1 HIS B 214      76.100  -0.412-149.933  1.00 33.03           N  
ANISOU 4306  ND1 HIS B 214     4723   3751   4077   -529   -462    241       N  
ATOM   4307  CD2 HIS B 214      76.776  -1.458-151.730  1.00 35.07           C  
ANISOU 4307  CD2 HIS B 214     4923   3975   4426   -521   -493    225       C  
ATOM   4308  CE1 HIS B 214      75.517   0.172-150.970  1.00 31.63           C  
ANISOU 4308  CE1 HIS B 214     4476   3588   3952   -561   -428    219       C  
ATOM   4309  NE2 HIS B 214      75.909  -0.447-152.073  1.00 32.86           N  
ANISOU 4309  NE2 HIS B 214     4595   3727   4161   -562   -451    208       N  
ATOM   4310  N   ILE B 215      79.161  -4.130-151.438  1.00 31.74           N  
ANISOU 4310  N   ILE B 215     4606   3470   3985   -357   -580    288       N  
ATOM   4311  CA  ILE B 215      79.594  -4.410-152.812  1.00 32.67           C  
ANISOU 4311  CA  ILE B 215     4685   3568   4159   -339   -576    259       C  
ATOM   4312  C   ILE B 215      79.211  -5.821-153.219  1.00 32.82           C  
ANISOU 4312  C   ILE B 215     4801   3482   4187   -334   -537    278       C  
ATOM   4313  O   ILE B 215      78.743  -6.057-154.347  1.00 30.32           O  
ANISOU 4313  O   ILE B 215     4486   3129   3905   -378   -509    245       O  
ATOM   4314  CB  ILE B 215      81.112  -4.181-152.963  1.00 33.82           C  
ANISOU 4314  CB  ILE B 215     4763   3773   4313   -254   -630    260       C  
ATOM   4315  CG1 ILE B 215      81.475  -2.694-152.774  1.00 32.47           C  
ANISOU 4315  CG1 ILE B 215     4497   3696   4143   -289   -668    228       C  
ATOM   4316  CG2 ILE B 215      81.601  -4.657-154.344  1.00 34.63           C  
ANISOU 4316  CG2 ILE B 215     4844   3848   4465   -212   -609    240       C  
ATOM   4317  CD1 ILE B 215      82.979  -2.431-152.792  1.00 31.05           C  
ANISOU 4317  CD1 ILE B 215     4234   3593   3969   -227   -729    238       C  
ATOM   4318  N   LYS B 216      79.377  -6.784-152.303  1.00 31.30           N  
ANISOU 4318  N   LYS B 216     4703   3235   3955   -286   -534    333       N  
ATOM   4319  CA  LYS B 216      79.064  -8.173-152.620  1.00 32.44           C  
ANISOU 4319  CA  LYS B 216     4966   3257   4103   -283   -491    354       C  
ATOM   4320  C   LYS B 216      77.568  -8.357-152.838  1.00 34.83           C  
ANISOU 4320  C   LYS B 216     5305   3512   4417   -416   -445    343       C  
ATOM   4321  O   LYS B 216      77.142  -8.990-153.815  1.00 34.64           O  
ANISOU 4321  O   LYS B 216     5326   3416   4419   -469   -419    315       O  
ATOM   4322  CB  LYS B 216      79.566  -9.090-151.495  1.00 35.75           C  
ANISOU 4322  CB  LYS B 216     5482   3627   4473   -196   -494    428       C  
ATOM   4323  CG  LYS B 216      79.518 -10.566-151.808  1.00 46.23           C  
ANISOU 4323  CG  LYS B 216     6953   4810   5803   -165   -445    455       C  
ATOM   4324  CD  LYS B 216      80.636 -11.280-151.037  1.00 57.91           C  
ANISOU 4324  CD  LYS B 216     8490   6271   7242    -11   -460    528       C  
ATOM   4325  CE  LYS B 216      80.265 -12.704-150.657  1.00 68.39           C  
ANISOU 4325  CE  LYS B 216     9997   7441   8546      6   -401    586       C  
ATOM   4326  NZ  LYS B 216      79.806 -13.515-151.814  1.00 69.91           N  
ANISOU 4326  NZ  LYS B 216    10289   7497   8776    -50   -345    540       N  
ATOM   4327  N   TYR B 217      76.756  -7.801-151.936  1.00 32.10           N  
ANISOU 4327  N   TYR B 217     4938   3213   4047   -474   -434    367       N  
ATOM   4328  CA  TYR B 217      75.309  -7.902-152.083  1.00 27.58           C  
ANISOU 4328  CA  TYR B 217     4369   2622   3487   -599   -388    372       C  
ATOM   4329  C   TYR B 217      74.844  -7.242-153.379  1.00 26.47           C  
ANISOU 4329  C   TYR B 217     4135   2529   3392   -665   -392    313       C  
ATOM   4330  O   TYR B 217      74.071  -7.827-154.150  1.00 33.59           O  
ANISOU 4330  O   TYR B 217     5060   3387   4314   -756   -372    300       O  
ATOM   4331  CB  TYR B 217      74.608  -7.238-150.909  1.00 27.90           C  
ANISOU 4331  CB  TYR B 217     4386   2724   3490   -624   -366    410       C  
ATOM   4332  CG  TYR B 217      73.105  -7.246-151.063  1.00 31.36           C  
ANISOU 4332  CG  TYR B 217     4799   3172   3946   -746   -313    428       C  
ATOM   4333  CD1 TYR B 217      72.356  -8.319-150.605  1.00 38.48           C  
ANISOU 4333  CD1 TYR B 217     5787   3998   4838   -812   -268    484       C  
ATOM   4334  CD2 TYR B 217      72.439  -6.197-151.719  1.00 31.39           C  
ANISOU 4334  CD2 TYR B 217     4685   3263   3979   -795   -307    397       C  
ATOM   4335  CE1 TYR B 217      70.984  -8.349-150.754  1.00 42.93           C  
ANISOU 4335  CE1 TYR B 217     6306   4586   5420   -935   -222    509       C  
ATOM   4336  CE2 TYR B 217      71.059  -6.225-151.873  1.00 34.17           C  
ANISOU 4336  CE2 TYR B 217     4993   3645   4347   -900   -261    427       C  
ATOM   4337  CZ  TYR B 217      70.343  -7.303-151.382  1.00 38.66           C  
ANISOU 4337  CZ  TYR B 217     5633   4150   4906   -974   -221    483       C  
ATOM   4338  OH  TYR B 217      68.976  -7.348-151.512  1.00 43.93           O  
ANISOU 4338  OH  TYR B 217     6237   4862   5591  -1090   -178    522       O  
ATOM   4339  N   ALA B 218      75.249  -5.995-153.587  1.00 27.49           N  
ANISOU 4339  N   ALA B 218     4162   2752   3531   -630   -417    282       N  
ATOM   4340  CA  ALA B 218      74.737  -5.224-154.719  1.00 27.81           C  
ANISOU 4340  CA  ALA B 218     4110   2850   3607   -684   -416    239       C  
ATOM   4341  C   ALA B 218      75.189  -5.818-156.047  1.00 33.82           C  
ANISOU 4341  C   ALA B 218     4892   3566   4393   -680   -430    196       C  
ATOM   4342  O   ALA B 218      74.435  -5.812-157.031  1.00 32.00           O  
ANISOU 4342  O   ALA B 218     4633   3348   4179   -757   -423    171       O  
ATOM   4343  CB  ALA B 218      75.194  -3.773-154.608  1.00 23.77           C  
ANISOU 4343  CB  ALA B 218     3505   2427   3098   -640   -433    218       C  
ATOM   4344  N   THR B 219      76.425  -6.303-156.107  1.00 31.61           N  
ANISOU 4344  N   THR B 219     4657   3244   4109   -584   -448    190       N  
ATOM   4345  CA  THR B 219      76.923  -6.864-157.359  1.00 34.62           C  
ANISOU 4345  CA  THR B 219     5071   3578   4505   -560   -448    149       C  
ATOM   4346  C   THR B 219      76.202  -8.164-157.696  1.00 36.14           C  
ANISOU 4346  C   THR B 219     5388   3658   4687   -634   -422    145       C  
ATOM   4347  O   THR B 219      75.730  -8.350-158.829  1.00 30.41           O  
ANISOU 4347  O   THR B 219     4673   2917   3965   -702   -420    101       O  
ATOM   4348  CB  THR B 219      78.433  -7.083-157.270  1.00 32.76           C  
ANISOU 4348  CB  THR B 219     4845   3333   4267   -423   -463    157       C  
ATOM   4349  OG1 THR B 219      79.074  -5.836-156.969  1.00 31.00           O  
ANISOU 4349  OG1 THR B 219     4503   3219   4055   -384   -494    158       O  
ATOM   4350  CG2 THR B 219      78.979  -7.624-158.587  1.00 35.32           C  
ANISOU 4350  CG2 THR B 219     5208   3611   4601   -380   -447    117       C  
ATOM   4351  N   ASN B 220      76.125  -9.095-156.729  1.00 33.09           N  
ANISOU 4351  N   ASN B 220     5107   3187   4281   -627   -403    192       N  
ATOM   4352  CA  ASN B 220      75.306 -10.297-156.877  1.00 34.31           C  
ANISOU 4352  CA  ASN B 220     5388   3223   4424   -725   -374    195       C  
ATOM   4353  C   ASN B 220      75.690 -11.070-158.140  1.00 35.62           C  
ANISOU 4353  C   ASN B 220     5649   3296   4586   -717   -366    138       C  
ATOM   4354  O   ASN B 220      74.832 -11.548-158.880  1.00 32.58           O  
ANISOU 4354  O   ASN B 220     5318   2865   4197   -843   -363    102       O  
ATOM   4355  CB  ASN B 220      73.820  -9.919-156.885  1.00 34.37           C  
ANISOU 4355  CB  ASN B 220     5329   3289   4441   -883   -370    202       C  
ATOM   4356  CG  ASN B 220      72.899 -11.111-156.768  1.00 34.88           C  
ANISOU 4356  CG  ASN B 220     5511   3244   4497  -1010   -342    221       C  
ATOM   4357  OD1 ASN B 220      73.251 -12.145-156.196  1.00 36.95           O  
ANISOU 4357  OD1 ASN B 220     5915   3382   4743   -976   -315    252       O  
ATOM   4358  ND2 ASN B 220      71.697 -10.970-157.308  1.00 37.30           N  
ANISOU 4358  ND2 ASN B 220     5759   3600   4813  -1162   -349    210       N  
ATOM   4359  N   ARG B 221      76.997 -11.163-158.399  1.00 35.19           N  
ANISOU 4359  N   ARG B 221     5614   3227   4531   -566   -364    130       N  
ATOM   4360  CA  ARG B 221      77.564 -11.877-159.548  1.00 36.74           C  
ANISOU 4360  CA  ARG B 221     5912   3334   4714   -517   -342     79       C  
ATOM   4361  C   ARG B 221      77.086 -11.335-160.892  1.00 36.00           C  
ANISOU 4361  C   ARG B 221     5761   3298   4621   -601   -360      8       C  
ATOM   4362  O   ARG B 221      77.082 -12.065-161.885  1.00 43.13           O  
ANISOU 4362  O   ARG B 221     6780   4110   5497   -621   -342    -45       O  
ATOM   4363  CB  ARG B 221      77.285 -13.383-159.470  1.00 38.44           C  
ANISOU 4363  CB  ARG B 221     6338   3363   4903   -550   -300     82       C  
ATOM   4364  CG  ARG B 221      77.983 -14.048-158.272  1.00 44.54           C  
ANISOU 4364  CG  ARG B 221     7192   4066   5667   -425   -273    161       C  
ATOM   4365  CD  ARG B 221      77.677 -15.531-158.155  1.00 58.37           C  
ANISOU 4365  CD  ARG B 221     9170   5615   7394   -457   -220    172       C  
ATOM   4366  NE  ARG B 221      76.420 -15.771-157.454  1.00 73.01           N  
ANISOU 4366  NE  ARG B 221    11051   7439   9249   -626   -218    202       N  
ATOM   4367  CZ  ARG B 221      75.367 -16.389-157.981  1.00 80.58           C  
ANISOU 4367  CZ  ARG B 221    12108   8307  10203   -806   -207    162       C  
ATOM   4368  NH1 ARG B 221      75.415 -16.847-159.225  1.00 89.67           N  
ANISOU 4368  NH1 ARG B 221    13358   9377  11336   -841   -201     81       N  
ATOM   4369  NH2 ARG B 221      74.267 -16.560-157.261  1.00 74.08           N  
ANISOU 4369  NH2 ARG B 221    11284   7477   9385   -956   -202    205       N  
ATOM   4370  N   GLY B 222      76.682 -10.071-160.957  1.00 35.92           N  
ANISOU 4370  N   GLY B 222     5585   3432   4632   -646   -393      7       N  
ATOM   4371  CA  GLY B 222      76.241  -9.450-162.187  1.00 38.49           C  
ANISOU 4371  CA  GLY B 222     5841   3829   4953   -712   -411    -46       C  
ATOM   4372  C   GLY B 222      74.762  -9.147-162.245  1.00 35.74           C  
ANISOU 4372  C   GLY B 222     5436   3538   4605   -878   -435    -44       C  
ATOM   4373  O   GLY B 222      74.347  -8.312-163.061  1.00 38.46           O  
ANISOU 4373  O   GLY B 222     5679   3985   4950   -919   -457    -67       O  
ATOM   4374  N   ASN B 223      73.948  -9.808-161.425  1.00 31.39           N  
ANISOU 4374  N   ASN B 223     4942   2932   4054   -971   -427     -9       N  
ATOM   4375  CA  ASN B 223      72.520  -9.502-161.353  1.00 31.49           C  
ANISOU 4375  CA  ASN B 223     4874   3019   4070  -1125   -443     11       C  
ATOM   4376  C   ASN B 223      72.329  -8.435-160.273  1.00 33.50           C  
ANISOU 4376  C   ASN B 223     4996   3381   4352  -1084   -435     72       C  
ATOM   4377  O   ASN B 223      71.948  -8.707-159.130  1.00 35.17           O  
ANISOU 4377  O   ASN B 223     5228   3570   4566  -1106   -412    126       O  
ATOM   4378  CB  ASN B 223      71.707 -10.752-161.061  1.00 34.78           C  
ANISOU 4378  CB  ASN B 223     5416   3325   4473  -1261   -432     22       C  
ATOM   4379  CG  ASN B 223      70.226 -10.475-161.030  1.00 48.23           C  
ANISOU 4379  CG  ASN B 223     7016   5126   6185  -1427   -449     54       C  
ATOM   4380  OD1 ASN B 223      69.758  -9.501-161.623  1.00 47.20           O  
ANISOU 4380  OD1 ASN B 223     6742   5135   6059  -1449   -477     50       O  
ATOM   4381  ND2 ASN B 223      69.476 -11.318-160.326  1.00 61.46           N  
ANISOU 4381  ND2 ASN B 223     8757   6733   7861  -1541   -428     95       N  
ATOM   4382  N   LEU B 224      72.579  -7.191-160.662  1.00 29.93           N  
ANISOU 4382  N   LEU B 224     4418   3042   3913  -1025   -448     63       N  
ATOM   4383  CA  LEU B 224      72.764  -6.109-159.697  1.00 30.23           C  
ANISOU 4383  CA  LEU B 224     4362   3157   3967   -954   -436    103       C  
ATOM   4384  C   LEU B 224      71.479  -5.781-158.938  1.00 34.65           C  
ANISOU 4384  C   LEU B 224     4856   3780   4530  -1037   -416    159       C  
ATOM   4385  O   LEU B 224      70.368  -5.861-159.472  1.00 31.76           O  
ANISOU 4385  O   LEU B 224     4442   3461   4163  -1147   -421    168       O  
ATOM   4386  CB  LEU B 224      73.287  -4.853-160.401  1.00 27.72           C  
ANISOU 4386  CB  LEU B 224     3939   2930   3663   -886   -448     79       C  
ATOM   4387  CG  LEU B 224      74.803  -4.735-160.579  1.00 36.74           C  
ANISOU 4387  CG  LEU B 224     5103   4046   4811   -764   -455     52       C  
ATOM   4388  CD1 LEU B 224      75.391  -5.907-161.316  1.00 40.73           C  
ANISOU 4388  CD1 LEU B 224     5720   4455   5301   -743   -455     16       C  
ATOM   4389  CD2 LEU B 224      75.155  -3.432-161.305  1.00 43.14           C  
ANISOU 4389  CD2 LEU B 224     5805   4948   5638   -723   -460     36       C  
ATOM   4390  N   ARG B 225      71.661  -5.367-157.683  1.00 29.46           N  
ANISOU 4390  N   ARG B 225     4190   3133   3869   -979   -393    199       N  
ATOM   4391  CA  ARG B 225      70.584  -5.020-156.764  1.00 33.34           C  
ANISOU 4391  CA  ARG B 225     4632   3680   4357  -1026   -356    260       C  
ATOM   4392  C   ARG B 225      70.873  -3.662-156.143  1.00 34.79           C  
ANISOU 4392  C   ARG B 225     4748   3936   4536   -937   -340    269       C  
ATOM   4393  O   ARG B 225      71.987  -3.427-155.665  1.00 31.58           O  
ANISOU 4393  O   ARG B 225     4380   3501   4119   -849   -357    250       O  
ATOM   4394  CB  ARG B 225      70.452  -6.062-155.640  1.00 30.14           C  
ANISOU 4394  CB  ARG B 225     4330   3189   3931  -1050   -330    304       C  
ATOM   4395  CG  ARG B 225      70.099  -7.443-156.151  1.00 39.14           C  
ANISOU 4395  CG  ARG B 225     5563   4235   5074  -1153   -336    297       C  
ATOM   4396  CD  ARG B 225      69.939  -8.411-155.018  1.00 40.25           C  
ANISOU 4396  CD  ARG B 225     5810   4286   5196  -1174   -300    352       C  
ATOM   4397  NE  ARG B 225      71.222  -8.799-154.441  1.00 37.51           N  
ANISOU 4397  NE  ARG B 225     5567   3856   4829  -1049   -307    348       N  
ATOM   4398  CZ  ARG B 225      71.422  -9.972-153.845  1.00 39.00           C  
ANISOU 4398  CZ  ARG B 225     5894   3925   5000  -1048   -285    381       C  
ATOM   4399  NH1 ARG B 225      70.430 -10.848-153.780  1.00 39.67           N  
ANISOU 4399  NH1 ARG B 225     6035   3949   5088  -1181   -254    414       N  
ATOM   4400  NH2 ARG B 225      72.604 -10.279-153.339  1.00 35.07           N  
ANISOU 4400  NH2 ARG B 225     5475   3369   4481   -918   -295    388       N  
ATOM   4401  N   SER B 226      69.869  -2.782-156.129  1.00 27.65           N  
ANISOU 4401  N   SER B 226     3746   3124   3636   -960   -308    302       N  
ATOM   4402  CA  SER B 226      70.056  -1.453-155.565  1.00 25.00           C  
ANISOU 4402  CA  SER B 226     3368   2840   3291   -879   -281    307       C  
ATOM   4403  C   SER B 226      70.186  -1.525-154.051  1.00 23.67           C  
ANISOU 4403  C   SER B 226     3270   2641   3084   -841   -252    337       C  
ATOM   4404  O   SER B 226      69.430  -2.247-153.393  1.00 27.88           O  
ANISOU 4404  O   SER B 226     3830   3161   3602   -891   -218    388       O  
ATOM   4405  CB  SER B 226      68.887  -0.548-155.928  1.00 34.75           C  
ANISOU 4405  CB  SER B 226     4491   4176   4536   -896   -239    344       C  
ATOM   4406  OG  SER B 226      68.759  -0.474-157.344  1.00 38.16           O  
ANISOU 4406  OG  SER B 226     4859   4649   4992   -928   -274    320       O  
ATOM   4407  N   ALA B 227      71.114  -0.739-153.502  1.00 27.09           N  
ANISOU 4407  N   ALA B 227     3730   3067   3496   -762   -264    309       N  
ATOM   4408  CA  ALA B 227      71.350  -0.820-152.056  1.00 29.27           C  
ANISOU 4408  CA  ALA B 227     4086   3317   3719   -725   -248    332       C  
ATOM   4409  C   ALA B 227      71.969   0.469-151.554  1.00 32.59           C  
ANISOU 4409  C   ALA B 227     4514   3760   4111   -661   -251    299       C  
ATOM   4410  O   ALA B 227      72.604   1.205-152.307  1.00 30.23           O  
ANISOU 4410  O   ALA B 227     4173   3474   3839   -642   -281    254       O  
ATOM   4411  CB  ALA B 227      72.257  -2.002-151.711  1.00 26.16           C  
ANISOU 4411  CB  ALA B 227     3779   2850   3311   -712   -295    330       C  
ATOM   4412  N   ILE B 228      71.827   0.704-150.245  1.00 28.47           N  
ANISOU 4412  N   ILE B 228     4057   3234   3525   -633   -221    321       N  
ATOM   4413  CA  ILE B 228      72.510   1.808-149.596  1.00 26.90           C  
ANISOU 4413  CA  ILE B 228     3899   3041   3281   -586   -233    281       C  
ATOM   4414  C   ILE B 228      72.957   1.298-148.237  1.00 28.98           C  
ANISOU 4414  C   ILE B 228     4263   3281   3466   -562   -254    297       C  
ATOM   4415  O   ILE B 228      72.243   0.521-147.599  1.00 30.80           O  
ANISOU 4415  O   ILE B 228     4533   3502   3670   -572   -210    354       O  
ATOM   4416  CB  ILE B 228      71.604   3.050-149.458  1.00 32.23           C  
ANISOU 4416  CB  ILE B 228     4557   3747   3941   -565   -152    288       C  
ATOM   4417  CG1 ILE B 228      72.334   4.211-148.771  1.00 32.94           C  
ANISOU 4417  CG1 ILE B 228     4720   3822   3976   -529   -164    235       C  
ATOM   4418  CG2 ILE B 228      70.299   2.695-148.728  1.00 28.68           C  
ANISOU 4418  CG2 ILE B 228     4119   3319   3459   -566    -63    359       C  
ATOM   4419  CD1 ILE B 228      71.563   5.523-148.841  1.00 29.24           C  
ANISOU 4419  CD1 ILE B 228     4248   3362   3498   -496    -77    234       C  
ATOM   4420  N   THR B 229      74.148   1.690-147.820  1.00 26.30           N  
ANISOU 4420  N   THR B 229     3962   2939   3090   -538   -323    254       N  
ATOM   4421  CA  THR B 229      74.594   1.404-146.450  1.00 24.76           C  
ANISOU 4421  CA  THR B 229     3867   2740   2803   -511   -350    268       C  
ATOM   4422  C   THR B 229      74.712   2.732-145.710  1.00 32.29           C  
ANISOU 4422  C   THR B 229     4877   3707   3685   -500   -341    223       C  
ATOM   4423  O   THR B 229      75.362   3.658-146.205  1.00 33.80           O  
ANISOU 4423  O   THR B 229     5038   3905   3899   -514   -379    165       O  
ATOM   4424  CB  THR B 229      75.934   0.667-146.463  1.00 26.93           C  
ANISOU 4424  CB  THR B 229     4142   3014   3078   -491   -451    263       C  
ATOM   4425  OG1 THR B 229      75.791  -0.595-147.131  1.00 33.06           O  
ANISOU 4425  OG1 THR B 229     4895   3755   3912   -493   -446    302       O  
ATOM   4426  CG2 THR B 229      76.426   0.438-145.004  1.00 26.97           C  
ANISOU 4426  CG2 THR B 229     4246   3031   2972   -458   -490    283       C  
ATOM   4427  N   VAL B 230      74.084   2.861-144.544  1.00 35.22           N  
ANISOU 4427  N   VAL B 230     5341   4076   3965   -479   -285    247       N  
ATOM   4428  CA  VAL B 230      74.113   4.167-143.902  1.00 31.75           C  
ANISOU 4428  CA  VAL B 230     4979   3634   3452   -469   -263    195       C  
ATOM   4429  C   VAL B 230      74.844   4.081-142.572  1.00 36.29           C  
ANISOU 4429  C   VAL B 230     5669   4217   3903   -458   -325    181       C  
ATOM   4430  O   VAL B 230      74.479   3.305-141.669  1.00 32.49           O  
ANISOU 4430  O   VAL B 230     5253   3739   3353   -431   -300    236       O  
ATOM   4431  CB  VAL B 230      72.725   4.840-143.832  1.00 46.22           C  
ANISOU 4431  CB  VAL B 230     6825   5460   5278   -442   -127    219       C  
ATOM   4432  CG1 VAL B 230      71.568   3.929-144.272  1.00 46.95           C  
ANISOU 4432  CG1 VAL B 230     6836   5570   5431   -443    -52    303       C  
ATOM   4433  CG2 VAL B 230      72.511   5.676-142.587  1.00 31.52           C  
ANISOU 4433  CG2 VAL B 230     5106   3582   3290   -407    -75    195       C  
ATOM   4434  N   PHE B 231      75.932   4.836-142.509  1.00 30.20           N  
ANISOU 4434  N   PHE B 231     4915   3454   3104   -488   -415    111       N  
ATOM   4435  CA  PHE B 231      76.855   4.889-141.391  1.00 32.55           C  
ANISOU 4435  CA  PHE B 231     5305   3779   3284   -496   -508     85       C  
ATOM   4436  C   PHE B 231      76.367   5.927-140.395  1.00 35.94           C  
ANISOU 4436  C   PHE B 231     5882   4182   3593   -493   -449     40       C  
ATOM   4437  O   PHE B 231      75.386   6.636-140.658  1.00 34.29           O  
ANISOU 4437  O   PHE B 231     5692   3930   3404   -474   -333     33       O  
ATOM   4438  CB  PHE B 231      78.258   5.181-141.935  1.00 31.63           C  
ANISOU 4438  CB  PHE B 231     5112   3698   3209   -546   -637     37       C  
ATOM   4439  CG  PHE B 231      78.837   4.027-142.725  1.00 34.91           C  
ANISOU 4439  CG  PHE B 231     5405   4142   3718   -525   -692     88       C  
ATOM   4440  CD1 PHE B 231      79.218   2.864-142.085  1.00 30.48           C  
ANISOU 4440  CD1 PHE B 231     4862   3610   3109   -481   -742    149       C  
ATOM   4441  CD2 PHE B 231      78.967   4.091-144.112  1.00 34.48           C  
ANISOU 4441  CD2 PHE B 231     5230   4078   3791   -540   -683     79       C  
ATOM   4442  CE1 PHE B 231      79.730   1.780-142.795  1.00 34.74           C  
ANISOU 4442  CE1 PHE B 231     5311   4160   3728   -447   -778    197       C  
ATOM   4443  CE2 PHE B 231      79.477   3.010-144.823  1.00 35.82           C  
ANISOU 4443  CE2 PHE B 231     5311   4265   4035   -511   -721    122       C  
ATOM   4444  CZ  PHE B 231      79.859   1.867-144.175  1.00 35.02           C  
ANISOU 4444  CZ  PHE B 231     5236   4183   3888   -463   -765    179       C  
ATOM   4445  N   PRO B 232      76.988   6.010-139.209  1.00 34.81           N  
ANISOU 4445  N   PRO B 232     5851   4062   3311   -502   -522     15       N  
ATOM   4446  CA  PRO B 232      76.439   6.866-138.146  1.00 38.68           C  
ANISOU 4446  CA  PRO B 232     6514   4519   3663   -489   -453    -25       C  
ATOM   4447  C   PRO B 232      76.263   8.317-138.564  1.00 33.26           C  
ANISOU 4447  C   PRO B 232     5873   3770   2993   -521   -401   -108       C  
ATOM   4448  O   PRO B 232      77.096   8.893-139.267  1.00 37.36           O  
ANISOU 4448  O   PRO B 232     6333   4286   3575   -589   -478   -164       O  
ATOM   4449  CB  PRO B 232      77.477   6.740-137.027  1.00 34.42           C  
ANISOU 4449  CB  PRO B 232     6067   4031   2980   -518   -586    -53       C  
ATOM   4450  CG  PRO B 232      78.002   5.347-137.197  1.00 32.95           C  
ANISOU 4450  CG  PRO B 232     5772   3906   2844   -491   -664     29       C  
ATOM   4451  CD  PRO B 232      78.073   5.152-138.706  1.00 36.31           C  
ANISOU 4451  CD  PRO B 232     6026   4318   3453   -506   -656     41       C  
ATOM   4452  N   GLN B 233      75.180   8.914-138.079  1.00 36.06           N  
ANISOU 4452  N   GLN B 233     6344   4074   3284   -466   -260   -109       N  
ATOM   4453  CA  GLN B 233      74.873  10.300-138.378  1.00 38.40           C  
ANISOU 4453  CA  GLN B 233     6715   4294   3582   -472   -182   -178       C  
ATOM   4454  C   GLN B 233      75.873  11.248-137.726  1.00 39.46           C  
ANISOU 4454  C   GLN B 233     6996   4396   3602   -555   -278   -289       C  
ATOM   4455  O   GLN B 233      76.538  10.925-136.736  1.00 38.02           O  
ANISOU 4455  O   GLN B 233     6894   4255   3295   -588   -379   -310       O  
ATOM   4456  CB  GLN B 233      73.474  10.661-137.890  1.00 37.32           C  
ANISOU 4456  CB  GLN B 233     6676   4116   3387   -371      2   -143       C  
ATOM   4457  CG  GLN B 233      73.350  10.710-136.373  1.00 42.37           C  
ANISOU 4457  CG  GLN B 233     7515   4750   3836   -340     26   -161       C  
ATOM   4458  CD  GLN B 233      71.928  10.491-135.930  1.00 45.06           C  
ANISOU 4458  CD  GLN B 233     7888   5090   4142   -225    207    -78       C  
ATOM   4459  OE1 GLN B 233      71.247   9.600-136.443  1.00 48.20           O  
ANISOU 4459  OE1 GLN B 233     8134   5538   4642   -192    257     22       O  
ATOM   4460  NE2 GLN B 233      71.457  11.314-134.991  1.00 43.09           N  
ANISOU 4460  NE2 GLN B 233     7839   4785   3746   -167    312   -117       N  
ATOM   4461  N   ARG B 234      75.964  12.437-138.312  1.00 41.38           N  
ANISOU 4461  N   ARG B 234     7274   4562   3885   -593   -246   -357       N  
ATOM   4462  CA  ARG B 234      76.693  13.538-137.705  1.00 43.44           C  
ANISOU 4462  CA  ARG B 234     7709   4763   4034   -681   -305   -470       C  
ATOM   4463  C   ARG B 234      76.095  13.863-136.344  1.00 41.89           C  
ANISOU 4463  C   ARG B 234     7744   4523   3650   -627   -225   -501       C  
ATOM   4464  O   ARG B 234      74.875  13.857-136.162  1.00 44.51           O  
ANISOU 4464  O   ARG B 234     8122   4824   3966   -507    -59   -448       O  
ATOM   4465  CB  ARG B 234      76.637  14.758-138.636  1.00 41.01           C  
ANISOU 4465  CB  ARG B 234     7414   4356   3811   -711   -241   -522       C  
ATOM   4466  CG  ARG B 234      77.219  16.049-138.065  1.00 46.87           C  
ANISOU 4466  CG  ARG B 234     8369   4999   4440   -809   -271   -645       C  
ATOM   4467  CD  ARG B 234      77.221  17.122-139.161  1.00 47.70           C  
ANISOU 4467  CD  ARG B 234     8461   5006   4657   -839   -208   -676       C  
ATOM   4468  NE  ARG B 234      78.209  16.817-140.198  1.00 45.39           N  
ANISOU 4468  NE  ARG B 234     7963   4781   4504   -934   -334   -661       N  
ATOM   4469  CZ  ARG B 234      78.146  17.246-141.461  1.00 49.79           C  
ANISOU 4469  CZ  ARG B 234     8412   5301   5204   -932   -284   -639       C  
ATOM   4470  NH1 ARG B 234      77.109  17.961-141.873  1.00 45.79           N  
ANISOU 4470  NH1 ARG B 234     7974   4699   4727   -834   -116   -621       N  
ATOM   4471  NH2 ARG B 234      79.104  16.931-142.320  1.00 40.82           N  
ANISOU 4471  NH2 ARG B 234     7097   4234   4178  -1017   -398   -625       N  
ATOM   4472  N   CYS B 235      76.958  14.126-135.371  1.00 48.14           N  
ANISOU 4472  N   CYS B 235     8677   5323   4291   -715   -344   -581       N  
ATOM   4473  CA  CYS B 235      76.463  14.393-134.029  1.00 54.19           C  
ANISOU 4473  CA  CYS B 235     9681   6053   4858   -665   -277   -615       C  
ATOM   4474  C   CYS B 235      77.431  15.323-133.320  1.00 57.10           C  
ANISOU 4474  C   CYS B 235    10240   6376   5078   -800   -394   -749       C  
ATOM   4475  O   CYS B 235      78.643  15.263-133.568  1.00 50.82           O  
ANISOU 4475  O   CYS B 235     9353   5643   4314   -935   -575   -785       O  
ATOM   4476  CB  CYS B 235      76.288  13.094-133.232  1.00 68.71           C  
ANISOU 4476  CB  CYS B 235    11485   7997   6623   -600   -305   -528       C  
ATOM   4477  SG  CYS B 235      77.808  12.164-133.048  1.00 73.20           S  
ANISOU 4477  SG  CYS B 235    11928   8705   7181   -708   -559   -518       S  
ATOM   4478  N   PRO B 236      76.934  16.190-132.441  1.00 66.82           N  
ANISOU 4478  N   PRO B 236    11739   7506   6145   -772   -294   -825       N  
ATOM   4479  CA  PRO B 236      77.827  17.118-131.743  1.00 65.89           C  
ANISOU 4479  CA  PRO B 236    11821   7335   5880   -916   -406   -961       C  
ATOM   4480  C   PRO B 236      78.821  16.369-130.868  1.00 57.62           C  
ANISOU 4480  C   PRO B 236    10712   6434   4748   -991   -602   -949       C  
ATOM   4481  O   PRO B 236      78.473  15.417-130.167  1.00 63.20           O  
ANISOU 4481  O   PRO B 236    11437   7221   5356   -905   -598   -884       O  
ATOM   4482  CB  PRO B 236      76.865  17.972-130.909  1.00 75.17           C  
ANISOU 4482  CB  PRO B 236    13240   8384   6936   -812   -219   -996       C  
ATOM   4483  CG  PRO B 236      75.649  17.105-130.733  1.00 74.08           C  
ANISOU 4483  CG  PRO B 236    13100   8282   6763   -632    -64   -894       C  
ATOM   4484  CD  PRO B 236      75.534  16.320-131.999  1.00 69.92           C  
ANISOU 4484  CD  PRO B 236    12258   7833   6475   -603    -72   -781       C  
ATOM   4485  N   GLY B 237      80.077  16.797-130.936  1.00 61.19           N  
ANISOU 4485  N   GLY B 237    11079   6928   5242  -1147   -768  -1001       N  
ATOM   4486  CA  GLY B 237      81.125  16.278-130.084  1.00 65.68           C  
ANISOU 4486  CA  GLY B 237    11585   7640   5728  -1223   -956   -997       C  
ATOM   4487  C   GLY B 237      82.062  15.306-130.756  1.00 58.76           C  
ANISOU 4487  C   GLY B 237    10448   6916   4962  -1275  -1121   -928       C  
ATOM   4488  O   GLY B 237      83.106  14.973-130.179  1.00 58.67           O  
ANISOU 4488  O   GLY B 237    10352   7037   4904  -1345  -1287   -922       O  
ATOM   4489  N   ARG B 238      81.732  14.864-131.966  1.00 54.88           N  
ANISOU 4489  N   ARG B 238     9826   6414   4614  -1237  -1078   -875       N  
ATOM   4490  CA  ARG B 238      82.502  13.857-132.666  1.00 63.05           C  
ANISOU 4490  CA  ARG B 238    10617   7582   5755  -1260  -1214   -797       C  
ATOM   4491  C   ARG B 238      82.587  14.259-134.130  1.00 54.98           C  
ANISOU 4491  C   ARG B 238     9447   6506   4937  -1299  -1175   -797       C  
ATOM   4492  O   ARG B 238      81.666  14.878-134.671  1.00 52.39           O  
ANISOU 4492  O   ARG B 238     9182   6049   4677  -1242  -1007   -812       O  
ATOM   4493  CB  ARG B 238      81.848  12.477-132.522  1.00 72.91           C  
ANISOU 4493  CB  ARG B 238    11787   8897   7017  -1101  -1158   -671       C  
ATOM   4494  CG  ARG B 238      82.778  11.295-132.675  1.00 79.05           C  
ANISOU 4494  CG  ARG B 238    12354   9834   7849  -1098  -1312   -580       C  
ATOM   4495  CD  ARG B 238      81.992   9.983-132.662  1.00 80.46           C  
ANISOU 4495  CD  ARG B 238    12462  10039   8071   -935  -1218   -452       C  
ATOM   4496  NE  ARG B 238      80.765  10.072-133.453  1.00 79.63           N  
ANISOU 4496  NE  ARG B 238    12338   9825   8095   -850  -1021   -423       N  
ATOM   4497  CZ  ARG B 238      80.003   9.031-133.780  1.00 82.76           C  
ANISOU 4497  CZ  ARG B 238    12642  10227   8576   -735   -925   -316       C  
ATOM   4498  NH1 ARG B 238      80.341   7.806-133.392  1.00 82.38           N  
ANISOU 4498  NH1 ARG B 238    12528  10269   8503   -683   -995   -226       N  
ATOM   4499  NH2 ARG B 238      78.902   9.216-134.501  1.00 79.81           N  
ANISOU 4499  NH2 ARG B 238    12244   9769   8312   -675   -759   -295       N  
ATOM   4500  N   GLY B 239      83.716  13.936-134.752  1.00 49.65           N  
ANISOU 4500  N   GLY B 239     8564   5938   4361  -1385  -1324   -771       N  
ATOM   4501  CA  GLY B 239      83.861  14.139-136.181  1.00 46.57           C  
ANISOU 4501  CA  GLY B 239     7997   5521   4178  -1403  -1285   -748       C  
ATOM   4502  C   GLY B 239      82.991  13.188-136.984  1.00 45.47           C  
ANISOU 4502  C   GLY B 239     7717   5381   4179  -1241  -1160   -638       C  
ATOM   4503  O   GLY B 239      82.335  12.286-136.458  1.00 48.41           O  
ANISOU 4503  O   GLY B 239     8110   5781   4503  -1122  -1110   -572       O  
ATOM   4504  N   ASP B 240      82.993  13.406-138.302  1.00 39.32           N  
ANISOU 4504  N   ASP B 240     6797   4568   3574  -1245  -1109   -620       N  
ATOM   4505  CA  ASP B 240      82.159  12.658-139.233  1.00 39.91           C  
ANISOU 4505  CA  ASP B 240     6743   4633   3789  -1115   -992   -530       C  
ATOM   4506  C   ASP B 240      82.845  11.367-139.660  1.00 40.56           C  
ANISOU 4506  C   ASP B 240     6616   4841   3952  -1081  -1088   -442       C  
ATOM   4507  O   ASP B 240      84.070  11.311-139.787  1.00 42.87           O  
ANISOU 4507  O   ASP B 240     6802   5224   4262  -1165  -1229   -446       O  
ATOM   4508  CB  ASP B 240      81.868  13.475-140.503  1.00 42.18           C  
ANISOU 4508  CB  ASP B 240     6977   4832   4217  -1131   -897   -547       C  
ATOM   4509  CG  ASP B 240      80.951  14.672-140.264  1.00 52.86           C  
ANISOU 4509  CG  ASP B 240     8532   6039   5512  -1118   -757   -611       C  
ATOM   4510  OD1 ASP B 240      80.210  14.698-139.264  1.00 54.40           O  
ANISOU 4510  OD1 ASP B 240     8892   6198   5581  -1056   -689   -623       O  
ATOM   4511  OD2 ASP B 240      80.951  15.584-141.120  1.00 53.63           O  
ANISOU 4511  OD2 ASP B 240     8625   6058   5694  -1158   -702   -641       O  
ATOM   4512  N   PHE B 241      82.039  10.337-139.918  1.00 35.16           N  
ANISOU 4512  N   PHE B 241     5874   4164   3323   -957  -1005   -357       N  
ATOM   4513  CA  PHE B 241      82.468   9.282-140.825  1.00 32.38           C  
ANISOU 4513  CA  PHE B 241     5325   3881   3098   -913  -1043   -279       C  
ATOM   4514  C   PHE B 241      82.457   9.833-142.249  1.00 35.12           C  
ANISOU 4514  C   PHE B 241     5563   4185   3596   -939   -989   -291       C  
ATOM   4515  O   PHE B 241      81.505  10.509-142.640  1.00 35.31           O  
ANISOU 4515  O   PHE B 241     5649   4117   3651   -919   -865   -313       O  
ATOM   4516  CB  PHE B 241      81.525   8.080-140.769  1.00 31.80           C  
ANISOU 4516  CB  PHE B 241     5239   3803   3042   -792   -958   -193       C  
ATOM   4517  CG  PHE B 241      81.732   7.196-139.567  1.00 37.49           C  
ANISOU 4517  CG  PHE B 241     6021   4585   3638   -750  -1023   -149       C  
ATOM   4518  CD1 PHE B 241      81.132   7.500-138.361  1.00 40.25           C  
ANISOU 4518  CD1 PHE B 241     6548   4905   3838   -737   -983   -172       C  
ATOM   4519  CD2 PHE B 241      82.523   6.064-139.662  1.00 41.56           C  
ANISOU 4519  CD2 PHE B 241     6423   5186   4182   -711  -1114    -78       C  
ATOM   4520  CE1 PHE B 241      81.320   6.668-137.241  1.00 44.97           C  
ANISOU 4520  CE1 PHE B 241     7209   5565   4313   -692  -1040   -124       C  
ATOM   4521  CE2 PHE B 241      82.723   5.240-138.560  1.00 42.06           C  
ANISOU 4521  CE2 PHE B 241     6547   5307   4129   -660  -1171    -26       C  
ATOM   4522  CZ  PHE B 241      82.120   5.545-137.353  1.00 41.33           C  
ANISOU 4522  CZ  PHE B 241     6629   5189   3884   -655  -1137    -48       C  
ATOM   4523  N   ARG B 242      83.510   9.546-143.020  1.00 34.36           N  
ANISOU 4523  N   ARG B 242     5305   4161   3589   -973  -1076   -270       N  
ATOM   4524  CA  ARG B 242      83.547   9.932-144.433  1.00 34.67           C  
ANISOU 4524  CA  ARG B 242     5233   4171   3770   -986  -1025   -269       C  
ATOM   4525  C   ARG B 242      84.252   8.872-145.260  1.00 39.67           C  
ANISOU 4525  C   ARG B 242     5686   4888   4501   -940  -1075   -200       C  
ATOM   4526  O   ARG B 242      85.252   8.299-144.823  1.00 37.57           O  
ANISOU 4526  O   ARG B 242     5353   4719   4201   -946  -1189   -172       O  
ATOM   4527  CB  ARG B 242      84.277  11.267-144.662  1.00 34.41           C  
ANISOU 4527  CB  ARG B 242     5213   4114   3745  -1116  -1065   -341       C  
ATOM   4528  CG  ARG B 242      83.582  12.500-144.106  1.00 43.81           C  
ANISOU 4528  CG  ARG B 242     6598   5189   4857  -1162   -991   -419       C  
ATOM   4529  CD  ARG B 242      82.289  12.815-144.860  1.00 46.30           C  
ANISOU 4529  CD  ARG B 242     6947   5406   5241  -1078   -825   -403       C  
ATOM   4530  NE  ARG B 242      82.497  13.186-146.265  1.00 51.76           N  
ANISOU 4530  NE  ARG B 242     7518   6082   6066  -1094   -790   -388       N  
ATOM   4531  CZ  ARG B 242      82.773  14.422-146.681  1.00 52.04           C  
ANISOU 4531  CZ  ARG B 242     7599   6046   6127  -1177   -766   -439       C  
ATOM   4532  NH1 ARG B 242      82.903  15.408-145.803  1.00 50.69           N  
ANISOU 4532  NH1 ARG B 242     7598   5805   5857  -1262   -778   -517       N  
ATOM   4533  NH2 ARG B 242      82.933  14.666-147.977  1.00 56.16           N  
ANISOU 4533  NH2 ARG B 242     8009   6562   6768  -1179   -729   -413       N  
ATOM   4534  N   ILE B 243      83.736   8.631-146.465  1.00 35.10           N  
ANISOU 4534  N   ILE B 243     5029   4272   4034   -888   -988   -171       N  
ATOM   4535  CA  ILE B 243      84.456   7.907-147.502  1.00 36.11           C  
ANISOU 4535  CA  ILE B 243     4996   4460   4262   -855  -1018   -122       C  
ATOM   4536  C   ILE B 243      85.079   8.961-148.409  1.00 36.44           C  
ANISOU 4536  C   ILE B 243     4967   4500   4377   -936  -1021   -157       C  
ATOM   4537  O   ILE B 243      84.366   9.798-148.959  1.00 35.97           O  
ANISOU 4537  O   ILE B 243     4955   4360   4353   -955   -931   -187       O  
ATOM   4538  CB  ILE B 243      83.517   6.980-148.292  1.00 34.66           C  
ANISOU 4538  CB  ILE B 243     4787   4237   4145   -759   -925    -75       C  
ATOM   4539  CG1 ILE B 243      82.881   5.958-147.342  1.00 33.61           C  
ANISOU 4539  CG1 ILE B 243     4734   4096   3940   -693   -915    -36       C  
ATOM   4540  CG2 ILE B 243      84.283   6.295-149.428  1.00 32.48           C  
ANISOU 4540  CG2 ILE B 243     4367   4009   3964   -721   -946    -35       C  
ATOM   4541  CD1 ILE B 243      81.683   5.256-147.929  1.00 32.91           C  
ANISOU 4541  CD1 ILE B 243     4654   3952   3899   -632   -814     -1       C  
ATOM   4542  N   TRP B 244      86.405   8.962-148.548  1.00 32.33           N  
ANISOU 4542  N   TRP B 244     4332   4072   3880   -985  -1119   -145       N  
ATOM   4543  CA  TRP B 244      87.015  10.040-149.320  1.00 30.71           C  
ANISOU 4543  CA  TRP B 244     4065   3864   3739  -1082  -1118   -175       C  
ATOM   4544  C   TRP B 244      86.823   9.839-150.819  1.00 28.04           C  
ANISOU 4544  C   TRP B 244     3630   3507   3517  -1023  -1033   -141       C  
ATOM   4545  O   TRP B 244      86.742  10.828-151.558  1.00 32.19           O  
ANISOU 4545  O   TRP B 244     4155   3981   4093  -1079   -979   -167       O  
ATOM   4546  CB  TRP B 244      88.506  10.162-149.005  1.00 31.77           C  
ANISOU 4546  CB  TRP B 244     4089   4119   3863  -1168  -1250   -166       C  
ATOM   4547  CG  TRP B 244      88.806  10.844-147.685  1.00 39.50           C  
ANISOU 4547  CG  TRP B 244     5174   5110   4725  -1282  -1342   -223       C  
ATOM   4548  CD1 TRP B 244      88.037  10.835-146.550  1.00 38.64           C  
ANISOU 4548  CD1 TRP B 244     5233   4948   4501  -1267  -1338   -259       C  
ATOM   4549  CD2 TRP B 244      89.945  11.653-147.391  1.00 43.74           C  
ANISOU 4549  CD2 TRP B 244     5660   5717   5241  -1436  -1451   -253       C  
ATOM   4550  NE1 TRP B 244      88.641  11.590-145.556  1.00 38.87           N  
ANISOU 4550  NE1 TRP B 244     5334   5005   4429  -1399  -1440   -317       N  
ATOM   4551  CE2 TRP B 244      89.814  12.099-146.051  1.00 44.46           C  
ANISOU 4551  CE2 TRP B 244     5907   5790   5195  -1513  -1517   -316       C  
ATOM   4552  CE3 TRP B 244      91.071  12.035-148.121  1.00 44.96           C  
ANISOU 4552  CE3 TRP B 244     5651   5955   5478  -1523  -1500   -231       C  
ATOM   4553  CZ2 TRP B 244      90.761  12.909-145.448  1.00 44.56           C  
ANISOU 4553  CZ2 TRP B 244     5918   5858   5155  -1664  -1618   -361       C  
ATOM   4554  CZ3 TRP B 244      92.008  12.837-147.519  1.00 44.26           C  
ANISOU 4554  CZ3 TRP B 244     5548   5924   5346  -1664  -1588   -268       C  
ATOM   4555  CH2 TRP B 244      91.853  13.269-146.192  1.00 50.32           C  
ANISOU 4555  CH2 TRP B 244     6472   6664   5982  -1722  -1636   -334       C  
ATOM   4556  N   ASN B 245      86.750   8.587-151.263  1.00 31.28           N  
ANISOU 4556  N   ASN B 245     3971   3952   3961   -912  -1020    -84       N  
ATOM   4557  CA  ASN B 245      86.503   8.271-152.676  1.00 32.49           C  
ANISOU 4557  CA  ASN B 245     4052   4087   4207   -850   -941    -56       C  
ATOM   4558  C   ASN B 245      85.125   8.754-153.120  1.00 37.07           C  
ANISOU 4558  C   ASN B 245     4722   4566   4798   -837   -833    -81       C  
ATOM   4559  O   ASN B 245      84.149   8.677-152.372  1.00 30.96           O  
ANISOU 4559  O   ASN B 245     4056   3741   3966   -819   -804    -94       O  
ATOM   4560  CB  ASN B 245      86.591   6.760-152.902  1.00 31.26           C  
ANISOU 4560  CB  ASN B 245     3846   3967   4064   -735   -945      0       C  
ATOM   4561  CG  ASN B 245      87.877   6.163-152.379  1.00 43.33           C  
ANISOU 4561  CG  ASN B 245     5285   5603   5573   -715  -1045     41       C  
ATOM   4562  OD1 ASN B 245      88.155   6.220-151.177  1.00 36.46           O  
ANISOU 4562  OD1 ASN B 245     4455   4771   4626   -750  -1124     36       O  
ATOM   4563  ND2 ASN B 245      88.655   5.555-153.270  1.00 37.41           N  
ANISOU 4563  ND2 ASN B 245     4417   4912   4886   -650  -1041     89       N  
ATOM   4564  N   SER B 246      85.035   9.206-154.381  1.00 34.76           N  
ANISOU 4564  N   SER B 246     4376   4253   4578   -836   -770    -76       N  
ATOM   4565  CA  SER B 246      83.747   9.652-154.909  1.00 31.68           C  
ANISOU 4565  CA  SER B 246     4051   3787   4200   -812   -671    -85       C  
ATOM   4566  C   SER B 246      82.830   8.487-155.253  1.00 30.57           C  
ANISOU 4566  C   SER B 246     3913   3641   4063   -725   -632    -53       C  
ATOM   4567  O   SER B 246      81.605   8.628-155.193  1.00 32.56           O  
ANISOU 4567  O   SER B 246     4229   3847   4298   -704   -569    -54       O  
ATOM   4568  CB  SER B 246      83.965  10.551-156.141  1.00 31.34           C  
ANISOU 4568  CB  SER B 246     3955   3730   4223   -838   -618    -83       C  
ATOM   4569  OG  SER B 246      84.712   9.852-157.121  1.00 37.39           O  
ANISOU 4569  OG  SER B 246     4605   4559   5044   -800   -631    -49       O  
ATOM   4570  N   GLN B 247      83.397   7.356-155.640  1.00 25.54           N  
ANISOU 4570  N   GLN B 247     3207   3049   3448   -675   -665    -24       N  
ATOM   4571  CA  GLN B 247      82.679   6.101-155.780  1.00 23.89           C  
ANISOU 4571  CA  GLN B 247     3020   2825   3232   -609   -644      1       C  
ATOM   4572  C   GLN B 247      83.470   4.988-155.114  1.00 26.68           C  
ANISOU 4572  C   GLN B 247     3363   3215   3561   -567   -710     27       C  
ATOM   4573  O   GLN B 247      84.689   5.079-154.949  1.00 31.92           O  
ANISOU 4573  O   GLN B 247     3960   3937   4230   -573   -770     36       O  
ATOM   4574  CB  GLN B 247      82.452   5.709-157.275  1.00 26.10           C  
ANISOU 4574  CB  GLN B 247     3247   3104   3566   -570   -595     14       C  
ATOM   4575  CG  GLN B 247      81.524   6.647-157.977  1.00 24.66           C  
ANISOU 4575  CG  GLN B 247     3075   2895   3401   -592   -529      4       C  
ATOM   4576  CD  GLN B 247      81.303   6.209-159.438  1.00 29.10           C  
ANISOU 4576  CD  GLN B 247     3592   3467   3999   -557   -492     17       C  
ATOM   4577  OE1 GLN B 247      81.340   5.019-159.754  1.00 31.70           O  
ANISOU 4577  OE1 GLN B 247     3921   3797   4325   -518   -502     26       O  
ATOM   4578  NE2 GLN B 247      81.065   7.158-160.299  1.00 34.41           N  
ANISOU 4578  NE2 GLN B 247     4238   4140   4695   -569   -446     17       N  
ATOM   4579  N   LEU B 248      82.777   3.896-154.794  1.00 31.20           N  
ANISOU 4579  N   LEU B 248     3993   3754   4108   -523   -696     48       N  
ATOM   4580  CA  LEU B 248      83.479   2.762-154.194  1.00 32.39           C  
ANISOU 4580  CA  LEU B 248     4148   3926   4232   -466   -747     83       C  
ATOM   4581  C   LEU B 248      84.449   2.121-155.182  1.00 34.37           C  
ANISOU 4581  C   LEU B 248     4319   4209   4532   -403   -753    106       C  
ATOM   4582  O   LEU B 248      85.515   1.648-154.778  1.00 34.39           O  
ANISOU 4582  O   LEU B 248     4278   4265   4524   -354   -806    139       O  
ATOM   4583  CB  LEU B 248      82.481   1.722-153.680  1.00 32.67           C  
ANISOU 4583  CB  LEU B 248     4278   3904   4232   -438   -718    104       C  
ATOM   4584  CG  LEU B 248      81.487   2.195-152.623  1.00 30.15           C  
ANISOU 4584  CG  LEU B 248     4040   3559   3857   -482   -699     95       C  
ATOM   4585  CD1 LEU B 248      80.590   1.034-152.141  1.00 28.97           C  
ANISOU 4585  CD1 LEU B 248     3971   3359   3678   -457   -667    131       C  
ATOM   4586  CD2 LEU B 248      82.254   2.851-151.442  1.00 34.59           C  
ANISOU 4586  CD2 LEU B 248     4616   4168   4360   -505   -768     84       C  
ATOM   4587  N   VAL B 249      84.104   2.093-156.473  1.00 31.58           N  
ANISOU 4587  N   VAL B 249     3944   3830   4224   -394   -696     94       N  
ATOM   4588  CA  VAL B 249      84.986   1.576-157.516  1.00 33.48           C  
ANISOU 4588  CA  VAL B 249     4120   4097   4505   -328   -683    112       C  
ATOM   4589  C   VAL B 249      85.331   2.719-158.467  1.00 34.19           C  
ANISOU 4589  C   VAL B 249     4126   4224   4639   -369   -661     93       C  
ATOM   4590  O   VAL B 249      84.435   3.341-159.057  1.00 33.35           O  
ANISOU 4590  O   VAL B 249     4043   4086   4544   -413   -616     67       O  
ATOM   4591  CB  VAL B 249      84.350   0.409-158.293  1.00 32.96           C  
ANISOU 4591  CB  VAL B 249     4121   3961   4440   -277   -633    112       C  
ATOM   4592  CG1 VAL B 249      85.372  -0.165-159.241  1.00 35.90           C  
ANISOU 4592  CG1 VAL B 249     4444   4356   4839   -190   -614    131       C  
ATOM   4593  CG2 VAL B 249      83.842  -0.664-157.342  1.00 35.50           C  
ANISOU 4593  CG2 VAL B 249     4542   4226   4719   -255   -643    132       C  
ATOM   4594  N   ARG B 250      86.626   2.982-158.624  1.00 30.63           N  
ANISOU 4594  N   ARG B 250     3575   3850   4215   -352   -689    117       N  
ATOM   4595  CA  ARG B 250      87.149   4.060-159.450  1.00 33.42           C  
ANISOU 4595  CA  ARG B 250     3840   4244   4613   -396   -668    111       C  
ATOM   4596  C   ARG B 250      88.506   3.631-159.971  1.00 33.79           C  
ANISOU 4596  C   ARG B 250     3776   4371   4691   -326   -673    157       C  
ATOM   4597  O   ARG B 250      89.238   2.906-159.291  1.00 35.19           O  
ANISOU 4597  O   ARG B 250     3923   4595   4852   -269   -721    195       O  
ATOM   4598  CB  ARG B 250      87.335   5.376-158.666  1.00 38.64           C  
ANISOU 4598  CB  ARG B 250     4485   4928   5270   -505   -711     91       C  
ATOM   4599  CG  ARG B 250      86.054   6.051-158.226  1.00 38.68           C  
ANISOU 4599  CG  ARG B 250     4594   4857   5246   -566   -686     50       C  
ATOM   4600  CD  ARG B 250      85.169   6.297-159.420  1.00 42.44           C  
ANISOU 4600  CD  ARG B 250     5090   5289   5748   -554   -606     41       C  
ATOM   4601  NE  ARG B 250      85.359   7.608-160.010  1.00 57.92           N  
ANISOU 4601  NE  ARG B 250     7015   7250   7741   -613   -574     32       N  
ATOM   4602  CZ  ARG B 250      84.692   8.030-161.075  1.00 55.68           C  
ANISOU 4602  CZ  ARG B 250     6739   6939   7476   -603   -506     33       C  
ATOM   4603  NH1 ARG B 250      83.813   7.224-161.659  1.00 66.15           N  
ANISOU 4603  NH1 ARG B 250     8098   8246   8789   -548   -475     35       N  
ATOM   4604  NH2 ARG B 250      84.910   9.241-161.561  1.00 53.11           N  
ANISOU 4604  NH2 ARG B 250     6392   6608   7180   -653   -472     33       N  
ATOM   4605  N   TYR B 251      88.849   4.106-161.170  1.00 31.28           N  
ANISOU 4605  N   TYR B 251     3394   4076   4416   -323   -619    163       N  
ATOM   4606  CA  TYR B 251      90.152   3.834-161.754  1.00 31.26           C  
ANISOU 4606  CA  TYR B 251     3270   4160   4446   -254   -607    214       C  
ATOM   4607  C   TYR B 251      91.111   4.971-161.463  1.00 35.23           C  
ANISOU 4607  C   TYR B 251     3649   4752   4983   -348   -649    235       C  
ATOM   4608  O   TYR B 251      90.736   6.144-161.536  1.00 35.32           O  
ANISOU 4608  O   TYR B 251     3676   4736   5008   -457   -641    203       O  
ATOM   4609  CB  TYR B 251      90.043   3.640-163.266  1.00 30.04           C  
ANISOU 4609  CB  TYR B 251     3119   3986   4309   -192   -516    214       C  
ATOM   4610  CG  TYR B 251      89.282   2.407-163.664  1.00 29.70           C  
ANISOU 4610  CG  TYR B 251     3196   3861   4228   -105   -479    194       C  
ATOM   4611  CD1 TYR B 251      89.596   1.161-163.115  1.00 29.92           C  
ANISOU 4611  CD1 TYR B 251     3260   3876   4232    -10   -497    218       C  
ATOM   4612  CD2 TYR B 251      88.235   2.481-164.573  1.00 30.26           C  
ANISOU 4612  CD2 TYR B 251     3349   3865   4283   -124   -428    153       C  
ATOM   4613  CE1 TYR B 251      88.902   0.010-163.489  1.00 33.78           C  
ANISOU 4613  CE1 TYR B 251     3879   4271   4685     56   -459    195       C  
ATOM   4614  CE2 TYR B 251      87.535   1.342-164.952  1.00 36.40           C  
ANISOU 4614  CE2 TYR B 251     4242   4568   5022    -68   -402    128       C  
ATOM   4615  CZ  TYR B 251      87.872   0.118-164.414  1.00 35.40           C  
ANISOU 4615  CZ  TYR B 251     4163   4412   4875     16   -415    146       C  
ATOM   4616  OH  TYR B 251      87.164  -1.004-164.786  1.00 32.23           O  
ANISOU 4616  OH  TYR B 251     3894   3918   4433     55   -386    117       O  
ATOM   4617  N   ALA B 252      92.356   4.608-161.156  1.00 35.45           N  
ANISOU 4617  N   ALA B 252     3555   4889   5024   -304   -691    293       N  
ATOM   4618  CA  ALA B 252      93.392   5.590-160.873  1.00 35.46           C  
ANISOU 4618  CA  ALA B 252     3418   4996   5059   -405   -741    321       C  
ATOM   4619  C   ALA B 252      93.642   6.494-162.074  1.00 38.85           C  
ANISOU 4619  C   ALA B 252     3783   5435   5543   -453   -666    329       C  
ATOM   4620  O   ALA B 252      93.530   6.078-163.229  1.00 38.10           O  
ANISOU 4620  O   ALA B 252     3695   5320   5462   -360   -576    342       O  
ATOM   4621  CB  ALA B 252      94.693   4.893-160.489  1.00 36.86           C  
ANISOU 4621  CB  ALA B 252     3451   5310   5242   -326   -792    401       C  
ATOM   4622  N   GLY B 253      93.981   7.747-161.781  1.00 37.05           N  
ANISOU 4622  N   GLY B 253     3506   5233   5340   -605   -701    319       N  
ATOM   4623  CA  GLY B 253      94.463   8.670-162.789  1.00 40.92           C  
ANISOU 4623  CA  GLY B 253     3913   5749   5886   -666   -637    343       C  
ATOM   4624  C   GLY B 253      95.851   9.155-162.437  1.00 45.00           C  
ANISOU 4624  C   GLY B 253     4251   6405   6441   -756   -698    400       C  
ATOM   4625  O   GLY B 253      96.031   9.876-161.446  1.00 43.58           O  
ANISOU 4625  O   GLY B 253     4072   6238   6249   -900   -787    373       O  
ATOM   4626  N   TYR B 254      96.845   8.745-163.219  1.00 50.26           N  
ANISOU 4626  N   TYR B 254     4763   7183   7149   -672   -651    479       N  
ATOM   4627  CA  TYR B 254      98.241   9.059-162.940  1.00 52.39           C  
ANISOU 4627  CA  TYR B 254     4826   7618   7460   -743   -707    553       C  
ATOM   4628  C   TYR B 254      98.679  10.251-163.784  1.00 60.21           C  
ANISOU 4628  C   TYR B 254     5739   8623   8513   -868   -644    577       C  
ATOM   4629  O   TYR B 254      98.853  10.128-165.001  1.00 56.04           O  
ANISOU 4629  O   TYR B 254     5168   8106   8017   -780   -530    620       O  
ATOM   4630  CB  TYR B 254      99.138   7.859-163.221  1.00 44.74           C  
ANISOU 4630  CB  TYR B 254     3718   6781   6501   -560   -686    644       C  
ATOM   4631  CG  TYR B 254      98.734   6.598-162.519  1.00 45.60           C  
ANISOU 4631  CG  TYR B 254     3914   6861   6549   -417   -727    633       C  
ATOM   4632  CD1 TYR B 254      98.789   6.500-161.128  1.00 47.66           C  
ANISOU 4632  CD1 TYR B 254     4184   7157   6767   -476   -857    620       C  
ATOM   4633  CD2 TYR B 254      98.327   5.487-163.241  1.00 45.63           C  
ANISOU 4633  CD2 TYR B 254     4002   6801   6534   -225   -635    638       C  
ATOM   4634  CE1 TYR B 254      98.433   5.331-160.490  1.00 44.18           C  
ANISOU 4634  CE1 TYR B 254     3828   6687   6270   -340   -887    621       C  
ATOM   4635  CE2 TYR B 254      97.965   4.323-162.611  1.00 42.53           C  
ANISOU 4635  CE2 TYR B 254     3703   6368   6090   -100   -664    632       C  
ATOM   4636  CZ  TYR B 254      98.025   4.245-161.235  1.00 43.35           C  
ANISOU 4636  CZ  TYR B 254     3807   6508   6157   -154   -787    629       C  
ATOM   4637  OH  TYR B 254      97.663   3.073-160.616  1.00 43.03           O  
ANISOU 4637  OH  TYR B 254     3865   6421   6062    -26   -808    632       O  
ATOM   4638  N   ARG B 255      98.861  11.400-163.133  1.00 65.09           N  
ANISOU 4638  N   ARG B 255     6352   9236   9143  -1076   -714    547       N  
ATOM   4639  CA  ARG B 255      99.528  12.526-163.769  1.00 68.89           C  
ANISOU 4639  CA  ARG B 255     6734   9752   9690  -1220   -670    585       C  
ATOM   4640  C   ARG B 255     100.880  12.084-164.302  1.00 72.21           C  
ANISOU 4640  C   ARG B 255     6919  10359  10158  -1152   -642    697       C  
ATOM   4641  O   ARG B 255     101.505  11.160-163.776  1.00 77.38           O  
ANISOU 4641  O   ARG B 255     7472  11135  10793  -1050   -702    740       O  
ATOM   4642  CB  ARG B 255      99.710  13.672-162.772  1.00 78.80           C  
ANISOU 4642  CB  ARG B 255     8050  10966  10925  -1433   -756    519       C  
ATOM   4643  CG  ARG B 255      98.710  14.803-162.914  1.00 82.97           C  
ANISOU 4643  CG  ARG B 255     8769  11308  11449  -1549   -708    443       C  
ATOM   4644  CD  ARG B 255      99.164  15.811-163.956  1.00 91.45           C  
ANISOU 4644  CD  ARG B 255     9804  12359  12583  -1627   -602    478       C  
ATOM   4645  NE  ARG B 255      98.247  15.903-165.090  1.00 97.46           N  
ANISOU 4645  NE  ARG B 255    10639  13022  13370  -1559   -485    497       N  
ATOM   4646  CZ  ARG B 255      97.079  16.537-165.058  1.00 98.08           C  
ANISOU 4646  CZ  ARG B 255    10924  12925  13416  -1581   -446    426       C  
ATOM   4647  NH1 ARG B 255      96.673  17.128-163.941  1.00 98.85           N  
ANISOU 4647  NH1 ARG B 255    11147  12935  13476  -1706   -525    349       N  
ATOM   4648  NH2 ARG B 255      96.313  16.578-166.139  1.00 95.24           N  
ANISOU 4648  NH2 ARG B 255    10647  12483  13056  -1470   -328    434       N  
ATOM   4649  N   GLN B 256     101.340  12.742-165.357  1.00 84.16           N  
ANISOU 4649  N   GLN B 256     8370  11883  11723  -1185   -536    740       N  
ATOM   4650  CA  GLN B 256     102.620  12.374-165.937  1.00 96.62           C  
ANISOU 4650  CA  GLN B 256     9752  13622  13336  -1101   -485    838       C  
ATOM   4651  C   GLN B 256     103.309  13.623-166.469  1.00103.55           C  
ANISOU 4651  C   GLN B 256    10584  14501  14259  -1254   -428    854       C  
ATOM   4652  O   GLN B 256     102.843  14.751-166.279  1.00104.23           O  
ANISOU 4652  O   GLN B 256    10794  14462  14348  -1423   -437    785       O  
ATOM   4653  CB  GLN B 256     102.442  11.330-167.047  1.00 95.67           C  
ANISOU 4653  CB  GLN B 256     9584  13538  13229   -877   -368    909       C  
ATOM   4654  CG  GLN B 256     102.160   9.922-166.565  1.00 94.60           C  
ANISOU 4654  CG  GLN B 256     9483  13419  13043   -685   -408    904       C  
ATOM   4655  CD  GLN B 256     102.169   8.922-167.700  1.00 91.63           C  
ANISOU 4655  CD  GLN B 256     9116  13044  12653   -445   -272    947       C  
ATOM   4656  OE1 GLN B 256     102.332   9.288-168.863  1.00 93.03           O  
ANISOU 4656  OE1 GLN B 256     9267  13222  12857   -423   -150    983       O  
ATOM   4657  NE2 GLN B 256     101.996   7.650-167.368  1.00 87.23           N  
ANISOU 4657  NE2 GLN B 256     8613  12483  12048   -265   -288    942       N  
ATOM   4658  N   GLN B 257     104.452  13.400-167.110  1.00107.26           N  
ANISOU 4658  N   GLN B 257    10877  15111  14764  -1188   -366    948       N  
ATOM   4659  CA  GLN B 257     105.134  14.377-167.951  1.00105.76           C  
ANISOU 4659  CA  GLN B 257    10622  14937  14625  -1287   -276    990       C  
ATOM   4660  C   GLN B 257     105.628  13.570-169.141  1.00104.01           C  
ANISOU 4660  C   GLN B 257    10280  14818  14421  -1085   -145   1094       C  
ATOM   4661  O   GLN B 257     106.540  12.753-168.978  1.00109.13           O  
ANISOU 4661  O   GLN B 257    10781  15615  15068   -969   -161   1162       O  
ATOM   4662  CB  GLN B 257     106.286  15.058-167.208  1.00106.96           C  
ANISOU 4662  CB  GLN B 257    10665  15179  14797  -1453   -362    996       C  
ATOM   4663  CG  GLN B 257     105.869  15.835-165.956  1.00106.58           C  
ANISOU 4663  CG  GLN B 257    10748  15029  14717  -1645   -491    887       C  
ATOM   4664  CD  GLN B 257     106.676  15.450-164.725  1.00109.44           C  
ANISOU 4664  CD  GLN B 257    11011  15521  15051  -1675   -636    888       C  
ATOM   4665  OE1 GLN B 257     106.930  14.270-164.481  1.00110.93           O  
ANISOU 4665  OE1 GLN B 257    11110  15823  15214  -1509   -669    939       O  
ATOM   4666  NE2 GLN B 257     107.090  16.449-163.946  1.00106.72           N  
ANISOU 4666  NE2 GLN B 257    10687  15158  14705  -1884   -720    836       N  
ATOM   4667  N   ASP B 258     105.058  13.765-170.334  1.00 99.79           N  
ANISOU 4667  N   ASP B 258     9812  14208  13897  -1028    -10   1112       N  
ATOM   4668  CA  ASP B 258     104.351  14.952-170.848  1.00 99.55           C  
ANISOU 4668  CA  ASP B 258     9913  14029  13882  -1167     49   1072       C  
ATOM   4669  C   ASP B 258     102.941  15.364-170.380  1.00 95.16           C  
ANISOU 4669  C   ASP B 258     9563  13295  13300  -1246      1    974       C  
ATOM   4670  O   ASP B 258     102.002  15.321-171.178  1.00 97.13           O  
ANISOU 4670  O   ASP B 258     9911  13453  13540  -1173     88    975       O  
ATOM   4671  CB  ASP B 258     104.254  14.773-172.367  1.00 99.77           C  
ANISOU 4671  CB  ASP B 258     9932  14062  13915  -1027    220   1143       C  
ATOM   4672  CG  ASP B 258     103.858  13.347-172.760  1.00 97.69           C  
ANISOU 4672  CG  ASP B 258     9666  13838  13614   -779    265   1167       C  
ATOM   4673  OD1 ASP B 258     104.539  12.746-173.619  1.00 98.01           O  
ANISOU 4673  OD1 ASP B 258     9611  13978  13650   -619    370   1245       O  
ATOM   4674  OD2 ASP B 258     102.883  12.815-172.184  1.00 95.08           O  
ANISOU 4674  OD2 ASP B 258     9436  13435  13255   -741    197   1105       O  
ATOM   4675  N   GLY B 259     102.788  15.805-169.134  1.00 89.77           N  
ANISOU 4675  N   GLY B 259     8947  12559  12601  -1391   -129    894       N  
ATOM   4676  CA  GLY B 259     101.550  16.405-168.661  1.00 90.18           C  
ANISOU 4676  CA  GLY B 259     9203  12433  12627  -1483   -164    801       C  
ATOM   4677  C   GLY B 259     100.263  15.601-168.757  1.00 86.90           C  
ANISOU 4677  C   GLY B 259     8897  11942  12177  -1351   -159    774       C  
ATOM   4678  O   GLY B 259      99.292  15.915-168.061  1.00 90.68           O  
ANISOU 4678  O   GLY B 259     9554  12284  12615  -1403   -214    682       O  
ATOM   4679  N   SER B 260     100.228  14.576-169.607  1.00 74.37           N  
ANISOU 4679  N   SER B 260     7283  10404  10570  -1137    -80    812       N  
ATOM   4680  CA  SER B 260      99.003  13.828-169.846  1.00 73.64           C  
ANISOU 4680  CA  SER B 260     7372  10199  10407   -975    -55    743       C  
ATOM   4681  C   SER B 260      98.731  12.830-168.722  1.00 75.64           C  
ANISOU 4681  C   SER B 260     7660  10464  10617   -911   -170    691       C  
ATOM   4682  O   SER B 260      99.645  12.360-168.039  1.00 83.55           O  
ANISOU 4682  O   SER B 260     8515  11595  11634   -915   -245    731       O  
ATOM   4683  CB  SER B 260      99.079  13.089-171.182  1.00 76.12           C  
ANISOU 4683  CB  SER B 260     7665  10552  10703   -782     71    794       C  
ATOM   4684  OG  SER B 260     100.083  12.090-171.153  1.00 78.15           O  
ANISOU 4684  OG  SER B 260     7760  10961  10971   -665     69    860       O  
ATOM   4685  N   VAL B 261      97.453  12.506-168.543  1.00 61.55           N  
ANISOU 4685  N   VAL B 261     6065   8549   8774   -850   -180    608       N  
ATOM   4686  CA  VAL B 261      97.013  11.586-167.501  1.00 52.12           C  
ANISOU 4686  CA  VAL B 261     4934   7339   7531   -791   -276    556       C  
ATOM   4687  C   VAL B 261      96.927  10.187-168.090  1.00 49.50           C  
ANISOU 4687  C   VAL B 261     4611   7034   7165   -580   -227    574       C  
ATOM   4688  O   VAL B 261      96.406  10.002-169.195  1.00 46.55           O  
ANISOU 4688  O   VAL B 261     4310   6607   6769   -488   -130    569       O  
ATOM   4689  CB  VAL B 261      95.659  12.029-166.921  1.00 47.61           C  
ANISOU 4689  CB  VAL B 261     4560   6614   6917   -851   -310    464       C  
ATOM   4690  CG1 VAL B 261      95.107  10.975-165.969  1.00 47.69           C  
ANISOU 4690  CG1 VAL B 261     4645   6604   6873   -773   -389    417       C  
ATOM   4691  CG2 VAL B 261      95.811  13.350-166.205  1.00 57.01           C  
ANISOU 4691  CG2 VAL B 261     5762   7767   8131  -1054   -361    440       C  
ATOM   4692  N   ARG B 262      97.446   9.199-167.367  1.00 49.02           N  
ANISOU 4692  N   ARG B 262     4485   7051   7092   -501   -292    595       N  
ATOM   4693  CA  ARG B 262      97.250   7.798-167.723  1.00 47.67           C  
ANISOU 4693  CA  ARG B 262     4365   6871   6878   -302   -252    598       C  
ATOM   4694  C   ARG B 262      96.158   7.237-166.823  1.00 50.20           C  
ANISOU 4694  C   ARG B 262     4848   7083   7142   -292   -324    519       C  
ATOM   4695  O   ARG B 262      96.273   7.298-165.594  1.00 44.07           O  
ANISOU 4695  O   ARG B 262     4055   6329   6360   -363   -429    507       O  
ATOM   4696  CB  ARG B 262      98.543   6.996-167.579  1.00 48.94           C  
ANISOU 4696  CB  ARG B 262     4353   7184   7059   -191   -257    688       C  
ATOM   4697  CG  ARG B 262      98.401   5.526-167.982  1.00 52.28           C  
ANISOU 4697  CG  ARG B 262     4850   7579   7434     27   -199    693       C  
ATOM   4698  CD  ARG B 262      99.749   4.925-168.340  1.00 59.33           C  
ANISOU 4698  CD  ARG B 262     5563   8625   8354    167   -146    803       C  
ATOM   4699  NE  ARG B 262      99.721   3.465-168.328  1.00 70.67           N  
ANISOU 4699  NE  ARG B 262     7076  10032   9742    374   -115    811       N  
ATOM   4700  CZ  ARG B 262      99.422   2.708-169.379  1.00 74.14           C  
ANISOU 4700  CZ  ARG B 262     7632  10397  10140    527      0    796       C  
ATOM   4701  NH1 ARG B 262      99.116   3.269-170.541  1.00 73.10           N  
ANISOU 4701  NH1 ARG B 262     7542  10228  10005    501     91    774       N  
ATOM   4702  NH2 ARG B 262      99.428   1.387-169.268  1.00 78.69           N  
ANISOU 4702  NH2 ARG B 262     8294  10933  10672    705     26    801       N  
ATOM   4703  N   GLY B 263      95.093   6.717-167.429  1.00 41.98           N  
ANISOU 4703  N   GLY B 263     3962   5932   6056   -213   -270    468       N  
ATOM   4704  CA  GLY B 263      93.947   6.305-166.639  1.00 37.92           C  
ANISOU 4704  CA  GLY B 263     3600   5314   5495   -224   -329    397       C  
ATOM   4705  C   GLY B 263      92.851   7.347-166.668  1.00 39.86           C  
ANISOU 4705  C   GLY B 263     3948   5464   5734   -343   -327    340       C  
ATOM   4706  O   GLY B 263      92.680   8.049-167.671  1.00 36.58           O  
ANISOU 4706  O   GLY B 263     3535   5031   5331   -364   -255    346       O  
ATOM   4707  N   ASP B 264      92.108   7.480-165.576  1.00 30.96           N  
ANISOU 4707  N   ASP B 264     2906   4276   4581   -410   -399    291       N  
ATOM   4708  CA  ASP B 264      90.916   8.318-165.585  1.00 31.10           C  
ANISOU 4708  CA  ASP B 264     3036   4197   4584   -489   -384    240       C  
ATOM   4709  C   ASP B 264      91.263   9.701-165.059  1.00 38.20           C  
ANISOU 4709  C   ASP B 264     3901   5099   5515   -635   -412    238       C  
ATOM   4710  O   ASP B 264      91.535   9.843-163.853  1.00 37.30           O  
ANISOU 4710  O   ASP B 264     3781   5001   5392   -706   -496    223       O  
ATOM   4711  CB  ASP B 264      89.810   7.674-164.744  1.00 30.41           C  
ANISOU 4711  CB  ASP B 264     3073   4036   4447   -472   -428    192       C  
ATOM   4712  CG  ASP B 264      88.468   8.353-164.902  1.00 30.94           C  
ANISOU 4712  CG  ASP B 264     3248   4015   4493   -517   -398    152       C  
ATOM   4713  OD1 ASP B 264      88.425   9.535-165.333  1.00 32.77           O  
ANISOU 4713  OD1 ASP B 264     3472   4230   4749   -582   -359    157       O  
ATOM   4714  OD2 ASP B 264      87.440   7.706-164.580  1.00 32.37           O  
ANISOU 4714  OD2 ASP B 264     3522   4143   4634   -486   -409    122       O  
ATOM   4715  N   PRO B 265      91.250  10.744-165.898  1.00 38.12           N  
ANISOU 4715  N   PRO B 265     3883   5068   5535   -688   -345    252       N  
ATOM   4716  CA  PRO B 265      91.605  12.087-165.407  1.00 34.93           C  
ANISOU 4716  CA  PRO B 265     3466   4646   5161   -840   -365    248       C  
ATOM   4717  C   PRO B 265      90.676  12.613-164.332  1.00 36.47           C  
ANISOU 4717  C   PRO B 265     3794   4745   5319   -912   -409    186       C  
ATOM   4718  O   PRO B 265      91.064  13.524-163.598  1.00 43.19           O  
ANISOU 4718  O   PRO B 265     4653   5580   6179  -1041   -449    168       O  
ATOM   4719  CB  PRO B 265      91.531  12.959-166.672  1.00 36.80           C  
ANISOU 4719  CB  PRO B 265     3702   4854   5428   -852   -263    279       C  
ATOM   4720  CG  PRO B 265      91.623  11.982-167.822  1.00 37.22           C  
ANISOU 4720  CG  PRO B 265     3712   4958   5471   -708   -202    313       C  
ATOM   4721  CD  PRO B 265      90.903  10.763-167.333  1.00 33.06           C  
ANISOU 4721  CD  PRO B 265     3257   4411   4893   -616   -247    273       C  
ATOM   4722  N   ALA B 266      89.461  12.083-164.207  1.00 32.14           N  
ANISOU 4722  N   ALA B 266     3353   4133   4724   -837   -399    152       N  
ATOM   4723  CA  ALA B 266      88.580  12.554-163.155  1.00 33.59           C  
ANISOU 4723  CA  ALA B 266     3659   4235   4870   -890   -428    101       C  
ATOM   4724  C   ALA B 266      89.116  12.217-161.763  1.00 36.40           C  
ANISOU 4724  C   ALA B 266     4004   4627   5199   -941   -531     79       C  
ATOM   4725  O   ALA B 266      88.693  12.840-160.785  1.00 40.80           O  
ANISOU 4725  O   ALA B 266     4658   5123   5721  -1014   -560     35       O  
ATOM   4726  CB  ALA B 266      87.188  11.955-163.331  1.00 30.59           C  
ANISOU 4726  CB  ALA B 266     3371   3802   4450   -798   -395     84       C  
ATOM   4727  N   ASN B 267      90.034  11.251-161.662  1.00 36.09           N  
ANISOU 4727  N   ASN B 267     3857   4688   5167   -895   -583    111       N  
ATOM   4728  CA  ASN B 267      90.445  10.667-160.386  1.00 39.50           C  
ANISOU 4728  CA  ASN B 267     4279   5169   5561   -907   -683    102       C  
ATOM   4729  C   ASN B 267      91.896  10.999-160.041  1.00 45.51           C  
ANISOU 4729  C   ASN B 267     4904   6041   6350   -995   -755    134       C  
ATOM   4730  O   ASN B 267      92.504  10.327-159.200  1.00 37.25           O  
ANISOU 4730  O   ASN B 267     3802   5077   5276   -979   -842    152       O  
ATOM   4731  CB  ASN B 267      90.216   9.148-160.413  1.00 33.39           C  
ANISOU 4731  CB  ASN B 267     3503   4418   4764   -766   -688    123       C  
ATOM   4732  CG  ASN B 267      88.752   8.789-160.623  1.00 38.27           C  
ANISOU 4732  CG  ASN B 267     4251   4938   5351   -706   -634     91       C  
ATOM   4733  OD1 ASN B 267      87.863   9.495-160.140  1.00 39.15           O  
ANISOU 4733  OD1 ASN B 267     4462   4975   5437   -762   -623     52       O  
ATOM   4734  ND2 ASN B 267      88.488   7.696-161.359  1.00 30.82           N  
ANISOU 4734  ND2 ASN B 267     3308   3995   4408   -595   -595    109       N  
ATOM   4735  N   VAL B 268      92.456  12.042-160.661  1.00 44.44           N  
ANISOU 4735  N   VAL B 268     4709   5913   6264  -1091   -721    149       N  
ATOM   4736  CA  VAL B 268      93.843  12.424-160.379  1.00 46.51           C  
ANISOU 4736  CA  VAL B 268     4824   6291   6558  -1198   -790    185       C  
ATOM   4737  C   VAL B 268      94.020  12.797-158.909  1.00 47.30           C  
ANISOU 4737  C   VAL B 268     4971   6399   6601  -1322   -908    140       C  
ATOM   4738  O   VAL B 268      94.998  12.394-158.264  1.00 43.66           O  
ANISOU 4738  O   VAL B 268     4391   6068   6129  -1348  -1008    173       O  
ATOM   4739  CB  VAL B 268      94.281  13.574-161.307  1.00 44.37           C  
ANISOU 4739  CB  VAL B 268     4502   6005   6350  -1300   -721    207       C  
ATOM   4740  CG1 VAL B 268      95.589  14.181-160.820  1.00 50.83           C  
ANISOU 4740  CG1 VAL B 268     5187   6930   7196  -1462   -804    234       C  
ATOM   4741  CG2 VAL B 268      94.442  13.066-162.732  1.00 42.92           C  
ANISOU 4741  CG2 VAL B 268     4235   5860   6214  -1172   -619    269       C  
ATOM   4742  N   GLU B 269      93.083  13.572-158.357  1.00 43.18           N  
ANISOU 4742  N   GLU B 269     4627   5745   6036  -1393   -897     66       N  
ATOM   4743  CA  GLU B 269      93.260  14.094-157.005  1.00 48.65           C  
ANISOU 4743  CA  GLU B 269     5390   6432   6664  -1526  -1001     12       C  
ATOM   4744  C   GLU B 269      93.171  12.978-155.963  1.00 40.83           C  
ANISOU 4744  C   GLU B 269     4408   5503   5602  -1442  -1088     13       C  
ATOM   4745  O   GLU B 269      94.008  12.892-155.055  1.00 40.57           O  
ANISOU 4745  O   GLU B 269     4311   5574   5530  -1517  -1208     19       O  
ATOM   4746  CB  GLU B 269      92.220  15.185-156.738  1.00 56.65           C  
ANISOU 4746  CB  GLU B 269     6610   7274   7643  -1597   -944    -64       C  
ATOM   4747  CG  GLU B 269      92.483  16.020-155.497  1.00 70.02           C  
ANISOU 4747  CG  GLU B 269     8403   8936   9267  -1754  -1027   -132       C  
ATOM   4748  CD  GLU B 269      91.596  17.253-155.425  1.00 82.47           C  
ANISOU 4748  CD  GLU B 269    10184  10330  10820  -1813   -941   -199       C  
ATOM   4749  OE1 GLU B 269      90.577  17.300-156.147  1.00 83.24           O  
ANISOU 4749  OE1 GLU B 269    10352  10334  10942  -1721   -833   -190       O  
ATOM   4750  OE2 GLU B 269      91.925  18.178-154.647  1.00 88.79           O  
ANISOU 4750  OE2 GLU B 269    11076  11085  11575  -1918   -965   -258       O  
ATOM   4751  N   ILE B 270      92.168  12.106-156.087  1.00 41.85           N  
ANISOU 4751  N   ILE B 270     4615   5576   5710  -1291  -1032     12       N  
ATOM   4752  CA  ILE B 270      92.021  10.995-155.149  1.00 47.42           C  
ANISOU 4752  CA  ILE B 270     5343   6325   6350  -1202  -1099     21       C  
ATOM   4753  C   ILE B 270      93.169  10.006-155.309  1.00 46.37           C  
ANISOU 4753  C   ILE B 270     5028   6346   6243  -1126  -1155    102       C  
ATOM   4754  O   ILE B 270      93.631   9.407-154.326  1.00 39.12           O  
ANISOU 4754  O   ILE B 270     4081   5513   5269  -1108  -1253    123       O  
ATOM   4755  CB  ILE B 270      90.644  10.317-155.334  1.00 45.67           C  
ANISOU 4755  CB  ILE B 270     5245   6000   6109  -1074  -1015      7       C  
ATOM   4756  CG1 ILE B 270      90.420   9.232-154.285  1.00 38.67           C  
ANISOU 4756  CG1 ILE B 270     4404   5139   5150   -996  -1076     17       C  
ATOM   4757  CG2 ILE B 270      90.490   9.728-156.747  1.00 38.47           C  
ANISOU 4757  CG2 ILE B 270     4267   5084   5267   -961   -923     49       C  
ATOM   4758  CD1 ILE B 270      90.486   9.764-152.845  1.00 45.26           C  
ANISOU 4758  CD1 ILE B 270     5325   5977   5894  -1098  -1167    -28       C  
ATOM   4759  N   THR B 271      93.664   9.833-156.533  1.00 41.14           N  
ANISOU 4759  N   THR B 271     4243   5726   5660  -1070  -1089    154       N  
ATOM   4760  CA  THR B 271      94.835   8.992-156.747  1.00 41.66           C  
ANISOU 4760  CA  THR B 271     4128   5945   5755   -988  -1126    239       C  
ATOM   4761  C   THR B 271      96.039   9.526-155.981  1.00 43.10           C  
ANISOU 4761  C   THR B 271     4181   6268   5928  -1122  -1249    264       C  
ATOM   4762  O   THR B 271      96.753   8.763-155.324  1.00 45.88           O  
ANISOU 4762  O   THR B 271     4437   6747   6248  -1065  -1337    319       O  
ATOM   4763  CB  THR B 271      95.153   8.903-158.238  1.00 36.35           C  
ANISOU 4763  CB  THR B 271     3359   5290   5165   -917  -1020    287       C  
ATOM   4764  OG1 THR B 271      94.031   8.347-158.928  1.00 37.69           O  
ANISOU 4764  OG1 THR B 271     3651   5339   5331   -800   -921    261       O  
ATOM   4765  CG2 THR B 271      96.381   8.036-158.474  1.00 41.12           C  
ANISOU 4765  CG2 THR B 271     3773   6053   5797   -812  -1042    383       C  
ATOM   4766  N   GLU B 272      96.286  10.837-156.065  1.00 47.39           N  
ANISOU 4766  N   GLU B 272     4720   6792   6494  -1304  -1260    227       N  
ATOM   4767  CA  GLU B 272      97.430  11.421-155.364  1.00 48.79           C  
ANISOU 4767  CA  GLU B 272     4797   7087   6654  -1437  -1359    234       C  
ATOM   4768  C   GLU B 272      97.282  11.280-153.855  1.00 48.87           C  
ANISOU 4768  C   GLU B 272     4909   7105   6555  -1468  -1469    186       C  
ATOM   4769  O   GLU B 272      98.267  11.051-153.139  1.00 50.62           O  
ANISOU 4769  O   GLU B 272     5029   7463   6742  -1477  -1560    218       O  
ATOM   4770  CB  GLU B 272      97.592  12.896-155.742  1.00 63.63           C  
ANISOU 4770  CB  GLU B 272     6722   8885   8568  -1595  -1302    179       C  
ATOM   4771  CG  GLU B 272      97.957  13.141-157.203  1.00 78.14           C  
ANISOU 4771  CG  GLU B 272     8443  10737  10508  -1578  -1196    237       C  
ATOM   4772  CD  GLU B 272      97.923  14.616-157.590  1.00 93.63           C  
ANISOU 4772  CD  GLU B 272    10484  12589  12501  -1729  -1130    184       C  
ATOM   4773  OE1 GLU B 272      97.536  15.454-156.745  1.00100.16           O  
ANISOU 4773  OE1 GLU B 272    11470  13314  13272  -1840  -1161     99       O  
ATOM   4774  OE2 GLU B 272      98.284  14.936-158.745  1.00 95.61           O  
ANISOU 4774  OE2 GLU B 272    10646  12852  12830  -1731  -1042    233       O  
ATOM   4775  N   LEU B 273      96.055  11.427-153.349  1.00 41.02           N  
ANISOU 4775  N   LEU B 273     4116   5968   5502  -1483  -1460    113       N  
ATOM   4776  CA  LEU B 273      95.821  11.256-151.919  1.00 45.32           C  
ANISOU 4776  CA  LEU B 273     4774   6515   5932  -1502  -1553     71       C  
ATOM   4777  C   LEU B 273      96.081   9.823-151.483  1.00 46.03           C  
ANISOU 4777  C   LEU B 273     4778   6726   5988  -1358  -1628    152       C  
ATOM   4778  O   LEU B 273      96.571   9.588-150.373  1.00 53.21           O  
ANISOU 4778  O   LEU B 273     5682   7723   6814  -1365  -1728    156       O  
ATOM   4779  CB  LEU B 273      94.391  11.657-151.576  1.00 44.61           C  
ANISOU 4779  CB  LEU B 273     4915   6244   5788  -1526  -1506    -13       C  
ATOM   4780  CG  LEU B 273      94.165  13.159-151.573  1.00 50.14           C  
ANISOU 4780  CG  LEU B 273     5741   6822   6487  -1667  -1449   -100       C  
ATOM   4781  CD1 LEU B 273      92.682  13.456-151.538  1.00 50.20           C  
ANISOU 4781  CD1 LEU B 273     5956   6655   6464  -1650  -1370   -160       C  
ATOM   4782  CD2 LEU B 273      94.906  13.765-150.380  1.00 46.63           C  
ANISOU 4782  CD2 LEU B 273     5326   6429   5960  -1779  -1543   -146       C  
ATOM   4783  N   CYS B 274      95.721   8.848-152.322  1.00 40.20           N  
ANISOU 4783  N   CYS B 274     4012   5959   5303  -1180  -1534    203       N  
ATOM   4784  CA  CYS B 274      95.994   7.457-151.978  1.00 40.12           C  
ANISOU 4784  CA  CYS B 274     3947   6033   5264  -1007  -1565    280       C  
ATOM   4785  C   CYS B 274      97.494   7.200-151.904  1.00 47.60           C  
ANISOU 4785  C   CYS B 274     4662   7195   6231  -1003  -1660    376       C  
ATOM   4786  O   CYS B 274      97.975   6.542-150.970  1.00 51.67           O  
ANISOU 4786  O   CYS B 274     5132   7822   6677   -950  -1762    427       O  
ATOM   4787  CB  CYS B 274      95.328   6.517-152.988  1.00 39.98           C  
ANISOU 4787  CB  CYS B 274     3968   5924   5301   -827  -1430    305       C  
ATOM   4788  SG  CYS B 274      93.525   6.379-152.828  1.00 45.08           S  
ANISOU 4788  SG  CYS B 274     4865   6358   5903   -793  -1340    223       S  
ATOM   4789  N   ILE B 275      98.252   7.722-152.872  1.00 48.64           N  
ANISOU 4789  N   ILE B 275     4635   7394   6454  -1057  -1626    409       N  
ATOM   4790  CA  ILE B 275      99.709   7.596-152.840  1.00 49.00           C  
ANISOU 4790  CA  ILE B 275     4475   7622   6520  -1036  -1668    486       C  
ATOM   4791  C   ILE B 275     100.272   8.274-151.595  1.00 56.95           C  
ANISOU 4791  C   ILE B 275     5505   8686   7447  -1173  -1778    437       C  
ATOM   4792  O   ILE B 275     101.080   7.695-150.857  1.00 63.12           O  
ANISOU 4792  O   ILE B 275     6191   9610   8182  -1113  -1865    496       O  
ATOM   4793  CB  ILE B 275     100.324   8.180-154.125  1.00 52.55           C  
ANISOU 4793  CB  ILE B 275     4793   8096   7077  -1070  -1574    513       C  
ATOM   4794  CG1 ILE B 275      99.658   7.573-155.359  1.00 51.27           C  
ANISOU 4794  CG1 ILE B 275     4630   7865   6985   -941  -1462    551       C  
ATOM   4795  CG2 ILE B 275     101.823   7.923-154.172  1.00 57.61           C  
ANISOU 4795  CG2 ILE B 275     5215   8928   7745  -1024  -1602    605       C  
ATOM   4796  CD1 ILE B 275     100.299   7.992-156.651  1.00 49.65           C  
ANISOU 4796  CD1 ILE B 275     4290   7698   6875   -944  -1360    593       C  
ATOM   4797  N   GLN B 276      99.842   9.514-151.343  1.00 49.13           N  
ANISOU 4797  N   GLN B 276     4648   7581   6436  -1352  -1774    329       N  
ATOM   4798  CA  GLN B 276     100.282  10.252-150.165  1.00 53.57           C  
ANISOU 4798  CA  GLN B 276     5260   8175   6917  -1494  -1874    269       C  
ATOM   4799  C   GLN B 276     100.014   9.477-148.878  1.00 57.28           C  
ANISOU 4799  C   GLN B 276     5810   8686   7269  -1425  -1973    273       C  
ATOM   4800  O   GLN B 276     100.754   9.621-147.897  1.00 63.65           O  
ANISOU 4800  O   GLN B 276     6581   9598   8006  -1482  -2079    271       O  
ATOM   4801  CB  GLN B 276      99.589  11.621-150.138  1.00 59.57           C  
ANISOU 4801  CB  GLN B 276     6200   8764   7668  -1663  -1829    150       C  
ATOM   4802  CG  GLN B 276      99.626  12.346-148.791  1.00 79.06           C  
ANISOU 4802  CG  GLN B 276     8799  11212  10027  -1797  -1921     66       C  
ATOM   4803  CD  GLN B 276      98.807  13.631-148.784  1.00 82.36           C  
ANISOU 4803  CD  GLN B 276     9423  11437  10432  -1932  -1856    -48       C  
ATOM   4804  OE1 GLN B 276      98.691  14.314-149.803  1.00 78.44           O  
ANISOU 4804  OE1 GLN B 276     8922  10858  10024  -1978  -1759    -58       O  
ATOM   4805  NE2 GLN B 276      98.227  13.959-147.633  1.00 85.90           N  
ANISOU 4805  NE2 GLN B 276    10060  11813  10767  -1985  -1902   -128       N  
ATOM   4806  N   HIS B 277      98.976   8.641-148.865  1.00 49.76           N  
ANISOU 4806  N   HIS B 277     4964   7654   6289  -1304  -1943    283       N  
ATOM   4807  CA  HIS B 277      98.640   7.812-147.718  1.00 51.99           C  
ANISOU 4807  CA  HIS B 277     5331   7965   6458  -1221  -2023    299       C  
ATOM   4808  C   HIS B 277      99.176   6.393-147.846  1.00 59.44           C  
ANISOU 4808  C   HIS B 277     6131   9038   7415  -1019  -2045    431       C  
ATOM   4809  O   HIS B 277      98.603   5.462-147.270  1.00 64.08           O  
ANISOU 4809  O   HIS B 277     6806   9609   7933   -903  -2071    467       O  
ATOM   4810  CB  HIS B 277      97.127   7.804-147.501  1.00 49.60           C  
ANISOU 4810  CB  HIS B 277     5255   7483   6105  -1221  -1979    232       C  
ATOM   4811  CG  HIS B 277      96.621   9.055-146.859  1.00 54.66           C  
ANISOU 4811  CG  HIS B 277     6074   8011   6683  -1388  -1978    107       C  
ATOM   4812  ND1 HIS B 277      96.332  10.197-147.576  1.00 54.71           N  
ANISOU 4812  ND1 HIS B 277     6131   7901   6755  -1503  -1893     36       N  
ATOM   4813  CD2 HIS B 277      96.408   9.364-145.557  1.00 63.14           C  
ANISOU 4813  CD2 HIS B 277     7290   9071   7629  -1450  -2047     47       C  
ATOM   4814  CE1 HIS B 277      95.940  11.147-146.745  1.00 64.92           C  
ANISOU 4814  CE1 HIS B 277     7596   9105   7967  -1622  -1906    -63       C  
ATOM   4815  NE2 HIS B 277      95.980  10.668-145.514  1.00 61.73           N  
ANISOU 4815  NE2 HIS B 277     7250   8762   7443  -1596  -1999    -61       N  
ATOM   4816  N   GLY B 278     100.263   6.210-148.586  1.00 64.68           N  
ANISOU 4816  N   GLY B 278     6586   9826   8164   -966  -2025    510       N  
ATOM   4817  CA  GLY B 278     100.992   4.962-148.550  1.00 65.19           C  
ANISOU 4817  CA  GLY B 278     6510  10030   8230   -769  -2046    639       C  
ATOM   4818  C   GLY B 278     100.615   3.929-149.587  1.00 60.79           C  
ANISOU 4818  C   GLY B 278     5921   9432   7744   -577  -1945    720       C  
ATOM   4819  O   GLY B 278     101.113   2.800-149.513  1.00 62.07           O  
ANISOU 4819  O   GLY B 278     6002   9684   7899   -384  -1947    829       O  
ATOM   4820  N   TRP B 279      99.757   4.263-150.549  1.00 53.53           N  
ANISOU 4820  N   TRP B 279     5071   8375   6891   -614  -1854    672       N  
ATOM   4821  CA  TRP B 279      99.412   3.305-151.588  1.00 48.17           C  
ANISOU 4821  CA  TRP B 279     4417   7605   6278   -414  -1706    711       C  
ATOM   4822  C   TRP B 279     100.540   3.209-152.599  1.00 50.72           C  
ANISOU 4822  C   TRP B 279     4509   8068   6694   -347  -1664    805       C  
ATOM   4823  O   TRP B 279     101.093   4.222-153.031  1.00 55.00           O  
ANISOU 4823  O   TRP B 279     4941   8669   7289   -494  -1670    785       O  
ATOM   4824  CB  TRP B 279      98.117   3.704-152.296  1.00 45.61           C  
ANISOU 4824  CB  TRP B 279     4282   7060   5988   -458  -1583    603       C  
ATOM   4825  CG  TRP B 279      97.667   2.715-153.355  1.00 41.52           C  
ANISOU 4825  CG  TRP B 279     3817   6437   5523   -271  -1438    627       C  
ATOM   4826  CD1 TRP B 279      97.435   1.376-153.183  1.00 42.34           C  
ANISOU 4826  CD1 TRP B 279     3995   6497   5594    -81  -1401    677       C  
ATOM   4827  CD2 TRP B 279      97.378   2.996-154.731  1.00 42.70           C  
ANISOU 4827  CD2 TRP B 279     3968   6504   5754   -265  -1313    598       C  
ATOM   4828  NE1 TRP B 279      97.033   0.808-154.360  1.00 43.99           N  
ANISOU 4828  NE1 TRP B 279     4256   6599   5860     32  -1265    674       N  
ATOM   4829  CE2 TRP B 279      96.980   1.780-155.330  1.00 39.21           C  
ANISOU 4829  CE2 TRP B 279     3604   5973   5319    -75  -1211    625       C  
ATOM   4830  CE3 TRP B 279      97.417   4.154-155.516  1.00 50.66           C  
ANISOU 4830  CE3 TRP B 279     4927   7499   6823   -402  -1275    554       C  
ATOM   4831  CZ2 TRP B 279      96.629   1.690-156.672  1.00 42.37           C  
ANISOU 4831  CZ2 TRP B 279     4034   6285   5778    -22  -1083    604       C  
ATOM   4832  CZ3 TRP B 279      97.062   4.065-156.844  1.00 44.88           C  
ANISOU 4832  CZ3 TRP B 279     4219   6683   6152   -339  -1144    543       C  
ATOM   4833  CH2 TRP B 279      96.677   2.842-157.412  1.00 44.65           C  
ANISOU 4833  CH2 TRP B 279     4266   6579   6121   -152  -1054    565       C  
ATOM   4834  N   THR B 280     100.886   1.979-152.968  1.00 53.88           N  
ANISOU 4834  N   THR B 280     4861   8501   7110   -115  -1600    901       N  
ATOM   4835  CA  THR B 280     101.841   1.755-154.039  1.00 59.31           C  
ANISOU 4835  CA  THR B 280     5353   9299   7882    -10  -1525    993       C  
ATOM   4836  C   THR B 280     101.088   1.810-155.360  1.00 54.47           C  
ANISOU 4836  C   THR B 280     4853   8510   7335     22  -1361    929       C  
ATOM   4837  O   THR B 280     100.284   0.910-155.638  1.00 54.69           O  
ANISOU 4837  O   THR B 280     5052   8383   7346    163  -1271    905       O  
ATOM   4838  CB  THR B 280     102.538   0.418-153.873  1.00 64.27           C  
ANISOU 4838  CB  THR B 280     5899  10030   8492    242  -1513   1126       C  
ATOM   4839  OG1 THR B 280     103.290   0.430-152.654  1.00 67.93           O  
ANISOU 4839  OG1 THR B 280     6302  10622   8886    208  -1637   1153       O  
ATOM   4840  CG2 THR B 280     103.479   0.168-155.044  1.00 60.60           C  
ANISOU 4840  CG2 THR B 280     5270   9646   8109    370  -1397   1205       C  
ATOM   4841  N   PRO B 281     101.291   2.830-156.184  1.00 56.26           N  
ANISOU 4841  N   PRO B 281     4997   8751   7630   -110  -1322    900       N  
ATOM   4842  CA  PRO B 281     100.483   2.956-157.400  1.00 54.60           C  
ANISOU 4842  CA  PRO B 281     4908   8373   7466    -90  -1177    834       C  
ATOM   4843  C   PRO B 281     100.924   1.970-158.468  1.00 61.38           C  
ANISOU 4843  C   PRO B 281     5712   9248   8363    134  -1049    912       C  
ATOM   4844  O   PRO B 281     102.079   1.544-158.515  1.00 68.45           O  
ANISOU 4844  O   PRO B 281     6416  10315   9279    244  -1057   1027       O  
ATOM   4845  CB  PRO B 281     100.727   4.404-157.841  1.00 51.88           C  
ANISOU 4845  CB  PRO B 281     4477   8060   7176   -303  -1184    797       C  
ATOM   4846  CG  PRO B 281     102.080   4.750-157.280  1.00 54.38           C  
ANISOU 4846  CG  PRO B 281     4550   8608   7504   -377  -1298    887       C  
ATOM   4847  CD  PRO B 281     102.248   3.942-156.016  1.00 51.54           C  
ANISOU 4847  CD  PRO B 281     4210   8313   7063   -296  -1407    920       C  
ATOM   4848  N   GLY B 282      99.974   1.593-159.319  1.00 56.65           N  
ANISOU 4848  N   GLY B 282     5288   8471   7767    204   -930    848       N  
ATOM   4849  CA  GLY B 282     100.263   0.865-160.534  1.00 51.34           C  
ANISOU 4849  CA  GLY B 282     4600   7782   7125    386   -792    894       C  
ATOM   4850  C   GLY B 282     100.595   1.833-161.643  1.00 55.39           C  
ANISOU 4850  C   GLY B 282     5009   8335   7703    299   -721    892       C  
ATOM   4851  O   GLY B 282     100.933   2.994-161.402  1.00 57.12           O  
ANISOU 4851  O   GLY B 282     5117   8634   7954    112   -788    886       O  
ATOM   4852  N   ASN B 283     100.481   1.356-162.888  1.00 55.43           N  
ANISOU 4852  N   ASN B 283     5065   8274   7722    431   -581    895       N  
ATOM   4853  CA  ASN B 283     100.661   2.270-164.012  1.00 56.42           C  
ANISOU 4853  CA  ASN B 283     5120   8419   7899    354   -501    890       C  
ATOM   4854  C   ASN B 283      99.841   1.860-165.231  1.00 55.14           C  
ANISOU 4854  C   ASN B 283     5131   8103   7717    445   -368    831       C  
ATOM   4855  O   ASN B 283     100.202   2.205-166.362  1.00 56.46           O  
ANISOU 4855  O   ASN B 283     5236   8302   7915    469   -268    857       O  
ATOM   4856  CB  ASN B 283     102.144   2.398-164.390  1.00 64.10           C  
ANISOU 4856  CB  ASN B 283     5829   9600   8926    411   -471   1017       C  
ATOM   4857  CG  ASN B 283     102.778   1.071-164.737  1.00 75.44           C  
ANISOU 4857  CG  ASN B 283     7233  11085  10346    679   -386   1106       C  
ATOM   4858  OD1 ASN B 283     102.104   0.044-164.809  1.00 83.53           O  
ANISOU 4858  OD1 ASN B 283     8451  11968  11319    819   -339   1065       O  
ATOM   4859  ND2 ASN B 283     104.087   1.086-164.962  1.00 79.85           N  
ANISOU 4859  ND2 ASN B 283     7548  11843  10949    753   -359   1233       N  
ATOM   4860  N   GLY B 284      98.741   1.132-165.024  1.00 51.84           N  
ANISOU 4860  N   GLY B 284     4928   7523   7244    489   -368    755       N  
ATOM   4861  CA  GLY B 284      97.793   0.866-166.084  1.00 49.85           C  
ANISOU 4861  CA  GLY B 284     4854   7124   6964    528   -270    683       C  
ATOM   4862  C   GLY B 284      96.726   1.947-166.178  1.00 52.13           C  
ANISOU 4862  C   GLY B 284     5228   7324   7254    341   -297    594       C  
ATOM   4863  O   GLY B 284      96.671   2.890-165.386  1.00 45.40           O  
ANISOU 4863  O   GLY B 284     4322   6504   6423    184   -385    580       O  
ATOM   4864  N   ARG B 285      95.861   1.793-167.183  1.00 42.12           N  
ANISOU 4864  N   ARG B 285     4102   5944   5957    366   -217    535       N  
ATOM   4865  CA  ARG B 285      94.764   2.716-167.418  1.00 36.30           C  
ANISOU 4865  CA  ARG B 285     3454   5124   5216    221   -227    461       C  
ATOM   4866  C   ARG B 285      93.498   2.359-166.654  1.00 30.79           C  
ANISOU 4866  C   ARG B 285     2919   4306   4475    173   -287    387       C  
ATOM   4867  O   ARG B 285      92.554   3.159-166.650  1.00 38.26           O  
ANISOU 4867  O   ARG B 285     3927   5192   5416     55   -304    334       O  
ATOM   4868  CB  ARG B 285      94.428   2.763-168.918  1.00 43.47           C  
ANISOU 4868  CB  ARG B 285     4425   5989   6104    269   -118    441       C  
ATOM   4869  CG  ARG B 285      95.585   3.136-169.801  1.00 46.27           C  
ANISOU 4869  CG  ARG B 285     4631   6456   6495    322    -37    516       C  
ATOM   4870  CD  ARG B 285      95.282   2.731-171.229  1.00 60.28           C  
ANISOU 4870  CD  ARG B 285     6503   8179   8221    422     76    497       C  
ATOM   4871  NE  ARG B 285      94.351   3.643-171.890  1.00 62.63           N  
ANISOU 4871  NE  ARG B 285     6871   8420   8504    315     92    448       N  
ATOM   4872  CZ  ARG B 285      93.583   3.297-172.919  1.00 64.08           C  
ANISOU 4872  CZ  ARG B 285     7194   8531   8624    363    151    401       C  
ATOM   4873  NH1 ARG B 285      93.619   2.053-173.384  1.00 60.06           N  
ANISOU 4873  NH1 ARG B 285     6785   7980   8056    503    200    383       N  
ATOM   4874  NH2 ARG B 285      92.770   4.188-173.477  1.00 53.47           N  
ANISOU 4874  NH2 ARG B 285     5896   7154   7266    271    159    371       N  
ATOM   4875  N   PHE B 286      93.443   1.183-166.036  1.00 33.28           N  
ANISOU 4875  N   PHE B 286     3304   4583   4757    266   -311    391       N  
ATOM   4876  CA  PHE B 286      92.245   0.707-165.359  1.00 33.31           C  
ANISOU 4876  CA  PHE B 286     3465   4473   4720    228   -355    331       C  
ATOM   4877  C   PHE B 286      92.606   0.066-164.016  1.00 32.85           C  
ANISOU 4877  C   PHE B 286     3398   4436   4649    264   -430    365       C  
ATOM   4878  O   PHE B 286      92.148  -1.023-163.682  1.00 36.13           O  
ANISOU 4878  O   PHE B 286     3936   4767   5025    334   -427    354       O  
ATOM   4879  CB  PHE B 286      91.492  -0.276-166.246  1.00 31.56           C  
ANISOU 4879  CB  PHE B 286     3402   4140   4452    306   -285    288       C  
ATOM   4880  CG  PHE B 286      91.073   0.321-167.551  1.00 34.48           C  
ANISOU 4880  CG  PHE B 286     3789   4496   4816    272   -221    255       C  
ATOM   4881  CD1 PHE B 286      89.996   1.192-167.603  1.00 33.56           C  
ANISOU 4881  CD1 PHE B 286     3713   4343   4697    144   -244    207       C  
ATOM   4882  CD2 PHE B 286      91.781   0.051-168.710  1.00 37.02           C  
ANISOU 4882  CD2 PHE B 286     4084   4849   5132    379   -132    281       C  
ATOM   4883  CE1 PHE B 286      89.603   1.765-168.800  1.00 38.18           C  
ANISOU 4883  CE1 PHE B 286     4311   4923   5271    120   -189    187       C  
ATOM   4884  CE2 PHE B 286      91.403   0.631-169.913  1.00 37.94           C  
ANISOU 4884  CE2 PHE B 286     4221   4961   5234    350    -74    256       C  
ATOM   4885  CZ  PHE B 286      90.319   1.491-169.954  1.00 31.49           C  
ANISOU 4885  CZ  PHE B 286     3442   4110   4414    220   -107    211       C  
ATOM   4886  N   ASP B 287      93.442   0.741-163.238  1.00 34.94           N  
ANISOU 4886  N   ASP B 287     3520   4815   4942    210   -499    409       N  
ATOM   4887  CA  ASP B 287      93.814   0.253-161.911  1.00 39.70           C  
ANISOU 4887  CA  ASP B 287     4103   5459   5522    235   -584    447       C  
ATOM   4888  C   ASP B 287      92.759   0.688-160.899  1.00 34.44           C  
ANISOU 4888  C   ASP B 287     3539   4723   4824    107   -653    387       C  
ATOM   4889  O   ASP B 287      92.541   1.890-160.704  1.00 33.09           O  
ANISOU 4889  O   ASP B 287     3335   4569   4668    -34   -687    353       O  
ATOM   4890  CB  ASP B 287      95.182   0.791-161.503  1.00 39.30           C  
ANISOU 4890  CB  ASP B 287     3848   5580   5506    221   -641    522       C  
ATOM   4891  CG  ASP B 287      96.307   0.320-162.413  1.00 44.46           C  
ANISOU 4891  CG  ASP B 287     4378   6324   6190    366   -565    601       C  
ATOM   4892  OD1 ASP B 287      96.185  -0.749-163.054  1.00 41.95           O  
ANISOU 4892  OD1 ASP B 287     4151   5934   5852    520   -480    608       O  
ATOM   4893  OD2 ASP B 287      97.336   1.020-162.452  1.00 40.78           O  
ANISOU 4893  OD2 ASP B 287     3723   6004   5768    324   -589    659       O  
ATOM   4894  N   VAL B 288      92.117  -0.281-160.247  1.00 39.99           N  
ANISOU 4894  N   VAL B 288     4371   5342   5480    158   -666    378       N  
ATOM   4895  CA  VAL B 288      91.091   0.026-159.257  1.00 35.56           C  
ANISOU 4895  CA  VAL B 288     3911   4717   4883     53   -719    330       C  
ATOM   4896  C   VAL B 288      91.745   0.677-158.037  1.00 32.34           C  
ANISOU 4896  C   VAL B 288     3416   4413   4461    -16   -822    355       C  
ATOM   4897  O   VAL B 288      92.759   0.191-157.525  1.00 33.13           O  
ANISOU 4897  O   VAL B 288     3429   4608   4551     61   -869    423       O  
ATOM   4898  CB  VAL B 288      90.318  -1.251-158.889  1.00 36.69           C  
ANISOU 4898  CB  VAL B 288     4209   4749   4982    127   -698    326       C  
ATOM   4899  CG1 VAL B 288      89.280  -0.972-157.782  1.00 31.85           C  
ANISOU 4899  CG1 VAL B 288     3691   4083   4328     27   -745    290       C  
ATOM   4900  CG2 VAL B 288      89.642  -1.830-160.139  1.00 37.84           C  
ANISOU 4900  CG2 VAL B 288     4450   4793   5135    167   -606    290       C  
ATOM   4901  N   LEU B 289      91.187   1.807-157.593  1.00 32.29           N  
ANISOU 4901  N   LEU B 289     3431   4391   4446   -161   -857    301       N  
ATOM   4902  CA  LEU B 289      91.752   2.554-156.468  1.00 33.52           C  
ANISOU 4902  CA  LEU B 289     3526   4635   4577   -254   -958    307       C  
ATOM   4903  C   LEU B 289      91.463   1.852-155.143  1.00 32.13           C  
ANISOU 4903  C   LEU B 289     3437   4444   4326   -222  -1019    321       C  
ATOM   4904  O   LEU B 289      90.452   1.159-155.005  1.00 31.25           O  
ANISOU 4904  O   LEU B 289     3460   4226   4187   -181   -977    302       O  
ATOM   4905  CB  LEU B 289      91.171   3.965-156.422  1.00 35.01           C  
ANISOU 4905  CB  LEU B 289     3749   4784   4771   -410   -959    239       C  
ATOM   4906  CG  LEU B 289      91.720   4.957-157.443  1.00 37.91           C  
ANISOU 4906  CG  LEU B 289     4011   5190   5203   -475   -924    237       C  
ATOM   4907  CD1 LEU B 289      90.860   6.214-157.476  1.00 44.10           C  
ANISOU 4907  CD1 LEU B 289     4877   5891   5988   -602   -898    169       C  
ATOM   4908  CD2 LEU B 289      93.160   5.279-157.107  1.00 37.66           C  
ANISOU 4908  CD2 LEU B 289     3815   5305   5188   -514  -1002    288       C  
ATOM   4909  N   PRO B 290      92.339   2.012-154.155  1.00 32.26           N  
ANISOU 4909  N   PRO B 290     3376   4574   4306   -246  -1121    357       N  
ATOM   4910  CA  PRO B 290      91.992   1.609-152.790  1.00 41.62           C  
ANISOU 4910  CA  PRO B 290     4657   5750   5405   -242  -1187    362       C  
ATOM   4911  C   PRO B 290      90.998   2.590-152.187  1.00 39.16           C  
ANISOU 4911  C   PRO B 290     4462   5364   5053   -379  -1196    280       C  
ATOM   4912  O   PRO B 290      90.771   3.693-152.693  1.00 35.37           O  
ANISOU 4912  O   PRO B 290     3972   4857   4609   -485  -1169    225       O  
ATOM   4913  CB  PRO B 290      93.334   1.642-152.050  1.00 37.96           C  
ANISOU 4913  CB  PRO B 290     4054   5457   4913   -237  -1303    427       C  
ATOM   4914  CG  PRO B 290      94.115   2.700-152.770  1.00 41.25           C  
ANISOU 4914  CG  PRO B 290     4322   5957   5396   -337  -1314    417       C  
ATOM   4915  CD  PRO B 290      93.661   2.657-154.229  1.00 31.88           C  
ANISOU 4915  CD  PRO B 290     3147   4678   4288   -295  -1186    396       C  
ATOM   4916  N   LEU B 291      90.407   2.181-151.075  1.00 35.68           N  
ANISOU 4916  N   LEU B 291     4138   4886   4532   -367  -1224    278       N  
ATOM   4917  CA  LEU B 291      89.509   3.052-150.329  1.00 39.55           C  
ANISOU 4917  CA  LEU B 291     4748   5314   4967   -478  -1229    208       C  
ATOM   4918  C   LEU B 291      90.261   3.822-149.245  1.00 36.65           C  
ANISOU 4918  C   LEU B 291     4354   5045   4527   -576  -1348    195       C  
ATOM   4919  O   LEU B 291      91.154   3.283-148.583  1.00 40.36           O  
ANISOU 4919  O   LEU B 291     4758   5626   4952   -531  -1440    254       O  
ATOM   4920  CB  LEU B 291      88.374   2.240-149.710  1.00 41.62           C  
ANISOU 4920  CB  LEU B 291     5160   5481   5174   -420  -1183    213       C  
ATOM   4921  CG  LEU B 291      87.477   1.563-150.752  1.00 38.41           C  
ANISOU 4921  CG  LEU B 291     4795   4969   4829   -359  -1071    214       C  
ATOM   4922  CD1 LEU B 291      86.325   0.836-150.078  1.00 47.83           C  
ANISOU 4922  CD1 LEU B 291     6129   6074   5970   -329  -1028    221       C  
ATOM   4923  CD2 LEU B 291      86.977   2.612-151.733  1.00 40.96           C  
ANISOU 4923  CD2 LEU B 291     5100   5250   5214   -438  -1011    155       C  
ATOM   4924  N   LEU B 292      89.900   5.101-149.091  1.00 36.96           N  
ANISOU 4924  N   LEU B 292     4447   5043   4551   -710  -1347    119       N  
ATOM   4925  CA  LEU B 292      90.349   5.970-147.997  1.00 35.93           C  
ANISOU 4925  CA  LEU B 292     4348   4969   4334   -831  -1452     79       C  
ATOM   4926  C   LEU B 292      89.141   6.222-147.110  1.00 38.53           C  
ANISOU 4926  C   LEU B 292     4872   5193   4576   -851  -1412     25       C  
ATOM   4927  O   LEU B 292      88.214   6.941-147.501  1.00 32.08           O  
ANISOU 4927  O   LEU B 292     4141   4266   3784   -890  -1320    -31       O  
ATOM   4928  CB  LEU B 292      90.920   7.291-148.508  1.00 37.40           C  
ANISOU 4928  CB  LEU B 292     4468   5174   4568   -976  -1471     30       C  
ATOM   4929  CG  LEU B 292      92.375   7.284-148.969  1.00 45.62           C  
ANISOU 4929  CG  LEU B 292     5304   6365   5666  -1002  -1548     86       C  
ATOM   4930  CD1 LEU B 292      92.763   8.615-149.597  1.00 47.32           C  
ANISOU 4930  CD1 LEU B 292     5471   6570   5939  -1155  -1540     38       C  
ATOM   4931  CD2 LEU B 292      93.287   6.967-147.798  1.00 44.51           C  
ANISOU 4931  CD2 LEU B 292     5109   6370   5432  -1021  -1697    123       C  
ATOM   4932  N   LEU B 293      89.147   5.631-145.920  1.00 34.20           N  
ANISOU 4932  N   LEU B 293     4391   4684   3921   -813  -1475     50       N  
ATOM   4933  CA  LEU B 293      87.993   5.642-145.040  1.00 36.48           C  
ANISOU 4933  CA  LEU B 293     4859   4881   4119   -803  -1426     18       C  
ATOM   4934  C   LEU B 293      88.363   6.400-143.772  1.00 36.06           C  
ANISOU 4934  C   LEU B 293     4890   4875   3934   -905  -1528    -31       C  
ATOM   4935  O   LEU B 293      89.407   6.135-143.167  1.00 41.45           O  
ANISOU 4935  O   LEU B 293     5503   5687   4560   -919  -1657      4       O  
ATOM   4936  CB  LEU B 293      87.545   4.212-144.697  1.00 35.78           C  
ANISOU 4936  CB  LEU B 293     4809   4781   4007   -664  -1395     93       C  
ATOM   4937  CG  LEU B 293      87.171   3.361-145.904  1.00 34.98           C  
ANISOU 4937  CG  LEU B 293     4648   4623   4020   -571  -1299    136       C  
ATOM   4938  CD1 LEU B 293      86.813   1.928-145.533  1.00 34.05           C  
ANISOU 4938  CD1 LEU B 293     4582   4481   3876   -449  -1272    210       C  
ATOM   4939  CD2 LEU B 293      86.012   4.028-146.645  1.00 34.40           C  
ANISOU 4939  CD2 LEU B 293     4630   4435   4004   -612  -1182     79       C  
ATOM   4940  N   GLN B 294      87.526   7.357-143.396  1.00 37.43           N  
ANISOU 4940  N   GLN B 294     5216   4950   4056   -975  -1471   -110       N  
ATOM   4941  CA  GLN B 294      87.786   8.220-142.245  1.00 37.29           C  
ANISOU 4941  CA  GLN B 294     5315   4951   3904  -1086  -1554   -178       C  
ATOM   4942  C   GLN B 294      86.758   7.915-141.167  1.00 35.57           C  
ANISOU 4942  C   GLN B 294     5279   4673   3564  -1024  -1502   -183       C  
ATOM   4943  O   GLN B 294      85.548   8.049-141.397  1.00 37.49           O  
ANISOU 4943  O   GLN B 294     5615   4799   3830   -977  -1364   -198       O  
ATOM   4944  CB  GLN B 294      87.739   9.690-142.666  1.00 43.93           C  
ANISOU 4944  CB  GLN B 294     6205   5713   4773  -1220  -1523   -270       C  
ATOM   4945  CG  GLN B 294      87.589  10.733-141.557  1.00 45.21           C  
ANISOU 4945  CG  GLN B 294     6559   5827   4792  -1332  -1557   -364       C  
ATOM   4946  CD  GLN B 294      87.267  12.103-142.148  1.00 53.18           C  
ANISOU 4946  CD  GLN B 294     7645   6711   5848  -1431  -1476   -447       C  
ATOM   4947  OE1 GLN B 294      88.002  12.603-142.988  1.00 48.03           O  
ANISOU 4947  OE1 GLN B 294     6876   6081   5292  -1516  -1505   -453       O  
ATOM   4948  NE2 GLN B 294      86.140  12.685-141.747  1.00 55.00           N  
ANISOU 4948  NE2 GLN B 294     8071   6809   6017  -1406  -1361   -500       N  
ATOM   4949  N   ALA B 295      87.243   7.475-140.000  1.00 38.12           N  
ANISOU 4949  N   ALA B 295     5644   5086   3755  -1017  -1610   -160       N  
ATOM   4950  CA  ALA B 295      86.423   7.371-138.813  1.00 42.56           C  
ANISOU 4950  CA  ALA B 295     6395   5603   4171   -980  -1575   -174       C  
ATOM   4951  C   ALA B 295      86.498   8.684-138.041  1.00 42.14           C  
ANISOU 4951  C   ALA B 295     6497   5521   3995  -1115  -1617   -284       C  
ATOM   4952  O   ALA B 295      87.407   9.486-138.265  1.00 43.02           O  
ANISOU 4952  O   ALA B 295     6551   5674   4119  -1246  -1712   -337       O  
ATOM   4953  CB  ALA B 295      86.900   6.199-137.953  1.00 44.51           C  
ANISOU 4953  CB  ALA B 295     6622   5961   4328   -895  -1666    -86       C  
ATOM   4954  N   PRO B 296      85.535   8.954-137.160  1.00 49.24           N  
ANISOU 4954  N   PRO B 296     7599   6338   4773  -1090  -1538   -322       N  
ATOM   4955  CA  PRO B 296      85.500  10.256-136.477  1.00 49.85           C  
ANISOU 4955  CA  PRO B 296     7858   6355   4727  -1210  -1554   -438       C  
ATOM   4956  C   PRO B 296      86.829  10.626-135.834  1.00 48.09           C  
ANISOU 4956  C   PRO B 296     7617   6253   4401  -1349  -1753   -480       C  
ATOM   4957  O   PRO B 296      87.424   9.841-135.093  1.00 44.31           O  
ANISOU 4957  O   PRO B 296     7099   5905   3830  -1319  -1873   -423       O  
ATOM   4958  CB  PRO B 296      84.406  10.062-135.428  1.00 51.80           C  
ANISOU 4958  CB  PRO B 296     8308   6540   4835  -1120  -1456   -438       C  
ATOM   4959  CG  PRO B 296      83.470   9.100-136.068  1.00 48.34           C  
ANISOU 4959  CG  PRO B 296     7789   6064   4515   -977  -1320   -343       C  
ATOM   4960  CD  PRO B 296      84.339   8.151-136.856  1.00 46.08           C  
ANISOU 4960  CD  PRO B 296     7277   5878   4353   -952  -1407   -262       C  
ATOM   4961  N   ASP B 297      87.307  11.829-136.158  1.00 46.05           N  
ANISOU 4961  N   ASP B 297     7357   5953   4187  -1482  -1763   -566       N  
ATOM   4962  CA  ASP B 297      88.467  12.439-135.506  1.00 48.64           C  
ANISOU 4962  CA  ASP B 297     7640   6371   4469  -1593  -1876   -608       C  
ATOM   4963  C   ASP B 297      89.739  11.628-135.712  1.00 51.46           C  
ANISOU 4963  C   ASP B 297     7745   6920   4885  -1588  -2019   -522       C  
ATOM   4964  O   ASP B 297      90.656  11.658-134.892  1.00 59.04           O  
ANISOU 4964  O   ASP B 297     8662   8004   5767  -1635  -2137   -525       O  
ATOM   4965  CB  ASP B 297      88.181  12.656-134.018  1.00 51.03           C  
ANISOU 4965  CB  ASP B 297     8150   6665   4575  -1591  -1889   -659       C  
ATOM   4966  CG  ASP B 297      86.886  13.399-133.807  1.00 53.41           C  
ANISOU 4966  CG  ASP B 297     8702   6779   4814  -1568  -1730   -733       C  
ATOM   4967  OD1 ASP B 297      86.830  14.593-134.189  1.00 50.99           O  
ANISOU 4967  OD1 ASP B 297     8460   6358   4557  -1654  -1666   -813       O  
ATOM   4968  OD2 ASP B 297      85.918  12.782-133.320  1.00 56.89           O  
ANISOU 4968  OD2 ASP B 297     9271   7184   5162  -1454  -1658   -702       O  
ATOM   4969  N   GLU B 298      89.809  10.924-136.832  1.00 51.91           N  
ANISOU 4969  N   GLU B 298     7636   7006   5082  -1527  -2005   -443       N  
ATOM   4970  CA  GLU B 298      90.927  10.064-137.166  1.00 57.23           C  
ANISOU 4970  CA  GLU B 298     8068   7853   5824  -1489  -2114   -346       C  
ATOM   4971  C   GLU B 298      91.353  10.385-138.592  1.00 53.14           C  
ANISOU 4971  C   GLU B 298     7376   7324   5490  -1530  -2078   -334       C  
ATOM   4972  O   GLU B 298      90.502  10.701-139.434  1.00 54.65           O  
ANISOU 4972  O   GLU B 298     7625   7379   5760  -1526  -1964   -361       O  
ATOM   4973  CB  GLU B 298      90.510   8.588-137.042  1.00 73.52           C  
ANISOU 4973  CB  GLU B 298    10116   9962   7855  -1328  -2124   -235       C  
ATOM   4974  CG  GLU B 298      91.635   7.593-136.857  1.00 83.69           C  
ANISOU 4974  CG  GLU B 298    11212  11441   9147  -1254  -2245   -126       C  
ATOM   4975  CD  GLU B 298      91.843   7.202-135.406  1.00 93.95           C  
ANISOU 4975  CD  GLU B 298    12595  12831  10269  -1214  -2328   -107       C  
ATOM   4976  OE1 GLU B 298      91.106   7.707-134.528  1.00 89.74           O  
ANISOU 4976  OE1 GLU B 298    12277  12212   9608  -1248  -2289   -182       O  
ATOM   4977  OE2 GLU B 298      92.752   6.385-135.144  1.00 99.96           O  
ANISOU 4977  OE2 GLU B 298    13209  13753  11018  -1139  -2426    -12       O  
ATOM   4978  N   PRO B 299      92.650  10.329-138.892  1.00 55.53           N  
ANISOU 4978  N   PRO B 299     7466   7771   5861  -1566  -2166   -292       N  
ATOM   4979  CA  PRO B 299      93.092  10.430-140.297  1.00 51.13           C  
ANISOU 4979  CA  PRO B 299     6727   7222   5478  -1578  -2125   -258       C  
ATOM   4980  C   PRO B 299      92.451   9.335-141.127  1.00 55.93           C  
ANISOU 4980  C   PRO B 299     7286   7802   6160  -1439  -2069   -176       C  
ATOM   4981  O   PRO B 299      92.038   8.302-140.580  1.00 52.00           O  
ANISOU 4981  O   PRO B 299     6841   7331   5588  -1326  -2095   -116       O  
ATOM   4982  CB  PRO B 299      94.615  10.243-140.214  1.00 55.25           C  
ANISOU 4982  CB  PRO B 299     7028   7937   6026  -1602  -2243   -202       C  
ATOM   4983  CG  PRO B 299      94.854   9.581-138.880  1.00 61.30           C  
ANISOU 4983  CG  PRO B 299     7836   8813   6642  -1547  -2349   -171       C  
ATOM   4984  CD  PRO B 299      93.779  10.100-137.971  1.00 59.08           C  
ANISOU 4984  CD  PRO B 299     7824   8396   6229  -1584  -2305   -264       C  
ATOM   4985  N   PRO B 300      92.333   9.525-142.442  1.00 55.03           N  
ANISOU 4985  N   PRO B 300     7086   7632   6191  -1442  -1990   -167       N  
ATOM   4986  CA  PRO B 300      91.785   8.461-143.278  1.00 49.63           C  
ANISOU 4986  CA  PRO B 300     6346   6912   5601  -1276  -1894    -91       C  
ATOM   4987  C   PRO B 300      92.729   7.276-143.310  1.00 47.04           C  
ANISOU 4987  C   PRO B 300     5837   6744   5292  -1164  -1973     24       C  
ATOM   4988  O   PRO B 300      93.948   7.414-143.186  1.00 55.24           O  
ANISOU 4988  O   PRO B 300     6722   7941   6325  -1231  -2100     58       O  
ATOM   4989  CB  PRO B 300      91.663   9.118-144.657  1.00 50.64           C  
ANISOU 4989  CB  PRO B 300     6408   6960   5873  -1316  -1792   -116       C  
ATOM   4990  CG  PRO B 300      92.763  10.110-144.667  1.00 51.81           C  
ANISOU 4990  CG  PRO B 300     6467   7189   6031  -1482  -1882   -149       C  
ATOM   4991  CD  PRO B 300      92.816  10.656-143.255  1.00 54.42           C  
ANISOU 4991  CD  PRO B 300     6939   7521   6216  -1558  -1944   -217       C  
ATOM   4992  N   GLU B 301      92.146   6.096-143.464  1.00 41.57           N  
ANISOU 4992  N   GLU B 301     5166   6008   4621   -989  -1893     89       N  
ATOM   4993  CA  GLU B 301      92.891   4.848-143.466  1.00 47.57           C  
ANISOU 4993  CA  GLU B 301     5792   6889   5393   -847  -1942    205       C  
ATOM   4994  C   GLU B 301      92.683   4.159-144.801  1.00 41.33           C  
ANISOU 4994  C   GLU B 301     4924   6036   4743   -725  -1818    251       C  
ATOM   4995  O   GLU B 301      91.567   4.147-145.328  1.00 41.22           O  
ANISOU 4995  O   GLU B 301     5016   5871   4774   -699  -1691    211       O  
ATOM   4996  CB  GLU B 301      92.440   3.935-142.324  1.00 50.61           C  
ANISOU 4996  CB  GLU B 301     6302   7271   5656   -742  -1962    249       C  
ATOM   4997  CG  GLU B 301      93.319   2.724-142.125  1.00 72.99           C  
ANISOU 4997  CG  GLU B 301     9013  10240   8478   -595  -2029    376       C  
ATOM   4998  CD  GLU B 301      93.019   1.995-140.826  1.00 89.16           C  
ANISOU 4998  CD  GLU B 301    11189  12305  10383   -515  -2072    421       C  
ATOM   4999  OE1 GLU B 301      93.274   0.771-140.757  1.00 92.65           O  
ANISOU 4999  OE1 GLU B 301    11594  12782  10825   -349  -2064    530       O  
ATOM   5000  OE2 GLU B 301      92.523   2.642-139.877  1.00 88.91           O  
ANISOU 5000  OE2 GLU B 301    11305  12243  10232   -612  -2106    349       O  
ATOM   5001  N   LEU B 302      93.756   3.580-145.335  1.00 41.44           N  
ANISOU 5001  N   LEU B 302     4752   6174   4819   -648  -1856    338       N  
ATOM   5002  CA  LEU B 302      93.747   2.973-146.666  1.00 35.79           C  
ANISOU 5002  CA  LEU B 302     3955   5413   4229   -536  -1745    380       C  
ATOM   5003  C   LEU B 302      93.298   1.519-146.568  1.00 44.40           C  
ANISOU 5003  C   LEU B 302     5118   6444   5307   -349  -1682    450       C  
ATOM   5004  O   LEU B 302      93.746   0.784-145.679  1.00 46.64           O  
ANISOU 5004  O   LEU B 302     5398   6813   5512   -265  -1757    524       O  
ATOM   5005  CB  LEU B 302      95.148   3.063-147.268  1.00 49.13           C  
ANISOU 5005  CB  LEU B 302     5414   7267   5987   -534  -1804    445       C  
ATOM   5006  CG  LEU B 302      95.419   3.021-148.769  1.00 58.32           C  
ANISOU 5006  CG  LEU B 302     6463   8413   7283   -486  -1703    465       C  
ATOM   5007  CD1 LEU B 302      94.656   4.105-149.505  1.00 54.37           C  
ANISOU 5007  CD1 LEU B 302     6034   7785   6839   -614  -1621    365       C  
ATOM   5008  CD2 LEU B 302      96.907   3.211-148.958  1.00 64.75           C  
ANISOU 5008  CD2 LEU B 302     7040   9429   8132   -505  -1790    540       C  
ATOM   5009  N   PHE B 303      92.390   1.118-147.455  1.00 41.17           N  
ANISOU 5009  N   PHE B 303     4785   5889   4967   -291  -1548    429       N  
ATOM   5010  CA  PHE B 303      91.941  -0.267-147.543  1.00 41.74           C  
ANISOU 5010  CA  PHE B 303     4937   5883   5042   -131  -1475    489       C  
ATOM   5011  C   PHE B 303      91.885  -0.678-149.005  1.00 44.09           C  
ANISOU 5011  C   PHE B 303     5188   6114   5450    -60  -1367    494       C  
ATOM   5012  O   PHE B 303      91.260   0.004-149.827  1.00 39.20           O  
ANISOU 5012  O   PHE B 303     4589   5416   4889   -141  -1299    423       O  
ATOM   5013  CB  PHE B 303      90.557  -0.479-146.905  1.00 34.74           C  
ANISOU 5013  CB  PHE B 303     4247   4857   4094   -148  -1419    449       C  
ATOM   5014  CG  PHE B 303      90.507  -0.186-145.413  1.00 36.23           C  
ANISOU 5014  CG  PHE B 303     4514   5097   4156   -199  -1510    445       C  
ATOM   5015  CD1 PHE B 303      90.350   1.116-144.964  1.00 35.29           C  
ANISOU 5015  CD1 PHE B 303     4422   4994   3992   -352  -1557    361       C  
ATOM   5016  CD2 PHE B 303      90.590  -1.206-144.480  1.00 42.09           C  
ANISOU 5016  CD2 PHE B 303     5318   5860   4814    -91  -1541    524       C  
ATOM   5017  CE1 PHE B 303      90.295   1.406-143.604  1.00 40.03           C  
ANISOU 5017  CE1 PHE B 303     5113   5637   4460   -401  -1638    348       C  
ATOM   5018  CE2 PHE B 303      90.533  -0.915-143.127  1.00 36.88           C  
ANISOU 5018  CE2 PHE B 303     4737   5252   4023   -138  -1624    519       C  
ATOM   5019  CZ  PHE B 303      90.377   0.392-142.699  1.00 40.68           C  
ANISOU 5019  CZ  PHE B 303     5249   5752   4455   -294  -1673    427       C  
ATOM   5020  N   LEU B 304      92.538  -1.789-149.318  1.00 48.29           N  
ANISOU 5020  N   LEU B 304     5668   6677   6003     99  -1348    582       N  
ATOM   5021  CA  LEU B 304      92.487  -2.368-150.653  1.00 46.15           C  
ANISOU 5021  CA  LEU B 304     5384   6331   5818    188  -1238    589       C  
ATOM   5022  C   LEU B 304      91.238  -3.224-150.797  1.00 44.27           C  
ANISOU 5022  C   LEU B 304     5333   5915   5573    229  -1142    566       C  
ATOM   5023  O   LEU B 304      90.864  -3.949-149.875  1.00 40.05           O  
ANISOU 5023  O   LEU B 304     4907   5337   4972    278  -1153    602       O  
ATOM   5024  CB  LEU B 304      93.733  -3.216-150.910  1.00 49.61           C  
ANISOU 5024  CB  LEU B 304     5702   6873   6275    355  -1247    696       C  
ATOM   5025  CG  LEU B 304      95.039  -2.425-151.003  1.00 49.74           C  
ANISOU 5025  CG  LEU B 304     5497   7084   6318    315  -1330    732       C  
ATOM   5026  CD1 LEU B 304      96.222  -3.302-150.650  1.00 53.89           C  
ANISOU 5026  CD1 LEU B 304     5907   7746   6822    486  -1374    862       C  
ATOM   5027  CD2 LEU B 304      95.194  -1.848-152.407  1.00 53.34           C  
ANISOU 5027  CD2 LEU B 304     5868   7529   6870    277  -1253    694       C  
ATOM   5028  N   LEU B 305      90.589  -3.135-151.956  1.00 42.07           N  
ANISOU 5028  N   LEU B 305     5089   5536   5358    203  -1049    510       N  
ATOM   5029  CA  LEU B 305      89.445  -4.000-152.205  1.00 41.18           C  
ANISOU 5029  CA  LEU B 305     5140   5264   5243    229   -963    490       C  
ATOM   5030  C   LEU B 305      89.934  -5.337-152.744  1.00 50.03           C  
ANISOU 5030  C   LEU B 305     6293   6337   6380    394   -905    553       C  
ATOM   5031  O   LEU B 305      90.749  -5.360-153.673  1.00 53.14           O  
ANISOU 5031  O   LEU B 305     6589   6779   6823    463   -878    570       O  
ATOM   5032  CB  LEU B 305      88.487  -3.367-153.213  1.00 38.46           C  
ANISOU 5032  CB  LEU B 305     4823   4841   4949    126   -896    406       C  
ATOM   5033  CG  LEU B 305      87.750  -2.099-152.796  1.00 39.60           C  
ANISOU 5033  CG  LEU B 305     4973   4994   5079    -23   -921    342       C  
ATOM   5034  CD1 LEU B 305      87.183  -1.376-154.008  1.00 37.67           C  
ANISOU 5034  CD1 LEU B 305     4707   4711   4895    -93   -860    279       C  
ATOM   5035  CD2 LEU B 305      86.647  -2.433-151.794  1.00 48.34           C  
ANISOU 5035  CD2 LEU B 305     6217   6024   6125    -55   -913    337       C  
ATOM   5036  N   PRO B 306      89.470  -6.457-152.199  1.00 55.55           N  
ANISOU 5036  N   PRO B 306     7134   6936   7037    464   -875    591       N  
ATOM   5037  CA  PRO B 306      89.794  -7.755-152.795  1.00 52.87           C  
ANISOU 5037  CA  PRO B 306     6865   6510   6711    618   -800    640       C  
ATOM   5038  C   PRO B 306      89.418  -7.753-154.262  1.00 55.70           C  
ANISOU 5038  C   PRO B 306     7248   6788   7128    595   -716    573       C  
ATOM   5039  O   PRO B 306      88.282  -7.398-154.614  1.00 57.85           O  
ANISOU 5039  O   PRO B 306     7587   6982   7412    466   -688    497       O  
ATOM   5040  CB  PRO B 306      88.931  -8.743-151.998  1.00 53.52           C  
ANISOU 5040  CB  PRO B 306     7134   6460   6742    633   -771    665       C  
ATOM   5041  CG  PRO B 306      88.648  -8.052-150.709  1.00 55.75           C  
ANISOU 5041  CG  PRO B 306     7398   6817   6966    543   -854    668       C  
ATOM   5042  CD  PRO B 306      88.560  -6.584-151.049  1.00 54.61           C  
ANISOU 5042  CD  PRO B 306     7133   6762   6854    402   -895    590       C  
ATOM   5043  N   PRO B 307      90.355  -8.094-155.146  1.00 58.73           N  
ANISOU 5043  N   PRO B 307     7570   7202   7545    718   -673    603       N  
ATOM   5044  CA  PRO B 307      90.052  -8.054-156.587  1.00 60.05           C  
ANISOU 5044  CA  PRO B 307     7763   7300   7755    699   -594    538       C  
ATOM   5045  C   PRO B 307      88.813  -8.853-156.978  1.00 59.93           C  
ANISOU 5045  C   PRO B 307     7948   7097   7724    651   -526    482       C  
ATOM   5046  O   PRO B 307      88.073  -8.432-157.875  1.00 51.73           O  
ANISOU 5046  O   PRO B 307     6931   6017   6707    549   -496    405       O  
ATOM   5047  CB  PRO B 307      91.333  -8.613-157.232  1.00 58.72           C  
ANISOU 5047  CB  PRO B 307     7528   7182   7604    885   -546    603       C  
ATOM   5048  CG  PRO B 307      92.150  -9.187-156.111  1.00 63.07           C  
ANISOU 5048  CG  PRO B 307     8045   7799   8119   1014   -593    710       C  
ATOM   5049  CD  PRO B 307      91.754  -8.459-154.870  1.00 57.74           C  
ANISOU 5049  CD  PRO B 307     7333   7192   7413    883   -697    704       C  
ATOM   5050  N   GLU B 308      88.543  -9.970-156.300  1.00 58.01           N  
ANISOU 5050  N   GLU B 308     7853   6746   7442    713   -505    524       N  
ATOM   5051  CA  GLU B 308      87.379 -10.790-156.617  1.00 51.49           C  
ANISOU 5051  CA  GLU B 308     7222   5740   6602    650   -444    476       C  
ATOM   5052  C   GLU B 308      86.066 -10.172-156.151  1.00 44.36           C  
ANISOU 5052  C   GLU B 308     6338   4823   5695    461   -478    425       C  
ATOM   5053  O   GLU B 308      85.000 -10.686-156.499  1.00 50.89           O  
ANISOU 5053  O   GLU B 308     7295   5524   6515    374   -436    381       O  
ATOM   5054  CB  GLU B 308      87.537 -12.186-156.006  1.00 58.14           C  
ANISOU 5054  CB  GLU B 308     8225   6460   7406    774   -403    547       C  
ATOM   5055  CG  GLU B 308      87.593 -12.212-154.486  1.00 74.21           C  
ANISOU 5055  CG  GLU B 308    10249   8546   9403    787   -465    622       C  
ATOM   5056  CD  GLU B 308      88.970 -11.876-153.924  1.00 85.94           C  
ANISOU 5056  CD  GLU B 308    11573  10201  10879    922   -526    706       C  
ATOM   5057  OE1 GLU B 308      89.880 -11.515-154.705  1.00 84.99           O  
ANISOU 5057  OE1 GLU B 308    11326  10174  10794    994   -520    709       O  
ATOM   5058  OE2 GLU B 308      89.141 -11.980-152.691  1.00 90.87           O  
ANISOU 5058  OE2 GLU B 308    12193  10876  11458    952   -581    775       O  
ATOM   5059  N   LEU B 309      86.109  -9.096-155.368  1.00 37.70           N  
ANISOU 5059  N   LEU B 309     5371   4106   4849    394   -551    431       N  
ATOM   5060  CA  LEU B 309      84.895  -8.369-155.045  1.00 37.44           C  
ANISOU 5060  CA  LEU B 309     5343   4070   4812    231   -569    382       C  
ATOM   5061  C   LEU B 309      84.507  -7.372-156.136  1.00 32.24           C  
ANISOU 5061  C   LEU B 309     4602   3452   4195    136   -560    307       C  
ATOM   5062  O   LEU B 309      83.327  -7.008-156.234  1.00 35.23           O  
ANISOU 5062  O   LEU B 309     5009   3801   4577     14   -549    265       O  
ATOM   5063  CB  LEU B 309      85.080  -7.616-153.727  1.00 45.38           C  
ANISOU 5063  CB  LEU B 309     6277   5179   5784    205   -642    414       C  
ATOM   5064  CG  LEU B 309      83.889  -7.637-152.781  1.00 57.16           C  
ANISOU 5064  CG  LEU B 309     7858   6622   7239    109   -639    413       C  
ATOM   5065  CD1 LEU B 309      83.578  -9.072-152.402  1.00 56.17           C  
ANISOU 5065  CD1 LEU B 309     7890   6367   7085    163   -592    464       C  
ATOM   5066  CD2 LEU B 309      84.217  -6.819-151.548  1.00 65.82           C  
ANISOU 5066  CD2 LEU B 309     8891   7827   8289     95   -711    437       C  
ATOM   5067  N   VAL B 310      85.463  -6.937-156.953  1.00 33.05           N  
ANISOU 5067  N   VAL B 310     4601   3628   4329    196   -560    301       N  
ATOM   5068  CA  VAL B 310      85.262  -5.875-157.943  1.00 31.07           C  
ANISOU 5068  CA  VAL B 310     4261   3431   4115    119   -554    244       C  
ATOM   5069  C   VAL B 310      85.019  -6.542-159.298  1.00 38.87           C  
ANISOU 5069  C   VAL B 310     5325   4334   5110    141   -487    205       C  
ATOM   5070  O   VAL B 310      85.958  -6.979-159.963  1.00 35.45           O  
ANISOU 5070  O   VAL B 310     4882   3905   4684    256   -454    222       O  
ATOM   5071  CB  VAL B 310      86.466  -4.930-157.992  1.00 37.36           C  
ANISOU 5071  CB  VAL B 310     4895   4364   4938    156   -592    265       C  
ATOM   5072  CG1 VAL B 310      86.206  -3.776-158.937  1.00 36.75           C  
ANISOU 5072  CG1 VAL B 310     4737   4332   4895     71   -580    213       C  
ATOM   5073  CG2 VAL B 310      86.799  -4.412-156.581  1.00 36.41           C  
ANISOU 5073  CG2 VAL B 310     4719   4323   4792    134   -669    301       C  
ATOM   5074  N   LEU B 311      83.755  -6.625-159.709  1.00 31.97           N  
ANISOU 5074  N   LEU B 311     4528   3390   4228     32   -468    156       N  
ATOM   5075  CA  LEU B 311      83.398  -7.248-160.981  1.00 30.30           C  
ANISOU 5075  CA  LEU B 311     4406   3098   4008     27   -417    109       C  
ATOM   5076  C   LEU B 311      83.606  -6.238-162.102  1.00 31.27           C  
ANISOU 5076  C   LEU B 311     4422   3305   4153      9   -409     74       C  
ATOM   5077  O   LEU B 311      83.134  -5.096-162.014  1.00 31.86           O  
ANISOU 5077  O   LEU B 311     4403   3455   4246    -78   -437     61       O  
ATOM   5078  CB  LEU B 311      81.939  -7.717-160.959  1.00 28.34           C  
ANISOU 5078  CB  LEU B 311     4266   2761   3739   -101   -411     76       C  
ATOM   5079  CG  LEU B 311      81.408  -8.370-162.238  1.00 33.63           C  
ANISOU 5079  CG  LEU B 311     5042   3348   4388   -142   -374     18       C  
ATOM   5080  CD1 LEU B 311      82.296  -9.564-162.627  1.00 37.75           C  
ANISOU 5080  CD1 LEU B 311     5689   3766   4886     -9   -323     22       C  
ATOM   5081  CD2 LEU B 311      79.953  -8.796-162.058  1.00 37.25           C  
ANISOU 5081  CD2 LEU B 311     5584   3741   4829   -292   -382     -3       C  
ATOM   5082  N   GLU B 312      84.318  -6.651-163.149  1.00 33.77           N  
ANISOU 5082  N   GLU B 312     4762   3606   4465    100   -363     62       N  
ATOM   5083  CA  GLU B 312      84.617  -5.778-164.278  1.00 28.80           C  
ANISOU 5083  CA  GLU B 312     4041   3053   3850     99   -344     37       C  
ATOM   5084  C   GLU B 312      84.205  -6.464-165.572  1.00 29.61           C  
ANISOU 5084  C   GLU B 312     4264   3076   3911     99   -295    -18       C  
ATOM   5085  O   GLU B 312      84.083  -7.691-165.634  1.00 34.89           O  
ANISOU 5085  O   GLU B 312     5087   3627   4545    135   -266    -32       O  
ATOM   5086  CB  GLU B 312      86.113  -5.431-164.341  1.00 33.61           C  
ANISOU 5086  CB  GLU B 312     4529   3753   4487    222   -330     87       C  
ATOM   5087  CG  GLU B 312      86.592  -4.515-163.214  1.00 40.30           C  
ANISOU 5087  CG  GLU B 312     5238   4705   5370    197   -392    133       C  
ATOM   5088  CD  GLU B 312      88.060  -4.186-163.345  1.00 43.54           C  
ANISOU 5088  CD  GLU B 312     5513   5220   5810    300   -385    187       C  
ATOM   5089  OE1 GLU B 312      88.890  -5.007-162.920  1.00 47.59           O  
ANISOU 5089  OE1 GLU B 312     6033   5734   6317    422   -377    239       O  
ATOM   5090  OE2 GLU B 312      88.391  -3.125-163.900  1.00 46.02           O  
ANISOU 5090  OE2 GLU B 312     5711   5619   6154    261   -381    184       O  
ATOM   5091  N   VAL B 313      84.019  -5.651-166.607  1.00 31.61           N  
ANISOU 5091  N   VAL B 313     4457   3391   4163     59   -285    -48       N  
ATOM   5092  CA  VAL B 313      83.550  -6.103-167.919  1.00 31.49           C  
ANISOU 5092  CA  VAL B 313     4547   3323   4095     40   -250   -107       C  
ATOM   5093  C   VAL B 313      84.561  -5.657-168.969  1.00 32.47           C  
ANISOU 5093  C   VAL B 313     4607   3514   4217    141   -197   -100       C  
ATOM   5094  O   VAL B 313      84.675  -4.452-169.218  1.00 31.78           O  
ANISOU 5094  O   VAL B 313     4384   3532   4160    111   -207    -83       O  
ATOM   5095  CB  VAL B 313      82.166  -5.513-168.242  1.00 36.99           C  
ANISOU 5095  CB  VAL B 313     5232   4046   4775   -115   -292   -143       C  
ATOM   5096  CG1 VAL B 313      81.682  -5.929-169.656  1.00 28.38           C  
ANISOU 5096  CG1 VAL B 313     4244   2921   3616   -145   -270   -206       C  
ATOM   5097  CG2 VAL B 313      81.145  -5.836-167.130  1.00 34.47           C  
ANISOU 5097  CG2 VAL B 313     4950   3682   4465   -218   -337   -137       C  
ATOM   5098  N   PRO B 314      85.323  -6.559-169.592  1.00 36.02           N  
ANISOU 5098  N   PRO B 314     5151   3904   4631    267   -131   -107       N  
ATOM   5099  CA  PRO B 314      86.143  -6.145-170.738  1.00 34.25           C  
ANISOU 5099  CA  PRO B 314     4874   3745   4393    358    -67   -102       C  
ATOM   5100  C   PRO B 314      85.231  -5.759-171.890  1.00 33.21           C  
ANISOU 5100  C   PRO B 314     4788   3622   4207    261    -72   -163       C  
ATOM   5101  O   PRO B 314      84.186  -6.369-172.094  1.00 32.11           O  
ANISOU 5101  O   PRO B 314     4782   3401   4016    168   -100   -222       O  
ATOM   5102  CB  PRO B 314      86.958  -7.403-171.063  1.00 44.68           C  
ANISOU 5102  CB  PRO B 314     6327   4974   5674    517     12   -100       C  
ATOM   5103  CG  PRO B 314      86.075  -8.536-170.620  1.00 46.29           C  
ANISOU 5103  CG  PRO B 314     6722   5028   5840    457    -10   -146       C  
ATOM   5104  CD  PRO B 314      85.365  -8.021-169.386  1.00 40.93           C  
ANISOU 5104  CD  PRO B 314     5954   4382   5213    331    -98   -122       C  
ATOM   5105  N   LEU B 315      85.608  -4.720-172.626  1.00 32.54           N  
ANISOU 5105  N   LEU B 315     4586   3643   4133    276    -49   -143       N  
ATOM   5106  CA  LEU B 315      84.747  -4.168-173.667  1.00 33.53           C  
ANISOU 5106  CA  LEU B 315     4731   3803   4207    188    -60   -184       C  
ATOM   5107  C   LEU B 315      85.148  -4.718-175.024  1.00 36.85           C  
ANISOU 5107  C   LEU B 315     5264   4195   4543    277     15   -222       C  
ATOM   5108  O   LEU B 315      86.326  -4.665-175.407  1.00 33.86           O  
ANISOU 5108  O   LEU B 315     4840   3851   4173    412     92   -183       O  
ATOM   5109  CB  LEU B 315      84.796  -2.637-173.689  1.00 33.97           C  
ANISOU 5109  CB  LEU B 315     4609   3981   4316    145    -75   -137       C  
ATOM   5110  CG  LEU B 315      84.351  -1.989-172.364  1.00 32.40           C  
ANISOU 5110  CG  LEU B 315     4314   3805   4190     56   -143   -107       C  
ATOM   5111  CD1 LEU B 315      84.274  -0.477-172.485  1.00 34.95           C  
ANISOU 5111  CD1 LEU B 315     4500   4224   4554      6   -149    -71       C  
ATOM   5112  CD2 LEU B 315      83.012  -2.583-171.897  1.00 29.24           C  
ANISOU 5112  CD2 LEU B 315     4011   3338   3761    -53   -203   -150       C  
ATOM   5113  N   GLU B 316      84.154  -5.228-175.740  1.00 32.27           N  
ANISOU 5113  N   GLU B 316     4828   3558   3875    196    -10   -294       N  
ATOM   5114  CA  GLU B 316      84.292  -5.714-177.106  1.00 28.37           C  
ANISOU 5114  CA  GLU B 316     4471   3034   3274    251     48   -347       C  
ATOM   5115  C   GLU B 316      83.086  -5.217-177.892  1.00 33.04           C  
ANISOU 5115  C   GLU B 316     5077   3678   3798    114    -14   -389       C  
ATOM   5116  O   GLU B 316      82.066  -4.823-177.320  1.00 33.26           O  
ANISOU 5116  O   GLU B 316     5044   3736   3858    -20    -98   -384       O  
ATOM   5117  CB  GLU B 316      84.399  -7.246-177.139  1.00 36.43           C  
ANISOU 5117  CB  GLU B 316     5713   3897   4232    302     84   -407       C  
ATOM   5118  CG  GLU B 316      83.114  -7.971-176.753  1.00 53.76           C  
ANISOU 5118  CG  GLU B 316     8036   5996   6394    140      1   -470       C  
ATOM   5119  CD  GLU B 316      83.125  -9.448-177.145  1.00 72.00           C  
ANISOU 5119  CD  GLU B 316    10610   8135   8614    170     44   -547       C  
ATOM   5120  OE1 GLU B 316      84.017 -10.184-176.670  1.00 74.10           O  
ANISOU 5120  OE1 GLU B 316    10941   8311   8904    310    115   -523       O  
ATOM   5121  OE2 GLU B 316      82.245  -9.867-177.933  1.00 72.44           O  
ANISOU 5121  OE2 GLU B 316    10810   8144   8569     55      7   -630       O  
ATOM   5122  N   HIS B 317      83.216  -5.216-179.218  1.00 37.36           N  
ANISOU 5122  N   HIS B 317     5701   4248   4247    156     30   -422       N  
ATOM   5123  CA  HIS B 317      82.137  -4.782-180.085  1.00 36.50           C  
ANISOU 5123  CA  HIS B 317     5609   4202   4055     40    -31   -457       C  
ATOM   5124  C   HIS B 317      81.621  -5.982-180.875  1.00 35.10           C  
ANISOU 5124  C   HIS B 317     5669   3926   3743     -6    -43   -559       C  
ATOM   5125  O   HIS B 317      82.416  -6.854-181.231  1.00 37.46           O  
ANISOU 5125  O   HIS B 317     6115   4127   3992    108     39   -596       O  
ATOM   5126  CB  HIS B 317      82.617  -3.680-181.043  1.00 33.25           C  
ANISOU 5126  CB  HIS B 317     5098   3913   3623    111     22   -408       C  
ATOM   5127  CG  HIS B 317      81.524  -3.086-181.877  1.00 41.65           C  
ANISOU 5127  CG  HIS B 317     6154   5066   4607      6    -44   -422       C  
ATOM   5128  ND1 HIS B 317      81.011  -3.719-182.992  1.00 38.38           N  
ANISOU 5128  ND1 HIS B 317     5906   4633   4043    -30    -62   -499       N  
ATOM   5129  CD2 HIS B 317      80.847  -1.917-181.759  1.00 33.94           C  
ANISOU 5129  CD2 HIS B 317     5026   4198   3670    -64    -96   -365       C  
ATOM   5130  CE1 HIS B 317      80.059  -2.970-183.520  1.00 43.44           C  
ANISOU 5130  CE1 HIS B 317     6483   5385   4637   -121   -132   -483       C  
ATOM   5131  NE2 HIS B 317      79.940  -1.871-182.795  1.00 36.12           N  
ANISOU 5131  NE2 HIS B 317     5365   4534   3825   -134   -147   -398       N  
ATOM   5132  N   PRO B 318      80.309  -6.100-181.110  1.00 35.11           N  
ANISOU 5132  N   PRO B 318     5715   3943   3681   -173   -143   -606       N  
ATOM   5133  CA  PRO B 318      79.797  -7.337-181.719  1.00 44.80           C  
ANISOU 5133  CA  PRO B 318     7181   5059   4783   -248   -167   -712       C  
ATOM   5134  C   PRO B 318      80.259  -7.548-183.147  1.00 45.66           C  
ANISOU 5134  C   PRO B 318     7434   5165   4749   -164   -105   -767       C  
ATOM   5135  O   PRO B 318      80.307  -8.697-183.605  1.00 50.86           O  
ANISOU 5135  O   PRO B 318     8329   5690   5306   -165    -81   -858       O  
ATOM   5136  CB  PRO B 318      78.273  -7.168-181.639  1.00 44.96           C  
ANISOU 5136  CB  PRO B 318     7158   5144   4779   -458   -299   -728       C  
ATOM   5137  CG  PRO B 318      78.056  -5.690-181.526  1.00 39.72           C  
ANISOU 5137  CG  PRO B 318     6254   4651   4185   -452   -323   -635       C  
ATOM   5138  CD  PRO B 318      79.215  -5.207-180.691  1.00 38.72           C  
ANISOU 5138  CD  PRO B 318     6012   4512   4187   -307   -239   -562       C  
ATOM   5139  N   THR B 319      80.580  -6.485-183.877  1.00 44.54           N  
ANISOU 5139  N   THR B 319     7173   5158   4591    -94    -74   -714       N  
ATOM   5140  CA  THR B 319      81.074  -6.651-185.231  1.00 42.65           C  
ANISOU 5140  CA  THR B 319     7071   4925   4211      0     -3   -758       C  
ATOM   5141  C   THR B 319      82.395  -5.951-185.525  1.00 50.10           C  
ANISOU 5141  C   THR B 319     7910   5928   5199    196    127   -678       C  
ATOM   5142  O   THR B 319      82.971  -6.221-186.569  1.00 32.95           O  
ANISOU 5142  O   THR B 319     5863   3742   2912    302    213   -710       O  
ATOM   5143  CB  THR B 319      80.021  -6.196-186.263  1.00 48.49           C  
ANISOU 5143  CB  THR B 319     7822   5779   4823   -123    -94   -786       C  
ATOM   5144  OG1 THR B 319      79.722  -4.811-186.091  1.00 47.20           O  
ANISOU 5144  OG1 THR B 319     7419   5775   4739   -140   -129   -685       O  
ATOM   5145  CG2 THR B 319      78.729  -6.993-186.114  1.00 50.87           C  
ANISOU 5145  CG2 THR B 319     8236   6031   5063   -330   -224   -869       C  
ATOM   5146  N   LEU B 320      82.910  -5.085-184.665  1.00 50.62           N  
ANISOU 5146  N   LEU B 320     7757   6058   5418    243    148   -578       N  
ATOM   5147  CA  LEU B 320      84.214  -4.472-184.927  1.00 43.71           C  
ANISOU 5147  CA  LEU B 320     6778   5242   4589    413    271   -499       C  
ATOM   5148  C   LEU B 320      85.251  -5.236-184.111  1.00 43.52           C  
ANISOU 5148  C   LEU B 320     6771   5120   4645    535    348   -484       C  
ATOM   5149  O   LEU B 320      85.468  -4.928-182.943  1.00 38.23           O  
ANISOU 5149  O   LEU B 320     5954   4461   4112    522    321   -425       O  
ATOM   5150  CB  LEU B 320      84.203  -2.985-184.580  1.00 38.68           C  
ANISOU 5150  CB  LEU B 320     5896   4739   4061    383    250   -397       C  
ATOM   5151  CG  LEU B 320      83.142  -2.118-185.267  1.00 39.34           C  
ANISOU 5151  CG  LEU B 320     5939   4930   4081    277    175   -389       C  
ATOM   5152  CD1 LEU B 320      83.116  -0.708-184.708  1.00 35.44           C  
ANISOU 5152  CD1 LEU B 320     5222   4534   3710    250    161   -287       C  
ATOM   5153  CD2 LEU B 320      83.415  -2.084-186.767  1.00 43.72           C  
ANISOU 5153  CD2 LEU B 320     6598   5528   4485    355    244   -407       C  
ATOM   5154  N   GLU B 321      85.901  -6.235-184.721  1.00 41.54           N  
ANISOU 5154  N   GLU B 321     6705   4775   4301    663    445   -533       N  
ATOM   5155  CA  GLU B 321      86.732  -7.136-183.915  1.00 43.56           C  
ANISOU 5155  CA  GLU B 321     7006   4924   4621    780    510   -521       C  
ATOM   5156  C   GLU B 321      87.986  -6.458-183.377  1.00 42.81           C  
ANISOU 5156  C   GLU B 321     6686   4922   4655    916    587   -400       C  
ATOM   5157  O   GLU B 321      88.524  -6.902-182.360  1.00 39.61           O  
ANISOU 5157  O   GLU B 321     6237   4471   4341    976    599   -362       O  
ATOM   5158  CB  GLU B 321      87.119  -8.388-184.709  1.00 45.77           C  
ANISOU 5158  CB  GLU B 321     7558   5068   4765    901    609   -601       C  
ATOM   5159  CG  GLU B 321      86.041  -9.461-184.738  1.00 49.50           C  
ANISOU 5159  CG  GLU B 321     8279   5388   5140    763    529   -724       C  
ATOM   5160  CD  GLU B 321      84.877  -9.093-185.631  1.00 56.22           C  
ANISOU 5160  CD  GLU B 321     9189   6298   5876    591    430   -793       C  
ATOM   5161  OE1 GLU B 321      85.062  -8.201-186.473  1.00 53.69           O  
ANISOU 5161  OE1 GLU B 321     8777   6108   5513    628    458   -757       O  
ATOM   5162  OE2 GLU B 321      83.783  -9.673-185.478  1.00 60.02           O  
ANISOU 5162  OE2 GLU B 321     9795   6702   6308    417    324   -875       O  
ATOM   5163  N   TRP B 322      88.465  -5.398-184.026  1.00 39.10           N  
ANISOU 5163  N   TRP B 322     6073   4588   4195    958    639   -334       N  
ATOM   5164  CA  TRP B 322      89.620  -4.685-183.502  1.00 39.18           C  
ANISOU 5164  CA  TRP B 322     5855   4698   4333   1054    701   -216       C  
ATOM   5165  C   TRP B 322      89.302  -3.938-182.208  1.00 39.90           C  
ANISOU 5165  C   TRP B 322     5756   4835   4567    927    592   -167       C  
ATOM   5166  O   TRP B 322      90.233  -3.510-181.516  1.00 38.83           O  
ANISOU 5166  O   TRP B 322     5443   4767   4544    985    621    -79       O  
ATOM   5167  CB  TRP B 322      90.156  -3.721-184.565  1.00 39.36           C  
ANISOU 5167  CB  TRP B 322     5783   4846   4327   1112    787   -156       C  
ATOM   5168  CG  TRP B 322      89.093  -2.876-185.160  1.00 37.62           C  
ANISOU 5168  CG  TRP B 322     5561   4679   4052    969    710   -181       C  
ATOM   5169  CD1 TRP B 322      88.465  -3.059-186.378  1.00 38.57           C  
ANISOU 5169  CD1 TRP B 322     5850   4792   4015    953    715   -250       C  
ATOM   5170  CD2 TRP B 322      88.522  -1.697-184.589  1.00 34.55           C  
ANISOU 5170  CD2 TRP B 322     5001   4367   3758    830    618   -134       C  
ATOM   5171  NE1 TRP B 322      87.536  -2.067-186.571  1.00 38.68           N  
ANISOU 5171  NE1 TRP B 322     5789   4883   4025    817    626   -237       N  
ATOM   5172  CE2 TRP B 322      87.555  -1.216-185.495  1.00 37.20           C  
ANISOU 5172  CE2 TRP B 322     5399   4743   3993    746    573   -166       C  
ATOM   5173  CE3 TRP B 322      88.729  -1.002-183.386  1.00 35.42           C  
ANISOU 5173  CE3 TRP B 322     4921   4515   4021    771    568    -68       C  
ATOM   5174  CZ2 TRP B 322      86.790  -0.076-185.238  1.00 38.99           C  
ANISOU 5174  CZ2 TRP B 322     5501   5040   4273    622    492   -127       C  
ATOM   5175  CZ3 TRP B 322      87.975   0.138-183.138  1.00 35.30           C  
ANISOU 5175  CZ3 TRP B 322     4798   4558   4054    639    491    -40       C  
ATOM   5176  CH2 TRP B 322      87.015   0.587-184.058  1.00 38.22           C  
ANISOU 5176  CH2 TRP B 322     5232   4962   4328    574    458    -66       C  
ATOM   5177  N   PHE B 323      88.019  -3.778-181.862  1.00 34.09           N  
ANISOU 5177  N   PHE B 323     5055   4073   3826    758    470   -220       N  
ATOM   5178  CA  PHE B 323      87.657  -2.968-180.694  1.00 30.40           C  
ANISOU 5178  CA  PHE B 323     4418   3651   3480    642    377   -174       C  
ATOM   5179  C   PHE B 323      88.209  -3.580-179.416  1.00 38.74           C  
ANISOU 5179  C   PHE B 323     5439   4656   4626    686    366   -149       C  
ATOM   5180  O   PHE B 323      88.672  -2.862-178.521  1.00 36.71           O  
ANISOU 5180  O   PHE B 323     5004   4467   4479    669    342    -79       O  
ATOM   5181  CB  PHE B 323      86.137  -2.808-180.597  1.00 34.58           C  
ANISOU 5181  CB  PHE B 323     5001   4162   3976    470    261   -232       C  
ATOM   5182  CG  PHE B 323      85.689  -1.701-179.648  1.00 39.58           C  
ANISOU 5182  CG  PHE B 323     5461   4861   4717    361    185   -180       C  
ATOM   5183  CD1 PHE B 323      85.528  -1.954-178.290  1.00 38.26           C  
ANISOU 5183  CD1 PHE B 323     5255   4649   4632    311    125   -173       C  
ATOM   5184  CD2 PHE B 323      85.419  -0.421-180.123  1.00 37.19           C  
ANISOU 5184  CD2 PHE B 323     5050   4656   4424    314    181   -136       C  
ATOM   5185  CE1 PHE B 323      85.123  -0.943-177.405  1.00 33.62           C  
ANISOU 5185  CE1 PHE B 323     4529   4114   4132    218     63   -131       C  
ATOM   5186  CE2 PHE B 323      84.999   0.595-179.247  1.00 36.80           C  
ANISOU 5186  CE2 PHE B 323     4866   4650   4468    223    122    -91       C  
ATOM   5187  CZ  PHE B 323      84.851   0.326-177.884  1.00 28.74           C  
ANISOU 5187  CZ  PHE B 323     3813   3582   3523    175     64    -93       C  
ATOM   5188  N   ALA B 324      88.197  -4.909-179.333  1.00 38.60           N  
ANISOU 5188  N   ALA B 324     5598   4515   4553    745    385   -204       N  
ATOM   5189  CA  ALA B 324      88.700  -5.591-178.144  1.00 38.77           C  
ANISOU 5189  CA  ALA B 324     5605   4480   4645    803    378   -173       C  
ATOM   5190  C   ALA B 324      90.173  -5.298-177.911  1.00 47.08           C  
ANISOU 5190  C   ALA B 324     6493   5623   5771    955    458    -73       C  
ATOM   5191  O   ALA B 324      90.642  -5.344-176.767  1.00 41.52           O  
ANISOU 5191  O   ALA B 324     5685   4938   5154    975    426    -18       O  
ATOM   5192  CB  ALA B 324      88.484  -7.095-178.279  1.00 39.70           C  
ANISOU 5192  CB  ALA B 324     5971   4435   4680    858    408   -246       C  
ATOM   5193  N   ALA B 325      90.915  -4.984-178.973  1.00 36.69           N  
ANISOU 5193  N   ALA B 325     5145   4377   4420   1060    560    -43       N  
ATOM   5194  CA  ALA B 325      92.340  -4.718-178.846  1.00 38.19           C  
ANISOU 5194  CA  ALA B 325     5163   4671   4679   1203    644     62       C  
ATOM   5195  C   ALA B 325      92.625  -3.351-178.240  1.00 38.19           C  
ANISOU 5195  C   ALA B 325     4912   4808   4792   1103    588    139       C  
ATOM   5196  O   ALA B 325      93.785  -3.051-177.941  1.00 42.48           O  
ANISOU 5196  O   ALA B 325     5281   5453   5408   1187    633    233       O  
ATOM   5197  CB  ALA B 325      93.029  -4.836-180.209  1.00 48.14           C  
ANISOU 5197  CB  ALA B 325     6472   5962   5859   1349    785     75       C  
ATOM   5198  N   LEU B 326      91.601  -2.519-178.068  1.00 33.96           N  
ANISOU 5198  N   LEU B 326     4355   4276   4270    928    494    104       N  
ATOM   5199  CA  LEU B 326      91.755  -1.277-177.321  1.00 37.74           C  
ANISOU 5199  CA  LEU B 326     4633   4852   4854    820    433    164       C  
ATOM   5200  C   LEU B 326      92.050  -1.546-175.855  1.00 39.06           C  
ANISOU 5200  C   LEU B 326     4725   5015   5099    806    361    193       C  
ATOM   5201  O   LEU B 326      92.569  -0.661-175.168  1.00 42.71           O  
ANISOU 5201  O   LEU B 326     5011   5568   5648    750    325    255       O  
ATOM   5202  CB  LEU B 326      90.493  -0.410-177.443  1.00 33.80           C  
ANISOU 5202  CB  LEU B 326     4158   4344   4343    654    357    119       C  
ATOM   5203  CG  LEU B 326      90.315   0.444-178.720  1.00 44.73           C  
ANISOU 5203  CG  LEU B 326     5534   5783   5679    638    412    128       C  
ATOM   5204  CD1 LEU B 326      90.726  -0.308-179.925  1.00 52.87           C  
ANISOU 5204  CD1 LEU B 326     6679   6798   6611    772    515    110       C  
ATOM   5205  CD2 LEU B 326      88.867   0.907-178.905  1.00 42.88           C  
ANISOU 5205  CD2 LEU B 326     5372   5519   5402    504    335     73       C  
ATOM   5206  N   GLY B 327      91.744  -2.750-175.374  1.00 35.66           N  
ANISOU 5206  N   GLY B 327     4435   4480   4634    853    341    151       N  
ATOM   5207  CA  GLY B 327      91.977  -3.081-173.978  1.00 37.11           C  
ANISOU 5207  CA  GLY B 327     4565   4656   4877    850    273    182       C  
ATOM   5208  C   GLY B 327      91.128  -2.293-173.007  1.00 40.97           C  
ANISOU 5208  C   GLY B 327     5002   5150   5414    675    158    164       C  
ATOM   5209  O   GLY B 327      91.564  -2.025-171.886  1.00 42.21           O  
ANISOU 5209  O   GLY B 327     5045   5357   5634    652    101    211       O  
ATOM   5210  N   LEU B 328      89.917  -1.924-173.400  1.00 31.54           N  
ANISOU 5210  N   LEU B 328     3890   3910   4182    556    124    100       N  
ATOM   5211  CA  LEU B 328      89.049  -1.140-172.537  1.00 31.98           C  
ANISOU 5211  CA  LEU B 328     3903   3970   4277    405     31     86       C  
ATOM   5212  C   LEU B 328      88.250  -2.047-171.606  1.00 33.71           C  
ANISOU 5212  C   LEU B 328     4238   4091   4479    367    -31     46       C  
ATOM   5213  O   LEU B 328      87.927  -3.194-171.931  1.00 36.51           O  
ANISOU 5213  O   LEU B 328     4747   4350   4774    414     -8      4       O  
ATOM   5214  CB  LEU B 328      88.099  -0.261-173.350  1.00 33.78           C  
ANISOU 5214  CB  LEU B 328     4145   4211   4477    306     26     54       C  
ATOM   5215  CG  LEU B 328      88.739   0.656-174.402  1.00 37.95           C  
ANISOU 5215  CG  LEU B 328     4583   4825   5011    336     96     94       C  
ATOM   5216  CD1 LEU B 328      87.678   1.321-175.275  1.00 36.18           C  
ANISOU 5216  CD1 LEU B 328     4407   4603   4738    258     92     63       C  
ATOM   5217  CD2 LEU B 328      89.613   1.714-173.766  1.00 39.93           C  
ANISOU 5217  CD2 LEU B 328     4656   5163   5352    305     88    164       C  
ATOM   5218  N   ARG B 329      87.962  -1.520-170.418  1.00 31.54           N  
ANISOU 5218  N   ARG B 329     3896   3835   4253    279   -105     62       N  
ATOM   5219  CA  ARG B 329      87.222  -2.219-169.381  1.00 37.87           C  
ANISOU 5219  CA  ARG B 329     4785   4558   5046    234   -163     39       C  
ATOM   5220  C   ARG B 329      86.349  -1.196-168.674  1.00 30.98           C  
ANISOU 5220  C   ARG B 329     3860   3710   4202     97   -228     32       C  
ATOM   5221  O   ARG B 329      86.636   0.000-168.696  1.00 34.39           O  
ANISOU 5221  O   ARG B 329     4176   4218   4672     56   -232     56       O  
ATOM   5222  CB  ARG B 329      88.156  -2.883-168.356  1.00 43.65           C  
ANISOU 5222  CB  ARG B 329     5490   5292   5803    325   -176     88       C  
ATOM   5223  CG  ARG B 329      89.312  -3.656-168.950  1.00 52.84           C  
ANISOU 5223  CG  ARG B 329     6659   6463   6955    490   -100    123       C  
ATOM   5224  CD  ARG B 329      90.430  -3.816-167.935  1.00 54.11           C  
ANISOU 5224  CD  ARG B 329     6710   6691   7158    575   -122    200       C  
ATOM   5225  NE  ARG B 329      89.964  -4.443-166.698  1.00 52.13           N  
ANISOU 5225  NE  ARG B 329     6532   6374   6899    551   -183    201       N  
ATOM   5226  CZ  ARG B 329      89.764  -5.753-166.552  1.00 65.36           C  
ANISOU 5226  CZ  ARG B 329     8366   7935   8535    630   -156    191       C  
ATOM   5227  NH1 ARG B 329      89.975  -6.580-167.566  1.00 64.30           N  
ANISOU 5227  NH1 ARG B 329     8343   7729   8359    737    -70    172       N  
ATOM   5228  NH2 ARG B 329      89.349  -6.244-165.392  1.00 65.99           N  
ANISOU 5228  NH2 ARG B 329     8506   7961   8609    603   -209    202       N  
ATOM   5229  N   TRP B 330      85.266  -1.666-168.063  1.00 34.09           N  
ANISOU 5229  N   TRP B 330     4344   4035   4573     27   -270      1       N  
ATOM   5230  CA  TRP B 330      84.608  -0.844-167.056  1.00 32.43           C  
ANISOU 5230  CA  TRP B 330     4084   3847   4391    -72   -324      8       C  
ATOM   5231  C   TRP B 330      84.087  -1.753-165.948  1.00 31.07           C  
ANISOU 5231  C   TRP B 330     3998   3604   4204    -91   -361      4       C  
ATOM   5232  O   TRP B 330      84.006  -2.975-166.107  1.00 29.74           O  
ANISOU 5232  O   TRP B 330     3941   3357   4003    -48   -344    -11       O  
ATOM   5233  CB  TRP B 330      83.491   0.033-167.639  1.00 27.51           C  
ANISOU 5233  CB  TRP B 330     3453   3243   3757   -164   -325    -15       C  
ATOM   5234  CG  TRP B 330      83.299   1.266-166.781  1.00 28.47           C  
ANISOU 5234  CG  TRP B 330     3493   3408   3918   -230   -354      7       C  
ATOM   5235  CD1 TRP B 330      82.306   1.490-165.885  1.00 25.54           C  
ANISOU 5235  CD1 TRP B 330     3144   3017   3544   -302   -386      2       C  
ATOM   5236  CD2 TRP B 330      84.162   2.412-166.727  1.00 32.64           C  
ANISOU 5236  CD2 TRP B 330     3915   3998   4489   -231   -346     35       C  
ATOM   5237  NE1 TRP B 330      82.482   2.723-165.277  1.00 27.48           N  
ANISOU 5237  NE1 TRP B 330     3320   3300   3822   -338   -396     20       N  
ATOM   5238  CE2 TRP B 330      83.622   3.302-165.762  1.00 30.56           C  
ANISOU 5238  CE2 TRP B 330     3634   3736   4241   -305   -376     38       C  
ATOM   5239  CE3 TRP B 330      85.335   2.778-167.404  1.00 30.80           C  
ANISOU 5239  CE3 TRP B 330     3604   3818   4281   -180   -311     61       C  
ATOM   5240  CZ2 TRP B 330      84.213   4.542-165.460  1.00 30.23           C  
ANISOU 5240  CZ2 TRP B 330     3516   3734   4237   -341   -378     56       C  
ATOM   5241  CZ3 TRP B 330      85.924   4.013-167.102  1.00 30.40           C  
ANISOU 5241  CZ3 TRP B 330     3457   3818   4274   -224   -315     87       C  
ATOM   5242  CH2 TRP B 330      85.358   4.880-166.143  1.00 27.50           C  
ANISOU 5242  CH2 TRP B 330     3093   3438   3920   -309   -351     80       C  
ATOM   5243  N   TYR B 331      83.771  -1.144-164.799  1.00 31.01           N  
ANISOU 5243  N   TYR B 331     3948   3617   4217   -152   -405     20       N  
ATOM   5244  CA  TYR B 331      83.309  -1.925-163.659  1.00 27.00           C  
ANISOU 5244  CA  TYR B 331     3515   3051   3692   -168   -435     27       C  
ATOM   5245  C   TYR B 331      81.778  -2.033-163.640  1.00 26.85           C  
ANISOU 5245  C   TYR B 331     3562   2989   3650   -268   -440      1       C  
ATOM   5246  O   TYR B 331      81.055  -1.199-164.192  1.00 29.58           O  
ANISOU 5246  O   TYR B 331     3869   3373   3999   -329   -434    -14       O  
ATOM   5247  CB  TYR B 331      83.830  -1.319-162.342  1.00 25.92           C  
ANISOU 5247  CB  TYR B 331     3311   2964   3575   -174   -480     61       C  
ATOM   5248  CG  TYR B 331      83.644   0.171-162.215  1.00 28.61           C  
ANISOU 5248  CG  TYR B 331     3566   3366   3937   -248   -493     56       C  
ATOM   5249  CD1 TYR B 331      82.474   0.699-161.686  1.00 28.21           C  
ANISOU 5249  CD1 TYR B 331     3543   3300   3875   -329   -500     43       C  
ATOM   5250  CD2 TYR B 331      84.641   1.058-162.617  1.00 27.17           C  
ANISOU 5250  CD2 TYR B 331     3281   3255   3789   -234   -490     69       C  
ATOM   5251  CE1 TYR B 331      82.310   2.044-161.542  1.00 25.16           C  
ANISOU 5251  CE1 TYR B 331     3102   2953   3505   -382   -500     39       C  
ATOM   5252  CE2 TYR B 331      84.469   2.406-162.479  1.00 28.54           C  
ANISOU 5252  CE2 TYR B 331     3400   3463   3981   -306   -495     63       C  
ATOM   5253  CZ  TYR B 331      83.297   2.883-161.934  1.00 29.19           C  
ANISOU 5253  CZ  TYR B 331     3530   3514   4046   -373   -499     46       C  
ATOM   5254  OH  TYR B 331      83.092   4.218-161.792  1.00 37.32           O  
ANISOU 5254  OH  TYR B 331     4528   4561   5089   -432   -492     40       O  
ATOM   5255  N   ALA B 332      81.296  -3.094-162.986  1.00 26.28           N  
ANISOU 5255  N   ALA B 332     3589   2841   3555   -280   -447      4       N  
ATOM   5256  CA  ALA B 332      79.866  -3.404-162.963  1.00 26.58           C  
ANISOU 5256  CA  ALA B 332     3687   2840   3571   -381   -450    -13       C  
ATOM   5257  C   ALA B 332      79.074  -2.432-162.090  1.00 29.59           C  
ANISOU 5257  C   ALA B 332     4006   3273   3964   -449   -467      7       C  
ATOM   5258  O   ALA B 332      77.938  -2.075-162.427  1.00 29.19           O  
ANISOU 5258  O   ALA B 332     3939   3246   3908   -526   -462      0       O  
ATOM   5259  CB  ALA B 332      79.648  -4.844-162.464  1.00 25.47           C  
ANISOU 5259  CB  ALA B 332     3677   2594   3406   -379   -445     -8       C  
ATOM   5260  N   LEU B 333      79.643  -2.011-160.951  1.00 25.85           N  
ANISOU 5260  N   LEU B 333     3501   2822   3501   -419   -486     34       N  
ATOM   5261  CA  LEU B 333      78.853  -1.419-159.874  1.00 30.13           C  
ANISOU 5261  CA  LEU B 333     4030   3382   4034   -474   -493     53       C  
ATOM   5262  C   LEU B 333      79.073   0.083-159.781  1.00 24.15           C  
ANISOU 5262  C   LEU B 333     3187   2693   3295   -481   -495     50       C  
ATOM   5263  O   LEU B 333      80.170   0.522-159.400  1.00 30.55           O  
ANISOU 5263  O   LEU B 333     3961   3532   4116   -442   -518     54       O  
ATOM   5264  CB  LEU B 333      79.203  -2.082-158.533  1.00 30.79           C  
ANISOU 5264  CB  LEU B 333     4171   3430   4096   -444   -513     83       C  
ATOM   5265  CG  LEU B 333      78.283  -1.677-157.377  1.00 32.75           C  
ANISOU 5265  CG  LEU B 333     4434   3687   4321   -496   -508    104       C  
ATOM   5266  CD1 LEU B 333      76.899  -2.249-157.617  1.00 31.53           C  
ANISOU 5266  CD1 LEU B 333     4319   3500   4161   -570   -478    110       C  
ATOM   5267  CD2 LEU B 333      78.855  -2.194-156.038  1.00 31.08           C  
ANISOU 5267  CD2 LEU B 333     4276   3456   4077   -453   -534    136       C  
ATOM   5268  N   PRO B 334      78.079   0.916-160.124  1.00 27.11           N  
ANISOU 5268  N   PRO B 334     3529   3098   3674   -530   -470     47       N  
ATOM   5269  CA  PRO B 334      78.207   2.357-159.856  1.00 27.67           C  
ANISOU 5269  CA  PRO B 334     3547   3209   3756   -535   -461     48       C  
ATOM   5270  C   PRO B 334      77.769   2.650-158.426  1.00 29.69           C  
ANISOU 5270  C   PRO B 334     3840   3455   3984   -552   -461     62       C  
ATOM   5271  O   PRO B 334      76.578   2.529-158.110  1.00 28.84           O  
ANISOU 5271  O   PRO B 334     3754   3344   3861   -582   -433     81       O  
ATOM   5272  CB  PRO B 334      77.256   2.989-160.874  1.00 26.93           C  
ANISOU 5272  CB  PRO B 334     3415   3147   3672   -559   -425     50       C  
ATOM   5273  CG  PRO B 334      76.153   1.957-161.000  1.00 30.58           C  
ANISOU 5273  CG  PRO B 334     3910   3595   4113   -599   -422     60       C  
ATOM   5274  CD  PRO B 334      76.802   0.585-160.792  1.00 31.22           C  
ANISOU 5274  CD  PRO B 334     4058   3620   4186   -583   -450     49       C  
ATOM   5275  N   ALA B 335      78.697   3.019-157.550  1.00 29.15           N  
ANISOU 5275  N   ALA B 335     3779   3390   3905   -537   -493     56       N  
ATOM   5276  CA  ALA B 335      78.372   3.156-156.124  1.00 26.62           C  
ANISOU 5276  CA  ALA B 335     3515   3058   3540   -549   -498     66       C  
ATOM   5277  C   ALA B 335      78.898   4.497-155.629  1.00 25.77           C  
ANISOU 5277  C   ALA B 335     3402   2967   3424   -565   -507     44       C  
ATOM   5278  O   ALA B 335      80.087   4.634-155.341  1.00 32.57           O  
ANISOU 5278  O   ALA B 335     4245   3848   4283   -563   -560     32       O  
ATOM   5279  CB  ALA B 335      78.939   1.989-155.302  1.00 27.64           C  
ANISOU 5279  CB  ALA B 335     3691   3169   3641   -520   -541     84       C  
ATOM   5280  N   VAL B 336      78.026   5.497-155.588  1.00 27.87           N  
ANISOU 5280  N   VAL B 336     3681   3224   3682   -582   -454     40       N  
ATOM   5281  CA  VAL B 336      78.448   6.840-155.220  1.00 25.63           C  
ANISOU 5281  CA  VAL B 336     3416   2933   3388   -604   -450     12       C  
ATOM   5282  C   VAL B 336      78.603   6.920-153.708  1.00 26.82           C  
ANISOU 5282  C   VAL B 336     3650   3071   3471   -616   -478      0       C  
ATOM   5283  O   VAL B 336      77.704   6.532-152.962  1.00 29.51           O  
ANISOU 5283  O   VAL B 336     4045   3398   3769   -601   -446     20       O  
ATOM   5284  CB  VAL B 336      77.454   7.873-155.746  1.00 31.02           C  
ANISOU 5284  CB  VAL B 336     4100   3601   4083   -599   -371     19       C  
ATOM   5285  CG1 VAL B 336      77.686   9.249-155.109  1.00 28.72           C  
ANISOU 5285  CG1 VAL B 336     3874   3273   3766   -620   -350    -11       C  
ATOM   5286  CG2 VAL B 336      77.660   7.936-157.281  1.00 33.77           C  
ANISOU 5286  CG2 VAL B 336     4367   3974   4491   -591   -362     27       C  
ATOM   5287  N   SER B 337      79.738   7.447-153.262  1.00 26.04           N  
ANISOU 5287  N   SER B 337     3556   2981   3356   -650   -537    -30       N  
ATOM   5288  CA  SER B 337      80.119   7.350-151.855  1.00 26.38           C  
ANISOU 5288  CA  SER B 337     3671   3028   3322   -665   -589    -43       C  
ATOM   5289  C   SER B 337      80.455   8.692-151.203  1.00 32.48           C  
ANISOU 5289  C   SER B 337     4513   3776   4050   -724   -598    -93       C  
ATOM   5290  O   SER B 337      80.831   8.711-150.019  1.00 34.52           O  
ANISOU 5290  O   SER B 337     4842   4043   4231   -748   -652   -112       O  
ATOM   5291  CB  SER B 337      81.304   6.385-151.739  1.00 29.02           C  
ANISOU 5291  CB  SER B 337     3949   3416   3661   -653   -680    -25       C  
ATOM   5292  OG  SER B 337      82.368   6.782-152.602  1.00 32.30           O  
ANISOU 5292  OG  SER B 337     4270   3867   4135   -677   -714    -35       O  
ATOM   5293  N   ASN B 338      80.309   9.813-151.913  1.00 31.90           N  
ANISOU 5293  N   ASN B 338     4438   3666   4015   -749   -546   -114       N  
ATOM   5294  CA  ASN B 338      80.727  11.108-151.377  1.00 33.93           C  
ANISOU 5294  CA  ASN B 338     4777   3881   4234   -818   -553   -167       C  
ATOM   5295  C   ASN B 338      79.565  12.060-151.139  1.00 30.14           C  
ANISOU 5295  C   ASN B 338     4410   3321   3721   -792   -445   -180       C  
ATOM   5296  O   ASN B 338      79.804  13.234-150.838  1.00 32.99           O  
ANISOU 5296  O   ASN B 338     4862   3620   4052   -845   -430   -228       O  
ATOM   5297  CB  ASN B 338      81.752  11.775-152.301  1.00 35.89           C  
ANISOU 5297  CB  ASN B 338     4946   4139   4550   -880   -582   -181       C  
ATOM   5298  CG  ASN B 338      81.182  12.083-153.666  1.00 33.95           C  
ANISOU 5298  CG  ASN B 338     4645   3872   4382   -839   -496   -153       C  
ATOM   5299  OD1 ASN B 338      80.039  11.733-153.971  1.00 35.37           O  
ANISOU 5299  OD1 ASN B 338     4830   4042   4567   -768   -428   -121       O  
ATOM   5300  ND2 ASN B 338      81.974  12.744-154.506  1.00 43.55           N  
ANISOU 5300  ND2 ASN B 338     5803   5089   5654   -889   -502   -158       N  
ATOM   5301  N   MET B 339      78.322  11.586-151.244  1.00 27.99           N  
ANISOU 5301  N   MET B 339     4137   3048   3450   -714   -368   -137       N  
ATOM   5302  CA  MET B 339      77.169  12.446-151.015  1.00 30.96           C  
ANISOU 5302  CA  MET B 339     4606   3364   3794   -667   -254   -132       C  
ATOM   5303  C   MET B 339      76.631  12.315-149.591  1.00 33.26           C  
ANISOU 5303  C   MET B 339     5018   3637   3983   -643   -231   -141       C  
ATOM   5304  O   MET B 339      76.866  11.326-148.903  1.00 32.35           O  
ANISOU 5304  O   MET B 339     4898   3565   3830   -648   -294   -132       O  
ATOM   5305  CB  MET B 339      76.073  12.135-152.033  1.00 32.78           C  
ANISOU 5305  CB  MET B 339     4747   3623   4087   -596   -177    -68       C  
ATOM   5306  CG  MET B 339      76.483  12.574-153.434  1.00 35.75           C  
ANISOU 5306  CG  MET B 339     5036   4004   4545   -609   -176    -62       C  
ATOM   5307  SD  MET B 339      75.131  12.472-154.626  1.00 35.96           S  
ANISOU 5307  SD  MET B 339     4971   4068   4622   -529    -87     12       S  
ATOM   5308  CE  MET B 339      74.141  13.891-154.133  1.00 33.58           C  
ANISOU 5308  CE  MET B 339     4787   3695   4277   -462     42     23       C  
ATOM   5309  N   LEU B 340      75.897  13.339-149.160  1.00 34.15           N  
ANISOU 5309  N   LEU B 340     5249   3680   4046   -607   -132   -155       N  
ATOM   5310  CA  LEU B 340      75.320  13.386-147.819  1.00 34.25           C  
ANISOU 5310  CA  LEU B 340     5397   3666   3949   -573    -87   -166       C  
ATOM   5311  C   LEU B 340      73.835  13.045-147.887  1.00 35.47           C  
ANISOU 5311  C   LEU B 340     5519   3846   4111   -470     31    -88       C  
ATOM   5312  O   LEU B 340      73.088  13.637-148.677  1.00 36.85           O  
ANISOU 5312  O   LEU B 340     5657   4009   4337   -413    122    -52       O  
ATOM   5313  CB  LEU B 340      75.524  14.766-147.196  1.00 34.68           C  
ANISOU 5313  CB  LEU B 340     5630   3618   3929   -598    -47   -237       C  
ATOM   5314  CG  LEU B 340      75.093  14.942-145.729  1.00 33.67           C  
ANISOU 5314  CG  LEU B 340     5678   3452   3664   -568     -3   -265       C  
ATOM   5315  CD1 LEU B 340      76.091  15.850-145.059  1.00 37.54           C  
ANISOU 5315  CD1 LEU B 340     6322   3869   4074   -668    -68   -366       C  
ATOM   5316  CD2 LEU B 340      73.689  15.544-145.692  1.00 36.24           C  
ANISOU 5316  CD2 LEU B 340     6067   3730   3971   -445    170   -222       C  
ATOM   5317  N   LEU B 341      73.413  12.095-147.059  1.00 32.75           N  
ANISOU 5317  N   LEU B 341     5184   3546   3716   -447     28    -55       N  
ATOM   5318  CA  LEU B 341      72.005  11.744-146.919  1.00 31.65           C  
ANISOU 5318  CA  LEU B 341     5015   3440   3571   -364    141     24       C  
ATOM   5319  C   LEU B 341      71.406  12.571-145.789  1.00 36.63           C  
ANISOU 5319  C   LEU B 341     5812   4014   4092   -300    248      9       C  
ATOM   5320  O   LEU B 341      71.901  12.524-144.662  1.00 37.43           O  
ANISOU 5320  O   LEU B 341     6040   4090   4092   -327    208    -38       O  
ATOM   5321  CB  LEU B 341      71.862  10.247-146.633  1.00 28.95           C  
ANISOU 5321  CB  LEU B 341     4601   3166   3233   -380     92     74       C  
ATOM   5322  CG  LEU B 341      70.483   9.731-146.216  1.00 32.44           C  
ANISOU 5322  CG  LEU B 341     5020   3651   3655   -318    199    159       C  
ATOM   5323  CD1 LEU B 341      69.458  10.058-147.299  1.00 30.15           C  
ANISOU 5323  CD1 LEU B 341     4610   3400   3447   -273    283    221       C  
ATOM   5324  CD2 LEU B 341      70.520   8.216-145.899  1.00 34.08           C  
ANISOU 5324  CD2 LEU B 341     5179   3905   3866   -355    141    202       C  
ATOM   5325  N   GLU B 342      70.342  13.317-146.078  1.00 33.89           N  
ANISOU 5325  N   GLU B 342     5468   3652   3756   -209    384     54       N  
ATOM   5326  CA  GLU B 342      69.663  14.120-145.067  1.00 38.29           C  
ANISOU 5326  CA  GLU B 342     6188   4151   4208   -123    512     49       C  
ATOM   5327  C   GLU B 342      68.246  13.601-144.877  1.00 34.62           C  
ANISOU 5327  C   GLU B 342     5645   3765   3743    -27    632    159       C  
ATOM   5328  O   GLU B 342      67.488  13.504-145.844  1.00 35.12           O  
ANISOU 5328  O   GLU B 342     5554   3892   3896     13    678    236       O  
ATOM   5329  CB  GLU B 342      69.628  15.605-145.453  1.00 39.23           C  
ANISOU 5329  CB  GLU B 342     6407   4172   4327    -77    595     13       C  
ATOM   5330  CG  GLU B 342      68.993  16.501-144.366  1.00 61.87           C  
ANISOU 5330  CG  GLU B 342     9480   6956   7071     22    738     -4       C  
ATOM   5331  CD  GLU B 342      67.533  16.875-144.642  1.00 74.53           C  
ANISOU 5331  CD  GLU B 342    11031   8592   8694    180    917    103       C  
ATOM   5332  OE1 GLU B 342      67.205  17.175-145.815  1.00 72.11           O  
ANISOU 5332  OE1 GLU B 342    10598   8312   8488    215    943    156       O  
ATOM   5333  OE2 GLU B 342      66.717  16.883-143.679  1.00 62.16           O  
ANISOU 5333  OE2 GLU B 342     9548   7032   7039    275   1034    139       O  
ATOM   5334  N   ILE B 343      67.896  13.260-143.639  1.00 35.03           N  
ANISOU 5334  N   ILE B 343     5795   3822   3692      5    679    170       N  
ATOM   5335  CA  ILE B 343      66.572  12.758-143.302  1.00 32.80           C  
ANISOU 5335  CA  ILE B 343     5443   3619   3400     90    801    281       C  
ATOM   5336  C   ILE B 343      66.115  13.516-142.054  1.00 44.75           C  
ANISOU 5336  C   ILE B 343     7156   5073   4775    190    934    267       C  
ATOM   5337  O   ILE B 343      66.772  13.443-141.006  1.00 42.40           O  
ANISOU 5337  O   ILE B 343     7019   4725   4365    153    886    197       O  
ATOM   5338  CB  ILE B 343      66.589  11.233-143.050  1.00 35.46           C  
ANISOU 5338  CB  ILE B 343     5683   4036   3754     19    723    328       C  
ATOM   5339  CG1 ILE B 343      67.038  10.459-144.292  1.00 35.58           C  
ANISOU 5339  CG1 ILE B 343     5525   4098   3897    -74    600    336       C  
ATOM   5340  CG2 ILE B 343      65.238  10.716-142.554  1.00 33.93           C  
ANISOU 5340  CG2 ILE B 343     5428   3922   3540     89    854    445       C  
ATOM   5341  CD1 ILE B 343      67.310   8.991-143.999  1.00 36.06           C  
ANISOU 5341  CD1 ILE B 343     5536   4201   3965   -150    512    362       C  
ATOM   5342  N   GLY B 344      65.011  14.249-142.169  1.00 40.75           N  
ANISOU 5342  N   GLY B 344     6643   4573   4268    322   1101    335       N  
ATOM   5343  CA  GLY B 344      64.418  14.885-140.989  1.00 46.77           C  
ANISOU 5343  CA  GLY B 344     7590   5286   4894    441   1256    338       C  
ATOM   5344  C   GLY B 344      65.378  15.755-140.211  1.00 47.44           C  
ANISOU 5344  C   GLY B 344     7941   5227   4857    414   1224    199       C  
ATOM   5345  O   GLY B 344      65.356  15.758-138.972  1.00 55.29           O  
ANISOU 5345  O   GLY B 344     9110   6188   5711    443   1269    169       O  
ATOM   5346  N   GLY B 345      66.232  16.502-140.917  1.00 44.98           N  
ANISOU 5346  N   GLY B 345     7669   4829   4591    350   1146    114       N  
ATOM   5347  CA  GLY B 345      67.226  17.334-140.284  1.00 44.09           C  
ANISOU 5347  CA  GLY B 345     7799   4582   4373    289   1095    -24       C  
ATOM   5348  C   GLY B 345      68.484  16.621-139.839  1.00 41.72           C  
ANISOU 5348  C   GLY B 345     7520   4297   4036    130    898   -105       C  
ATOM   5349  O   GLY B 345      69.473  17.290-139.517  1.00 46.79           O  
ANISOU 5349  O   GLY B 345     8324   4843   4611     42    818   -222       O  
ATOM   5350  N   LEU B 346      68.492  15.294-139.795  1.00 39.09           N  
ANISOU 5350  N   LEU B 346     7032   4078   3740     88    817    -44       N  
ATOM   5351  CA  LEU B 346      69.710  14.581-139.450  1.00 40.08           C  
ANISOU 5351  CA  LEU B 346     7162   4228   3839    -45    630   -106       C  
ATOM   5352  C   LEU B 346      70.548  14.387-140.700  1.00 43.90           C  
ANISOU 5352  C   LEU B 346     7480   4734   4466   -145    497   -122       C  
ATOM   5353  O   LEU B 346      70.022  14.274-141.810  1.00 40.53           O  
ANISOU 5353  O   LEU B 346     6888   4345   4166   -113    536    -56       O  
ATOM   5354  CB  LEU B 346      69.394  13.227-138.814  1.00 39.77           C  
ANISOU 5354  CB  LEU B 346     7053   4287   3770    -38    610    -30       C  
ATOM   5355  CG  LEU B 346      68.453  13.279-137.622  1.00 38.78           C  
ANISOU 5355  CG  LEU B 346     7066   4160   3510     70    758     11       C  
ATOM   5356  CD1 LEU B 346      68.067  11.870-137.171  1.00 46.27           C  
ANISOU 5356  CD1 LEU B 346     7917   5209   4456     72    747    107       C  
ATOM   5357  CD2 LEU B 346      69.105  14.062-136.480  1.00 39.98           C  
ANISOU 5357  CD2 LEU B 346     7485   4222   3483     52    736   -105       C  
ATOM   5358  N   GLU B 347      71.861  14.352-140.522  1.00 36.50           N  
ANISOU 5358  N   GLU B 347     6584   3781   3501   -264    339   -207       N  
ATOM   5359  CA  GLU B 347      72.776  14.286-141.656  1.00 37.86           C  
ANISOU 5359  CA  GLU B 347     6616   3970   3798   -356    219   -228       C  
ATOM   5360  C   GLU B 347      73.653  13.054-141.521  1.00 35.95           C  
ANISOU 5360  C   GLU B 347     6273   3817   3570   -432     62   -217       C  
ATOM   5361  O   GLU B 347      74.210  12.797-140.444  1.00 40.00           O  
ANISOU 5361  O   GLU B 347     6890   4341   3966   -468    -12   -254       O  
ATOM   5362  CB  GLU B 347      73.627  15.568-141.755  1.00 38.13           C  
ANISOU 5362  CB  GLU B 347     6778   3903   3807   -434    182   -334       C  
ATOM   5363  CG  GLU B 347      72.799  16.849-141.892  1.00 47.70           C  
ANISOU 5363  CG  GLU B 347     8117   5004   5001   -348    349   -344       C  
ATOM   5364  CD  GLU B 347      73.645  18.119-141.856  1.00 55.80           C  
ANISOU 5364  CD  GLU B 347     9308   5905   5986   -439    318   -455       C  
ATOM   5365  OE1 GLU B 347      74.442  18.284-140.913  1.00 51.50           O  
ANISOU 5365  OE1 GLU B 347     8908   5333   5326   -533    227   -543       O  
ATOM   5366  OE2 GLU B 347      73.517  18.945-142.781  1.00 55.65           O  
ANISOU 5366  OE2 GLU B 347     9276   5818   6049   -422    383   -452       O  
ATOM   5367  N   PHE B 348      73.750  12.291-142.609  1.00 33.46           N  
ANISOU 5367  N   PHE B 348     5762   3562   3387   -446     17   -163       N  
ATOM   5368  CA  PHE B 348      74.563  11.078-142.692  1.00 35.19           C  
ANISOU 5368  CA  PHE B 348     5874   3857   3640   -499   -117   -142       C  
ATOM   5369  C   PHE B 348      75.629  11.359-143.746  1.00 31.49           C  
ANISOU 5369  C   PHE B 348     5305   3392   3268   -576   -216   -181       C  
ATOM   5370  O   PHE B 348      75.396  11.147-144.947  1.00 33.21           O  
ANISOU 5370  O   PHE B 348     5385   3628   3605   -563   -195   -142       O  
ATOM   5371  CB  PHE B 348      73.708   9.853-143.042  1.00 34.86           C  
ANISOU 5371  CB  PHE B 348     5708   3874   3662   -446    -73    -43       C  
ATOM   5372  CG  PHE B 348      72.624   9.558-142.037  1.00 33.73           C  
ANISOU 5372  CG  PHE B 348     5647   3737   3432   -375     35     10       C  
ATOM   5373  CD1 PHE B 348      71.384  10.173-142.131  1.00 35.23           C  
ANISOU 5373  CD1 PHE B 348     5852   3909   3626   -298    189     47       C  
ATOM   5374  CD2 PHE B 348      72.858   8.679-140.987  1.00 34.61           C  
ANISOU 5374  CD2 PHE B 348     5819   3879   3455   -377    -11     31       C  
ATOM   5375  CE1 PHE B 348      70.386   9.919-141.197  1.00 34.97           C  
ANISOU 5375  CE1 PHE B 348     5885   3891   3512   -227    300    105       C  
ATOM   5376  CE2 PHE B 348      71.869   8.404-140.038  1.00 36.41           C  
ANISOU 5376  CE2 PHE B 348     6125   4114   3596   -311     97     87       C  
ATOM   5377  CZ  PHE B 348      70.637   9.026-140.122  1.00 35.41           C  
ANISOU 5377  CZ  PHE B 348     6007   3971   3474   -238    255    123       C  
ATOM   5378  N   PRO B 349      76.794  11.889-143.350  1.00 32.39           N  
ANISOU 5378  N   PRO B 349     5483   3492   3330   -662   -320   -256       N  
ATOM   5379  CA  PRO B 349      77.830  12.228-144.339  1.00 37.24           C  
ANISOU 5379  CA  PRO B 349     5997   4117   4038   -741   -404   -286       C  
ATOM   5380  C   PRO B 349      78.451  11.025-145.014  1.00 43.84           C  
ANISOU 5380  C   PRO B 349     6657   5038   4960   -745   -494   -235       C  
ATOM   5381  O   PRO B 349      79.140  11.197-146.022  1.00 36.02           O  
ANISOU 5381  O   PRO B 349     5560   4064   4063   -787   -536   -242       O  
ATOM   5382  CB  PRO B 349      78.875  13.003-143.519  1.00 38.62           C  
ANISOU 5382  CB  PRO B 349     6289   4269   4115   -844   -500   -374       C  
ATOM   5383  CG  PRO B 349      78.194  13.341-142.204  1.00 36.69           C  
ANISOU 5383  CG  PRO B 349     6243   3976   3722   -807   -436   -403       C  
ATOM   5384  CD  PRO B 349      77.201  12.242-141.976  1.00 31.40           C  
ANISOU 5384  CD  PRO B 349     5529   3350   3052   -698   -367   -316       C  
ATOM   5385  N   ALA B 350      78.233   9.819-144.507  1.00 33.95           N  
ANISOU 5385  N   ALA B 350     5383   3838   3679   -698   -514   -181       N  
ATOM   5386  CA  ALA B 350      78.750   8.607-145.122  1.00 29.74           C  
ANISOU 5386  CA  ALA B 350     4710   3369   3222   -686   -582   -129       C  
ATOM   5387  C   ALA B 350      77.577   7.661-145.315  1.00 33.30           C  
ANISOU 5387  C   ALA B 350     5131   3818   3705   -614   -494    -58       C  
ATOM   5388  O   ALA B 350      77.091   7.057-144.351  1.00 34.19           O  
ANISOU 5388  O   ALA B 350     5314   3935   3740   -579   -472    -24       O  
ATOM   5389  CB  ALA B 350      79.849   7.969-144.268  1.00 31.00           C  
ANISOU 5389  CB  ALA B 350     4876   3592   3311   -710   -711   -128       C  
ATOM   5390  N   ALA B 351      77.120   7.519-146.565  1.00 28.66           N  
ANISOU 5390  N   ALA B 351     4438   3226   3225   -600   -446    -31       N  
ATOM   5391  CA  ALA B 351      76.016   6.616-146.834  1.00 29.68           C  
ANISOU 5391  CA  ALA B 351     4528   3361   3389   -556   -374     35       C  
ATOM   5392  C   ALA B 351      76.078   6.189-148.301  1.00 30.67           C  
ANISOU 5392  C   ALA B 351     4524   3501   3629   -563   -382     53       C  
ATOM   5393  O   ALA B 351      75.275   6.676-149.112  1.00 29.75           O  
ANISOU 5393  O   ALA B 351     4362   3378   3563   -553   -310     63       O  
ATOM   5394  CB  ALA B 351      74.677   7.282-146.532  1.00 30.03           C  
ANISOU 5394  CB  ALA B 351     4627   3380   3402   -520   -249     52       C  
ATOM   5395  N   PRO B 352      77.040   5.346-148.685  1.00 31.23           N  
ANISOU 5395  N   PRO B 352     4537   3595   3734   -571   -466     57       N  
ATOM   5396  CA  PRO B 352      77.199   5.015-150.117  1.00 30.17           C  
ANISOU 5396  CA  PRO B 352     4297   3470   3697   -574   -471     64       C  
ATOM   5397  C   PRO B 352      75.991   4.264-150.631  1.00 25.92           C  
ANISOU 5397  C   PRO B 352     3731   2926   3193   -563   -406    110       C  
ATOM   5398  O   PRO B 352      75.431   3.408-149.945  1.00 28.88           O  
ANISOU 5398  O   PRO B 352     4148   3292   3532   -555   -387    150       O  
ATOM   5399  CB  PRO B 352      78.459   4.133-150.148  1.00 26.97           C  
ANISOU 5399  CB  PRO B 352     3859   3089   3301   -564   -563     68       C  
ATOM   5400  CG  PRO B 352      78.509   3.508-148.725  1.00 27.90           C  
ANISOU 5400  CG  PRO B 352     4064   3208   3329   -545   -591     93       C  
ATOM   5401  CD  PRO B 352      77.969   4.586-147.827  1.00 31.22           C  
ANISOU 5401  CD  PRO B 352     4568   3615   3678   -564   -552     66       C  
ATOM   5402  N   PHE B 353      75.608   4.565-151.884  1.00 27.14           N  
ANISOU 5402  N   PHE B 353     3810   3089   3414   -571   -375    108       N  
ATOM   5403  CA  PHE B 353      74.465   3.920-152.498  1.00 26.32           C  
ANISOU 5403  CA  PHE B 353     3665   2995   3342   -579   -326    150       C  
ATOM   5404  C   PHE B 353      74.836   3.504-153.933  1.00 28.38           C  
ANISOU 5404  C   PHE B 353     3852   3265   3667   -591   -357    138       C  
ATOM   5405  O   PHE B 353      75.708   4.103-154.564  1.00 29.13           O  
ANISOU 5405  O   PHE B 353     3914   3366   3789   -584   -385    105       O  
ATOM   5406  CB  PHE B 353      73.227   4.856-152.534  1.00 26.42           C  
ANISOU 5406  CB  PHE B 353     3662   3027   3349   -569   -239    173       C  
ATOM   5407  CG  PHE B 353      73.497   6.231-153.145  1.00 33.07           C  
ANISOU 5407  CG  PHE B 353     4482   3869   4213   -552   -220    141       C  
ATOM   5408  CD1 PHE B 353      73.411   6.437-154.526  1.00 32.50           C  
ANISOU 5408  CD1 PHE B 353     4328   3823   4200   -555   -218    144       C  
ATOM   5409  CD2 PHE B 353      73.797   7.317-152.332  1.00 31.33           C  
ANISOU 5409  CD2 PHE B 353     4339   3618   3947   -536   -200    111       C  
ATOM   5410  CE1 PHE B 353      73.631   7.697-155.068  1.00 30.63           C  
ANISOU 5410  CE1 PHE B 353     4080   3577   3981   -537   -192    126       C  
ATOM   5411  CE2 PHE B 353      74.029   8.571-152.866  1.00 31.87           C  
ANISOU 5411  CE2 PHE B 353     4407   3667   4035   -528   -175     84       C  
ATOM   5412  CZ  PHE B 353      73.943   8.770-154.245  1.00 33.71           C  
ANISOU 5412  CZ  PHE B 353     4552   3924   4333   -525   -167     97       C  
ATOM   5413  N   SER B 354      74.198   2.444-154.414  1.00 26.40           N  
ANISOU 5413  N   SER B 354     3585   3011   3434   -615   -350    165       N  
ATOM   5414  CA  SER B 354      74.548   1.877-155.712  1.00 29.37           C  
ANISOU 5414  CA  SER B 354     3919   3386   3853   -626   -379    148       C  
ATOM   5415  C   SER B 354      73.298   1.370-156.401  1.00 33.44           C  
ANISOU 5415  C   SER B 354     4401   3922   4383   -675   -349    176       C  
ATOM   5416  O   SER B 354      72.329   0.986-155.748  1.00 29.21           O  
ANISOU 5416  O   SER B 354     3880   3390   3829   -706   -317    215       O  
ATOM   5417  CB  SER B 354      75.568   0.732-155.601  1.00 28.59           C  
ANISOU 5417  CB  SER B 354     3866   3245   3753   -607   -429    139       C  
ATOM   5418  OG  SER B 354      75.077  -0.324-154.782  1.00 32.42           O  
ANISOU 5418  OG  SER B 354     4418   3690   4208   -623   -420    173       O  
ATOM   5419  N   GLY B 355      73.317   1.415-157.744  1.00 30.92           N  
ANISOU 5419  N   GLY B 355     4030   3625   4093   -687   -361    157       N  
ATOM   5420  CA  GLY B 355      72.269   0.842-158.556  1.00 29.33           C  
ANISOU 5420  CA  GLY B 355     3795   3451   3898   -748   -355    175       C  
ATOM   5421  C   GLY B 355      72.882   0.004-159.663  1.00 33.73           C  
ANISOU 5421  C   GLY B 355     4375   3976   4464   -761   -395    136       C  
ATOM   5422  O   GLY B 355      73.688  -0.889-159.403  1.00 30.90           O  
ANISOU 5422  O   GLY B 355     4089   3550   4101   -743   -417    118       O  
ATOM   5423  N   TRP B 356      72.539   0.302-160.909  1.00 29.14           N  
ANISOU 5423  N   TRP B 356     3739   3444   3889   -779   -400    126       N  
ATOM   5424  CA  TRP B 356      73.229  -0.278-162.048  1.00 26.18           C  
ANISOU 5424  CA  TRP B 356     3394   3042   3512   -774   -429     82       C  
ATOM   5425  C   TRP B 356      73.341   0.811-163.109  1.00 27.54           C  
ANISOU 5425  C   TRP B 356     3492   3282   3692   -742   -422     77       C  
ATOM   5426  O   TRP B 356      72.694   1.859-163.021  1.00 28.32           O  
ANISOU 5426  O   TRP B 356     3522   3442   3796   -734   -396    111       O  
ATOM   5427  CB  TRP B 356      72.526  -1.521-162.608  1.00 29.88           C  
ANISOU 5427  CB  TRP B 356     3910   3483   3958   -862   -451     71       C  
ATOM   5428  CG  TRP B 356      71.084  -1.327-162.945  1.00 29.93           C  
ANISOU 5428  CG  TRP B 356     3844   3573   3955   -946   -452    105       C  
ATOM   5429  CD1 TRP B 356      70.555  -0.720-164.073  1.00 32.18           C  
ANISOU 5429  CD1 TRP B 356     4051   3949   4229   -962   -463    109       C  
ATOM   5430  CD2 TRP B 356      69.975  -1.761-162.159  1.00 32.45           C  
ANISOU 5430  CD2 TRP B 356     4150   3907   4273  -1025   -440    151       C  
ATOM   5431  NE1 TRP B 356      69.177  -0.748-164.005  1.00 31.55           N  
ANISOU 5431  NE1 TRP B 356     3899   3948   4141  -1044   -466    158       N  
ATOM   5432  CE2 TRP B 356      68.799  -1.377-162.843  1.00 32.96           C  
ANISOU 5432  CE2 TRP B 356     4112   4082   4328  -1087   -448    185       C  
ATOM   5433  CE3 TRP B 356      69.862  -2.419-160.914  1.00 31.14           C  
ANISOU 5433  CE3 TRP B 356     4043   3678   4109  -1045   -420    176       C  
ATOM   5434  CZ2 TRP B 356      67.525  -1.649-162.347  1.00 36.84           C  
ANISOU 5434  CZ2 TRP B 356     4547   4630   4820  -1174   -437    244       C  
ATOM   5435  CZ3 TRP B 356      68.592  -2.694-160.423  1.00 39.74           C  
ANISOU 5435  CZ3 TRP B 356     5091   4813   5197  -1133   -402    232       C  
ATOM   5436  CH2 TRP B 356      67.438  -2.307-161.137  1.00 39.50           C  
ANISOU 5436  CH2 TRP B 356     4945   4900   5164  -1199   -410    267       C  
ATOM   5437  N   TYR B 357      74.216   0.579-164.074  1.00 27.79           N  
ANISOU 5437  N   TYR B 357     3544   3295   3719   -710   -435     40       N  
ATOM   5438  CA  TYR B 357      74.555   1.629-165.025  1.00 30.01           C  
ANISOU 5438  CA  TYR B 357     3765   3630   4007   -667   -421     39       C  
ATOM   5439  C   TYR B 357      73.508   1.783-166.120  1.00 29.28           C  
ANISOU 5439  C   TYR B 357     3629   3610   3885   -711   -428     51       C  
ATOM   5440  O   TYR B 357      72.903   0.809-166.576  1.00 29.57           O  
ANISOU 5440  O   TYR B 357     3700   3645   3891   -778   -458     35       O  
ATOM   5441  CB  TYR B 357      75.887   1.326-165.688  1.00 23.74           C  
ANISOU 5441  CB  TYR B 357     3003   2802   3215   -611   -423      4       C  
ATOM   5442  CG  TYR B 357      77.076   1.971-165.024  1.00 28.43           C  
ANISOU 5442  CG  TYR B 357     3575   3383   3844   -551   -412      9       C  
ATOM   5443  CD1 TYR B 357      77.246   3.346-165.056  1.00 30.14           C  
ANISOU 5443  CD1 TYR B 357     3729   3639   4084   -533   -388     28       C  
ATOM   5444  CD2 TYR B 357      78.057   1.198-164.400  1.00 29.94           C  
ANISOU 5444  CD2 TYR B 357     3810   3523   4043   -515   -426     -2       C  
ATOM   5445  CE1 TYR B 357      78.354   3.957-164.467  1.00 32.42           C  
ANISOU 5445  CE1 TYR B 357     3999   3919   4402   -503   -386     29       C  
ATOM   5446  CE2 TYR B 357      79.178   1.801-163.802  1.00 26.93           C  
ANISOU 5446  CE2 TYR B 357     3392   3150   3689   -472   -429      7       C  
ATOM   5447  CZ  TYR B 357      79.310   3.174-163.840  1.00 28.12           C  
ANISOU 5447  CZ  TYR B 357     3480   3342   3863   -478   -413     18       C  
ATOM   5448  OH  TYR B 357      80.416   3.765-163.301  1.00 28.62           O  
ANISOU 5448  OH  TYR B 357     3508   3417   3951   -459   -423     23       O  
ATOM   5449  N   MET B 358      73.333   3.031-166.568  1.00 30.44           N  
ANISOU 5449  N   MET B 358     3705   3822   4040   -673   -402     82       N  
ATOM   5450  CA  MET B 358      72.798   3.324-167.892  1.00 28.07           C  
ANISOU 5450  CA  MET B 358     3362   3597   3705   -680   -410     93       C  
ATOM   5451  C   MET B 358      73.970   3.425-168.865  1.00 27.22           C  
ANISOU 5451  C   MET B 358     3280   3471   3590   -627   -401     60       C  
ATOM   5452  O   MET B 358      74.987   4.048-168.562  1.00 28.84           O  
ANISOU 5452  O   MET B 358     3482   3643   3832   -570   -371     60       O  
ATOM   5453  CB  MET B 358      71.983   4.621-167.863  1.00 29.71           C  
ANISOU 5453  CB  MET B 358     3484   3882   3921   -650   -375    158       C  
ATOM   5454  CG  MET B 358      71.431   5.048-169.269  1.00 35.74           C  
ANISOU 5454  CG  MET B 358     4195   4743   4644   -642   -384    185       C  
ATOM   5455  SD  MET B 358      70.212   6.325-169.101  1.00 48.44           S  
ANISOU 5455  SD  MET B 358     5702   6446   6256   -599   -342    279       S  
ATOM   5456  CE  MET B 358      71.287   7.734-168.920  1.00 34.37           C  
ANISOU 5456  CE  MET B 358     3945   4598   4517   -501   -269    286       C  
ATOM   5457  N   SER B 359      73.835   2.807-170.044  1.00 28.30           N  
ANISOU 5457  N   SER B 359     3445   3632   3674   -649   -427     34       N  
ATOM   5458  CA  SER B 359      75.025   2.584-170.860  1.00 27.62           C  
ANISOU 5458  CA  SER B 359     3407   3513   3574   -594   -411     -4       C  
ATOM   5459  C   SER B 359      75.697   3.883-171.291  1.00 24.58           C  
ANISOU 5459  C   SER B 359     2964   3162   3214   -521   -364     29       C  
ATOM   5460  O   SER B 359      76.925   3.905-171.482  1.00 29.89           O  
ANISOU 5460  O   SER B 359     3651   3799   3904   -466   -335     14       O  
ATOM   5461  CB  SER B 359      74.656   1.728-172.077  1.00 31.28           C  
ANISOU 5461  CB  SER B 359     3929   3995   3960   -633   -444    -43       C  
ATOM   5462  OG  SER B 359      73.542   2.288-172.751  1.00 29.11           O  
ANISOU 5462  OG  SER B 359     3590   3825   3645   -670   -468     -7       O  
ATOM   5463  N   THR B 360      74.925   4.977-171.456  1.00 29.10           N  
ANISOU 5463  N   THR B 360     3468   3801   3787   -516   -348     82       N  
ATOM   5464  CA  THR B 360      75.515   6.239-171.906  1.00 28.81           C  
ANISOU 5464  CA  THR B 360     3392   3782   3772   -453   -295    119       C  
ATOM   5465  C   THR B 360      76.450   6.827-170.862  1.00 28.44           C  
ANISOU 5465  C   THR B 360     3340   3671   3794   -432   -264    120       C  
ATOM   5466  O   THR B 360      77.366   7.570-171.212  1.00 29.52           O  
ANISOU 5466  O   THR B 360     3460   3799   3955   -395   -223    133       O  
ATOM   5467  CB  THR B 360      74.446   7.285-172.258  1.00 35.32           C  
ANISOU 5467  CB  THR B 360     4158   4683   4581   -438   -278    184       C  
ATOM   5468  OG1 THR B 360      73.542   7.458-171.168  1.00 35.74           O  
ANISOU 5468  OG1 THR B 360     4184   4737   4659   -463   -282    210       O  
ATOM   5469  CG2 THR B 360      73.664   6.883-173.500  1.00 34.00           C  
ANISOU 5469  CG2 THR B 360     3981   4604   4334   -455   -315    192       C  
ATOM   5470  N   GLU B 361      76.253   6.519-169.575  1.00 28.29           N  
ANISOU 5470  N   GLU B 361     3334   3611   3803   -463   -283    109       N  
ATOM   5471  CA  GLU B 361      77.222   7.019-168.598  1.00 27.19           C  
ANISOU 5471  CA  GLU B 361     3197   3418   3716   -453   -267    103       C  
ATOM   5472  C   GLU B 361      78.621   6.507-168.918  1.00 23.46           C  
ANISOU 5472  C   GLU B 361     2731   2925   3256   -428   -270     76       C  
ATOM   5473  O   GLU B 361      79.608   7.245-168.824  1.00 31.06           O  
ANISOU 5473  O   GLU B 361     3665   3879   4257   -413   -245     86       O  
ATOM   5474  CB  GLU B 361      76.837   6.588-167.177  1.00 30.89           C  
ANISOU 5474  CB  GLU B 361     3692   3850   4195   -486   -293     92       C  
ATOM   5475  CG  GLU B 361      75.434   6.938-166.761  1.00 26.02           C  
ANISOU 5475  CG  GLU B 361     3063   3261   3564   -504   -282    125       C  
ATOM   5476  CD  GLU B 361      75.147   6.399-165.360  1.00 37.27           C  
ANISOU 5476  CD  GLU B 361     4522   4648   4993   -533   -300    116       C  
ATOM   5477  OE1 GLU B 361      75.666   6.985-164.386  1.00 36.36           O  
ANISOU 5477  OE1 GLU B 361     4427   4492   4897   -526   -288    111       O  
ATOM   5478  OE2 GLU B 361      74.442   5.380-165.243  1.00 33.56           O  
ANISOU 5478  OE2 GLU B 361     4065   4187   4501   -571   -328    113       O  
ATOM   5479  N   ILE B 362      78.717   5.244-169.310  1.00 25.03           N  
ANISOU 5479  N   ILE B 362     2970   3115   3424   -423   -295     44       N  
ATOM   5480  CA  ILE B 362      80.006   4.645-169.636  1.00 29.23           C  
ANISOU 5480  CA  ILE B 362     3513   3631   3964   -376   -286     26       C  
ATOM   5481  C   ILE B 362      80.433   5.002-171.052  1.00 29.40           C  
ANISOU 5481  C   ILE B 362     3516   3692   3962   -334   -244     36       C  
ATOM   5482  O   ILE B 362      81.539   5.500-171.277  1.00 29.38           O  
ANISOU 5482  O   ILE B 362     3469   3703   3991   -298   -209     55       O  
ATOM   5483  CB  ILE B 362      79.933   3.117-169.484  1.00 29.40           C  
ANISOU 5483  CB  ILE B 362     3610   3607   3953   -374   -316    -12       C  
ATOM   5484  CG1 ILE B 362      79.505   2.733-168.061  1.00 26.46           C  
ANISOU 5484  CG1 ILE B 362     3260   3194   3598   -414   -352    -13       C  
ATOM   5485  CG2 ILE B 362      81.276   2.494-169.859  1.00 31.99           C  
ANISOU 5485  CG2 ILE B 362     3950   3919   4285   -300   -293    -21       C  
ATOM   5486  CD1 ILE B 362      79.077   1.276-167.943  1.00 27.13           C  
ANISOU 5486  CD1 ILE B 362     3435   3225   3649   -433   -377    -43       C  
ATOM   5487  N   GLY B 363      79.592   4.663-172.022  1.00 27.63           N  
ANISOU 5487  N   GLY B 363     3327   3494   3676   -342   -250     25       N  
ATOM   5488  CA  GLY B 363      80.008   4.761-173.411  1.00 30.68           C  
ANISOU 5488  CA  GLY B 363     3720   3917   4019   -295   -212     28       C  
ATOM   5489  C   GLY B 363      80.180   6.195-173.871  1.00 35.35           C  
ANISOU 5489  C   GLY B 363     4245   4552   4634   -277   -165     82       C  
ATOM   5490  O   GLY B 363      81.114   6.512-174.606  1.00 36.51           O  
ANISOU 5490  O   GLY B 363     4372   4717   4783   -229   -114    100       O  
ATOM   5491  N   THR B 364      79.291   7.082-173.443  1.00 29.79           N  
ANISOU 5491  N   THR B 364     3510   3861   3946   -310   -172    114       N  
ATOM   5492  CA  THR B 364      79.386   8.460-173.901  1.00 30.12           C  
ANISOU 5492  CA  THR B 364     3510   3928   4006   -289   -118    170       C  
ATOM   5493  C   THR B 364      80.236   9.313-172.960  1.00 33.42           C  
ANISOU 5493  C   THR B 364     3894   4299   4503   -304    -91    186       C  
ATOM   5494  O   THR B 364      81.219   9.925-173.386  1.00 31.69           O  
ANISOU 5494  O   THR B 364     3647   4082   4313   -288    -43    211       O  
ATOM   5495  CB  THR B 364      77.986   9.053-174.060  1.00 28.69           C  
ANISOU 5495  CB  THR B 364     3319   3788   3794   -297   -126    207       C  
ATOM   5496  OG1 THR B 364      77.182   8.165-174.837  1.00 31.21           O  
ANISOU 5496  OG1 THR B 364     3663   4161   4035   -307   -171    187       O  
ATOM   5497  CG2 THR B 364      78.077  10.376-174.793  1.00 32.54           C  
ANISOU 5497  CG2 THR B 364     3782   4298   4284   -256    -61    272       C  
ATOM   5498  N   ARG B 365      79.893   9.355-171.671  1.00 28.64           N  
ANISOU 5498  N   ARG B 365     3296   3654   3930   -344   -122    171       N  
ATOM   5499  CA  ARG B 365      80.606  10.305-170.822  1.00 25.64           C  
ANISOU 5499  CA  ARG B 365     2899   3232   3613   -373   -101    182       C  
ATOM   5500  C   ARG B 365      81.976   9.773-170.421  1.00 28.74           C  
ANISOU 5500  C   ARG B 365     3263   3617   4039   -381   -120    160       C  
ATOM   5501  O   ARG B 365      83.000  10.420-170.672  1.00 32.61           O  
ANISOU 5501  O   ARG B 365     3711   4113   4567   -388    -86    183       O  
ATOM   5502  CB  ARG B 365      79.759  10.656-169.592  1.00 30.16           C  
ANISOU 5502  CB  ARG B 365     3500   3766   4194   -405   -120    177       C  
ATOM   5503  CG  ARG B 365      78.361  11.203-169.955  1.00 30.81           C  
ANISOU 5503  CG  ARG B 365     3592   3871   4244   -381    -94    215       C  
ATOM   5504  CD  ARG B 365      78.421  12.508-170.791  1.00 28.86           C  
ANISOU 5504  CD  ARG B 365     3339   3623   4002   -349    -24    269       C  
ATOM   5505  NE  ARG B 365      79.348  13.479-170.213  1.00 28.71           N  
ANISOU 5505  NE  ARG B 365     3336   3536   4037   -384     10    269       N  
ATOM   5506  CZ  ARG B 365      79.080  14.205-169.128  1.00 32.96           C  
ANISOU 5506  CZ  ARG B 365     3919   4010   4595   -409     24    264       C  
ATOM   5507  NH1 ARG B 365      77.891  14.116-168.532  1.00 30.82           N  
ANISOU 5507  NH1 ARG B 365     3672   3739   4297   -387     19    269       N  
ATOM   5508  NH2 ARG B 365      79.996  15.030-168.655  1.00 32.90           N  
ANISOU 5508  NH2 ARG B 365     3935   3939   4628   -461     46    254       N  
ATOM   5509  N   ASN B 366      82.020   8.597-169.786  1.00 28.28           N  
ANISOU 5509  N   ASN B 366     3223   3550   3971   -379   -172    124       N  
ATOM   5510  CA  ASN B 366      83.291   8.161-169.220  1.00 31.94           C  
ANISOU 5510  CA  ASN B 366     3652   4015   4468   -377   -193    115       C  
ATOM   5511  C   ASN B 366      84.325   7.891-170.304  1.00 32.50           C  
ANISOU 5511  C   ASN B 366     3680   4128   4541   -322   -152    133       C  
ATOM   5512  O   ASN B 366      85.510   8.200-170.127  1.00 31.37           O  
ANISOU 5512  O   ASN B 366     3468   4010   4442   -327   -142    156       O  
ATOM   5513  CB  ASN B 366      83.089   6.926-168.346  1.00 32.63           C  
ANISOU 5513  CB  ASN B 366     3780   4080   4538   -370   -248     83       C  
ATOM   5514  CG  ASN B 366      82.171   7.191-167.144  1.00 30.77           C  
ANISOU 5514  CG  ASN B 366     3583   3808   4300   -421   -281     71       C  
ATOM   5515  OD1 ASN B 366      81.879   8.335-166.803  1.00 34.01           O  
ANISOU 5515  OD1 ASN B 366     3991   4207   4726   -458   -263     83       O  
ATOM   5516  ND2 ASN B 366      81.679   6.115-166.537  1.00 31.97           N  
ANISOU 5516  ND2 ASN B 366     3783   3938   4427   -418   -318     51       N  
ATOM   5517  N   LEU B 367      83.903   7.337-171.444  1.00 30.00           N  
ANISOU 5517  N   LEU B 367     3399   3826   4172   -273   -127    127       N  
ATOM   5518  CA  LEU B 367      84.867   6.977-172.472  1.00 35.89           C  
ANISOU 5518  CA  LEU B 367     4121   4610   4908   -207    -78    142       C  
ATOM   5519  C   LEU B 367      85.075   8.062-173.519  1.00 32.48           C  
ANISOU 5519  C   LEU B 367     3651   4212   4477   -201    -11    187       C  
ATOM   5520  O   LEU B 367      86.176   8.156-174.067  1.00 32.41           O  
ANISOU 5520  O   LEU B 367     3587   4240   4487   -163     40    218       O  
ATOM   5521  CB  LEU B 367      84.442   5.679-173.166  1.00 33.68           C  
ANISOU 5521  CB  LEU B 367     3923   4318   4555   -153    -83    103       C  
ATOM   5522  CG  LEU B 367      84.490   4.438-172.280  1.00 33.53           C  
ANISOU 5522  CG  LEU B 367     3951   4254   4533   -141   -130     67       C  
ATOM   5523  CD1 LEU B 367      83.984   3.213-173.068  1.00 30.54           C  
ANISOU 5523  CD1 LEU B 367     3682   3844   4077   -103   -128     22       C  
ATOM   5524  CD2 LEU B 367      85.902   4.239-171.789  1.00 27.95           C  
ANISOU 5524  CD2 LEU B 367     3177   3568   3877    -92   -117     94       C  
ATOM   5525  N   CYS B 368      84.067   8.901-173.803  1.00 30.70           N  
ANISOU 5525  N   CYS B 368     3451   3980   4233   -231     -3    201       N  
ATOM   5526  CA  CYS B 368      84.181   9.886-174.883  1.00 32.48           C  
ANISOU 5526  CA  CYS B 368     3658   4234   4450   -214     66    251       C  
ATOM   5527  C   CYS B 368      84.327  11.342-174.436  1.00 31.80           C  
ANISOU 5527  C   CYS B 368     3539   4119   4424   -271     97    293       C  
ATOM   5528  O   CYS B 368      84.653  12.182-175.278  1.00 34.77           O  
ANISOU 5528  O   CYS B 368     3898   4510   4804   -260    165    344       O  
ATOM   5529  CB  CYS B 368      82.974   9.791-175.827  1.00 34.14           C  
ANISOU 5529  CB  CYS B 368     3926   4469   4578   -185     66    251       C  
ATOM   5530  SG  CYS B 368      82.863   8.210-176.736  1.00 37.75           S  
ANISOU 5530  SG  CYS B 368     4449   4953   4940   -128     46    199       S  
ATOM   5531  N   ASP B 369      84.089  11.683-173.165  1.00 30.31           N  
ANISOU 5531  N   ASP B 369     3357   3882   4276   -333     54    274       N  
ATOM   5532  CA  ASP B 369      84.319  13.062-172.749  1.00 31.25           C  
ANISOU 5532  CA  ASP B 369     3469   3957   4447   -394     89    305       C  
ATOM   5533  C   ASP B 369      85.767  13.436-173.068  1.00 29.94           C  
ANISOU 5533  C   ASP B 369     3229   3816   4331   -420    129    338       C  
ATOM   5534  O   ASP B 369      86.679  12.634-172.822  1.00 30.54           O  
ANISOU 5534  O   ASP B 369     3246   3932   4424   -414    101    324       O  
ATOM   5535  CB  ASP B 369      84.067  13.243-171.233  1.00 30.35           C  
ANISOU 5535  CB  ASP B 369     3383   3788   4362   -459     34    268       C  
ATOM   5536  CG  ASP B 369      82.632  13.638-170.888  1.00 35.02           C  
ANISOU 5536  CG  ASP B 369     4043   4339   4922   -448     34    265       C  
ATOM   5537  OD1 ASP B 369      81.759  13.677-171.782  1.00 32.91           O  
ANISOU 5537  OD1 ASP B 369     3793   4100   4612   -392     62    293       O  
ATOM   5538  OD2 ASP B 369      82.369  13.930-169.683  1.00 34.64           O  
ANISOU 5538  OD2 ASP B 369     4032   4240   4888   -493      7    239       O  
ATOM   5539  N   PRO B 370      86.021  14.632-173.612  1.00 32.16           N  
ANISOU 5539  N   PRO B 370     3507   4076   4637   -448    200    391       N  
ATOM   5540  CA  PRO B 370      87.415  15.012-173.903  1.00 38.03           C  
ANISOU 5540  CA  PRO B 370     4166   4850   5434   -490    243    431       C  
ATOM   5541  C   PRO B 370      88.283  15.041-172.661  1.00 36.50           C  
ANISOU 5541  C   PRO B 370     3917   4650   5299   -586    182    406       C  
ATOM   5542  O   PRO B 370      89.500  14.816-172.756  1.00 36.54           O  
ANISOU 5542  O   PRO B 370     3820   4720   5342   -604    187    432       O  
ATOM   5543  CB  PRO B 370      87.289  16.413-174.524  1.00 38.31           C  
ANISOU 5543  CB  PRO B 370     4236   4835   5484   -521    328    490       C  
ATOM   5544  CG  PRO B 370      85.858  16.552-174.911  1.00 44.62           C  
ANISOU 5544  CG  PRO B 370     5126   5607   6222   -451    339    492       C  
ATOM   5545  CD  PRO B 370      85.071  15.702-173.952  1.00 39.45           C  
ANISOU 5545  CD  PRO B 370     4501   4947   5543   -442    250    424       C  
ATOM   5546  N   HIS B 371      87.695  15.328-171.502  1.00 33.55           N  
ANISOU 5546  N   HIS B 371     3607   4211   4928   -643    126    361       N  
ATOM   5547  CA  HIS B 371      88.440  15.364-170.252  1.00 35.88           C  
ANISOU 5547  CA  HIS B 371     3865   4506   5263   -739     56    331       C  
ATOM   5548  C   HIS B 371      88.353  14.047-169.489  1.00 38.11           C  
ANISOU 5548  C   HIS B 371     4133   4827   5519   -693    -29    286       C  
ATOM   5549  O   HIS B 371      88.717  13.999-168.308  1.00 35.23           O  
ANISOU 5549  O   HIS B 371     3758   4459   5167   -760   -100    256       O  
ATOM   5550  CB  HIS B 371      87.953  16.533-169.385  1.00 34.92           C  
ANISOU 5550  CB  HIS B 371     3839   4278   5151   -835     52    306       C  
ATOM   5551  CG  HIS B 371      86.468  16.558-169.185  1.00 38.00           C  
ANISOU 5551  CG  HIS B 371     4341   4605   5491   -773     60    281       C  
ATOM   5552  ND1 HIS B 371      85.579  16.695-170.232  1.00 39.80           N  
ANISOU 5552  ND1 HIS B 371     4606   4829   5687   -684    125    316       N  
ATOM   5553  CD2 HIS B 371      85.716  16.465-168.063  1.00 38.43           C  
ANISOU 5553  CD2 HIS B 371     4472   4611   5520   -784     12    232       C  
ATOM   5554  CE1 HIS B 371      84.344  16.687-169.761  1.00 37.24           C  
ANISOU 5554  CE1 HIS B 371     4361   4463   5325   -646    114    295       C  
ATOM   5555  NE2 HIS B 371      84.400  16.546-168.446  1.00 40.31           N  
ANISOU 5555  NE2 HIS B 371     4777   4820   5717   -703     53    243       N  
ATOM   5556  N   ARG B 372      87.893  12.975-170.130  1.00 34.76           N  
ANISOU 5556  N   ARG B 372     3719   4437   5053   -584    -22    281       N  
ATOM   5557  CA  ARG B 372      87.963  11.668-169.493  1.00 29.76           C  
ANISOU 5557  CA  ARG B 372     3076   3834   4399   -537    -90    247       C  
ATOM   5558  C   ARG B 372      88.875  10.756-170.324  1.00 31.24           C  
ANISOU 5558  C   ARG B 372     3186   4098   4585   -452    -62    277       C  
ATOM   5559  O   ARG B 372      90.011  11.138-170.640  1.00 36.77           O  
ANISOU 5559  O   ARG B 372     3787   4855   5329   -473    -31    323       O  
ATOM   5560  CB  ARG B 372      86.580  11.069-169.334  1.00 31.35           C  
ANISOU 5560  CB  ARG B 372     3374   3991   4545   -492   -112    208       C  
ATOM   5561  CG  ARG B 372      85.625  11.882-168.484  1.00 26.06           C  
ANISOU 5561  CG  ARG B 372     2780   3252   3870   -552   -127    186       C  
ATOM   5562  CD  ARG B 372      86.060  11.930-166.999  1.00 29.30           C  
ANISOU 5562  CD  ARG B 372     3191   3645   4296   -623   -197    157       C  
ATOM   5563  NE  ARG B 372      86.037  10.606-166.380  1.00 26.79           N  
ANISOU 5563  NE  ARG B 372     2874   3352   3953   -579   -258    133       N  
ATOM   5564  CZ  ARG B 372      84.932   9.968-166.025  1.00 30.36           C  
ANISOU 5564  CZ  ARG B 372     3397   3772   4365   -547   -275    108       C  
ATOM   5565  NH1 ARG B 372      83.738  10.516-166.243  1.00 28.04           N  
ANISOU 5565  NH1 ARG B 372     3164   3439   4051   -547   -240    107       N  
ATOM   5566  NH2 ARG B 372      85.014   8.763-165.465  1.00 36.42           N  
ANISOU 5566  NH2 ARG B 372     4172   4553   5113   -512   -324     92       N  
ATOM   5567  N   TYR B 373      88.411   9.553-170.689  1.00 29.26           N  
ANISOU 5567  N   TYR B 373     2983   3850   4285   -358    -67    253       N  
ATOM   5568  CA  TYR B 373      89.290   8.665-171.447  1.00 31.36           C  
ANISOU 5568  CA  TYR B 373     3197   4177   4542   -262    -28    278       C  
ATOM   5569  C   TYR B 373      89.469   9.135-172.891  1.00 32.19           C  
ANISOU 5569  C   TYR B 373     3288   4309   4633   -224     65    317       C  
ATOM   5570  O   TYR B 373      90.487   8.813-173.503  1.00 33.16           O  
ANISOU 5570  O   TYR B 373     3338   4495   4765   -161    117    357       O  
ATOM   5571  CB  TYR B 373      88.773   7.227-171.378  1.00 27.65           C  
ANISOU 5571  CB  TYR B 373     2809   3680   4018   -180    -56    235       C  
ATOM   5572  CG  TYR B 373      89.170   6.531-170.075  1.00 30.31           C  
ANISOU 5572  CG  TYR B 373     3126   4017   4372   -181   -129    225       C  
ATOM   5573  CD1 TYR B 373      88.440   6.723-168.920  1.00 27.84           C  
ANISOU 5573  CD1 TYR B 373     2861   3657   4060   -254   -197    192       C  
ATOM   5574  CD2 TYR B 373      90.309   5.725-170.008  1.00 31.13           C  
ANISOU 5574  CD2 TYR B 373     3161   4176   4489    -99   -122    257       C  
ATOM   5575  CE1 TYR B 373      88.808   6.098-167.728  1.00 32.41           C  
ANISOU 5575  CE1 TYR B 373     3429   4242   4645   -251   -263    188       C  
ATOM   5576  CE2 TYR B 373      90.683   5.099-168.827  1.00 31.44           C  
ANISOU 5576  CE2 TYR B 373     3182   4225   4539    -89   -189    259       C  
ATOM   5577  CZ  TYR B 373      89.934   5.296-167.690  1.00 31.46           C  
ANISOU 5577  CZ  TYR B 373     3239   4179   4536   -170   -263    223       C  
ATOM   5578  OH  TYR B 373      90.322   4.688-166.506  1.00 34.28           O  
ANISOU 5578  OH  TYR B 373     3581   4552   4893   -157   -331    230       O  
ATOM   5579  N   ASN B 374      88.523   9.901-173.430  1.00 30.98           N  
ANISOU 5579  N   ASN B 374     3197   4117   4455   -252     91    314       N  
ATOM   5580  CA  ASN B 374      88.736  10.648-174.677  1.00 34.61           C  
ANISOU 5580  CA  ASN B 374     3639   4603   4906   -233    180    365       C  
ATOM   5581  C   ASN B 374      89.129   9.729-175.844  1.00 32.74           C  
ANISOU 5581  C   ASN B 374     3409   4416   4613   -117    238    374       C  
ATOM   5582  O   ASN B 374      90.107   9.975-176.550  1.00 31.78           O  
ANISOU 5582  O   ASN B 374     3215   4350   4509    -85    313    429       O  
ATOM   5583  CB  ASN B 374      89.797  11.745-174.464  1.00 32.77           C  
ANISOU 5583  CB  ASN B 374     3305   4393   4752   -314    213    421       C  
ATOM   5584  CG  ASN B 374      89.911  12.691-175.653  1.00 39.72           C  
ANISOU 5584  CG  ASN B 374     4180   5284   5628   -310    311    481       C  
ATOM   5585  OD1 ASN B 374      88.924  12.959-176.327  1.00 36.72           O  
ANISOU 5585  OD1 ASN B 374     3885   4873   5193   -279    336    480       O  
ATOM   5586  ND2 ASN B 374      91.114  13.197-175.910  1.00 36.46           N  
ANISOU 5586  ND2 ASN B 374     3661   4922   5271   -344    366    543       N  
ATOM   5587  N   ILE B 375      88.364   8.648-176.044  1.00 30.42           N  
ANISOU 5587  N   ILE B 375     3210   4099   4248    -58    207    319       N  
ATOM   5588  CA  ILE B 375      88.749   7.655-177.053  1.00 34.88           C  
ANISOU 5588  CA  ILE B 375     3810   4693   4748     53    260    313       C  
ATOM   5589  C   ILE B 375      88.119   7.915-178.410  1.00 33.50           C  
ANISOU 5589  C   ILE B 375     3707   4532   4491     88    312    319       C  
ATOM   5590  O   ILE B 375      88.366   7.143-179.349  1.00 33.72           O  
ANISOU 5590  O   ILE B 375     3787   4579   4445    180    361    307       O  
ATOM   5591  CB  ILE B 375      88.393   6.203-176.653  1.00 29.38           C  
ANISOU 5591  CB  ILE B 375     3200   3955   4007    101    207    247       C  
ATOM   5592  CG1 ILE B 375      86.875   5.991-176.668  1.00 28.97           C  
ANISOU 5592  CG1 ILE B 375     3259   3853   3894     55    147    191       C  
ATOM   5593  CG2 ILE B 375      88.912   5.890-175.222  1.00 30.34           C  
ANISOU 5593  CG2 ILE B 375     3262   4066   4200     73    146    245       C  
ATOM   5594  CD1 ILE B 375      86.434   4.524-176.459  1.00 27.07           C  
ANISOU 5594  CD1 ILE B 375     3126   3560   3598     87    104    125       C  
ATOM   5595  N   LEU B 376      87.323   8.977-178.548  1.00 31.58           N  
ANISOU 5595  N   LEU B 376     3472   4278   4247     27    306    340       N  
ATOM   5596  CA  LEU B 376      86.410   9.083-179.682  1.00 36.84           C  
ANISOU 5596  CA  LEU B 376     4220   4961   4818     58    324    338       C  
ATOM   5597  C   LEU B 376      87.160   9.130-181.005  1.00 38.95           C  
ANISOU 5597  C   LEU B 376     4485   5282   5034    140    424    381       C  
ATOM   5598  O   LEU B 376      86.801   8.430-181.955  1.00 32.17           O  
ANISOU 5598  O   LEU B 376     3715   4442   4068    203    435    351       O  
ATOM   5599  CB  LEU B 376      85.516  10.309-179.517  1.00 36.88           C  
ANISOU 5599  CB  LEU B 376     4221   4950   4842     -6    311    372       C  
ATOM   5600  CG  LEU B 376      84.290  10.390-180.411  1.00 47.69           C  
ANISOU 5600  CG  LEU B 376     5663   6345   6111     17    297    373       C  
ATOM   5601  CD1 LEU B 376      83.398   9.174-180.252  1.00 40.71           C  
ANISOU 5601  CD1 LEU B 376     4851   5456   5161     12    212    296       C  
ATOM   5602  CD2 LEU B 376      83.540  11.652-180.052  1.00 52.84           C  
ANISOU 5602  CD2 LEU B 376     6299   6977   6800    -29    295    420       C  
ATOM   5603  N   GLU B 377      88.209   9.945-181.093  1.00 35.94           N  
ANISOU 5603  N   GLU B 377     4007   4928   4721    134    499    453       N  
ATOM   5604  CA  GLU B 377      88.892  10.063-182.373  1.00 41.74           C  
ANISOU 5604  CA  GLU B 377     4736   5719   5404    214    607    506       C  
ATOM   5605  C   GLU B 377      89.647   8.785-182.709  1.00 42.86           C  
ANISOU 5605  C   GLU B 377     4897   5885   5502    318    642    476       C  
ATOM   5606  O   GLU B 377      89.675   8.360-183.869  1.00 40.35           O  
ANISOU 5606  O   GLU B 377     4653   5596   5081    407    705    473       O  
ATOM   5607  CB  GLU B 377      89.839  11.258-182.361  1.00 40.50           C  
ANISOU 5607  CB  GLU B 377     4464   5585   5338    169    684    598       C  
ATOM   5608  CG  GLU B 377      90.400  11.594-183.739  1.00 51.99           C  
ANISOU 5608  CG  GLU B 377     5916   7100   6738    244    808    669       C  
ATOM   5609  CD  GLU B 377      91.446  12.687-183.677  1.00 73.91           C  
ANISOU 5609  CD  GLU B 377     8568   9900   9615    184    889    765       C  
ATOM   5610  OE1 GLU B 377      92.193  12.727-182.677  1.00 83.21           O  
ANISOU 5610  OE1 GLU B 377     9640  11079  10896    118    859    770       O  
ATOM   5611  OE2 GLU B 377      91.517  13.503-184.619  1.00 82.28           O  
ANISOU 5611  OE2 GLU B 377     9637  10979  10647    197    979    838       O  
ATOM   5612  N   ASP B 378      90.254   8.147-181.708  1.00 41.07           N  
ANISOU 5612  N   ASP B 378     4615   5645   5344    316    606    454       N  
ATOM   5613  CA  ASP B 378      90.960   6.900-181.973  1.00 39.41           C  
ANISOU 5613  CA  ASP B 378     4433   5448   5092    433    647    432       C  
ATOM   5614  C   ASP B 378      89.999   5.834-182.488  1.00 41.02           C  
ANISOU 5614  C   ASP B 378     4812   5601   5172    479    611    342       C  
ATOM   5615  O   ASP B 378      90.325   5.092-183.423  1.00 42.91           O  
ANISOU 5615  O   ASP B 378     5134   5850   5321    589    682    327       O  
ATOM   5616  CB  ASP B 378      91.681   6.425-180.714  1.00 44.09           C  
ANISOU 5616  CB  ASP B 378     4936   6038   5779    425    602    433       C  
ATOM   5617  CG  ASP B 378      92.758   5.390-181.007  1.00 75.60           C  
ANISOU 5617  CG  ASP B 378     8911  10064   9751    568    679    450       C  
ATOM   5618  OD1 ASP B 378      92.990   5.067-182.194  1.00 87.27           O  
ANISOU 5618  OD1 ASP B 378    10452  11563  11144    673    775    458       O  
ATOM   5619  OD2 ASP B 378      93.381   4.902-180.041  1.00 91.99           O  
ANISOU 5619  OD2 ASP B 378    10913  12148  11892    584    645    460       O  
ATOM   5620  N   VAL B 379      88.787   5.777-181.927  1.00 34.91           N  
ANISOU 5620  N   VAL B 379     4102   4774   4387    392    505    284       N  
ATOM   5621  CA  VAL B 379      87.789   4.839-182.446  1.00 35.09           C  
ANISOU 5621  CA  VAL B 379     4286   4756   4292    405    460    202       C  
ATOM   5622  C   VAL B 379      87.369   5.220-183.866  1.00 37.18           C  
ANISOU 5622  C   VAL B 379     4618   5066   4441    434    506    213       C  
ATOM   5623  O   VAL B 379      87.216   4.353-184.734  1.00 33.70           O  
ANISOU 5623  O   VAL B 379     4309   4616   3880    496    526    160       O  
ATOM   5624  CB  VAL B 379      86.582   4.763-181.497  1.00 36.91           C  
ANISOU 5624  CB  VAL B 379     4543   4938   4544    295    339    153       C  
ATOM   5625  CG1 VAL B 379      85.468   3.946-182.118  1.00 37.51           C  
ANISOU 5625  CG1 VAL B 379     4768   4988   4496    279    286     77       C  
ATOM   5626  CG2 VAL B 379      86.997   4.142-180.143  1.00 31.67           C  
ANISOU 5626  CG2 VAL B 379     3843   4223   3966    282    295    133       C  
ATOM   5627  N   ALA B 380      87.155   6.515-184.124  1.00 32.90           N  
ANISOU 5627  N   ALA B 380     4004   4570   3927    391    523    281       N  
ATOM   5628  CA  ALA B 380      86.709   6.931-185.459  1.00 31.87           C  
ANISOU 5628  CA  ALA B 380     3937   4491   3681    424    563    304       C  
ATOM   5629  C   ALA B 380      87.761   6.632-186.519  1.00 37.00           C  
ANISOU 5629  C   ALA B 380     4614   5179   4266    543    687    330       C  
ATOM   5630  O   ALA B 380      87.427   6.244-187.645  1.00 39.35           O  
ANISOU 5630  O   ALA B 380     5030   5500   4420    597    710    302       O  
ATOM   5631  CB  ALA B 380      86.361   8.422-185.455  1.00 31.11           C  
ANISOU 5631  CB  ALA B 380     3758   4425   3636    368    571    386       C  
ATOM   5632  N   VAL B 381      89.038   6.823-186.184  1.00 39.36           N  
ANISOU 5632  N   VAL B 381     4800   5494   4662    584    769    389       N  
ATOM   5633  CA  VAL B 381      90.113   6.498-187.117  1.00 41.70           C  
ANISOU 5633  CA  VAL B 381     5104   5834   4905    710    901    425       C  
ATOM   5634  C   VAL B 381      90.106   5.006-187.437  1.00 43.02           C  
ANISOU 5634  C   VAL B 381     5422   5957   4966    802    904    333       C  
ATOM   5635  O   VAL B 381      90.155   4.597-188.606  1.00 38.73           O  
ANISOU 5635  O   VAL B 381     4999   5432   4286    892    974    315       O  
ATOM   5636  CB  VAL B 381      91.464   6.956-186.537  1.00 44.27           C  
ANISOU 5636  CB  VAL B 381     5251   6198   5370    723    975    512       C  
ATOM   5637  CG1 VAL B 381      92.621   6.238-187.233  1.00 44.67           C  
ANISOU 5637  CG1 VAL B 381     5305   6292   5377    875   1106    540       C  
ATOM   5638  CG2 VAL B 381      91.602   8.468-186.690  1.00 43.82           C  
ANISOU 5638  CG2 VAL B 381     5085   6182   5381    648   1015    610       C  
ATOM   5639  N   CYS B 382      90.011   4.170-186.400  1.00 38.36           N  
ANISOU 5639  N   CYS B 382     4846   5300   4428    779    829    273       N  
ATOM   5640  CA  CYS B 382      89.957   2.728-186.613  1.00 42.01           C  
ANISOU 5640  CA  CYS B 382     5473   5695   4794    858    832    183       C  
ATOM   5641  C   CYS B 382      88.751   2.323-187.456  1.00 39.86           C  
ANISOU 5641  C   CYS B 382     5386   5394   4363    819    773     96       C  
ATOM   5642  O   CYS B 382      88.828   1.362-188.228  1.00 46.45           O  
ANISOU 5642  O   CYS B 382     6388   6191   5069    903    818     33       O  
ATOM   5643  CB  CYS B 382      89.934   2.001-185.271  1.00 41.63           C  
ANISOU 5643  CB  CYS B 382     5409   5573   4834    823    753    142       C  
ATOM   5644  SG  CYS B 382      91.495   2.103-184.357  1.00 47.32           S  
ANISOU 5644  SG  CYS B 382     5934   6337   5707    898    821    235       S  
ATOM   5645  N   MET B 383      87.623   3.025-187.308  1.00 39.10           N  
ANISOU 5645  N   MET B 383     5268   5317   4270    694    670     93       N  
ATOM   5646  CA  MET B 383      86.438   2.764-188.126  1.00 40.10           C  
ANISOU 5646  CA  MET B 383     5541   5449   4247    643    600     26       C  
ATOM   5647  C   MET B 383      86.589   3.240-189.559  1.00 43.72           C  
ANISOU 5647  C   MET B 383     6049   5984   4578    715    682     63       C  
ATOM   5648  O   MET B 383      85.639   3.084-190.335  1.00 44.07           O  
ANISOU 5648  O   MET B 383     6210   6053   4483    675    620     15       O  
ATOM   5649  CB  MET B 383      85.204   3.438-187.518  1.00 37.01           C  
ANISOU 5649  CB  MET B 383     5085   5077   3902    503    473     33       C  
ATOM   5650  CG  MET B 383      84.792   2.854-186.167  1.00 40.21           C  
ANISOU 5650  CG  MET B 383     5473   5405   4401    421    379    -17       C  
ATOM   5651  SD  MET B 383      83.340   3.669-185.475  1.00 42.07           S  
ANISOU 5651  SD  MET B 383     5627   5673   4685    275    250      2       S  
ATOM   5652  CE  MET B 383      82.144   3.508-186.811  1.00 41.85           C  
ANISOU 5652  CE  MET B 383     5721   5712   4469    239    189    -37       C  
ATOM   5653  N   ASP B 384      87.725   3.850-189.898  1.00 40.11           N  
ANISOU 5653  N   ASP B 384     5498   5575   4167    809    813    154       N  
ATOM   5654  CA  ASP B 384      87.983   4.388-191.233  1.00 44.32           C  
ANISOU 5654  CA  ASP B 384     6067   6185   4587    886    911    208       C  
ATOM   5655  C   ASP B 384      87.003   5.512-191.588  1.00 44.67           C  
ANISOU 5655  C   ASP B 384     6073   6296   4605    804    848    258       C  
ATOM   5656  O   ASP B 384      86.608   5.684-192.742  1.00 47.09           O  
ANISOU 5656  O   ASP B 384     6471   6660   4760    836    864    264       O  
ATOM   5657  CB  ASP B 384      87.963   3.268-192.273  1.00 62.47           C  
ANISOU 5657  CB  ASP B 384     8580   8461   6696    973    948    119       C  
ATOM   5658  CG  ASP B 384      88.356   3.746-193.644  1.00 88.88           C  
ANISOU 5658  CG  ASP B 384    11971  11887   9913   1071   1065    176       C  
ATOM   5659  OD1 ASP B 384      87.508   3.644-194.552  1.00104.27           O  
ANISOU 5659  OD1 ASP B 384    14057  13866  11693   1050   1014    130       O  
ATOM   5660  OD2 ASP B 384      89.481   4.265-193.796  1.00 91.74           O  
ANISOU 5660  OD2 ASP B 384    12222  12290  10343   1160   1203    274       O  
ATOM   5661  N   LEU B 385      86.612   6.298-190.590  1.00 40.76           N  
ANISOU 5661  N   LEU B 385     5446   5793   4250    706    779    300       N  
ATOM   5662  CA  LEU B 385      85.783   7.465-190.854  1.00 46.31           C  
ANISOU 5662  CA  LEU B 385     6101   6552   4944    650    741    367       C  
ATOM   5663  C   LEU B 385      86.650   8.661-191.245  1.00 45.75           C  
ANISOU 5663  C   LEU B 385     5926   6524   4932    698    870    494       C  
ATOM   5664  O   LEU B 385      87.831   8.749-190.901  1.00 46.09           O  
ANISOU 5664  O   LEU B 385     5881   6553   5077    732    962    535       O  
ATOM   5665  CB  LEU B 385      84.938   7.819-189.629  1.00 42.05           C  
ANISOU 5665  CB  LEU B 385     5481   5977   4519    534    624    359       C  
ATOM   5666  CG  LEU B 385      84.063   6.680-189.110  1.00 41.86           C  
ANISOU 5666  CG  LEU B 385     5540   5908   4455    468    498    245       C  
ATOM   5667  CD1 LEU B 385      83.359   7.081-187.822  1.00 33.30           C  
ANISOU 5667  CD1 LEU B 385     4363   4792   3496    366    405    251       C  
ATOM   5668  CD2 LEU B 385      83.060   6.256-190.183  1.00 44.22           C  
ANISOU 5668  CD2 LEU B 385     5970   6263   4569    459    433    197       C  
ATOM   5669  N   ASP B 386      86.044   9.598-191.965  1.00 40.90           N  
ANISOU 5669  N   ASP B 386     5319   5968   4254    696    875    563       N  
ATOM   5670  CA  ASP B 386      86.756  10.802-192.396  1.00 42.47           C  
ANISOU 5670  CA  ASP B 386     5437   6198   4502    731   1000    691       C  
ATOM   5671  C   ASP B 386      86.715  11.817-191.265  1.00 42.14           C  
ANISOU 5671  C   ASP B 386     5267   6107   4637    638    977    747       C  
ATOM   5672  O   ASP B 386      85.714  12.511-191.077  1.00 42.88           O  
ANISOU 5672  O   ASP B 386     5357   6200   4734    590    911    773       O  
ATOM   5673  CB  ASP B 386      86.130  11.367-193.667  1.00 55.77           C  
ANISOU 5673  CB  ASP B 386     7198   7959   6031    781   1022    749       C  
ATOM   5674  CG  ASP B 386      86.736  12.701-194.080  1.00 72.86           C  
ANISOU 5674  CG  ASP B 386     9289  10144   8249    808   1151    893       C  
ATOM   5675  OD1 ASP B 386      87.828  13.060-193.586  1.00 74.68           O  
ANISOU 5675  OD1 ASP B 386     9416  10340   8619    794   1242    942       O  
ATOM   5676  OD2 ASP B 386      86.108  13.397-194.907  1.00 80.08           O  
ANISOU 5676  OD2 ASP B 386    10250  11113   9065    838   1160    962       O  
ATOM   5677  N   THR B 387      87.813  11.921-190.518  1.00 44.67           N  
ANISOU 5677  N   THR B 387     5482   6390   5100    617   1035    769       N  
ATOM   5678  CA  THR B 387      87.880  12.798-189.355  1.00 47.98           C  
ANISOU 5678  CA  THR B 387     5793   6753   5683    516   1008    805       C  
ATOM   5679  C   THR B 387      88.365  14.206-189.688  1.00 58.85           C  
ANISOU 5679  C   THR B 387     7108   8132   7119    498   1116    931       C  
ATOM   5680  O   THR B 387      88.551  15.013-188.771  1.00 61.08           O  
ANISOU 5680  O   THR B 387     7313   8357   7536    407   1109    963       O  
ATOM   5681  CB  THR B 387      88.786  12.192-188.275  1.00 51.93           C  
ANISOU 5681  CB  THR B 387     6208   7219   6305    482    995    763       C  
ATOM   5682  OG1 THR B 387      90.124  12.077-188.775  1.00 58.78           O  
ANISOU 5682  OG1 THR B 387     7015   8130   7188    547   1120    816       O  
ATOM   5683  CG2 THR B 387      88.279  10.816-187.856  1.00 48.82           C  
ANISOU 5683  CG2 THR B 387     5887   6802   5860    495    892    643       C  
ATOM   5684  N   ARG B 388      88.564  14.528-190.967  1.00 62.31           N  
ANISOU 5684  N   ARG B 388     7591   8628   7456    579   1217   1002       N  
ATOM   5685  CA  ARG B 388      89.046  15.857-191.328  1.00 69.72           C  
ANISOU 5685  CA  ARG B 388     8481   9560   8449    560   1331   1131       C  
ATOM   5686  C   ARG B 388      87.932  16.892-191.394  1.00 69.89           C  
ANISOU 5686  C   ARG B 388     8552   9551   8452    536   1298   1183       C  
ATOM   5687  O   ARG B 388      88.224  18.093-191.387  1.00 74.98           O  
ANISOU 5687  O   ARG B 388     9165  10153   9171    497   1379   1283       O  
ATOM   5688  CB  ARG B 388      89.770  15.817-192.675  1.00 67.83           C  
ANISOU 5688  CB  ARG B 388     8268   9396   8107    664   1470   1201       C  
ATOM   5689  CG  ARG B 388      90.931  14.840-192.745  1.00 74.41           C  
ANISOU 5689  CG  ARG B 388     9054  10270   8950    719   1533   1170       C  
ATOM   5690  CD  ARG B 388      91.623  14.914-194.100  1.00 84.37           C  
ANISOU 5690  CD  ARG B 388    10345  11608  10105    830   1688   1253       C  
ATOM   5691  NE  ARG B 388      90.795  14.388-195.184  1.00 93.41           N  
ANISOU 5691  NE  ARG B 388    11649  12798  11044    928   1666   1211       N  
ATOM   5692  CZ  ARG B 388      91.101  14.489-196.474  1.00106.27           C  
ANISOU 5692  CZ  ARG B 388    13344  14495  12538   1033   1786   1277       C  
ATOM   5693  NH1 ARG B 388      92.215  15.107-196.848  1.00112.89           N  
ANISOU 5693  NH1 ARG B 388    14096  15364  13435   1055   1947   1395       N  
ATOM   5694  NH2 ARG B 388      90.292  13.977-197.393  1.00109.52           N  
ANISOU 5694  NH2 ARG B 388    13909  14952  12752   1109   1743   1226       N  
ATOM   5695  N   THR B 389      86.672  16.463-191.465  1.00 61.03           N  
ANISOU 5695  N   THR B 389     7506   8450   7233    559   1185   1123       N  
ATOM   5696  CA  THR B 389      85.537  17.365-191.607  1.00 55.41           C  
ANISOU 5696  CA  THR B 389     6834   7732   6486    563   1153   1182       C  
ATOM   5697  C   THR B 389      84.436  16.963-190.638  1.00 47.07           C  
ANISOU 5697  C   THR B 389     5780   6652   5453    512   1006   1098       C  
ATOM   5698  O   THR B 389      84.200  15.771-190.415  1.00 43.97           O  
ANISOU 5698  O   THR B 389     5405   6284   5018    505    916    991       O  
ATOM   5699  CB  THR B 389      85.000  17.359-193.043  1.00 62.61           C  
ANISOU 5699  CB  THR B 389     7835   8742   7213    668   1176   1231       C  
ATOM   5700  OG1 THR B 389      83.812  18.157-193.115  1.00 68.85           O  
ANISOU 5700  OG1 THR B 389     8652   9541   7966    684   1131   1292       O  
ATOM   5701  CG2 THR B 389      84.683  15.939-193.483  1.00 65.79           C  
ANISOU 5701  CG2 THR B 389     8302   9216   7478    705   1091   1118       C  
ATOM   5702  N   THR B 390      83.763  17.962-190.058  1.00 42.61           N  
ANISOU 5702  N   THR B 390     5203   6031   4954    480    993   1150       N  
ATOM   5703  CA  THR B 390      82.753  17.667-189.044  1.00 44.52           C  
ANISOU 5703  CA  THR B 390     5435   6249   5230    433    870   1082       C  
ATOM   5704  C   THR B 390      81.466  17.147-189.667  1.00 40.98           C  
ANISOU 5704  C   THR B 390     5032   5903   4636    485    774   1064       C  
ATOM   5705  O   THR B 390      80.733  16.390-189.018  1.00 39.31           O  
ANISOU 5705  O   THR B 390     4811   5703   4422    444    659    981       O  
ATOM   5706  CB  THR B 390      82.443  18.908-188.197  1.00 44.16           C  
ANISOU 5706  CB  THR B 390     5373   6107   5297    393    898   1143       C  
ATOM   5707  OG1 THR B 390      82.225  20.041-189.055  1.00 50.65           O  
ANISOU 5707  OG1 THR B 390     6235   6934   6074    461    990   1270       O  
ATOM   5708  CG2 THR B 390      83.587  19.198-187.228  1.00 48.79           C  
ANISOU 5708  CG2 THR B 390     5910   6592   6038    297    944   1122       C  
ATOM   5709  N   SER B 391      81.186  17.529-190.918  1.00 40.86           N  
ANISOU 5709  N   SER B 391     5063   5969   4494    570    815   1145       N  
ATOM   5710  CA  SER B 391      79.911  17.194-191.540  1.00 40.44           C  
ANISOU 5710  CA  SER B 391     5042   6029   4294    613    716   1145       C  
ATOM   5711  C   SER B 391      79.817  15.729-191.952  1.00 43.72           C  
ANISOU 5711  C   SER B 391     5501   6515   4594    596    626   1027       C  
ATOM   5712  O   SER B 391      78.737  15.285-192.359  1.00 44.42           O  
ANISOU 5712  O   SER B 391     5611   6703   4562    600    519   1007       O  
ATOM   5713  CB  SER B 391      79.660  18.101-192.752  1.00 39.77           C  
ANISOU 5713  CB  SER B 391     4997   6016   4100    713    788   1277       C  
ATOM   5714  OG  SER B 391      80.745  18.049-193.659  1.00 44.43           O  
ANISOU 5714  OG  SER B 391     5629   6615   4639    755    895   1300       O  
ATOM   5715  N   SER B 392      80.904  14.964-191.864  1.00 37.12           N  
ANISOU 5715  N   SER B 392     4681   5634   3789    577    665    952       N  
ATOM   5716  CA  SER B 392      80.762  13.519-192.025  1.00 43.21           C  
ANISOU 5716  CA  SER B 392     5511   6438   4468    553    577    827       C  
ATOM   5717  C   SER B 392      80.106  12.871-190.811  1.00 43.37           C  
ANISOU 5717  C   SER B 392     5496   6415   4566    462    459    738       C  
ATOM   5718  O   SER B 392      79.740  11.687-190.882  1.00 40.71           O  
ANISOU 5718  O   SER B 392     5216   6101   4151    426    369    636       O  
ATOM   5719  CB  SER B 392      82.129  12.877-192.292  1.00 39.34           C  
ANISOU 5719  CB  SER B 392     5053   5910   3985    584    669    782       C  
ATOM   5720  OG  SER B 392      82.887  12.859-191.087  1.00 42.60           O  
ANISOU 5720  OG  SER B 392     5389   6225   4573    530    693    757       O  
ATOM   5721  N   LEU B 393      79.939  13.632-189.715  1.00 34.82           N  
ANISOU 5721  N   LEU B 393     4333   5267   3629    422    461    777       N  
ATOM   5722  CA  LEU B 393      79.362  13.137-188.452  1.00 33.65           C  
ANISOU 5722  CA  LEU B 393     4147   5073   3566    339    365    706       C  
ATOM   5723  C   LEU B 393      80.152  11.957-187.896  1.00 34.92           C  
ANISOU 5723  C   LEU B 393     4329   5171   3769    298    349    596       C  
ATOM   5724  O   LEU B 393      79.585  11.027-187.308  1.00 34.44           O  
ANISOU 5724  O   LEU B 393     4282   5099   3704    238    252    512       O  
ATOM   5725  CB  LEU B 393      77.882  12.772-188.609  1.00 35.88           C  
ANISOU 5725  CB  LEU B 393     4434   5448   3751    314    241    692       C  
ATOM   5726  CG  LEU B 393      77.012  13.953-189.054  1.00 40.10           C  
ANISOU 5726  CG  LEU B 393     4932   6055   4248    372    253    815       C  
ATOM   5727  CD1 LEU B 393      75.541  13.636-188.927  1.00 38.95           C  
ANISOU 5727  CD1 LEU B 393     4752   6009   4040    338    126    812       C  
ATOM   5728  CD2 LEU B 393      77.367  15.180-188.231  1.00 39.47           C  
ANISOU 5728  CD2 LEU B 393     4803   5877   4317    386    344    891       C  
ATOM   5729  N   TRP B 394      81.479  12.005-188.067  1.00 32.22           N  
ANISOU 5729  N   TRP B 394     3983   4787   3471    333    451    606       N  
ATOM   5730  CA  TRP B 394      82.311  10.923-187.560  1.00 33.71           C  
ANISOU 5730  CA  TRP B 394     4185   4921   3700    318    449    518       C  
ATOM   5731  C   TRP B 394      82.208  10.800-186.053  1.00 32.58           C  
ANISOU 5731  C   TRP B 394     3984   4705   3691    240    390    480       C  
ATOM   5732  O   TRP B 394      82.271   9.686-185.523  1.00 32.12           O  
ANISOU 5732  O   TRP B 394     3955   4612   3638    214    336    394       O  
ATOM   5733  CB  TRP B 394      83.773  11.110-187.976  1.00 39.50           C  
ANISOU 5733  CB  TRP B 394     4896   5643   4467    377    577    558       C  
ATOM   5734  CG  TRP B 394      84.466  12.360-187.497  1.00 37.47           C  
ANISOU 5734  CG  TRP B 394     4542   5350   4343    356    657    649       C  
ATOM   5735  CD1 TRP B 394      84.573  13.547-188.177  1.00 42.02           C  
ANISOU 5735  CD1 TRP B 394     5104   5948   4912    384    743    754       C  
ATOM   5736  CD2 TRP B 394      85.213  12.532-186.278  1.00 36.34           C  
ANISOU 5736  CD2 TRP B 394     4314   5140   4353    295    663    642       C  
ATOM   5737  NE1 TRP B 394      85.308  14.447-187.444  1.00 43.35           N  
ANISOU 5737  NE1 TRP B 394     5192   6057   5223    333    801    808       N  
ATOM   5738  CE2 TRP B 394      85.711  13.852-186.275  1.00 36.95           C  
ANISOU 5738  CE2 TRP B 394     4332   5197   4508    274    748    739       C  
ATOM   5739  CE3 TRP B 394      85.482  11.708-185.177  1.00 33.41           C  
ANISOU 5739  CE3 TRP B 394     3917   4725   4054    252    601    567       C  
ATOM   5740  CZ2 TRP B 394      86.482  14.358-185.229  1.00 38.76           C  
ANISOU 5740  CZ2 TRP B 394     4478   5369   4882    199    765    754       C  
ATOM   5741  CZ3 TRP B 394      86.246  12.212-184.134  1.00 38.78           C  
ANISOU 5741  CZ3 TRP B 394     4506   5358   4872    192    616    589       C  
ATOM   5742  CH2 TRP B 394      86.734  13.523-184.165  1.00 46.69           C  
ANISOU 5742  CH2 TRP B 394     5450   6345   5945    159    693    677       C  
ATOM   5743  N   LYS B 395      82.047  11.922-185.344  1.00 32.48           N  
ANISOU 5743  N   LYS B 395     3903   4660   3780    207    405    542       N  
ATOM   5744  CA  LYS B 395      81.948  11.854-183.889  1.00 34.90           C  
ANISOU 5744  CA  LYS B 395     4163   4896   4200    135    353    505       C  
ATOM   5745  C   LYS B 395      80.691  11.105-183.467  1.00 32.31           C  
ANISOU 5745  C   LYS B 395     3865   4584   3828     94    239    445       C  
ATOM   5746  O   LYS B 395      80.727  10.252-182.575  1.00 32.45           O  
ANISOU 5746  O   LYS B 395     3886   4557   3887     48    184    375       O  
ATOM   5747  CB  LYS B 395      81.965  13.264-183.287  1.00 35.17           C  
ANISOU 5747  CB  LYS B 395     4145   4885   4334    109    398    580       C  
ATOM   5748  CG  LYS B 395      83.313  13.966-183.352  1.00 37.62           C  
ANISOU 5748  CG  LYS B 395     4412   5161   4722    108    500    632       C  
ATOM   5749  CD  LYS B 395      83.275  15.297-182.570  1.00 42.98           C  
ANISOU 5749  CD  LYS B 395     5062   5767   5500     56    533    687       C  
ATOM   5750  CE  LYS B 395      84.539  16.127-182.786  1.00 44.51           C  
ANISOU 5750  CE  LYS B 395     5216   5932   5764     36    637    750       C  
ATOM   5751  NZ  LYS B 395      84.550  17.333-181.914  1.00 49.83           N  
ANISOU 5751  NZ  LYS B 395     5885   6514   6535    -37    662    785       N  
ATOM   5752  N   ASP B 396      79.565  11.423-184.105  1.00 32.86           N  
ANISOU 5752  N   ASP B 396     3949   4725   3812    107    204    481       N  
ATOM   5753  CA  ASP B 396      78.304  10.764-183.786  1.00 31.20           C  
ANISOU 5753  CA  ASP B 396     3748   4552   3556     57     95    438       C  
ATOM   5754  C   ASP B 396      78.367   9.270-184.088  1.00 31.59           C  
ANISOU 5754  C   ASP B 396     3872   4603   3527     30     37    337       C  
ATOM   5755  O   ASP B 396      77.945   8.444-183.269  1.00 31.34           O  
ANISOU 5755  O   ASP B 396     3849   4537   3520    -36    -35    274       O  
ATOM   5756  CB  ASP B 396      77.178  11.424-184.583  1.00 31.57           C  
ANISOU 5756  CB  ASP B 396     3781   4700   3514     88     72    511       C  
ATOM   5757  CG  ASP B 396      77.287  12.949-184.589  1.00 44.35           C  
ANISOU 5757  CG  ASP B 396     5357   6303   5190    144    160    622       C  
ATOM   5758  OD1 ASP B 396      78.225  13.495-185.217  1.00 38.62           O  
ANISOU 5758  OD1 ASP B 396     4648   5559   4467    192    253    664       O  
ATOM   5759  OD2 ASP B 396      76.421  13.589-183.957  1.00 47.42           O  
ANISOU 5759  OD2 ASP B 396     5702   6694   5620    140    143    669       O  
ATOM   5760  N   LYS B 397      78.876   8.906-185.279  1.00 35.52           N  
ANISOU 5760  N   LYS B 397     4438   5136   3923     81     73    324       N  
ATOM   5761  CA  LYS B 397      78.964   7.491-185.646  1.00 34.00           C  
ANISOU 5761  CA  LYS B 397     4347   4928   3642     63     30    223       C  
ATOM   5762  C   LYS B 397      79.852   6.718-184.680  1.00 36.26           C  
ANISOU 5762  C   LYS B 397     4644   5111   4022     53     48    163       C  
ATOM   5763  O   LYS B 397      79.507   5.610-184.261  1.00 33.81           O  
ANISOU 5763  O   LYS B 397     4395   4758   3693     -1    -18     83       O  
ATOM   5764  CB  LYS B 397      79.485   7.335-187.075  1.00 32.65           C  
ANISOU 5764  CB  LYS B 397     4260   4804   3342    138     87    222       C  
ATOM   5765  CG  LYS B 397      78.566   7.911-188.110  1.00 36.03           C  
ANISOU 5765  CG  LYS B 397     4694   5347   3648    149     54    276       C  
ATOM   5766  CD  LYS B 397      79.199   7.767-189.511  1.00 42.54           C  
ANISOU 5766  CD  LYS B 397     5613   6213   4337    232    123    276       C  
ATOM   5767  CE  LYS B 397      78.498   8.623-190.541  1.00 58.35           C  
ANISOU 5767  CE  LYS B 397     7605   8335   6228    267    113    360       C  
ATOM   5768  NZ  LYS B 397      79.235   8.601-191.848  1.00 67.77           N  
ANISOU 5768  NZ  LYS B 397     8889   9566   7295    359    201    373       N  
ATOM   5769  N   ALA B 398      81.022   7.269-184.343  1.00 33.20           N  
ANISOU 5769  N   ALA B 398     4198   4685   3732    103    138    205       N  
ATOM   5770  CA  ALA B 398      81.916   6.561-183.430  1.00 33.64           C  
ANISOU 5770  CA  ALA B 398     4249   4661   3873    104    152    161       C  
ATOM   5771  C   ALA B 398      81.299   6.425-182.041  1.00 34.07           C  
ANISOU 5771  C   ALA B 398     4264   4668   4014     23     74    138       C  
ATOM   5772  O   ALA B 398      81.427   5.372-181.395  1.00 32.37           O  
ANISOU 5772  O   ALA B 398     4092   4393   3814      3     38     75       O  
ATOM   5773  CB  ALA B 398      83.267   7.276-183.353  1.00 27.67           C  
ANISOU 5773  CB  ALA B 398     3412   3898   3203    160    255    224       C  
ATOM   5774  N   ALA B 399      80.622   7.468-181.558  1.00 29.19           N  
ANISOU 5774  N   ALA B 399     3573   4071   3448    -17     55    193       N  
ATOM   5775  CA  ALA B 399      80.051   7.385-180.213  1.00 30.55           C  
ANISOU 5775  CA  ALA B 399     3711   4199   3696    -86     -7    175       C  
ATOM   5776  C   ALA B 399      78.946   6.338-180.158  1.00 34.27           C  
ANISOU 5776  C   ALA B 399     4243   4678   4099   -145    -98    115       C  
ATOM   5777  O   ALA B 399      78.825   5.611-179.170  1.00 29.54           O  
ANISOU 5777  O   ALA B 399     3658   4023   3543   -191   -140     72       O  
ATOM   5778  CB  ALA B 399      79.526   8.748-179.770  1.00 29.21           C  
ANISOU 5778  CB  ALA B 399     3469   4045   3585   -101      6    248       C  
ATOM   5779  N   VAL B 400      78.158   6.216-181.231  1.00 34.76           N  
ANISOU 5779  N   VAL B 400     4344   4813   4050   -151   -129    114       N  
ATOM   5780  CA  VAL B 400      77.105   5.201-181.258  1.00 35.82           C  
ANISOU 5780  CA  VAL B 400     4534   4963   4113   -231   -223     56       C  
ATOM   5781  C   VAL B 400      77.696   3.799-181.158  1.00 34.74           C  
ANISOU 5781  C   VAL B 400     4507   4739   3952   -241   -229    -35       C  
ATOM   5782  O   VAL B 400      77.198   2.955-180.399  1.00 33.38           O  
ANISOU 5782  O   VAL B 400     4368   4517   3797   -315   -288    -82       O  
ATOM   5783  CB  VAL B 400      76.241   5.375-182.519  1.00 40.94           C  
ANISOU 5783  CB  VAL B 400     5201   5723   4634   -239   -262     74       C  
ATOM   5784  CG1 VAL B 400      75.481   4.109-182.816  1.00 39.57           C  
ANISOU 5784  CG1 VAL B 400     5116   5556   4362   -330   -354     -7       C  
ATOM   5785  CG2 VAL B 400      75.284   6.536-182.311  1.00 41.56           C  
ANISOU 5785  CG2 VAL B 400     5167   5884   4740   -242   -278    166       C  
ATOM   5786  N   GLU B 401      78.778   3.526-181.903  1.00 31.06           N  
ANISOU 5786  N   GLU B 401     4104   4249   3448   -159   -160    -55       N  
ATOM   5787  CA  GLU B 401      79.371   2.193-181.831  1.00 33.13           C  
ANISOU 5787  CA  GLU B 401     4485   4420   3684   -145   -151   -135       C  
ATOM   5788  C   GLU B 401      80.043   1.940-180.484  1.00 34.09           C  
ANISOU 5788  C   GLU B 401     4566   4458   3928   -133   -134   -133       C  
ATOM   5789  O   GLU B 401      80.119   0.790-180.039  1.00 30.81           O  
ANISOU 5789  O   GLU B 401     4240   3959   3506   -150   -154   -193       O  
ATOM   5790  CB  GLU B 401      80.376   1.983-182.957  1.00 35.45           C  
ANISOU 5790  CB  GLU B 401     4853   4713   3902    -39    -65   -147       C  
ATOM   5791  CG  GLU B 401      79.752   2.026-184.353  1.00 40.35           C  
ANISOU 5791  CG  GLU B 401     5548   5410   4373    -48    -86   -163       C  
ATOM   5792  CD  GLU B 401      78.529   1.126-184.493  1.00 46.96           C  
ANISOU 5792  CD  GLU B 401     6482   6245   5117   -167   -197   -238       C  
ATOM   5793  OE1 GLU B 401      78.473   0.040-183.870  1.00 43.60           O  
ANISOU 5793  OE1 GLU B 401     6140   5721   4705   -216   -228   -306       O  
ATOM   5794  OE2 GLU B 401      77.605   1.510-185.235  1.00 46.52           O  
ANISOU 5794  OE2 GLU B 401     6416   6289   4971   -217   -257   -222       O  
ATOM   5795  N   ILE B 402      80.562   2.980-179.830  1.00 30.54           N  
ANISOU 5795  N   ILE B 402     3993   4027   3584   -106    -98    -66       N  
ATOM   5796  CA  ILE B 402      81.104   2.761-178.478  1.00 25.71           C  
ANISOU 5796  CA  ILE B 402     3341   3351   3077   -109   -100    -64       C  
ATOM   5797  C   ILE B 402      79.997   2.350-177.522  1.00 29.69           C  
ANISOU 5797  C   ILE B 402     3856   3826   3599   -207   -183    -89       C  
ATOM   5798  O   ILE B 402      80.170   1.442-176.691  1.00 28.59           O  
ANISOU 5798  O   ILE B 402     3764   3612   3487   -219   -202   -123       O  
ATOM   5799  CB  ILE B 402      81.856   4.019-178.007  1.00 26.40           C  
ANISOU 5799  CB  ILE B 402     3301   3467   3262    -82    -53      8       C  
ATOM   5800  CG1 ILE B 402      83.164   4.159-178.804  1.00 27.02           C  
ANISOU 5800  CG1 ILE B 402     3364   3567   3336     14     37     34       C  
ATOM   5801  CG2 ILE B 402      82.183   3.963-176.516  1.00 27.45           C  
ANISOU 5801  CG2 ILE B 402     3385   3552   3492   -109    -79     12       C  
ATOM   5802  CD1 ILE B 402      83.606   5.600-178.986  1.00 29.71           C  
ANISOU 5802  CD1 ILE B 402     3598   3958   3730     21     90    110       C  
ATOM   5803  N   ASN B 403      78.842   3.009-177.613  1.00 27.86           N  
ANISOU 5803  N   ASN B 403     3580   3656   3351   -270   -226    -62       N  
ATOM   5804  CA  ASN B 403      77.709   2.646-176.766  1.00 27.81           C  
ANISOU 5804  CA  ASN B 403     3570   3639   3357   -363   -297    -74       C  
ATOM   5805  C   ASN B 403      77.182   1.250-177.088  1.00 31.69           C  
ANISOU 5805  C   ASN B 403     4182   4090   3770   -425   -347   -146       C  
ATOM   5806  O   ASN B 403      76.772   0.507-176.183  1.00 29.92           O  
ANISOU 5806  O   ASN B 403     3988   3807   3572   -488   -385   -170       O  
ATOM   5807  CB  ASN B 403      76.614   3.697-176.908  1.00 31.82           C  
ANISOU 5807  CB  ASN B 403     3993   4239   3860   -398   -320    -16       C  
ATOM   5808  CG  ASN B 403      76.906   4.953-176.072  1.00 41.06           C  
ANISOU 5808  CG  ASN B 403     5068   5409   5125   -365   -277     46       C  
ATOM   5809  OD1 ASN B 403      76.360   5.108-174.991  1.00 34.93           O  
ANISOU 5809  OD1 ASN B 403     4257   4616   4399   -405   -299     61       O  
ATOM   5810  ND2 ASN B 403      77.774   5.836-176.570  1.00 38.28           N  
ANISOU 5810  ND2 ASN B 403     4684   5068   4792   -298   -213     82       N  
ATOM   5811  N   VAL B 404      77.159   0.878-178.374  1.00 28.65           N  
ANISOU 5811  N   VAL B 404     3875   3729   3281   -416   -348   -182       N  
ATOM   5812  CA  VAL B 404      76.825  -0.498-178.737  1.00 30.34           C  
ANISOU 5812  CA  VAL B 404     4235   3881   3412   -477   -388   -263       C  
ATOM   5813  C   VAL B 404      77.783  -1.473-178.068  1.00 28.66           C  
ANISOU 5813  C   VAL B 404     4111   3538   3239   -426   -347   -303       C  
ATOM   5814  O   VAL B 404      77.371  -2.516-177.548  1.00 30.96           O  
ANISOU 5814  O   VAL B 404     4492   3747   3522   -497   -384   -348       O  
ATOM   5815  CB  VAL B 404      76.845  -0.665-180.269  1.00 30.38           C  
ANISOU 5815  CB  VAL B 404     4328   3928   3286   -457   -384   -300       C  
ATOM   5816  CG1 VAL B 404      76.709  -2.144-180.651  1.00 35.22           C  
ANISOU 5816  CG1 VAL B 404     5129   4447   3807   -513   -411   -399       C  
ATOM   5817  CG2 VAL B 404      75.738   0.145-180.875  1.00 32.73           C  
ANISOU 5817  CG2 VAL B 404     4541   4362   3532   -517   -442   -257       C  
ATOM   5818  N   ALA B 405      79.082  -1.166-178.107  1.00 28.49           N  
ANISOU 5818  N   ALA B 405     4065   3501   3258   -301   -267   -279       N  
ATOM   5819  CA  ALA B 405      80.064  -2.040-177.476  1.00 26.13           C  
ANISOU 5819  CA  ALA B 405     3832   3098   2999   -229   -224   -299       C  
ATOM   5820  C   ALA B 405      79.783  -2.207-175.990  1.00 31.58           C  
ANISOU 5820  C   ALA B 405     4479   3744   3777   -281   -263   -280       C  
ATOM   5821  O   ALA B 405      79.899  -3.311-175.452  1.00 31.74           O  
ANISOU 5821  O   ALA B 405     4601   3662   3796   -283   -266   -314       O  
ATOM   5822  CB  ALA B 405      81.473  -1.491-177.678  1.00 29.68           C  
ANISOU 5822  CB  ALA B 405     4212   3573   3491    -93   -136   -254       C  
ATOM   5823  N   VAL B 406      79.415  -1.119-175.317  1.00 32.85           N  
ANISOU 5823  N   VAL B 406     4500   3973   4007   -317   -286   -223       N  
ATOM   5824  CA  VAL B 406      79.154  -1.200-173.883  1.00 29.29           C  
ANISOU 5824  CA  VAL B 406     4011   3487   3630   -361   -317   -203       C  
ATOM   5825  C   VAL B 406      77.978  -2.131-173.615  1.00 30.82           C  
ANISOU 5825  C   VAL B 406     4290   3635   3786   -474   -376   -241       C  
ATOM   5826  O   VAL B 406      78.073  -3.057-172.807  1.00 29.68           O  
ANISOU 5826  O   VAL B 406     4219   3400   3660   -485   -382   -257       O  
ATOM   5827  CB  VAL B 406      78.927   0.205-173.313  1.00 29.19           C  
ANISOU 5827  CB  VAL B 406     3855   3552   3683   -376   -322   -142       C  
ATOM   5828  CG1 VAL B 406      78.374   0.115-171.898  1.00 31.56           C  
ANISOU 5828  CG1 VAL B 406     4132   3823   4036   -434   -358   -126       C  
ATOM   5829  CG2 VAL B 406      80.243   0.974-173.332  1.00 29.38           C  
ANISOU 5829  CG2 VAL B 406     3805   3599   3759   -282   -266   -106       C  
ATOM   5830  N   LEU B 407      76.865  -1.924-174.325  1.00 28.42           N  
ANISOU 5830  N   LEU B 407     3977   3396   3425   -562   -419   -249       N  
ATOM   5831  CA  LEU B 407      75.676  -2.739-174.105  1.00 32.80           C  
ANISOU 5831  CA  LEU B 407     4590   3928   3946   -693   -481   -277       C  
ATOM   5832  C   LEU B 407      75.953  -4.202-174.415  1.00 36.51           C  
ANISOU 5832  C   LEU B 407     5243   4273   4357   -709   -478   -352       C  
ATOM   5833  O   LEU B 407      75.626  -5.088-173.619  1.00 35.99           O  
ANISOU 5833  O   LEU B 407     5248   4120   4308   -773   -495   -366       O  
ATOM   5834  CB  LEU B 407      74.521  -2.223-174.958  1.00 31.72           C  
ANISOU 5834  CB  LEU B 407     4395   3909   3749   -778   -534   -266       C  
ATOM   5835  CG  LEU B 407      73.948  -0.911-174.435  1.00 32.71           C  
ANISOU 5835  CG  LEU B 407     4353   4141   3934   -774   -537   -185       C  
ATOM   5836  CD1 LEU B 407      73.264  -0.147-175.580  1.00 35.23           C  
ANISOU 5836  CD1 LEU B 407     4607   4591   4188   -788   -563   -158       C  
ATOM   5837  CD2 LEU B 407      72.976  -1.194-173.266  1.00 30.30           C  
ANISOU 5837  CD2 LEU B 407     4009   3829   3672   -869   -571   -159       C  
ATOM   5838  N   HIS B 408      76.562  -4.465-175.571  1.00 32.30           N  
ANISOU 5838  N   HIS B 408     4799   3723   3750   -647   -447   -396       N  
ATOM   5839  CA  HIS B 408      76.920  -5.828-175.948  1.00 39.03           C  
ANISOU 5839  CA  HIS B 408     5852   4442   4537   -641   -426   -472       C  
ATOM   5840  C   HIS B 408      77.805  -6.489-174.894  1.00 33.22           C  
ANISOU 5840  C   HIS B 408     5167   3586   3867   -554   -376   -459       C  
ATOM   5841  O   HIS B 408      77.585  -7.649-174.525  1.00 34.50           O  
ANISOU 5841  O   HIS B 408     5475   3624   4011   -604   -381   -498       O  
ATOM   5842  CB  HIS B 408      77.626  -5.804-177.303  1.00 36.15           C  
ANISOU 5842  CB  HIS B 408     5562   4088   4086   -548   -378   -510       C  
ATOM   5843  CG  HIS B 408      78.372  -7.059-177.612  1.00 38.35           C  
ANISOU 5843  CG  HIS B 408     6046   4217   4309   -478   -320   -575       C  
ATOM   5844  ND1 HIS B 408      77.739  -8.236-177.952  1.00 41.05           N  
ANISOU 5844  ND1 HIS B 408     6583   4451   4563   -585   -353   -658       N  
ATOM   5845  CD2 HIS B 408      79.700  -7.326-177.624  1.00 40.57           C  
ANISOU 5845  CD2 HIS B 408     6371   4437   4607   -307   -226   -566       C  
ATOM   5846  CE1 HIS B 408      78.647  -9.174-178.163  1.00 46.00           C  
ANISOU 5846  CE1 HIS B 408     7385   4941   5154   -473   -274   -701       C  
ATOM   5847  NE2 HIS B 408      79.844  -8.649-177.967  1.00 44.72           N  
ANISOU 5847  NE2 HIS B 408     7125   4811   5054   -296   -194   -641       N  
ATOM   5848  N   SER B 409      78.815  -5.767-174.410  1.00 31.63           N  
ANISOU 5848  N   SER B 409     4851   3425   3741   -428   -328   -401       N  
ATOM   5849  CA  SER B 409      79.791  -6.367-173.507  1.00 35.18           C  
ANISOU 5849  CA  SER B 409     5337   3785   4244   -325   -282   -380       C  
ATOM   5850  C   SER B 409      79.174  -6.696-172.151  1.00 36.00           C  
ANISOU 5850  C   SER B 409     5432   3844   4402   -405   -324   -356       C  
ATOM   5851  O   SER B 409      79.453  -7.760-171.586  1.00 33.54           O  
ANISOU 5851  O   SER B 409     5240   3411   4091   -377   -304   -365       O  
ATOM   5852  CB  SER B 409      80.988  -5.431-173.354  1.00 32.54           C  
ANISOU 5852  CB  SER B 409     4861   3530   3973   -192   -234   -319       C  
ATOM   5853  OG  SER B 409      81.610  -5.219-174.621  1.00 35.97           O  
ANISOU 5853  OG  SER B 409     5312   4000   4354   -109   -180   -335       O  
ATOM   5854  N   TYR B 410      78.354  -5.787-171.606  1.00 34.92           N  
ANISOU 5854  N   TYR B 410     5160   3800   4308   -494   -373   -317       N  
ATOM   5855  CA  TYR B 410      77.687  -6.066-170.332  1.00 35.61           C  
ANISOU 5855  CA  TYR B 410     5238   3853   4438   -572   -406   -290       C  
ATOM   5856  C   TYR B 410      76.675  -7.197-170.488  1.00 38.99           C  
ANISOU 5856  C   TYR B 410     5806   4196   4814   -704   -438   -336       C  
ATOM   5857  O   TYR B 410      76.592  -8.088-169.636  1.00 34.71           O  
ANISOU 5857  O   TYR B 410     5353   3549   4286   -727   -433   -332       O  
ATOM   5858  CB  TYR B 410      77.014  -4.800-169.803  1.00 26.68           C  
ANISOU 5858  CB  TYR B 410     3939   2842   3355   -624   -437   -238       C  
ATOM   5859  CG  TYR B 410      77.937  -3.899-169.010  1.00 29.74           C  
ANISOU 5859  CG  TYR B 410     4216   3273   3810   -527   -414   -188       C  
ATOM   5860  CD1 TYR B 410      77.717  -3.676-167.649  1.00 28.75           C  
ANISOU 5860  CD1 TYR B 410     4044   3147   3732   -547   -429   -147       C  
ATOM   5861  CD2 TYR B 410      79.045  -3.306-169.607  1.00 31.69           C  
ANISOU 5861  CD2 TYR B 410     4413   3561   4067   -422   -377   -181       C  
ATOM   5862  CE1 TYR B 410      78.556  -2.853-166.925  1.00 28.58           C  
ANISOU 5862  CE1 TYR B 410     3933   3166   3760   -475   -418   -109       C  
ATOM   5863  CE2 TYR B 410      79.895  -2.514-168.897  1.00 33.30           C  
ANISOU 5863  CE2 TYR B 410     4517   3806   4330   -356   -365   -137       C  
ATOM   5864  CZ  TYR B 410      79.649  -2.286-167.545  1.00 27.75           C  
ANISOU 5864  CZ  TYR B 410     3774   3101   3667   -388   -391   -106       C  
ATOM   5865  OH  TYR B 410      80.499  -1.483-166.849  1.00 29.91           O  
ANISOU 5865  OH  TYR B 410     3958   3417   3989   -338   -388    -70       O  
ATOM   5866  N   GLN B 411      75.929  -7.212-171.601  1.00 33.41           N  
ANISOU 5866  N   GLN B 411     5127   3528   4038   -796   -471   -381       N  
ATOM   5867  CA  GLN B 411      74.989  -8.306-171.822  1.00 31.93           C  
ANISOU 5867  CA  GLN B 411     5078   3260   3795   -945   -509   -432       C  
ATOM   5868  C   GLN B 411      75.725  -9.629-171.978  1.00 36.71           C  
ANISOU 5868  C   GLN B 411     5902   3687   4360   -889   -461   -487       C  
ATOM   5869  O   GLN B 411      75.304 -10.651-171.424  1.00 45.31           O  
ANISOU 5869  O   GLN B 411     7115   4655   5445   -973   -466   -502       O  
ATOM   5870  CB  GLN B 411      74.118  -8.009-173.044  1.00 40.68           C  
ANISOU 5870  CB  GLN B 411     6167   4465   4826  -1053   -565   -468       C  
ATOM   5871  CG  GLN B 411      73.163  -6.834-172.794  1.00 47.63           C  
ANISOU 5871  CG  GLN B 411     6839   5514   5744  -1118   -612   -401       C  
ATOM   5872  CD  GLN B 411      72.555  -6.268-174.069  1.00 56.12           C  
ANISOU 5872  CD  GLN B 411     7861   6718   6745  -1171   -660   -416       C  
ATOM   5873  OE1 GLN B 411      72.928  -6.660-175.173  1.00 50.75           O  
ANISOU 5873  OE1 GLN B 411     7295   6007   5979  -1153   -658   -480       O  
ATOM   5874  NE2 GLN B 411      71.615  -5.342-173.917  1.00 54.11           N  
ANISOU 5874  NE2 GLN B 411     7436   6610   6515  -1225   -700   -352       N  
ATOM   5875  N   LEU B 412      76.852  -9.618-172.697  1.00 36.19           N  
ANISOU 5875  N   LEU B 412     5887   3599   4265   -738   -403   -511       N  
ATOM   5876  CA  LEU B 412      77.654 -10.831-172.850  1.00 40.61           C  
ANISOU 5876  CA  LEU B 412     6657   3988   4786   -647   -338   -554       C  
ATOM   5877  C   LEU B 412      78.144 -11.335-171.496  1.00 44.13           C  
ANISOU 5877  C   LEU B 412     7121   4345   5303   -576   -305   -499       C  
ATOM   5878  O   LEU B 412      78.172 -12.547-171.240  1.00 43.55           O  
ANISOU 5878  O   LEU B 412     7237   4105   5204   -582   -275   -525       O  
ATOM   5879  CB  LEU B 412      78.843 -10.548-173.763  1.00 47.13           C  
ANISOU 5879  CB  LEU B 412     7490   4837   5579   -472   -269   -566       C  
ATOM   5880  CG  LEU B 412      79.589 -11.730-174.365  1.00 66.08           C  
ANISOU 5880  CG  LEU B 412    10125   7076   7907   -368   -190   -624       C  
ATOM   5881  CD1 LEU B 412      78.707 -12.454-175.382  1.00 61.87           C  
ANISOU 5881  CD1 LEU B 412     9784   6466   7256   -515   -224   -726       C  
ATOM   5882  CD2 LEU B 412      80.881 -11.240-175.004  1.00 71.50           C  
ANISOU 5882  CD2 LEU B 412    10756   7823   8589   -166   -109   -601       C  
ATOM   5883  N   ALA B 413      78.539 -10.419-170.626  1.00 41.53           N  
ANISOU 5883  N   ALA B 413     6605   4118   5055   -507   -309   -422       N  
ATOM   5884  CA  ALA B 413      79.071 -10.749-169.312  1.00 37.96           C  
ANISOU 5884  CA  ALA B 413     6148   3612   4664   -429   -286   -361       C  
ATOM   5885  C   ALA B 413      77.981 -11.031-168.288  1.00 36.85           C  
ANISOU 5885  C   ALA B 413     6011   3441   4548   -575   -331   -338       C  
ATOM   5886  O   ALA B 413      78.310 -11.397-167.153  1.00 37.77           O  
ANISOU 5886  O   ALA B 413     6143   3505   4703   -521   -315   -286       O  
ATOM   5887  CB  ALA B 413      79.963  -9.606-168.818  1.00 35.29           C  
ANISOU 5887  CB  ALA B 413     5612   3405   4392   -310   -281   -294       C  
ATOM   5888  N   LYS B 414      76.708 -10.879-168.667  1.00 35.74           N  
ANISOU 5888  N   LYS B 414     5852   3343   4383   -753   -386   -367       N  
ATOM   5889  CA  LYS B 414      75.564 -11.064-167.769  1.00 38.49           C  
ANISOU 5889  CA  LYS B 414     6179   3688   4757   -904   -424   -336       C  
ATOM   5890  C   LYS B 414      75.656 -10.132-166.561  1.00 38.77           C  
ANISOU 5890  C   LYS B 414     6045   3824   4864   -856   -430   -256       C  
ATOM   5891  O   LYS B 414      75.510 -10.542-165.404  1.00 42.24           O  
ANISOU 5891  O   LYS B 414     6509   4209   5331   -867   -421   -210       O  
ATOM   5892  CB  LYS B 414      75.425 -12.529-167.346  1.00 36.41           C  
ANISOU 5892  CB  LYS B 414     6128   3236   4472   -952   -397   -352       C  
ATOM   5893  CG  LYS B 414      75.265 -13.476-168.581  1.00 43.69           C  
ANISOU 5893  CG  LYS B 414     7250   4040   5309  -1020   -392   -446       C  
ATOM   5894  CD  LYS B 414      75.141 -14.927-168.144  1.00 59.84           C  
ANISOU 5894  CD  LYS B 414     9529   5874   7334  -1070   -356   -462       C  
ATOM   5895  CE  LYS B 414      75.074 -15.853-169.348  1.00 76.05           C  
ANISOU 5895  CE  LYS B 414    11808   7792   9294  -1131   -345   -565       C  
ATOM   5896  NZ  LYS B 414      73.968 -15.477-170.275  1.00 88.82           N  
ANISOU 5896  NZ  LYS B 414    13368   9515  10862  -1329   -428   -619       N  
ATOM   5897  N   VAL B 415      75.931  -8.861-166.849  1.00 33.91           N  
ANISOU 5897  N   VAL B 415     5267   3348   4271   -799   -441   -239       N  
ATOM   5898  CA  VAL B 415      75.940  -7.780-165.869  1.00 29.67           C  
ANISOU 5898  CA  VAL B 415     4570   2914   3790   -769   -450   -177       C  
ATOM   5899  C   VAL B 415      74.833  -6.808-166.253  1.00 36.09           C  
ANISOU 5899  C   VAL B 415     5255   3855   4604   -871   -485   -168       C  
ATOM   5900  O   VAL B 415      74.805  -6.307-167.389  1.00 31.47           O  
ANISOU 5900  O   VAL B 415     4630   3335   3992   -871   -495   -197       O  
ATOM   5901  CB  VAL B 415      77.297  -7.067-165.819  1.00 28.23           C  
ANISOU 5901  CB  VAL B 415     4312   2777   3636   -611   -426   -158       C  
ATOM   5902  CG1 VAL B 415      77.266  -5.887-164.835  1.00 28.11           C  
ANISOU 5902  CG1 VAL B 415     4150   2860   3668   -599   -441   -105       C  
ATOM   5903  CG2 VAL B 415      78.397  -8.050-165.459  1.00 33.62           C  
ANISOU 5903  CG2 VAL B 415     5107   3351   4316   -492   -390   -152       C  
ATOM   5904  N   THR B 416      73.915  -6.566-165.315  1.00 34.90           N  
ANISOU 5904  N   THR B 416     5040   3743   4478   -949   -497   -122       N  
ATOM   5905  CA  THR B 416      72.801  -5.632-165.498  1.00 35.46           C  
ANISOU 5905  CA  THR B 416     4977   3943   4554  -1029   -521    -94       C  
ATOM   5906  C   THR B 416      73.261  -4.310-166.102  1.00 30.38           C  
ANISOU 5906  C   THR B 416     4220   3401   3921   -944   -515    -89       C  
ATOM   5907  O   THR B 416      74.252  -3.722-165.656  1.00 32.94           O  
ANISOU 5907  O   THR B 416     4513   3725   4277   -836   -492    -77       O  
ATOM   5908  CB  THR B 416      72.136  -5.366-164.140  1.00 37.73           C  
ANISOU 5908  CB  THR B 416     5205   4257   4876  -1061   -509    -30       C  
ATOM   5909  OG1 THR B 416      71.737  -6.607-163.562  1.00 38.10           O  
ANISOU 5909  OG1 THR B 416     5361   4203   4913  -1142   -506    -26       O  
ATOM   5910  CG2 THR B 416      70.895  -4.492-164.299  1.00 33.66           C  
ANISOU 5910  CG2 THR B 416     4551   3874   4363  -1134   -521     11       C  
ATOM   5911  N   ILE B 417      72.530  -3.845-167.116  1.00 30.93           N  
ANISOU 5911  N   ILE B 417     4227   3562   3963  -1000   -540    -95       N  
ATOM   5912  CA  ILE B 417      72.749  -2.526-167.692  1.00 30.78           C  
ANISOU 5912  CA  ILE B 417     4099   3643   3952   -930   -529    -77       C  
ATOM   5913  C   ILE B 417      71.460  -2.145-168.405  1.00 31.40           C  
ANISOU 5913  C   ILE B 417     4095   3835   3999  -1018   -563    -54       C  
ATOM   5914  O   ILE B 417      70.698  -3.016-168.845  1.00 35.16           O  
ANISOU 5914  O   ILE B 417     4617   4308   4433  -1132   -604    -76       O  
ATOM   5915  CB  ILE B 417      73.975  -2.523-168.642  1.00 32.71           C  
ANISOU 5915  CB  ILE B 417     4393   3857   4177   -837   -512   -120       C  
ATOM   5916  CG1 ILE B 417      74.366  -1.088-169.019  1.00 36.53           C  
ANISOU 5916  CG1 ILE B 417     4767   4429   4683   -759   -488    -90       C  
ATOM   5917  CG2 ILE B 417      73.680  -3.339-169.927  1.00 32.31           C  
ANISOU 5917  CG2 ILE B 417     4432   3792   4054   -897   -540   -176       C  
ATOM   5918  CD1 ILE B 417      75.801  -0.915-169.397  1.00 36.64           C  
ANISOU 5918  CD1 ILE B 417     4802   4412   4709   -651   -454   -108       C  
ATOM   5919  N   VAL B 418      71.207  -0.840-168.521  1.00 29.71           N  
ANISOU 5919  N   VAL B 418     3762   3723   3802   -968   -546     -6       N  
ATOM   5920  CA  VAL B 418      70.003  -0.338-169.174  1.00 32.65           C  
ANISOU 5920  CA  VAL B 418     4035   4225   4145  -1026   -574     35       C  
ATOM   5921  C   VAL B 418      70.413   0.688-170.223  1.00 29.89           C  
ANISOU 5921  C   VAL B 418     3638   3943   3776   -941   -561     43       C  
ATOM   5922  O   VAL B 418      71.276   1.538-169.972  1.00 29.40           O  
ANISOU 5922  O   VAL B 418     3561   3856   3752   -840   -513     53       O  
ATOM   5923  CB  VAL B 418      68.988   0.250-168.165  1.00 31.94           C  
ANISOU 5923  CB  VAL B 418     3840   4204   4092  -1042   -553    112       C  
ATOM   5924  CG1 VAL B 418      69.546   1.453-167.423  1.00 31.81           C  
ANISOU 5924  CG1 VAL B 418     3785   4179   4124   -925   -491    145       C  
ATOM   5925  CG2 VAL B 418      67.670   0.598-168.878  1.00 34.32           C  
ANISOU 5925  CG2 VAL B 418     4026   4655   4358  -1104   -587    166       C  
ATOM   5926  N   ASP B 419      69.872   0.543-171.444  1.00 34.55           N  
ANISOU 5926  N   ASP B 419     4216   4612   4300   -991   -606     33       N  
ATOM   5927  CA  ASP B 419      70.193   1.546-172.445  1.00 34.00           C  
ANISOU 5927  CA  ASP B 419     4101   4612   4205   -907   -589     53       C  
ATOM   5928  C   ASP B 419      69.357   2.813-172.210  1.00 32.55           C  
ANISOU 5928  C   ASP B 419     3781   4540   4046   -865   -565    146       C  
ATOM   5929  O   ASP B 419      68.354   2.804-171.485  1.00 31.06           O  
ANISOU 5929  O   ASP B 419     3523   4401   3878   -914   -573    195       O  
ATOM   5930  CB  ASP B 419      69.988   0.976-173.859  1.00 28.73           C  
ANISOU 5930  CB  ASP B 419     3482   3991   3442   -961   -644     10       C  
ATOM   5931  CG  ASP B 419      68.538   0.714-174.182  1.00 38.79           C  
ANISOU 5931  CG  ASP B 419     4686   5387   4667  -1081   -717     42       C  
ATOM   5932  OD1 ASP B 419      67.782   1.681-174.374  1.00 40.87           O  
ANISOU 5932  OD1 ASP B 419     4819   5781   4927  -1052   -718    123       O  
ATOM   5933  OD2 ASP B 419      68.147  -0.467-174.269  1.00 49.31           O  
ANISOU 5933  OD2 ASP B 419     6091   6685   5959  -1207   -773    -10       O  
ATOM   5934  N   HIS B 420      69.752   3.910-172.871  1.00 33.20           N  
ANISOU 5934  N   HIS B 420     3828   4664   4123   -768   -527    178       N  
ATOM   5935  CA  HIS B 420      69.100   5.194-172.621  1.00 28.02           C  
ANISOU 5935  CA  HIS B 420     3066   4088   3493   -701   -485    269       C  
ATOM   5936  C   HIS B 420      67.667   5.250-173.131  1.00 30.73           C  
ANISOU 5936  C   HIS B 420     3305   4586   3787   -748   -533    335       C  
ATOM   5937  O   HIS B 420      66.892   6.082-172.647  1.00 31.96           O  
ANISOU 5937  O   HIS B 420     3365   4809   3968   -700   -496    420       O  
ATOM   5938  CB  HIS B 420      69.916   6.366-173.205  1.00 27.36           C  
ANISOU 5938  CB  HIS B 420     2985   3994   3418   -589   -426    293       C  
ATOM   5939  CG  HIS B 420      70.291   6.216-174.649  1.00 32.59           C  
ANISOU 5939  CG  HIS B 420     3678   4696   4008   -579   -450    270       C  
ATOM   5940  ND1 HIS B 420      71.169   5.250-175.099  1.00 36.21           N  
ANISOU 5940  ND1 HIS B 420     4235   5085   4438   -607   -472    186       N  
ATOM   5941  CD2 HIS B 420      69.954   6.952-175.736  1.00 35.90           C  
ANISOU 5941  CD2 HIS B 420     4053   5216   4373   -528   -447    325       C  
ATOM   5942  CE1 HIS B 420      71.327   5.377-176.407  1.00 40.03           C  
ANISOU 5942  CE1 HIS B 420     4736   5626   4848   -581   -481    184       C  
ATOM   5943  NE2 HIS B 420      70.593   6.398-176.818  1.00 33.95           N  
ANISOU 5943  NE2 HIS B 420     3878   4962   4059   -537   -471    269       N  
ATOM   5944  N   HIS B 421      67.285   4.391-174.091  1.00 32.35           N  
ANISOU 5944  N   HIS B 421     3524   4852   3914   -840   -614    301       N  
ATOM   5945  CA  HIS B 421      65.898   4.363-174.539  1.00 30.49           C  
ANISOU 5945  CA  HIS B 421     3174   4783   3628   -906   -676    366       C  
ATOM   5946  C   HIS B 421      64.985   3.697-173.513  1.00 32.44           C  
ANISOU 5946  C   HIS B 421     3368   5047   3909  -1010   -698    387       C  
ATOM   5947  O   HIS B 421      63.886   4.195-173.227  1.00 33.64           O  
ANISOU 5947  O   HIS B 421     3383   5328   4072  -1003   -694    484       O  
ATOM   5948  CB  HIS B 421      65.792   3.640-175.894  1.00 29.13           C  
ANISOU 5948  CB  HIS B 421     3046   4673   3349   -990   -766    315       C  
ATOM   5949  CG  HIS B 421      66.608   4.283-176.969  1.00 36.75           C  
ANISOU 5949  CG  HIS B 421     4059   5638   4267   -886   -739    306       C  
ATOM   5950  ND1 HIS B 421      66.224   5.452-177.588  1.00 38.33           N  
ANISOU 5950  ND1 HIS B 421     4163   5958   4441   -787   -718    400       N  
ATOM   5951  CD2 HIS B 421      67.801   3.944-177.508  1.00 36.93           C  
ANISOU 5951  CD2 HIS B 421     4212   5553   4266   -855   -719    224       C  
ATOM   5952  CE1 HIS B 421      67.145   5.806-178.467  1.00 35.40           C  
ANISOU 5952  CE1 HIS B 421     3867   5552   4032   -710   -687    375       C  
ATOM   5953  NE2 HIS B 421      68.106   4.900-178.447  1.00 36.54           N  
ANISOU 5953  NE2 HIS B 421     4143   5565   4176   -751   -687    268       N  
ATOM   5954  N   ALA B 422      65.376   2.517-173.025  1.00 35.82           N  
ANISOU 5954  N   ALA B 422     3903   5356   4350  -1106   -720    304       N  
ATOM   5955  CA  ALA B 422      64.588   1.853-171.994  1.00 37.13           C  
ANISOU 5955  CA  ALA B 422     4033   5522   4553  -1207   -730    326       C  
ATOM   5956  C   ALA B 422      64.535   2.698-170.726  1.00 32.94           C  
ANISOU 5956  C   ALA B 422     3446   4968   4100  -1105   -639    391       C  
ATOM   5957  O   ALA B 422      63.485   2.816-170.088  1.00 33.40           O  
ANISOU 5957  O   ALA B 422     3396   5115   4180  -1134   -627    469       O  
ATOM   5958  CB  ALA B 422      65.176   0.473-171.692  1.00 33.24           C  
ANISOU 5958  CB  ALA B 422     3694   4877   4060  -1308   -756    226       C  
ATOM   5959  N   ALA B 423      65.655   3.322-170.370  1.00 30.12           N  
ANISOU 5959  N   ALA B 423     3163   4500   3783   -987   -574    363       N  
ATOM   5960  CA  ALA B 423      65.722   4.072-169.112  1.00 31.34           C  
ANISOU 5960  CA  ALA B 423     3299   4610   4000   -901   -490    406       C  
ATOM   5961  C   ALA B 423      64.805   5.285-169.157  1.00 38.99           C  
ANISOU 5961  C   ALA B 423     4138   5705   4970   -815   -444    514       C  
ATOM   5962  O   ALA B 423      64.048   5.532-168.215  1.00 30.03           O  
ANISOU 5962  O   ALA B 423     2940   4605   3863   -799   -398    578       O  
ATOM   5963  CB  ALA B 423      67.165   4.481-168.832  1.00 28.87           C  
ANISOU 5963  CB  ALA B 423     3090   4159   3719   -813   -445    348       C  
ATOM   5964  N   THR B 424      64.815   6.026-170.275  1.00 31.80           N  
ANISOU 5964  N   THR B 424     3187   4870   4025   -751   -450    543       N  
ATOM   5965  CA  THR B 424      63.973   7.216-170.360  1.00 30.48           C  
ANISOU 5965  CA  THR B 424     2905   4819   3857   -646   -397    656       C  
ATOM   5966  C   THR B 424      62.505   6.847-170.493  1.00 29.29           C  
ANISOU 5966  C   THR B 424     2606   4845   3678   -716   -443    739       C  
ATOM   5967  O   THR B 424      61.642   7.575-169.988  1.00 34.55           O  
ANISOU 5967  O   THR B 424     3168   5596   4362   -637   -382    842       O  
ATOM   5968  CB  THR B 424      64.415   8.114-171.528  1.00 30.66           C  
ANISOU 5968  CB  THR B 424     2933   4871   3847   -552   -387    674       C  
ATOM   5969  OG1 THR B 424      64.518   7.329-172.715  1.00 32.64           O  
ANISOU 5969  OG1 THR B 424     3196   5173   4031   -638   -481    626       O  
ATOM   5970  CG2 THR B 424      65.785   8.747-171.233  1.00 27.66           C  
ANISOU 5970  CG2 THR B 424     2674   4328   3509   -472   -319    618       C  
ATOM   5971  N   ALA B 425      62.195   5.731-171.162  1.00 27.66           N  
ANISOU 5971  N   ALA B 425     2388   4697   3424   -864   -549    699       N  
ATOM   5972  CA  ALA B 425      60.807   5.274-171.210  1.00 29.11           C  
ANISOU 5972  CA  ALA B 425     2422   5054   3585   -964   -604    776       C  
ATOM   5973  C   ALA B 425      60.309   4.910-169.814  1.00 39.38           C  
ANISOU 5973  C   ALA B 425     3695   6325   4944  -1003   -553    806       C  
ATOM   5974  O   ALA B 425      59.173   5.221-169.440  1.00 39.95           O  
ANISOU 5974  O   ALA B 425     3615   6538   5025   -988   -526    918       O  
ATOM   5975  CB  ALA B 425      60.677   4.080-172.148  1.00 35.36           C  
ANISOU 5975  CB  ALA B 425     3240   5886   4310  -1141   -731    707       C  
ATOM   5976  N   SER B 426      61.149   4.265-169.021  1.00 35.75           N  
ANISOU 5976  N   SER B 426     3376   5686   4519  -1042   -533    715       N  
ATOM   5977  CA  SER B 426      60.727   3.934-167.664  1.00 39.84           C  
ANISOU 5977  CA  SER B 426     3882   6170   5084  -1070   -479    746       C  
ATOM   5978  C   SER B 426      60.626   5.183-166.793  1.00 40.87           C  
ANISOU 5978  C   SER B 426     3982   6296   5252   -898   -358    819       C  
ATOM   5979  O   SER B 426      59.779   5.238-165.892  1.00 38.81           O  
ANISOU 5979  O   SER B 426     3641   6094   5012   -891   -301    898       O  
ATOM   5980  CB  SER B 426      61.684   2.917-167.054  1.00 34.15           C  
ANISOU 5980  CB  SER B 426     3329   5262   4382  -1144   -491    637       C  
ATOM   5981  OG  SER B 426      62.783   3.579-166.427  1.00 42.54           O  
ANISOU 5981  OG  SER B 426     4500   6187   5477  -1015   -420    596       O  
ATOM   5982  N   PHE B 427      61.461   6.199-167.047  1.00 34.56           N  
ANISOU 5982  N   PHE B 427     3250   5425   4455   -762   -312    797       N  
ATOM   5983  CA  PHE B 427      61.320   7.441-166.296  1.00 34.20           C  
ANISOU 5983  CA  PHE B 427     3194   5365   4435   -603   -195    863       C  
ATOM   5984  C   PHE B 427      60.006   8.137-166.626  1.00 43.40           C  
ANISOU 5984  C   PHE B 427     4185   6721   5585   -529   -161   1003       C  
ATOM   5985  O   PHE B 427      59.410   8.786-165.758  1.00 38.48           O  
ANISOU 5985  O   PHE B 427     3519   6122   4979   -429    -60   1082       O  
ATOM   5986  CB  PHE B 427      62.499   8.383-166.559  1.00 31.42           C  
ANISOU 5986  CB  PHE B 427     2957   4890   4090   -493   -155    810       C  
ATOM   5987  CG  PHE B 427      62.466   9.632-165.700  1.00 33.14           C  
ANISOU 5987  CG  PHE B 427     3208   5055   4331   -344    -32    859       C  
ATOM   5988  CD1 PHE B 427      62.766   9.560-164.343  1.00 37.23           C  
ANISOU 5988  CD1 PHE B 427     3814   5461   4870   -338     24    824       C  
ATOM   5989  CD2 PHE B 427      62.093  10.854-166.235  1.00 35.03           C  
ANISOU 5989  CD2 PHE B 427     3398   5353   4559   -208     31    941       C  
ATOM   5990  CE1 PHE B 427      62.714  10.695-163.536  1.00 32.99           C  
ANISOU 5990  CE1 PHE B 427     3329   4866   4340   -207    139    859       C  
ATOM   5991  CE2 PHE B 427      62.050  12.004-165.449  1.00 27.53           C  
ANISOU 5991  CE2 PHE B 427     2503   4335   3623    -69    154    981       C  
ATOM   5992  CZ  PHE B 427      62.355  11.923-164.083  1.00 32.87           C  
ANISOU 5992  CZ  PHE B 427     3279   4894   4317    -73    208    935       C  
ATOM   5993  N   MET B 428      59.543   8.038-167.880  1.00 40.35           N  
ANISOU 5993  N   MET B 428     3697   6478   5157   -567   -241   1039       N  
ATOM   5994  CA  MET B 428      58.243   8.618-168.214  1.00 40.05           C  
ANISOU 5994  CA  MET B 428     3470   6649   5100   -500   -221   1185       C  
ATOM   5995  C   MET B 428      57.127   7.959-167.403  1.00 41.59           C  
ANISOU 5995  C   MET B 428     3538   6953   5312   -584   -214   1257       C  
ATOM   5996  O   MET B 428      56.200   8.631-166.934  1.00 40.41           O  
ANISOU 5996  O   MET B 428     3265   6916   5172   -473   -127   1384       O  
ATOM   5997  CB  MET B 428      57.986   8.489-169.717  1.00 39.42           C  
ANISOU 5997  CB  MET B 428     3306   6712   4959   -548   -331   1204       C  
ATOM   5998  CG  MET B 428      58.964   9.322-170.557  1.00 39.78           C  
ANISOU 5998  CG  MET B 428     3458   6674   4984   -437   -315   1164       C  
ATOM   5999  SD  MET B 428      58.800  11.100-170.290  1.00 42.04           S  
ANISOU 5999  SD  MET B 428     3730   6953   5290   -181   -161   1279       S  
ATOM   6000  CE  MET B 428      57.066  11.352-170.649  1.00 36.26           C  
ANISOU 6000  CE  MET B 428     2741   6513   4524   -131   -170   1466       C  
ATOM   6001  N   LYS B 429      57.195   6.641-167.235  1.00 41.55           N  
ANISOU 6001  N   LYS B 429     3564   6914   5309   -776   -296   1184       N  
ATOM   6002  CA  LYS B 429      56.225   5.955-166.388  1.00 44.40           C  
ANISOU 6002  CA  LYS B 429     3821   7357   5692   -872   -282   1249       C  
ATOM   6003  C   LYS B 429      56.324   6.433-164.943  1.00 43.18           C  
ANISOU 6003  C   LYS B 429     3729   7098   5578   -756   -142   1272       C  
ATOM   6004  O   LYS B 429      55.306   6.552-164.250  1.00 42.19           O  
ANISOU 6004  O   LYS B 429     3476   7087   5467   -727    -71   1385       O  
ATOM   6005  CB  LYS B 429      56.442   4.442-166.473  1.00 47.10           C  
ANISOU 6005  CB  LYS B 429     4230   7637   6028  -1102   -389   1152       C  
ATOM   6006  CG  LYS B 429      55.356   3.622-165.802  1.00 61.91           C  
ANISOU 6006  CG  LYS B 429     6014   9593   7916  -1224   -387   1213       C  
ATOM   6007  CD  LYS B 429      54.047   3.741-166.567  1.00 67.80           C  
ANISOU 6007  CD  LYS B 429     6607  10538   8615  -1226   -430   1303       C  
ATOM   6008  CE  LYS B 429      52.859   3.305-165.721  1.00 75.67           C  
ANISOU 6008  CE  LYS B 429     7506  11617   9628  -1274   -386   1389       C  
ATOM   6009  NZ  LYS B 429      53.047   1.949-165.149  1.00 81.76           N  
ANISOU 6009  NZ  LYS B 429     8387  12260  10417  -1455   -419   1306       N  
ATOM   6010  N   HIS B 430      57.538   6.733-164.479  1.00 35.78           N  
ANISOU 6010  N   HIS B 430     2986   5955   4655   -686   -100   1169       N  
ATOM   6011  CA  HIS B 430      57.703   7.223-163.110  1.00 32.08           C  
ANISOU 6011  CA  HIS B 430     2599   5380   4210   -579     25   1179       C  
ATOM   6012  C   HIS B 430      57.021   8.574-162.936  1.00 40.59           C  
ANISOU 6012  C   HIS B 430     3595   6543   5283   -381    146   1297       C  
ATOM   6013  O   HIS B 430      56.312   8.798-161.944  1.00 36.81           O  
ANISOU 6013  O   HIS B 430     3072   6103   4813   -315    250   1377       O  
ATOM   6014  CB  HIS B 430      59.190   7.317-162.777  1.00 32.73           C  
ANISOU 6014  CB  HIS B 430     2896   5242   4300   -555     27   1045       C  
ATOM   6015  CG  HIS B 430      59.475   7.968-161.458  1.00 38.99           C  
ANISOU 6015  CG  HIS B 430     3793   5921   5099   -441    144   1042       C  
ATOM   6016  ND1 HIS B 430      59.190   7.360-160.251  1.00 40.71           N  
ANISOU 6016  ND1 HIS B 430     4038   6109   5322   -485    187   1052       N  
ATOM   6017  CD2 HIS B 430      60.021   9.172-161.158  1.00 32.15           C  
ANISOU 6017  CD2 HIS B 430     3026   4961   4230   -292    228   1027       C  
ATOM   6018  CE1 HIS B 430      59.550   8.163-159.264  1.00 36.28           C  
ANISOU 6018  CE1 HIS B 430     3588   5446   4751   -363    288   1040       C  
ATOM   6019  NE2 HIS B 430      60.050   9.271-159.786  1.00 38.06           N  
ANISOU 6019  NE2 HIS B 430     3861   5627   4973   -250    314   1022       N  
ATOM   6020  N   LEU B 431      57.188   9.469-163.920  1.00 37.25           N  
ANISOU 6020  N   LEU B 431     3154   6154   4845   -279    141   1317       N  
ATOM   6021  CA  LEU B 431      56.530  10.771-163.866  1.00 33.88           C  
ANISOU 6021  CA  LEU B 431     2659   5803   4411    -77    260   1438       C  
ATOM   6022  C   LEU B 431      55.021  10.621-163.760  1.00 36.24           C  
ANISOU 6022  C   LEU B 431     2731   6331   4707    -67    288   1594       C  
ATOM   6023  O   LEU B 431      54.362  11.376-163.035  1.00 43.96           O  
ANISOU 6023  O   LEU B 431     3667   7348   5687     90    425   1696       O  
ATOM   6024  CB  LEU B 431      56.883  11.603-165.111  1.00 34.33           C  
ANISOU 6024  CB  LEU B 431     2719   5878   4448     11    235   1447       C  
ATOM   6025  CG  LEU B 431      58.303  12.189-165.213  1.00 34.89           C  
ANISOU 6025  CG  LEU B 431     2999   5733   4525     57    250   1329       C  
ATOM   6026  CD1 LEU B 431      58.464  13.026-166.503  1.00 36.32           C  
ANISOU 6026  CD1 LEU B 431     3158   5959   4682    148    236   1368       C  
ATOM   6027  CD2 LEU B 431      58.627  13.020-163.988  1.00 39.21           C  
ANISOU 6027  CD2 LEU B 431     3686   6126   5087    180    389   1315       C  
ATOM   6028  N   GLU B 432      54.453   9.686-164.526  1.00 48.14           N  
ANISOU 6028  N   GLU B 432     4088   7999   6203   -230    161   1618       N  
ATOM   6029  CA  GLU B 432      53.015   9.435-164.477  1.00 50.37           C  
ANISOU 6029  CA  GLU B 432     4129   8524   6485   -256    168   1770       C  
ATOM   6030  C   GLU B 432      52.614   8.861-163.122  1.00 46.27           C  
ANISOU 6030  C   GLU B 432     3617   7971   5993   -305    243   1786       C  
ATOM   6031  O   GLU B 432      51.638   9.308-162.511  1.00 48.72           O  
ANISOU 6031  O   GLU B 432     3850   8365   6298   -186    343   1897       O  
ATOM   6032  CB  GLU B 432      52.622   8.484-165.610  1.00 54.95           C  
ANISOU 6032  CB  GLU B 432     4652   9204   7023   -443     -9   1734       C  
ATOM   6033  CG  GLU B 432      51.129   8.288-165.803  1.00 74.02           C  
ANISOU 6033  CG  GLU B 432     6913  11807   9402   -462    -34   1846       C  
ATOM   6034  CD  GLU B 432      50.809   7.095-166.691  1.00 89.56           C  
ANISOU 6034  CD  GLU B 432     8859  13839  11330   -691   -200   1785       C  
ATOM   6035  OE1 GLU B 432      51.136   5.956-166.294  1.00 95.82           O  
ANISOU 6035  OE1 GLU B 432     9731  14532  12142   -872   -251   1689       O  
ATOM   6036  OE2 GLU B 432      50.235   7.293-167.785  1.00 96.71           O  
ANISOU 6036  OE2 GLU B 432     9681  14885  12179   -688   -272   1834       O  
ATOM   6037  N   ASN B 433      53.358   7.863-162.639  1.00 41.22           N  
ANISOU 6037  N   ASN B 433     3114   7178   5368   -465    190   1661       N  
ATOM   6038  CA  ASN B 433      53.126   7.348-161.287  1.00 40.28           C  
ANISOU 6038  CA  ASN B 433     3030   7004   5270   -501    271   1673       C  
ATOM   6039  C   ASN B 433      53.151   8.474-160.260  1.00 45.42           C  
ANISOU 6039  C   ASN B 433     3762   7579   5917   -274    447   1715       C  
ATOM   6040  O   ASN B 433      52.259   8.582-159.408  1.00 51.70           O  
ANISOU 6040  O   ASN B 433     4463   8464   6715   -212    559   1826       O  
ATOM   6041  CB  ASN B 433      54.184   6.293-160.931  1.00 38.33           C  
ANISOU 6041  CB  ASN B 433     2977   6556   5031   -660    197   1517       C  
ATOM   6042  CG  ASN B 433      54.044   5.022-161.751  1.00 46.87           C  
ANISOU 6042  CG  ASN B 433     4000   7696   6112   -898     42   1476       C  
ATOM   6043  OD1 ASN B 433      52.993   4.761-162.335  1.00 49.05           O  
ANISOU 6043  OD1 ASN B 433     4129   8138   6371   -958    -13   1546       O  
ATOM   6044  ND2 ASN B 433      55.097   4.222-161.786  1.00 45.65           N  
ANISOU 6044  ND2 ASN B 433     4026   7362   5957  -1008    -32   1335       N  
ATOM   6045  N   GLU B 434      54.174   9.333-160.329  1.00 45.76           N  
ANISOU 6045  N   GLU B 434     3985   7452   5949   -151    477   1627       N  
ATOM   6046  CA  GLU B 434      54.349  10.350-159.293  1.00 37.11           C  
ANISOU 6046  CA  GLU B 434     3017   6242   4840     40    637   1637       C  
ATOM   6047  C   GLU B 434      53.318  11.460-159.406  1.00 43.26           C  
ANISOU 6047  C   GLU B 434     3661   7166   5608    246    763   1795       C  
ATOM   6048  O   GLU B 434      52.941  12.055-158.388  1.00 42.76           O  
ANISOU 6048  O   GLU B 434     3642   7076   5530    393    917   1851       O  
ATOM   6049  CB  GLU B 434      55.756  10.932-159.357  1.00 37.99           C  
ANISOU 6049  CB  GLU B 434     3360   6132   4945     87    625   1496       C  
ATOM   6050  CG  GLU B 434      56.830   9.991-158.902  1.00 35.96           C  
ANISOU 6050  CG  GLU B 434     3258   5713   4693    -65    541   1351       C  
ATOM   6051  CD  GLU B 434      56.761   9.723-157.393  1.00 43.62           C  
ANISOU 6051  CD  GLU B 434     4319   6607   5648    -55    630   1346       C  
ATOM   6052  OE1 GLU B 434      55.937   8.898-156.954  1.00 44.55           O  
ANISOU 6052  OE1 GLU B 434     4327   6827   5772   -137    638   1415       O  
ATOM   6053  OE2 GLU B 434      57.527  10.360-156.653  1.00 45.29           O  
ANISOU 6053  OE2 GLU B 434     4713   6658   5836     31    693   1275       O  
ATOM   6054  N   GLN B 435      52.858  11.769-160.625  1.00 42.62           N  
ANISOU 6054  N   GLN B 435     3425   7242   5527    273    705   1871       N  
ATOM   6055  CA  GLN B 435      51.792  12.757-160.746  1.00 44.33           C  
ANISOU 6055  CA  GLN B 435     3491   7621   5732    480    825   2043       C  
ATOM   6056  C   GLN B 435      50.542  12.297-160.007  1.00 47.92           C  
ANISOU 6056  C   GLN B 435     3828   8198   6181    467    861   2140       C  
ATOM   6057  O   GLN B 435      49.862  13.103-159.362  1.00 54.23           O  
ANISOU 6057  O   GLN B 435     4633   9010   6961    661   1002   2233       O  
ATOM   6058  CB  GLN B 435      51.466  13.037-162.210  1.00 45.54           C  
ANISOU 6058  CB  GLN B 435     3525   7910   5867    492    718   2095       C  
ATOM   6059  CG  GLN B 435      50.530  14.237-162.388  1.00 53.80           C  
ANISOU 6059  CG  GLN B 435     4523   9040   6881    732    820   2237       C  
ATOM   6060  CD  GLN B 435      51.192  15.559-162.024  1.00 53.49           C  
ANISOU 6060  CD  GLN B 435     4653   8830   6840    959    985   2229       C  
ATOM   6061  OE1 GLN B 435      52.405  15.716-162.160  1.00 51.35           O  
ANISOU 6061  OE1 GLN B 435     4541   8387   6581    927    971   2106       O  
ATOM   6062  NE2 GLN B 435      50.399  16.507-161.549  1.00 56.23           N  
ANISOU 6062  NE2 GLN B 435     5017   9187   7161   1174   1125   2339       N  
ATOM   6063  N   LYS B 436      50.226  11.002-160.087  1.00 52.48           N  
ANISOU 6063  N   LYS B 436     4320   8850   6771    241    734   2115       N  
ATOM   6064  CA  LYS B 436      49.064  10.479-159.372  1.00 55.04           C  
ANISOU 6064  CA  LYS B 436     4539   9281   7092    208    764   2200       C  
ATOM   6065  C   LYS B 436      49.323  10.401-157.872  1.00 52.14           C  
ANISOU 6065  C   LYS B 436     4289   8788   6732    250    904   2178       C  
ATOM   6066  O   LYS B 436      48.440  10.709-157.067  1.00 57.10           O  
ANISOU 6066  O   LYS B 436     4879   9469   7348    369   1019   2273       O  
ATOM   6067  CB  LYS B 436      48.693   9.100-159.911  1.00 63.00           C  
ANISOU 6067  CB  LYS B 436     5449  10381   8108    -56    593   2169       C  
ATOM   6068  CG  LYS B 436      48.301   9.077-161.376  1.00 72.61           C  
ANISOU 6068  CG  LYS B 436     6555  11736   9297   -113    451   2193       C  
ATOM   6069  CD  LYS B 436      48.554   7.701-161.987  1.00 80.92           C  
ANISOU 6069  CD  LYS B 436     7613  12782  10350   -392    277   2089       C  
ATOM   6070  CE  LYS B 436      47.968   6.579-161.130  1.00 87.90           C  
ANISOU 6070  CE  LYS B 436     8466  13676  11255   -550    274   2095       C  
ATOM   6071  NZ  LYS B 436      48.331   5.226-161.652  1.00 88.04           N  
ANISOU 6071  NZ  LYS B 436     8536  13640  11273   -815    121   1979       N  
ATOM   6072  N   ALA B 437      50.531   9.996-157.478  1.00 48.23           N  
ANISOU 6072  N   ALA B 437     3947   8129   6249    157    899   2058       N  
ATOM   6073  CA  ALA B 437      50.820   9.762-156.067  1.00 51.81           C  
ANISOU 6073  CA  ALA B 437     4527   8465   6692    166   1016   2033       C  
ATOM   6074  C   ALA B 437      50.992  11.060-155.283  1.00 54.17           C  
ANISOU 6074  C   ALA B 437     4968   8660   6953    421   1203   2051       C  
ATOM   6075  O   ALA B 437      50.494  11.172-154.158  1.00 50.30           O  
ANISOU 6075  O   ALA B 437     4518   8157   6438    509   1331   2098       O  
ATOM   6076  CB  ALA B 437      52.071   8.896-155.929  1.00 56.46           C  
ANISOU 6076  CB  ALA B 437     5304   8862   7287    -11    903   1862       C  
ATOM   6077  N   ARG B 438      51.690  12.046-155.853  1.00 52.79           N  
ANISOU 6077  N   ARG B 438     4917   8375   6767    538   1201   1988       N  
ATOM   6078  CA  ARG B 438      52.105  13.231-155.112  1.00 49.45           C  
ANISOU 6078  CA  ARG B 438     4705   7784   6301    745   1351   1954       C  
ATOM   6079  C   ARG B 438      51.797  14.550-155.801  1.00 51.96           C  
ANISOU 6079  C   ARG B 438     4994   8137   6610    960   1436   2034       C  
ATOM   6080  O   ARG B 438      52.077  15.604-155.216  1.00 49.98           O  
ANISOU 6080  O   ARG B 438     4931   7739   6321   1139   1573   2011       O  
ATOM   6081  CB  ARG B 438      53.617  13.193-154.836  1.00 49.81           C  
ANISOU 6081  CB  ARG B 438     5022   7573   6332    666   1278   1757       C  
ATOM   6082  CG  ARG B 438      54.069  12.048-153.955  1.00 61.16           C  
ANISOU 6082  CG  ARG B 438     6541   8933   7762    497   1221   1672       C  
ATOM   6083  CD  ARG B 438      55.351  12.395-153.198  1.00 57.78           C  
ANISOU 6083  CD  ARG B 438     6399   8260   7293    509   1226   1516       C  
ATOM   6084  NE  ARG B 438      56.521  12.511-154.070  1.00 50.82           N  
ANISOU 6084  NE  ARG B 438     5606   7267   6435    436   1096   1393       N  
ATOM   6085  CZ  ARG B 438      57.749  12.759-153.623  1.00 49.25           C  
ANISOU 6085  CZ  ARG B 438     5626   6874   6210    416   1067   1255       C  
ATOM   6086  NH1 ARG B 438      57.959  12.916-152.317  1.00 50.24           N  
ANISOU 6086  NH1 ARG B 438     5915   6895   6279    460   1150   1216       N  
ATOM   6087  NH2 ARG B 438      58.765  12.840-154.469  1.00 42.80           N  
ANISOU 6087  NH2 ARG B 438     4864   5979   5421    348    954   1160       N  
ATOM   6088  N   GLY B 439      51.260  14.536-157.017  1.00 45.82           N  
ANISOU 6088  N   GLY B 439     4006   7543   5861    947   1357   2125       N  
ATOM   6089  CA  GLY B 439      50.990  15.776-157.712  1.00 47.94           C  
ANISOU 6089  CA  GLY B 439     4277   7822   6115   1151   1412   2194       C  
ATOM   6090  C   GLY B 439      52.184  16.402-158.393  1.00 52.95           C  
ANISOU 6090  C   GLY B 439     5080   8289   6750   1165   1374   2083       C  
ATOM   6091  O   GLY B 439      52.188  17.614-158.629  1.00 55.16           O  
ANISOU 6091  O   GLY B 439     5439   8507   7012   1366   1482   2126       O  
ATOM   6092  N   GLY B 440      53.195  15.620-158.721  1.00 47.18           N  
ANISOU 6092  N   GLY B 440     4430   7460   6038    957   1214   1933       N  
ATOM   6093  CA  GLY B 440      54.348  16.153-159.417  1.00 49.10           C  
ANISOU 6093  CA  GLY B 440     4835   7539   6283    949   1153   1820       C  
ATOM   6094  C   GLY B 440      55.581  15.328-159.120  1.00 42.83           C  
ANISOU 6094  C   GLY B 440     4195   6580   5499    751   1035   1640       C  
ATOM   6095  O   GLY B 440      55.537  14.334-158.402  1.00 49.30           O  
ANISOU 6095  O   GLY B 440     5003   7406   6322    625    998   1604       O  
ATOM   6096  N   CYS B 441      56.690  15.774-159.695  1.00 41.52           N  
ANISOU 6096  N   CYS B 441     4171   6267   5337    734    982   1537       N  
ATOM   6097  CA  CYS B 441      57.971  15.094-159.574  1.00 39.84           C  
ANISOU 6097  CA  CYS B 441     4096   5906   5136    565    868   1374       C  
ATOM   6098  C   CYS B 441      59.115  16.064-159.855  1.00 43.28           C  
ANISOU 6098  C   CYS B 441     4720   6157   5570    615    883   1284       C  
ATOM   6099  O   CYS B 441      59.207  16.614-160.960  1.00 38.75           O  
ANISOU 6099  O   CYS B 441     4107   5612   5003    662    864   1317       O  
ATOM   6100  CB  CYS B 441      58.029  13.900-160.532  1.00 45.46           C  
ANISOU 6100  CB  CYS B 441     4670   6731   5871    385    700   1352       C  
ATOM   6101  SG  CYS B 441      59.591  12.978-160.499  1.00 45.89           S  
ANISOU 6101  SG  CYS B 441     4878   6618   5941    196    563   1167       S  
ATOM   6102  N   PRO B 442      60.008  16.292-158.892  1.00 36.16           N  
ANISOU 6102  N   PRO B 442     4020   5068   4653    596    913   1174       N  
ATOM   6103  CA  PRO B 442      61.186  17.126-159.166  1.00 36.91           C  
ANISOU 6103  CA  PRO B 442     4285   4988   4750    604    910   1082       C  
ATOM   6104  C   PRO B 442      62.112  16.441-160.163  1.00 36.91           C  
ANISOU 6104  C   PRO B 442     4249   4992   4783    457    757   1006       C  
ATOM   6105  O   PRO B 442      62.538  15.302-159.961  1.00 32.46           O  
ANISOU 6105  O   PRO B 442     3665   4437   4230    314    652    938       O  
ATOM   6106  CB  PRO B 442      61.848  17.270-157.794  1.00 40.04           C  
ANISOU 6106  CB  PRO B 442     4881   5218   5115    583    952    982       C  
ATOM   6107  CG  PRO B 442      61.446  16.053-157.061  1.00 38.14           C  
ANISOU 6107  CG  PRO B 442     4566   5059   4868    494    908    983       C  
ATOM   6108  CD  PRO B 442      60.066  15.670-157.553  1.00 35.52           C  
ANISOU 6108  CD  PRO B 442     4012   4934   4549    540    929   1124       C  
ATOM   6109  N   ALA B 443      62.440  17.152-161.235  1.00 40.03           N  
ANISOU 6109  N   ALA B 443     4646   5373   5191    502    754   1022       N  
ATOM   6110  CA  ALA B 443      63.268  16.579-162.285  1.00 36.10           C  
ANISOU 6110  CA  ALA B 443     4111   4888   4717    383    625    963       C  
ATOM   6111  C   ALA B 443      64.106  17.667-162.945  1.00 33.82           C  
ANISOU 6111  C   ALA B 443     3929   4485   4437    433    658    940       C  
ATOM   6112  O   ALA B 443      63.626  18.776-163.197  1.00 32.09           O  
ANISOU 6112  O   ALA B 443     3732   4253   4206    576    764   1021       O  
ATOM   6113  CB  ALA B 443      62.421  15.858-163.341  1.00 40.95           C  
ANISOU 6113  CB  ALA B 443     4525   5703   5331    355    549   1043       C  
ATOM   6114  N   ASP B 444      65.359  17.330-163.211  1.00 33.81           N  
ANISOU 6114  N   ASP B 444     3990   4400   4455    317    573    835       N  
ATOM   6115  CA  ASP B 444      66.341  18.236-163.794  1.00 34.67           C  
ANISOU 6115  CA  ASP B 444     4200   4393   4579    327    593    802       C  
ATOM   6116  C   ASP B 444      66.512  17.821-165.258  1.00 27.74           C  
ANISOU 6116  C   ASP B 444     3213   3618   3709    292    511    825       C  
ATOM   6117  O   ASP B 444      67.243  16.876-165.560  1.00 31.44           O  
ANISOU 6117  O   ASP B 444     3656   4100   4189    173    407    752       O  
ATOM   6118  CB  ASP B 444      67.647  18.150-163.007  1.00 35.85           C  
ANISOU 6118  CB  ASP B 444     4486   4394   4742    220    557    677       C  
ATOM   6119  CG  ASP B 444      68.710  19.144-163.480  1.00 44.50           C  
ANISOU 6119  CG  ASP B 444     5689   5362   5857    211    585    642       C  
ATOM   6120  OD1 ASP B 444      68.728  19.531-164.673  1.00 40.70           O  
ANISOU 6120  OD1 ASP B 444     5160   4918   5386    250    593    695       O  
ATOM   6121  OD2 ASP B 444      69.570  19.498-162.647  1.00 37.31           O  
ANISOU 6121  OD2 ASP B 444     4910   4317   4949    152    592    560       O  
ATOM   6122  N   TRP B 445      65.828  18.541-166.152  1.00 34.81           N  
ANISOU 6122  N   TRP B 445     4052   4586   4590    406    565    931       N  
ATOM   6123  CA  TRP B 445      65.787  18.194-167.575  1.00 31.12           C  
ANISOU 6123  CA  TRP B 445     3476   4240   4110    390    492    969       C  
ATOM   6124  C   TRP B 445      67.177  17.927-168.146  1.00 31.88           C  
ANISOU 6124  C   TRP B 445     3630   4257   4224    286    426    875       C  
ATOM   6125  O   TRP B 445      67.408  16.917-168.825  1.00 35.77           O  
ANISOU 6125  O   TRP B 445     4051   4832   4707    199    323    841       O  
ATOM   6126  CB  TRP B 445      65.099  19.330-168.328  1.00 32.13           C  
ANISOU 6126  CB  TRP B 445     3580   4412   4216    549    583   1096       C  
ATOM   6127  CG  TRP B 445      64.720  19.007-169.751  1.00 35.32           C  
ANISOU 6127  CG  TRP B 445     3853   4981   4586    557    512   1163       C  
ATOM   6128  CD1 TRP B 445      63.519  18.528-170.192  1.00 35.69           C  
ANISOU 6128  CD1 TRP B 445     3734   5230   4597    587    467   1255       C  
ATOM   6129  CD2 TRP B 445      65.542  19.167-170.910  1.00 33.75           C  
ANISOU 6129  CD2 TRP B 445     3680   4766   4378    533    478   1147       C  
ATOM   6130  NE1 TRP B 445      63.539  18.388-171.569  1.00 36.05           N  
ANISOU 6130  NE1 TRP B 445     3710   5386   4603    581    399   1291       N  
ATOM   6131  CE2 TRP B 445      64.772  18.769-172.028  1.00 35.47           C  
ANISOU 6131  CE2 TRP B 445     3756   5178   4543    554    410   1226       C  
ATOM   6132  CE3 TRP B 445      66.858  19.605-171.112  1.00 33.52           C  
ANISOU 6132  CE3 TRP B 445     3774   4585   4375    490    497   1076       C  
ATOM   6133  CZ2 TRP B 445      65.275  18.794-173.333  1.00 33.13           C  
ANISOU 6133  CZ2 TRP B 445     3455   4922   4213    545    367   1233       C  
ATOM   6134  CZ3 TRP B 445      67.356  19.628-172.407  1.00 36.35           C  
ANISOU 6134  CZ3 TRP B 445     4115   4985   4710    482    463   1091       C  
ATOM   6135  CH2 TRP B 445      66.558  19.232-173.506  1.00 32.86           C  
ANISOU 6135  CH2 TRP B 445     3546   4731   4207    516    401   1168       C  
ATOM   6136  N   ALA B 446      68.117  18.830-167.888  1.00 28.78           N  
ANISOU 6136  N   ALA B 446     3373   3706   3858    292    488    835       N  
ATOM   6137  CA  ALA B 446      69.443  18.704-168.482  1.00 38.69           C  
ANISOU 6137  CA  ALA B 446     4667   4899   5134    204    439    765       C  
ATOM   6138  C   ALA B 446      70.188  17.458-168.024  1.00 34.83           C  
ANISOU 6138  C   ALA B 446     4165   4407   4660     71    336    660       C  
ATOM   6139  O   ALA B 446      71.095  17.009-168.732  1.00 31.61           O  
ANISOU 6139  O   ALA B 446     3745   4005   4262      7    279    617       O  
ATOM   6140  CB  ALA B 446      70.270  19.947-168.174  1.00 33.10           C  
ANISOU 6140  CB  ALA B 446     4103   4020   4453    219    527    747       C  
ATOM   6141  N   TRP B 447      69.853  16.902-166.850  1.00 32.33           N  
ANISOU 6141  N   TRP B 447     3859   4081   4345     38    318    624       N  
ATOM   6142  CA  TRP B 447      70.479  15.660-166.425  1.00 29.20           C  
ANISOU 6142  CA  TRP B 447     3450   3687   3958    -73    223    538       C  
ATOM   6143  C   TRP B 447      69.681  14.423-166.832  1.00 30.73           C  
ANISOU 6143  C   TRP B 447     3534   4015   4127   -106    148    556       C  
ATOM   6144  O   TRP B 447      70.259  13.344-167.004  1.00 28.13           O  
ANISOU 6144  O   TRP B 447     3191   3696   3800   -190     67    495       O  
ATOM   6145  CB  TRP B 447      70.677  15.694-164.893  1.00 27.24           C  
ANISOU 6145  CB  TRP B 447     3289   3346   3716   -102    241    486       C  
ATOM   6146  CG  TRP B 447      71.852  16.545-164.530  1.00 30.83           C  
ANISOU 6146  CG  TRP B 447     3856   3667   4193   -131    268    432       C  
ATOM   6147  CD1 TRP B 447      72.000  17.880-164.749  1.00 34.96           C  
ANISOU 6147  CD1 TRP B 447     4454   4106   4722    -78    355    460       C  
ATOM   6148  CD2 TRP B 447      73.068  16.101-163.911  1.00 39.93           C  
ANISOU 6148  CD2 TRP B 447     5053   4758   5363   -229    205    344       C  
ATOM   6149  NE1 TRP B 447      73.229  18.299-164.302  1.00 39.86           N  
ANISOU 6149  NE1 TRP B 447     5164   4616   5365   -157    345    390       N  
ATOM   6150  CE2 TRP B 447      73.904  17.226-163.786  1.00 40.99           C  
ANISOU 6150  CE2 TRP B 447     5279   4781   5514   -247    250    321       C  
ATOM   6151  CE3 TRP B 447      73.518  14.864-163.435  1.00 44.15           C  
ANISOU 6151  CE3 TRP B 447     5559   5320   5897   -301    116    290       C  
ATOM   6152  CZ2 TRP B 447      75.166  17.157-163.195  1.00 47.82           C  
ANISOU 6152  CZ2 TRP B 447     6191   5582   6395   -344    198    247       C  
ATOM   6153  CZ3 TRP B 447      74.778  14.794-162.859  1.00 51.07           C  
ANISOU 6153  CZ3 TRP B 447     6483   6132   6788   -376     72    222       C  
ATOM   6154  CH2 TRP B 447      75.583  15.937-162.742  1.00 46.06           C  
ANISOU 6154  CH2 TRP B 447     5923   5407   6171   -400    108    201       C  
ATOM   6155  N   ILE B 448      68.362  14.563-166.963  1.00 28.52           N  
ANISOU 6155  N   ILE B 448     3177   3836   3823    -43    177    641       N  
ATOM   6156  CA  ILE B 448      67.505  13.444-167.321  1.00 27.91           C  
ANISOU 6156  CA  ILE B 448     2990   3894   3721    -93    104    664       C  
ATOM   6157  C   ILE B 448      67.650  13.111-168.809  1.00 32.62           C  
ANISOU 6157  C   ILE B 448     3531   4573   4289   -115     40    671       C  
ATOM   6158  O   ILE B 448      67.655  11.945-169.205  1.00 28.22           O  
ANISOU 6158  O   ILE B 448     2940   4070   3714   -205    -47    630       O  
ATOM   6159  CB  ILE B 448      66.048  13.789-166.946  1.00 29.25           C  
ANISOU 6159  CB  ILE B 448     3078   4162   3875    -17    159    766       C  
ATOM   6160  CG1 ILE B 448      65.894  13.867-165.416  1.00 31.93           C  
ANISOU 6160  CG1 ILE B 448     3480   4422   4228     -7    217    748       C  
ATOM   6161  CG2 ILE B 448      65.066  12.788-167.534  1.00 27.41           C  
ANISOU 6161  CG2 ILE B 448     2708   4094   3612    -78     80    808       C  
ATOM   6162  CD1 ILE B 448      66.113  12.534-164.667  1.00 29.18           C  
ANISOU 6162  CD1 ILE B 448     3142   4060   3886   -128    144    677       C  
ATOM   6163  N   VAL B 449      67.781  14.124-169.650  1.00 29.43           N  
ANISOU 6163  N   VAL B 449     3132   4174   3876    -32     89    722       N  
ATOM   6164  CA  VAL B 449      67.948  13.887-171.089  1.00 26.94           C  
ANISOU 6164  CA  VAL B 449     2776   3939   3521    -42     36    732       C  
ATOM   6165  C   VAL B 449      69.336  13.313-171.348  1.00 30.33           C  
ANISOU 6165  C   VAL B 449     3277   4282   3965   -118     -6    632       C  
ATOM   6166  O   VAL B 449      70.332  13.926-170.946  1.00 28.74           O  
ANISOU 6166  O   VAL B 449     3154   3960   3805   -107     43    598       O  
ATOM   6167  CB  VAL B 449      67.711  15.182-171.875  1.00 31.04           C  
ANISOU 6167  CB  VAL B 449     3288   4482   4022     80    110    827       C  
ATOM   6168  CG1 VAL B 449      67.950  14.944-173.375  1.00 30.44           C  
ANISOU 6168  CG1 VAL B 449     3181   4491   3894     72     57    838       C  
ATOM   6169  CG2 VAL B 449      66.297  15.661-171.602  1.00 29.73           C  
ANISOU 6169  CG2 VAL B 449     3038   4419   3840    171    154    938       C  
ATOM   6170  N   PRO B 450      69.449  12.155-172.005  1.00 29.47           N  
ANISOU 6170  N   PRO B 450     3146   4230   3822   -194    -93    585       N  
ATOM   6171  CA  PRO B 450      70.755  11.492-172.161  1.00 31.99           C  
ANISOU 6171  CA  PRO B 450     3533   4469   4155   -251   -124    493       C  
ATOM   6172  C   PRO B 450      71.717  12.286-173.029  1.00 31.59           C  
ANISOU 6172  C   PRO B 450     3516   4382   4105   -201    -78    503       C  
ATOM   6173  O   PRO B 450      71.302  13.129-173.847  1.00 34.45           O  
ANISOU 6173  O   PRO B 450     3851   4800   4437   -130    -41    578       O  
ATOM   6174  CB  PRO B 450      70.395  10.147-172.817  1.00 32.78           C  
ANISOU 6174  CB  PRO B 450     3610   4646   4199   -328   -216    455       C  
ATOM   6175  CG  PRO B 450      69.020  10.314-173.336  1.00 42.89           C  
ANISOU 6175  CG  PRO B 450     4800   6068   5430   -313   -239    535       C  
ATOM   6176  CD  PRO B 450      68.338  11.294-172.428  1.00 32.61           C  
ANISOU 6176  CD  PRO B 450     3461   4763   4167   -243   -168    608       C  
ATOM   6177  N   PRO B 451      73.023  12.016-172.902  1.00 31.70           N  
ANISOU 6177  N   PRO B 451     3584   4310   4152   -233    -77    437       N  
ATOM   6178  CA  PRO B 451      74.025  12.835-173.599  1.00 29.86           C  
ANISOU 6178  CA  PRO B 451     3377   4037   3932   -194    -20    452       C  
ATOM   6179  C   PRO B 451      74.214  12.507-175.078  1.00 36.44           C  
ANISOU 6179  C   PRO B 451     4201   4945   4702   -175    -37    461       C  
ATOM   6180  O   PRO B 451      74.918  13.262-175.766  1.00 35.24           O  
ANISOU 6180  O   PRO B 451     4064   4773   4554   -134     21    492       O  
ATOM   6181  CB  PRO B 451      75.310  12.554-172.811  1.00 28.94           C  
ANISOU 6181  CB  PRO B 451     3300   3824   3874   -242    -22    384       C  
ATOM   6182  CG  PRO B 451      75.106  11.172-172.240  1.00 27.88           C  
ANISOU 6182  CG  PRO B 451     3166   3699   3729   -298    -96    323       C  
ATOM   6183  CD  PRO B 451      73.635  11.089-171.921  1.00 30.17           C  
ANISOU 6183  CD  PRO B 451     3424   4048   3992   -298   -116    359       C  
ATOM   6184  N   ILE B 452      73.669  11.398-175.578  1.00 35.69           N  
ANISOU 6184  N   ILE B 452     4091   4925   4544   -210   -110    432       N  
ATOM   6185  CA  ILE B 452      73.517  11.192-177.020  1.00 32.00           C  
ANISOU 6185  CA  ILE B 452     3621   4548   3991   -188   -131    449       C  
ATOM   6186  C   ILE B 452      72.038  10.998-177.296  1.00 37.58           C  
ANISOU 6186  C   ILE B 452     4269   5374   4634   -198   -189    493       C  
ATOM   6187  O   ILE B 452      71.270  10.604-176.409  1.00 34.73           O  
ANISOU 6187  O   ILE B 452     3876   5023   4296   -244   -224    487       O  
ATOM   6188  CB  ILE B 452      74.315   9.985-177.575  1.00 35.27           C  
ANISOU 6188  CB  ILE B 452     4089   4947   4365   -227   -169    366       C  
ATOM   6189  CG1 ILE B 452      74.007   8.719-176.768  1.00 35.45           C  
ANISOU 6189  CG1 ILE B 452     4131   4942   4395   -308   -239    295       C  
ATOM   6190  CG2 ILE B 452      75.809  10.272-177.639  1.00 39.68           C  
ANISOU 6190  CG2 ILE B 452     4680   5426   4972   -196   -104    348       C  
ATOM   6191  CD1 ILE B 452      74.490   7.437-177.420  1.00 38.81           C  
ANISOU 6191  CD1 ILE B 452     4628   5357   4762   -341   -279    217       C  
ATOM   6192  N   SER B 453      71.637  11.295-178.537  1.00 37.87           N  
ANISOU 6192  N   SER B 453     4286   5513   4588   -156   -198    545       N  
ATOM   6193  CA  SER B 453      70.302  10.964-179.034  1.00 39.17           C  
ANISOU 6193  CA  SER B 453     4385   5824   4673   -179   -274    585       C  
ATOM   6194  C   SER B 453      69.195  11.570-178.181  1.00 35.03           C  
ANISOU 6194  C   SER B 453     3776   5344   4191   -152   -260    664       C  
ATOM   6195  O   SER B 453      68.136  10.965-178.019  1.00 36.81           O  
ANISOU 6195  O   SER B 453     3933   5666   4385   -211   -331    675       O  
ATOM   6196  CB  SER B 453      70.127   9.450-179.130  1.00 40.99           C  
ANISOU 6196  CB  SER B 453     4645   6074   4855   -295   -372    492       C  
ATOM   6197  OG  SER B 453      71.032   8.912-180.092  1.00 41.55           O  
ANISOU 6197  OG  SER B 453     4803   6119   4864   -299   -378    428       O  
ATOM   6198  N   GLY B 454      69.425  12.768-177.637  1.00 34.78           N  
ANISOU 6198  N   GLY B 454     3750   5240   4226    -65   -162    721       N  
ATOM   6199  CA  GLY B 454      68.475  13.384-176.725  1.00 34.38           C  
ANISOU 6199  CA  GLY B 454     3640   5208   4217    -21   -126    792       C  
ATOM   6200  C   GLY B 454      67.035  13.393-177.203  1.00 32.96           C  
ANISOU 6200  C   GLY B 454     3344   5208   3970      4   -174    885       C  
ATOM   6201  O   GLY B 454      66.148  12.867-176.524  1.00 33.60           O  
ANISOU 6201  O   GLY B 454     3355   5350   4061    -46   -215    893       O  
ATOM   6202  N   SER B 455      66.772  13.973-178.381  1.00 31.29           N  
ANISOU 6202  N   SER B 455     3104   5099   3688     81   -172    964       N  
ATOM   6203  CA  SER B 455      65.386  14.120-178.787  1.00 31.48           C  
ANISOU 6203  CA  SER B 455     2999   5311   3649    120   -215   1073       C  
ATOM   6204  C   SER B 455      64.789  12.832-179.335  1.00 34.34           C  
ANISOU 6204  C   SER B 455     3301   5814   3931    -12   -357   1028       C  
ATOM   6205  O   SER B 455      63.608  12.824-179.691  1.00 34.15           O  
ANISOU 6205  O   SER B 455     3152   5973   3850     -6   -415   1116       O  
ATOM   6206  CB  SER B 455      65.254  15.236-179.843  1.00 35.26           C  
ANISOU 6206  CB  SER B 455     3465   5860   4070    260   -164   1189       C  
ATOM   6207  OG  SER B 455      65.790  14.800-181.073  1.00 37.51           O  
ANISOU 6207  OG  SER B 455     3794   6188   4269    222   -223   1148       O  
ATOM   6208  N   LEU B 456      65.575  11.763-179.443  1.00 33.05           N  
ANISOU 6208  N   LEU B 456     3226   5572   3758   -130   -412    898       N  
ATOM   6209  CA  LEU B 456      65.021  10.456-179.767  1.00 34.40           C  
ANISOU 6209  CA  LEU B 456     3370   5839   3862   -277   -540    838       C  
ATOM   6210  C   LEU B 456      64.396   9.778-178.554  1.00 33.91           C  
ANISOU 6210  C   LEU B 456     3256   5763   3864   -370   -566    816       C  
ATOM   6211  O   LEU B 456      63.739   8.744-178.708  1.00 37.64           O  
ANISOU 6211  O   LEU B 456     3691   6323   4289   -505   -669    784       O  
ATOM   6212  CB  LEU B 456      66.109   9.549-180.349  1.00 35.26           C  
ANISOU 6212  CB  LEU B 456     3615   5851   3930   -352   -575    708       C  
ATOM   6213  CG  LEU B 456      66.982  10.143-181.475  1.00 37.87           C  
ANISOU 6213  CG  LEU B 456     4019   6164   4205   -261   -529    715       C  
ATOM   6214  CD1 LEU B 456      67.976   9.103-181.989  1.00 33.18           C  
ANISOU 6214  CD1 LEU B 456     3556   5484   3566   -334   -559    587       C  
ATOM   6215  CD2 LEU B 456      66.150  10.706-182.633  1.00 39.04           C  
ANISOU 6215  CD2 LEU B 456     4091   6501   4242   -202   -570    820       C  
ATOM   6216  N   THR B 457      64.617  10.321-177.338  1.00 35.59           N  
ANISOU 6216  N   THR B 457     3480   5863   4180   -311   -471    831       N  
ATOM   6217  CA  THR B 457      64.032   9.770-176.127  1.00 35.82           C  
ANISOU 6217  CA  THR B 457     3465   5879   4267   -382   -478    822       C  
ATOM   6218  C   THR B 457      62.822  10.596-175.716  1.00 39.89           C  
ANISOU 6218  C   THR B 457     3839   6520   4798   -294   -435    960       C  
ATOM   6219  O   THR B 457      62.768  11.798-175.988  1.00 36.28           O  
ANISOU 6219  O   THR B 457     3364   6082   4341   -147   -358   1049       O  
ATOM   6220  CB  THR B 457      65.059   9.757-174.989  1.00 32.53           C  
ANISOU 6220  CB  THR B 457     3159   5260   3940   -375   -406    745       C  
ATOM   6221  OG1 THR B 457      65.377  11.105-174.610  1.00 35.32           O  
ANISOU 6221  OG1 THR B 457     3530   5546   4342   -235   -293    803       O  
ATOM   6222  CG2 THR B 457      66.327   9.074-175.454  1.00 30.24           C  
ANISOU 6222  CG2 THR B 457     2996   4856   3637   -429   -433    628       C  
ATOM   6223  N   PRO B 458      61.819   9.993-175.074  1.00 35.72           N  
ANISOU 6223  N   PRO B 458     3210   6080   4281   -374   -473    990       N  
ATOM   6224  CA  PRO B 458      60.605  10.754-174.777  1.00 37.32           C  
ANISOU 6224  CA  PRO B 458     3259   6431   4491   -278   -428   1137       C  
ATOM   6225  C   PRO B 458      60.817  11.848-173.743  1.00 38.43           C  
ANISOU 6225  C   PRO B 458     3443   6452   4706   -126   -281   1181       C  
ATOM   6226  O   PRO B 458      60.021  12.796-173.712  1.00 38.78           O  
ANISOU 6226  O   PRO B 458     3392   6593   4747     12   -213   1312       O  
ATOM   6227  CB  PRO B 458      59.625   9.680-174.272  1.00 38.35           C  
ANISOU 6227  CB  PRO B 458     3281   6669   4622   -428   -504   1144       C  
ATOM   6228  CG  PRO B 458      60.501   8.631-173.679  1.00 39.48           C  
ANISOU 6228  CG  PRO B 458     3566   6635   4801   -558   -528    999       C  
ATOM   6229  CD  PRO B 458      61.737   8.613-174.565  1.00 35.27           C  
ANISOU 6229  CD  PRO B 458     3175   5992   4234   -549   -548    902       C  
ATOM   6230  N   VAL B 459      61.862  11.769-172.910  1.00 39.00           N  
ANISOU 6230  N   VAL B 459     3661   6321   4839   -142   -230   1080       N  
ATOM   6231  CA  VAL B 459      62.032  12.802-171.891  1.00 35.09           C  
ANISOU 6231  CA  VAL B 459     3221   5709   4401    -14    -97   1113       C  
ATOM   6232  C   VAL B 459      62.396  14.150-172.501  1.00 38.26           C  
ANISOU 6232  C   VAL B 459     3670   6073   4796    141    -14   1172       C  
ATOM   6233  O   VAL B 459      62.105  15.188-171.903  1.00 36.46           O  
ANISOU 6233  O   VAL B 459     3456   5801   4594    276    101   1244       O  
ATOM   6234  CB  VAL B 459      63.075  12.391-170.830  1.00 29.10           C  
ANISOU 6234  CB  VAL B 459     2604   4754   3700    -78    -75    990       C  
ATOM   6235  CG1 VAL B 459      62.576  11.184-170.028  1.00 30.37           C  
ANISOU 6235  CG1 VAL B 459     2723   4943   3873   -207   -129    957       C  
ATOM   6236  CG2 VAL B 459      64.420  12.097-171.480  1.00 30.95           C  
ANISOU 6236  CG2 VAL B 459     2951   4879   3929   -132   -118    884       C  
ATOM   6237  N   PHE B 460      62.992  14.170-173.699  1.00 36.57           N  
ANISOU 6237  N   PHE B 460     3487   5870   4539    131    -61   1148       N  
ATOM   6238  CA  PHE B 460      63.344  15.440-174.330  1.00 36.55           C  
ANISOU 6238  CA  PHE B 460     3534   5828   4526    273     22   1213       C  
ATOM   6239  C   PHE B 460      62.114  16.325-174.492  1.00 32.03           C  
ANISOU 6239  C   PHE B 460     2847   5395   3928    424     81   1375       C  
ATOM   6240  O   PHE B 460      62.195  17.554-174.359  1.00 38.68           O  
ANISOU 6240  O   PHE B 460     3748   6159   4789    573    201   1444       O  
ATOM   6241  CB  PHE B 460      64.007  15.162-175.684  1.00 36.30           C  
ANISOU 6241  CB  PHE B 460     3531   5826   4435    232    -47   1176       C  
ATOM   6242  CG  PHE B 460      64.486  16.386-176.394  1.00 35.87           C  
ANISOU 6242  CG  PHE B 460     3539   5721   4370    363     38   1239       C  
ATOM   6243  CD1 PHE B 460      63.627  17.105-177.199  1.00 37.71           C  
ANISOU 6243  CD1 PHE B 460     3686   6097   4543    486     56   1377       C  
ATOM   6244  CD2 PHE B 460      65.805  16.800-176.283  1.00 38.21           C  
ANISOU 6244  CD2 PHE B 460     3974   5833   4711    359    100   1166       C  
ATOM   6245  CE1 PHE B 460      64.060  18.237-177.864  1.00 38.61           C  
ANISOU 6245  CE1 PHE B 460     3869   6156   4645    611    143   1445       C  
ATOM   6246  CE2 PHE B 460      66.248  17.928-176.957  1.00 33.06           C  
ANISOU 6246  CE2 PHE B 460     3382   5128   4050    466    184   1230       C  
ATOM   6247  CZ  PHE B 460      65.374  18.641-177.746  1.00 34.44           C  
ANISOU 6247  CZ  PHE B 460     3488   5431   4166    594    210   1369       C  
ATOM   6248  N   HIS B 461      60.965  15.716-174.775  1.00 37.91           N  
ANISOU 6248  N   HIS B 461     3429   6349   4628    386     -1   1442       N  
ATOM   6249  CA  HIS B 461      59.751  16.434-175.135  1.00 39.18           C  
ANISOU 6249  CA  HIS B 461     3444   6691   4750    528     33   1613       C  
ATOM   6250  C   HIS B 461      58.867  16.707-173.936  1.00 41.29           C  
ANISOU 6250  C   HIS B 461     3642   6980   5065    603    120   1687       C  
ATOM   6251  O   HIS B 461      57.748  17.205-174.093  1.00 41.10           O  
ANISOU 6251  O   HIS B 461     3474   7127   5014    725    153   1840       O  
ATOM   6252  CB  HIS B 461      58.985  15.641-176.184  1.00 42.24           C  
ANISOU 6252  CB  HIS B 461     3676   7320   5054    439   -115   1653       C  
ATOM   6253  CG  HIS B 461      59.848  15.194-177.320  1.00 45.94           C  
ANISOU 6253  CG  HIS B 461     4226   7765   5462    350   -205   1563       C  
ATOM   6254  ND1 HIS B 461      60.265  16.054-178.312  1.00 44.52           N  
ANISOU 6254  ND1 HIS B 461     4099   7580   5237    467   -168   1615       N  
ATOM   6255  CD2 HIS B 461      60.413  13.995-177.598  1.00 47.59           C  
ANISOU 6255  CD2 HIS B 461     4490   7942   5649    168   -316   1426       C  
ATOM   6256  CE1 HIS B 461      61.034  15.400-179.166  1.00 43.36           C  
ANISOU 6256  CE1 HIS B 461     4027   7411   5038    360   -254   1515       C  
ATOM   6257  NE2 HIS B 461      61.133  14.148-178.762  1.00 46.80           N  
ANISOU 6257  NE2 HIS B 461     4468   7829   5485    182   -343   1398       N  
ATOM   6258  N   GLN B 462      59.358  16.408-172.748  1.00 40.94           N  
ANISOU 6258  N   GLN B 462     3698   6773   5084    541    162   1589       N  
ATOM   6259  CA  GLN B 462      58.623  16.572-171.503  1.00 41.24           C  
ANISOU 6259  CA  GLN B 462     3696   6812   5162    600    251   1641       C  
ATOM   6260  C   GLN B 462      59.197  17.770-170.759  1.00 37.51           C  
ANISOU 6260  C   GLN B 462     3393   6129   4729    744    410   1634       C  
ATOM   6261  O   GLN B 462      60.377  17.767-170.387  1.00 40.26           O  
ANISOU 6261  O   GLN B 462     3910   6277   5109    679    420   1507       O  
ATOM   6262  CB  GLN B 462      58.721  15.304-170.650  1.00 36.35           C  
ANISOU 6262  CB  GLN B 462     3077   6163   4572    418    182   1536       C  
ATOM   6263  CG  GLN B 462      58.032  15.410-169.298  1.00 35.44           C  
ANISOU 6263  CG  GLN B 462     2934   6039   4493    471    280   1583       C  
ATOM   6264  CD  GLN B 462      56.550  15.633-169.428  1.00 35.18           C  
ANISOU 6264  CD  GLN B 462     2689   6241   4437    566    306   1756       C  
ATOM   6265  OE1 GLN B 462      55.838  14.794-169.978  1.00 41.03           O  
ANISOU 6265  OE1 GLN B 462     3260   7179   5149    453    191   1795       O  
ATOM   6266  NE2 GLN B 462      56.071  16.769-168.929  1.00 40.72           N  
ANISOU 6266  NE2 GLN B 462     3398   6926   5147    774    459   1863       N  
ATOM   6267  N   GLU B 463      58.382  18.802-170.586  1.00 38.95           N  
ANISOU 6267  N   GLU B 463     3536   6360   4905    940    532   1774       N  
ATOM   6268  CA  GLU B 463      58.747  19.875-169.680  1.00 37.73           C  
ANISOU 6268  CA  GLU B 463     3553   6000   4782   1071    693   1766       C  
ATOM   6269  C   GLU B 463      58.818  19.329-168.254  1.00 39.30           C  
ANISOU 6269  C   GLU B 463     3808   6107   5016    992    718   1681       C  
ATOM   6270  O   GLU B 463      58.071  18.421-167.874  1.00 36.65           O  
ANISOU 6270  O   GLU B 463     3334   5912   4680    916    663   1702       O  
ATOM   6271  CB  GLU B 463      57.734  21.005-169.766  1.00 38.86           C  
ANISOU 6271  CB  GLU B 463     3638   6222   4903   1312    828   1944       C  
ATOM   6272  CG  GLU B 463      57.712  21.652-171.149  1.00 42.73           C  
ANISOU 6272  CG  GLU B 463     4093   6790   5353   1410    816   2039       C  
ATOM   6273  CD  GLU B 463      56.678  22.752-171.267  1.00 50.24           C  
ANISOU 6273  CD  GLU B 463     4981   7829   6279   1668    952   2231       C  
ATOM   6274  OE1 GLU B 463      55.762  22.809-170.417  1.00 61.77           O  
ANISOU 6274  OE1 GLU B 463     6363   9359   7748   1759   1032   2309       O  
ATOM   6275  OE2 GLU B 463      56.792  23.560-172.211  1.00 52.69           O  
ANISOU 6275  OE2 GLU B 463     5322   8139   6559   1787    986   2311       O  
ATOM   6276  N   MET B 464      59.759  19.861-167.480  1.00 37.44           N  
ANISOU 6276  N   MET B 464     3782   5636   4806    997    794   1582       N  
ATOM   6277  CA  MET B 464      60.007  19.371-166.129  1.00 39.25           C  
ANISOU 6277  CA  MET B 464     4094   5761   5057    917    810   1487       C  
ATOM   6278  C   MET B 464      60.197  20.547-165.184  1.00 41.74           C  
ANISOU 6278  C   MET B 464     4597   5887   5375   1052    973   1483       C  
ATOM   6279  O   MET B 464      60.569  21.650-165.592  1.00 41.72           O  
ANISOU 6279  O   MET B 464     4709   5774   5370   1156   1053   1505       O  
ATOM   6280  CB  MET B 464      61.241  18.456-166.082  1.00 35.25           C  
ANISOU 6280  CB  MET B 464     3667   5154   4573    715    688   1325       C  
ATOM   6281  CG  MET B 464      61.077  17.162-166.840  1.00 36.05           C  
ANISOU 6281  CG  MET B 464     3618   5412   4666    568    534   1308       C  
ATOM   6282  SD  MET B 464      62.644  16.308-166.950  1.00 41.46           S  
ANISOU 6282  SD  MET B 464     4421   5960   5374    381    419   1132       S  
ATOM   6283  CE  MET B 464      62.306  15.185-168.315  1.00 44.40           C  
ANISOU 6283  CE  MET B 464     4635   6521   5715    269    267   1145       C  
ATOM   6284  N   VAL B 465      59.963  20.291-163.898  1.00 41.17           N  
ANISOU 6284  N   VAL B 465     4572   5768   5302   1043   1024   1450       N  
ATOM   6285  CA  VAL B 465      60.071  21.304-162.855  1.00 38.18           C  
ANISOU 6285  CA  VAL B 465     4388   5210   4909   1161   1178   1434       C  
ATOM   6286  C   VAL B 465      61.107  20.817-161.853  1.00 42.11           C  
ANISOU 6286  C   VAL B 465     5039   5549   5414   1008   1129   1271       C  
ATOM   6287  O   VAL B 465      60.961  19.723-161.293  1.00 39.84           O  
ANISOU 6287  O   VAL B 465     4678   5332   5128    898   1056   1235       O  
ATOM   6288  CB  VAL B 465      58.726  21.559-162.157  1.00 45.66           C  
ANISOU 6288  CB  VAL B 465     5259   6259   5832   1327   1308   1562       C  
ATOM   6289  CG1 VAL B 465      58.843  22.716-161.183  1.00 41.49           C  
ANISOU 6289  CG1 VAL B 465     4961   5528   5276   1470   1483   1545       C  
ATOM   6290  CG2 VAL B 465      57.628  21.805-163.180  1.00 49.95           C  
ANISOU 6290  CG2 VAL B 465     5595   7016   6369   1462   1326   1738       C  
ATOM   6291  N   ASN B 466      62.147  21.616-161.627  1.00 36.76           N  
ANISOU 6291  N   ASN B 466     4571   4661   4737    996   1167   1180       N  
ATOM   6292  CA  ASN B 466      63.238  21.231-160.739  1.00 37.26           C  
ANISOU 6292  CA  ASN B 466     4776   4581   4800    847   1108   1028       C  
ATOM   6293  C   ASN B 466      63.080  21.937-159.400  1.00 42.30           C  
ANISOU 6293  C   ASN B 466     5598   5079   5395    930   1239   1001       C  
ATOM   6294  O   ASN B 466      62.898  23.157-159.359  1.00 40.96           O  
ANISOU 6294  O   ASN B 466     5560   4800   5205   1069   1374   1040       O  
ATOM   6295  CB  ASN B 466      64.600  21.570-161.346  1.00 39.59           C  
ANISOU 6295  CB  ASN B 466     5172   4748   5122    746   1045    936       C  
ATOM   6296  CG  ASN B 466      65.737  20.838-160.647  1.00 40.99           C  
ANISOU 6296  CG  ASN B 466     5422   4845   5307    568    939    793       C  
ATOM   6297  OD1 ASN B 466      65.491  19.947-159.855  1.00 43.55           O  
ANISOU 6297  OD1 ASN B 466     5708   5223   5618    515    897    766       O  
ATOM   6298  ND2 ASN B 466      66.980  21.197-160.964  1.00 44.03           N  
ANISOU 6298  ND2 ASN B 466     5903   5112   5714    477    895    711       N  
ATOM   6299  N   TYR B 467      63.156  21.173-158.311  1.00 35.47           N  
ANISOU 6299  N   TYR B 467     4759   4211   4508    849   1204    935       N  
ATOM   6300  CA  TYR B 467      63.062  21.756-156.975  1.00 36.78           C  
ANISOU 6300  CA  TYR B 467     5115   4244   4616    915   1320    897       C  
ATOM   6301  C   TYR B 467      63.575  20.738-155.967  1.00 35.34           C  
ANISOU 6301  C   TYR B 467     4961   4053   4414    769   1227    796       C  
ATOM   6302  O   TYR B 467      63.812  19.574-156.299  1.00 34.07           O  
ANISOU 6302  O   TYR B 467     4661   3997   4287    642   1093    777       O  
ATOM   6303  CB  TYR B 467      61.635  22.200-156.634  1.00 35.25           C  
ANISOU 6303  CB  TYR B 467     4876   4130   4390   1119   1481   1032       C  
ATOM   6304  CG  TYR B 467      60.577  21.154-156.872  1.00 43.33           C  
ANISOU 6304  CG  TYR B 467     5639   5390   5432   1122   1440   1139       C  
ATOM   6305  CD1 TYR B 467      60.000  21.008-158.130  1.00 41.41           C  
ANISOU 6305  CD1 TYR B 467     5190   5314   5231   1157   1400   1248       C  
ATOM   6306  CD2 TYR B 467      60.140  20.314-155.837  1.00 47.84           C  
ANISOU 6306  CD2 TYR B 467     6176   6023   5978   1083   1441   1135       C  
ATOM   6307  CE1 TYR B 467      59.036  20.065-158.364  1.00 45.92           C  
ANISOU 6307  CE1 TYR B 467     5525   6106   5817   1137   1353   1343       C  
ATOM   6308  CE2 TYR B 467      59.164  19.353-156.062  1.00 37.03           C  
ANISOU 6308  CE2 TYR B 467     4569   4870   4631   1066   1405   1237       C  
ATOM   6309  CZ  TYR B 467      58.617  19.237-157.343  1.00 44.17           C  
ANISOU 6309  CZ  TYR B 467     5267   5937   5577   1086   1356   1338       C  
ATOM   6310  OH  TYR B 467      57.646  18.303-157.626  1.00 44.68           O  
ANISOU 6310  OH  TYR B 467     5092   6223   5662   1047   1308   1438       O  
ATOM   6311  N   PHE B 468      63.748  21.199-154.728  1.00 38.42           N  
ANISOU 6311  N   PHE B 468     5550   4310   4740    794   1304    732       N  
ATOM   6312  CA  PHE B 468      64.415  20.429-153.686  1.00 44.21           C  
ANISOU 6312  CA  PHE B 468     6356   5004   5437    661   1219    626       C  
ATOM   6313  C   PHE B 468      63.407  19.984-152.635  1.00 39.64           C  
ANISOU 6313  C   PHE B 468     5760   4497   4804    738   1303    681       C  
ATOM   6314  O   PHE B 468      62.816  20.820-151.939  1.00 43.64           O  
ANISOU 6314  O   PHE B 468     6397   4935   5249    881   1458    710       O  
ATOM   6315  CB  PHE B 468      65.526  21.246-153.027  1.00 51.01           C  
ANISOU 6315  CB  PHE B 468     7469   5661   6252    601   1221    497       C  
ATOM   6316  CG  PHE B 468      66.185  20.542-151.862  1.00 59.95           C  
ANISOU 6316  CG  PHE B 468     8687   6760   7330    480   1138    395       C  
ATOM   6317  CD1 PHE B 468      67.315  19.762-152.057  1.00 57.45           C  
ANISOU 6317  CD1 PHE B 468     8323   6458   7049    309    970    316       C  
ATOM   6318  CD2 PHE B 468      65.678  20.666-150.569  1.00 67.90           C  
ANISOU 6318  CD2 PHE B 468     9826   7727   8245    549   1232    386       C  
ATOM   6319  CE1 PHE B 468      67.929  19.120-150.988  1.00 63.79           C  
ANISOU 6319  CE1 PHE B 468     9201   7241   7797    210    891    234       C  
ATOM   6320  CE2 PHE B 468      66.284  20.023-149.496  1.00 60.92           C  
ANISOU 6320  CE2 PHE B 468     9026   6820   7301    443   1152    299       C  
ATOM   6321  CZ  PHE B 468      67.411  19.252-149.707  1.00 57.34           C  
ANISOU 6321  CZ  PHE B 468     8516   6386   6884    275    978    226       C  
ATOM   6322  N   LEU B 469      63.243  18.675-152.504  1.00 35.83           N  
ANISOU 6322  N   LEU B 469     5131   4142   4341    644   1208    694       N  
ATOM   6323  CA  LEU B 469      62.477  18.060-151.433  1.00 36.37           C  
ANISOU 6323  CA  LEU B 469     5183   4275   4359    676   1265    735       C  
ATOM   6324  C   LEU B 469      63.421  17.336-150.480  1.00 41.96           C  
ANISOU 6324  C   LEU B 469     6003   4916   5025    537   1165    621       C  
ATOM   6325  O   LEU B 469      64.523  16.924-150.856  1.00 37.68           O  
ANISOU 6325  O   LEU B 469     5463   4337   4516    401   1023    535       O  
ATOM   6326  CB  LEU B 469      61.448  17.073-151.992  1.00 41.95           C  
ANISOU 6326  CB  LEU B 469     5632   5188   5119    670   1242    856       C  
ATOM   6327  CG  LEU B 469      60.389  17.649-152.940  1.00 42.79           C  
ANISOU 6327  CG  LEU B 469     5587   5410   5262    807   1327    992       C  
ATOM   6328  CD1 LEU B 469      59.500  16.553-153.494  1.00 38.66           C  
ANISOU 6328  CD1 LEU B 469     4803   5098   4788    753   1269   1095       C  
ATOM   6329  CD2 LEU B 469      59.556  18.727-152.250  1.00 42.29           C  
ANISOU 6329  CD2 LEU B 469     5622   5307   5139   1014   1530   1063       C  
ATOM   6330  N   SER B 470      62.985  17.197-149.232  1.00 40.18           N  
ANISOU 6330  N   SER B 470     5867   4678   4720    584   1245    627       N  
ATOM   6331  CA  SER B 470      63.718  16.434-148.246  1.00 38.03           C  
ANISOU 6331  CA  SER B 470     5689   4366   4395    471   1158    541       C  
ATOM   6332  C   SER B 470      62.823  15.310-147.735  1.00 35.73           C  
ANISOU 6332  C   SER B 470     5272   4206   4097    469   1179    628       C  
ATOM   6333  O   SER B 470      61.604  15.496-147.650  1.00 40.63           O  
ANISOU 6333  O   SER B 470     5813   4912   4712    590   1313    741       O  
ATOM   6334  CB  SER B 470      64.150  17.332-147.076  1.00 47.80           C  
ANISOU 6334  CB  SER B 470     7195   5449   5519    515   1230    452       C  
ATOM   6335  OG  SER B 470      64.837  16.591-146.083  1.00 42.80           O  
ANISOU 6335  OG  SER B 470     6648   4792   4821    411   1141    377       O  
ATOM   6336  N   PRO B 471      63.378  14.127-147.392  1.00 33.65           N  
ANISOU 6336  N   PRO B 471     4983   3966   3835    337   1057    589       N  
ATOM   6337  CA  PRO B 471      64.762  13.624-147.406  1.00 33.24           C  
ANISOU 6337  CA  PRO B 471     4991   3849   3790    197    895    478       C  
ATOM   6338  C   PRO B 471      65.456  13.748-148.773  1.00 39.29           C  
ANISOU 6338  C   PRO B 471     5667   4611   4648    131    791    446       C  
ATOM   6339  O   PRO B 471      64.812  13.693-149.820  1.00 34.54           O  
ANISOU 6339  O   PRO B 471     4909   4097   4119    156    805    520       O  
ATOM   6340  CB  PRO B 471      64.605  12.158-147.050  1.00 31.51           C  
ANISOU 6340  CB  PRO B 471     4682   3711   3579    114    830    514       C  
ATOM   6341  CG  PRO B 471      63.347  12.104-146.238  1.00 36.08           C  
ANISOU 6341  CG  PRO B 471     5251   4353   4107    209    976    611       C  
ATOM   6342  CD  PRO B 471      62.444  13.100-146.903  1.00 36.54           C  
ANISOU 6342  CD  PRO B 471     5239   4450   4196    334   1096    683       C  
ATOM   6343  N   ALA B 472      66.779  13.872-148.740  1.00 35.01           N  
ANISOU 6343  N   ALA B 472     5221   3982   4100     45    685    340       N  
ATOM   6344  CA  ALA B 472      67.517  14.255-149.928  1.00 32.65           C  
ANISOU 6344  CA  ALA B 472     4871   3659   3873     -1    613    304       C  
ATOM   6345  C   ALA B 472      68.931  13.713-149.832  1.00 37.63           C  
ANISOU 6345  C   ALA B 472     5536   4252   4509   -126    465    213       C  
ATOM   6346  O   ALA B 472      69.464  13.512-148.734  1.00 30.85           O  
ANISOU 6346  O   ALA B 472     4792   3351   3577   -163    430    159       O  
ATOM   6347  CB  ALA B 472      67.541  15.782-150.086  1.00 31.32           C  
ANISOU 6347  CB  ALA B 472     4821   3392   3687     76    706    283       C  
ATOM   6348  N   PHE B 473      69.508  13.443-150.997  1.00 30.53           N  
ANISOU 6348  N   PHE B 473     4529   3381   3690   -184    380    205       N  
ATOM   6349  CA  PHE B 473      70.949  13.326-151.162  1.00 29.89           C  
ANISOU 6349  CA  PHE B 473     4474   3258   3625   -281    260    124       C  
ATOM   6350  C   PHE B 473      71.482  14.683-151.587  1.00 37.24           C  
ANISOU 6350  C   PHE B 473     5482   4102   4566   -278    289     81       C  
ATOM   6351  O   PHE B 473      70.959  15.287-152.527  1.00 35.09           O  
ANISOU 6351  O   PHE B 473     5157   3837   4340   -221    354    127       O  
ATOM   6352  CB  PHE B 473      71.324  12.272-152.208  1.00 29.74           C  
ANISOU 6352  CB  PHE B 473     4305   3311   3684   -338    165    141       C  
ATOM   6353  CG  PHE B 473      70.965  10.864-151.810  1.00 33.52           C  
ANISOU 6353  CG  PHE B 473     4728   3852   4155   -362    126    174       C  
ATOM   6354  CD1 PHE B 473      71.738  10.176-150.885  1.00 28.56           C  
ANISOU 6354  CD1 PHE B 473     4163   3205   3483   -410     53    134       C  
ATOM   6355  CD2 PHE B 473      69.850  10.240-152.346  1.00 27.15           C  
ANISOU 6355  CD2 PHE B 473     3809   3124   3382   -341    163    250       C  
ATOM   6356  CE1 PHE B 473      71.407   8.874-150.511  1.00 32.08           C  
ANISOU 6356  CE1 PHE B 473     4573   3693   3922   -428     27    172       C  
ATOM   6357  CE2 PHE B 473      69.521   8.941-151.980  1.00 30.06           C  
ANISOU 6357  CE2 PHE B 473     4139   3535   3746   -379    132    281       C  
ATOM   6358  CZ  PHE B 473      70.309   8.261-151.067  1.00 31.16           C  
ANISOU 6358  CZ  PHE B 473     4356   3639   3845   -418     69    242       C  
ATOM   6359  N   ARG B 474      72.521  15.153-150.899  1.00 31.28           N  
ANISOU 6359  N   ARG B 474     4852   3269   3766   -345    238     -3       N  
ATOM   6360  CA  ARG B 474      73.116  16.458-151.138  1.00 33.04           C  
ANISOU 6360  CA  ARG B 474     5175   3389   3988   -369    263    -53       C  
ATOM   6361  C   ARG B 474      74.601  16.296-151.433  1.00 35.09           C  
ANISOU 6361  C   ARG B 474     5403   3648   4282   -494    132   -114       C  
ATOM   6362  O   ARG B 474      75.252  15.379-150.926  1.00 33.04           O  
ANISOU 6362  O   ARG B 474     5111   3439   4004   -554     28   -138       O  
ATOM   6363  CB  ARG B 474      72.945  17.400-149.909  1.00 40.80           C  
ANISOU 6363  CB  ARG B 474     6371   4263   4866   -346    338   -105       C  
ATOM   6364  CG  ARG B 474      71.504  17.547-149.446  1.00 46.17           C  
ANISOU 6364  CG  ARG B 474     7091   4950   5500   -208    481    -40       C  
ATOM   6365  CD  ARG B 474      71.343  18.551-148.313  1.00 68.47           C  
ANISOU 6365  CD  ARG B 474    10149   7653   8214   -170    571    -95       C  
ATOM   6366  NE  ARG B 474      70.619  19.732-148.776  1.00 84.93           N  
ANISOU 6366  NE  ARG B 474    12303   9658  10309    -58    720    -58       N  
ATOM   6367  CZ  ARG B 474      71.170  20.925-148.979  1.00 94.94           C  
ANISOU 6367  CZ  ARG B 474    13713  10790  11570    -88    750   -116       C  
ATOM   6368  NH1 ARG B 474      72.459  21.120-148.734  1.00104.54           N  
ANISOU 6368  NH1 ARG B 474    15007  11944  12770   -241    635   -216       N  
ATOM   6369  NH2 ARG B 474      70.426  21.928-149.420  1.00 94.11           N  
ANISOU 6369  NH2 ARG B 474    13670  10613  11475     36    897    -66       N  
ATOM   6370  N   TYR B 475      75.137  17.196-152.253  1.00 32.18           N  
ANISOU 6370  N   TYR B 475     5040   3224   3961   -527    142   -130       N  
ATOM   6371  CA  TYR B 475      76.586  17.291-152.375  1.00 35.63           C  
ANISOU 6371  CA  TYR B 475     5465   3651   4420   -653     32   -189       C  
ATOM   6372  C   TYR B 475      77.171  17.873-151.091  1.00 35.40           C  
ANISOU 6372  C   TYR B 475     5607   3545   4299   -732     -1   -273       C  
ATOM   6373  O   TYR B 475      76.512  18.620-150.370  1.00 37.06           O  
ANISOU 6373  O   TYR B 475     5977   3666   4436   -686     90   -294       O  
ATOM   6374  CB  TYR B 475      76.995  18.172-153.560  1.00 38.98           C  
ANISOU 6374  CB  TYR B 475     5861   4031   4918   -676     64   -179       C  
ATOM   6375  CG  TYR B 475      76.471  17.668-154.891  1.00 29.14           C  
ANISOU 6375  CG  TYR B 475     4457   2866   3750   -603     90   -100       C  
ATOM   6376  CD1 TYR B 475      76.763  16.388-155.334  1.00 38.70           C  
ANISOU 6376  CD1 TYR B 475     5520   4187   4999   -616      5    -79       C  
ATOM   6377  CD2 TYR B 475      75.702  18.493-155.712  1.00 52.71           C  
ANISOU 6377  CD2 TYR B 475     7453   5814   6762   -520    200    -48       C  
ATOM   6378  CE1 TYR B 475      76.288  15.927-156.553  1.00 47.38           C  
ANISOU 6378  CE1 TYR B 475     6493   5355   6154   -561     23    -17       C  
ATOM   6379  CE2 TYR B 475      75.220  18.040-156.935  1.00 54.70           C  
ANISOU 6379  CE2 TYR B 475     7562   6150   7071   -459    213     23       C  
ATOM   6380  CZ  TYR B 475      75.520  16.758-157.347  1.00 55.85           C  
ANISOU 6380  CZ  TYR B 475     7570   6403   7247   -488    121     32       C  
ATOM   6381  OH  TYR B 475      75.051  16.299-158.559  1.00 70.59           O  
ANISOU 6381  OH  TYR B 475     9313   8351   9157   -439    128     92       O  
ATOM   6382  N   GLN B 476      78.429  17.554-150.827  1.00 34.94           N  
ANISOU 6382  N   GLN B 476     5515   3523   4239   -849   -130   -319       N  
ATOM   6383  CA  GLN B 476      79.126  18.064-149.656  1.00 35.28           C  
ANISOU 6383  CA  GLN B 476     5705   3512   4188   -950   -190   -402       C  
ATOM   6384  C   GLN B 476      80.576  18.293-150.040  1.00 36.88           C  
ANISOU 6384  C   GLN B 476     5838   3738   4436  -1094   -302   -436       C  
ATOM   6385  O   GLN B 476      81.056  17.723-151.023  1.00 43.55           O  
ANISOU 6385  O   GLN B 476     6508   4665   5373  -1096   -344   -390       O  
ATOM   6386  CB  GLN B 476      79.027  17.082-148.477  1.00 36.57           C  
ANISOU 6386  CB  GLN B 476     5889   3743   4264   -933   -254   -409       C  
ATOM   6387  CG  GLN B 476      79.567  15.698-148.771  1.00 35.42           C  
ANISOU 6387  CG  GLN B 476     5561   3729   4168   -935   -360   -364       C  
ATOM   6388  CD  GLN B 476      79.403  14.762-147.577  1.00 41.01           C  
ANISOU 6388  CD  GLN B 476     6307   4490   4783   -908   -409   -360       C  
ATOM   6389  OE1 GLN B 476      79.354  15.211-146.423  1.00 36.10           O  
ANISOU 6389  OE1 GLN B 476     5845   3823   4048   -933   -411   -412       O  
ATOM   6390  NE2 GLN B 476      79.321  13.467-147.844  1.00 35.04           N  
ANISOU 6390  NE2 GLN B 476     5421   3823   4069   -857   -444   -300       N  
ATOM   6391  N   PRO B 477      81.297  19.134-149.304  1.00 43.09           N  
ANISOU 6391  N   PRO B 477     6758   4457   5156  -1220   -350   -515       N  
ATOM   6392  CA  PRO B 477      82.693  19.394-149.670  1.00 46.24           C  
ANISOU 6392  CA  PRO B 477     7074   4892   5602  -1373   -459   -539       C  
ATOM   6393  C   PRO B 477      83.561  18.166-149.450  1.00 48.84           C  
ANISOU 6393  C   PRO B 477     7236   5382   5939  -1402   -603   -515       C  
ATOM   6394  O   PRO B 477      83.245  17.288-148.641  1.00 45.49           O  
ANISOU 6394  O   PRO B 477     6819   5016   5448  -1341   -640   -507       O  
ATOM   6395  CB  PRO B 477      83.106  20.539-148.737  1.00 49.89           C  
ANISOU 6395  CB  PRO B 477     7745   5241   5969  -1508   -479   -637       C  
ATOM   6396  CG  PRO B 477      81.828  21.066-148.162  1.00 52.93           C  
ANISOU 6396  CG  PRO B 477     8336   5501   6275  -1398   -342   -657       C  
ATOM   6397  CD  PRO B 477      80.879  19.927-148.134  1.00 46.66           C  
ANISOU 6397  CD  PRO B 477     7449   4796   5485  -1235   -304   -587       C  
ATOM   6398  N   ASP B 478      84.664  18.111-150.190  1.00 49.33           N  
ANISOU 6398  N   ASP B 478     7146   5516   6082  -1486   -676   -495       N  
ATOM   6399  CA  ASP B 478      85.620  17.036-149.995  1.00 50.84           C  
ANISOU 6399  CA  ASP B 478     7175   5861   6281  -1509   -810   -466       C  
ATOM   6400  C   ASP B 478      86.265  17.180-148.619  1.00 53.81           C  
ANISOU 6400  C   ASP B 478     7640   6265   6540  -1622   -930   -528       C  
ATOM   6401  O   ASP B 478      86.537  18.298-148.171  1.00 59.31           O  
ANISOU 6401  O   ASP B 478     8473   6875   7185  -1753   -941   -600       O  
ATOM   6402  CB  ASP B 478      86.697  17.041-151.080  1.00 50.60           C  
ANISOU 6402  CB  ASP B 478     6961   5907   6360  -1572   -850   -425       C  
ATOM   6403  CG  ASP B 478      86.160  16.618-152.451  1.00 60.09           C  
ANISOU 6403  CG  ASP B 478     8055   7114   7663  -1448   -752   -356       C  
ATOM   6404  OD1 ASP B 478      85.284  15.724-152.516  1.00 62.07           O  
ANISOU 6404  OD1 ASP B 478     8294   7382   7909  -1314   -710   -322       O  
ATOM   6405  OD2 ASP B 478      86.623  17.178-153.463  1.00 65.03           O  
ANISOU 6405  OD2 ASP B 478     8610   7728   8369  -1493   -718   -335       O  
ATOM   6406  N   PRO B 479      86.517  16.074-147.921  1.00 47.40           N  
ANISOU 6406  N   PRO B 479     6765   5568   5677  -1578  -1023   -502       N  
ATOM   6407  CA  PRO B 479      87.035  16.170-146.551  1.00 44.18           C  
ANISOU 6407  CA  PRO B 479     6451   5197   5138  -1673  -1141   -557       C  
ATOM   6408  C   PRO B 479      88.483  16.621-146.458  1.00 53.62           C  
ANISOU 6408  C   PRO B 479     7540   6485   6349  -1809  -1251   -568       C  
ATOM   6409  O   PRO B 479      88.960  16.833-145.339  1.00 62.76           O  
ANISOU 6409  O   PRO B 479     8760   7682   7405  -1869  -1330   -609       O  
ATOM   6410  CB  PRO B 479      86.862  14.742-146.018  1.00 53.04           C  
ANISOU 6410  CB  PRO B 479     7508   6425   6221  -1549  -1188   -498       C  
ATOM   6411  CG  PRO B 479      86.871  13.886-147.249  1.00 49.42           C  
ANISOU 6411  CG  PRO B 479     6860   6022   5894  -1445  -1146   -414       C  
ATOM   6412  CD  PRO B 479      86.221  14.685-148.319  1.00 43.89           C  
ANISOU 6412  CD  PRO B 479     6186   5210   5280  -1432  -1014   -422       C  
ATOM   6413  N   TRP B 480      89.200  16.778-147.567  1.00 58.37           N  
ANISOU 6413  N   TRP B 480     7972   7131   7074  -1839  -1243   -526       N  
ATOM   6414  CA  TRP B 480      90.590  17.243-147.485  1.00 61.15           C  
ANISOU 6414  CA  TRP B 480     8206   7579   7449  -1950  -1325   -526       C  
ATOM   6415  C   TRP B 480      90.731  18.716-147.860  1.00 74.16           C  
ANISOU 6415  C   TRP B 480     9937   9109   9133  -2056  -1251   -577       C  
ATOM   6416  O   TRP B 480      89.742  19.427-148.035  1.00 78.44           O  
ANISOU 6416  O   TRP B 480    10650   9488   9665  -2036  -1138   -616       O  
ATOM   6417  CB  TRP B 480      91.492  16.401-148.378  1.00 52.77           C  
ANISOU 6417  CB  TRP B 480     6889   6670   6493  -1916  -1372   -437       C  
ATOM   6418  CG  TRP B 480      91.092  16.434-149.804  1.00 56.31           C  
ANISOU 6418  CG  TRP B 480     7274   7062   7059  -1867  -1266   -397       C  
ATOM   6419  CD1 TRP B 480      91.496  17.336-150.746  1.00 60.20           C  
ANISOU 6419  CD1 TRP B 480     7719   7512   7641  -1932  -1202   -393       C  
ATOM   6420  CD2 TRP B 480      90.204  15.530-150.469  1.00 53.65           C  
ANISOU 6420  CD2 TRP B 480     6917   6705   6762  -1745  -1214   -351       C  
ATOM   6421  NE1 TRP B 480      90.916  17.050-151.957  1.00 57.20           N  
ANISOU 6421  NE1 TRP B 480     7293   7093   7348  -1853  -1111   -346       N  
ATOM   6422  CE2 TRP B 480      90.118  15.946-151.815  1.00 53.60           C  
ANISOU 6422  CE2 TRP B 480     6850   6651   6865  -1738  -1118   -322       C  
ATOM   6423  CE3 TRP B 480      89.474  14.408-150.062  1.00 50.27           C  
ANISOU 6423  CE3 TRP B 480     6515   6295   6291  -1601  -1208   -325       C  
ATOM   6424  CZ2 TRP B 480      89.335  15.282-152.755  1.00 51.94           C  
ANISOU 6424  CZ2 TRP B 480     6600   6419   6715  -1576  -1015   -273       C  
ATOM   6425  CZ3 TRP B 480      88.696  13.741-151.011  1.00 44.94           C  
ANISOU 6425  CZ3 TRP B 480     5798   5591   5686  -1451  -1102   -276       C  
ATOM   6426  CH2 TRP B 480      88.631  14.186-152.332  1.00 48.82           C  
ANISOU 6426  CH2 TRP B 480     6229   6044   6278  -1442  -1012   -254       C  
ATOM   6427  OXT TRP B 480      91.846  19.224-147.996  1.00 78.16           O  
ANISOU 6427  OXT TRP B 480    10343   9676   9677  -2161  -1302   -574       O  
TER    6428      TRP B 480                                                      
ATOM   6429  N   PHE C  68     105.111 -40.429-222.054  1.00 54.52           N  
ANISOU 6429  N   PHE C  68     9913   4938   5863   1768    -92   -593       N  
ATOM   6430  CA  PHE C  68     105.699 -40.089-220.757  1.00 51.77           C  
ANISOU 6430  CA  PHE C  68     9363   4683   5623   1798    -73   -541       C  
ATOM   6431  C   PHE C  68     106.015 -38.595-220.652  1.00 55.72           C  
ANISOU 6431  C   PHE C  68     9662   5355   6155   1757     16   -513       C  
ATOM   6432  O   PHE C  68     107.011 -38.131-221.211  1.00 53.80           O  
ANISOU 6432  O   PHE C  68     9358   5186   5898   1846    143   -555       O  
ATOM   6433  CB  PHE C  68     106.981 -40.886-220.505  1.00 54.41           C  
ANISOU 6433  CB  PHE C  68     9691   4990   5991   1981    -17   -586       C  
ATOM   6434  CG  PHE C  68     106.757 -42.351-220.288  1.00 66.38           C  
ANISOU 6434  CG  PHE C  68    11386   6336   7499   2029   -117   -601       C  
ATOM   6435  CD1 PHE C  68     107.771 -43.259-220.541  1.00 79.99           C  
ANISOU 6435  CD1 PHE C  68    13185   7990   9217   2210    -70   -669       C  
ATOM   6436  CD2 PHE C  68     105.543 -42.821-219.825  1.00 61.38           C  
ANISOU 6436  CD2 PHE C  68    10845   5611   6864   1893   -256   -548       C  
ATOM   6437  CE1 PHE C  68     107.575 -44.610-220.345  1.00 82.94           C  
ANISOU 6437  CE1 PHE C  68    13693   8238   9585   2222   -169   -668       C  
ATOM   6438  CE2 PHE C  68     105.339 -44.169-219.629  1.00 67.71           C  
ANISOU 6438  CE2 PHE C  68    11823   6248   7656   1926   -351   -558       C  
ATOM   6439  CZ  PHE C  68     106.356 -45.067-219.888  1.00 77.65           C  
ANISOU 6439  CZ  PHE C  68    13130   7466   8908   2081   -310   -614       C  
ATOM   6440  N   PRO C  69     105.190 -37.863-219.901  1.00 50.67           N  
ANISOU 6440  N   PRO C  69     8918   4775   5559   1624    -47   -441       N  
ATOM   6441  CA  PRO C  69     105.348 -36.401-219.819  1.00 52.02           C  
ANISOU 6441  CA  PRO C  69     8918   5093   5755   1571     24   -412       C  
ATOM   6442  C   PRO C  69     106.716 -35.996-219.284  1.00 52.04           C  
ANISOU 6442  C   PRO C  69     8751   5199   5823   1676    125   -418       C  
ATOM   6443  O   PRO C  69     107.203 -36.538-218.287  1.00 49.16           O  
ANISOU 6443  O   PRO C  69     8326   4827   5525   1738     96   -401       O  
ATOM   6444  CB  PRO C  69     104.229 -35.968-218.861  1.00 45.88           C  
ANISOU 6444  CB  PRO C  69     8068   4339   5026   1431    -76   -336       C  
ATOM   6445  CG  PRO C  69     103.324 -37.141-218.710  1.00 55.65           C  
ANISOU 6445  CG  PRO C  69     9455   5443   6248   1386   -195   -325       C  
ATOM   6446  CD  PRO C  69     104.100 -38.372-219.049  1.00 50.54           C  
ANISOU 6446  CD  PRO C  69     8937   4692   5575   1519   -180   -382       C  
ATOM   6447  N   ARG C  70     107.328 -35.022-219.955  1.00 47.37           N  
ANISOU 6447  N   ARG C  70     8084   4705   5210   1690    239   -440       N  
ATOM   6448  CA  ARG C  70     108.566 -34.412-219.488  1.00 50.69           C  
ANISOU 6448  CA  ARG C  70     8318   5243   5697   1762    336   -440       C  
ATOM   6449  C   ARG C  70     108.246 -33.298-218.497  1.00 50.70           C  
ANISOU 6449  C   ARG C  70     8157   5344   5764   1658    303   -372       C  
ATOM   6450  O   ARG C  70     107.373 -32.463-218.746  1.00 48.42           O  
ANISOU 6450  O   ARG C  70     7875   5076   5445   1542    279   -343       O  
ATOM   6451  CB  ARG C  70     109.370 -33.861-220.666  1.00 51.64           C  
ANISOU 6451  CB  ARG C  70     8434   5424   5764   1811    481   -491       C  
ATOM   6452  CG  ARG C  70     110.672 -33.202-220.260  1.00 61.02           C  
ANISOU 6452  CG  ARG C  70     9419   6741   7026   1874    587   -491       C  
ATOM   6453  CD  ARG C  70     111.445 -32.644-221.444  1.00 73.17           C  
ANISOU 6453  CD  ARG C  70    10951   8343   8507   1910    742   -537       C  
ATOM   6454  NE  ARG C  70     111.766 -31.232-221.236  1.00 84.38           N  
ANISOU 6454  NE  ARG C  70    12205   9891   9963   1828    801   -498       N  
ATOM   6455  CZ  ARG C  70     112.622 -30.528-221.973  1.00 84.83           C  
ANISOU 6455  CZ  ARG C  70    12198  10035   9998   1843    945   -520       C  
ATOM   6456  NH1 ARG C  70     113.268 -31.095-222.987  1.00 89.70           N  
ANISOU 6456  NH1 ARG C  70    12895  10634  10554   1943   1056   -586       N  
ATOM   6457  NH2 ARG C  70     112.831 -29.247-221.688  1.00 77.14           N  
ANISOU 6457  NH2 ARG C  70    11083   9165   9061   1754    980   -477       N  
ATOM   6458  N   VAL C  71     108.956 -33.279-217.374  1.00 45.86           N  
ANISOU 6458  N   VAL C  71     7401   4787   5238   1704    298   -348       N  
ATOM   6459  CA  VAL C  71     108.643 -32.380-216.266  1.00 43.30           C  
ANISOU 6459  CA  VAL C  71     6938   4540   4973   1613    252   -285       C  
ATOM   6460  C   VAL C  71     109.912 -31.645-215.868  1.00 39.03           C  
ANISOU 6460  C   VAL C  71     6214   4119   4498   1665    334   -287       C  
ATOM   6461  O   VAL C  71     110.932 -32.276-215.564  1.00 44.09           O  
ANISOU 6461  O   VAL C  71     6804   4765   5185   1783    357   -311       O  
ATOM   6462  CB  VAL C  71     108.048 -33.145-215.074  1.00 59.06           C  
ANISOU 6462  CB  VAL C  71     8960   6475   7007   1592    132   -242       C  
ATOM   6463  CG1 VAL C  71     108.222 -32.368-213.788  1.00 56.67           C  
ANISOU 6463  CG1 VAL C  71     8496   6262   6772   1549    108   -191       C  
ATOM   6464  CG2 VAL C  71     106.587 -33.377-215.330  1.00 72.42           C  
ANISOU 6464  CG2 VAL C  71    10781   8087   8647   1484     51   -221       C  
ATOM   6465  N   LYS C  72     109.853 -30.319-215.867  1.00 34.75           N  
ANISOU 6465  N   LYS C  72     5573   3668   3963   1579    372   -263       N  
ATOM   6466  CA  LYS C  72     111.023 -29.492-215.626  1.00 40.86           C  
ANISOU 6466  CA  LYS C  72     6174   4556   4793   1605    453   -265       C  
ATOM   6467  C   LYS C  72     110.898 -28.690-214.335  1.00 40.68           C  
ANISOU 6467  C   LYS C  72     6023   4599   4834   1533    391   -211       C  
ATOM   6468  O   LYS C  72     109.823 -28.185-213.999  1.00 36.70           O  
ANISOU 6468  O   LYS C  72     5550   4082   4311   1430    329   -174       O  
ATOM   6469  CB  LYS C  72     111.246 -28.547-216.799  1.00 39.56           C  
ANISOU 6469  CB  LYS C  72     6009   4445   4579   1566    564   -285       C  
ATOM   6470  CG  LYS C  72     112.316 -27.503-216.572  1.00 43.32           C  
ANISOU 6470  CG  LYS C  72     6305   5042   5111   1557    645   -278       C  
ATOM   6471  CD  LYS C  72     112.840 -27.027-217.926  1.00 44.01           C  
ANISOU 6471  CD  LYS C  72     6415   5165   5140   1560    782   -312       C  
ATOM   6472  CE  LYS C  72     113.827 -25.882-217.784  1.00 47.81           C  
ANISOU 6472  CE  LYS C  72     6723   5768   5675   1524    867   -299       C  
ATOM   6473  NZ  LYS C  72     114.443 -25.595-219.110  1.00 60.03           N  
ANISOU 6473  NZ  LYS C  72     8297   7349   7163   1538   1015   -334       N  
ATOM   6474  N   ASN C  73     112.020 -28.558-213.635  1.00 38.37           N  
ANISOU 6474  N   ASN C  73     5584   4379   4617   1591    411   -210       N  
ATOM   6475  CA  ASN C  73     112.185 -27.586-212.564  1.00 41.70           C  
ANISOU 6475  CA  ASN C  73     5870   4881   5095   1525    376   -170       C  
ATOM   6476  C   ASN C  73     112.896 -26.356-213.118  1.00 39.34           C  
ANISOU 6476  C   ASN C  73     5461   4679   4806   1484    476   -178       C  
ATOM   6477  O   ASN C  73     114.041 -26.445-213.575  1.00 43.61           O  
ANISOU 6477  O   ASN C  73     5922   5271   5377   1557    563   -210       O  
ATOM   6478  CB  ASN C  73     112.981 -28.173-211.402  1.00 39.65           C  
ANISOU 6478  CB  ASN C  73     5518   4639   4909   1605    317   -160       C  
ATOM   6479  CG  ASN C  73     113.042 -27.220-210.225  1.00 44.31           C  
ANISOU 6479  CG  ASN C  73     5992   5300   5546   1531    264   -118       C  
ATOM   6480  OD1 ASN C  73     113.707 -26.188-210.281  1.00 47.39           O  
ANISOU 6480  OD1 ASN C  73     6260   5779   5968   1495    318   -119       O  
ATOM   6481  ND2 ASN C  73     112.337 -27.555-209.161  1.00 40.03           N  
ANISOU 6481  ND2 ASN C  73     5493   4716   5000   1501    161    -81       N  
ATOM   6482  N   TRP C  74     112.226 -25.216-213.060  1.00 37.12           N  
ANISOU 6482  N   TRP C  74     5176   4424   4505   1367    466   -149       N  
ATOM   6483  CA  TRP C  74     112.710 -23.987-213.677  1.00 43.36           C  
ANISOU 6483  CA  TRP C  74     5897   5288   5292   1307    555   -151       C  
ATOM   6484  C   TRP C  74     113.684 -23.207-212.806  1.00 47.48           C  
ANISOU 6484  C   TRP C  74     6243   5903   5894   1288    558   -135       C  
ATOM   6485  O   TRP C  74     114.352 -22.301-213.313  1.00 45.83           O  
ANISOU 6485  O   TRP C  74     5959   5762   5695   1247    642   -139       O  
ATOM   6486  CB  TRP C  74     111.512 -23.110-214.060  1.00 41.80           C  
ANISOU 6486  CB  TRP C  74     5789   5061   5034   1195    533   -127       C  
ATOM   6487  CG  TRP C  74     110.813 -23.717-215.226  1.00 40.29           C  
ANISOU 6487  CG  TRP C  74     5756   4793   4760   1210    552   -150       C  
ATOM   6488  CD1 TRP C  74     109.828 -24.657-215.186  1.00 38.27           C  
ANISOU 6488  CD1 TRP C  74     5620   4449   4472   1224    475   -150       C  
ATOM   6489  CD2 TRP C  74     111.095 -23.487-216.609  1.00 45.49           C  
ANISOU 6489  CD2 TRP C  74     6477   5452   5355   1212    654   -177       C  
ATOM   6490  NE1 TRP C  74     109.461 -25.012-216.462  1.00 44.93           N  
ANISOU 6490  NE1 TRP C  74     6599   5237   5237   1234    513   -178       N  
ATOM   6491  CE2 TRP C  74     110.227 -24.310-217.353  1.00 44.88           C  
ANISOU 6491  CE2 TRP C  74     6565   5283   5205   1230    625   -195       C  
ATOM   6492  CE3 TRP C  74     111.995 -22.662-217.290  1.00 48.09           C  
ANISOU 6492  CE3 TRP C  74     6743   5851   5678   1192    769   -185       C  
ATOM   6493  CZ2 TRP C  74     110.223 -24.322-218.747  1.00 49.57           C  
ANISOU 6493  CZ2 TRP C  74     7271   5850   5713   1234    701   -224       C  
ATOM   6494  CZ3 TRP C  74     111.983 -22.668-218.670  1.00 53.43           C  
ANISOU 6494  CZ3 TRP C  74     7529   6503   6267   1194    854   -210       C  
ATOM   6495  CH2 TRP C  74     111.107 -23.497-219.384  1.00 54.02           C  
ANISOU 6495  CH2 TRP C  74     7777   6485   6265   1219    818   -231       C  
ATOM   6496  N   GLU C  75     113.786 -23.535-211.517  1.00 44.31           N  
ANISOU 6496  N   GLU C  75     5782   5507   5547   1311    465   -116       N  
ATOM   6497  CA  GLU C  75     114.806 -22.924-210.674  1.00 49.19           C  
ANISOU 6497  CA  GLU C  75     6235   6212   6243   1303    455   -105       C  
ATOM   6498  C   GLU C  75     116.162 -23.578-210.897  1.00 53.50           C  
ANISOU 6498  C   GLU C  75     6674   6805   6849   1414    512   -137       C  
ATOM   6499  O   GLU C  75     117.190 -22.894-210.929  1.00 53.71           O  
ANISOU 6499  O   GLU C  75     6556   6920   6932   1399    568   -141       O  
ATOM   6500  CB  GLU C  75     114.407 -23.020-209.196  1.00 45.92           C  
ANISOU 6500  CB  GLU C  75     5809   5785   5855   1286    330    -72       C  
ATOM   6501  CG  GLU C  75     115.431 -22.413-208.226  1.00 50.73           C  
ANISOU 6501  CG  GLU C  75     6257   6476   6540   1275    297    -61       C  
ATOM   6502  CD  GLU C  75     115.096 -22.653-206.747  1.00 55.59           C  
ANISOU 6502  CD  GLU C  75     6879   7074   7169   1272    170    -31       C  
ATOM   6503  OE1 GLU C  75     113.960 -23.078-206.442  1.00 52.23           O  
ANISOU 6503  OE1 GLU C  75     6576   6579   6691   1255    117    -14       O  
ATOM   6504  OE2 GLU C  75     115.981 -22.422-205.885  1.00 59.34           O  
ANISOU 6504  OE2 GLU C  75     7235   7606   7705   1283    122    -24       O  
ATOM   6505  N   VAL C  76     116.175 -24.897-211.068  1.00 47.28           N  
ANISOU 6505  N   VAL C  76     5954   5956   6053   1527    500   -160       N  
ATOM   6506  CA  VAL C  76     117.414 -25.648-211.192  1.00 53.13           C  
ANISOU 6506  CA  VAL C  76     6598   6733   6857   1656    543   -193       C  
ATOM   6507  C   VAL C  76     117.696 -26.090-212.622  1.00 51.86           C  
ANISOU 6507  C   VAL C  76     6492   6558   6653   1721    672   -241       C  
ATOM   6508  O   VAL C  76     118.868 -26.313-212.958  1.00 56.36           O  
ANISOU 6508  O   VAL C  76     6946   7191   7277   1808    752   -274       O  
ATOM   6509  CB  VAL C  76     117.408 -26.866-210.244  1.00 54.63           C  
ANISOU 6509  CB  VAL C  76     6818   6862   7077   1757    430   -187       C  
ATOM   6510  CG1 VAL C  76     118.764 -27.551-210.213  1.00 65.23           C  
ANISOU 6510  CG1 VAL C  76     8036   8248   8501   1899    458   -220       C  
ATOM   6511  CG2 VAL C  76     116.991 -26.423-208.848  1.00 48.43           C  
ANISOU 6511  CG2 VAL C  76     6008   6083   6311   1683    306   -138       C  
ATOM   6512  N   GLY C  77     116.676 -26.194-213.481  1.00 50.28           N  
ANISOU 6512  N   GLY C  77     6464   6284   6358   1681    694   -248       N  
ATOM   6513  CA  GLY C  77     116.842 -26.688-214.834  1.00 44.44           C  
ANISOU 6513  CA  GLY C  77     5810   5517   5559   1743    807   -296       C  
ATOM   6514  C   GLY C  77     116.790 -28.196-214.975  1.00 51.91           C  
ANISOU 6514  C   GLY C  77     6863   6371   6491   1877    778   -332       C  
ATOM   6515  O   GLY C  77     116.970 -28.704-216.087  1.00 58.28           O  
ANISOU 6515  O   GLY C  77     7752   7147   7243   1943    870   -380       O  
ATOM   6516  N   SER C  78     116.545 -28.927-213.894  1.00 48.16           N  
ANISOU 6516  N   SER C  78     6401   5843   6054   1918    652   -311       N  
ATOM   6517  CA  SER C  78     116.544 -30.376-213.978  1.00 56.36           C  
ANISOU 6517  CA  SER C  78     7548   6784   7082   2047    616   -343       C  
ATOM   6518  C   SER C  78     115.276 -30.884-214.661  1.00 54.66           C  
ANISOU 6518  C   SER C  78     7553   6450   6764   2004    588   -349       C  
ATOM   6519  O   SER C  78     114.216 -30.248-214.637  1.00 52.51           O  
ANISOU 6519  O   SER C  78     7343   6162   6445   1875    548   -313       O  
ATOM   6520  CB  SER C  78     116.677 -30.992-212.585  1.00 48.88           C  
ANISOU 6520  CB  SER C  78     6559   5811   6202   2096    485   -311       C  
ATOM   6521  OG  SER C  78     115.813 -30.344-211.682  1.00 45.34           O  
ANISOU 6521  OG  SER C  78     6116   5366   5747   1967    392   -252       O  
ATOM   6522  N   ILE C  79     115.400 -32.063-215.257  1.00 45.97           N  
ANISOU 6522  N   ILE C  79     6569   5263   5632   2120    605   -396       N  
ATOM   6523  CA  ILE C  79     114.345 -32.703-216.030  1.00 52.17           C  
ANISOU 6523  CA  ILE C  79     7573   5929   6322   2096    580   -414       C  
ATOM   6524  C   ILE C  79     114.124 -34.111-215.493  1.00 54.24           C  
ANISOU 6524  C   ILE C  79     7946   6070   6592   2184    476   -418       C  
ATOM   6525  O   ILE C  79     115.087 -34.839-215.230  1.00 57.23           O  
ANISOU 6525  O   ILE C  79     8274   6444   7026   2326    484   -447       O  
ATOM   6526  CB  ILE C  79     114.720 -32.758-217.526  1.00 56.17           C  
ANISOU 6526  CB  ILE C  79     8150   6435   6757   2148    717   -478       C  
ATOM   6527  CG1 ILE C  79     114.875 -31.345-218.095  1.00 59.81           C  
ANISOU 6527  CG1 ILE C  79     8522   7006   7198   2047    818   -466       C  
ATOM   6528  CG2 ILE C  79     113.697 -33.550-218.306  1.00 52.50           C  
ANISOU 6528  CG2 ILE C  79     7921   5834   6191   2136    676   -502       C  
ATOM   6529  CD1 ILE C  79     113.579 -30.651-218.311  1.00 54.84           C  
ANISOU 6529  CD1 ILE C  79     7991   6346   6501   1894    763   -427       C  
ATOM   6530  N   THR C  80     112.860 -34.495-215.324  1.00 48.56           N  
ANISOU 6530  N   THR C  80     7377   5251   5822   2099    375   -388       N  
ATOM   6531  CA  THR C  80     112.484 -35.886-215.093  1.00 50.95           C  
ANISOU 6531  CA  THR C  80     7835   5414   6109   2163    283   -396       C  
ATOM   6532  C   THR C  80     111.356 -36.245-216.053  1.00 53.52           C  
ANISOU 6532  C   THR C  80     8362   5636   6336   2094    264   -413       C  
ATOM   6533  O   THR C  80     110.772 -35.380-216.710  1.00 48.13           O  
ANISOU 6533  O   THR C  80     7690   4993   5604   1989    302   -408       O  
ATOM   6534  CB  THR C  80     112.036 -36.153-213.640  1.00 52.29           C  
ANISOU 6534  CB  THR C  80     7985   5557   6327   2117    151   -328       C  
ATOM   6535  OG1 THR C  80     110.845 -35.407-213.351  1.00 54.29           O  
ANISOU 6535  OG1 THR C  80     8250   5827   6552   1949    103   -275       O  
ATOM   6536  CG2 THR C  80     113.121 -35.758-212.636  1.00 52.89           C  
ANISOU 6536  CG2 THR C  80     7866   5734   6496   2177    151   -308       C  
ATOM   6537  N   TYR C  81     111.042 -37.534-216.128  1.00 48.08           N  
ANISOU 6537  N   TYR C  81     7840   4808   5620   2151    195   -432       N  
ATOM   6538  CA  TYR C  81     109.918 -38.024-216.911  1.00 52.86           C  
ANISOU 6538  CA  TYR C  81     8649   5299   6137   2079    149   -445       C  
ATOM   6539  C   TYR C  81     109.002 -38.808-215.985  1.00 50.58           C  
ANISOU 6539  C   TYR C  81     8451   4908   5861   2014      5   -392       C  
ATOM   6540  O   TYR C  81     109.458 -39.711-215.281  1.00 48.35           O  
ANISOU 6540  O   TYR C  81     8190   4562   5618   2105    -48   -387       O  
ATOM   6541  CB  TYR C  81     110.393 -38.893-218.089  1.00 55.72           C  
ANISOU 6541  CB  TYR C  81     9159   5574   6437   2205    211   -530       C  
ATOM   6542  CG  TYR C  81     111.132 -38.094-219.149  1.00 61.19           C  
ANISOU 6542  CG  TYR C  81     9786   6366   7096   2245    364   -581       C  
ATOM   6543  CD1 TYR C  81     112.499 -37.872-219.050  1.00 61.85           C  
ANISOU 6543  CD1 TYR C  81     9711   6548   7241   2370    470   -610       C  
ATOM   6544  CD2 TYR C  81     110.458 -37.546-220.237  1.00 60.86           C  
ANISOU 6544  CD2 TYR C  81     9838   6324   6962   2153    401   -596       C  
ATOM   6545  CE1 TYR C  81     113.177 -37.129-220.001  1.00 61.17           C  
ANISOU 6545  CE1 TYR C  81     9560   6558   7124   2395    620   -652       C  
ATOM   6546  CE2 TYR C  81     111.134 -36.802-221.199  1.00 62.20           C  
ANISOU 6546  CE2 TYR C  81     9959   6583   7092   2182    546   -637       C  
ATOM   6547  CZ  TYR C  81     112.492 -36.600-221.073  1.00 64.45           C  
ANISOU 6547  CZ  TYR C  81    10085   6965   7438   2300    661   -664       C  
ATOM   6548  OH  TYR C  81     113.174 -35.865-222.013  1.00 71.78           O  
ANISOU 6548  OH  TYR C  81    10960   7986   8327   2318    814   -700       O  
ATOM   6549  N   ASP C  82     107.721 -38.453-215.968  1.00 47.27           N  
ANISOU 6549  N   ASP C  82     8081   4472   5408   1857    -58   -349       N  
ATOM   6550  CA  ASP C  82     106.765 -39.165-215.128  1.00 49.47           C  
ANISOU 6550  CA  ASP C  82     8443   4659   5695   1775   -184   -294       C  
ATOM   6551  C   ASP C  82     106.286 -40.398-215.883  1.00 57.39           C  
ANISOU 6551  C   ASP C  82     9673   5499   6635   1794   -239   -333       C  
ATOM   6552  O   ASP C  82     105.471 -40.304-216.803  1.00 64.93           O  
ANISOU 6552  O   ASP C  82    10730   6416   7526   1713   -250   -351       O  
ATOM   6553  CB  ASP C  82     105.604 -38.260-214.726  1.00 52.67           C  
ANISOU 6553  CB  ASP C  82     8785   5126   6102   1602   -225   -233       C  
ATOM   6554  CG  ASP C  82     104.720 -38.895-213.647  1.00 61.30           C  
ANISOU 6554  CG  ASP C  82     9926   6152   7215   1514   -338   -167       C  
ATOM   6555  OD1 ASP C  82     104.238 -40.025-213.867  1.00 66.96           O  
ANISOU 6555  OD1 ASP C  82    10811   6732   7900   1506   -409   -173       O  
ATOM   6556  OD2 ASP C  82     104.528 -38.286-212.576  1.00 59.19           O  
ANISOU 6556  OD2 ASP C  82     9536   5964   6992   1451   -355   -109       O  
ATOM   6557  N   THR C  83     106.797 -41.567-215.493  1.00 55.67           N  
ANISOU 6557  N   THR C  83     9541   5178   6433   1902   -283   -345       N  
ATOM   6558  CA  THR C  83     106.316 -42.818-216.061  1.00 55.80           C  
ANISOU 6558  CA  THR C  83     9787   5021   6393   1914   -352   -377       C  
ATOM   6559  C   THR C  83     105.163 -43.408-215.270  1.00 56.75           C  
ANISOU 6559  C   THR C  83     9995   5050   6517   1778   -483   -306       C  
ATOM   6560  O   THR C  83     104.448 -44.266-215.797  1.00 58.00           O  
ANISOU 6560  O   THR C  83    10343   5070   6624   1732   -554   -322       O  
ATOM   6561  CB  THR C  83     107.447 -43.847-216.138  1.00 55.99           C  
ANISOU 6561  CB  THR C  83     9885   4961   6429   2110   -335   -433       C  
ATOM   6562  OG1 THR C  83     108.002 -44.040-214.833  1.00 56.95           O  
ANISOU 6562  OG1 THR C  83     9906   5105   6628   2164   -376   -383       O  
ATOM   6563  CG2 THR C  83     108.529 -43.366-217.079  1.00 56.54           C  
ANISOU 6563  CG2 THR C  83     9883   5113   6485   2243   -193   -511       C  
ATOM   6564  N   LEU C  84     104.963 -42.957-214.025  1.00 53.69           N  
ANISOU 6564  N   LEU C  84     9475   4738   6186   1707   -515   -230       N  
ATOM   6565  CA  LEU C  84     103.883 -43.477-213.192  1.00 50.34           C  
ANISOU 6565  CA  LEU C  84     9120   4240   5765   1571   -625   -157       C  
ATOM   6566  C   LEU C  84     102.510 -43.057-213.704  1.00 50.30           C  
ANISOU 6566  C   LEU C  84     9144   4241   5725   1395   -656   -137       C  
ATOM   6567  O   LEU C  84     101.531 -43.787-213.508  1.00 49.47           O  
ANISOU 6567  O   LEU C  84     9158   4034   5605   1285   -749   -101       O  
ATOM   6568  CB  LEU C  84     104.071 -43.008-211.748  1.00 51.91           C  
ANISOU 6568  CB  LEU C  84     9167   4533   6025   1546   -636    -84       C  
ATOM   6569  CG  LEU C  84     103.056 -43.469-210.700  1.00 48.72           C  
ANISOU 6569  CG  LEU C  84     8813   4073   5624   1407   -732      1       C  
ATOM   6570  CD1 LEU C  84     103.043 -44.995-210.605  1.00 53.29           C  
ANISOU 6570  CD1 LEU C  84     9600   4467   6183   1446   -821      3       C  
ATOM   6571  CD2 LEU C  84     103.361 -42.839-209.347  1.00 44.09           C  
ANISOU 6571  CD2 LEU C  84     8070   3596   5084   1395   -725     62       C  
ATOM   6572  N   SER C  85     102.414 -41.892-214.354  1.00 49.09           N  
ANISOU 6572  N   SER C  85     8883   4205   5563   1364   -584   -159       N  
ATOM   6573  CA  SER C  85     101.122 -41.410-214.838  1.00 45.12           C  
ANISOU 6573  CA  SER C  85     8393   3717   5034   1206   -620   -140       C  
ATOM   6574  C   SER C  85     100.475 -42.378-215.822  1.00 57.18           C  
ANISOU 6574  C   SER C  85    10132   5094   6498   1170   -691   -176       C  
ATOM   6575  O   SER C  85      99.250 -42.349-215.984  1.00 55.57           O  
ANISOU 6575  O   SER C  85     9964   4868   6284   1022   -761   -146       O  
ATOM   6576  CB  SER C  85     101.276 -40.029-215.485  1.00 50.37           C  
ANISOU 6576  CB  SER C  85     8929   4518   5691   1203   -532   -163       C  
ATOM   6577  OG  SER C  85     102.103 -40.080-216.640  1.00 58.39           O  
ANISOU 6577  OG  SER C  85    10011   5515   6658   1319   -460   -241       O  
ATOM   6578  N   ALA C  86     101.266 -43.243-216.466  1.00 60.37           N  
ANISOU 6578  N   ALA C  86    10679   5395   6865   1303   -676   -242       N  
ATOM   6579  CA  ALA C  86     100.713 -44.232-217.389  1.00 68.45           C  
ANISOU 6579  CA  ALA C  86    11925   6260   7821   1277   -749   -284       C  
ATOM   6580  C   ALA C  86      99.739 -45.184-216.702  1.00 76.17           C  
ANISOU 6580  C   ALA C  86    13007   7121   8814   1153   -876   -224       C  
ATOM   6581  O   ALA C  86      98.819 -45.697-217.348  1.00 81.91           O  
ANISOU 6581  O   ALA C  86    13878   7747   9498   1052   -959   -234       O  
ATOM   6582  CB  ALA C  86     101.842 -45.026-218.047  1.00 61.79           C  
ANISOU 6582  CB  ALA C  86    11213   5325   6938   1463   -703   -367       C  
ATOM   6583  N   GLN C  87      99.917 -45.432-215.402  1.00 70.79           N  
ANISOU 6583  N   GLN C  87    12258   6449   8189   1152   -896   -161       N  
ATOM   6584  CA  GLN C  87      99.071 -46.349-214.651  1.00 63.31           C  
ANISOU 6584  CA  GLN C  87    11409   5392   7254   1033  -1006    -96       C  
ATOM   6585  C   GLN C  87      97.896 -45.663-213.972  1.00 68.57           C  
ANISOU 6585  C   GLN C  87    11942   6154   7957    845  -1033    -16       C  
ATOM   6586  O   GLN C  87      97.299 -46.247-213.059  1.00 72.85           O  
ANISOU 6586  O   GLN C  87    12515   6642   8520    744  -1100     54       O  
ATOM   6587  CB  GLN C  87      99.893 -47.088-213.596  1.00 73.44           C  
ANISOU 6587  CB  GLN C  87    12717   6618   8568   1134  -1020    -67       C  
ATOM   6588  CG  GLN C  87     100.824 -48.127-214.169  1.00 86.01           C  
ANISOU 6588  CG  GLN C  87    14456   8098  10126   1293  -1021   -139       C  
ATOM   6589  CD  GLN C  87     102.234 -47.956-213.666  1.00 89.26           C  
ANISOU 6589  CD  GLN C  87    14759   8578  10576   1478   -947   -158       C  
ATOM   6590  OE1 GLN C  87     102.546 -48.307-212.528  1.00 88.61           O  
ANISOU 6590  OE1 GLN C  87    14643   8493  10533   1497   -980   -103       O  
ATOM   6591  NE2 GLN C  87     103.098 -47.402-214.510  1.00 89.91           N  
ANISOU 6591  NE2 GLN C  87    14784   8728  10648   1611   -848   -234       N  
ATOM   6592  N   ALA C  88      97.565 -44.437-214.371  1.00 57.10           N  
ANISOU 6592  N   ALA C  88    10344   4840   6511    799   -980    -22       N  
ATOM   6593  CA  ALA C  88      96.434 -43.749-213.768  1.00 59.55           C  
ANISOU 6593  CA  ALA C  88    10523   5244   6861    633  -1001     47       C  
ATOM   6594  C   ALA C  88      95.156 -44.517-214.063  1.00 72.79           C  
ANISOU 6594  C   ALA C  88    12322   6812   8523    474  -1111     72       C  
ATOM   6595  O   ALA C  88      94.846 -44.808-215.223  1.00 73.25           O  
ANISOU 6595  O   ALA C  88    12503   6794   8536    460  -1154     20       O  
ATOM   6596  CB  ALA C  88      96.343 -42.314-214.289  1.00 54.13           C  
ANISOU 6596  CB  ALA C  88     9679   4709   6180    629   -931     26       C  
ATOM   6597  N   GLN C  89      94.428 -44.866-213.005  1.00 85.71           N  
ANISOU 6597  N   GLN C  89    13930   8440  10195    350  -1156    151       N  
ATOM   6598  CA  GLN C  89      93.212 -45.656-213.138  1.00 94.08           C  
ANISOU 6598  CA  GLN C  89    15096   9399  11253    182  -1261    185       C  
ATOM   6599  C   GLN C  89      92.093 -44.811-213.726  1.00 98.77           C  
ANISOU 6599  C   GLN C  89    15582  10082  11863     57  -1279    188       C  
ATOM   6600  O   GLN C  89      91.921 -44.755-214.950  1.00104.41           O  
ANISOU 6600  O   GLN C  89    16373  10759  12540     64  -1313    129       O  
ATOM   6601  CB  GLN C  89      92.793 -46.227-211.779  1.00 95.58           C  
ANISOU 6601  CB  GLN C  89    15277   9566  11475     82  -1289    275       C  
ATOM   6602  CG  GLN C  89      93.839 -46.084-210.668  1.00 98.20           C  
ANISOU 6602  CG  GLN C  89    15544   9947  11820    200  -1222    301       C  
ATOM   6603  CD  GLN C  89      94.964 -47.114-210.745  1.00 99.17           C  
ANISOU 6603  CD  GLN C  89    15840   9928  11911    352  -1243    266       C  
ATOM   6604  OE1 GLN C  89      95.828 -47.170-209.866  1.00 92.29           O  
ANISOU 6604  OE1 GLN C  89    14940   9075  11051    451  -1211    287       O  
ATOM   6605  NE2 GLN C  89      94.955 -47.932-211.791  1.00103.49           N  
ANISOU 6605  NE2 GLN C  89    16573  10331  12418    375  -1303    209       N  
ATOM   6606  N   GLN C  90      91.338 -44.140-212.862  1.00 92.78           N  
ANISOU 6606  N   GLN C  90    14649   9443  11158    -52  -1258    254       N  
ATOM   6607  CA  GLN C  90      90.171 -43.398-213.304  1.00 88.12           C  
ANISOU 6607  CA  GLN C  90    13947   8936  10597   -176  -1286    264       C  
ATOM   6608  C   GLN C  90      90.603 -42.186-214.125  1.00 87.81           C  
ANISOU 6608  C   GLN C  90    13819   9001  10544    -76  -1225    206       C  
ATOM   6609  O   GLN C  90      91.792 -41.895-214.295  1.00 89.25           O  
ANISOU 6609  O   GLN C  90    14011   9201  10698     77  -1152    162       O  
ATOM   6610  CB  GLN C  90      89.315 -42.986-212.109  1.00 85.88           C  
ANISOU 6610  CB  GLN C  90    13496   8760  10375   -302  -1264    346       C  
ATOM   6611  CG  GLN C  90      89.058 -44.106-211.093  1.00 91.12           C  
ANISOU 6611  CG  GLN C  90    14240   9335  11046   -392  -1299    414       C  
ATOM   6612  CD  GLN C  90      88.256 -45.279-211.651  1.00 95.31           C  
ANISOU 6612  CD  GLN C  90    14936   9713  11565   -522  -1419    422       C  
ATOM   6613  OE1 GLN C  90      87.589 -45.167-212.682  1.00 93.60           O  
ANISOU 6613  OE1 GLN C  90    14735   9481  11348   -582  -1483    388       O  
ATOM   6614  NE2 GLN C  90      88.318 -46.413-210.961  1.00 97.73           N  
ANISOU 6614  NE2 GLN C  90    15371   9901  11860   -570  -1456    468       N  
ATOM   6615  N   ASP C  91      89.619 -41.471-214.648  1.00 77.93           N  
ANISOU 6615  N   ASP C  91    12478   7819   9315   -168  -1258    208       N  
ATOM   6616  CA  ASP C  91      89.867 -40.357-215.545  1.00 68.23           C  
ANISOU 6616  CA  ASP C  91    11188   6671   8066    -94  -1219    158       C  
ATOM   6617  C   ASP C  91      89.542 -39.049-214.844  1.00 66.62           C  
ANISOU 6617  C   ASP C  91    10759   6633   7919   -112  -1153    194       C  
ATOM   6618  O   ASP C  91      88.490 -38.922-214.209  1.00 75.12           O  
ANISOU 6618  O   ASP C  91    11728   7763   9053   -235  -1181    248       O  
ATOM   6619  CB  ASP C  91      89.049 -40.504-216.827  1.00 68.30           C  
ANISOU 6619  CB  ASP C  91    11289   6617   8044   -166  -1322    125       C  
ATOM   6620  CG  ASP C  91      89.649 -41.510-217.778  1.00 64.40           C  
ANISOU 6620  CG  ASP C  91    11029   5968   7470   -102  -1364     63       C  
ATOM   6621  OD1 ASP C  91      90.721 -42.069-217.458  1.00 74.49           O  
ANISOU 6621  OD1 ASP C  91    12388   7192   8723     10  -1309     45       O  
ATOM   6622  OD2 ASP C  91      89.054 -41.743-218.847  1.00 73.49           O  
ANISOU 6622  OD2 ASP C  91    12288   7052   8584   -157  -1455     31       O  
ATOM   6623  N   GLY C  92      90.457 -38.089-214.954  1.00 48.65           N  
ANISOU 6623  N   GLY C  92     8416   4440   5630     10  -1063    163       N  
ATOM   6624  CA  GLY C  92      90.225 -36.759-214.451  1.00 40.62           C  
ANISOU 6624  CA  GLY C  92     7206   3570   4658      7  -1003    186       C  
ATOM   6625  C   GLY C  92      89.392 -35.929-215.412  1.00 42.15           C  
ANISOU 6625  C   GLY C  92     7354   3806   4855    -39  -1049    168       C  
ATOM   6626  O   GLY C  92      88.897 -36.399-216.438  1.00 46.02           O  
ANISOU 6626  O   GLY C  92     7956   4215   5312    -83  -1136    143       O  
ATOM   6627  N   PRO C  93      89.220 -34.655-215.059  1.00 43.54           N  
ANISOU 6627  N   PRO C  93     7367   4107   5068    -28   -997    181       N  
ATOM   6628  CA  PRO C  93      88.268 -33.794-215.776  1.00 45.14           C  
ANISOU 6628  CA  PRO C  93     7501   4360   5289    -78  -1050    177       C  
ATOM   6629  C   PRO C  93      88.804 -33.103-217.019  1.00 40.23           C  
ANISOU 6629  C   PRO C  93     6945   3732   4607      3  -1042    125       C  
ATOM   6630  O   PRO C  93      88.022 -32.456-217.730  1.00 42.09           O  
ANISOU 6630  O   PRO C  93     7151   3992   4848    -35  -1103    120       O  
ATOM   6631  CB  PRO C  93      87.914 -32.757-214.710  1.00 48.01           C  
ANISOU 6631  CB  PRO C  93     7667   4854   5719    -90   -989    214       C  
ATOM   6632  CG  PRO C  93      89.208 -32.610-213.929  1.00 45.82           C  
ANISOU 6632  CG  PRO C  93     7379   4604   5425     11   -882    210       C  
ATOM   6633  CD  PRO C  93      89.817 -33.985-213.892  1.00 41.30           C  
ANISOU 6633  CD  PRO C  93     6956   3921   4816     26   -898    205       C  
ATOM   6634  N   CYS C  94      90.094 -33.198-217.303  1.00 42.92           N  
ANISOU 6634  N   CYS C  94     7371   4044   4891    113   -970     87       N  
ATOM   6635  CA  CYS C  94      90.679 -32.424-218.386  1.00 42.82           C  
ANISOU 6635  CA  CYS C  94     7408   4042   4818    188   -938     43       C  
ATOM   6636  C   CYS C  94      90.546 -33.158-219.715  1.00 42.72           C  
ANISOU 6636  C   CYS C  94     7585   3918   4729    179  -1014      1       C  
ATOM   6637  O   CYS C  94      90.430 -34.382-219.767  1.00 40.68           O  
ANISOU 6637  O   CYS C  94     7442   3560   4454    150  -1068     -6       O  
ATOM   6638  CB  CYS C  94      92.152 -32.133-218.104  1.00 41.03           C  
ANISOU 6638  CB  CYS C  94     7171   3849   4569    307   -816     21       C  
ATOM   6639  SG  CYS C  94      92.475 -31.035-216.699  1.00 37.56           S  
ANISOU 6639  SG  CYS C  94     6526   3544   4203    329   -726     60       S  
ATOM   6640  N   THR C  95      90.543 -32.395-220.795  1.00 38.95           N  
ANISOU 6640  N   THR C  95     7150   3450   4198    202  -1024    -27       N  
ATOM   6641  CA  THR C  95      90.594 -32.927-222.150  1.00 42.19           C  
ANISOU 6641  CA  THR C  95     7755   3760   4513    212  -1079    -75       C  
ATOM   6642  C   THR C  95      91.601 -32.119-222.954  1.00 36.69           C  
ANISOU 6642  C   THR C  95     7107   3093   3741    310   -986   -113       C  
ATOM   6643  O   THR C  95      92.066 -31.062-222.511  1.00 37.30           O  
ANISOU 6643  O   THR C  95     7057   3268   3849    351   -899    -96       O  
ATOM   6644  CB  THR C  95      89.217 -32.895-222.854  1.00 49.51           C  
ANISOU 6644  CB  THR C  95     8713   4657   5442    106  -1227    -65       C  
ATOM   6645  OG1 THR C  95      88.872 -31.547-223.209  1.00 45.65           O  
ANISOU 6645  OG1 THR C  95     8136   4250   4960    108  -1231    -53       O  
ATOM   6646  CG2 THR C  95      88.120 -33.507-221.977  1.00 49.49           C  
ANISOU 6646  CG2 THR C  95     8621   4652   5532     -9  -1312    -18       C  
ATOM   6647  N   PRO C  96      91.994 -32.609-224.135  1.00 40.47           N  
ANISOU 6647  N   PRO C  96     7775   3485   4115    348   -994   -165       N  
ATOM   6648  CA  PRO C  96      92.853 -31.795-225.007  1.00 41.09           C  
ANISOU 6648  CA  PRO C  96     7906   3594   4112    427   -904   -198       C  
ATOM   6649  C   PRO C  96      92.233 -30.462-225.363  1.00 45.69           C  
ANISOU 6649  C   PRO C  96     8415   4246   4700    387   -937   -170       C  
ATOM   6650  O   PRO C  96      92.963 -29.521-225.702  1.00 48.69           O  
ANISOU 6650  O   PRO C  96     8779   4680   5041    442   -844   -177       O  
ATOM   6651  CB  PRO C  96      93.021 -32.677-226.258  1.00 40.39           C  
ANISOU 6651  CB  PRO C  96     8055   3387   3905    449   -940   -257       C  
ATOM   6652  CG  PRO C  96      92.878 -34.084-225.720  1.00 41.83           C  
ANISOU 6652  CG  PRO C  96     8294   3481   4118    431   -990   -263       C  
ATOM   6653  CD  PRO C  96      91.841 -33.988-224.641  1.00 40.57           C  
ANISOU 6653  CD  PRO C  96     7972   3368   4076    331  -1068   -200       C  
ATOM   6654  N   ARG C  97      90.910 -30.344-225.286  1.00 42.64           N  
ANISOU 6654  N   ARG C  97     7980   3859   4364    292  -1069   -138       N  
ATOM   6655  CA  ARG C  97      90.268 -29.079-225.615  1.00 43.39           C  
ANISOU 6655  CA  ARG C  97     8003   4014   4470    263  -1113   -112       C  
ATOM   6656  C   ARG C  97      90.362 -28.062-224.481  1.00 41.83           C  
ANISOU 6656  C   ARG C  97     7595   3930   4370    277  -1041    -71       C  
ATOM   6657  O   ARG C  97      90.500 -26.865-224.749  1.00 40.21           O  
ANISOU 6657  O   ARG C  97     7350   3778   4152    301  -1009    -62       O  
ATOM   6658  CB  ARG C  97      88.806 -29.323-225.994  1.00 47.91           C  
ANISOU 6658  CB  ARG C  97     8592   4546   5066    164  -1287    -95       C  
ATOM   6659  CG  ARG C  97      88.182 -28.182-226.778  1.00 68.94           C  
ANISOU 6659  CG  ARG C  97    11254   7236   7705    148  -1360    -83       C  
ATOM   6660  CD  ARG C  97      87.223 -28.684-227.848  1.00 87.79           C  
ANISOU 6660  CD  ARG C  97    13782   9538  10039     80  -1528    -97       C  
ATOM   6661  NE  ARG C  97      85.873 -28.897-227.331  1.00 99.44           N  
ANISOU 6661  NE  ARG C  97    15130  11029  11623    -15  -1661    -61       N  
ATOM   6662  CZ  ARG C  97      84.819 -29.188-228.089  1.00102.58           C  
ANISOU 6662  CZ  ARG C  97    15596  11372  12008    -91  -1831    -62       C  
ATOM   6663  NH1 ARG C  97      84.957 -29.302-229.405  1.00 95.53           N  
ANISOU 6663  NH1 ARG C  97    14912  10397  10986    -81  -1893    -98       N  
ATOM   6664  NH2 ARG C  97      83.626 -29.361-227.533  1.00106.41           N  
ANISOU 6664  NH2 ARG C  97    15937  11887  12607   -180  -1938    -27       N  
ATOM   6665  N   ARG C  98      90.305 -28.499-223.221  1.00 38.97           N  
ANISOU 6665  N   ARG C  98     7109   3601   4097    261  -1014    -47       N  
ATOM   6666  CA  ARG C  98      90.239 -27.537-222.128  1.00 35.82           C  
ANISOU 6666  CA  ARG C  98     6519   3307   3787    266   -960    -10       C  
ATOM   6667  C   ARG C  98      90.756 -28.188-220.860  1.00 33.20           C  
ANISOU 6667  C   ARG C  98     6108   2996   3510    281   -889      3       C  
ATOM   6668  O   ARG C  98      90.475 -29.361-220.598  1.00 37.88           O  
ANISOU 6668  O   ARG C  98     6748   3530   4115    243   -934      5       O  
ATOM   6669  CB  ARG C  98      88.804 -27.057-221.892  1.00 39.03           C  
ANISOU 6669  CB  ARG C  98     6814   3749   4267    189  -1068     25       C  
ATOM   6670  CG  ARG C  98      87.821 -28.225-222.156  1.00 55.52           C  
ANISOU 6670  CG  ARG C  98     8965   5764   6366    104  -1193     27       C  
ATOM   6671  CD  ARG C  98      86.648 -28.160-221.241  1.00 58.94           C  
ANISOU 6671  CD  ARG C  98     9233   6254   6910     27  -1250     70       C  
ATOM   6672  NE  ARG C  98      85.882 -29.402-221.122  1.00 49.38           N  
ANISOU 6672  NE  ARG C  98     8054   4983   5726    -65  -1340     80       N  
ATOM   6673  CZ  ARG C  98      86.258 -30.465-220.406  1.00 45.82           C  
ANISOU 6673  CZ  ARG C  98     7629   4495   5284    -81  -1301     86       C  
ATOM   6674  NH1 ARG C  98      87.440 -30.504-219.816  1.00 40.12           N  
ANISOU 6674  NH1 ARG C  98     6912   3788   4543     -2  -1179     78       N  
ATOM   6675  NH2 ARG C  98      85.468 -31.519-220.323  1.00 56.64           N  
ANISOU 6675  NH2 ARG C  98     9031   5809   6683   -178  -1391    101       N  
ATOM   6676  N   CYS C  99      91.482 -27.405-220.076  1.00 33.08           N  
ANISOU 6676  N   CYS C  99     5982   3060   3528    331   -788     14       N  
ATOM   6677  CA  CYS C  99      92.015 -27.852-218.796  1.00 36.27           C  
ANISOU 6677  CA  CYS C  99     6303   3494   3983    351   -722     30       C  
ATOM   6678  C   CYS C  99      91.096 -27.383-217.674  1.00 33.73           C  
ANISOU 6678  C   CYS C  99     5821   3243   3750    294   -745     73       C  
ATOM   6679  O   CYS C  99      90.741 -26.201-217.603  1.00 35.74           O  
ANISOU 6679  O   CYS C  99     5985   3563   4031    293   -741     84       O  
ATOM   6680  CB  CYS C  99      93.438 -27.329-218.592  1.00 30.98           C  
ANISOU 6680  CB  CYS C  99     5609   2868   3294    439   -600     13       C  
ATOM   6681  SG  CYS C  99      94.172 -27.691-216.977  1.00 36.44           S  
ANISOU 6681  SG  CYS C  99     6192   3606   4048    471   -529     34       S  
ATOM   6682  N   LEU C 100      90.710 -28.323-216.802  1.00 37.69           N  
ANISOU 6682  N   LEU C 100     6297   3730   4294    248   -767     97       N  
ATOM   6683  CA  LEU C 100      89.888 -28.047-215.629  1.00 34.85           C  
ANISOU 6683  CA  LEU C 100     5791   3439   4012    192   -771    138       C  
ATOM   6684  C   LEU C 100      90.654 -28.331-214.343  1.00 37.70           C  
ANISOU 6684  C   LEU C 100     6100   3830   4393    223   -692    155       C  
ATOM   6685  O   LEU C 100      90.052 -28.616-213.297  1.00 37.31           O  
ANISOU 6685  O   LEU C 100     5974   3811   4392    168   -695    191       O  
ATOM   6686  CB  LEU C 100      88.595 -28.862-215.667  1.00 36.23           C  
ANISOU 6686  CB  LEU C 100     5970   3575   4219     89   -872    161       C  
ATOM   6687  CG  LEU C 100      87.617 -28.531-216.795  1.00 40.28           C  
ANISOU 6687  CG  LEU C 100     6508   4069   4728     45   -973    152       C  
ATOM   6688  CD1 LEU C 100      86.426 -29.484-216.763  1.00 44.74           C  
ANISOU 6688  CD1 LEU C 100     7074   4594   5333    -67  -1074    176       C  
ATOM   6689  CD2 LEU C 100      87.160 -27.079-216.691  1.00 37.90           C  
ANISOU 6689  CD2 LEU C 100     6075   3857   4467     63   -962    159       C  
ATOM   6690  N   GLY C 101      91.985 -28.242-214.411  1.00 35.62           N  
ANISOU 6690  N   GLY C 101     5878   3564   4092    310   -619    131       N  
ATOM   6691  CA  GLY C 101      92.801 -28.538-213.241  1.00 36.20           C  
ANISOU 6691  CA  GLY C 101     5910   3661   4182    347   -556    145       C  
ATOM   6692  C   GLY C 101      92.491 -27.669-212.034  1.00 38.27           C  
ANISOU 6692  C   GLY C 101     6028   4018   4494    328   -520    175       C  
ATOM   6693  O   GLY C 101      92.717 -28.085-210.893  1.00 37.41           O  
ANISOU 6693  O   GLY C 101     5886   3926   4404    325   -495    200       O  
ATOM   6694  N   SER C 102      91.956 -26.463-212.249  1.00 32.75           N  
ANISOU 6694  N   SER C 102     5251   3378   3815    318   -520    172       N  
ATOM   6695  CA  SER C 102      91.695 -25.575-211.110  1.00 35.93           C  
ANISOU 6695  CA  SER C 102     5525   3867   4260    311   -479    193       C  
ATOM   6696  C   SER C 102      90.371 -25.860-210.393  1.00 38.59           C  
ANISOU 6696  C   SER C 102     5790   4229   4642    229   -514    227       C  
ATOM   6697  O   SER C 102      90.091 -25.222-209.374  1.00 38.35           O  
ANISOU 6697  O   SER C 102     5659   4271   4642    223   -474    242       O  
ATOM   6698  CB  SER C 102      91.719 -24.106-211.557  1.00 39.95           C  
ANISOU 6698  CB  SER C 102     5983   4425   4773    344   -461    174       C  
ATOM   6699  OG  SER C 102      90.535 -23.763-212.256  1.00 39.04           O  
ANISOU 6699  OG  SER C 102     5853   4306   4676    302   -527    176       O  
ATOM   6700  N   LEU C 103      89.548 -26.794-210.873  1.00 37.67           N  
ANISOU 6700  N   LEU C 103     5724   4059   4532    163   -583    239       N  
ATOM   6701  CA  LEU C 103      88.269 -27.045-210.222  1.00 39.73           C  
ANISOU 6701  CA  LEU C 103     5902   4351   4843     75   -610    274       C  
ATOM   6702  C   LEU C 103      88.486 -27.852-208.943  1.00 37.88           C  
ANISOU 6702  C   LEU C 103     5665   4120   4609     47   -569    308       C  
ATOM   6703  O   LEU C 103      89.277 -28.800-208.911  1.00 35.94           O  
ANISOU 6703  O   LEU C 103     5522   3806   4326     65   -570    310       O  
ATOM   6704  CB  LEU C 103      87.307 -27.776-211.160  1.00 38.67           C  
ANISOU 6704  CB  LEU C 103     5818   4157   4719      0   -707    277       C  
ATOM   6705  CG  LEU C 103      86.409 -26.831-211.988  1.00 44.34           C  
ANISOU 6705  CG  LEU C 103     6472   4907   5467     -8   -762    263       C  
ATOM   6706  CD1 LEU C 103      87.208 -25.844-212.852  1.00 39.30           C  
ANISOU 6706  CD1 LEU C 103     5879   4266   4787     82   -747    226       C  
ATOM   6707  CD2 LEU C 103      85.454 -27.628-212.838  1.00 45.40           C  
ANISOU 6707  CD2 LEU C 103     6655   4983   5613    -91   -871    269       C  
ATOM   6708  N   VAL C 104      87.795 -27.449-207.878  1.00 37.72           N  
ANISOU 6708  N   VAL C 104     5531   4177   4625      7   -531    335       N  
ATOM   6709  CA  VAL C 104      87.936 -28.142-206.593  1.00 33.21           C  
ANISOU 6709  CA  VAL C 104     4961   3613   4043    -26   -489    373       C  
ATOM   6710  C   VAL C 104      87.375 -29.556-206.677  1.00 36.32           C  
ANISOU 6710  C   VAL C 104     5428   3933   4438   -119   -544    407       C  
ATOM   6711  O   VAL C 104      88.017 -30.525-206.250  1.00 40.71           O  
ANISOU 6711  O   VAL C 104     6081   4428   4960   -119   -543    426       O  
ATOM   6712  CB  VAL C 104      87.249 -27.332-205.485  1.00 35.61           C  
ANISOU 6712  CB  VAL C 104     5132   4021   4379    -48   -428    391       C  
ATOM   6713  CG1 VAL C 104      87.338 -28.089-204.161  1.00 39.16           C  
ANISOU 6713  CG1 VAL C 104     5597   4476   4805    -93   -384    435       C  
ATOM   6714  CG2 VAL C 104      87.888 -25.960-205.359  1.00 41.11           C  
ANISOU 6714  CG2 VAL C 104     5775   4776   5068     44   -379    356       C  
ATOM   6715  N   PHE C 105      86.153 -29.686-207.187  1.00 39.59           N  
ANISOU 6715  N   PHE C 105     5797   4351   4896   -203   -598    417       N  
ATOM   6716  CA  PHE C 105      85.498 -30.971-207.380  1.00 50.12           C  
ANISOU 6716  CA  PHE C 105     7197   5611   6237   -309   -663    448       C  
ATOM   6717  C   PHE C 105      85.420 -31.299-208.866  1.00 60.22           C  
ANISOU 6717  C   PHE C 105     8567   6808   7507   -309   -757    416       C  
ATOM   6718  O   PHE C 105      84.614 -30.688-209.587  1.00 55.87           O  
ANISOU 6718  O   PHE C 105     7946   6289   6992   -329   -804    401       O  
ATOM   6719  CB  PHE C 105      84.096 -30.957-206.769  1.00 53.12           C  
ANISOU 6719  CB  PHE C 105     7447   6061   6677   -422   -657    489       C  
ATOM   6720  CG  PHE C 105      84.087 -30.746-205.284  1.00 51.77           C  
ANISOU 6720  CG  PHE C 105     7201   5966   6501   -434   -559    523       C  
ATOM   6721  CD1 PHE C 105      83.583 -29.579-204.743  1.00 53.47           C  
ANISOU 6721  CD1 PHE C 105     7267   6298   6752   -410   -495    515       C  
ATOM   6722  CD2 PHE C 105      84.589 -31.710-204.433  1.00 56.52           C  
ANISOU 6722  CD2 PHE C 105     7896   6520   7060   -464   -535    562       C  
ATOM   6723  CE1 PHE C 105      83.575 -29.380-203.375  1.00 62.86           C  
ANISOU 6723  CE1 PHE C 105     8401   7556   7926   -419   -402    542       C  
ATOM   6724  CE2 PHE C 105      84.590 -31.513-203.064  1.00 62.07           C  
ANISOU 6724  CE2 PHE C 105     8546   7290   7746   -476   -448    594       C  
ATOM   6725  CZ  PHE C 105      84.080 -30.347-202.535  1.00 66.23           C  
ANISOU 6725  CZ  PHE C 105     8925   7936   8302   -455   -378    583       C  
ATOM   6726  N   PRO C 106      86.237 -32.234-209.374  1.00 71.76           N  
ANISOU 6726  N   PRO C 106    10189   8160   8917   -281   -791    401       N  
ATOM   6727  CA  PRO C 106      86.123 -32.740-210.747  1.00 85.83           C  
ANISOU 6727  CA  PRO C 106    12085   9849  10678   -292   -883    370       C  
ATOM   6728  C   PRO C 106      84.918 -33.668-210.926  1.00 85.61           C  
ANISOU 6728  C   PRO C 106    12073   9772  10683   -433   -971    402       C  
ATOM   6729  O   PRO C 106      84.793 -34.650-210.186  1.00 83.27           O  
ANISOU 6729  O   PRO C 106    11819   9433  10387   -504   -971    443       O  
ATOM   6730  CB  PRO C 106      87.437 -33.511-210.952  1.00 86.55           C  
ANISOU 6730  CB  PRO C 106    12337   9845  10704   -209   -870    347       C  
ATOM   6731  CG  PRO C 106      88.352 -33.056-209.842  1.00 78.19           C  
ANISOU 6731  CG  PRO C 106    11223   8849   9639   -133   -773    357       C  
ATOM   6732  CD  PRO C 106      87.441 -32.744-208.697  1.00 73.81           C  
ANISOU 6732  CD  PRO C 106    10531   8381   9131   -214   -740    406       C  
ATOM   6733  N   ALA C 119      77.282 -55.687-210.007  1.00 92.82           N  
ANISOU 6733  N   ALA C 119    15244   8550  11475  -2751  -2339   1036       N  
ATOM   6734  CA  ALA C 119      78.570 -55.683-210.692  1.00 88.06           C  
ANISOU 6734  CA  ALA C 119    14809   7860  10791  -2505  -2349    941       C  
ATOM   6735  C   ALA C 119      79.649 -56.373-209.859  1.00 87.68           C  
ANISOU 6735  C   ALA C 119    14915   7732  10669  -2377  -2289    956       C  
ATOM   6736  O   ALA C 119      80.489 -55.703-209.246  1.00 74.16           O  
ANISOU 6736  O   ALA C 119    13161   6070   8947  -2239  -2189    958       O  
ATOM   6737  CB  ALA C 119      78.987 -54.266-211.019  1.00 79.19           C  
ANISOU 6737  CB  ALA C 119    13558   6834   9696  -2378  -2291    895       C  
ATOM   6738  N   PRO C 120      79.629 -57.715-209.837  1.00 85.63           N  
ANISOU 6738  N   PRO C 120    14833   7347  10357  -2422  -2358    965       N  
ATOM   6739  CA  PRO C 120      80.668 -58.458-209.112  1.00 83.78           C  
ANISOU 6739  CA  PRO C 120    14756   7025  10050  -2294  -2321    973       C  
ATOM   6740  C   PRO C 120      81.980 -58.500-209.877  1.00 87.33           C  
ANISOU 6740  C   PRO C 120    15348   7402  10432  -2034  -2330    866       C  
ATOM   6741  O   PRO C 120      83.056 -58.554-209.273  1.00 82.50           O  
ANISOU 6741  O   PRO C 120    14792   6773   9783  -1871  -2266    859       O  
ATOM   6742  CB  PRO C 120      80.065 -59.865-208.961  1.00 82.87           C  
ANISOU 6742  CB  PRO C 120    14780   6798   9908  -2449  -2406   1016       C  
ATOM   6743  CG  PRO C 120      78.622 -59.740-209.393  1.00 85.75           C  
ANISOU 6743  CG  PRO C 120    15018   7220  10345  -2680  -2467   1050       C  
ATOM   6744  CD  PRO C 120      78.594 -58.612-210.370  1.00 87.04           C  
ANISOU 6744  CD  PRO C 120    15065   7461  10544  -2607  -2475    980       C  
ATOM   6745  N   GLU C 121      81.901 -58.484-211.212  1.00 85.51           N  
ANISOU 6745  N   GLU C 121    15173   7134  10184  -1993  -2408    782       N  
ATOM   6746  CA  GLU C 121      83.116 -58.501-212.020  1.00 81.14           C  
ANISOU 6746  CA  GLU C 121    14745   6522   9561  -1749  -2405    677       C  
ATOM   6747  C   GLU C 121      83.886 -57.195-211.894  1.00 75.10           C  
ANISOU 6747  C   GLU C 121    13849   5866   8818  -1587  -2296    647       C  
ATOM   6748  O   GLU C 121      85.119 -57.194-211.976  1.00 78.88           O  
ANISOU 6748  O   GLU C 121    14402   6319   9250  -1371  -2248    589       O  
ATOM   6749  CB  GLU C 121      82.776 -58.782-213.485  1.00 91.53           C  
ANISOU 6749  CB  GLU C 121    16156   7778  10843  -1756  -2511    598       C  
ATOM   6750  CG  GLU C 121      83.988 -59.122-214.345  1.00105.26           C  
ANISOU 6750  CG  GLU C 121    18064   9436  12494  -1520  -2512    492       C  
ATOM   6751  CD  GLU C 121      83.622 -59.454-215.788  1.00118.52           C  
ANISOU 6751  CD  GLU C 121    19855  11052  14124  -1533  -2617    419       C  
ATOM   6752  OE1 GLU C 121      82.506 -59.966-216.023  1.00123.05           O  
ANISOU 6752  OE1 GLU C 121    20445  11592  14715  -1730  -2719    457       O  
ATOM   6753  OE2 GLU C 121      84.452 -59.197-216.688  1.00121.38           O  
ANISOU 6753  OE2 GLU C 121    20287  11404  14429  -1349  -2596    327       O  
ATOM   6754  N   GLN C 122      83.182 -56.079-211.689  1.00 68.83           N  
ANISOU 6754  N   GLN C 122    12857   5196   8099  -1688  -2257    688       N  
ATOM   6755  CA  GLN C 122      83.859 -54.806-211.466  1.00 67.68           C  
ANISOU 6755  CA  GLN C 122    12585   5154   7977  -1549  -2153    671       C  
ATOM   6756  C   GLN C 122      84.640 -54.822-210.158  1.00 65.38           C  
ANISOU 6756  C   GLN C 122    12281   4883   7678  -1466  -2059    725       C  
ATOM   6757  O   GLN C 122      85.797 -54.386-210.112  1.00 66.43           O  
ANISOU 6757  O   GLN C 122    12422   5034   7785  -1260  -1992    680       O  
ATOM   6758  CB  GLN C 122      82.850 -53.657-211.470  1.00 70.60           C  
ANISOU 6758  CB  GLN C 122    12746   5647   8431  -1691  -2140    709       C  
ATOM   6759  CG  GLN C 122      82.096 -53.497-212.783  1.00 84.30           C  
ANISOU 6759  CG  GLN C 122    14476   7375  10177  -1762  -2241    653       C  
ATOM   6760  CD  GLN C 122      81.725 -52.050-213.066  1.00 92.60           C  
ANISOU 6760  CD  GLN C 122    15341   8548  11294  -1774  -2212    645       C  
ATOM   6761  OE1 GLN C 122      82.570 -51.248-213.469  1.00 94.73           O  
ANISOU 6761  OE1 GLN C 122    15572   8886  11534  -1579  -2143    578       O  
ATOM   6762  NE2 GLN C 122      80.458 -51.707-212.851  1.00 95.38           N  
ANISOU 6762  NE2 GLN C 122    15508   9006  11726  -1968  -2234    701       N  
ATOM   6763  N   LEU C 123      84.018 -55.308-209.081  1.00 62.80           N  
ANISOU 6763  N   LEU C 123    11930   4560   7371  -1627  -2051    823       N  
ATOM   6764  CA  LEU C 123      84.716 -55.371-207.798  1.00 56.59           C  
ANISOU 6764  CA  LEU C 123    11143   3792   6566  -1557  -1970    879       C  
ATOM   6765  C   LEU C 123      85.942 -56.264-207.894  1.00 60.69           C  
ANISOU 6765  C   LEU C 123    11844   4200   7014  -1363  -1990    822       C  
ATOM   6766  O   LEU C 123      87.032 -55.895-207.442  1.00 57.14           O  
ANISOU 6766  O   LEU C 123    11383   3780   6549  -1183  -1923    805       O  
ATOM   6767  CB  LEU C 123      83.766 -55.879-206.714  1.00 62.00           C  
ANISOU 6767  CB  LEU C 123    11794   4490   7271  -1777  -1963    992       C  
ATOM   6768  CG  LEU C 123      84.354 -56.023-205.308  1.00 61.10           C  
ANISOU 6768  CG  LEU C 123    11692   4394   7128  -1732  -1887   1061       C  
ATOM   6769  CD1 LEU C 123      84.891 -54.691-204.823  1.00 55.85           C  
ANISOU 6769  CD1 LEU C 123    10880   3855   6485  -1622  -1782   1069       C  
ATOM   6770  CD2 LEU C 123      83.315 -56.579-204.351  1.00 63.05           C  
ANISOU 6770  CD2 LEU C 123    11915   4653   7386  -1966  -1879   1169       C  
ATOM   6771  N   LEU C 124      85.771 -57.439-208.503  1.00 56.88           N  
ANISOU 6771  N   LEU C 124    11525   3593   6492  -1398  -2086    790       N  
ATOM   6772  CA  LEU C 124      86.852 -58.399-208.691  1.00 61.64           C  
ANISOU 6772  CA  LEU C 124    12311   4082   7028  -1224  -2116    732       C  
ATOM   6773  C   LEU C 124      88.080 -57.766-209.338  1.00 60.03           C  
ANISOU 6773  C   LEU C 124    12097   3905   6806   -972  -2065    635       C  
ATOM   6774  O   LEU C 124      89.211 -57.983-208.895  1.00 62.07           O  
ANISOU 6774  O   LEU C 124    12402   4143   7039   -797  -2027    616       O  
ATOM   6775  CB  LEU C 124      86.335 -59.552-209.554  1.00 70.74           C  
ANISOU 6775  CB  LEU C 124    13630   5107   8143  -1307  -2232    699       C  
ATOM   6776  CG  LEU C 124      86.487 -60.998-209.092  1.00 77.47           C  
ANISOU 6776  CG  LEU C 124    14667   5824   8944  -1331  -2296    726       C  
ATOM   6777  CD1 LEU C 124      87.669 -61.654-209.794  1.00 79.83           C  
ANISOU 6777  CD1 LEU C 124    15132   6021   9178  -1107  -2323    628       C  
ATOM   6778  CD2 LEU C 124      86.625 -61.072-207.567  1.00 70.62           C  
ANISOU 6778  CD2 LEU C 124    13759   4985   8087  -1368  -2238    821       C  
ATOM   6779  N   SER C 125      87.882 -57.003-210.412  1.00 64.25           N  
ANISOU 6779  N   SER C 125    12572   4486   7353   -951  -2065    573       N  
ATOM   6780  CA  SER C 125      89.036 -56.510-211.158  1.00 64.58           C  
ANISOU 6780  CA  SER C 125    12622   4547   7368   -717  -2016    475       C  
ATOM   6781  C   SER C 125      89.817 -55.485-210.349  1.00 55.37           C  
ANISOU 6781  C   SER C 125    11314   3490   6235   -594  -1907    496       C  
ATOM   6782  O   SER C 125      91.052 -55.482-210.374  1.00 58.51           O  
ANISOU 6782  O   SER C 125    11737   3886   6609   -386  -1860    443       O  
ATOM   6783  CB  SER C 125      88.591 -55.921-212.494  1.00 69.09           C  
ANISOU 6783  CB  SER C 125    13171   5143   7936   -733  -2043    407       C  
ATOM   6784  OG  SER C 125      87.474 -55.074-212.312  1.00 71.83           O  
ANISOU 6784  OG  SER C 125    13367   5578   8347   -911  -2044    466       O  
ATOM   6785  N   GLN C 126      89.117 -54.601-209.635  1.00 54.91           N  
ANISOU 6785  N   GLN C 126    11099   3531   6231   -720  -1866    573       N  
ATOM   6786  CA  GLN C 126      89.794 -53.693-208.715  1.00 53.54           C  
ANISOU 6786  CA  GLN C 126    10801   3459   6083   -621  -1769    607       C  
ATOM   6787  C   GLN C 126      90.473 -54.462-207.588  1.00 51.11           C  
ANISOU 6787  C   GLN C 126    10560   3108   5750   -562  -1760    652       C  
ATOM   6788  O   GLN C 126      91.596 -54.132-207.185  1.00 49.64           O  
ANISOU 6788  O   GLN C 126    10343   2960   5559   -383  -1704    632       O  
ATOM   6789  CB  GLN C 126      88.804 -52.689-208.128  1.00 49.10           C  
ANISOU 6789  CB  GLN C 126    10072   3006   5578   -786  -1731    689       C  
ATOM   6790  CG  GLN C 126      88.141 -51.763-209.135  1.00 55.37           C  
ANISOU 6790  CG  GLN C 126    10771   3860   6406   -839  -1739    650       C  
ATOM   6791  CD  GLN C 126      87.181 -50.802-208.457  1.00 67.15           C  
ANISOU 6791  CD  GLN C 126    12014   5546   7954   -979  -1672    713       C  
ATOM   6792  OE1 GLN C 126      87.562 -49.698-208.066  1.00 75.65           O  
ANISOU 6792  OE1 GLN C 126    12908   6788   9047   -887  -1571    705       O  
ATOM   6793  NE2 GLN C 126      85.934 -51.230-208.288  1.00 71.25           N  
ANISOU 6793  NE2 GLN C 126    12525   6044   8504  -1202  -1726    776       N  
ATOM   6794  N   ALA C 127      89.803 -55.484-207.058  1.00 51.02           N  
ANISOU 6794  N   ALA C 127    10639   3021   5724   -714  -1819    713       N  
ATOM   6795  CA  ALA C 127      90.387 -56.241-205.955  1.00 63.79           C  
ANISOU 6795  CA  ALA C 127    12331   4592   7313   -670  -1819    761       C  
ATOM   6796  C   ALA C 127      91.662 -56.948-206.400  1.00 59.06           C  
ANISOU 6796  C   ALA C 127    11858   3909   6675   -449  -1842    677       C  
ATOM   6797  O   ALA C 127      92.681 -56.925-205.700  1.00 54.78           O  
ANISOU 6797  O   ALA C 127    11306   3382   6125   -301  -1808    680       O  
ATOM   6798  CB  ALA C 127      89.366 -57.237-205.401  1.00 58.49           C  
ANISOU 6798  CB  ALA C 127    11745   3850   6630   -885  -1879    841       C  
ATOM   6799  N   ARG C 128      91.631 -57.557-207.584  1.00 53.82           N  
ANISOU 6799  N   ARG C 128    11307   3158   5983   -422  -1901    599       N  
ATOM   6800  CA  ARG C 128      92.817 -58.233-208.094  1.00 63.35           C  
ANISOU 6800  CA  ARG C 128    12631   4288   7151   -212  -1916    515       C  
ATOM   6801  C   ARG C 128      93.975 -57.260-208.272  1.00 58.92           C  
ANISOU 6801  C   ARG C 128    11956   3822   6609      3  -1828    456       C  
ATOM   6802  O   ARG C 128      95.112 -57.564-207.892  1.00 59.45           O  
ANISOU 6802  O   ARG C 128    12048   3873   6668    177  -1811    434       O  
ATOM   6803  CB  ARG C 128      92.488 -58.922-209.411  1.00 63.35           C  
ANISOU 6803  CB  ARG C 128    12766   4192   7112   -230  -1986    442       C  
ATOM   6804  CG  ARG C 128      91.546 -60.087-209.248  1.00 71.76           C  
ANISOU 6804  CG  ARG C 128    13970   5144   8152   -416  -2085    492       C  
ATOM   6805  CD  ARG C 128      91.187 -60.609-210.608  1.00 82.51           C  
ANISOU 6805  CD  ARG C 128    15451   6425   9473   -436  -2155    418       C  
ATOM   6806  NE  ARG C 128      90.901 -62.031-210.594  1.00 90.87           N  
ANISOU 6806  NE  ARG C 128    16702   7338  10487   -508  -2253    432       N  
ATOM   6807  CZ  ARG C 128      91.819 -62.977-210.421  1.00 99.93           C  
ANISOU 6807  CZ  ARG C 128    17990   8387  11593   -365  -2276    403       C  
ATOM   6808  NH1 ARG C 128      93.093 -62.659-210.229  1.00104.29           N  
ANISOU 6808  NH1 ARG C 128    18499   8977  12149   -143  -2207    360       N  
ATOM   6809  NH2 ARG C 128      91.460 -64.248-210.438  1.00100.13           N  
ANISOU 6809  NH2 ARG C 128    18195   8275  11575   -446  -2372    418       N  
ATOM   6810  N   ASP C 129      93.701 -56.082-208.839  1.00 55.52           N  
ANISOU 6810  N   ASP C 129    11397   3491   6207     -7  -1775    433       N  
ATOM   6811  CA  ASP C 129      94.751 -55.095-209.055  1.00 62.71           C  
ANISOU 6811  CA  ASP C 129    12193   4497   7136    185  -1688    378       C  
ATOM   6812  C   ASP C 129      95.422 -54.698-207.750  1.00 58.21           C  
ANISOU 6812  C   ASP C 129    11528   3997   6593    255  -1639    437       C  
ATOM   6813  O   ASP C 129      96.649 -54.564-207.689  1.00 57.45           O  
ANISOU 6813  O   ASP C 129    11400   3927   6500    452  -1598    392       O  
ATOM   6814  CB  ASP C 129      94.172 -53.860-209.749  1.00 69.84           C  
ANISOU 6814  CB  ASP C 129    12976   5494   8064    129  -1647    360       C  
ATOM   6815  CG  ASP C 129      94.088 -54.028-211.248  1.00 90.70           C  
ANISOU 6815  CG  ASP C 129    15700   8090  10670    161  -1672    267       C  
ATOM   6816  OD1 ASP C 129      94.671 -55.011-211.764  1.00 89.82           O  
ANISOU 6816  OD1 ASP C 129    15728   7886  10512    261  -1703    208       O  
ATOM   6817  OD2 ASP C 129      93.446 -53.177-211.907  1.00101.01           O  
ANISOU 6817  OD2 ASP C 129    16937   9453  11989     90  -1661    253       O  
ATOM   6818  N   PHE C 130      94.636 -54.497-206.696  1.00 59.63           N  
ANISOU 6818  N   PHE C 130    11656   4211   6790     94  -1642    538       N  
ATOM   6819  CA  PHE C 130      95.221 -54.082-205.427  1.00 51.48           C  
ANISOU 6819  CA  PHE C 130    10538   3249   5772    152  -1599    598       C  
ATOM   6820  C   PHE C 130      96.095 -55.184-204.825  1.00 50.88           C  
ANISOU 6820  C   PHE C 130    10576   3088   5670    259  -1643    599       C  
ATOM   6821  O   PHE C 130      97.191 -54.902-204.328  1.00 54.59           O  
ANISOU 6821  O   PHE C 130    10987   3604   6150    422  -1611    587       O  
ATOM   6822  CB  PHE C 130      94.125 -53.667-204.456  1.00 51.19           C  
ANISOU 6822  CB  PHE C 130    10433   3268   5748    -54  -1587    707       C  
ATOM   6823  CG  PHE C 130      94.616 -53.504-203.040  1.00 57.53           C  
ANISOU 6823  CG  PHE C 130    11191   4122   6545    -21  -1559    778       C  
ATOM   6824  CD1 PHE C 130      95.380 -52.400-202.687  1.00 57.81           C  
ANISOU 6824  CD1 PHE C 130    11092   4273   6602    106  -1493    771       C  
ATOM   6825  CD2 PHE C 130      94.330 -54.462-202.076  1.00 61.95           C  
ANISOU 6825  CD2 PHE C 130    11851   4614   7073   -118  -1603    851       C  
ATOM   6826  CE1 PHE C 130      95.847 -52.248-201.402  1.00 57.08           C  
ANISOU 6826  CE1 PHE C 130    10964   4228   6496    138  -1477    834       C  
ATOM   6827  CE2 PHE C 130      94.791 -54.317-200.781  1.00 57.16           C  
ANISOU 6827  CE2 PHE C 130    11214   4053   6450    -87  -1582    915       C  
ATOM   6828  CZ  PHE C 130      95.549 -53.202-200.441  1.00 60.65           C  
ANISOU 6828  CZ  PHE C 130    11520   4612   6912     41  -1521    906       C  
ATOM   6829  N   ILE C 131      95.643 -56.441-204.887  1.00 59.47           N  
ANISOU 6829  N   ILE C 131    11824   4049   6724    172  -1721    611       N  
ATOM   6830  CA  ILE C 131      96.419 -57.553-204.328  1.00 58.21           C  
ANISOU 6830  CA  ILE C 131    11788   3794   6536    268  -1772    614       C  
ATOM   6831  C   ILE C 131      97.764 -57.663-205.031  1.00 60.24           C  
ANISOU 6831  C   ILE C 131    12054   4039   6796    515  -1757    513       C  
ATOM   6832  O   ILE C 131      98.797 -57.914-204.401  1.00 58.75           O  
ANISOU 6832  O   ILE C 131    11864   3846   6612    661  -1760    513       O  
ATOM   6833  CB  ILE C 131      95.627 -58.871-204.428  1.00 58.90           C  
ANISOU 6833  CB  ILE C 131    12055   3741   6584    124  -1862    639       C  
ATOM   6834  CG1 ILE C 131      94.311 -58.776-203.653  1.00 64.35           C  
ANISOU 6834  CG1 ILE C 131    12722   4454   7275   -128  -1867    745       C  
ATOM   6835  CG2 ILE C 131      96.457 -60.046-203.920  1.00 58.61           C  
ANISOU 6835  CG2 ILE C 131    12159   3594   6514    234  -1921    637       C  
ATOM   6836  CD1 ILE C 131      94.481 -58.595-202.156  1.00 65.87           C  
ANISOU 6836  CD1 ILE C 131    12867   4696   7463   -153  -1841    837       C  
ATOM   6837  N   ASN C 132      97.772 -57.457-206.347  1.00 58.76           N  
ANISOU 6837  N   ASN C 132    11871   3850   6607    565  -1738    427       N  
ATOM   6838  CA  ASN C 132      99.018 -57.498-207.103  1.00 62.63           C  
ANISOU 6838  CA  ASN C 132    12358   4340   7098    795  -1706    329       C  
ATOM   6839  C   ASN C 132      99.953 -56.374-206.680  1.00 59.60           C  
ANISOU 6839  C   ASN C 132    11794   4092   6761    936  -1624    323       C  
ATOM   6840  O   ASN C 132     101.160 -56.592-206.518  1.00 57.82           O  
ANISOU 6840  O   ASN C 132    11551   3869   6549   1122  -1612    286       O  
ATOM   6841  CB  ASN C 132      98.710 -57.420-208.598  1.00 60.59           C  
ANISOU 6841  CB  ASN C 132    12143   4062   6817    796  -1696    244       C  
ATOM   6842  CG  ASN C 132      97.736 -58.490-209.037  1.00 70.78           C  
ANISOU 6842  CG  ASN C 132    13609   5223   8062    645  -1786    252       C  
ATOM   6843  OD1 ASN C 132      97.908 -59.673-208.726  1.00 70.59           O  
ANISOU 6843  OD1 ASN C 132    13727   5084   8008    657  -1854    262       O  
ATOM   6844  ND2 ASN C 132      96.688 -58.080-209.736  1.00 79.12           N  
ANISOU 6844  ND2 ASN C 132    14654   6296   9112    498  -1794    249       N  
ATOM   6845  N   GLN C 133      99.411 -55.161-206.521  1.00 59.97           N  
ANISOU 6845  N   GLN C 133    11701   4251   6834    849  -1570    357       N  
ATOM   6846  CA  GLN C 133     100.182 -54.053-205.965  1.00 61.45           C  
ANISOU 6846  CA  GLN C 133    11717   4568   7063    956  -1500    366       C  
ATOM   6847  C   GLN C 133     100.806 -54.441-204.637  1.00 55.61           C  
ANISOU 6847  C   GLN C 133    10975   3824   6329   1007  -1531    426       C  
ATOM   6848  O   GLN C 133     101.996 -54.213-204.395  1.00 57.87           O  
ANISOU 6848  O   GLN C 133    11185   4161   6643   1184  -1506    396       O  
ATOM   6849  CB  GLN C 133      99.287 -52.834-205.750  1.00 63.71           C  
ANISOU 6849  CB  GLN C 133    11880   4957   7368    817  -1455    418       C  
ATOM   6850  CG  GLN C 133      99.051 -51.950-206.946  1.00 72.46           C  
ANISOU 6850  CG  GLN C 133    12923   6121   8486    826  -1401    354       C  
ATOM   6851  CD  GLN C 133      98.468 -50.619-206.522  1.00 77.16           C  
ANISOU 6851  CD  GLN C 133    13373   6835   9110    734  -1351    408       C  
ATOM   6852  OE1 GLN C 133      97.278 -50.360-206.708  1.00 80.41           O  
ANISOU 6852  OE1 GLN C 133    13787   7246   9520    562  -1365    444       O  
ATOM   6853  NE2 GLN C 133      99.301 -49.776-205.918  1.00 79.33           N  
ANISOU 6853  NE2 GLN C 133    13518   7212   9413    847  -1297    417       N  
ATOM   6854  N   TYR C 134      99.992 -54.985-203.740  1.00 57.08           N  
ANISOU 6854  N   TYR C 134    11240   3958   6491    847  -1585    514       N  
ATOM   6855  CA  TYR C 134     100.482 -55.290-202.404  1.00 49.98           C  
ANISOU 6855  CA  TYR C 134    10345   3058   5587    875  -1617    580       C  
ATOM   6856  C   TYR C 134     101.625 -56.296-202.462  1.00 51.80           C  
ANISOU 6856  C   TYR C 134    10663   3204   5814   1054  -1665    530       C  
ATOM   6857  O   TYR C 134     102.675 -56.093-201.846  1.00 55.25           O  
ANISOU 6857  O   TYR C 134    11026   3689   6275   1198  -1661    529       O  
ATOM   6858  CB  TYR C 134      99.332 -55.795-201.534  1.00 53.12           C  
ANISOU 6858  CB  TYR C 134    10829   3404   5948    658  -1661    680       C  
ATOM   6859  CG  TYR C 134      99.759 -56.132-200.115  1.00 60.80           C  
ANISOU 6859  CG  TYR C 134    11826   4373   6902    671  -1695    754       C  
ATOM   6860  CD1 TYR C 134     100.407 -55.196-199.330  1.00 63.32           C  
ANISOU 6860  CD1 TYR C 134    12009   4810   7241    751  -1656    778       C  
ATOM   6861  CD2 TYR C 134      99.508 -57.384-199.572  1.00 67.55           C  
ANISOU 6861  CD2 TYR C 134    12845   5106   7715    601  -1771    798       C  
ATOM   6862  CE1 TYR C 134     100.801 -55.490-198.044  1.00 67.38           C  
ANISOU 6862  CE1 TYR C 134    12551   5320   7731    763  -1693    843       C  
ATOM   6863  CE2 TYR C 134      99.898 -57.691-198.274  1.00 74.54           C  
ANISOU 6863  CE2 TYR C 134    13761   5984   8576    613  -1806    866       C  
ATOM   6864  CZ  TYR C 134     100.543 -56.732-197.519  1.00 76.56           C  
ANISOU 6864  CZ  TYR C 134    13880   6360   8850    694  -1767    888       C  
ATOM   6865  OH  TYR C 134     100.941 -57.011-196.232  1.00 82.25           O  
ANISOU 6865  OH  TYR C 134    14636   7076   9540    705  -1807    953       O  
ATOM   6866  N   TYR C 135     101.463 -57.370-203.244  1.00 59.51           N  
ANISOU 6866  N   TYR C 135    11793   4056   6763   1055  -1713    484       N  
ATOM   6867  CA  TYR C 135     102.482 -58.417-203.209  1.00 62.66           C  
ANISOU 6867  CA  TYR C 135    12289   4363   7156   1217  -1766    445       C  
ATOM   6868  C   TYR C 135     103.747 -58.001-203.946  1.00 57.52           C  
ANISOU 6868  C   TYR C 135    11537   3774   6546   1446  -1709    350       C  
ATOM   6869  O   TYR C 135     104.840 -58.453-203.594  1.00 61.01           O  
ANISOU 6869  O   TYR C 135    11979   4196   7007   1609  -1734    330       O  
ATOM   6870  CB  TYR C 135     101.920 -59.735-203.746  1.00 64.91           C  
ANISOU 6870  CB  TYR C 135    12781   4490   7392   1146  -1840    429       C  
ATOM   6871  CG  TYR C 135     101.181 -60.492-202.662  1.00 66.77           C  
ANISOU 6871  CG  TYR C 135    13132   4645   7591    982  -1914    528       C  
ATOM   6872  CD1 TYR C 135     101.871 -61.242-201.716  1.00 68.18           C  
ANISOU 6872  CD1 TYR C 135    13382   4763   7759   1060  -1974    562       C  
ATOM   6873  CD2 TYR C 135      99.800 -60.408-202.551  1.00 69.43           C  
ANISOU 6873  CD2 TYR C 135    13498   4976   7906    746  -1920    591       C  
ATOM   6874  CE1 TYR C 135     101.197 -61.917-200.705  1.00 69.12           C  
ANISOU 6874  CE1 TYR C 135    13614   4811   7838    905  -2036    656       C  
ATOM   6875  CE2 TYR C 135      99.119 -61.068-201.546  1.00 67.21           C  
ANISOU 6875  CE2 TYR C 135    13315   4631   7591    588  -1975    684       C  
ATOM   6876  CZ  TYR C 135      99.819 -61.825-200.628  1.00 73.91           C  
ANISOU 6876  CZ  TYR C 135    14247   5415   8421    668  -2031    717       C  
ATOM   6877  OH  TYR C 135      99.129 -62.482-199.630  1.00 65.32           O  
ANISOU 6877  OH  TYR C 135    13265   4263   7291    505  -2082    812       O  
ATOM   6878  N   SER C 136     103.638 -57.118-204.938  1.00 58.63           N  
ANISOU 6878  N   SER C 136    11582   3992   6702   1461  -1632    292       N  
ATOM   6879  CA  SER C 136     104.853 -56.573-205.532  1.00 60.50           C  
ANISOU 6879  CA  SER C 136    11696   4309   6980   1668  -1561    211       C  
ATOM   6880  C   SER C 136     105.604 -55.707-204.531  1.00 56.66           C  
ANISOU 6880  C   SER C 136    11040   3945   6545   1744  -1534    250       C  
ATOM   6881  O   SER C 136     106.840 -55.721-204.489  1.00 63.89           O  
ANISOU 6881  O   SER C 136    11880   4895   7501   1930  -1519    207       O  
ATOM   6882  CB  SER C 136     104.511 -55.769-206.787  1.00 58.35           C  
ANISOU 6882  CB  SER C 136    11367   4096   6705   1653  -1482    146       C  
ATOM   6883  OG  SER C 136     103.618 -56.507-207.601  1.00 73.74           O  
ANISOU 6883  OG  SER C 136    13478   5937   8602   1545  -1522    125       O  
ATOM   6884  N   SER C 137     104.869 -54.957-203.703  1.00 51.57           N  
ANISOU 6884  N   SER C 137    10330   3365   5898   1600  -1530    331       N  
ATOM   6885  CA  SER C 137     105.475 -54.013-202.774  1.00 58.93           C  
ANISOU 6885  CA  SER C 137    11101   4421   6870   1654  -1504    369       C  
ATOM   6886  C   SER C 137     106.191 -54.700-201.617  1.00 61.24           C  
ANISOU 6886  C   SER C 137    11427   4675   7165   1724  -1579    415       C  
ATOM   6887  O   SER C 137     107.034 -54.074-200.969  1.00 66.73           O  
ANISOU 6887  O   SER C 137    11990   5465   7899   1821  -1570    425       O  
ATOM   6888  CB  SER C 137     104.406 -53.065-202.228  1.00 67.49           C  
ANISOU 6888  CB  SER C 137    12125   5579   7941   1473  -1479    445       C  
ATOM   6889  OG  SER C 137     103.708 -53.660-201.145  1.00 63.15           O  
ANISOU 6889  OG  SER C 137    11675   4969   7352   1331  -1544    538       O  
ATOM   6890  N   ILE C 138     105.871 -55.961-201.329  1.00 61.79           N  
ANISOU 6890  N   ILE C 138    11675   4609   7194   1673  -1660    442       N  
ATOM   6891  CA  ILE C 138     106.588 -56.717-200.308  1.00 68.15           C  
ANISOU 6891  CA  ILE C 138    12534   5363   7999   1750  -1739    480       C  
ATOM   6892  C   ILE C 138     107.561 -57.721-200.920  1.00 74.62           C  
ANISOU 6892  C   ILE C 138    13424   6094   8835   1931  -1772    404       C  
ATOM   6893  O   ILE C 138     108.120 -58.553-200.199  1.00 75.29           O  
ANISOU 6893  O   ILE C 138    13584   6108   8915   1999  -1851    429       O  
ATOM   6894  CB  ILE C 138     105.622 -57.415-199.336  1.00 64.33           C  
ANISOU 6894  CB  ILE C 138    12198   4792   7453   1567  -1810    577       C  
ATOM   6895  CG1 ILE C 138     104.618 -58.280-200.092  1.00 63.06           C  
ANISOU 6895  CG1 ILE C 138    12204   4508   7249   1442  -1832    565       C  
ATOM   6896  CG2 ILE C 138     104.902 -56.382-198.472  1.00 66.52           C  
ANISOU 6896  CG2 ILE C 138    12383   5175   7718   1418  -1774    659       C  
ATOM   6897  CD1 ILE C 138     103.843 -59.214-199.198  1.00 58.08           C  
ANISOU 6897  CD1 ILE C 138    11737   3771   6561   1285  -1909    652       C  
ATOM   6898  N   LYS C 139     107.786 -57.651-202.237  1.00 75.69           N  
ANISOU 6898  N   LYS C 139    13540   6232   8986   2014  -1712    312       N  
ATOM   6899  CA  LYS C 139     108.774 -58.478-202.936  1.00 79.10           C  
ANISOU 6899  CA  LYS C 139    14019   6598   9437   2203  -1722    229       C  
ATOM   6900  C   LYS C 139     108.412 -59.962-202.891  1.00 80.50           C  
ANISOU 6900  C   LYS C 139    14426   6599   9560   2165  -1816    241       C  
ATOM   6901  O   LYS C 139     109.292 -60.829-202.857  1.00 77.46           O  
ANISOU 6901  O   LYS C 139    14101   6142   9190   2316  -1864    209       O  
ATOM   6902  CB  LYS C 139     110.187 -58.254-202.383  1.00 82.94           C  
ANISOU 6902  CB  LYS C 139    14365   7158   9991   2396  -1725    215       C  
ATOM   6903  CG  LYS C 139     110.492 -56.806-202.014  1.00 89.75           C  
ANISOU 6903  CG  LYS C 139    15007   8192  10902   2404  -1659    232       C  
ATOM   6904  CD  LYS C 139     111.697 -56.273-202.764  1.00 94.91           C  
ANISOU 6904  CD  LYS C 139    15492   8942  11626   2599  -1580    145       C  
ATOM   6905  CE  LYS C 139     112.766 -55.769-201.801  1.00 96.59           C  
ANISOU 6905  CE  LYS C 139    15539   9256  11906   2709  -1603    171       C  
ATOM   6906  NZ  LYS C 139     114.070 -55.550-202.489  1.00 98.07           N  
ANISOU 6906  NZ  LYS C 139    15574   9517  12171   2915  -1539     85       N  
ATOM   6907  N   ARG C 140     107.115 -60.265-202.891  1.00 82.77           N  
ANISOU 6907  N   ARG C 140    14842   6816   9790   1962  -1846    287       N  
ATOM   6908  CA  ARG C 140     106.629 -61.642-202.919  1.00 88.91           C  
ANISOU 6908  CA  ARG C 140    15844   7424  10511   1898  -1935    300       C  
ATOM   6909  C   ARG C 140     105.511 -61.780-203.952  1.00 92.90           C  
ANISOU 6909  C   ARG C 140    16447   7880  10973   1755  -1919    274       C  
ATOM   6910  O   ARG C 140     104.438 -62.317-203.675  1.00101.90           O  
ANISOU 6910  O   ARG C 140    17716   8936  12066   1569  -1975    331       O  
ATOM   6911  CB  ARG C 140     106.150 -62.093-201.538  1.00 90.91           C  
ANISOU 6911  CB  ARG C 140    16181   7626  10733   1770  -2016    408       C  
ATOM   6912  CG  ARG C 140     106.618 -61.224-200.380  1.00 93.57           C  
ANISOU 6912  CG  ARG C 140    16364   8083  11104   1794  -2003    468       C  
ATOM   6913  CD  ARG C 140     107.285 -62.028-199.273  1.00101.43           C  
ANISOU 6913  CD  ARG C 140    17438   9009  12093   1866  -2096    515       C  
ATOM   6914  NE  ARG C 140     108.633 -62.457-199.635  1.00105.92           N  
ANISOU 6914  NE  ARG C 140    17980   9557  12708   2107  -2113    441       N  
ATOM   6915  CZ  ARG C 140     108.935 -63.664-200.102  1.00111.81           C  
ANISOU 6915  CZ  ARG C 140    18882  10164  13435   2192  -2171    397       C  
ATOM   6916  NH1 ARG C 140     107.981 -64.571-200.261  1.00115.41           N  
ANISOU 6916  NH1 ARG C 140    19538  10486  13826   2051  -2223    420       N  
ATOM   6917  NH2 ARG C 140     110.189 -63.969-200.406  1.00112.97           N  
ANISOU 6917  NH2 ARG C 140    18984  10306  13632   2418  -2177    330       N  
ATOM   6918  N   SER C 141     105.758 -61.295-205.168  1.00 83.60           N  
ANISOU 6918  N   SER C 141    15204   6752   9809   1836  -1843    186       N  
ATOM   6919  CA  SER C 141     104.770 -61.369-206.235  1.00 86.00           C  
ANISOU 6919  CA  SER C 141    15593   7013  10069   1713  -1831    153       C  
ATOM   6920  C   SER C 141     104.958 -62.658-207.023  1.00 89.69           C  
ANISOU 6920  C   SER C 141    16253   7332  10494   1784  -1886     90       C  
ATOM   6921  O   SER C 141     106.087 -63.071-207.301  1.00 94.79           O  
ANISOU 6921  O   SER C 141    16901   7957  11158   1988  -1876     27       O  
ATOM   6922  CB  SER C 141     104.875 -60.159-207.163  1.00 82.87           C  
ANISOU 6922  CB  SER C 141    15043   6744   9698   1754  -1723     93       C  
ATOM   6923  OG  SER C 141     103.692 -60.006-207.928  1.00 87.77           O  
ANISOU 6923  OG  SER C 141    15725   7345  10280   1587  -1721     88       O  
ATOM   6924  N   GLY C 142     103.840 -63.292-207.382  1.00 87.88           N  
ANISOU 6924  N   GLY C 142    16181   7001  10207   1614  -1944    107       N  
ATOM   6925  CA  GLY C 142     103.845 -64.631-207.931  1.00 89.26           C  
ANISOU 6925  CA  GLY C 142    16569   7016  10331   1645  -2018     66       C  
ATOM   6926  C   GLY C 142     103.877 -65.730-206.892  1.00 94.48           C  
ANISOU 6926  C   GLY C 142    17367   7556  10973   1620  -2121    130       C  
ATOM   6927  O   GLY C 142     103.663 -66.899-207.235  1.00100.86           O  
ANISOU 6927  O   GLY C 142    18374   8216  11731   1605  -2199    112       O  
ATOM   6928  N   SER C 143     104.123 -65.378-205.632  1.00 93.62           N  
ANISOU 6928  N   SER C 143    17166   7505  10898   1612  -2127    206       N  
ATOM   6929  CA  SER C 143     104.243 -66.311-204.518  1.00 88.72           C  
ANISOU 6929  CA  SER C 143    16663   6785  10260   1595  -2221    274       C  
ATOM   6930  C   SER C 143     103.077 -67.280-204.394  1.00 89.02           C  
ANISOU 6930  C   SER C 143    16903   6686  10235   1390  -2309    327       C  
ATOM   6931  O   SER C 143     102.000 -67.051-204.955  1.00 82.09           O  
ANISOU 6931  O   SER C 143    16042   5814   9335   1218  -2297    333       O  
ATOM   6932  CB  SER C 143     104.362 -65.535-203.205  1.00 86.80           C  
ANISOU 6932  CB  SER C 143    16278   6649  10052   1558  -2203    359       C  
ATOM   6933  OG  SER C 143     105.620 -64.904-203.099  1.00 94.66           O  
ANISOU 6933  OG  SER C 143    17113   7747  11108   1767  -2151    319       O  
ATOM   6934  N   GLN C 144     103.302 -68.369-203.651  1.00 89.19           N  
ANISOU 6934  N   GLN C 144    17078   6583  10229   1405  -2402    367       N  
ATOM   6935  CA  GLN C 144     102.197 -69.176-203.147  1.00 91.69           C  
ANISOU 6935  CA  GLN C 144    17560   6787  10490   1186  -2484    446       C  
ATOM   6936  C   GLN C 144     101.242 -68.322-202.328  1.00 84.43           C  
ANISOU 6936  C   GLN C 144    16528   5972   9579    975  -2445    543       C  
ATOM   6937  O   GLN C 144     100.019 -68.484-202.413  1.00 85.87           O  
ANISOU 6937  O   GLN C 144    16773   6123   9732    754  -2464    588       O  
ATOM   6938  CB  GLN C 144     102.731 -70.326-202.290  1.00 96.89           C  
ANISOU 6938  CB  GLN C 144    18379   7314  11122   1251  -2583    482       C  
ATOM   6939  CG  GLN C 144     103.451 -71.408-203.060  1.00108.16           C  
ANISOU 6939  CG  GLN C 144    19964   8602  12527   1424  -2641    398       C  
ATOM   6940  CD  GLN C 144     102.519 -72.523-203.483  1.00120.12           C  
ANISOU 6940  CD  GLN C 144    21711   9955  13974   1273  -2727    406       C  
ATOM   6941  OE1 GLN C 144     101.450 -72.704-202.901  1.00125.78           O  
ANISOU 6941  OE1 GLN C 144    22490  10642  14659   1044  -2763    493       O  
ATOM   6942  NE2 GLN C 144     102.917 -73.276-204.502  1.00121.52           N  
ANISOU 6942  NE2 GLN C 144    22017  10029  14127   1398  -2758    317       N  
ATOM   6943  N   ALA C 145     101.787 -67.417-201.513  1.00 78.83           N  
ANISOU 6943  N   ALA C 145    15650   5389   8911   1039  -2392    576       N  
ATOM   6944  CA  ALA C 145     100.937 -66.511-200.749  1.00 80.54           C  
ANISOU 6944  CA  ALA C 145    15749   5716   9136    854  -2343    663       C  
ATOM   6945  C   ALA C 145     100.113 -65.629-201.679  1.00 76.65           C  
ANISOU 6945  C   ALA C 145    15150   5311   8662    747  -2271    634       C  
ATOM   6946  O   ALA C 145      98.962 -65.299-201.375  1.00 77.08           O  
ANISOU 6946  O   ALA C 145    15180   5401   8707    531  -2256    703       O  
ATOM   6947  CB  ALA C 145     101.785 -65.659-199.805  1.00 73.22           C  
ANISOU 6947  CB  ALA C 145    14663   4911   8248    966  -2301    693       C  
ATOM   6948  N   HIS C 146     100.681 -65.259-202.831  1.00 73.27           N  
ANISOU 6948  N   HIS C 146    14661   4918   8258    896  -2226    533       N  
ATOM   6949  CA  HIS C 146      99.968 -64.414-203.788  1.00 70.45           C  
ANISOU 6949  CA  HIS C 146    14212   4641   7916    810  -2163    498       C  
ATOM   6950  C   HIS C 146      98.744 -65.137-204.348  1.00 70.34           C  
ANISOU 6950  C   HIS C 146    14345   4524   7858    613  -2222    510       C  
ATOM   6951  O   HIS C 146      97.640 -64.582-204.389  1.00 63.35           O  
ANISOU 6951  O   HIS C 146    13397   3694   6979    421  -2199    554       O  
ATOM   6952  CB  HIS C 146     100.931 -63.995-204.907  1.00 70.40           C  
ANISOU 6952  CB  HIS C 146    14134   4681   7935   1023  -2105    384       C  
ATOM   6953  CG  HIS C 146     100.438 -62.871-205.773  1.00 69.74           C  
ANISOU 6953  CG  HIS C 146    13920   4707   7871    971  -2026    348       C  
ATOM   6954  ND1 HIS C 146     101.232 -62.277-206.730  1.00 71.43           N  
ANISOU 6954  ND1 HIS C 146    14045   4988   8108   1143  -1954    254       N  
ATOM   6955  CD2 HIS C 146      99.240 -62.240-205.838  1.00 67.35           C  
ANISOU 6955  CD2 HIS C 146    13562   4458   7571    768  -2007    393       C  
ATOM   6956  CE1 HIS C 146     100.550 -61.326-207.343  1.00 67.66           C  
ANISOU 6956  CE1 HIS C 146    13472   4596   7639   1049  -1899    243       C  
ATOM   6957  NE2 HIS C 146      99.336 -61.287-206.825  1.00 69.71           N  
ANISOU 6957  NE2 HIS C 146    13748   4849   7890    824  -1933    326       N  
ATOM   6958  N   GLU C 147      98.910 -66.397-204.747  1.00 76.85           N  
ANISOU 6958  N   GLU C 147    15364   5196   8640    654  -2303    476       N  
ATOM   6959  CA  GLU C 147      97.808 -67.109-205.386  1.00 76.08           C  
ANISOU 6959  CA  GLU C 147    15410   4997   8499    478  -2367    479       C  
ATOM   6960  C   GLU C 147      96.697 -67.440-204.394  1.00 73.32           C  
ANISOU 6960  C   GLU C 147    15108   4618   8134    231  -2411    595       C  
ATOM   6961  O   GLU C 147      95.513 -67.362-204.740  1.00 71.08           O  
ANISOU 6961  O   GLU C 147    14828   4336   7845     28  -2423    623       O  
ATOM   6962  CB  GLU C 147      98.331 -68.376-206.059  1.00 81.10           C  
ANISOU 6962  CB  GLU C 147    16251   5475   9088    596  -2443    410       C  
ATOM   6963  CG  GLU C 147      99.640 -68.177-206.806  1.00 95.05           C  
ANISOU 6963  CG  GLU C 147    17975   7269  10872    867  -2394    304       C  
ATOM   6964  CD  GLU C 147      99.509 -67.291-208.038  1.00114.97           C  
ANISOU 6964  CD  GLU C 147    20396   9883  13406    893  -2319    227       C  
ATOM   6965  OE1 GLU C 147      98.371 -66.952-208.433  1.00118.59           O  
ANISOU 6965  OE1 GLU C 147    20840  10364  13855    703  -2323    249       O  
ATOM   6966  OE2 GLU C 147     100.558 -66.938-208.620  1.00125.16           O  
ANISOU 6966  OE2 GLU C 147    21619  11223  14715   1105  -2256    145       O  
ATOM   6967  N   GLN C 148      97.049 -67.808-203.158  1.00 74.10           N  
ANISOU 6967  N   GLN C 148    15240   4691   8225    242  -2435    665       N  
ATOM   6968  CA  GLN C 148      96.023 -68.150-202.175  1.00 74.18           C  
ANISOU 6968  CA  GLN C 148    15300   4674   8213      7  -2467    778       C  
ATOM   6969  C   GLN C 148      95.127 -66.953-201.895  1.00 69.07           C  
ANISOU 6969  C   GLN C 148    14465   4177   7602   -157  -2384    835       C  
ATOM   6970  O   GLN C 148      93.898 -67.080-201.843  1.00 67.74           O  
ANISOU 6970  O   GLN C 148    14313   3999   7425   -388  -2398    894       O  
ATOM   6971  CB  GLN C 148      96.664 -68.653-200.877  1.00 80.78           C  
ANISOU 6971  CB  GLN C 148    16199   5467   9029     66  -2500    841       C  
ATOM   6972  CG  GLN C 148      95.662 -69.213-199.848  1.00 92.98           C  
ANISOU 6972  CG  GLN C 148    17833   6960  10534   -172  -2539    958       C  
ATOM   6973  CD  GLN C 148      95.294 -68.234-198.728  1.00101.79           C  
ANISOU 6973  CD  GLN C 148    18791   8218  11669   -278  -2460   1050       C  
ATOM   6974  OE1 GLN C 148      95.038 -67.050-198.966  1.00108.50           O  
ANISOU 6974  OE1 GLN C 148    19455   9209  12562   -299  -2374   1041       O  
ATOM   6975  NE2 GLN C 148      95.262 -68.737-197.498  1.00 95.90           N  
ANISOU 6975  NE2 GLN C 148    18126   7429  10883   -344  -2490   1138       N  
ATOM   6976  N   ARG C 149      95.732 -65.776-201.720  1.00 65.40           N  
ANISOU 6976  N   ARG C 149    13816   3852   7180    -41  -2298    819       N  
ATOM   6977  CA  ARG C 149      94.947 -64.579-201.448  1.00 65.10           C  
ANISOU 6977  CA  ARG C 149    13598   3960   7177   -180  -2217    870       C  
ATOM   6978  C   ARG C 149      94.018 -64.256-202.615  1.00 67.10           C  
ANISOU 6978  C   ARG C 149    13816   4232   7447   -295  -2209    831       C  
ATOM   6979  O   ARG C 149      92.835 -63.959-202.411  1.00 62.75           O  
ANISOU 6979  O   ARG C 149    13210   3724   6906   -513  -2194    896       O  
ATOM   6980  CB  ARG C 149      95.883 -63.407-201.145  1.00 63.12           C  
ANISOU 6980  CB  ARG C 149    13170   3847   6966    -11  -2135    848       C  
ATOM   6981  CG  ARG C 149      95.185 -62.157-200.662  1.00 62.06           C  
ANISOU 6981  CG  ARG C 149    12855   3862   6862   -138  -2051    909       C  
ATOM   6982  CD  ARG C 149      94.265 -62.452-199.484  1.00 60.63           C  
ANISOU 6982  CD  ARG C 149    12708   3676   6653   -352  -2057   1028       C  
ATOM   6983  NE  ARG C 149      93.525 -61.248-199.084  1.00 60.30           N  
ANISOU 6983  NE  ARG C 149    12491   3780   6639   -479  -1970   1085       N  
ATOM   6984  CZ  ARG C 149      92.284 -61.269-198.605  1.00 59.51           C  
ANISOU 6984  CZ  ARG C 149    12379   3702   6531   -717  -1953   1171       C  
ATOM   6985  NH1 ARG C 149      91.636 -62.427-198.483  1.00 61.37           N  
ANISOU 6985  NH1 ARG C 149    12765   3821   6732   -860  -2020   1211       N  
ATOM   6986  NH2 ARG C 149      91.684 -60.133-198.279  1.00 57.97           N  
ANISOU 6986  NH2 ARG C 149    12017   3646   6363   -813  -1867   1216       N  
ATOM   6987  N   LEU C 150      94.529 -64.329-203.847  1.00 62.94           N  
ANISOU 6987  N   LEU C 150    13322   3673   6921   -155  -2221    725       N  
ATOM   6988  CA  LEU C 150      93.677 -64.075-205.006  1.00 62.87           C  
ANISOU 6988  CA  LEU C 150    13296   3672   6918   -258  -2226    683       C  
ATOM   6989  C   LEU C 150      92.466 -64.999-205.005  1.00 64.28           C  
ANISOU 6989  C   LEU C 150    13603   3752   7069   -491  -2307    738       C  
ATOM   6990  O   LEU C 150      91.326 -64.550-205.171  1.00 63.81           O  
ANISOU 6990  O   LEU C 150    13464   3747   7033   -685  -2298    777       O  
ATOM   6991  CB  LEU C 150      94.483 -64.229-206.295  1.00 66.13           C  
ANISOU 6991  CB  LEU C 150    13765   4044   7316    -64  -2233    561       C  
ATOM   6992  CG  LEU C 150      95.464 -63.094-206.620  1.00 63.26           C  
ANISOU 6992  CG  LEU C 150    13243   3804   6990    134  -2139    497       C  
ATOM   6993  CD1 LEU C 150      96.351 -63.511-207.780  1.00 71.16           C  
ANISOU 6993  CD1 LEU C 150    14330   4745   7965    332  -2146    382       C  
ATOM   6994  CD2 LEU C 150      94.761 -61.754-206.927  1.00 58.87           C  
ANISOU 6994  CD2 LEU C 150    12508   3385   6475     36  -2070    507       C  
ATOM   6995  N   GLN C 151      92.691 -66.295-204.763  1.00 68.78           N  
ANISOU 6995  N   GLN C 151    14365   4177   7592   -478  -2390    747       N  
ATOM   6996  CA  GLN C 151      91.589 -67.250-204.773  1.00 73.15           C  
ANISOU 6996  CA  GLN C 151    15053   4627   8116   -697  -2473    798       C  
ATOM   6997  C   GLN C 151      90.659 -67.056-203.581  1.00 68.20           C  
ANISOU 6997  C   GLN C 151    14353   4056   7503   -917  -2447    923       C  
ATOM   6998  O   GLN C 151      89.459 -67.327-203.689  1.00 69.60           O  
ANISOU 6998  O   GLN C 151    14546   4216   7684  -1143  -2480    972       O  
ATOM   6999  CB  GLN C 151      92.131 -68.681-204.801  1.00 90.10           C  
ANISOU 6999  CB  GLN C 151    17432   6597  10204   -617  -2568    775       C  
ATOM   7000  CG  GLN C 151      92.534 -69.177-206.191  1.00100.14           C  
ANISOU 7000  CG  GLN C 151    18822   7782  11446   -489  -2618    662       C  
ATOM   7001  CD  GLN C 151      93.321 -68.145-206.985  1.00104.11           C  
ANISOU 7001  CD  GLN C 151    19189   8392  11978   -294  -2536    569       C  
ATOM   7002  OE1 GLN C 151      92.762 -67.421-207.811  1.00108.79           O  
ANISOU 7002  OE1 GLN C 151    19689   9057  12589   -355  -2508    538       O  
ATOM   7003  NE2 GLN C 151      94.624 -68.072-206.737  1.00103.45           N  
ANISOU 7003  NE2 GLN C 151    19090   8319  11899    -61  -2500    527       N  
ATOM   7004  N   GLU C 152      91.185 -66.603-202.442  1.00 68.56           N  
ANISOU 7004  N   GLU C 152    14319   4172   7557   -859  -2386    976       N  
ATOM   7005  CA  GLU C 152      90.318 -66.320-201.301  1.00 74.08           C  
ANISOU 7005  CA  GLU C 152    14942   4941   8265  -1063  -2344   1093       C  
ATOM   7006  C   GLU C 152      89.333 -65.201-201.632  1.00 65.81           C  
ANISOU 7006  C   GLU C 152    13703   4031   7272  -1208  -2275   1112       C  
ATOM   7007  O   GLU C 152      88.134 -65.308-201.348  1.00 66.50           O  
ANISOU 7007  O   GLU C 152    13762   4135   7368  -1444  -2275   1187       O  
ATOM   7008  CB  GLU C 152      91.157 -65.953-200.073  1.00 68.16           C  
ANISOU 7008  CB  GLU C 152    14142   4248   7507   -951  -2291   1137       C  
ATOM   7009  CG  GLU C 152      91.206 -67.020-199.000  1.00 73.71           C  
ANISOU 7009  CG  GLU C 152    15004   4847   8156  -1009  -2345   1213       C  
ATOM   7010  CD  GLU C 152      91.683 -66.455-197.673  1.00 92.09           C  
ANISOU 7010  CD  GLU C 152    17252   7263  10475   -965  -2283   1280       C  
ATOM   7011  OE1 GLU C 152      92.229 -65.328-197.679  1.00 86.11           O  
ANISOU 7011  OE1 GLU C 152    16332   6631   9753   -842  -2209   1249       O  
ATOM   7012  OE2 GLU C 152      91.500 -67.125-196.630  1.00100.89           O  
ANISOU 7012  OE2 GLU C 152    18469   8323  11542  -1057  -2308   1363       O  
ATOM   7013  N   VAL C 153      89.826 -64.127-202.253  1.00 63.83           N  
ANISOU 7013  N   VAL C 153    13314   3879   7058  -1069  -2217   1043       N  
ATOM   7014  CA  VAL C 153      88.968 -62.993-202.597  1.00 62.30           C  
ANISOU 7014  CA  VAL C 153    12937   3817   6919  -1187  -2155   1055       C  
ATOM   7015  C   VAL C 153      87.896 -63.410-203.598  1.00 66.18           C  
ANISOU 7015  C   VAL C 153    13470   4256   7419  -1351  -2222   1038       C  
ATOM   7016  O   VAL C 153      86.721 -63.049-203.450  1.00 63.23           O  
ANISOU 7016  O   VAL C 153    12994   3950   7081  -1563  -2203   1100       O  
ATOM   7017  CB  VAL C 153      89.820 -61.820-203.114  1.00 67.43           C  
ANISOU 7017  CB  VAL C 153    13453   4567   7600   -988  -2088    979       C  
ATOM   7018  CG1 VAL C 153      88.940 -60.717-203.687  1.00 60.70           C  
ANISOU 7018  CG1 VAL C 153    12433   3830   6800  -1099  -2042    978       C  
ATOM   7019  CG2 VAL C 153      90.681 -61.260-201.988  1.00 69.39           C  
ANISOU 7019  CG2 VAL C 153    13626   4892   7848   -867  -2019   1016       C  
ATOM   7020  N   GLU C 154      88.271 -64.193-204.615  1.00 65.47           N  
ANISOU 7020  N   GLU C 154    13532   4048   7297  -1259  -2304    954       N  
ATOM   7021  CA  GLU C 154      87.287 -64.692-205.572  1.00 65.90           C  
ANISOU 7021  CA  GLU C 154    13648   4040   7350  -1412  -2384    936       C  
ATOM   7022  C   GLU C 154      86.187 -65.484-204.873  1.00 73.15           C  
ANISOU 7022  C   GLU C 154    14621   4910   8262  -1663  -2427   1038       C  
ATOM   7023  O   GLU C 154      84.997 -65.274-205.131  1.00 70.85           O  
ANISOU 7023  O   GLU C 154    14247   4663   8009  -1868  -2439   1075       O  
ATOM   7024  CB  GLU C 154      87.967 -65.564-206.630  1.00 68.88           C  
ANISOU 7024  CB  GLU C 154    14212   4283   7675  -1261  -2465    835       C  
ATOM   7025  CG  GLU C 154      88.946 -64.822-207.519  1.00 86.90           C  
ANISOU 7025  CG  GLU C 154    16442   6614   9960  -1029  -2420    728       C  
ATOM   7026  CD  GLU C 154      89.553 -65.716-208.589  1.00104.05           C  
ANISOU 7026  CD  GLU C 154    18801   8657  12075   -891  -2493    630       C  
ATOM   7027  OE1 GLU C 154      88.840 -66.595-209.128  1.00108.28           O  
ANISOU 7027  OE1 GLU C 154    19473   9089  12579  -1017  -2588    629       O  
ATOM   7028  OE2 GLU C 154      90.753 -65.543-208.884  1.00105.87           O  
ANISOU 7028  OE2 GLU C 154    19043   8892  12292   -655  -2453    554       O  
ATOM   7029  N   ALA C 155      86.567 -66.417-203.996  1.00 68.64           N  
ANISOU 7029  N   ALA C 155    14189   4246   7646  -1652  -2454   1084       N  
ATOM   7030  CA  ALA C 155      85.560 -67.231-203.325  1.00 70.57           C  
ANISOU 7030  CA  ALA C 155    14499   4437   7878  -1891  -2493   1182       C  
ATOM   7031  C   ALA C 155      84.683 -66.378-202.418  1.00 69.76           C  
ANISOU 7031  C   ALA C 155    14200   4483   7823  -2071  -2397   1281       C  
ATOM   7032  O   ALA C 155      83.460 -66.552-202.382  1.00 70.78           O  
ANISOU 7032  O   ALA C 155    14285   4630   7978  -2308  -2410   1343       O  
ATOM   7033  CB  ALA C 155      86.232 -68.356-202.533  1.00 72.25           C  
ANISOU 7033  CB  ALA C 155    14906   4520   8026  -1827  -2539   1211       C  
ATOM   7034  N   GLU C 156      85.288 -65.440-201.691  1.00 68.01           N  
ANISOU 7034  N   GLU C 156    13854   4372   7614  -1962  -2298   1297       N  
ATOM   7035  CA  GLU C 156      84.524 -64.623-200.753  1.00 71.44           C  
ANISOU 7035  CA  GLU C 156    14109   4950   8084  -2120  -2197   1392       C  
ATOM   7036  C   GLU C 156      83.512 -63.739-201.479  1.00 68.76           C  
ANISOU 7036  C   GLU C 156    13587   4722   7817  -2251  -2169   1384       C  
ATOM   7037  O   GLU C 156      82.356 -63.632-201.054  1.00 67.05           O  
ANISOU 7037  O   GLU C 156    13271   4573   7634  -2477  -2136   1464       O  
ATOM   7038  CB  GLU C 156      85.474 -63.781-199.899  1.00 71.19           C  
ANISOU 7038  CB  GLU C 156    13994   5010   8045  -1955  -2105   1401       C  
ATOM   7039  CG  GLU C 156      84.770 -63.008-198.806  1.00 78.68           C  
ANISOU 7039  CG  GLU C 156    14782   6101   9012  -2106  -1995   1501       C  
ATOM   7040  CD  GLU C 156      85.720 -62.448-197.761  1.00 86.28           C  
ANISOU 7040  CD  GLU C 156    15711   7128   9944  -1958  -1922   1525       C  
ATOM   7041  OE1 GLU C 156      86.955 -62.541-197.937  1.00 85.80           O  
ANISOU 7041  OE1 GLU C 156    15724   7014   9861  -1729  -1954   1458       O  
ATOM   7042  OE2 GLU C 156      85.217 -61.911-196.755  1.00 93.35           O  
ANISOU 7042  OE2 GLU C 156    16500   8132  10837  -2073  -1831   1610       O  
ATOM   7043  N   VAL C 157      83.912 -63.139-202.602  1.00 65.00           N  
ANISOU 7043  N   VAL C 157    13067   4264   7366  -2114  -2186   1286       N  
ATOM   7044  CA  VAL C 157      82.978 -62.313-203.367  1.00 64.20           C  
ANISOU 7044  CA  VAL C 157    12802   4260   7333  -2229  -2176   1273       C  
ATOM   7045  C   VAL C 157      81.880 -63.167-203.988  1.00 66.17           C  
ANISOU 7045  C   VAL C 157    13115   4434   7592  -2430  -2273   1286       C  
ATOM   7046  O   VAL C 157      80.730 -62.725-204.098  1.00 66.30           O  
ANISOU 7046  O   VAL C 157    12981   4539   7670  -2621  -2259   1327       O  
ATOM   7047  CB  VAL C 157      83.738 -61.487-204.423  1.00 67.14           C  
ANISOU 7047  CB  VAL C 157    13131   4662   7719  -2025  -2173   1164       C  
ATOM   7048  CG1 VAL C 157      82.787 -60.966-205.505  1.00 68.95           C  
ANISOU 7048  CG1 VAL C 157    13254   4941   8003  -2138  -2209   1131       C  
ATOM   7049  CG2 VAL C 157      84.455 -60.324-203.760  1.00 60.29           C  
ANISOU 7049  CG2 VAL C 157    12126   3915   6866  -1890  -2060   1171       C  
ATOM   7050  N   ALA C 158      82.195 -64.404-204.384  1.00 67.85           N  
ANISOU 7050  N   ALA C 158    13545   4486   7747  -2394  -2375   1252       N  
ATOM   7051  CA  ALA C 158      81.150 -65.284-204.892  1.00 69.93           C  
ANISOU 7051  CA  ALA C 158    13882   4672   8015  -2593  -2473   1272       C  
ATOM   7052  C   ALA C 158      80.191 -65.679-203.777  1.00 78.01           C  
ANISOU 7052  C   ALA C 158    14864   5724   9054  -2832  -2439   1395       C  
ATOM   7053  O   ALA C 158      78.973 -65.745-203.986  1.00 75.93           O  
ANISOU 7053  O   ALA C 158    14513   5497   8839  -3051  -2464   1438       O  
ATOM   7054  CB  ALA C 158      81.769 -66.524-205.548  1.00 71.46           C  
ANISOU 7054  CB  ALA C 158    14334   4683   8136  -2489  -2588   1207       C  
ATOM   7055  N   ALA C 159      80.726 -65.924-202.579  1.00 71.59           N  
ANISOU 7055  N   ALA C 159    14103   4899   8198  -2791  -2381   1453       N  
ATOM   7056  CA  ALA C 159      79.889 -66.315-201.452  1.00 80.41           C  
ANISOU 7056  CA  ALA C 159    15193   6044   9316  -3009  -2336   1572       C  
ATOM   7057  C   ALA C 159      79.034 -65.154-200.954  1.00 84.96           C  
ANISOU 7057  C   ALA C 159    15504   6813   9965  -3146  -2216   1634       C  
ATOM   7058  O   ALA C 159      77.857 -65.341-200.625  1.00 92.34           O  
ANISOU 7058  O   ALA C 159    16353   7795  10936  -3384  -2197   1710       O  
ATOM   7059  CB  ALA C 159      80.767 -66.848-200.319  1.00 74.45           C  
ANISOU 7059  CB  ALA C 159    14575   5225   8487  -2911  -2309   1613       C  
ATOM   7060  N   THR C 160      79.597 -63.949-200.887  1.00 77.33           N  
ANISOU 7060  N   THR C 160    14399   5961   9021  -3001  -2132   1602       N  
ATOM   7061  CA  THR C 160      78.950 -62.884-200.135  1.00 83.68           C  
ANISOU 7061  CA  THR C 160    14972   6945   9877  -3110  -2002   1670       C  
ATOM   7062  C   THR C 160      78.755 -61.578-200.888  1.00 81.09           C  
ANISOU 7062  C   THR C 160    14442   6745   9624  -3068  -1967   1618       C  
ATOM   7063  O   THR C 160      78.067 -60.696-200.364  1.00 85.52           O  
ANISOU 7063  O   THR C 160    14796   7460  10236  -3178  -1864   1672       O  
ATOM   7064  CB  THR C 160      79.738 -62.588-198.851  1.00 84.61           C  
ANISOU 7064  CB  THR C 160    15102   7105   9940  -3007  -1902   1718       C  
ATOM   7065  OG1 THR C 160      78.866 -61.982-197.891  1.00100.72           O  
ANISOU 7065  OG1 THR C 160    16963   9296  12009  -3179  -1778   1811       O  
ATOM   7066  CG2 THR C 160      80.893 -61.650-199.144  1.00 65.56           C  
ANISOU 7066  CG2 THR C 160    12652   4732   7524  -2754  -1874   1641       C  
ATOM   7067  N   GLY C 161      79.331 -61.415-202.078  1.00 74.14           N  
ANISOU 7067  N   GLY C 161    13614   5809   8747  -2912  -2044   1513       N  
ATOM   7068  CA  GLY C 161      79.204 -60.181-202.824  1.00 68.77           C  
ANISOU 7068  CA  GLY C 161    12758   5239   8131  -2862  -2018   1460       C  
ATOM   7069  C   GLY C 161      80.286 -59.155-202.563  1.00 68.60           C  
ANISOU 7069  C   GLY C 161    12684   5285   8096  -2646  -1936   1425       C  
ATOM   7070  O   GLY C 161      80.375 -58.169-203.306  1.00 71.56           O  
ANISOU 7070  O   GLY C 161    12947   5729   8514  -2570  -1927   1367       O  
ATOM   7071  N   THR C 162      81.101 -59.346-201.529  1.00 67.90           N  
ANISOU 7071  N   THR C 162    12671   5179   7949  -2548  -1880   1460       N  
ATOM   7072  CA  THR C 162      82.172 -58.418-201.173  1.00 60.93           C  
ANISOU 7072  CA  THR C 162    11740   4361   7050  -2343  -1805   1433       C  
ATOM   7073  C   THR C 162      83.331 -59.252-200.633  1.00 62.82           C  
ANISOU 7073  C   THR C 162    12169   4488   7210  -2183  -1831   1424       C  
ATOM   7074  O   THR C 162      83.328 -60.482-200.749  1.00 61.71           O  
ANISOU 7074  O   THR C 162    12201   4214   7032  -2215  -1915   1422       O  
ATOM   7075  CB  THR C 162      81.654 -57.363-200.176  1.00 62.19           C  
ANISOU 7075  CB  THR C 162    11702   4690   7240  -2439  -1674   1514       C  
ATOM   7076  OG1 THR C 162      82.685 -56.415-199.872  1.00 60.90           O  
ANISOU 7076  OG1 THR C 162    11491   4590   7059  -2240  -1607   1487       O  
ATOM   7077  CG2 THR C 162      81.158 -58.016-198.890  1.00 67.78           C  
ANISOU 7077  CG2 THR C 162    12441   5403   7908  -2595  -1625   1620       C  
ATOM   7078  N   TYR C 163      84.332 -58.595-200.044  1.00 64.15           N  
ANISOU 7078  N   TYR C 163    12307   4710   7356  -2008  -1765   1416       N  
ATOM   7079  CA  TYR C 163      85.389 -59.348-199.369  1.00 68.31           C  
ANISOU 7079  CA  TYR C 163    12992   5146   7815  -1867  -1788   1418       C  
ATOM   7080  C   TYR C 163      86.015 -58.494-198.277  1.00 66.96           C  
ANISOU 7080  C   TYR C 163    12734   5082   7624  -1774  -1691   1458       C  
ATOM   7081  O   TYR C 163      85.805 -57.280-198.208  1.00 60.16           O  
ANISOU 7081  O   TYR C 163    11703   4356   6800  -1780  -1609   1467       O  
ATOM   7082  CB  TYR C 163      86.474 -59.825-200.337  1.00 60.44           C  
ANISOU 7082  CB  TYR C 163    12127   4037   6800  -1649  -1870   1308       C  
ATOM   7083  CG  TYR C 163      87.336 -58.710-200.886  1.00 65.01           C  
ANISOU 7083  CG  TYR C 163    12602   4693   7406  -1446  -1826   1231       C  
ATOM   7084  CD1 TYR C 163      86.873 -57.895-201.916  1.00 60.49           C  
ANISOU 7084  CD1 TYR C 163    11916   4182   6885  -1468  -1817   1181       C  
ATOM   7085  CD2 TYR C 163      88.618 -58.484-200.395  1.00 61.52           C  
ANISOU 7085  CD2 TYR C 163    12175   4261   6937  -1233  -1798   1207       C  
ATOM   7086  CE1 TYR C 163      87.653 -56.877-202.431  1.00 55.74           C  
ANISOU 7086  CE1 TYR C 163    11226   3649   6305  -1287  -1776   1112       C  
ATOM   7087  CE2 TYR C 163      89.411 -57.467-200.906  1.00 63.58           C  
ANISOU 7087  CE2 TYR C 163    12336   4596   7225  -1052  -1756   1137       C  
ATOM   7088  CZ  TYR C 163      88.922 -56.670-201.931  1.00 61.96           C  
ANISOU 7088  CZ  TYR C 163    12027   4448   7066  -1080  -1742   1090       C  
ATOM   7089  OH  TYR C 163      89.695 -55.655-202.450  1.00 58.28           O  
ANISOU 7089  OH  TYR C 163    11467   4054   6623   -905  -1697   1022       O  
ATOM   7090  N   GLN C 164      86.824 -59.154-197.446  1.00 66.44           N  
ANISOU 7090  N   GLN C 164    12795   4950   7498  -1680  -1709   1479       N  
ATOM   7091  CA  GLN C 164      87.470 -58.548-196.288  1.00 66.18           C  
ANISOU 7091  CA  GLN C 164    12713   5001   7431  -1594  -1636   1523       C  
ATOM   7092  C   GLN C 164      88.966 -58.399-196.525  1.00 58.03           C  
ANISOU 7092  C   GLN C 164    11722   3938   6390  -1318  -1667   1442       C  
ATOM   7093  O   GLN C 164      89.624 -59.341-196.977  1.00 62.81           O  
ANISOU 7093  O   GLN C 164    12473   4415   6978  -1209  -1753   1388       O  
ATOM   7094  CB  GLN C 164      87.241 -59.392-195.032  1.00 66.62           C  
ANISOU 7094  CB  GLN C 164    12877   5013   7422  -1705  -1635   1616       C  
ATOM   7095  CG  GLN C 164      85.793 -59.541-194.662  1.00 70.13           C  
ANISOU 7095  CG  GLN C 164    13269   5502   7874  -1979  -1588   1703       C  
ATOM   7096  CD  GLN C 164      85.121 -58.206-194.440  1.00 71.72           C  
ANISOU 7096  CD  GLN C 164    13254   5882   8115  -2065  -1469   1736       C  
ATOM   7097  OE1 GLN C 164      85.717 -57.276-193.890  1.00 79.20           O  
ANISOU 7097  OE1 GLN C 164    14120   6926   9046  -1953  -1401   1738       O  
ATOM   7098  NE2 GLN C 164      83.872 -58.099-194.873  1.00 80.41           N  
ANISOU 7098  NE2 GLN C 164    14255   7029   9267  -2266  -1447   1761       N  
ATOM   7099  N   LEU C 165      89.497 -57.222-196.208  1.00 55.19           N  
ANISOU 7099  N   LEU C 165    11229   3699   6041  -1209  -1595   1435       N  
ATOM   7100  CA  LEU C 165      90.937 -57.018-196.222  1.00 56.16           C  
ANISOU 7100  CA  LEU C 165    11368   3814   6157   -956  -1614   1371       C  
ATOM   7101  C   LEU C 165      91.583 -57.663-194.996  1.00 60.65           C  
ANISOU 7101  C   LEU C 165    12042   4339   6663   -906  -1638   1423       C  
ATOM   7102  O   LEU C 165      91.038 -57.602-193.891  1.00 63.70           O  
ANISOU 7102  O   LEU C 165    12421   4774   7010  -1041  -1592   1514       O  
ATOM   7103  CB  LEU C 165      91.262 -55.527-196.248  1.00 52.29           C  
ANISOU 7103  CB  LEU C 165    10699   3470   5697   -866  -1533   1352       C  
ATOM   7104  CG  LEU C 165      90.809 -54.759-197.496  1.00 56.23           C  
ANISOU 7104  CG  LEU C 165    11092   4017   6258   -879  -1512   1292       C  
ATOM   7105  CD1 LEU C 165      90.960 -53.249-197.312  1.00 57.49           C  
ANISOU 7105  CD1 LEU C 165    11076   4327   6439   -826  -1425   1294       C  
ATOM   7106  CD2 LEU C 165      91.597 -55.242-198.707  1.00 57.19           C  
ANISOU 7106  CD2 LEU C 165    11289   4041   6398   -711  -1581   1183       C  
ATOM   7107  N   ARG C 166      92.739 -58.298-195.201  1.00 59.97           N  
ANISOU 7107  N   ARG C 166    12056   4160   6568   -714  -1710   1363       N  
ATOM   7108  CA  ARG C 166      93.604 -58.642-194.078  1.00 61.82           C  
ANISOU 7108  CA  ARG C 166    12360   4374   6754   -617  -1735   1398       C  
ATOM   7109  C   ARG C 166      94.119 -57.362-193.429  1.00 60.93           C  
ANISOU 7109  C   ARG C 166    12096   4409   6645   -531  -1663   1410       C  
ATOM   7110  O   ARG C 166      94.207 -56.314-194.064  1.00 53.40           O  
ANISOU 7110  O   ARG C 166    11002   3550   5738   -471  -1611   1363       O  
ATOM   7111  CB  ARG C 166      94.792 -59.494-194.532  1.00 57.57           C  
ANISOU 7111  CB  ARG C 166    11937   3719   6219   -411  -1826   1321       C  
ATOM   7112  CG  ARG C 166      94.441 -60.859-195.082  1.00 60.15           C  
ANISOU 7112  CG  ARG C 166    12440   3885   6528   -473  -1910   1307       C  
ATOM   7113  CD  ARG C 166      95.697 -61.636-195.481  1.00 60.30           C  
ANISOU 7113  CD  ARG C 166    12565   3797   6548   -251  -1991   1229       C  
ATOM   7114  NE  ARG C 166      95.379 -62.989-195.936  1.00 62.72           N  
ANISOU 7114  NE  ARG C 166    13059   3943   6828   -308  -2077   1218       N  
ATOM   7115  CZ  ARG C 166      96.235 -63.792-196.566  1.00 70.95           C  
ANISOU 7115  CZ  ARG C 166    14212   4875   7871   -141  -2149   1141       C  
ATOM   7116  NH1 ARG C 166      97.473 -63.382-196.828  1.00 69.74           N  
ANISOU 7116  NH1 ARG C 166    13987   4760   7749     93  -2140   1070       N  
ATOM   7117  NH2 ARG C 166      95.853 -65.005-196.942  1.00 72.69           N  
ANISOU 7117  NH2 ARG C 166    14610   4948   8060   -210  -2227   1137       N  
ATOM   7118  N   GLU C 167      94.479 -57.452-192.147  1.00 61.76           N  
ANISOU 7118  N   GLU C 167    12239   4532   6694   -522  -1664   1473       N  
ATOM   7119  CA  GLU C 167      94.887 -56.246-191.430  1.00 60.90           C  
ANISOU 7119  CA  GLU C 167    11996   4566   6576   -460  -1599   1492       C  
ATOM   7120  C   GLU C 167      96.097 -55.591-192.088  1.00 60.24           C  
ANISOU 7120  C   GLU C 167    11819   4523   6546   -225  -1612   1400       C  
ATOM   7121  O   GLU C 167      96.209 -54.362-192.112  1.00 56.10           O  
ANISOU 7121  O   GLU C 167    11146   4126   6044   -186  -1547   1387       O  
ATOM   7122  CB  GLU C 167      95.181 -56.572-189.963  1.00 66.44           C  
ANISOU 7122  CB  GLU C 167    12778   5264   7201   -476  -1615   1568       C  
ATOM   7123  CG  GLU C 167      94.660 -55.533-188.981  1.00 79.00           C  
ANISOU 7123  CG  GLU C 167    14267   7001   8748   -579  -1517   1638       C  
ATOM   7124  CD  GLU C 167      94.543 -56.084-187.571  1.00 95.82           C  
ANISOU 7124  CD  GLU C 167    16510   9109  10786   -664  -1525   1726       C  
ATOM   7125  OE1 GLU C 167      95.489 -56.769-187.126  1.00102.38           O  
ANISOU 7125  OE1 GLU C 167    17449   9858  11592   -542  -1614   1719       O  
ATOM   7126  OE2 GLU C 167      93.503 -55.849-186.917  1.00100.06           O  
ANISOU 7126  OE2 GLU C 167    17030   9711  11277   -854  -1442   1803       O  
ATOM   7127  N   SER C 168      97.006 -56.392-192.648  1.00 61.94           N  
ANISOU 7127  N   SER C 168    12116   4633   6784    -67  -1693   1332       N  
ATOM   7128  CA  SER C 168      98.180 -55.807-193.290  1.00 58.21           C  
ANISOU 7128  CA  SER C 168    11545   4205   6366    156  -1697   1243       C  
ATOM   7129  C   SER C 168      97.810 -55.124-194.603  1.00 56.62           C  
ANISOU 7129  C   SER C 168    11243   4048   6222    157  -1645   1176       C  
ATOM   7130  O   SER C 168      98.374 -54.077-194.943  1.00 51.19           O  
ANISOU 7130  O   SER C 168    10416   3461   5574    273  -1601   1130       O  
ATOM   7131  CB  SER C 168      99.239 -56.882-193.518  1.00 56.75           C  
ANISOU 7131  CB  SER C 168    11473   3900   6190    324  -1789   1190       C  
ATOM   7132  OG  SER C 168      98.754 -57.888-194.387  1.00 62.57           O  
ANISOU 7132  OG  SER C 168    12333   4512   6929    269  -1829   1159       O  
ATOM   7133  N   GLU C 169      96.865 -55.701-195.353  1.00 57.05           N  
ANISOU 7133  N   GLU C 169    11369   4027   6281     26  -1655   1171       N  
ATOM   7134  CA  GLU C 169      96.380 -55.052-196.574  1.00 50.74           C  
ANISOU 7134  CA  GLU C 169    10483   3267   5529      4  -1612   1114       C  
ATOM   7135  C   GLU C 169      95.670 -53.741-196.272  1.00 53.01           C  
ANISOU 7135  C   GLU C 169    10620   3697   5825   -102  -1524   1160       C  
ATOM   7136  O   GLU C 169      95.726 -52.807-197.081  1.00 53.49           O  
ANISOU 7136  O   GLU C 169    10567   3829   5929    -48  -1481   1107       O  
ATOM   7137  CB  GLU C 169      95.441 -55.988-197.339  1.00 54.47           C  
ANISOU 7137  CB  GLU C 169    11070   3628   5998   -135  -1653   1107       C  
ATOM   7138  CG  GLU C 169      96.075 -57.278-197.816  1.00 53.27           C  
ANISOU 7138  CG  GLU C 169    11076   3331   5834    -31  -1740   1052       C  
ATOM   7139  CD  GLU C 169      95.041 -58.350-198.148  1.00 61.14           C  
ANISOU 7139  CD  GLU C 169    12213   4210   6807   -208  -1793   1076       C  
ATOM   7140  OE1 GLU C 169      93.842 -58.131-197.861  1.00 64.56           O  
ANISOU 7140  OE1 GLU C 169    12614   4680   7235   -419  -1762   1145       O  
ATOM   7141  OE2 GLU C 169      95.427 -59.411-198.688  1.00 62.81           O  
ANISOU 7141  OE2 GLU C 169    12564   4296   7005   -137  -1866   1026       O  
ATOM   7142  N   LEU C 170      94.981 -53.653-195.133  1.00 52.38           N  
ANISOU 7142  N   LEU C 170    10541   3659   5701   -255  -1494   1257       N  
ATOM   7143  CA  LEU C 170      94.325 -52.399-194.773  1.00 54.36           C  
ANISOU 7143  CA  LEU C 170    10650   4050   5953   -351  -1404   1302       C  
ATOM   7144  C   LEU C 170      95.348 -51.318-194.439  1.00 54.96           C  
ANISOU 7144  C   LEU C 170    10613   4234   6036   -181  -1373   1276       C  
ATOM   7145  O   LEU C 170      95.207 -50.171-194.874  1.00 53.25           O  
ANISOU 7145  O   LEU C 170    10266   4116   5850   -166  -1315   1253       O  
ATOM   7146  CB  LEU C 170      93.365 -52.605-193.599  1.00 54.81           C  
ANISOU 7146  CB  LEU C 170    10739   4133   5954   -554  -1367   1411       C  
ATOM   7147  CG  LEU C 170      92.726 -51.311-193.071  1.00 55.17           C  
ANISOU 7147  CG  LEU C 170    10641   4333   5988   -649  -1264   1462       C  
ATOM   7148  CD1 LEU C 170      91.785 -50.714-194.108  1.00 56.25           C  
ANISOU 7148  CD1 LEU C 170    10680   4510   6184   -749  -1224   1441       C  
ATOM   7149  CD2 LEU C 170      92.012 -51.530-191.744  1.00 65.41           C  
ANISOU 7149  CD2 LEU C 170    11974   5666   7215   -817  -1217   1566       C  
ATOM   7150  N   VAL C 171      96.387 -51.670-193.679  1.00 54.04           N  
ANISOU 7150  N   VAL C 171    10544   4097   5892    -53  -1417   1278       N  
ATOM   7151  CA  VAL C 171      97.469 -50.728-193.402  1.00 55.32           C  
ANISOU 7151  CA  VAL C 171    10597   4355   6066    118  -1404   1245       C  
ATOM   7152  C   VAL C 171      98.125 -50.268-194.700  1.00 54.33           C  
ANISOU 7152  C   VAL C 171    10390   4242   6012    274  -1400   1143       C  
ATOM   7153  O   VAL C 171      98.270 -49.065-194.952  1.00 52.58           O  
ANISOU 7153  O   VAL C 171    10034   4130   5816    322  -1346   1119       O  
ATOM   7154  CB  VAL C 171      98.494 -51.365-192.448  1.00 53.94           C  
ANISOU 7154  CB  VAL C 171    10498   4139   5859    229  -1472   1260       C  
ATOM   7155  CG1 VAL C 171      99.759 -50.525-192.383  1.00 55.69           C  
ANISOU 7155  CG1 VAL C 171    10602   4446   6112    427  -1477   1209       C  
ATOM   7156  CG2 VAL C 171      97.888 -51.513-191.066  1.00 52.75           C  
ANISOU 7156  CG2 VAL C 171    10408   4009   5628     81  -1458   1362       C  
ATOM   7157  N   PHE C 172      98.537 -51.220-195.541  1.00 55.43           N  
ANISOU 7157  N   PHE C 172    10613   4269   6178    356  -1455   1080       N  
ATOM   7158  CA  PHE C 172      99.166 -50.869-196.812  1.00 53.17           C  
ANISOU 7158  CA  PHE C 172    10261   3991   5950    503  -1443    980       C  
ATOM   7159  C   PHE C 172      98.275 -49.950-197.634  1.00 50.32           C  
ANISOU 7159  C   PHE C 172     9813   3693   5614    410  -1378    966       C  
ATOM   7160  O   PHE C 172      98.749 -48.959-198.207  1.00 50.15           O  
ANISOU 7160  O   PHE C 172     9663   3762   5630    513  -1331    908       O  
ATOM   7161  CB  PHE C 172      99.499 -52.136-197.605  1.00 54.05           C  
ANISOU 7161  CB  PHE C 172    10501   3964   6070    570  -1505    920       C  
ATOM   7162  CG  PHE C 172     100.002 -51.862-199.009  1.00 57.19           C  
ANISOU 7162  CG  PHE C 172    10849   4365   6516    701  -1481    814       C  
ATOM   7163  CD1 PHE C 172     101.308 -51.446-199.225  1.00 56.06           C  
ANISOU 7163  CD1 PHE C 172    10615   4275   6410    909  -1468    750       C  
ATOM   7164  CD2 PHE C 172      99.172 -52.039-200.110  1.00 56.26           C  
ANISOU 7164  CD2 PHE C 172    10775   4199   6404    613  -1474    780       C  
ATOM   7165  CE1 PHE C 172     101.779 -51.202-200.507  1.00 54.82           C  
ANISOU 7165  CE1 PHE C 172    10414   4126   6290   1026  -1433    653       C  
ATOM   7166  CE2 PHE C 172      99.636 -51.797-201.399  1.00 54.49           C  
ANISOU 7166  CE2 PHE C 172    10517   3976   6211    732  -1448    681       C  
ATOM   7167  CZ  PHE C 172     100.944 -51.384-201.594  1.00 54.58           C  
ANISOU 7167  CZ  PHE C 172    10441   4044   6254    939  -1422    618       C  
ATOM   7168  N   GLY C 173      96.977 -50.250-197.691  1.00 53.01           N  
ANISOU 7168  N   GLY C 173    10207   3998   5936    210  -1373   1016       N  
ATOM   7169  CA  GLY C 173      96.085 -49.459-198.529  1.00 51.20           C  
ANISOU 7169  CA  GLY C 173     9868   3847   5740    114  -1314    988       C  
ATOM   7170  C   GLY C 173      95.856 -48.058-197.996  1.00 50.52           C  
ANISOU 7170  C   GLY C 173     9558   3973   5665     79  -1214    991       C  
ATOM   7171  O   GLY C 173      95.732 -47.102-198.767  1.00 46.30           O  
ANISOU 7171  O   GLY C 173     8867   3553   5171    100  -1153    925       O  
ATOM   7172  N   ALA C 174      95.780 -47.914-196.672  1.00 48.30           N  
ANISOU 7172  N   ALA C 174     9270   3742   5341     24  -1196   1068       N  
ATOM   7173  CA  ALA C 174      95.634 -46.582-196.095  1.00 43.65           C  
ANISOU 7173  CA  ALA C 174     8483   3346   4755      5  -1103   1066       C  
ATOM   7174  C   ALA C 174      96.864 -45.728-196.373  1.00 47.85           C  
ANISOU 7174  C   ALA C 174     8897   3964   5320    197  -1085    989       C  
ATOM   7175  O   ALA C 174      96.739 -44.551-196.729  1.00 49.09           O  
ANISOU 7175  O   ALA C 174     8877   4264   5511    205  -1010    940       O  
ATOM   7176  CB  ALA C 174      95.375 -46.680-194.589  1.00 46.83           C  
ANISOU 7176  CB  ALA C 174     8930   3772   5091    -85  -1092   1162       C  
ATOM   7177  N   LYS C 175      98.062 -46.305-196.223  1.00 47.31           N  
ANISOU 7177  N   LYS C 175     8922   3809   5247    354  -1155    978       N  
ATOM   7178  CA  LYS C 175      99.289 -45.570-196.528  1.00 49.25           C  
ANISOU 7178  CA  LYS C 175     9048   4131   5532    537  -1140    904       C  
ATOM   7179  C   LYS C 175      99.366 -45.196-198.007  1.00 45.19           C  
ANISOU 7179  C   LYS C 175     8458   3639   5073    595  -1104    811       C  
ATOM   7180  O   LYS C 175      99.706 -44.052-198.346  1.00 41.73           O  
ANISOU 7180  O   LYS C 175     7850   3335   4668    648  -1038    757       O  
ATOM   7181  CB  LYS C 175     100.511 -46.390-196.116  1.00 45.47           C  
ANISOU 7181  CB  LYS C 175     8687   3545   5044    695  -1231    912       C  
ATOM   7182  CG  LYS C 175     100.713 -46.452-194.589  1.00 43.21           C  
ANISOU 7182  CG  LYS C 175     8445   3271   4700    672  -1267    995       C  
ATOM   7183  CD  LYS C 175     101.956 -47.246-194.198  1.00 49.04           C  
ANISOU 7183  CD  LYS C 175     9294   3902   5436    841  -1372   1002       C  
ATOM   7184  CE  LYS C 175     102.095 -47.304-192.686  1.00 57.47           C  
ANISOU 7184  CE  LYS C 175    10407   4989   6439    804  -1411   1083       C  
ATOM   7185  NZ  LYS C 175     103.357 -47.956-192.220  1.00 53.48           N  
ANISOU 7185  NZ  LYS C 175     9928   4444   5947    957  -1494   1063       N  
ATOM   7186  N   GLN C 176      99.041 -46.138-198.902  1.00 43.92           N  
ANISOU 7186  N   GLN C 176     8429   3342   4915    579  -1147    793       N  
ATOM   7187  CA  GLN C 176      99.075 -45.822-200.332  1.00 41.91           C  
ANISOU 7187  CA  GLN C 176     8123   3102   4700    628  -1114    705       C  
ATOM   7188  C   GLN C 176      98.074 -44.736-200.695  1.00 44.65           C  
ANISOU 7188  C   GLN C 176     8318   3584   5064    503  -1036    694       C  
ATOM   7189  O   GLN C 176      98.328 -43.921-201.592  1.00 42.88           O  
ANISOU 7189  O   GLN C 176     7982   3439   4870    564   -985    623       O  
ATOM   7190  CB  GLN C 176      98.809 -47.079-201.163  1.00 43.76           C  
ANISOU 7190  CB  GLN C 176     8549   3154   4923    619  -1182    690       C  
ATOM   7191  CG  GLN C 176      99.921 -48.100-201.100  1.00 56.12           C  
ANISOU 7191  CG  GLN C 176    10261   4580   6483    783  -1256    676       C  
ATOM   7192  CD  GLN C 176     101.222 -47.602-201.704  1.00 58.42           C  
ANISOU 7192  CD  GLN C 176    10455   4930   6813    989  -1220    589       C  
ATOM   7193  OE1 GLN C 176     102.251 -47.561-201.030  1.00 68.47           O  
ANISOU 7193  OE1 GLN C 176    11694   6224   8098   1116  -1237    595       O  
ATOM   7194  NE2 GLN C 176     101.189 -47.254-202.984  1.00 61.42           N  
ANISOU 7194  NE2 GLN C 176    10792   5333   7211   1020  -1173    510       N  
ATOM   7195  N   ALA C 177      96.905 -44.733-200.053  1.00 44.57           N  
ANISOU 7195  N   ALA C 177     8306   3597   5033    328  -1027    763       N  
ATOM   7196  CA  ALA C 177      95.921 -43.717-200.399  1.00 38.99           C  
ANISOU 7196  CA  ALA C 177     7449   3018   4350    218   -958    750       C  
ATOM   7197  C   ALA C 177      96.392 -42.331-199.974  1.00 41.91           C  
ANISOU 7197  C   ALA C 177     7635   3555   4734    280   -883    727       C  
ATOM   7198  O   ALA C 177      96.119 -41.340-200.664  1.00 38.02           O  
ANISOU 7198  O   ALA C 177     7013   3161   4273    276   -830    679       O  
ATOM   7199  CB  ALA C 177      94.567 -44.055-199.786  1.00 42.48           C  
ANISOU 7199  CB  ALA C 177     7916   3452   4772     19   -958    828       C  
ATOM   7200  N   TRP C 178      97.131 -42.244-198.870  1.00 43.23           N  
ANISOU 7200  N   TRP C 178     7798   3748   4878    341   -887    759       N  
ATOM   7201  CA  TRP C 178      97.796 -40.996-198.513  1.00 38.57           C  
ANISOU 7201  CA  TRP C 178     7053   3300   4303    419   -831    729       C  
ATOM   7202  C   TRP C 178      98.895 -40.658-199.516  1.00 41.94           C  
ANISOU 7202  C   TRP C 178     7430   3736   4770    575   -825    646       C  
ATOM   7203  O   TRP C 178      98.969 -39.532-200.019  1.00 40.19           O  
ANISOU 7203  O   TRP C 178     7069   3624   4576    596   -765    598       O  
ATOM   7204  CB  TRP C 178      98.365 -41.107-197.097  1.00 35.18           C  
ANISOU 7204  CB  TRP C 178     6654   2881   3833    446   -855    784       C  
ATOM   7205  CG  TRP C 178      99.047 -39.882-196.574  1.00 41.29           C  
ANISOU 7205  CG  TRP C 178     7284   3791   4616    514   -811    759       C  
ATOM   7206  CD1 TRP C 178      99.073 -38.631-197.136  1.00 38.82           C  
ANISOU 7206  CD1 TRP C 178     6813   3596   4339    533   -745    702       C  
ATOM   7207  CD2 TRP C 178      99.803 -39.794-195.370  1.00 39.37           C  
ANISOU 7207  CD2 TRP C 178     7049   3570   4338    566   -841    793       C  
ATOM   7208  NE1 TRP C 178      99.800 -37.775-196.351  1.00 39.41           N  
ANISOU 7208  NE1 TRP C 178     6800   3766   4409    590   -729    697       N  
ATOM   7209  CE2 TRP C 178     100.265 -38.469-195.259  1.00 35.33           C  
ANISOU 7209  CE2 TRP C 178     6381   3195   3849    612   -790    751       C  
ATOM   7210  CE3 TRP C 178     100.128 -40.707-194.365  1.00 41.20           C  
ANISOU 7210  CE3 TRP C 178     7416   3717   4519    576   -912    858       C  
ATOM   7211  CZ2 TRP C 178     101.041 -38.043-194.184  1.00 41.48           C  
ANISOU 7211  CZ2 TRP C 178     7132   4027   4602    665   -813    768       C  
ATOM   7212  CZ3 TRP C 178     100.902 -40.282-193.303  1.00 44.74           C  
ANISOU 7212  CZ3 TRP C 178     7838   4221   4940    634   -936    876       C  
ATOM   7213  CH2 TRP C 178     101.342 -38.965-193.218  1.00 41.51           C  
ANISOU 7213  CH2 TRP C 178     7268   3949   4554    675   -887    830       C  
ATOM   7214  N   ARG C 179      99.749 -41.631-199.826  1.00 41.65           N  
ANISOU 7214  N   ARG C 179     7507   3583   4734    687   -885    629       N  
ATOM   7215  CA  ARG C 179     100.861 -41.418-200.745  1.00 41.36           C  
ANISOU 7215  CA  ARG C 179     7427   3553   4734    844   -871    551       C  
ATOM   7216  C   ARG C 179     100.383 -40.972-202.128  1.00 40.18           C  
ANISOU 7216  C   ARG C 179     7236   3427   4604    819   -824    490       C  
ATOM   7217  O   ARG C 179     101.104 -40.255-202.836  1.00 37.69           O  
ANISOU 7217  O   ARG C 179     6826   3179   4316    912   -775    427       O  
ATOM   7218  CB  ARG C 179     101.654 -42.714-200.854  1.00 41.33           C  
ANISOU 7218  CB  ARG C 179     7575   3402   4726    959   -946    546       C  
ATOM   7219  CG  ARG C 179     102.846 -42.699-201.776  1.00 46.60           C  
ANISOU 7219  CG  ARG C 179     8212   4063   5430   1133   -929    465       C  
ATOM   7220  CD  ARG C 179     103.308 -44.133-202.015  1.00 49.79           C  
ANISOU 7220  CD  ARG C 179     8798   4295   5825   1228  -1006    458       C  
ATOM   7221  NE  ARG C 179     104.652 -44.201-202.573  1.00 54.91           N  
ANISOU 7221  NE  ARG C 179     9409   4944   6512   1422   -993    389       N  
ATOM   7222  CZ  ARG C 179     105.243 -45.324-202.965  1.00 56.11           C  
ANISOU 7222  CZ  ARG C 179     9697   4956   6665   1544  -1045    360       C  
ATOM   7223  NH1 ARG C 179     104.602 -46.486-202.863  1.00 50.99           N  
ANISOU 7223  NH1 ARG C 179     9246   4149   5979   1487  -1121    398       N  
ATOM   7224  NH2 ARG C 179     106.472 -45.280-203.465  1.00 51.04           N  
ANISOU 7224  NH2 ARG C 179     8993   4335   6063   1724  -1018    293       N  
ATOM   7225  N   ASN C 180      99.171 -41.364-202.513  1.00 41.23           N  
ANISOU 7225  N   ASN C 180     7438   3507   4722    688   -839    510       N  
ATOM   7226  CA  ASN C 180      98.619 -41.063-203.837  1.00 39.64           C  
ANISOU 7226  CA  ASN C 180     7221   3310   4531    655   -814    458       C  
ATOM   7227  C   ASN C 180      97.815 -39.766-203.895  1.00 38.39           C  
ANISOU 7227  C   ASN C 180     6908   3291   4389    562   -753    458       C  
ATOM   7228  O   ASN C 180      97.372 -39.389-204.984  1.00 43.55           O  
ANISOU 7228  O   ASN C 180     7540   3958   5050    538   -737    415       O  
ATOM   7229  CB  ASN C 180      97.730 -42.227-204.311  1.00 37.70           C  
ANISOU 7229  CB  ASN C 180     7137   2923   4264    562   -880    475       C  
ATOM   7230  CG  ASN C 180      98.515 -43.488-204.610  1.00 40.64           C  
ANISOU 7230  CG  ASN C 180     7681   3141   4621    671   -941    455       C  
ATOM   7231  OD1 ASN C 180      99.693 -43.442-204.965  1.00 46.15           O  
ANISOU 7231  OD1 ASN C 180     8368   3838   5329    831   -923    401       O  
ATOM   7232  ND2 ASN C 180      97.845 -44.632-204.496  1.00 40.81           N  
ANISOU 7232  ND2 ASN C 180     7862   3025   4618    583  -1014    495       N  
ATOM   7233  N   ALA C 181      97.612 -39.092-202.773  1.00 34.53           N  
ANISOU 7233  N   ALA C 181     6321   2898   3900    513   -724    502       N  
ATOM   7234  CA  ALA C 181      96.762 -37.911-202.666  1.00 38.26           C  
ANISOU 7234  CA  ALA C 181     6655   3495   4387    424   -668    507       C  
ATOM   7235  C   ALA C 181      97.413 -36.710-203.336  1.00 38.99           C  
ANISOU 7235  C   ALA C 181     6629   3682   4504    510   -613    444       C  
ATOM   7236  O   ALA C 181      98.347 -36.143-202.765  1.00 36.05           O  
ANISOU 7236  O   ALA C 181     6187   3373   4137    590   -587    436       O  
ATOM   7237  CB  ALA C 181      96.487 -37.586-201.176  1.00 36.51           C  
ANISOU 7237  CB  ALA C 181     6381   3342   4148    364   -648    568       C  
ATOM   7238  N   PRO C 182      96.968 -36.284-204.524  1.00 36.84           N  
ANISOU 7238  N   PRO C 182     6334   3422   4244    492   -599    402       N  
ATOM   7239  CA  PRO C 182      97.728 -35.258-205.254  1.00 37.79           C  
ANISOU 7239  CA  PRO C 182     6367   3614   4379    580   -547    343       C  
ATOM   7240  C   PRO C 182      97.795 -33.911-204.559  1.00 36.45           C  
ANISOU 7240  C   PRO C 182     6051   3575   4226    573   -494    350       C  
ATOM   7241  O   PRO C 182      98.752 -33.165-204.799  1.00 37.33           O  
ANISOU 7241  O   PRO C 182     6094   3740   4348    657   -455    312       O  
ATOM   7242  CB  PRO C 182      96.977 -35.146-206.600  1.00 32.07           C  
ANISOU 7242  CB  PRO C 182     5670   2864   3652    536   -555    309       C  
ATOM   7243  CG  PRO C 182      96.177 -36.402-206.700  1.00 38.32           C  
ANISOU 7243  CG  PRO C 182     6588   3542   4428    458   -623    337       C  
ATOM   7244  CD  PRO C 182      95.801 -36.759-205.291  1.00 38.38           C  
ANISOU 7244  CD  PRO C 182     6589   3557   4436    391   -636    405       C  
ATOM   7245  N   ARG C 183      96.821 -33.562-203.726  1.00 37.07           N  
ANISOU 7245  N   ARG C 183     6078   3704   4304    474   -487    393       N  
ATOM   7246  CA  ARG C 183      96.777 -32.225-203.139  1.00 38.01           C  
ANISOU 7246  CA  ARG C 183     6067   3940   4434    466   -436    391       C  
ATOM   7247  C   ARG C 183      97.435 -32.140-201.769  1.00 36.81           C  
ANISOU 7247  C   ARG C 183     5894   3824   4268    495   -429    420       C  
ATOM   7248  O   ARG C 183      97.337 -31.090-201.114  1.00 37.58           O  
ANISOU 7248  O   ARG C 183     5898   4013   4366    480   -391    422       O  
ATOM   7249  CB  ARG C 183      95.335 -31.734-203.042  1.00 36.59           C  
ANISOU 7249  CB  ARG C 183     5829   3808   4265    354   -422    412       C  
ATOM   7250  CG  ARG C 183      94.646 -31.645-204.391  1.00 39.56           C  
ANISOU 7250  CG  ARG C 183     6213   4159   4658    323   -439    382       C  
ATOM   7251  CD  ARG C 183      93.160 -31.359-204.276  1.00 34.45           C  
ANISOU 7251  CD  ARG C 183     5507   3552   4031    211   -441    407       C  
ATOM   7252  NE  ARG C 183      92.641 -30.938-205.584  1.00 37.05           N  
ANISOU 7252  NE  ARG C 183     5823   3877   4379    201   -460    371       N  
ATOM   7253  CZ  ARG C 183      91.369 -30.656-205.840  1.00 42.56           C  
ANISOU 7253  CZ  ARG C 183     6464   4602   5103    117   -477    382       C  
ATOM   7254  NH1 ARG C 183      90.463 -30.750-204.884  1.00 34.92           N  
ANISOU 7254  NH1 ARG C 183     5440   3676   4152     32   -463    425       N  
ATOM   7255  NH2 ARG C 183      91.005 -30.277-207.062  1.00 43.21           N  
ANISOU 7255  NH2 ARG C 183     6546   4674   5197    117   -507    349       N  
ATOM   7256  N   CYS C 184      98.105 -33.200-201.325  1.00 38.27           N  
ANISOU 7256  N   CYS C 184     6170   3936   4436    539   -472    442       N  
ATOM   7257  CA  CYS C 184      98.703 -33.240-199.997  1.00 34.32           C  
ANISOU 7257  CA  CYS C 184     5668   3458   3913    564   -483    476       C  
ATOM   7258  C   CYS C 184     100.181 -32.879-200.072  1.00 31.17           C  
ANISOU 7258  C   CYS C 184     5225   3085   3534    689   -484    438       C  
ATOM   7259  O   CYS C 184     100.977 -33.638-200.632  1.00 32.97           O  
ANISOU 7259  O   CYS C 184     5510   3244   3773    774   -513    418       O  
ATOM   7260  CB  CYS C 184      98.543 -34.619-199.361  1.00 31.48           C  
ANISOU 7260  CB  CYS C 184     5440   3000   3522    537   -539    531       C  
ATOM   7261  SG  CYS C 184      99.255 -34.660-197.677  1.00 38.88           S  
ANISOU 7261  SG  CYS C 184     6391   3961   4419    565   -564    578       S  
ATOM   7262  N   VAL C 185     100.554 -31.759-199.441  1.00 33.82           N  
ANISOU 7262  N   VAL C 185     5461   3516   3872    699   -455    430       N  
ATOM   7263  CA  VAL C 185     101.965 -31.374-199.371  1.00 35.84           C  
ANISOU 7263  CA  VAL C 185     5659   3805   4151    804   -461    400       C  
ATOM   7264  C   VAL C 185     102.732 -32.112-198.283  1.00 36.41           C  
ANISOU 7264  C   VAL C 185     5785   3844   4205    855   -524    436       C  
ATOM   7265  O   VAL C 185     103.966 -32.056-198.267  1.00 36.90           O  
ANISOU 7265  O   VAL C 185     5806   3920   4295    952   -545    413       O  
ATOM   7266  CB  VAL C 185     102.090 -29.847-199.182  1.00 35.86           C  
ANISOU 7266  CB  VAL C 185     5540   3917   4166    789   -415    375       C  
ATOM   7267  CG1 VAL C 185     101.758 -29.433-197.742  1.00 33.92           C  
ANISOU 7267  CG1 VAL C 185     5286   3719   3882    737   -423    412       C  
ATOM   7268  CG2 VAL C 185     103.472 -29.346-199.598  1.00 38.38           C  
ANISOU 7268  CG2 VAL C 185     5784   4273   4525    883   -408    333       C  
ATOM   7269  N   GLY C 186     102.053 -32.839-197.402  1.00 36.13           N  
ANISOU 7269  N   GLY C 186     5840   3763   4124    792   -556    492       N  
ATOM   7270  CA  GLY C 186     102.739 -33.477-196.290  1.00 38.18           C  
ANISOU 7270  CA  GLY C 186     6162   3990   4357    835   -623    532       C  
ATOM   7271  C   GLY C 186     103.150 -34.919-196.508  1.00 39.11           C  
ANISOU 7271  C   GLY C 186     6401   3986   4475    898   -688    550       C  
ATOM   7272  O   GLY C 186     103.396 -35.643-195.536  1.00 39.26           O  
ANISOU 7272  O   GLY C 186     6507   3953   4458    910   -752    599       O  
ATOM   7273  N   ARG C 187     103.262 -35.357-197.764  1.00 36.55           N  
ANISOU 7273  N   ARG C 187     6095   3607   4186    944   -677    509       N  
ATOM   7274  CA  ARG C 187     103.396 -36.786-198.040  1.00 37.35           C  
ANISOU 7274  CA  ARG C 187     6334   3575   4281    989   -736    524       C  
ATOM   7275  C   ARG C 187     104.790 -37.351-197.788  1.00 34.84           C  
ANISOU 7275  C   ARG C 187     6034   3218   3987   1135   -798    514       C  
ATOM   7276  O   ARG C 187     104.959 -38.571-197.836  1.00 38.10           O  
ANISOU 7276  O   ARG C 187     6574   3511   4391   1184   -858    531       O  
ATOM   7277  CB  ARG C 187     102.971 -37.084-199.485  1.00 38.49           C  
ANISOU 7277  CB  ARG C 187     6509   3668   4446    985   -704    480       C  
ATOM   7278  CG  ARG C 187     101.468 -37.049-199.672  1.00 31.61           C  
ANISOU 7278  CG  ARG C 187     5670   2790   3549    837   -679    505       C  
ATOM   7279  CD  ARG C 187     101.081 -37.298-201.165  1.00 35.14           C  
ANISOU 7279  CD  ARG C 187     6151   3186   4014    835   -661    457       C  
ATOM   7280  NE  ARG C 187     101.237 -36.105-202.001  1.00 36.90           N  
ANISOU 7280  NE  ARG C 187     6249   3506   4265    854   -594    401       N  
ATOM   7281  CZ  ARG C 187     101.218 -36.122-203.334  1.00 36.23           C  
ANISOU 7281  CZ  ARG C 187     6181   3395   4191    880   -572    350       C  
ATOM   7282  NH1 ARG C 187     101.069 -37.271-203.980  1.00 40.08           N  
ANISOU 7282  NH1 ARG C 187     6803   3761   4665    895   -613    341       N  
ATOM   7283  NH2 ARG C 187     101.352 -34.991-204.025  1.00 38.81           N  
ANISOU 7283  NH2 ARG C 187     6401   3809   4536    891   -512    307       N  
ATOM   7284  N   ILE C 188     105.787 -36.521-197.514  1.00 41.50           N  
ANISOU 7284  N   ILE C 188     6752   4153   4862   1208   -791    488       N  
ATOM   7285  CA  ILE C 188     107.078 -37.031-197.069  1.00 41.46           C  
ANISOU 7285  CA  ILE C 188     6748   4122   4884   1342   -862    487       C  
ATOM   7286  C   ILE C 188     106.865 -37.972-195.874  1.00 46.38           C  
ANISOU 7286  C   ILE C 188     7512   4660   5452   1320   -953    561       C  
ATOM   7287  O   ILE C 188     107.650 -38.901-195.667  1.00 40.11           O  
ANISOU 7287  O   ILE C 188     6787   3783   4669   1429  -1032    571       O  
ATOM   7288  CB  ILE C 188     108.033 -35.870-196.721  1.00 43.66           C  
ANISOU 7288  CB  ILE C 188     6861   4526   5200   1387   -849    460       C  
ATOM   7289  CG1 ILE C 188     109.483 -36.351-196.644  1.00 40.90           C  
ANISOU 7289  CG1 ILE C 188     6475   4161   4905   1545   -912    440       C  
ATOM   7290  CG2 ILE C 188     107.654 -35.214-195.377  1.00 46.42           C  
ANISOU 7290  CG2 ILE C 188     7201   4937   5499   1297   -873    509       C  
ATOM   7291  CD1 ILE C 188     109.973 -36.972-197.879  1.00 46.06           C  
ANISOU 7291  CD1 ILE C 188     7135   4760   5605   1651   -883    387       C  
ATOM   7292  N   GLN C 189     105.776 -37.778-195.117  1.00 40.34           N  
ANISOU 7292  N   GLN C 189     6795   3908   4623   1181   -940    615       N  
ATOM   7293  CA  GLN C 189     105.474 -38.554-193.913  1.00 45.33           C  
ANISOU 7293  CA  GLN C 189     7566   4470   5189   1137  -1013    693       C  
ATOM   7294  C   GLN C 189     104.661 -39.818-194.184  1.00 49.84           C  
ANISOU 7294  C   GLN C 189     8306   4903   5728   1082  -1037    732       C  
ATOM   7295  O   GLN C 189     104.233 -40.472-193.224  1.00 45.17           O  
ANISOU 7295  O   GLN C 189     7841   4248   5072   1018  -1086    805       O  
ATOM   7296  CB  GLN C 189     104.704 -37.690-192.910  1.00 43.45           C  
ANISOU 7296  CB  GLN C 189     7296   4322   4891   1010   -974    731       C  
ATOM   7297  CG  GLN C 189     105.506 -36.581-192.279  1.00 47.76           C  
ANISOU 7297  CG  GLN C 189     7719   4982   5446   1052   -979    710       C  
ATOM   7298  CD  GLN C 189     106.438 -37.104-191.217  1.00 50.89           C  
ANISOU 7298  CD  GLN C 189     8180   5340   5816   1130  -1090    750       C  
ATOM   7299  OE1 GLN C 189     106.194 -38.160-190.627  1.00 50.05           O  
ANISOU 7299  OE1 GLN C 189     8228   5131   5655   1114  -1152    811       O  
ATOM   7300  NE2 GLN C 189     107.528 -36.384-190.981  1.00 46.12           N  
ANISOU 7300  NE2 GLN C 189     7461   4813   5251   1213  -1121    716       N  
ATOM   7301  N   TRP C 190     104.444 -40.182-195.455  1.00 41.65           N  
ANISOU 7301  N   TRP C 190     7282   3813   4729   1100  -1006    686       N  
ATOM   7302  CA  TRP C 190     103.398 -41.152-195.783  1.00 46.02           C  
ANISOU 7302  CA  TRP C 190     7982   4254   5252   1005  -1016    720       C  
ATOM   7303  C   TRP C 190     103.669 -42.534-195.209  1.00 44.18           C  
ANISOU 7303  C   TRP C 190     7932   3869   4984   1044  -1118    775       C  
ATOM   7304  O   TRP C 190     102.725 -43.297-194.990  1.00 46.01           O  
ANISOU 7304  O   TRP C 190     8298   4011   5170    930  -1136    831       O  
ATOM   7305  CB  TRP C 190     103.205 -41.248-197.304  1.00 42.41           C  
ANISOU 7305  CB  TRP C 190     7510   3766   4838   1027   -974    653       C  
ATOM   7306  CG  TRP C 190     104.284 -42.012-198.043  1.00 47.56           C  
ANISOU 7306  CG  TRP C 190     8213   4329   5528   1192  -1017    603       C  
ATOM   7307  CD1 TRP C 190     105.399 -41.485-198.635  1.00 48.07           C  
ANISOU 7307  CD1 TRP C 190     8158   4457   5648   1331   -988    534       C  
ATOM   7308  CD2 TRP C 190     104.324 -43.424-198.303  1.00 43.63           C  
ANISOU 7308  CD2 TRP C 190     7897   3662   5017   1236  -1089    615       C  
ATOM   7309  NE1 TRP C 190     106.134 -42.480-199.236  1.00 47.60           N  
ANISOU 7309  NE1 TRP C 190     8187   4286   5611   1466  -1031    500       N  
ATOM   7310  CE2 TRP C 190     105.499 -43.679-199.046  1.00 51.97           C  
ANISOU 7310  CE2 TRP C 190     8932   4691   6123   1416  -1097    547       C  
ATOM   7311  CE3 TRP C 190     103.482 -44.498-197.982  1.00 47.90           C  
ANISOU 7311  CE3 TRP C 190     8620   4070   5510   1139  -1145    677       C  
ATOM   7312  CZ2 TRP C 190     105.854 -44.965-199.475  1.00 50.22           C  
ANISOU 7312  CZ2 TRP C 190     8870   4309   5902   1513  -1162    533       C  
ATOM   7313  CZ3 TRP C 190     103.835 -45.771-198.408  1.00 58.24           C  
ANISOU 7313  CZ3 TRP C 190    10095   5215   6820   1225  -1217    667       C  
ATOM   7314  CH2 TRP C 190     105.013 -45.995-199.147  1.00 53.47           C  
ANISOU 7314  CH2 TRP C 190     9471   4582   6264   1416  -1226    593       C  
ATOM   7315  N   GLY C 191     104.932 -42.886-194.984  1.00 41.59           N  
ANISOU 7315  N   GLY C 191     7613   3507   4680   1202  -1187    761       N  
ATOM   7316  CA  GLY C 191     105.227 -44.193-194.409  1.00 50.55           C  
ANISOU 7316  CA  GLY C 191     8933   4491   5783   1251  -1295    815       C  
ATOM   7317  C   GLY C 191     104.959 -44.320-192.926  1.00 54.02           C  
ANISOU 7317  C   GLY C 191     9453   4925   6147   1171  -1346    906       C  
ATOM   7318  O   GLY C 191     104.966 -45.435-192.396  1.00 54.63           O  
ANISOU 7318  O   GLY C 191     9711   4866   6182   1177  -1434    966       O  
ATOM   7319  N   LYS C 192     104.709 -43.210-192.247  1.00 50.69           N  
ANISOU 7319  N   LYS C 192     8916   4644   5701   1095  -1293    918       N  
ATOM   7320  CA  LYS C 192     104.540 -43.179-190.796  1.00 48.20           C  
ANISOU 7320  CA  LYS C 192     8669   4342   5304   1026  -1332    998       C  
ATOM   7321  C   LYS C 192     103.082 -42.808-190.517  1.00 51.98           C  
ANISOU 7321  C   LYS C 192     9154   4870   5726    828  -1241   1038       C  
ATOM   7322  O   LYS C 192     102.726 -41.632-190.433  1.00 53.28           O  
ANISOU 7322  O   LYS C 192     9177   5174   5893    770  -1157   1012       O  
ATOM   7323  CB  LYS C 192     105.523 -42.193-190.174  1.00 47.56           C  
ANISOU 7323  CB  LYS C 192     8453   4381   5236   1111  -1350    973       C  
ATOM   7324  CG  LYS C 192     105.296 -41.911-188.682  1.00 64.96           C  
ANISOU 7324  CG  LYS C 192    10713   6625   7344   1030  -1376   1045       C  
ATOM   7325  CD  LYS C 192     106.043 -42.861-187.781  1.00 75.97           C  
ANISOU 7325  CD  LYS C 192    12259   7911   8695   1111  -1514   1106       C  
ATOM   7326  CE  LYS C 192     105.935 -42.406-186.334  1.00 82.15           C  
ANISOU 7326  CE  LYS C 192    13085   8751   9377   1040  -1538   1167       C  
ATOM   7327  NZ  LYS C 192     106.372 -40.989-186.163  1.00 78.69           N  
ANISOU 7327  NZ  LYS C 192    12460   8475   8964   1060  -1496   1111       N  
ATOM   7328  N   LEU C 193     102.240 -43.828-190.367  1.00 52.75           N  
ANISOU 7328  N   LEU C 193     9416   4852   5775    724  -1259   1103       N  
ATOM   7329  CA  LEU C 193     100.800 -43.648-190.207  1.00 47.80           C  
ANISOU 7329  CA  LEU C 193     8794   4261   5105    531  -1173   1143       C  
ATOM   7330  C   LEU C 193     100.264 -44.730-189.284  1.00 52.61           C  
ANISOU 7330  C   LEU C 193     9608   4754   5626    427  -1223   1246       C  
ATOM   7331  O   LEU C 193     100.485 -45.916-189.535  1.00 53.17           O  
ANISOU 7331  O   LEU C 193     9837   4668   5698    463  -1306   1271       O  
ATOM   7332  CB  LEU C 193     100.079 -43.729-191.551  1.00 43.69           C  
ANISOU 7332  CB  LEU C 193     8231   3724   4647    482  -1119   1095       C  
ATOM   7333  CG  LEU C 193      98.555 -43.612-191.551  1.00 49.95           C  
ANISOU 7333  CG  LEU C 193     9012   4550   5415    285  -1037   1131       C  
ATOM   7334  CD1 LEU C 193      98.097 -42.259-191.023  1.00 48.62           C  
ANISOU 7334  CD1 LEU C 193     8683   4557   5233    223   -938   1121       C  
ATOM   7335  CD2 LEU C 193      98.034 -43.821-192.980  1.00 47.70           C  
ANISOU 7335  CD2 LEU C 193     8701   4227   5197    263  -1018   1078       C  
ATOM   7336  N   GLN C 194      99.537 -44.323-188.249  1.00 50.97           N  
ANISOU 7336  N   GLN C 194     9406   4620   5341    296  -1166   1306       N  
ATOM   7337  CA  GLN C 194      98.929 -45.253-187.309  1.00 58.70           C  
ANISOU 7337  CA  GLN C 194    10575   5504   6224    173  -1193   1411       C  
ATOM   7338  C   GLN C 194      97.525 -45.597-187.793  1.00 58.58           C  
ANISOU 7338  C   GLN C 194    10574   5469   6215     -6  -1118   1438       C  
ATOM   7339  O   GLN C 194      96.664 -44.718-187.893  1.00 52.67           O  
ANISOU 7339  O   GLN C 194     9682   4851   5479   -104  -1006   1417       O  
ATOM   7340  CB  GLN C 194      98.888 -44.652-185.903  1.00 55.63           C  
ANISOU 7340  CB  GLN C 194    10192   5206   5737    124  -1165   1462       C  
ATOM   7341  CG  GLN C 194      98.345 -45.599-184.861  1.00 60.09           C  
ANISOU 7341  CG  GLN C 194    10968   5675   6190     -2  -1191   1577       C  
ATOM   7342  CD  GLN C 194      99.124 -46.893-184.819  1.00 60.88           C  
ANISOU 7342  CD  GLN C 194    11181   5640   6312     85  -1306   1572       C  
ATOM   7343  OE1 GLN C 194     100.336 -46.896-184.614  1.00 70.45           O  
ANISOU 7343  OE1 GLN C 194    12379   6843   7544    243  -1393   1535       O  
ATOM   7344  NE2 GLN C 194      98.436 -48.000-185.032  1.00 68.08           N  
ANISOU 7344  NE2 GLN C 194    12200   6445   7222    -20  -1310   1605       N  
ATOM   7345  N   VAL C 195      97.295 -46.866-188.099  1.00 53.32           N  
ANISOU 7345  N   VAL C 195    10077   4637   5544    -48  -1184   1481       N  
ATOM   7346  CA  VAL C 195      96.026 -47.311-188.659  1.00 55.90           C  
ANISOU 7346  CA  VAL C 195    10423   4928   5887   -218  -1134   1505       C  
ATOM   7347  C   VAL C 195      95.247 -48.013-187.560  1.00 61.84           C  
ANISOU 7347  C   VAL C 195    11319   5634   6545   -389  -1120   1614       C  
ATOM   7348  O   VAL C 195      95.646 -49.085-187.084  1.00 64.61           O  
ANISOU 7348  O   VAL C 195    11796   5885   6869   -369  -1193   1633       O  
ATOM   7349  CB  VAL C 195      96.225 -48.222-189.876  1.00 54.39           C  
ANISOU 7349  CB  VAL C 195    10315   4587   5762   -161  -1211   1466       C  
ATOM   7350  CG1 VAL C 195      94.879 -48.666-190.417  1.00 55.10           C  
ANISOU 7350  CG1 VAL C 195    10426   4641   5868   -352  -1169   1492       C  
ATOM   7351  CG2 VAL C 195      97.015 -47.487-190.937  1.00 51.81           C  
ANISOU 7351  CG2 VAL C 195     9834   4327   5525      7  -1205   1351       C  
ATOM   7352  N   PHE C 196      94.138 -47.407-187.149  1.00 57.68           N  
ANISOU 7352  N   PHE C 196    10708   5221   5986   -552  -1004   1651       N  
ATOM   7353  CA  PHE C 196      93.262 -47.980-186.137  1.00 60.29           C  
ANISOU 7353  CA  PHE C 196    11152   5529   6226   -736   -962   1754       C  
ATOM   7354  C   PHE C 196      92.110 -48.679-186.844  1.00 56.65           C  
ANISOU 7354  C   PHE C 196    10709   5007   5810   -904   -939   1777       C  
ATOM   7355  O   PHE C 196      91.364 -48.048-187.597  1.00 58.04           O  
ANISOU 7355  O   PHE C 196    10727   5272   6054   -965   -866   1736       O  
ATOM   7356  CB  PHE C 196      92.749 -46.904-185.181  1.00 63.50           C  
ANISOU 7356  CB  PHE C 196    11450   6110   6569   -811   -837   1777       C  
ATOM   7357  CG  PHE C 196      93.805 -46.354-184.261  1.00 68.81           C  
ANISOU 7357  CG  PHE C 196    12142   6829   7175   -676   -871   1770       C  
ATOM   7358  CD1 PHE C 196      94.364 -47.151-183.268  1.00 65.34           C  
ANISOU 7358  CD1 PHE C 196    11857   6311   6658   -653   -943   1818       C  
ATOM   7359  CD2 PHE C 196      94.224 -45.039-184.372  1.00 62.87           C  
ANISOU 7359  CD2 PHE C 196    11200   6229   6460   -569   -822   1684       C  
ATOM   7360  CE1 PHE C 196      95.334 -46.650-182.416  1.00 60.29           C  
ANISOU 7360  CE1 PHE C 196    11224   5720   5963   -532   -984   1805       C  
ATOM   7361  CE2 PHE C 196      95.191 -44.530-183.521  1.00 61.28           C  
ANISOU 7361  CE2 PHE C 196    11017   6068   6197   -455   -862   1678       C  
ATOM   7362  CZ  PHE C 196      95.744 -45.337-182.538  1.00 59.54           C  
ANISOU 7362  CZ  PHE C 196    11005   5741   5876   -441   -954   1759       C  
ATOM   7363  N   ASP C 197      91.977 -49.982-186.611  1.00 57.60           N  
ANISOU 7363  N   ASP C 197    10967   5005   5912   -966   -996   1810       N  
ATOM   7364  CA  ASP C 197      90.987 -50.792-187.312  1.00 58.66           C  
ANISOU 7364  CA  ASP C 197    11135   5063   6092  -1118   -999   1826       C  
ATOM   7365  C   ASP C 197      89.706 -50.845-186.481  1.00 66.81           C  
ANISOU 7365  C   ASP C 197    12155   6162   7068  -1350   -891   1916       C  
ATOM   7366  O   ASP C 197      89.656 -51.508-185.438  1.00 59.49           O  
ANISOU 7366  O   ASP C 197    11337   5203   6062  -1411   -891   1975       O  
ATOM   7367  CB  ASP C 197      91.554 -52.179-187.590  1.00 56.08           C  
ANISOU 7367  CB  ASP C 197    10967   4566   5777  -1055  -1122   1806       C  
ATOM   7368  CG  ASP C 197      90.547 -53.109-188.217  1.00 65.67           C  
ANISOU 7368  CG  ASP C 197    12236   5692   7026  -1219  -1136   1825       C  
ATOM   7369  OD1 ASP C 197      89.415 -52.672-188.514  1.00 66.98           O  
ANISOU 7369  OD1 ASP C 197    12300   5929   7218  -1381  -1055   1850       O  
ATOM   7370  OD2 ASP C 197      90.896 -54.289-188.419  1.00 69.42           O  
ANISOU 7370  OD2 ASP C 197    12853   6024   7501  -1186  -1233   1812       O  
ATOM   7371  N   ALA C 198      88.664 -50.156-186.960  1.00 55.96           N  
ANISOU 7371  N   ALA C 198    10643   4882   5736  -1480   -798   1924       N  
ATOM   7372  CA  ALA C 198      87.362 -50.109-186.306  1.00 58.52           C  
ANISOU 7372  CA  ALA C 198    10917   5293   6026  -1705   -677   2000       C  
ATOM   7373  C   ALA C 198      86.288 -50.818-187.128  1.00 63.03           C  
ANISOU 7373  C   ALA C 198    11472   5806   6671  -1875   -687   2013       C  
ATOM   7374  O   ALA C 198      85.096 -50.533-186.983  1.00 63.03           O  
ANISOU 7374  O   ALA C 198    11362   5903   6684  -2061   -581   2058       O  
ATOM   7375  CB  ALA C 198      86.958 -48.662-186.033  1.00 59.25           C  
ANISOU 7375  CB  ALA C 198    10817   5582   6114  -1717   -543   1987       C  
ATOM   7376  N   ARG C 199      86.697 -51.757-187.987  1.00 64.33           N  
ANISOU 7376  N   ARG C 199    11741   5818   6884  -1814   -814   1971       N  
ATOM   7377  CA  ARG C 199      85.779 -52.483-188.862  1.00 65.27           C  
ANISOU 7377  CA  ARG C 199    11861   5866   7073  -1961   -848   1971       C  
ATOM   7378  C   ARG C 199      84.831 -53.404-188.109  1.00 63.01           C  
ANISOU 7378  C   ARG C 199    11639   5557   6745  -2170   -812   2056       C  
ATOM   7379  O   ARG C 199      83.965 -54.016-188.744  1.00 67.80           O  
ANISOU 7379  O   ARG C 199    12238   6115   7407  -2316   -836   2064       O  
ATOM   7380  CB  ARG C 199      86.571 -53.292-189.893  1.00 64.51           C  
ANISOU 7380  CB  ARG C 199    11882   5607   7020  -1823   -994   1897       C  
ATOM   7381  CG  ARG C 199      87.213 -52.436-190.989  1.00 67.18           C  
ANISOU 7381  CG  ARG C 199    12134   5966   7424  -1654  -1024   1807       C  
ATOM   7382  CD  ARG C 199      88.086 -53.288-191.888  1.00 73.24           C  
ANISOU 7382  CD  ARG C 199    13028   6580   8221  -1503  -1154   1730       C  
ATOM   7383  NE  ARG C 199      89.186 -53.901-191.149  1.00 74.28           N  
ANISOU 7383  NE  ARG C 199    13293   6640   8291  -1362  -1211   1731       N  
ATOM   7384  CZ  ARG C 199      89.872 -54.959-191.571  1.00 72.30           C  
ANISOU 7384  CZ  ARG C 199    13185   6244   8043  -1260  -1320   1686       C  
ATOM   7385  NH1 ARG C 199      89.565 -55.530-192.726  1.00 66.35           N  
ANISOU 7385  NH1 ARG C 199    12469   5400   7341  -1285  -1380   1636       N  
ATOM   7386  NH2 ARG C 199      90.859 -55.453-190.833  1.00 70.88           N  
ANISOU 7386  NH2 ARG C 199    13111   6009   7811  -1134  -1371   1691       N  
ATOM   7387  N   ASP C 200      84.961 -53.515-186.788  1.00 60.36           N  
ANISOU 7387  N   ASP C 200    11366   5256   6313  -2192   -757   2117       N  
ATOM   7388  CA  ASP C 200      84.034 -54.284-185.972  1.00 75.76           C  
ANISOU 7388  CA  ASP C 200    13368   7201   8215  -2396   -702   2203       C  
ATOM   7389  C   ASP C 200      83.042 -53.395-185.230  1.00 77.43           C  
ANISOU 7389  C   ASP C 200    13417   7600   8403  -2543   -527   2257       C  
ATOM   7390  O   ASP C 200      82.377 -53.864-184.301  1.00 68.04           O  
ANISOU 7390  O   ASP C 200    12263   6435   7154  -2693   -453   2332       O  
ATOM   7391  CB  ASP C 200      84.798 -55.172-184.981  1.00 82.68           C  
ANISOU 7391  CB  ASP C 200    14447   7976   8993  -2333   -763   2238       C  
ATOM   7392  CG  ASP C 200      86.251 -54.739-184.795  1.00 95.54           C  
ANISOU 7392  CG  ASP C 200    16126   9586  10588  -2085   -829   2186       C  
ATOM   7393  OD1 ASP C 200      86.651 -53.692-185.361  1.00 83.17           O  
ANISOU 7393  OD1 ASP C 200    14437   8097   9068  -1966   -814   2126       O  
ATOM   7394  OD2 ASP C 200      86.998 -55.455-184.085  1.00102.63           O  
ANISOU 7394  OD2 ASP C 200    17185  10393  11416  -2010   -900   2204       O  
ATOM   7395  N   CYS C 201      82.919 -52.131-185.637  1.00 76.25           N  
ANISOU 7395  N   CYS C 201    13091   7583   8299  -2502   -455   2219       N  
ATOM   7396  CA  CYS C 201      82.100 -51.167-184.911  1.00 77.07           C  
ANISOU 7396  CA  CYS C 201    13031   7876   8374  -2610   -281   2257       C  
ATOM   7397  C   CYS C 201      80.614 -51.469-185.072  1.00 80.01           C  
ANISOU 7397  C   CYS C 201    13285   8308   8807  -2851   -199   2303       C  
ATOM   7398  O   CYS C 201      80.151 -51.842-186.153  1.00 76.47           O  
ANISOU 7398  O   CYS C 201    12795   7801   8459  -2916   -269   2279       O  
ATOM   7399  CB  CYS C 201      82.401 -49.752-185.403  1.00 68.69           C  
ANISOU 7399  CB  CYS C 201    11816   6932   7350  -2495   -238   2198       C  
ATOM   7400  SG  CYS C 201      81.734 -48.437-184.371  1.00 74.87           S  
ANISOU 7400  SG  CYS C 201    12412   7957   8077  -2553    -26   2218       S  
ATOM   7401  N   ARG C 202      79.857 -51.285-183.988  1.00 86.46           N  
ANISOU 7401  N   ARG C 202    14040   9246   9563  -2981    -49   2365       N  
ATOM   7402  CA  ARG C 202      78.439 -51.636-183.964  1.00 91.40           C  
ANISOU 7402  CA  ARG C 202    14547   9938  10241  -3213     42   2415       C  
ATOM   7403  C   ARG C 202      77.530 -50.414-184.056  1.00 92.49           C  
ANISOU 7403  C   ARG C 202    14416  10287  10438  -3285    198   2401       C  
ATOM   7404  O   ARG C 202      76.712 -50.316-184.974  1.00100.02           O  
ANISOU 7404  O   ARG C 202    15214  11278  11512  -3386    192   2383       O  
ATOM   7405  CB  ARG C 202      78.112 -52.444-182.698  1.00 99.36           C  
ANISOU 7405  CB  ARG C 202    15673  10931  11148  -3326    107   2498       C  
ATOM   7406  CG  ARG C 202      78.882 -53.749-182.567  1.00107.21           C  
ANISOU 7406  CG  ARG C 202    16931  11718  12088  -3278    -46   2517       C  
ATOM   7407  CD  ARG C 202      78.925 -54.505-183.889  1.00117.36           C  
ANISOU 7407  CD  ARG C 202    18262  12855  13474  -3280   -204   2477       C  
ATOM   7408  NE  ARG C 202      77.604 -54.640-184.500  1.00126.13           N  
ANISOU 7408  NE  ARG C 202    19215  14021  14688  -3481   -159   2493       N  
ATOM   7409  CZ  ARG C 202      77.400 -54.937-185.780  1.00126.42           C  
ANISOU 7409  CZ  ARG C 202    19221  13983  14831  -3499   -269   2446       C  
ATOM   7410  NH1 ARG C 202      78.432 -55.131-186.590  1.00124.59           N  
ANISOU 7410  NH1 ARG C 202    19108  13616  14613  -3326   -419   2380       N  
ATOM   7411  NH2 ARG C 202      76.165 -55.033-186.252  1.00126.41           N  
ANISOU 7411  NH2 ARG C 202    19065  14043  14923  -3688   -229   2463       N  
ATOM   7412  N   SER C 203      77.650 -49.481-183.116  1.00 89.57           N  
ANISOU 7412  N   SER C 203    13986  10059   9986  -3232    334   2406       N  
ATOM   7413  CA  SER C 203      76.718 -48.368-183.007  1.00 87.89           C  
ANISOU 7413  CA  SER C 203    13517  10060   9815  -3305    506   2394       C  
ATOM   7414  C   SER C 203      77.464 -47.041-183.049  1.00 85.28           C  
ANISOU 7414  C   SER C 203    13106   9830   9468  -3101    533   2313       C  
ATOM   7415  O   SER C 203      78.697 -46.990-183.072  1.00 76.43           O  
ANISOU 7415  O   SER C 203    12129   8616   8296  -2917    427   2276       O  
ATOM   7416  CB  SER C 203      75.908 -48.454-181.711  1.00 83.91           C  
ANISOU 7416  CB  SER C 203    12975   9673   9234  -3432    683   2457       C  
ATOM   7417  OG  SER C 203      76.767 -48.294-180.597  1.00 83.14           O  
ANISOU 7417  OG  SER C 203    13036   9566   8987  -3316    709   2469       O  
ATOM   7418  N   ALA C 204      76.685 -45.956-183.040  1.00 86.88           N  
ANISOU 7418  N   ALA C 204    13040  10237   9734  -3095    674   2258       N  
ATOM   7419  CA  ALA C 204      77.271 -44.621-182.967  1.00 80.49           C  
ANISOU 7419  CA  ALA C 204    12114   9548   8921  -2875    714   2153       C  
ATOM   7420  C   ALA C 204      77.997 -44.408-181.643  1.00 71.46           C  
ANISOU 7420  C   ALA C 204    11131   8415   7606  -2807    776   2185       C  
ATOM   7421  O   ALA C 204      79.009 -43.696-181.587  1.00 60.56           O  
ANISOU 7421  O   ALA C 204     9778   7040   6192  -2603    730   2114       O  
ATOM   7422  CB  ALA C 204      76.188 -43.559-183.166  1.00 79.83           C  
ANISOU 7422  CB  ALA C 204    11720   9674   8937  -2895    855   2094       C  
ATOM   7423  N   GLN C 205      77.495 -45.018-180.566  1.00 82.12           N  
ANISOU 7423  N   GLN C 205    12592   9768   8843  -2981    880   2294       N  
ATOM   7424  CA  GLN C 205      78.178 -44.930-179.280  1.00 86.33           C  
ANISOU 7424  CA  GLN C 205    13310  10295   9197  -2931    927   2335       C  
ATOM   7425  C   GLN C 205      79.577 -45.526-179.361  1.00 86.67           C  
ANISOU 7425  C   GLN C 205    13599  10147   9183  -2791    734   2338       C  
ATOM   7426  O   GLN C 205      80.530 -44.977-178.796  1.00 89.24           O  
ANISOU 7426  O   GLN C 205    14012  10480   9415  -2637    714   2308       O  
ATOM   7427  CB  GLN C 205      77.354 -45.631-178.199  1.00 77.67           C  
ANISOU 7427  CB  GLN C 205    12254   9229   8030  -3091   1044   2415       C  
ATOM   7428  CG  GLN C 205      77.951 -45.532-176.809  1.00 82.69           C  
ANISOU 7428  CG  GLN C 205    13049   9873   8495  -3016   1092   2435       C  
ATOM   7429  CD  GLN C 205      77.966 -44.108-176.280  1.00 91.39           C  
ANISOU 7429  CD  GLN C 205    14035  11154   9536  -2923   1236   2377       C  
ATOM   7430  OE1 GLN C 205      76.921 -43.545-175.951  1.00 96.47           O  
ANISOU 7430  OE1 GLN C 205    14497  11964  10193  -3009   1421   2371       O  
ATOM   7431  NE2 GLN C 205      79.155 -43.518-176.196  1.00 87.88           N  
ANISOU 7431  NE2 GLN C 205    13690  10675   9025  -2741   1150   2328       N  
ATOM   7432  N   GLU C 206      79.722 -46.648-180.065  1.00 80.81           N  
ANISOU 7432  N   GLU C 206    12957   9239   8507  -2826    587   2359       N  
ATOM   7433  CA  GLU C 206      81.042 -47.230-180.269  1.00 73.86           C  
ANISOU 7433  CA  GLU C 206    12282   8182   7599  -2672    399   2344       C  
ATOM   7434  C   GLU C 206      81.877 -46.388-181.225  1.00 65.28           C  
ANISOU 7434  C   GLU C 206    11124   7098   6583  -2482    313   2250       C  
ATOM   7435  O   GLU C 206      83.095 -46.264-181.047  1.00 61.79           O  
ANISOU 7435  O   GLU C 206    10799   6589   6088  -2307    216   2220       O  
ATOM   7436  CB  GLU C 206      80.899 -48.659-180.787  1.00 78.22           C  
ANISOU 7436  CB  GLU C 206    12950   8562   8208  -2755    275   2379       C  
ATOM   7437  CG  GLU C 206      82.197 -49.433-180.844  1.00 87.02           C  
ANISOU 7437  CG  GLU C 206    14283   9494   9287  -2602     92   2366       C  
ATOM   7438  CD  GLU C 206      81.971 -50.919-181.047  1.00 96.64           C  
ANISOU 7438  CD  GLU C 206    15640  10551  10529  -2701     -6   2408       C  
ATOM   7439  OE1 GLU C 206      80.812 -51.367-180.904  1.00100.64           O  
ANISOU 7439  OE1 GLU C 206    16089  11092  11056  -2899     78   2461       O  
ATOM   7440  OE2 GLU C 206      82.948 -51.636-181.352  1.00 98.74           O  
ANISOU 7440  OE2 GLU C 206    16064  10658  10794  -2579   -164   2386       O  
ATOM   7441  N   MET C 207      81.240 -45.804-182.242  1.00 61.76           N  
ANISOU 7441  N   MET C 207    10441   6744   6282  -2478    341   2173       N  
ATOM   7442  CA  MET C 207      81.945 -44.874-183.122  1.00 66.12           C  
ANISOU 7442  CA  MET C 207    10864   7337   6923  -2266    276   2049       C  
ATOM   7443  C   MET C 207      82.577 -43.751-182.311  1.00 69.48           C  
ANISOU 7443  C   MET C 207    11252   7877   7269  -2117    343   2000       C  
ATOM   7444  O   MET C 207      83.743 -43.394-182.516  1.00 70.85           O  
ANISOU 7444  O   MET C 207    11473   8009   7439  -1930    247   1940       O  
ATOM   7445  CB  MET C 207      80.982 -44.306-184.170  1.00 72.54           C  
ANISOU 7445  CB  MET C 207    11420   8255   7887  -2305    320   1984       C  
ATOM   7446  CG  MET C 207      81.443 -44.446-185.616  1.00 82.74           C  
ANISOU 7446  CG  MET C 207    12688   9453   9296  -2202    172   1910       C  
ATOM   7447  SD  MET C 207      80.424 -43.514-186.788  1.00 88.47           S  
ANISOU 7447  SD  MET C 207    13106  10323  10187  -2211    218   1821       S  
ATOM   7448  CE  MET C 207      78.789 -44.077-186.315  1.00 81.74           C  
ANISOU 7448  CE  MET C 207    12172   9536   9349  -2493    339   1918       C  
ATOM   7449  N   PHE C 208      81.822 -43.206-181.355  1.00 65.19           N  
ANISOU 7449  N   PHE C 208    10631   7478   6660  -2204    511   2027       N  
ATOM   7450  CA  PHE C 208      82.332 -42.116-180.530  1.00 63.59           C  
ANISOU 7450  CA  PHE C 208    10401   7386   6373  -2075    582   1978       C  
ATOM   7451  C   PHE C 208      83.548 -42.554-179.725  1.00 68.46           C  
ANISOU 7451  C   PHE C 208    11268   7888   6854  -1991    485   2020       C  
ATOM   7452  O   PHE C 208      84.504 -41.783-179.558  1.00 62.87           O  
ANISOU 7452  O   PHE C 208    10561   7206   6119  -1817    442   1953       O  
ATOM   7453  CB  PHE C 208      81.221 -41.611-179.614  1.00 65.67           C  
ANISOU 7453  CB  PHE C 208    10560   7812   6578  -2199    786   2007       C  
ATOM   7454  CG  PHE C 208      81.628 -40.468-178.736  1.00 70.34           C  
ANISOU 7454  CG  PHE C 208    11129   8521   7078  -2078    871   1954       C  
ATOM   7455  CD1 PHE C 208      81.876 -39.219-179.275  1.00 67.71           C  
ANISOU 7455  CD1 PHE C 208    10617   8283   6825  -1917    875   1836       C  
ATOM   7456  CD2 PHE C 208      81.744 -40.640-177.367  1.00 76.97           C  
ANISOU 7456  CD2 PHE C 208    12135   9369   7741  -2130    944   2023       C  
ATOM   7457  CE1 PHE C 208      82.245 -38.160-178.469  1.00 73.82           C  
ANISOU 7457  CE1 PHE C 208    11380   9157   7513  -1810    947   1784       C  
ATOM   7458  CE2 PHE C 208      82.112 -39.585-176.550  1.00 77.94           C  
ANISOU 7458  CE2 PHE C 208    12248   9594   7770  -2021   1017   1970       C  
ATOM   7459  CZ  PHE C 208      82.360 -38.341-177.104  1.00 74.59           C  
ANISOU 7459  CZ  PHE C 208    11645   9263   7435  -1861   1017   1848       C  
ATOM   7460  N   THR C 209      83.540 -43.799-179.237  1.00 69.80           N  
ANISOU 7460  N   THR C 209    11654   7925   6941  -2114    440   2131       N  
ATOM   7461  CA  THR C 209      84.669 -44.299-178.460  1.00 69.24           C  
ANISOU 7461  CA  THR C 209    11833   7735   6741  -2037    333   2178       C  
ATOM   7462  C   THR C 209      85.908 -44.480-179.331  1.00 63.60           C  
ANISOU 7462  C   THR C 209    11167   6896   6100  -1851    144   2118       C  
ATOM   7463  O   THR C 209      87.019 -44.134-178.913  1.00 60.96           O  
ANISOU 7463  O   THR C 209    10911   6544   5707  -1696     69   2090       O  
ATOM   7464  CB  THR C 209      84.296 -45.612-177.778  1.00 70.07           C  
ANISOU 7464  CB  THR C 209    12101   7740   6783  -2177    323   2274       C  
ATOM   7465  OG1 THR C 209      83.005 -45.483-177.165  1.00 76.96           O  
ANISOU 7465  OG1 THR C 209    12878   8739   7625  -2354    508   2317       O  
ATOM   7466  CG2 THR C 209      85.319 -45.941-176.710  1.00 60.39           C  
ANISOU 7466  CG2 THR C 209    11061   6447   5438  -2071    241   2289       C  
ATOM   7467  N   TYR C 210      85.743 -45.035-180.535  1.00 55.26           N  
ANISOU 7467  N   TYR C 210    10069   5756   5170  -1866     65   2098       N  
ATOM   7468  CA  TYR C 210      86.863 -45.103-181.472  1.00 57.59           C  
ANISOU 7468  CA  TYR C 210    10382   5953   5545  -1682    -93   2027       C  
ATOM   7469  C   TYR C 210      87.401 -43.712-181.810  1.00 64.17           C  
ANISOU 7469  C   TYR C 210    11027   6918   6435  -1506    -71   1909       C  
ATOM   7470  O   TYR C 210      88.620 -43.506-181.876  1.00 56.93           O  
ANISOU 7470  O   TYR C 210    10160   5958   5514  -1333   -175   1864       O  
ATOM   7471  CB  TYR C 210      86.438 -45.815-182.756  1.00 60.43           C  
ANISOU 7471  CB  TYR C 210    10712   6220   6030  -1738   -159   2015       C  
ATOM   7472  CG  TYR C 210      86.534 -47.316-182.702  1.00 66.17           C  
ANISOU 7472  CG  TYR C 210    11680   6745   6715  -1827   -264   2109       C  
ATOM   7473  CD1 TYR C 210      87.767 -47.950-182.603  1.00 62.22           C  
ANISOU 7473  CD1 TYR C 210    11336   6113   6193  -1672   -410   2093       C  
ATOM   7474  CD2 TYR C 210      85.392 -48.105-182.776  1.00 72.74           C  
ANISOU 7474  CD2 TYR C 210    12516   7551   7572  -2031   -219   2167       C  
ATOM   7475  CE1 TYR C 210      87.856 -49.334-182.560  1.00 63.50           C  
ANISOU 7475  CE1 TYR C 210    11647   6125   6355  -1708   -503   2123       C  
ATOM   7476  CE2 TYR C 210      85.471 -49.482-182.743  1.00 72.44           C  
ANISOU 7476  CE2 TYR C 210    12630   7360   7532  -2072   -315   2199       C  
ATOM   7477  CZ  TYR C 210      86.704 -50.090-182.636  1.00 71.64           C  
ANISOU 7477  CZ  TYR C 210    12685   7129   7404  -1909   -456   2176       C  
ATOM   7478  OH  TYR C 210      86.781 -51.457-182.601  1.00 79.18           O  
ANISOU 7478  OH  TYR C 210    13797   7933   8355  -1947   -551   2204       O  
ATOM   7479  N   ILE C 211      86.507 -42.748-182.037  1.00 58.92           N  
ANISOU 7479  N   ILE C 211    10145   6414   5829  -1548     60   1858       N  
ATOM   7480  CA  ILE C 211      86.937 -41.404-182.418  1.00 57.24           C  
ANISOU 7480  CA  ILE C 211     9756   6320   5675  -1392     81   1746       C  
ATOM   7481  C   ILE C 211      87.683 -40.736-181.270  1.00 63.35           C  
ANISOU 7481  C   ILE C 211    10592   7148   6330  -1301    100   1740       C  
ATOM   7482  O   ILE C 211      88.740 -40.122-181.465  1.00 57.07           O  
ANISOU 7482  O   ILE C 211     9774   6357   5553  -1134     26   1671       O  
ATOM   7483  CB  ILE C 211      85.730 -40.567-182.874  1.00 57.52           C  
ANISOU 7483  CB  ILE C 211     9554   6505   5796  -1462    213   1700       C  
ATOM   7484  CG1 ILE C 211      85.220 -41.072-184.230  1.00 53.61           C  
ANISOU 7484  CG1 ILE C 211     8983   5952   5436  -1511    157   1682       C  
ATOM   7485  CG2 ILE C 211      86.092 -39.083-182.928  1.00 58.39           C  
ANISOU 7485  CG2 ILE C 211     9507   6746   5932  -1316    259   1598       C  
ATOM   7486  CD1 ILE C 211      83.974 -40.381-184.716  1.00 57.17           C  
ANISOU 7486  CD1 ILE C 211     9204   6539   5979  -1590    269   1645       C  
ATOM   7487  N   CYS C 212      87.152 -40.856-180.050  1.00 66.53           N  
ANISOU 7487  N   CYS C 212    11078   7594   6606  -1415    199   1813       N  
ATOM   7488  CA  CYS C 212      87.831 -40.273-178.899  1.00 67.33           C  
ANISOU 7488  CA  CYS C 212    11263   7741   6578  -1338    212   1811       C  
ATOM   7489  C   CYS C 212      89.211 -40.885-178.711  1.00 63.64           C  
ANISOU 7489  C   CYS C 212    10984   7133   6063  -1222     38   1832       C  
ATOM   7490  O   CYS C 212      90.174 -40.178-178.392  1.00 56.97           O  
ANISOU 7490  O   CYS C 212    10142   6317   5188  -1080    -15   1780       O  
ATOM   7491  CB  CYS C 212      86.979 -40.447-177.642  1.00 70.32           C  
ANISOU 7491  CB  CYS C 212    11725   8177   6816  -1494    351   1895       C  
ATOM   7492  SG  CYS C 212      85.570 -39.311-177.595  1.00 70.03           S  
ANISOU 7492  SG  CYS C 212    11438   8350   6819  -1573    573   1843       S  
ATOM   7493  N   ASN C 213      89.332 -42.195-178.933  1.00 61.17           N  
ANISOU 7493  N   ASN C 213    10829   6664   5750  -1276    -59   1906       N  
ATOM   7494  CA  ASN C 213      90.641 -42.829-178.841  1.00 62.36           C  
ANISOU 7494  CA  ASN C 213    11150   6673   5870  -1152   -233   1924       C  
ATOM   7495  C   ASN C 213      91.582 -42.307-179.917  1.00 55.40           C  
ANISOU 7495  C   ASN C 213    10144   5788   5117   -967   -329   1817       C  
ATOM   7496  O   ASN C 213      92.772 -42.086-179.657  1.00 53.15           O  
ANISOU 7496  O   ASN C 213     9908   5477   4809   -820   -432   1790       O  
ATOM   7497  CB  ASN C 213      90.494 -44.344-178.935  1.00 64.11           C  
ANISOU 7497  CB  ASN C 213    11566   6720   6074  -1248   -314   2021       C  
ATOM   7498  CG  ASN C 213      90.144 -44.970-177.604  1.00 80.88           C  
ANISOU 7498  CG  ASN C 213    13816   8836   8077  -1354   -270   2092       C  
ATOM   7499  OD1 ASN C 213      90.965 -44.994-176.688  1.00 86.87           O  
ANISOU 7499  OD1 ASN C 213    14673   9580   8755  -1267   -334   2094       O  
ATOM   7500  ND2 ASN C 213      88.921 -45.477-177.485  1.00 83.87           N  
ANISOU 7500  ND2 ASN C 213    14187   9230   8451  -1542   -163   2149       N  
ATOM   7501  N   HIS C 214      91.066 -42.098-181.129  1.00 55.70           N  
ANISOU 7501  N   HIS C 214    10018   5856   5290   -976   -297   1758       N  
ATOM   7502  CA  HIS C 214      91.878 -41.531-182.196  1.00 52.91           C  
ANISOU 7502  CA  HIS C 214     9538   5511   5054   -812   -367   1656       C  
ATOM   7503  C   HIS C 214      92.373 -40.146-181.803  1.00 51.08           C  
ANISOU 7503  C   HIS C 214     9186   5414   4807   -706   -326   1583       C  
ATOM   7504  O   HIS C 214      93.579 -39.870-181.820  1.00 49.23           O  
ANISOU 7504  O   HIS C 214     8964   5159   4581   -557   -424   1542       O  
ATOM   7505  CB  HIS C 214      91.050 -41.503-183.484  1.00 49.20           C  
ANISOU 7505  CB  HIS C 214     8923   5059   4713   -866   -326   1613       C  
ATOM   7506  CG  HIS C 214      91.747 -40.898-184.666  1.00 51.60           C  
ANISOU 7506  CG  HIS C 214     9095   5378   5133   -715   -380   1510       C  
ATOM   7507  ND1 HIS C 214      91.792 -41.525-185.892  1.00 52.60           N  
ANISOU 7507  ND1 HIS C 214     9220   5410   5354   -695   -448   1486       N  
ATOM   7508  CD2 HIS C 214      92.373 -39.708-184.831  1.00 50.21           C  
ANISOU 7508  CD2 HIS C 214     8786   5300   4990   -587   -369   1426       C  
ATOM   7509  CE1 HIS C 214      92.439 -40.761-186.754  1.00 49.11           C  
ANISOU 7509  CE1 HIS C 214     8654   5012   4995   -558   -472   1393       C  
ATOM   7510  NE2 HIS C 214      92.800 -39.651-186.137  1.00 49.65           N  
ANISOU 7510  NE2 HIS C 214     8638   5196   5031   -495   -426   1357       N  
ATOM   7511  N   ILE C 215      91.445 -39.275-181.410  1.00 52.83           N  
ANISOU 7511  N   ILE C 215     9293   5775   5006   -785   -183   1568       N  
ATOM   7512  CA  ILE C 215      91.805 -37.916-181.007  1.00 55.81           C  
ANISOU 7512  CA  ILE C 215     9564   6278   5363   -696   -136   1496       C  
ATOM   7513  C   ILE C 215      92.848 -37.945-179.897  1.00 56.72           C  
ANISOU 7513  C   ILE C 215     9831   6361   5359   -624   -215   1524       C  
ATOM   7514  O   ILE C 215      93.836 -37.199-179.931  1.00 49.45           O  
ANISOU 7514  O   ILE C 215     8863   5469   4457   -489   -278   1459       O  
ATOM   7515  CB  ILE C 215      90.546 -37.138-180.587  1.00 52.90           C  
ANISOU 7515  CB  ILE C 215     9081   6050   4968   -802     38   1488       C  
ATOM   7516  CG1 ILE C 215      89.629 -36.929-181.800  1.00 52.79           C  
ANISOU 7516  CG1 ILE C 215     8887   6079   5092   -845     96   1445       C  
ATOM   7517  CG2 ILE C 215      90.919 -35.813-179.932  1.00 51.57           C  
ANISOU 7517  CG2 ILE C 215     8852   5996   4749   -717     85   1423       C  
ATOM   7518  CD1 ILE C 215      88.270 -36.372-181.444  1.00 53.11           C  
ANISOU 7518  CD1 ILE C 215     8811   6249   5122   -960    264   1447       C  
ATOM   7519  N   LYS C 216      92.655 -38.822-178.907  1.00 56.04           N  
ANISOU 7519  N   LYS C 216     9935   6210   5149   -716   -221   1623       N  
ATOM   7520  CA  LYS C 216      93.607 -38.920-177.808  1.00 53.34           C  
ANISOU 7520  CA  LYS C 216     9755   5828   4682   -654   -309   1657       C  
ATOM   7521  C   LYS C 216      94.982 -39.346-178.304  1.00 56.16           C  
ANISOU 7521  C   LYS C 216    10159   6077   5100   -501   -490   1636       C  
ATOM   7522  O   LYS C 216      95.996 -38.715-177.975  1.00 49.87           O  
ANISOU 7522  O   LYS C 216     9351   5309   4288   -380   -564   1592       O  
ATOM   7523  CB  LYS C 216      93.095 -39.900-176.749  1.00 57.27           C  
ANISOU 7523  CB  LYS C 216    10464   6260   5035   -791   -286   1777       C  
ATOM   7524  CG  LYS C 216      93.877 -39.849-175.445  1.00 76.54           C  
ANISOU 7524  CG  LYS C 216    13079   8683   7320   -748   -354   1816       C  
ATOM   7525  CD  LYS C 216      93.441 -40.948-174.471  1.00 82.12           C  
ANISOU 7525  CD  LYS C 216    13980   9315   7908   -873   -343   1922       C  
ATOM   7526  CE  LYS C 216      91.963 -40.842-174.115  1.00 88.20           C  
ANISOU 7526  CE  LYS C 216    14718  10173   8621  -1056   -145   1963       C  
ATOM   7527  NZ  LYS C 216      91.547 -41.926-173.168  1.00 93.35           N  
ANISOU 7527  NZ  LYS C 216    15509  10766   9192  -1169   -128   2042       N  
ATOM   7528  N   TYR C 217      95.039 -40.428-179.088  1.00 49.64           N  
ANISOU 7528  N   TYR C 217     9387   5127   4345   -505   -564   1667       N  
ATOM   7529  CA  TYR C 217      96.316 -40.875-179.637  1.00 52.82           C  
ANISOU 7529  CA  TYR C 217     9824   5429   4816   -350   -725   1641       C  
ATOM   7530  C   TYR C 217      96.947 -39.802-180.524  1.00 50.79           C  
ANISOU 7530  C   TYR C 217     9361   5257   4679   -217   -732   1526       C  
ATOM   7531  O   TYR C 217      98.141 -39.499-180.401  1.00 45.88           O  
ANISOU 7531  O   TYR C 217     8731   4631   4069    -80   -833   1491       O  
ATOM   7532  CB  TYR C 217      96.126 -42.172-180.429  1.00 51.06           C  
ANISOU 7532  CB  TYR C 217     9689   5059   4652   -381   -785   1683       C  
ATOM   7533  CG  TYR C 217      97.390 -42.595-181.146  1.00 56.99           C  
ANISOU 7533  CG  TYR C 217    10452   5713   5489   -208   -935   1642       C  
ATOM   7534  CD1 TYR C 217      98.315 -43.442-180.534  1.00 61.96           C  
ANISOU 7534  CD1 TYR C 217    11257   6222   6062   -131  -1076   1694       C  
ATOM   7535  CD2 TYR C 217      97.678 -42.118-182.423  1.00 60.09           C  
ANISOU 7535  CD2 TYR C 217    10672   6140   6019   -116   -931   1547       C  
ATOM   7536  CE1 TYR C 217      99.479 -43.810-181.188  1.00 67.40           C  
ANISOU 7536  CE1 TYR C 217    11922   6840   6847     37  -1200   1641       C  
ATOM   7537  CE2 TYR C 217      98.830 -42.471-183.069  1.00 61.25           C  
ANISOU 7537  CE2 TYR C 217    10821   6210   6242     43  -1051   1506       C  
ATOM   7538  CZ  TYR C 217      99.725 -43.312-182.462  1.00 66.97           C  
ANISOU 7538  CZ  TYR C 217    11712   6818   6916    123  -1187   1558       C  
ATOM   7539  OH  TYR C 217     100.870 -43.652-183.142  1.00 77.06           O  
ANISOU 7539  OH  TYR C 217    12974   8026   8280    293  -1299   1511       O  
ATOM   7540  N   ALA C 218      96.169 -39.244-181.453  1.00 51.41           N  
ANISOU 7540  N   ALA C 218     9273   5411   4851   -258   -629   1470       N  
ATOM   7541  CA  ALA C 218      96.747 -38.328-182.435  1.00 53.86           C  
ANISOU 7541  CA  ALA C 218     9402   5785   5278   -139   -638   1367       C  
ATOM   7542  C   ALA C 218      97.263 -37.056-181.775  1.00 56.41           C  
ANISOU 7542  C   ALA C 218     9648   6221   5563    -76   -620   1316       C  
ATOM   7543  O   ALA C 218      98.329 -36.551-182.144  1.00 58.81           O  
ANISOU 7543  O   ALA C 218     9878   6539   5927     52   -692   1255       O  
ATOM   7544  CB  ALA C 218      95.723 -37.988-183.519  1.00 49.39           C  
ANISOU 7544  CB  ALA C 218     8688   5272   4808   -205   -536   1323       C  
ATOM   7545  N   THR C 219      96.527 -36.521-180.799  1.00 51.92           N  
ANISOU 7545  N   THR C 219     9097   5736   4894   -168   -521   1338       N  
ATOM   7546  CA  THR C 219      96.956 -35.274-180.173  1.00 54.81           C  
ANISOU 7546  CA  THR C 219     9400   6206   5219   -113   -502   1284       C  
ATOM   7547  C   THR C 219      98.241 -35.477-179.375  1.00 50.35           C  
ANISOU 7547  C   THR C 219     8953   5589   4587    -21   -643   1305       C  
ATOM   7548  O   THR C 219      99.211 -34.732-179.549  1.00 49.91           O  
ANISOU 7548  O   THR C 219     8815   5571   4580     89   -708   1240       O  
ATOM   7549  CB  THR C 219      95.843 -34.704-179.290  1.00 60.03           C  
ANISOU 7549  CB  THR C 219    10067   6963   5780   -228   -358   1301       C  
ATOM   7550  OG1 THR C 219      94.663 -34.494-180.083  1.00 56.82           O  
ANISOU 7550  OG1 THR C 219     9528   6609   5451   -305   -235   1278       O  
ATOM   7551  CG2 THR C 219      96.282 -33.379-178.683  1.00 54.01           C  
ANISOU 7551  CG2 THR C 219     9249   6299   4973   -167   -341   1236       C  
ATOM   7552  N   ASN C 220      98.275 -36.486-178.499  1.00 53.05           N  
ANISOU 7552  N   ASN C 220     9491   5845   4821    -66   -699   1396       N  
ATOM   7553  CA  ASN C 220      99.510 -36.849-177.797  1.00 50.09           C  
ANISOU 7553  CA  ASN C 220     9240   5403   4389     28   -857   1424       C  
ATOM   7554  C   ASN C 220     100.088 -35.652-177.034  1.00 54.04           C  
ANISOU 7554  C   ASN C 220     9701   6000   4832     79   -871   1373       C  
ATOM   7555  O   ASN C 220     101.289 -35.369-177.089  1.00 50.23           O  
ANISOU 7555  O   ASN C 220     9181   5511   4393    199   -994   1335       O  
ATOM   7556  CB  ASN C 220     100.528 -37.429-178.788  1.00 50.46           C  
ANISOU 7556  CB  ASN C 220     9245   5363   4563    156   -985   1399       C  
ATOM   7557  CG  ASN C 220     101.729 -38.052-178.104  1.00 53.43           C  
ANISOU 7557  CG  ASN C 220     9757   5652   4891    254  -1159   1440       C  
ATOM   7558  OD1 ASN C 220     101.637 -38.522-176.980  1.00 56.02           O  
ANISOU 7558  OD1 ASN C 220    10266   5938   5083    202  -1195   1517       O  
ATOM   7559  ND2 ASN C 220     102.865 -38.057-178.789  1.00 57.20           N  
ANISOU 7559  ND2 ASN C 220    10149   6105   5480    397  -1266   1390       N  
ATOM   7560  N   ARG C 221      99.218 -34.923-176.333  1.00 52.42           N  
ANISOU 7560  N   ARG C 221     9497   5887   4532    -13   -743   1369       N  
ATOM   7561  CA  ARG C 221      99.596 -33.747-175.543  1.00 53.79           C  
ANISOU 7561  CA  ARG C 221     9653   6150   4635     18   -740   1319       C  
ATOM   7562  C   ARG C 221     100.305 -32.681-176.378  1.00 54.81           C  
ANISOU 7562  C   ARG C 221     9589   6342   4895    122   -769   1215       C  
ATOM   7563  O   ARG C 221     101.068 -31.874-175.841  1.00 49.33           O  
ANISOU 7563  O   ARG C 221     8887   5689   4166    179   -833   1174       O  
ATOM   7564  CB  ARG C 221     100.472 -34.133-174.335  1.00 57.75           C  
ANISOU 7564  CB  ARG C 221    10343   6595   5004     52   -880   1373       C  
ATOM   7565  CG  ARG C 221     100.057 -35.405-173.605  1.00 60.32           C  
ANISOU 7565  CG  ARG C 221    10886   6825   5208    -32   -896   1489       C  
ATOM   7566  CD  ARG C 221      99.430 -35.104-172.245  1.00 79.32           C  
ANISOU 7566  CD  ARG C 221    13438   9280   7420   -131   -812   1528       C  
ATOM   7567  NE  ARG C 221      99.971 -35.953-171.183  1.00 91.67           N  
ANISOU 7567  NE  ARG C 221    15178  10764   8888   -131   -924   1592       N  
ATOM   7568  CZ  ARG C 221     100.619 -35.495-170.115  1.00 96.03           C  
ANISOU 7568  CZ  ARG C 221    15794  11342   9351    -97   -994   1571       C  
ATOM   7569  NH1 ARG C 221     100.794 -34.190-169.958  1.00101.71           N  
ANISOU 7569  NH1 ARG C 221    16451  12157  10036    -63   -971   1502       N  
ATOM   7570  NH2 ARG C 221     101.084 -36.335-169.196  1.00 93.88           N  
ANISOU 7570  NH2 ARG C 221    15655  10997   9020    -98  -1091   1618       N  
ATOM   7571  N   GLY C 222     100.085 -32.665-177.692  1.00 53.81           N  
ANISOU 7571  N   GLY C 222     9312   6218   4915    142   -728   1174       N  
ATOM   7572  CA  GLY C 222     100.676 -31.665-178.559  1.00 56.76           C  
ANISOU 7572  CA  GLY C 222     9506   6648   5411    228   -740   1081       C  
ATOM   7573  C   GLY C 222     101.780 -32.175-179.457  1.00 57.04           C  
ANISOU 7573  C   GLY C 222     9486   6620   5568    337   -863   1066       C  
ATOM   7574  O   GLY C 222     102.161 -31.470-180.400  1.00 48.31           O  
ANISOU 7574  O   GLY C 222     8222   5556   4576    396   -854    993       O  
ATOM   7575  N   ASN C 223     102.307 -33.373-179.206  1.00 53.13           N  
ANISOU 7575  N   ASN C 223     9118   6021   5048    368   -973   1131       N  
ATOM   7576  CA  ASN C 223     103.312 -33.974-180.080  1.00 56.98           C  
ANISOU 7576  CA  ASN C 223     9558   6441   5652    481  -1082   1116       C  
ATOM   7577  C   ASN C 223     102.573 -34.865-181.076  1.00 53.33           C  
ANISOU 7577  C   ASN C 223     9096   5912   5254    443  -1025   1137       C  
ATOM   7578  O   ASN C 223     102.494 -36.084-180.929  1.00 48.11           O  
ANISOU 7578  O   ASN C 223     8573   5144   4561    430  -1078   1205       O  
ATOM   7579  CB  ASN C 223     104.348 -34.741-179.257  1.00 56.27           C  
ANISOU 7579  CB  ASN C 223     9603   6270   5506    553  -1246   1170       C  
ATOM   7580  CG  ASN C 223     105.446 -35.333-180.116  1.00 66.94           C  
ANISOU 7580  CG  ASN C 223    10894   7558   6981    685  -1358   1149       C  
ATOM   7581  OD1 ASN C 223     105.643 -34.930-181.272  1.00 62.71           O  
ANISOU 7581  OD1 ASN C 223    10199   7058   6571    734  -1316   1081       O  
ATOM   7582  ND2 ASN C 223     106.166 -36.303-179.561  1.00 61.60           N  
ANISOU 7582  ND2 ASN C 223    10351   6786   6269    749  -1498   1206       N  
ATOM   7583  N   LEU C 224     102.027 -34.230-182.115  1.00 51.43           N  
ANISOU 7583  N   LEU C 224     8705   5731   5104    424   -923   1076       N  
ATOM   7584  CA  LEU C 224     101.015 -34.871-182.951  1.00 44.64           C  
ANISOU 7584  CA  LEU C 224     7845   4830   4287    354   -846   1093       C  
ATOM   7585  C   LEU C 224     101.583 -36.045-183.742  1.00 42.26           C  
ANISOU 7585  C   LEU C 224     7591   4409   4055    426   -935   1109       C  
ATOM   7586  O   LEU C 224     102.746 -36.046-184.158  1.00 47.17           O  
ANISOU 7586  O   LEU C 224     8163   5013   4746    551  -1023   1071       O  
ATOM   7587  CB  LEU C 224     100.397 -33.851-183.906  1.00 42.57           C  
ANISOU 7587  CB  LEU C 224     7410   4658   4107    331   -734   1020       C  
ATOM   7588  CG  LEU C 224      99.787 -32.605-183.250  1.00 51.31           C  
ANISOU 7588  CG  LEU C 224     8457   5881   5157    273   -637    992       C  
ATOM   7589  CD1 LEU C 224      99.050 -31.760-184.278  1.00 47.18           C  
ANISOU 7589  CD1 LEU C 224     7777   5428   4721    249   -533    929       C  
ATOM   7590  CD2 LEU C 224      98.857 -32.966-182.120  1.00 61.51           C  
ANISOU 7590  CD2 LEU C 224     9874   7175   6322    160   -578   1061       C  
ATOM   7591  N   ARG C 225     100.732 -37.057-183.943  1.00 46.70           N  
ANISOU 7591  N   ARG C 225     8253   4892   4601    343   -909   1164       N  
ATOM   7592  CA  ARG C 225     101.077 -38.305-184.613  1.00 44.55           C  
ANISOU 7592  CA  ARG C 225     8064   4487   4377    393   -990   1186       C  
ATOM   7593  C   ARG C 225     100.007 -38.605-185.654  1.00 46.64           C  
ANISOU 7593  C   ARG C 225     8292   4731   4698    309   -906   1177       C  
ATOM   7594  O   ARG C 225      98.810 -38.545-185.351  1.00 45.45           O  
ANISOU 7594  O   ARG C 225     8156   4614   4500    171   -815   1212       O  
ATOM   7595  CB  ARG C 225     101.175 -39.477-183.617  1.00 49.40           C  
ANISOU 7595  CB  ARG C 225     8892   4986   4892    368  -1077   1283       C  
ATOM   7596  CG  ARG C 225     102.259 -39.315-182.573  1.00 45.54           C  
ANISOU 7596  CG  ARG C 225     8460   4501   4342    455  -1183   1299       C  
ATOM   7597  CD  ARG C 225     102.304 -40.513-181.600  1.00 45.93           C  
ANISOU 7597  CD  ARG C 225     8741   4426   4285    426  -1276   1401       C  
ATOM   7598  NE  ARG C 225     101.193 -40.527-180.646  1.00 49.74           N  
ANISOU 7598  NE  ARG C 225     9327   4932   4640    264  -1189   1471       N  
ATOM   7599  CZ  ARG C 225     101.192 -41.245-179.521  1.00 56.37           C  
ANISOU 7599  CZ  ARG C 225    10369   5697   5354    218  -1250   1563       C  
ATOM   7600  NH1 ARG C 225     102.237 -42.007-179.215  1.00 51.77           N  
ANISOU 7600  NH1 ARG C 225     9857   5028   4787    324  -1390   1570       N  
ATOM   7601  NH2 ARG C 225     100.152 -41.204-178.696  1.00 49.25           N  
ANISOU 7601  NH2 ARG C 225     9551   4828   4335     65  -1152   1623       N  
ATOM   7602  N   SER C 226     100.429 -38.945-186.868  1.00 43.78           N  
ANISOU 7602  N   SER C 226     7884   4317   4434    390   -939   1130       N  
ATOM   7603  CA  SER C 226      99.460 -39.196-187.928  1.00 46.01           C  
ANISOU 7603  CA  SER C 226     8133   4578   4771    314   -873   1114       C  
ATOM   7604  C   SER C 226      98.679 -40.473-187.647  1.00 48.85           C  
ANISOU 7604  C   SER C 226     8664   4821   5077    205   -892   1198       C  
ATOM   7605  O   SER C 226      99.226 -41.457-187.143  1.00 54.99           O  
ANISOU 7605  O   SER C 226     9598   5485   5812    243   -988   1250       O  
ATOM   7606  CB  SER C 226     100.165 -39.281-189.278  1.00 50.46           C  
ANISOU 7606  CB  SER C 226     8627   5107   5437    433   -906   1042       C  
ATOM   7607  OG  SER C 226     100.822 -38.059-189.549  1.00 43.40           O  
ANISOU 7607  OG  SER C 226     7573   4326   4592    514   -879    970       O  
ATOM   7608  N   ALA C 227      97.386 -40.455-187.963  1.00 49.04           N  
ANISOU 7608  N   ALA C 227     8658   4869   5105     65   -805   1212       N  
ATOM   7609  CA  ALA C 227      96.570 -41.619-187.661  1.00 53.54           C  
ANISOU 7609  CA  ALA C 227     9383   5334   5626    -62   -815   1295       C  
ATOM   7610  C   ALA C 227      95.323 -41.628-188.531  1.00 54.73           C  
ANISOU 7610  C   ALA C 227     9462   5503   5830   -185   -739   1284       C  
ATOM   7611  O   ALA C 227      94.834 -40.578-188.965  1.00 46.68           O  
ANISOU 7611  O   ALA C 227     8274   4605   4856   -202   -655   1229       O  
ATOM   7612  CB  ALA C 227      96.194 -41.664-186.168  1.00 42.57           C  
ANISOU 7612  CB  ALA C 227     8087   3971   4116   -158   -786   1378       C  
ATOM   7613  N   ILE C 228      94.829 -42.833-188.793  1.00 55.28           N  
ANISOU 7613  N   ILE C 228     9665   5444   5894   -268   -780   1336       N  
ATOM   7614  CA  ILE C 228      93.546 -43.025-189.452  1.00 52.53           C  
ANISOU 7614  CA  ILE C 228     9273   5099   5585   -413   -723   1344       C  
ATOM   7615  C   ILE C 228      92.800 -44.120-188.695  1.00 54.34           C  
ANISOU 7615  C   ILE C 228     9667   5237   5742   -572   -730   1450       C  
ATOM   7616  O   ILE C 228      93.409 -45.070-188.188  1.00 53.14           O  
ANISOU 7616  O   ILE C 228     9699   4956   5535   -541   -818   1504       O  
ATOM   7617  CB  ILE C 228      93.715 -43.355-190.958  1.00 47.31           C  
ANISOU 7617  CB  ILE C 228     8594   4365   5016   -351   -775   1278       C  
ATOM   7618  CG1 ILE C 228      92.355 -43.461-191.648  1.00 48.09           C  
ANISOU 7618  CG1 ILE C 228     8634   4478   5159   -507   -725   1283       C  
ATOM   7619  CG2 ILE C 228      94.507 -44.637-191.140  1.00 44.35           C  
ANISOU 7619  CG2 ILE C 228     8413   3809   4630   -277   -895   1300       C  
ATOM   7620  CD1 ILE C 228      92.434 -43.580-193.200  1.00 42.40           C  
ANISOU 7620  CD1 ILE C 228     7881   3706   4524   -450   -768   1208       C  
ATOM   7621  N   THR C 229      91.491 -43.941-188.548  1.00 49.87           N  
ANISOU 7621  N   THR C 229     9032   4743   5174   -741   -634   1483       N  
ATOM   7622  CA  THR C 229      90.607 -44.965-188.011  1.00 52.31           C  
ANISOU 7622  CA  THR C 229     9474   4972   5429   -922   -626   1583       C  
ATOM   7623  C   THR C 229      89.637 -45.380-189.101  1.00 62.45           C  
ANISOU 7623  C   THR C 229    10713   6220   6795  -1034   -625   1571       C  
ATOM   7624  O   THR C 229      88.953 -44.531-189.680  1.00 60.80           O  
ANISOU 7624  O   THR C 229    10315   6132   6654  -1064   -552   1519       O  
ATOM   7625  CB  THR C 229      89.830 -44.468-186.794  1.00 50.17           C  
ANISOU 7625  CB  THR C 229     9160   4822   5079  -1046   -505   1641       C  
ATOM   7626  OG1 THR C 229      90.753 -44.119-185.760  1.00 55.39           O  
ANISOU 7626  OG1 THR C 229     9885   5507   5653   -945   -520   1652       O  
ATOM   7627  CG2 THR C 229      88.890 -45.557-186.288  1.00 52.33           C  
ANISOU 7627  CG2 THR C 229     9569   5014   5298  -1248   -489   1749       C  
ATOM   7628  N   VAL C 230      89.576 -46.681-189.371  1.00 61.00           N  
ANISOU 7628  N   VAL C 230    10708   5865   6605  -1095   -713   1621       N  
ATOM   7629  CA  VAL C 230      88.793 -47.231-190.470  1.00 58.79           C  
ANISOU 7629  CA  VAL C 230    10420   5518   6399  -1194   -743   1608       C  
ATOM   7630  C   VAL C 230      87.574 -47.944-189.895  1.00 58.48           C  
ANISOU 7630  C   VAL C 230    10443   5453   6325  -1431   -700   1709       C  
ATOM   7631  O   VAL C 230      87.705 -48.933-189.159  1.00 57.65           O  
ANISOU 7631  O   VAL C 230    10539   5224   6143  -1496   -745   1797       O  
ATOM   7632  CB  VAL C 230      89.632 -48.182-191.332  1.00 59.62           C  
ANISOU 7632  CB  VAL C 230    10687   5438   6528  -1085   -880   1577       C  
ATOM   7633  CG1 VAL C 230      88.833 -48.637-192.540  1.00 62.36           C  
ANISOU 7633  CG1 VAL C 230    11022   5722   6949  -1181   -913   1551       C  
ATOM   7634  CG2 VAL C 230      90.922 -47.500-191.762  1.00 56.64           C  
ANISOU 7634  CG2 VAL C 230    10249   5094   6179   -850   -910   1485       C  
ATOM   7635  N   PHE C 231      86.399 -47.456-190.247  1.00 58.66           N  
ANISOU 7635  N   PHE C 231    10293   5589   6407  -1562   -617   1700       N  
ATOM   7636  CA  PHE C 231      85.112 -48.005-189.847  1.00 66.20           C  
ANISOU 7636  CA  PHE C 231    11254   6548   7352  -1800   -561   1787       C  
ATOM   7637  C   PHE C 231      84.591 -48.960-190.918  1.00 60.42           C  
ANISOU 7637  C   PHE C 231    10591   5679   6686  -1902   -656   1789       C  
ATOM   7638  O   PHE C 231      85.160 -49.053-192.005  1.00 57.72           O  
ANISOU 7638  O   PHE C 231    10272   5260   6397  -1780   -749   1713       O  
ATOM   7639  CB  PHE C 231      84.140 -46.850-189.573  1.00 62.49           C  
ANISOU 7639  CB  PHE C 231    10534   6293   6915  -1872   -414   1771       C  
ATOM   7640  CG  PHE C 231      84.473 -46.087-188.318  1.00 59.55           C  
ANISOU 7640  CG  PHE C 231    10132   6040   6456  -1818   -314   1788       C  
ATOM   7641  CD1 PHE C 231      84.208 -46.639-187.079  1.00 60.43           C  
ANISOU 7641  CD1 PHE C 231    10369   6132   6462  -1942   -262   1892       C  
ATOM   7642  CD2 PHE C 231      85.060 -44.832-188.377  1.00 54.10           C  
ANISOU 7642  CD2 PHE C 231     9301   5473   5782  -1648   -275   1702       C  
ATOM   7643  CE1 PHE C 231      84.520 -45.957-185.912  1.00 55.76           C  
ANISOU 7643  CE1 PHE C 231     9768   5642   5776  -1892   -174   1907       C  
ATOM   7644  CE2 PHE C 231      85.362 -44.135-187.224  1.00 60.50           C  
ANISOU 7644  CE2 PHE C 231    10095   6384   6507  -1602   -191   1715       C  
ATOM   7645  CZ  PHE C 231      85.091 -44.705-185.979  1.00 52.50           C  
ANISOU 7645  CZ  PHE C 231     9214   5351   5382  -1722   -141   1816       C  
ATOM   7646  N   PRO C 232      83.540 -49.736-190.631  1.00 65.49           N  
ANISOU 7646  N   PRO C 232    11283   6279   7321  -2129   -637   1877       N  
ATOM   7647  CA  PRO C 232      83.135 -50.786-191.580  1.00 60.97           C  
ANISOU 7647  CA  PRO C 232    10820   5547   6800  -2231   -748   1885       C  
ATOM   7648  C   PRO C 232      82.837 -50.253-192.977  1.00 61.25           C  
ANISOU 7648  C   PRO C 232    10697   5630   6947  -2184   -783   1785       C  
ATOM   7649  O   PRO C 232      82.291 -49.160-193.153  1.00 53.64           O  
ANISOU 7649  O   PRO C 232     9495   4846   6039  -2181   -695   1739       O  
ATOM   7650  CB  PRO C 232      81.885 -51.385-190.934  1.00 56.10           C  
ANISOU 7650  CB  PRO C 232    10211   4937   6166  -2504   -687   1995       C  
ATOM   7651  CG  PRO C 232      82.129 -51.210-189.464  1.00 61.76           C  
ANISOU 7651  CG  PRO C 232    10962   5726   6777  -2497   -588   2056       C  
ATOM   7652  CD  PRO C 232      82.830 -49.875-189.343  1.00 62.52           C  
ANISOU 7652  CD  PRO C 232    10918   5966   6870  -2301   -528   1982       C  
ATOM   7653  N   GLN C 233      83.195 -51.056-193.974  1.00 57.65           N  
ANISOU 7653  N   GLN C 233    10386   5002   6516  -2147   -916   1750       N  
ATOM   7654  CA  GLN C 233      82.951 -50.698-195.358  1.00 58.60           C  
ANISOU 7654  CA  GLN C 233    10399   5140   6728  -2107   -967   1657       C  
ATOM   7655  C   GLN C 233      81.455 -50.727-195.668  1.00 61.31           C  
ANISOU 7655  C   GLN C 233    10604   5549   7141  -2335   -942   1689       C  
ATOM   7656  O   GLN C 233      80.659 -51.385-194.991  1.00 62.85           O  
ANISOU 7656  O   GLN C 233    10843   5719   7317  -2541   -915   1786       O  
ATOM   7657  CB  GLN C 233      83.695 -51.660-196.292  1.00 64.31           C  
ANISOU 7657  CB  GLN C 233    11341   5648   7445  -2017  -1114   1615       C  
ATOM   7658  CG  GLN C 233      83.243 -53.114-196.162  1.00 62.66           C  
ANISOU 7658  CG  GLN C 233    11322   5275   7211  -2175  -1192   1679       C  
ATOM   7659  CD  GLN C 233      84.392 -54.113-196.266  1.00 71.48           C  
ANISOU 7659  CD  GLN C 233    12646   6236   8276  -2004  -1289   1632       C  
ATOM   7660  OE1 GLN C 233      84.453 -54.915-197.202  1.00 67.88           O  
ANISOU 7660  OE1 GLN C 233    12294   5660   7838  -1984  -1390   1577       O  
ATOM   7661  NE2 GLN C 233      85.298 -54.077-195.294  1.00 78.09           N  
ANISOU 7661  NE2 GLN C 233    13542   7081   9046  -1881  -1259   1653       N  
ATOM   7662  N   ARG C 234      81.076 -49.998-196.712  1.00 62.69           N  
ANISOU 7662  N   ARG C 234    10608   5811   7401  -2299   -952   1607       N  
ATOM   7663  CA  ARG C 234      79.744 -50.180-197.256  1.00 68.29           C  
ANISOU 7663  CA  ARG C 234    11208   6548   8189  -2502   -972   1626       C  
ATOM   7664  C   ARG C 234      79.629 -51.564-197.886  1.00 69.57           C  
ANISOU 7664  C   ARG C 234    11597   6489   8348  -2611  -1115   1650       C  
ATOM   7665  O   ARG C 234      80.620 -52.176-198.290  1.00 67.06           O  
ANISOU 7665  O   ARG C 234    11489   6005   7984  -2482  -1209   1616       O  
ATOM   7666  CB  ARG C 234      79.426 -49.112-198.303  1.00 62.46           C  
ANISOU 7666  CB  ARG C 234    10257   5937   7537  -2424   -973   1530       C  
ATOM   7667  CG  ARG C 234      80.127 -49.287-199.623  1.00 65.43           C  
ANISOU 7667  CG  ARG C 234    10743   6193   7924  -2285  -1097   1439       C  
ATOM   7668  CD  ARG C 234      79.431 -48.453-200.688  1.00 69.20           C  
ANISOU 7668  CD  ARG C 234    11023   6779   8491  -2287  -1116   1370       C  
ATOM   7669  NE  ARG C 234      78.948 -47.185-200.145  1.00 64.81           N  
ANISOU 7669  NE  ARG C 234    10206   6444   7974  -2272   -986   1367       N  
ATOM   7670  CZ  ARG C 234      79.315 -45.984-200.584  1.00 67.22           C  
ANISOU 7670  CZ  ARG C 234    10373   6865   8303  -2107   -950   1287       C  
ATOM   7671  NH1 ARG C 234      80.171 -45.866-201.590  1.00 63.27           N  
ANISOU 7671  NH1 ARG C 234     9959   6289   7791  -1947  -1027   1206       N  
ATOM   7672  NH2 ARG C 234      78.816 -44.893-200.019  1.00 68.64           N  
ANISOU 7672  NH2 ARG C 234    10329   7234   8516  -2102   -834   1289       N  
ATOM   7673  N   CYS C 235      78.400 -52.059-197.958  1.00 82.06           N  
ANISOU 7673  N   CYS C 235    13132   8068   9980  -2851  -1131   1708       N  
ATOM   7674  CA  CYS C 235      78.098 -53.272-198.704  1.00 93.17           C  
ANISOU 7674  CA  CYS C 235    14714   9288  11400  -2966  -1272   1714       C  
ATOM   7675  C   CYS C 235      76.603 -53.297-198.990  1.00 95.73           C  
ANISOU 7675  C   CYS C 235    14862   9697  11815  -3204  -1272   1746       C  
ATOM   7676  O   CYS C 235      75.837 -52.565-198.352  1.00 91.28           O  
ANISOU 7676  O   CYS C 235    14082   9308  11291  -3308  -1151   1794       O  
ATOM   7677  CB  CYS C 235      78.542 -54.532-197.939  1.00 99.67           C  
ANISOU 7677  CB  CYS C 235    15747   9990  12132  -2961  -1293   1754       C  
ATOM   7678  SG  CYS C 235      78.180 -54.535-196.184  1.00104.77           S  
ANISOU 7678  SG  CYS C 235    16345  10744  12720  -3078  -1140   1870       S  
ATOM   7679  N   PRO C 236      76.163 -54.101-199.978  1.00102.30           N  
ANISOU 7679  N   PRO C 236    15762  10425  12681  -3272  -1402   1708       N  
ATOM   7680  CA  PRO C 236      74.744 -54.122-200.368  1.00105.47           C  
ANISOU 7680  CA  PRO C 236    15987  10908  13180  -3490  -1422   1730       C  
ATOM   7681  C   PRO C 236      73.760 -54.324-199.227  1.00108.89           C  
ANISOU 7681  C   PRO C 236    16294  11454  13627  -3692  -1305   1831       C  
ATOM   7682  O   PRO C 236      74.103 -54.900-198.189  1.00106.60           O  
ANISOU 7682  O   PRO C 236    16122  11126  13254  -3696  -1242   1889       O  
ATOM   7683  CB  PRO C 236      74.670 -55.305-201.345  1.00103.56           C  
ANISOU 7683  CB  PRO C 236    15922  10496  12929  -3514  -1584   1685       C  
ATOM   7684  CG  PRO C 236      76.082 -55.605-201.754  1.00101.00           C  
ANISOU 7684  CG  PRO C 236    15831  10024  12521  -3279  -1650   1614       C  
ATOM   7685  CD  PRO C 236      77.021 -54.724-201.001  1.00100.44           C  
ANISOU 7685  CD  PRO C 236    15736  10018  12409  -3117  -1539   1621       C  
ATOM   7686  N   GLY C 237      72.529 -53.853-199.417  1.00112.80           N  
ANISOU 7686  N   GLY C 237    16543  12090  14227  -3857  -1275   1850       N  
ATOM   7687  CA  GLY C 237      71.444 -54.141-198.499  1.00117.01           C  
ANISOU 7687  CA  GLY C 237    16940  12732  14788  -4064  -1170   1937       C  
ATOM   7688  C   GLY C 237      71.452 -53.334-197.218  1.00119.03           C  
ANISOU 7688  C   GLY C 237    17064  13150  15014  -4061   -977   1996       C  
ATOM   7689  O   GLY C 237      70.409 -52.821-196.800  1.00120.58           O  
ANISOU 7689  O   GLY C 237    17012  13523  15281  -4197   -867   2035       O  
ATOM   7690  N   ARG C 238      72.613 -53.225-196.578  1.00121.59           N  
ANISOU 7690  N   ARG C 238    17549  13420  15230  -3900   -932   2000       N  
ATOM   7691  CA  ARG C 238      72.755 -52.509-195.320  1.00123.76           C  
ANISOU 7691  CA  ARG C 238    17739  13834  15452  -3879   -755   2053       C  
ATOM   7692  C   ARG C 238      73.398 -51.146-195.549  1.00112.02           C  
ANISOU 7692  C   ARG C 238    16131  12459  13974  -3668   -709   1978       C  
ATOM   7693  O   ARG C 238      74.021 -50.887-196.582  1.00106.86           O  
ANISOU 7693  O   ARG C 238    15515  11747  13342  -3500   -816   1884       O  
ATOM   7694  CB  ARG C 238      73.573 -53.323-194.308  1.00133.98           C  
ANISOU 7694  CB  ARG C 238    19276  15018  16612  -3820   -731   2099       C  
ATOM   7695  CG  ARG C 238      74.951 -53.750-194.790  1.00134.63           C  
ANISOU 7695  CG  ARG C 238    19614  14915  16626  -3613   -859   2041       C  
ATOM   7696  CD  ARG C 238      75.078 -55.274-194.861  1.00136.07           C  
ANISOU 7696  CD  ARG C 238    20029  14911  16762  -3657   -970   2055       C  
ATOM   7697  NE  ARG C 238      75.141 -55.912-193.545  1.00135.36           N  
ANISOU 7697  NE  ARG C 238    20045  14808  16579  -3712   -892   2136       N  
ATOM   7698  CZ  ARG C 238      76.258 -56.068-192.839  1.00130.34           C  
ANISOU 7698  CZ  ARG C 238    19580  14105  15840  -3558   -885   2142       C  
ATOM   7699  NH1 ARG C 238      77.414 -55.622-193.312  1.00132.34           N  
ANISOU 7699  NH1 ARG C 238    19906  14305  16073  -3335   -944   2071       N  
ATOM   7700  NH2 ARG C 238      76.221 -56.664-191.655  1.00123.86           N  
ANISOU 7700  NH2 ARG C 238    18853  13274  14936  -3623   -821   2218       N  
ATOM   7701  N   GLY C 239      73.246 -50.277-194.555  1.00105.11           N  
ANISOU 7701  N   GLY C 239    15092  11769  13076  -3633   -538   1996       N  
ATOM   7702  CA  GLY C 239      73.563 -48.869-194.700  1.00 97.87           C  
ANISOU 7702  CA  GLY C 239    13983  11018  12185  -3421   -468   1903       C  
ATOM   7703  C   GLY C 239      75.037 -48.531-194.635  1.00 94.50           C  
ANISOU 7703  C   GLY C 239    13708  10528  11671  -3165   -491   1845       C  
ATOM   7704  O   GLY C 239      75.908 -49.322-195.020  1.00 96.15           O  
ANISOU 7704  O   GLY C 239    14157  10546  11829  -3101   -612   1837       O  
ATOM   7705  N   ASP C 240      75.316 -47.322-194.144  1.00 89.37           N  
ANISOU 7705  N   ASP C 240    12909  10041  11007  -3016   -374   1800       N  
ATOM   7706  CA  ASP C 240      76.655 -46.752-194.120  1.00 79.80           C  
ANISOU 7706  CA  ASP C 240    11783   8808   9730  -2767   -386   1734       C  
ATOM   7707  C   ASP C 240      76.926 -46.097-192.775  1.00 80.47           C  
ANISOU 7707  C   ASP C 240    11828   9015   9733  -2711   -233   1762       C  
ATOM   7708  O   ASP C 240      76.041 -45.459-192.197  1.00 87.75           O  
ANISOU 7708  O   ASP C 240    12554  10106  10682  -2790   -100   1781       O  
ATOM   7709  CB  ASP C 240      76.838 -45.700-195.225  1.00 82.06           C  
ANISOU 7709  CB  ASP C 240    11916   9168  10095  -2600   -427   1619       C  
ATOM   7710  CG  ASP C 240      77.516 -46.257-196.448  1.00 82.41           C  
ANISOU 7710  CG  ASP C 240    12118   9044  10152  -2517   -590   1564       C  
ATOM   7711  OD1 ASP C 240      78.290 -47.218-196.293  1.00 87.42           O  
ANISOU 7711  OD1 ASP C 240    12993   9510  10714  -2500   -659   1594       O  
ATOM   7712  OD2 ASP C 240      77.286 -45.733-197.556  1.00 83.27           O  
ANISOU 7712  OD2 ASP C 240    12116   9185  10337  -2463   -650   1490       O  
ATOM   7713  N   PHE C 241      78.153 -46.253-192.286  1.00 73.16           N  
ANISOU 7713  N   PHE C 241    11088   8003   8708  -2572   -256   1762       N  
ATOM   7714  CA  PHE C 241      78.647 -45.396-191.219  1.00 71.98           C  
ANISOU 7714  CA  PHE C 241    10898   7969   8482  -2462   -137   1757       C  
ATOM   7715  C   PHE C 241      79.091 -44.074-191.832  1.00 66.02           C  
ANISOU 7715  C   PHE C 241     9984   7322   7779  -2260   -129   1644       C  
ATOM   7716  O   PHE C 241      79.829 -44.062-192.821  1.00 70.58           O  
ANISOU 7716  O   PHE C 241    10616   7816   8387  -2129   -240   1577       O  
ATOM   7717  CB  PHE C 241      79.817 -46.046-190.483  1.00 70.96           C  
ANISOU 7717  CB  PHE C 241    11025   7707   8232  -2385   -180   1799       C  
ATOM   7718  CG  PHE C 241      79.436 -47.227-189.634  1.00 68.99           C  
ANISOU 7718  CG  PHE C 241    10947   7361   7907  -2577   -169   1919       C  
ATOM   7719  CD1 PHE C 241      79.400 -48.496-190.175  1.00 66.14           C  
ANISOU 7719  CD1 PHE C 241    10763   6811   7557  -2676   -294   1962       C  
ATOM   7720  CD2 PHE C 241      79.146 -47.068-188.289  1.00 76.45           C  
ANISOU 7720  CD2 PHE C 241    11890   8394   8761  -2655    -34   1990       C  
ATOM   7721  CE1 PHE C 241      79.069 -49.588-189.395  1.00 72.35           C  
ANISOU 7721  CE1 PHE C 241    11723   7497   8271  -2858   -289   2077       C  
ATOM   7722  CE2 PHE C 241      78.812 -48.153-187.505  1.00 75.53           C  
ANISOU 7722  CE2 PHE C 241    11945   8185   8567  -2837    -22   2107       C  
ATOM   7723  CZ  PHE C 241      78.774 -49.416-188.060  1.00 75.78           C  
ANISOU 7723  CZ  PHE C 241    12153   8026   8616  -2940   -151   2153       C  
ATOM   7724  N   ARG C 242      78.631 -42.964-191.259  1.00 62.92           N  
ANISOU 7724  N   ARG C 242     9400   7113   7395  -2237      6   1624       N  
ATOM   7725  CA  ARG C 242      79.044 -41.645-191.718  1.00 60.25           C  
ANISOU 7725  CA  ARG C 242     8918   6878   7098  -2050     22   1522       C  
ATOM   7726  C   ARG C 242      79.340 -40.750-190.528  1.00 64.02           C  
ANISOU 7726  C   ARG C 242     9351   7477   7497  -1971    152   1519       C  
ATOM   7727  O   ARG C 242      78.611 -40.761-189.532  1.00 67.64           O  
ANISOU 7727  O   ARG C 242     9764   8022   7916  -2089    274   1578       O  
ATOM   7728  CB  ARG C 242      77.978 -40.972-192.587  1.00 63.72           C  
ANISOU 7728  CB  ARG C 242     9121   7428   7663  -2088     35   1474       C  
ATOM   7729  CG  ARG C 242      77.776 -41.594-193.965  1.00 64.51           C  
ANISOU 7729  CG  ARG C 242     9249   7418   7845  -2128   -110   1451       C  
ATOM   7730  CD  ARG C 242      79.040 -41.568-194.809  1.00 64.86           C  
ANISOU 7730  CD  ARG C 242     9424   7348   7872  -1948   -226   1383       C  
ATOM   7731  NE  ARG C 242      79.502 -40.217-195.119  1.00 66.42           N  
ANISOU 7731  NE  ARG C 242     9495   7648   8092  -1767   -195   1295       N  
ATOM   7732  CZ  ARG C 242      79.124 -39.512-196.185  1.00 65.20           C  
ANISOU 7732  CZ  ARG C 242     9202   7547   8026  -1719   -233   1228       C  
ATOM   7733  NH1 ARG C 242      78.258 -40.019-197.056  1.00 60.64           N  
ANISOU 7733  NH1 ARG C 242     8583   6933   7525  -1837   -309   1235       N  
ATOM   7734  NH2 ARG C 242      79.609 -38.293-196.380  1.00 51.57           N  
ANISOU 7734  NH2 ARG C 242     7382   5904   6310  -1557   -203   1155       N  
ATOM   7735  N   ILE C 243      80.417 -39.983-190.641  1.00 51.85           N  
ANISOU 7735  N   ILE C 243     7828   5941   5930  -1776    126   1449       N  
ATOM   7736  CA  ILE C 243      80.650 -38.838-189.774  1.00 56.15           C  
ANISOU 7736  CA  ILE C 243     8291   6618   6425  -1678    237   1417       C  
ATOM   7737  C   ILE C 243      80.128 -37.612-190.514  1.00 58.04           C  
ANISOU 7737  C   ILE C 243     8304   6982   6766  -1606    270   1332       C  
ATOM   7738  O   ILE C 243      80.693 -37.208-191.531  1.00 60.13           O  
ANISOU 7738  O   ILE C 243     8550   7211   7084  -1485    183   1262       O  
ATOM   7739  CB  ILE C 243      82.132 -38.696-189.417  1.00 53.54           C  
ANISOU 7739  CB  ILE C 243     8111   6221   6011  -1516    184   1393       C  
ATOM   7740  CG1 ILE C 243      82.647 -40.004-188.794  1.00 59.15           C  
ANISOU 7740  CG1 ILE C 243     9057   6788   6629  -1581    127   1479       C  
ATOM   7741  CG2 ILE C 243      82.327 -37.516-188.476  1.00 55.77           C  
ANISOU 7741  CG2 ILE C 243     8318   6636   6236  -1429    294   1360       C  
ATOM   7742  CD1 ILE C 243      84.137 -40.005-188.508  1.00 57.33           C  
ANISOU 7742  CD1 ILE C 243     8977   6479   6327  -1420     53   1459       C  
ATOM   7743  N   TRP C 244      79.029 -37.034-190.021  1.00 60.12           N  
ANISOU 7743  N   TRP C 244     8397   7391   7057  -1681    397   1339       N  
ATOM   7744  CA  TRP C 244      78.408 -35.909-190.717  1.00 66.35           C  
ANISOU 7744  CA  TRP C 244     8965   8296   7950  -1618    424   1264       C  
ATOM   7745  C   TRP C 244      79.281 -34.659-190.685  1.00 59.34           C  
ANISOU 7745  C   TRP C 244     8051   7455   7039  -1421    435   1181       C  
ATOM   7746  O   TRP C 244      79.193 -33.819-191.587  1.00 59.63           O  
ANISOU 7746  O   TRP C 244     7967   7532   7159  -1331    400   1109       O  
ATOM   7747  CB  TRP C 244      77.038 -35.600-190.113  1.00 73.95           C  
ANISOU 7747  CB  TRP C 244     9745   9405   8946  -1735    565   1290       C  
ATOM   7748  CG  TRP C 244      75.959 -36.535-190.554  1.00 76.15           C  
ANISOU 7748  CG  TRP C 244     9967   9664   9301  -1924    541   1349       C  
ATOM   7749  CD1 TRP C 244      76.090 -37.857-190.857  1.00 70.30           C  
ANISOU 7749  CD1 TRP C 244     9383   8780   8548  -2040    442   1411       C  
ATOM   7750  CD2 TRP C 244      74.579 -36.209-190.763  1.00 75.66           C  
ANISOU 7750  CD2 TRP C 244     9672   9728   9346  -2019    608   1347       C  
ATOM   7751  NE1 TRP C 244      74.875 -38.379-191.232  1.00 68.27           N  
ANISOU 7751  NE1 TRP C 244     9010   8550   8380  -2214    442   1451       N  
ATOM   7752  CE2 TRP C 244      73.932 -37.387-191.182  1.00 72.49           C  
ANISOU 7752  CE2 TRP C 244     9296   9254   8992  -2204    543   1414       C  
ATOM   7753  CE3 TRP C 244      73.829 -35.035-190.629  1.00 75.99           C  
ANISOU 7753  CE3 TRP C 244     9487   9936   9451  -1963    713   1295       C  
ATOM   7754  CZ2 TRP C 244      72.570 -37.429-191.469  1.00 76.01           C  
ANISOU 7754  CZ2 TRP C 244     9535   9794   9550  -2341    578   1432       C  
ATOM   7755  CZ3 TRP C 244      72.479 -35.076-190.916  1.00 78.46           C  
ANISOU 7755  CZ3 TRP C 244     9591  10343   9876  -2086    751   1311       C  
ATOM   7756  CH2 TRP C 244      71.862 -36.266-191.332  1.00 80.75           C  
ANISOU 7756  CH2 TRP C 244     9900  10565  10216  -2276    682   1380       C  
ATOM   7757  N   ASN C 245      80.109 -34.510-189.660  1.00 56.64           N  
ANISOU 7757  N   ASN C 245     7826   7109   6585  -1359    478   1191       N  
ATOM   7758  CA  ASN C 245      80.998 -33.363-189.574  1.00 55.81           C  
ANISOU 7758  CA  ASN C 245     7709   7041   6455  -1184    481   1116       C  
ATOM   7759  C   ASN C 245      82.108 -33.483-190.613  1.00 54.18           C  
ANISOU 7759  C   ASN C 245     7588   6723   6276  -1073    340   1074       C  
ATOM   7760  O   ASN C 245      82.590 -34.581-190.904  1.00 53.14           O  
ANISOU 7760  O   ASN C 245     7599   6465   6125  -1108    249   1114       O  
ATOM   7761  CB  ASN C 245      81.583 -33.267-188.163  1.00 57.22           C  
ANISOU 7761  CB  ASN C 245     8002   7238   6500  -1162    553   1144       C  
ATOM   7762  CG  ASN C 245      80.505 -33.137-187.095  1.00 58.07           C  
ANISOU 7762  CG  ASN C 245     8036   7462   6567  -1270    709   1184       C  
ATOM   7763  OD1 ASN C 245      79.626 -33.991-186.977  1.00 63.26           O  
ANISOU 7763  OD1 ASN C 245     8681   8117   7237  -1427    744   1253       O  
ATOM   7764  ND2 ASN C 245      80.570 -32.064-186.313  1.00 57.13           N  
ANISOU 7764  ND2 ASN C 245     7869   7445   6395  -1189    807   1141       N  
ATOM   7765  N   SER C 246      82.503 -32.345-191.190  1.00 47.45           N  
ANISOU 7765  N   SER C 246     6649   5914   5466   -937    324    993       N  
ATOM   7766  CA  SER C 246      83.593 -32.369-192.163  1.00 50.80           C  
ANISOU 7766  CA  SER C 246     7146   6243   5911   -828    207    949       C  
ATOM   7767  C   SER C 246      84.933 -32.620-191.485  1.00 48.13           C  
ANISOU 7767  C   SER C 246     6966   5840   5479   -751    174    961       C  
ATOM   7768  O   SER C 246      85.842 -33.184-192.101  1.00 45.66           O  
ANISOU 7768  O   SER C 246     6757   5422   5169   -696     75    954       O  
ATOM   7769  CB  SER C 246      83.638 -31.060-192.955  1.00 43.25           C  
ANISOU 7769  CB  SER C 246     6060   5352   5023   -715    203    865       C  
ATOM   7770  OG  SER C 246      84.063 -30.000-192.116  1.00 48.99           O  
ANISOU 7770  OG  SER C 246     6761   6155   5698   -627    274    830       O  
ATOM   7771  N   GLN C 247      85.075 -32.207-190.226  1.00 46.06           N  
ANISOU 7771  N   GLN C 247     6726   5641   5135   -742    254    975       N  
ATOM   7772  CA  GLN C 247      86.256 -32.500-189.431  1.00 44.49           C  
ANISOU 7772  CA  GLN C 247     6679   5384   4841   -683    219    995       C  
ATOM   7773  C   GLN C 247      85.820 -32.877-188.023  1.00 43.00           C  
ANISOU 7773  C   GLN C 247     6558   5229   4552   -778    304   1063       C  
ATOM   7774  O   GLN C 247      84.713 -32.551-187.587  1.00 50.76           O  
ANISOU 7774  O   GLN C 247     7442   6307   5536   -859    414   1075       O  
ATOM   7775  CB  GLN C 247      87.220 -31.315-189.356  1.00 40.63           C  
ANISOU 7775  CB  GLN C 247     6160   4937   4339   -537    211    924       C  
ATOM   7776  CG  GLN C 247      87.907 -30.964-190.649  1.00 41.72           C  
ANISOU 7776  CG  GLN C 247     6261   5033   4556   -435    127    862       C  
ATOM   7777  CD  GLN C 247      88.980 -29.922-190.437  1.00 45.24           C  
ANISOU 7777  CD  GLN C 247     6699   5510   4980   -307    115    804       C  
ATOM   7778  OE1 GLN C 247      89.573 -29.830-189.357  1.00 44.52           O  
ANISOU 7778  OE1 GLN C 247     6682   5428   4805   -284    126    820       O  
ATOM   7779  NE2 GLN C 247      89.239 -29.127-191.463  1.00 48.56           N  
ANISOU 7779  NE2 GLN C 247     7034   5943   5471   -229     89    740       N  
ATOM   7780  N   LEU C 248      86.707 -33.571-187.309  1.00 48.12           N  
ANISOU 7780  N   LEU C 248     7377   5798   5110   -765    253   1109       N  
ATOM   7781  CA  LEU C 248      86.393 -33.946-185.936  1.00 52.84           C  
ANISOU 7781  CA  LEU C 248     8066   6417   5593   -853    328   1178       C  
ATOM   7782  C   LEU C 248      86.265 -32.717-185.046  1.00 59.24           C  
ANISOU 7782  C   LEU C 248     8808   7353   6347   -807    433   1137       C  
ATOM   7783  O   LEU C 248      85.401 -32.672-184.160  1.00 53.03           O  
ANISOU 7783  O   LEU C 248     8007   6641   5500   -899    551   1173       O  
ATOM   7784  CB  LEU C 248      87.455 -34.898-185.391  1.00 50.91           C  
ANISOU 7784  CB  LEU C 248     8027   6052   5262   -831    232   1233       C  
ATOM   7785  CG  LEU C 248      87.571 -36.225-186.140  1.00 48.93           C  
ANISOU 7785  CG  LEU C 248     7876   5663   5053   -879    129   1279       C  
ATOM   7786  CD1 LEU C 248      88.578 -37.124-185.446  1.00 45.23           C  
ANISOU 7786  CD1 LEU C 248     7615   5079   4492   -851     40   1336       C  
ATOM   7787  CD2 LEU C 248      86.220 -36.916-186.264  1.00 48.36           C  
ANISOU 7787  CD2 LEU C 248     7772   5595   5009  -1053    190   1337       C  
ATOM   7788  N   VAL C 249      87.104 -31.710-185.273  1.00 49.61           N  
ANISOU 7788  N   VAL C 249     7547   6157   5144   -668    397   1061       N  
ATOM   7789  CA  VAL C 249      87.079 -30.474-184.505  1.00 48.36           C  
ANISOU 7789  CA  VAL C 249     7335   6105   4934   -612    482   1011       C  
ATOM   7790  C   VAL C 249      86.704 -29.350-185.462  1.00 53.45           C  
ANISOU 7790  C   VAL C 249     7801   6818   5690   -544    504    927       C  
ATOM   7791  O   VAL C 249      87.441 -29.053-186.410  1.00 50.96           O  
ANISOU 7791  O   VAL C 249     7459   6459   5443   -454    414    879       O  
ATOM   7792  CB  VAL C 249      88.424 -30.207-183.810  1.00 40.88           C  
ANISOU 7792  CB  VAL C 249     6510   5122   3900   -514    412    998       C  
ATOM   7793  CG1 VAL C 249      88.324 -28.990-182.926  1.00 41.75           C  
ANISOU 7793  CG1 VAL C 249     6586   5333   3942   -471    501    949       C  
ATOM   7794  CG2 VAL C 249      88.849 -31.417-182.978  1.00 43.92           C  
ANISOU 7794  CG2 VAL C 249     7085   5422   4181   -573    364   1086       C  
ATOM   7795  N   ARG C 250      85.539 -28.750-185.232  1.00 55.34           N  
ANISOU 7795  N   ARG C 250     7918   7162   5947   -588    626    910       N  
ATOM   7796  CA  ARG C 250      85.056 -27.625-186.018  1.00 53.48           C  
ANISOU 7796  CA  ARG C 250     7514   6997   5811   -524    654    833       C  
ATOM   7797  C   ARG C 250      84.440 -26.600-185.077  1.00 55.96           C  
ANISOU 7797  C   ARG C 250     7764   7425   6072   -506    787    797       C  
ATOM   7798  O   ARG C 250      83.837 -26.956-184.062  1.00 64.33           O  
ANISOU 7798  O   ARG C 250     8859   8531   7052   -589    888    843       O  
ATOM   7799  CB  ARG C 250      84.012 -28.059-187.046  1.00 54.16           C  
ANISOU 7799  CB  ARG C 250     7479   7087   6011   -598    654    846       C  
ATOM   7800  CG  ARG C 250      84.494 -29.077-188.057  1.00 52.69           C  
ANISOU 7800  CG  ARG C 250     7357   6785   5878   -619    527    875       C  
ATOM   7801  CD  ARG C 250      84.748 -28.406-189.386  1.00 54.78           C  
ANISOU 7801  CD  ARG C 250     7533   7036   6245   -527    454    807       C  
ATOM   7802  NE  ARG C 250      86.025 -27.710-189.385  1.00 58.36           N  
ANISOU 7802  NE  ARG C 250     8041   7464   6668   -400    401    757       N  
ATOM   7803  CZ  ARG C 250      86.429 -26.890-190.347  1.00 58.12           C  
ANISOU 7803  CZ  ARG C 250     7947   7431   6705   -307    352    692       C  
ATOM   7804  NH1 ARG C 250      85.647 -26.646-191.391  1.00 59.28           N  
ANISOU 7804  NH1 ARG C 250     7980   7597   6948   -318    344    668       N  
ATOM   7805  NH2 ARG C 250      87.616 -26.308-190.256  1.00 62.35           N  
ANISOU 7805  NH2 ARG C 250     8535   7946   7211   -207    309    654       N  
ATOM   7806  N   TYR C 251      84.591 -25.326-185.422  1.00 43.97           N  
ANISOU 7806  N   TYR C 251     6160   5950   4597   -397    791    714       N  
ATOM   7807  CA  TYR C 251      83.945 -24.258-184.674  1.00 44.50           C  
ANISOU 7807  CA  TYR C 251     6156   6123   4629   -364    915    666       C  
ATOM   7808  C   TYR C 251      82.578 -23.948-185.271  1.00 52.91           C  
ANISOU 7808  C   TYR C 251     7035   7266   5803   -392    990    647       C  
ATOM   7809  O   TYR C 251      82.410 -23.941-186.495  1.00 52.24           O  
ANISOU 7809  O   TYR C 251     6861   7155   5834   -378    917    631       O  
ATOM   7810  CB  TYR C 251      84.812 -23.000-184.673  1.00 49.30           C  
ANISOU 7810  CB  TYR C 251     6779   6728   5223   -232    876    585       C  
ATOM   7811  CG  TYR C 251      86.100 -23.138-183.905  1.00 45.52           C  
ANISOU 7811  CG  TYR C 251     6468   6193   4634   -200    812    597       C  
ATOM   7812  CD1 TYR C 251      86.099 -23.596-182.593  1.00 46.95           C  
ANISOU 7812  CD1 TYR C 251     6768   6389   4681   -256    872    643       C  
ATOM   7813  CD2 TYR C 251      87.320 -22.820-184.490  1.00 41.74           C  
ANISOU 7813  CD2 TYR C 251     6029   5648   4183   -118    690    564       C  
ATOM   7814  CE1 TYR C 251      87.263 -23.722-181.888  1.00 41.37           C  
ANISOU 7814  CE1 TYR C 251     6216   5630   3874   -226    799    654       C  
ATOM   7815  CE2 TYR C 251      88.497 -22.942-183.786  1.00 46.12           C  
ANISOU 7815  CE2 TYR C 251     6722   6156   4646    -89    623    574       C  
ATOM   7816  CZ  TYR C 251      88.455 -23.399-182.474  1.00 44.96           C  
ANISOU 7816  CZ  TYR C 251     6693   6022   4368   -142    672    619       C  
ATOM   7817  OH  TYR C 251      89.619 -23.528-181.762  1.00 47.81           O  
ANISOU 7817  OH  TYR C 251     7194   6336   4637   -111    592    631       O  
ATOM   7818  N   ALA C 252      81.605 -23.681-184.400  1.00 55.63           N  
ANISOU 7818  N   ALA C 252     7319   7710   6107   -430   1135    648       N  
ATOM   7819  CA  ALA C 252      80.264 -23.363-184.867  1.00 55.07           C  
ANISOU 7819  CA  ALA C 252     7055   7727   6143   -453   1214    629       C  
ATOM   7820  C   ALA C 252      80.252 -22.070-185.678  1.00 46.83           C  
ANISOU 7820  C   ALA C 252     5899   6702   5191   -321   1178    538       C  
ATOM   7821  O   ALA C 252      81.109 -21.194-185.524  1.00 46.84           O  
ANISOU 7821  O   ALA C 252     5969   6678   5151   -214   1143    482       O  
ATOM   7822  CB  ALA C 252      79.299 -23.217-183.694  1.00 49.53           C  
ANISOU 7822  CB  ALA C 252     6307   7137   5373   -502   1392    638       C  
ATOM   7823  N   GLY C 253      79.239 -21.951-186.532  1.00 53.86           N  
ANISOU 7823  N   GLY C 253     6618   7636   6209   -335   1184    527       N  
ATOM   7824  CA  GLY C 253      78.931 -20.705-187.207  1.00 54.24           C  
ANISOU 7824  CA  GLY C 253     6543   7718   6347   -217   1171    446       C  
ATOM   7825  C   GLY C 253      77.454 -20.374-187.103  1.00 59.70           C  
ANISOU 7825  C   GLY C 253     7043   8527   7115   -232   1287    430       C  
ATOM   7826  O   GLY C 253      76.615 -21.161-187.550  1.00 57.83           O  
ANISOU 7826  O   GLY C 253     6703   8314   6955   -334   1287    479       O  
ATOM   7827  N   TYR C 254      77.121 -19.218-186.523  1.00 66.59           N  
ANISOU 7827  N   TYR C 254     7861   9472   7968   -131   1383    361       N  
ATOM   7828  CA  TYR C 254      75.740 -18.821-186.262  1.00 66.10           C  
ANISOU 7828  CA  TYR C 254     7612   9534   7971   -127   1514    338       C  
ATOM   7829  C   TYR C 254      75.345 -17.635-187.137  1.00 69.61           C  
ANISOU 7829  C   TYR C 254     7923   9992   8532      6   1468    259       C  
ATOM   7830  O   TYR C 254      76.080 -16.646-187.209  1.00 72.89           O  
ANISOU 7830  O   TYR C 254     8416  10360   8919    127   1421    196       O  
ATOM   7831  CB  TYR C 254      75.546 -18.436-184.794  1.00 67.65           C  
ANISOU 7831  CB  TYR C 254     7852   9810   8044   -109   1684    317       C  
ATOM   7832  CG  TYR C 254      76.161 -19.366-183.767  1.00 67.82           C  
ANISOU 7832  CG  TYR C 254     8052   9802   7914   -212   1724    384       C  
ATOM   7833  CD1 TYR C 254      75.606 -20.614-183.502  1.00 63.95           C  
ANISOU 7833  CD1 TYR C 254     7545   9339   7415   -371   1775    474       C  
ATOM   7834  CD2 TYR C 254      77.274 -18.975-183.032  1.00 65.22           C  
ANISOU 7834  CD2 TYR C 254     7912   9420   7450   -152   1706    359       C  
ATOM   7835  CE1 TYR C 254      76.156 -21.456-182.547  1.00 67.66           C  
ANISOU 7835  CE1 TYR C 254     8193   9776   7741   -463   1807    539       C  
ATOM   7836  CE2 TYR C 254      77.831 -19.809-182.077  1.00 67.82           C  
ANISOU 7836  CE2 TYR C 254     8410   9720   7637   -240   1732    422       C  
ATOM   7837  CZ  TYR C 254      77.267 -21.049-181.836  1.00 68.65           C  
ANISOU 7837  CZ  TYR C 254     8505   9847   7732   -393   1783    513       C  
ATOM   7838  OH  TYR C 254      77.819 -21.883-180.882  1.00 64.53           O  
ANISOU 7838  OH  TYR C 254     8165   9288   7064   -479   1803    580       O  
ATOM   7839  N   ARG C 255      74.170 -17.716-187.760  1.00 73.53           N  
ANISOU 7839  N   ARG C 255     8222  10556   9161    -19   1479    264       N  
ATOM   7840  CA  ARG C 255      73.610 -16.634-188.562  1.00 78.18           C  
ANISOU 7840  CA  ARG C 255     8667  11168   9869    106   1438    195       C  
ATOM   7841  C   ARG C 255      72.774 -15.688-187.688  1.00 76.46           C  
ANISOU 7841  C   ARG C 255     8339  11064   9647    198   1599    131       C  
ATOM   7842  O   ARG C 255      72.285 -16.067-186.625  1.00 74.35           O  
ANISOU 7842  O   ARG C 255     8050  10884   9317    135   1753    153       O  
ATOM   7843  CB  ARG C 255      72.756 -17.212-189.694  1.00 80.48           C  
ANISOU 7843  CB  ARG C 255     8799  11473  10308     36   1354    232       C  
ATOM   7844  CG  ARG C 255      72.761 -16.413-190.989  1.00 85.80           C  
ANISOU 7844  CG  ARG C 255     9415  12094  11089    143   1213    184       C  
ATOM   7845  CD  ARG C 255      71.928 -17.121-192.059  1.00 94.96           C  
ANISOU 7845  CD  ARG C 255    10433  13265  12382     56   1121    227       C  
ATOM   7846  NE  ARG C 255      72.581 -18.318-192.592  1.00100.38           N  
ANISOU 7846  NE  ARG C 255    11242  13858  13041    -68   1016    296       N  
ATOM   7847  CZ  ARG C 255      71.988 -19.205-193.390  1.00100.30           C  
ANISOU 7847  CZ  ARG C 255    11151  13841  13117   -179    936    346       C  
ATOM   7848  NH1 ARG C 255      70.721 -19.042-193.747  1.00 99.30           N  
ANISOU 7848  NH1 ARG C 255    10808  13802  13118   -187    944    339       N  
ATOM   7849  NH2 ARG C 255      72.660 -20.262-193.832  1.00 96.84           N  
ANISOU 7849  NH2 ARG C 255    10848  13306  12642   -279    843    401       N  
ATOM   7850  N   GLN C 256      72.616 -14.442-188.153  1.00 84.29           N  
ANISOU 7850  N   GLN C 256     9269  12052  10704    352   1565     51       N  
ATOM   7851  CA  GLN C 256      71.907 -13.401-187.403  1.00 92.83           C  
ANISOU 7851  CA  GLN C 256    10260  13226  11785    471   1705    -25       C  
ATOM   7852  C   GLN C 256      70.996 -12.608-188.346  1.00100.94           C  
ANISOU 7852  C   GLN C 256    11093  14285  12975    579   1651    -74       C  
ATOM   7853  O   GLN C 256      71.086 -12.738-189.569  1.00109.90           O  
ANISOU 7853  O   GLN C 256    12199  15356  14203    571   1494    -55       O  
ATOM   7854  CB  GLN C 256      72.899 -12.459-186.697  1.00 87.30           C  
ANISOU 7854  CB  GLN C 256     9747  12466  10956    581   1723    -89       C  
ATOM   7855  CG  GLN C 256      74.286 -13.063-186.413  1.00 83.39           C  
ANISOU 7855  CG  GLN C 256     9482  11872  10330    505   1655    -45       C  
ATOM   7856  CD  GLN C 256      74.449 -13.564-184.976  1.00 89.79           C  
ANISOU 7856  CD  GLN C 256    10397  12730  10988    435   1797    -20       C  
ATOM   7857  OE1 GLN C 256      74.463 -12.778-184.027  1.00 90.54           O  
ANISOU 7857  OE1 GLN C 256    10548  12859  10996    518   1903    -81       O  
ATOM   7858  NE2 GLN C 256      74.583 -14.875-184.817  1.00 90.06           N  
ANISOU 7858  NE2 GLN C 256    10474  12760  10986    282   1796     71       N  
ATOM   7859  N   GLN C 257      70.098 -11.777-187.773  1.00 92.56           N  
ANISOU 7859  N   GLN C 257     9900  13323  11945    686   1782   -140       N  
ATOM   7860  CA  GLN C 257      69.346 -10.813-188.591  1.00 87.55           C  
ANISOU 7860  CA  GLN C 257     9104  12706  11455    826   1724   -200       C  
ATOM   7861  C   GLN C 257      70.272  -9.805-189.253  1.00 90.46           C  
ANISOU 7861  C   GLN C 257     9618  12942  11810    951   1580   -252       C  
ATOM   7862  O   GLN C 257      69.885  -9.186-190.251  1.00 99.55           O  
ANISOU 7862  O   GLN C 257    10678  14067  13081   1041   1471   -281       O  
ATOM   7863  CB  GLN C 257      68.261 -10.072-187.768  1.00 86.72           C  
ANISOU 7863  CB  GLN C 257     8838  12730  11380    935   1902   -269       C  
ATOM   7864  CG  GLN C 257      67.714  -8.697-188.359  1.00 84.83           C  
ANISOU 7864  CG  GLN C 257     8490  12485  11256   1140   1850   -360       C  
ATOM   7865  CD  GLN C 257      66.483  -8.805-189.309  1.00 80.46           C  
ANISOU 7865  CD  GLN C 257     7667  12004  10900   1151   1789   -347       C  
ATOM   7866  OE1 GLN C 257      65.865  -9.863-189.428  1.00 83.73           O  
ANISOU 7866  OE1 GLN C 257     7945  12496  11374   1005   1812   -277       O  
ATOM   7867  NE2 GLN C 257      66.127  -7.692-189.966  1.00 52.34           N  
ANISOU 7867  NE2 GLN C 257     4034   8414   7438   1323   1707   -415       N  
ATOM   7868  N   ASP C 258      71.495  -9.651-188.740  1.00 89.87           N  
ANISOU 7868  N   ASP C 258     9770  12783  11594    951   1571   -261       N  
ATOM   7869  CA  ASP C 258      72.544  -8.984-189.499  1.00 90.57           C  
ANISOU 7869  CA  ASP C 258    10009  12736  11668   1019   1416   -285       C  
ATOM   7870  C   ASP C 258      72.749  -9.621-190.868  1.00 87.03           C  
ANISOU 7870  C   ASP C 258     9543  12221  11304    944   1246   -225       C  
ATOM   7871  O   ASP C 258      73.303  -8.973-191.764  1.00 85.52           O  
ANISOU 7871  O   ASP C 258     9422  11932  11140   1013   1112   -248       O  
ATOM   7872  CB  ASP C 258      73.859  -9.025-188.713  1.00 90.97           C  
ANISOU 7872  CB  ASP C 258    10293  12717  11556    989   1429   -284       C  
ATOM   7873  CG  ASP C 258      74.529  -7.670-188.616  1.00 96.01           C  
ANISOU 7873  CG  ASP C 258    11058  13275  12148   1129   1392   -365       C  
ATOM   7874  OD1 ASP C 258      73.914  -6.749-188.040  1.00100.20           O  
ANISOU 7874  OD1 ASP C 258    11540  13853  12680   1249   1487   -439       O  
ATOM   7875  OD2 ASP C 258      75.675  -7.528-189.099  1.00 96.49           O  
ANISOU 7875  OD2 ASP C 258    11268  13225  12168   1119   1270   -356       O  
ATOM   7876  N   GLY C 259      72.299 -10.867-191.053  1.00 89.40           N  
ANISOU 7876  N   GLY C 259     9757  12569  11642    802   1250   -151       N  
ATOM   7877  CA  GLY C 259      72.694 -11.681-192.181  1.00 88.73           C  
ANISOU 7877  CA  GLY C 259     9704  12409  11599    707   1099    -89       C  
ATOM   7878  C   GLY C 259      74.083 -12.264-192.065  1.00 88.92           C  
ANISOU 7878  C   GLY C 259     9942  12339  11506    633   1048    -50       C  
ATOM   7879  O   GLY C 259      74.381 -13.266-192.726  1.00 84.76           O  
ANISOU 7879  O   GLY C 259     9447  11766  10993    526    960     12       O  
ATOM   7880  N   SER C 260      74.931 -11.680-191.222  1.00 91.78           N  
ANISOU 7880  N   SER C 260    10449  12670  11754    689   1100    -88       N  
ATOM   7881  CA  SER C 260      76.303 -12.120-191.049  1.00 85.63           C  
ANISOU 7881  CA  SER C 260     9866  11804  10866    635   1049    -59       C  
ATOM   7882  C   SER C 260      76.349 -13.456-190.314  1.00 83.50           C  
ANISOU 7882  C   SER C 260     9629  11569  10528    493   1117     13       C  
ATOM   7883  O   SER C 260      75.326 -14.045-189.948  1.00 84.59           O  
ANISOU 7883  O   SER C 260     9642  11798  10701    425   1207     43       O  
ATOM   7884  CB  SER C 260      77.103 -11.065-190.287  1.00 81.68           C  
ANISOU 7884  CB  SER C 260     9499  11268  10267    733   1083   -122       C  
ATOM   7885  OG  SER C 260      76.604 -10.893-188.967  1.00 81.27           O  
ANISOU 7885  OG  SER C 260     9430  11303  10147    749   1241   -148       O  
ATOM   7886  N   VAL C 261      77.568 -13.935-190.095  1.00 77.81           N  
ANISOU 7886  N   VAL C 261     9081  10774   9711    446   1070     42       N  
ATOM   7887  CA  VAL C 261      77.819 -15.143-189.325  1.00 70.04           C  
ANISOU 7887  CA  VAL C 261     8170   9801   8642    323   1120    110       C  
ATOM   7888  C   VAL C 261      78.775 -14.798-188.194  1.00 72.22           C  
ANISOU 7888  C   VAL C 261     8607  10055   8777    354   1168     88       C  
ATOM   7889  O   VAL C 261      79.761 -14.079-188.393  1.00 75.07           O  
ANISOU 7889  O   VAL C 261     9070  10345   9107    428   1093     48       O  
ATOM   7890  CB  VAL C 261      78.401 -16.278-190.196  1.00 64.43           C  
ANISOU 7890  CB  VAL C 261     7518   9010   7954    227    999    177       C  
ATOM   7891  CG1 VAL C 261      78.668 -17.522-189.352  1.00 62.09           C  
ANISOU 7891  CG1 VAL C 261     7311   8714   7566    106   1046    248       C  
ATOM   7892  CG2 VAL C 261      77.465 -16.604-191.347  1.00 65.22           C  
ANISOU 7892  CG2 VAL C 261     7469   9123   8187    194    938    195       C  
ATOM   7893  N   ARG C 262      78.463 -15.291-187.003  1.00 69.77           N  
ANISOU 7893  N   ARG C 262     8322   9809   8379    293   1291    114       N  
ATOM   7894  CA  ARG C 262      79.382 -15.282-185.880  1.00 65.61           C  
ANISOU 7894  CA  ARG C 262     7967   9258   7703    291   1324    113       C  
ATOM   7895  C   ARG C 262      79.974 -16.678-185.748  1.00 61.48           C  
ANISOU 7895  C   ARG C 262     7546   8689   7125    166   1278    201       C  
ATOM   7896  O   ARG C 262      79.238 -17.669-185.684  1.00 58.17           O  
ANISOU 7896  O   ARG C 262     7065   8310   6727     60   1327    263       O  
ATOM   7897  CB  ARG C 262      78.667 -14.863-184.598  1.00 64.60           C  
ANISOU 7897  CB  ARG C 262     7823   9227   7496    312   1495     81       C  
ATOM   7898  CG  ARG C 262      79.357 -15.277-183.323  1.00 67.40           C  
ANISOU 7898  CG  ARG C 262     8351   9573   7684    263   1546    107       C  
ATOM   7899  CD  ARG C 262      78.621 -14.714-182.122  1.00 78.54           C  
ANISOU 7899  CD  ARG C 262     9748  11080   9012    299   1721     63       C  
ATOM   7900  NE  ARG C 262      79.144 -13.410-181.721  1.00 89.98           N  
ANISOU 7900  NE  ARG C 262    11282  12503  10402    428   1717    -29       N  
ATOM   7901  CZ  ARG C 262      80.072 -13.241-180.784  1.00 96.01           C  
ANISOU 7901  CZ  ARG C 262    12232  13227  11019    436   1711    -41       C  
ATOM   7902  NH1 ARG C 262      80.575 -14.293-180.153  1.00 99.55           N  
ANISOU 7902  NH1 ARG C 262    12801  13660  11365    330   1706     33       N  
ATOM   7903  NH2 ARG C 262      80.496 -12.023-180.472  1.00 94.13           N  
ANISOU 7903  NH2 ARG C 262    12068  12962  10736    548   1701   -128       N  
ATOM   7904  N   GLY C 263      81.299 -16.754-185.733  1.00 59.54           N  
ANISOU 7904  N   GLY C 263     7452   8356   6816    180   1180    206       N  
ATOM   7905  CA  GLY C 263      81.973 -18.031-185.806  1.00 54.75           C  
ANISOU 7905  CA  GLY C 263     6943   7687   6174     84   1109    284       C  
ATOM   7906  C   GLY C 263      82.479 -18.320-187.206  1.00 51.74           C  
ANISOU 7906  C   GLY C 263     6544   7226   5891     89    968    296       C  
ATOM   7907  O   GLY C 263      82.831 -17.401-187.954  1.00 47.84           O  
ANISOU 7907  O   GLY C 263     6024   6701   5452    178    903    241       O  
ATOM   7908  N   ASP C 264      82.499 -19.596-187.578  1.00 51.17           N  
ANISOU 7908  N   ASP C 264     6492   7114   5835     -8    921    367       N  
ATOM   7909  CA  ASP C 264      83.099 -20.019-188.834  1.00 46.95           C  
ANISOU 7909  CA  ASP C 264     5971   6495   5372     -7    789    381       C  
ATOM   7910  C   ASP C 264      82.019 -20.162-189.897  1.00 46.75           C  
ANISOU 7910  C   ASP C 264     5799   6492   5469    -36    774    385       C  
ATOM   7911  O   ASP C 264      81.184 -21.072-189.795  1.00 48.59           O  
ANISOU 7911  O   ASP C 264     5984   6755   5724   -138    813    438       O  
ATOM   7912  CB  ASP C 264      83.844 -21.341-188.645  1.00 42.30           C  
ANISOU 7912  CB  ASP C 264     5511   5836   4726    -84    732    451       C  
ATOM   7913  CG  ASP C 264      84.725 -21.693-189.831  1.00 42.34           C  
ANISOU 7913  CG  ASP C 264     5557   5747   4784    -61    600    454       C  
ATOM   7914  OD1 ASP C 264      84.474 -21.171-190.938  1.00 43.10           O  
ANISOU 7914  OD1 ASP C 264     5568   5837   4972    -19    556    418       O  
ATOM   7915  OD2 ASP C 264      85.660 -22.510-189.659  1.00 45.95           O  
ANISOU 7915  OD2 ASP C 264     6134   6136   5189    -82    541    492       O  
ATOM   7916  N   PRO C 265      81.999 -19.312-190.930  1.00 42.66           N  
ANISOU 7916  N   PRO C 265     5215   5960   5035     43    713    334       N  
ATOM   7917  CA  PRO C 265      80.959 -19.433-191.967  1.00 48.72           C  
ANISOU 7917  CA  PRO C 265     5846   6747   5920     18    684    337       C  
ATOM   7918  C   PRO C 265      80.978 -20.765-192.688  1.00 49.28           C  
ANISOU 7918  C   PRO C 265     5946   6758   6020    -82    606    399       C  
ATOM   7919  O   PRO C 265      79.956 -21.149-193.269  1.00 50.87           O  
ANISOU 7919  O   PRO C 265     6037   6986   6304   -141    596    419       O  
ATOM   7920  CB  PRO C 265      81.277 -18.282-192.940  1.00 41.97           C  
ANISOU 7920  CB  PRO C 265     4966   5861   5122    129    610    275       C  
ATOM   7921  CG  PRO C 265      82.157 -17.354-192.178  1.00 48.34           C  
ANISOU 7921  CG  PRO C 265     5859   6661   5848    212    639    229       C  
ATOM   7922  CD  PRO C 265      82.922 -18.198-191.193  1.00 44.36           C  
ANISOU 7922  CD  PRO C 265     5480   6137   5239    154    663    273       C  
ATOM   7923  N   ALA C 266      82.106 -21.480-192.678  1.00 43.20           N  
ANISOU 7923  N   ALA C 266     5320   5906   5190   -101    546    429       N  
ATOM   7924  CA  ALA C 266      82.155 -22.782-193.334  1.00 45.21           C  
ANISOU 7924  CA  ALA C 266     5620   6091   5465   -190    471    484       C  
ATOM   7925  C   ALA C 266      81.245 -23.801-192.662  1.00 44.12           C  
ANISOU 7925  C   ALA C 266     5456   5990   5317   -318    537    548       C  
ATOM   7926  O   ALA C 266      80.850 -24.782-193.297  1.00 50.49           O  
ANISOU 7926  O   ALA C 266     6259   6756   6169   -407    482    590       O  
ATOM   7927  CB  ALA C 266      83.593 -23.307-193.359  1.00 46.44           C  
ANISOU 7927  CB  ALA C 266     5936   6153   5556   -168    400    498       C  
ATOM   7928  N   ASN C 267      80.886 -23.590-191.400  1.00 50.27           N  
ANISOU 7928  N   ASN C 267     6223   6845   6034   -336    655    556       N  
ATOM   7929  CA  ASN C 267      80.169 -24.600-190.635  1.00 54.18           C  
ANISOU 7929  CA  ASN C 267     6717   7371   6498   -468    728    625       C  
ATOM   7930  C   ASN C 267      78.750 -24.171-190.281  1.00 51.21           C  
ANISOU 7930  C   ASN C 267     6166   7117   6174   -503    844    617       C  
ATOM   7931  O   ASN C 267      78.163 -24.717-189.345  1.00 55.25           O  
ANISOU 7931  O   ASN C 267     6670   7681   6639   -598    946    665       O  
ATOM   7932  CB  ASN C 267      80.960 -24.947-189.375  1.00 49.08           C  
ANISOU 7932  CB  ASN C 267     6225   6707   5718   -480    774    657       C  
ATOM   7933  CG  ASN C 267      82.398 -25.306-189.683  1.00 51.75           C  
ANISOU 7933  CG  ASN C 267     6720   6932   6011   -431    660    660       C  
ATOM   7934  OD1 ASN C 267      82.684 -25.957-190.691  1.00 52.78           O  
ANISOU 7934  OD1 ASN C 267     6878   6982   6194   -448    557    675       O  
ATOM   7935  ND2 ASN C 267      83.315 -24.857-188.836  1.00 47.02           N  
ANISOU 7935  ND2 ASN C 267     6220   6328   5318   -364    675    642       N  
ATOM   7936  N   VAL C 268      78.182 -23.213-191.016  1.00 50.63           N  
ANISOU 7936  N   VAL C 268     5950   7089   6198   -426    831    559       N  
ATOM   7937  CA  VAL C 268      76.807 -22.794-190.750  1.00 60.72           C  
ANISOU 7937  CA  VAL C 268     7041   8487   7542   -447    935    547       C  
ATOM   7938  C   VAL C 268      75.845 -23.960-190.949  1.00 62.92           C  
ANISOU 7938  C   VAL C 268     7243   8784   7879   -606    940    617       C  
ATOM   7939  O   VAL C 268      74.914 -24.160-190.158  1.00 65.59           O  
ANISOU 7939  O   VAL C 268     7488   9218   8216   -683   1065    645       O  
ATOM   7940  CB  VAL C 268      76.433 -21.588-191.632  1.00 60.16           C  
ANISOU 7940  CB  VAL C 268     6841   8445   7573   -326    892    473       C  
ATOM   7941  CG1 VAL C 268      74.937 -21.338-191.581  1.00 66.00           C  
ANISOU 7941  CG1 VAL C 268     7365   9302   8409   -354    974    466       C  
ATOM   7942  CG2 VAL C 268      77.181 -20.350-191.169  1.00 61.22           C  
ANISOU 7942  CG2 VAL C 268     7037   8579   7644   -183    921    404       C  
ATOM   7943  N   GLU C 269      76.073 -24.762-191.993  1.00 56.91           N  
ANISOU 7943  N   GLU C 269     6528   7930   7165   -661    806    647       N  
ATOM   7944  CA  GLU C 269      75.194 -25.890-192.293  1.00 55.90           C  
ANISOU 7944  CA  GLU C 269     6339   7803   7097   -820    788    712       C  
ATOM   7945  C   GLU C 269      75.214 -26.927-191.174  1.00 58.99           C  
ANISOU 7945  C   GLU C 269     6829   8191   7393   -950    873    789       C  
ATOM   7946  O   GLU C 269      74.163 -27.309-190.645  1.00 58.96           O  
ANISOU 7946  O   GLU C 269     6716   8272   7413  -1064    972    831       O  
ATOM   7947  CB  GLU C 269      75.607 -26.517-193.628  1.00 58.30           C  
ANISOU 7947  CB  GLU C 269     6713   7989   7451   -840    619    721       C  
ATOM   7948  CG  GLU C 269      74.606 -27.487-194.225  1.00 65.17           C  
ANISOU 7948  CG  GLU C 269     7499   8855   8408   -990    568    772       C  
ATOM   7949  CD  GLU C 269      74.910 -27.805-195.679  1.00 80.48           C  
ANISOU 7949  CD  GLU C 269     9488  10688  10403   -979    398    758       C  
ATOM   7950  OE1 GLU C 269      76.051 -27.546-196.127  1.00 85.79           O  
ANISOU 7950  OE1 GLU C 269    10294  11275  11027   -875    327    724       O  
ATOM   7951  OE2 GLU C 269      74.005 -28.304-196.379  1.00 87.95           O  
ANISOU 7951  OE2 GLU C 269    10339  11638  11440  -1077    336    779       O  
ATOM   7952  N   ILE C 270      76.406 -27.400-190.799  1.00 61.47           N  
ANISOU 7952  N   ILE C 270     7348   8409   7598   -935    836    811       N  
ATOM   7953  CA  ILE C 270      76.488 -28.415-189.752  1.00 60.76           C  
ANISOU 7953  CA  ILE C 270     7376   8300   7408  -1056    902    889       C  
ATOM   7954  C   ILE C 270      76.080 -27.839-188.399  1.00 64.21           C  
ANISOU 7954  C   ILE C 270     7771   8854   7771  -1049   1075    885       C  
ATOM   7955  O   ILE C 270      75.534 -28.559-187.551  1.00 64.38           O  
ANISOU 7955  O   ILE C 270     7807   8912   7741  -1180   1172    953       O  
ATOM   7956  CB  ILE C 270      77.902 -29.027-189.712  1.00 64.16           C  
ANISOU 7956  CB  ILE C 270     8036   8595   7746  -1024    805    910       C  
ATOM   7957  CG1 ILE C 270      78.019 -30.070-188.590  1.00 62.58           C  
ANISOU 7957  CG1 ILE C 270     7977   8365   7434  -1142    863    995       C  
ATOM   7958  CG2 ILE C 270      78.951 -27.942-189.552  1.00 62.13           C  
ANISOU 7958  CG2 ILE C 270     7833   8334   7438   -856    793    840       C  
ATOM   7959  CD1 ILE C 270      77.088 -31.254-188.748  1.00 67.29           C  
ANISOU 7959  CD1 ILE C 270     8547   8946   8074  -1326    864   1074       C  
ATOM   7960  N   THR C 271      76.325 -26.545-188.167  1.00 57.66           N  
ANISOU 7960  N   THR C 271     6897   8082   6927   -902   1120    808       N  
ATOM   7961  CA  THR C 271      75.897 -25.941-186.910  1.00 64.38           C  
ANISOU 7961  CA  THR C 271     7711   9046   7705   -886   1289    794       C  
ATOM   7962  C   THR C 271      74.379 -25.991-186.778  1.00 65.28           C  
ANISOU 7962  C   THR C 271     7617   9284   7901   -977   1407    811       C  
ATOM   7963  O   THR C 271      73.849 -26.315-185.706  1.00 58.87           O  
ANISOU 7963  O   THR C 271     6803   8545   7019  -1066   1551    853       O  
ATOM   7964  CB  THR C 271      76.414 -24.502-186.809  1.00 64.62           C  
ANISOU 7964  CB  THR C 271     7733   9103   7717   -707   1300    699       C  
ATOM   7965  OG1 THR C 271      77.851 -24.508-186.784  1.00 57.57           O  
ANISOU 7965  OG1 THR C 271     7030   8103   6741   -639   1202    691       O  
ATOM   7966  CG2 THR C 271      75.902 -23.831-185.550  1.00 61.76           C  
ANISOU 7966  CG2 THR C 271     7331   8856   7279   -682   1478    674       C  
ATOM   7967  N   GLU C 272      73.663 -25.719-187.873  1.00 59.34           N  
ANISOU 7967  N   GLU C 272     6691   8559   7298   -963   1345    782       N  
ATOM   7968  CA  GLU C 272      72.206 -25.790-187.841  1.00 68.21           C  
ANISOU 7968  CA  GLU C 272     7594   9803   8519  -1050   1442    798       C  
ATOM   7969  C   GLU C 272      71.711 -27.231-187.764  1.00 70.09           C  
ANISOU 7969  C   GLU C 272     7850  10018   8763  -1259   1443    898       C  
ATOM   7970  O   GLU C 272      70.646 -27.489-187.187  1.00 69.74           O  
ANISOU 7970  O   GLU C 272     7673  10084   8742  -1368   1576    935       O  
ATOM   7971  CB  GLU C 272      71.628 -25.072-189.061  1.00 74.79           C  
ANISOU 7971  CB  GLU C 272     8242  10663   9510   -969   1353    738       C  
ATOM   7972  CG  GLU C 272      71.566 -23.555-188.887  1.00 84.12           C  
ANISOU 7972  CG  GLU C 272     9337  11919  10707   -786   1414    642       C  
ATOM   7973  CD  GLU C 272      71.832 -22.788-190.169  1.00 92.99           C  
ANISOU 7973  CD  GLU C 272    10420  12986  11925   -659   1263    579       C  
ATOM   7974  OE1 GLU C 272      71.967 -23.425-191.236  1.00 96.20           O  
ANISOU 7974  OE1 GLU C 272    10849  13310  12392   -714   1116    607       O  
ATOM   7975  OE2 GLU C 272      71.916 -21.541-190.106  1.00 97.09           O  
ANISOU 7975  OE2 GLU C 272    10899  13541  12451   -504   1290    502       O  
ATOM   7976  N   LEU C 273      72.463 -28.180-188.327  1.00 75.79           N  
ANISOU 7976  N   LEU C 273     8734  10599   9462  -1318   1300    944       N  
ATOM   7977  CA  LEU C 273      72.092 -29.585-188.192  1.00 77.70           C  
ANISOU 7977  CA  LEU C 273     9031  10798   9695  -1518   1294   1042       C  
ATOM   7978  C   LEU C 273      72.264 -30.065-186.757  1.00 79.50           C  
ANISOU 7978  C   LEU C 273     9388  11044   9774  -1598   1431   1103       C  
ATOM   7979  O   LEU C 273      71.427 -30.818-186.242  1.00 83.07           O  
ANISOU 7979  O   LEU C 273     9793  11546  10223  -1767   1524   1176       O  
ATOM   7980  CB  LEU C 273      72.919 -30.443-189.148  1.00 73.64           C  
ANISOU 7980  CB  LEU C 273     8677  10116   9186  -1541   1105   1066       C  
ATOM   7981  CG  LEU C 273      72.477 -30.407-190.611  1.00 75.28           C  
ANISOU 7981  CG  LEU C 273     8764  10297   9542  -1536    966   1036       C  
ATOM   7982  CD1 LEU C 273      73.318 -31.351-191.457  1.00 71.42           C  
ANISOU 7982  CD1 LEU C 273     8460   9639   9039  -1564    796   1062       C  
ATOM   7983  CD2 LEU C 273      71.001 -30.753-190.722  1.00 80.11           C  
ANISOU 7983  CD2 LEU C 273     9165  11007  10264  -1685   1019   1073       C  
ATOM   7984  N   CYS C 274      73.342 -29.643-186.093  1.00 73.67           N  
ANISOU 7984  N   CYS C 274     8818  10266   8907  -1486   1443   1077       N  
ATOM   7985  CA  CYS C 274      73.517 -30.006-184.691  1.00 68.49           C  
ANISOU 7985  CA  CYS C 274     8296   9630   8097  -1550   1570   1132       C  
ATOM   7986  C   CYS C 274      72.412 -29.410-183.834  1.00 72.21           C  
ANISOU 7986  C   CYS C 274     8599  10272   8565  -1576   1777   1119       C  
ATOM   7987  O   CYS C 274      71.910 -30.063-182.911  1.00 76.00           O  
ANISOU 7987  O   CYS C 274     9110  10797   8969  -1717   1903   1192       O  
ATOM   7988  CB  CYS C 274      74.887 -29.552-184.189  1.00 68.87           C  
ANISOU 7988  CB  CYS C 274     8543   9607   8016  -1412   1529   1096       C  
ATOM   7989  SG  CYS C 274      76.279 -30.460-184.895  1.00 74.33           S  
ANISOU 7989  SG  CYS C 274     9460  10100   8681  -1397   1314   1128       S  
ATOM   7990  N   ILE C 275      72.018 -28.170-184.126  1.00 70.14           N  
ANISOU 7990  N   ILE C 275     8162  10106   8383  -1438   1817   1027       N  
ATOM   7991  CA  ILE C 275      70.965 -27.521-183.353  1.00 80.18           C  
ANISOU 7991  CA  ILE C 275     9262  11545   9660  -1437   2017   1001       C  
ATOM   7992  C   ILE C 275      69.670 -28.317-183.440  1.00 81.23           C  
ANISOU 7992  C   ILE C 275     9221  11756   9884  -1625   2092   1071       C  
ATOM   7993  O   ILE C 275      68.963 -28.492-182.439  1.00 80.03           O  
ANISOU 7993  O   ILE C 275     9022  11711   9675  -1719   2276   1109       O  
ATOM   7994  CB  ILE C 275      70.786 -26.064-183.821  1.00 78.88           C  
ANISOU 7994  CB  ILE C 275     8939  11449   9583  -1244   2018    886       C  
ATOM   7995  CG1 ILE C 275      71.902 -25.190-183.241  1.00 72.86           C  
ANISOU 7995  CG1 ILE C 275     8346  10645   8692  -1083   2017    823       C  
ATOM   7996  CG2 ILE C 275      69.407 -25.534-183.438  1.00 80.58           C  
ANISOU 7996  CG2 ILE C 275     8905  11840   9872  -1255   2197    861       C  
ATOM   7997  CD1 ILE C 275      71.790 -23.727-183.595  1.00 69.81           C  
ANISOU 7997  CD1 ILE C 275     7836  10313   8374   -893   2022    710       C  
ATOM   7998  N   GLN C 276      69.349 -28.836-184.626  1.00 85.87           N  
ANISOU 7998  N   GLN C 276     9720  12293  10612  -1689   1950   1090       N  
ATOM   7999  CA  GLN C 276      68.159 -29.667-184.769  1.00 91.43           C  
ANISOU 7999  CA  GLN C 276    10267  13062  11412  -1884   1999   1161       C  
ATOM   8000  C   GLN C 276      68.292 -30.952-183.962  1.00 97.14           C  
ANISOU 8000  C   GLN C 276    11167  13728  12014  -2079   2049   1274       C  
ATOM   8001  O   GLN C 276      67.519 -31.202-183.032  1.00107.06           O  
ANISOU 8001  O   GLN C 276    12358  15092  13227  -2199   2230   1324       O  
ATOM   8002  CB  GLN C 276      67.910 -29.987-186.241  1.00 93.49           C  
ANISOU 8002  CB  GLN C 276    10431  13258  11834  -1912   1810   1157       C  
ATOM   8003  CG  GLN C 276      67.614 -28.784-187.105  1.00 98.09           C  
ANISOU 8003  CG  GLN C 276    10824  13899  12547  -1741   1754   1055       C  
ATOM   8004  CD  GLN C 276      67.330 -29.177-188.538  1.00104.61           C  
ANISOU 8004  CD  GLN C 276    11569  14659  13520  -1784   1564   1058       C  
ATOM   8005  OE1 GLN C 276      67.521 -30.332-188.923  1.00107.91           O  
ANISOU 8005  OE1 GLN C 276    12102  14968  13932  -1926   1461   1128       O  
ATOM   8006  NE2 GLN C 276      66.867 -28.222-189.335  1.00105.36           N  
ANISOU 8006  NE2 GLN C 276    11477  14813  13743  -1660   1512    983       N  
ATOM   8007  N   HIS C 277      69.283 -31.776-184.299  1.00 93.82           N  
ANISOU 8007  N   HIS C 277    10978  13136  11534  -2109   1893   1317       N  
ATOM   8008  CA  HIS C 277      69.455 -33.068-183.644  1.00 90.02           C  
ANISOU 8008  CA  HIS C 277    10685  12574  10943  -2292   1911   1429       C  
ATOM   8009  C   HIS C 277      69.974 -32.913-182.219  1.00 91.94           C  
ANISOU 8009  C   HIS C 277    11099  12839  10994  -2267   2050   1449       C  
ATOM   8010  O   HIS C 277      70.903 -33.619-181.813  1.00101.57           O  
ANISOU 8010  O   HIS C 277    12575  13930  12086  -2295   1985   1503       O  
ATOM   8011  CB  HIS C 277      70.403 -33.959-184.452  1.00 85.04           C  
ANISOU 8011  CB  HIS C 277    10257  11745  10307  -2309   1695   1461       C  
ATOM   8012  CG  HIS C 277      69.937 -34.232-185.849  1.00 89.73           C  
ANISOU 8012  CG  HIS C 277    10721  12301  11071  -2348   1547   1447       C  
ATOM   8013  ND1 HIS C 277      69.813 -33.241-186.800  1.00 89.83           N  
ANISOU 8013  ND1 HIS C 277    10568  12358  11204  -2200   1479   1352       N  
ATOM   8014  CD2 HIS C 277      69.575 -35.385-186.459  1.00 90.52           C  
ANISOU 8014  CD2 HIS C 277    10846  12314  11233  -2520   1447   1516       C  
ATOM   8015  CE1 HIS C 277      69.389 -33.771-187.933  1.00 90.00           C  
ANISOU 8015  CE1 HIS C 277    10518  12326  11352  -2277   1343   1363       C  
ATOM   8016  NE2 HIS C 277      69.238 -35.071-187.753  1.00 91.11           N  
ANISOU 8016  NE2 HIS C 277    10771  12387  11461  -2472   1321   1460       N  
ATOM   8017  N   GLY C 278      69.394 -31.988-181.458  1.00 85.85           N  
ANISOU 8017  N   GLY C 278    10194  12227  10199  -2207   2237   1403       N  
ATOM   8018  CA  GLY C 278      69.624 -31.941-180.030  1.00 86.92           C  
ANISOU 8018  CA  GLY C 278    10475  12404  10148  -2222   2397   1432       C  
ATOM   8019  C   GLY C 278      70.385 -30.752-179.477  1.00 86.75           C  
ANISOU 8019  C   GLY C 278    10529  12407  10027  -2012   2434   1339       C  
ATOM   8020  O   GLY C 278      69.996 -30.206-178.442  1.00 87.48           O  
ANISOU 8020  O   GLY C 278    10595  12617  10027  -1993   2624   1321       O  
ATOM   8021  N   TRP C 279      71.451 -30.331-180.157  1.00 83.72           N  
ANISOU 8021  N   TRP C 279    10236  11915   9659  -1858   2260   1279       N  
ATOM   8022  CA  TRP C 279      72.477 -29.519-179.513  1.00 84.00           C  
ANISOU 8022  CA  TRP C 279    10428  11925   9562  -1695   2259   1218       C  
ATOM   8023  C   TRP C 279      71.945 -28.172-179.038  1.00 85.09           C  
ANISOU 8023  C   TRP C 279    10416  12212   9701  -1566   2415   1123       C  
ATOM   8024  O   TRP C 279      71.149 -27.517-179.716  1.00 86.48           O  
ANISOU 8024  O   TRP C 279    10355  12475  10027  -1512   2439   1063       O  
ATOM   8025  CB  TRP C 279      73.655 -29.298-180.461  1.00 80.23           C  
ANISOU 8025  CB  TRP C 279    10043  11314   9128  -1560   2043   1170       C  
ATOM   8026  CG  TRP C 279      74.826 -28.656-179.792  1.00 73.51           C  
ANISOU 8026  CG  TRP C 279     9374  10418   8137  -1420   2019   1124       C  
ATOM   8027  CD1 TRP C 279      75.456 -29.090-178.668  1.00 72.12           C  
ANISOU 8027  CD1 TRP C 279     9422  10199   7782  -1458   2053   1175       C  
ATOM   8028  CD2 TRP C 279      75.516 -27.472-180.208  1.00 74.01           C  
ANISOU 8028  CD2 TRP C 279     9419  10471   8230  -1227   1945   1019       C  
ATOM   8029  NE1 TRP C 279      76.490 -28.247-178.348  1.00 70.16           N  
ANISOU 8029  NE1 TRP C 279     9287   9919   7452  -1301   2002   1107       N  
ATOM   8030  CE2 TRP C 279      76.552 -27.248-179.281  1.00 71.89           C  
ANISOU 8030  CE2 TRP C 279     9361  10156   7799  -1160   1938   1011       C  
ATOM   8031  CE3 TRP C 279      75.360 -26.581-181.274  1.00 74.70           C  
ANISOU 8031  CE3 TRP C 279     9340  10579   8464  -1108   1880    934       C  
ATOM   8032  CZ2 TRP C 279      77.426 -26.172-179.386  1.00 71.05           C  
ANISOU 8032  CZ2 TRP C 279     9293  10025   7675   -988   1870    921       C  
ATOM   8033  CZ3 TRP C 279      76.231 -25.512-181.377  1.00 74.29           C  
ANISOU 8033  CZ3 TRP C 279     9336  10500   8390   -936   1818    847       C  
ATOM   8034  CH2 TRP C 279      77.251 -25.318-180.439  1.00 73.99           C  
ANISOU 8034  CH2 TRP C 279     9502  10418   8194   -881   1815    841       C  
ATOM   8035  N   THR C 280      72.412 -27.761-177.859  1.00 83.22           N  
ANISOU 8035  N   THR C 280    10332  11997   9292  -1512   2515   1108       N  
ATOM   8036  CA  THR C 280      72.112 -26.444-177.317  1.00 82.76           C  
ANISOU 8036  CA  THR C 280    10185  12056   9205  -1370   2652   1008       C  
ATOM   8037  C   THR C 280      73.187 -25.462-177.769  1.00 80.23           C  
ANISOU 8037  C   THR C 280     9936  11660   8890  -1172   2509    913       C  
ATOM   8038  O   THR C 280      74.370 -25.682-177.479  1.00 78.46           O  
ANISOU 8038  O   THR C 280     9936  11322   8552  -1143   2403    930       O  
ATOM   8039  CB  THR C 280      72.045 -26.492-175.798  1.00 80.10           C  
ANISOU 8039  CB  THR C 280     9988  11780   8667  -1418   2835   1037       C  
ATOM   8040  OG1 THR C 280      71.006 -27.389-175.393  1.00 83.30           O  
ANISOU 8040  OG1 THR C 280    10318  12263   9070  -1613   2980   1128       O  
ATOM   8041  CG2 THR C 280      71.744 -25.119-175.233  1.00 82.45           C  
ANISOU 8041  CG2 THR C 280    10207  12193   8929  -1262   2978    926       C  
ATOM   8042  N   PRO C 281      72.831 -24.380-178.458  1.00 70.19           N  
ANISOU 8042  N   PRO C 281     8480  10442   7746  -1035   2500    817       N  
ATOM   8043  CA  PRO C 281      73.845 -23.549-179.119  1.00 71.92           C  
ANISOU 8043  CA  PRO C 281     8757  10573   7995   -868   2341    738       C  
ATOM   8044  C   PRO C 281      74.635 -22.697-178.139  1.00 77.49           C  
ANISOU 8044  C   PRO C 281     9628  11271   8543   -750   2382    677       C  
ATOM   8045  O   PRO C 281      74.115 -22.235-177.121  1.00 84.50           O  
ANISOU 8045  O   PRO C 281    10511  12258   9338   -735   2559    650       O  
ATOM   8046  CB  PRO C 281      73.017 -22.657-180.058  1.00 67.33           C  
ANISOU 8046  CB  PRO C 281     7922  10065   7594   -772   2342    660       C  
ATOM   8047  CG  PRO C 281      71.591 -23.166-179.977  1.00 69.02           C  
ANISOU 8047  CG  PRO C 281     7935  10401   7888   -900   2483    706       C  
ATOM   8048  CD  PRO C 281      71.469 -23.866-178.672  1.00 73.23           C  
ANISOU 8048  CD  PRO C 281     8594  10973   8258  -1026   2634    777       C  
ATOM   8049  N   GLY C 282      75.906 -22.483-178.466  1.00 68.90           N  
ANISOU 8049  N   GLY C 282     8688  10064   7425   -666   2216    653       N  
ATOM   8050  CA  GLY C 282      76.678 -21.430-177.843  1.00 68.49           C  
ANISOU 8050  CA  GLY C 282     8756   9998   7267   -529   2216    574       C  
ATOM   8051  C   GLY C 282      76.422 -20.101-178.532  1.00 71.12           C  
ANISOU 8051  C   GLY C 282     8938  10366   7717   -373   2203    464       C  
ATOM   8052  O   GLY C 282      75.476 -19.934-179.304  1.00 69.46           O  
ANISOU 8052  O   GLY C 282     8519  10217   7658   -368   2228    448       O  
ATOM   8053  N   ASN C 283      77.292 -19.135-178.244  1.00 80.40           N  
ANISOU 8053  N   ASN C 283    10228  11498   8822   -246   2155    390       N  
ATOM   8054  CA  ASN C 283      77.269 -17.879-178.990  1.00 87.27           C  
ANISOU 8054  CA  ASN C 283    10991  12368   9799    -96   2106    290       C  
ATOM   8055  C   ASN C 283      78.645 -17.227-178.970  1.00 79.94           C  
ANISOU 8055  C   ASN C 283    10231  11338   8805      0   1973    243       C  
ATOM   8056  O   ASN C 283      78.766 -15.999-178.913  1.00 77.77           O  
ANISOU 8056  O   ASN C 283     9952  11068   8530    128   1980    150       O  
ATOM   8057  CB  ASN C 283      76.206 -16.918-178.454  1.00 93.02           C  
ANISOU 8057  CB  ASN C 283    11595  13216  10530    -16   2284    214       C  
ATOM   8058  CG  ASN C 283      76.271 -16.755-176.952  1.00102.88           C  
ANISOU 8058  CG  ASN C 283    12992  14512  11587    -19   2429    201       C  
ATOM   8059  OD1 ASN C 283      77.234 -16.206-176.416  1.00103.17           O  
ANISOU 8059  OD1 ASN C 283    13206  14486  11507     49   2377    159       O  
ATOM   8060  ND2 ASN C 283      75.236 -17.221-176.262  1.00110.26           N  
ANISOU 8060  ND2 ASN C 283    13853  15556  12483   -103   2613    237       N  
ATOM   8061  N   GLY C 284      79.696 -18.042-179.010  1.00 72.93           N  
ANISOU 8061  N   GLY C 284     9492  10355   7864    -62   1847    305       N  
ATOM   8062  CA  GLY C 284      81.047 -17.550-179.132  1.00 67.67           C  
ANISOU 8062  CA  GLY C 284     8962   9592   7159     15   1703    270       C  
ATOM   8063  C   GLY C 284      81.555 -17.729-180.550  1.00 67.02           C  
ANISOU 8063  C   GLY C 284     8817   9430   7217     30   1541    280       C  
ATOM   8064  O   GLY C 284      80.971 -18.455-181.348  1.00 61.28           O  
ANISOU 8064  O   GLY C 284     7979   8709   6596    -37   1525    328       O  
ATOM   8065  N   ARG C 285      82.656 -17.040-180.857  1.00 67.81           N  
ANISOU 8065  N   ARG C 285     8994   9456   7315    115   1420    233       N  
ATOM   8066  CA  ARG C 285      83.283 -17.159-182.166  1.00 57.27           C  
ANISOU 8066  CA  ARG C 285     7620   8042   6095    134   1270    239       C  
ATOM   8067  C   ARG C 285      84.067 -18.454-182.323  1.00 58.99           C  
ANISOU 8067  C   ARG C 285     7935   8188   6291     49   1171    323       C  
ATOM   8068  O   ARG C 285      84.473 -18.781-183.444  1.00 55.03           O  
ANISOU 8068  O   ARG C 285     7398   7626   5887     49   1059    338       O  
ATOM   8069  CB  ARG C 285      84.215 -15.971-182.413  1.00 49.14           C  
ANISOU 8069  CB  ARG C 285     6640   6962   5069    245   1183    162       C  
ATOM   8070  CG  ARG C 285      83.552 -14.624-182.255  1.00 59.98           C  
ANISOU 8070  CG  ARG C 285     7943   8387   6460    343   1266     73       C  
ATOM   8071  CD  ARG C 285      84.492 -13.641-181.582  1.00 69.32           C  
ANISOU 8071  CD  ARG C 285     9261   9532   7547    417   1231     10       C  
ATOM   8072  NE  ARG C 285      85.540 -13.173-182.482  1.00 79.59           N  
ANISOU 8072  NE  ARG C 285    10584  10748   8911    462   1083    -12       N  
ATOM   8073  CZ  ARG C 285      86.658 -12.579-182.078  1.00 81.24           C  
ANISOU 8073  CZ  ARG C 285    10916  10903   9050    499   1008    -47       C  
ATOM   8074  NH1 ARG C 285      86.878 -12.395-180.781  1.00 78.12           N  
ANISOU 8074  NH1 ARG C 285    10644  10524   8513    499   1057    -64       N  
ATOM   8075  NH2 ARG C 285      87.560 -12.174-182.970  1.00 80.15           N  
ANISOU 8075  NH2 ARG C 285    10779  10694   8980    531    884    -63       N  
ATOM   8076  N   PHE C 286      84.306 -19.188-181.239  1.00 49.31           N  
ANISOU 8076  N   PHE C 286     6839   6961   4937    -19   1206    377       N  
ATOM   8077  CA  PHE C 286      85.077 -20.424-181.319  1.00 48.43           C  
ANISOU 8077  CA  PHE C 286     6832   6770   4797    -90   1106    457       C  
ATOM   8078  C   PHE C 286      84.438 -21.515-180.462  1.00 52.22           C  
ANISOU 8078  C   PHE C 286     7369   7280   5192   -210   1197    539       C  
ATOM   8079  O   PHE C 286      85.106 -22.188-179.677  1.00 59.35           O  
ANISOU 8079  O   PHE C 286     8431   8138   5980   -251   1163    591       O  
ATOM   8080  CB  PHE C 286      86.534 -20.181-180.923  1.00 43.26           C  
ANISOU 8080  CB  PHE C 286     6327   6047   4065    -34    994    441       C  
ATOM   8081  CG  PHE C 286      87.230 -19.150-181.765  1.00 48.10           C  
ANISOU 8081  CG  PHE C 286     6890   6627   4759     68    903    368       C  
ATOM   8082  CD1 PHE C 286      87.709 -19.471-183.035  1.00 46.71           C  
ANISOU 8082  CD1 PHE C 286     6661   6390   4697     79    793    379       C  
ATOM   8083  CD2 PHE C 286      87.398 -17.858-181.303  1.00 51.49           C  
ANISOU 8083  CD2 PHE C 286     7335   7081   5146    148    930    289       C  
ATOM   8084  CE1 PHE C 286      88.356 -18.518-183.814  1.00 46.27           C  
ANISOU 8084  CE1 PHE C 286     6566   6305   4711    164    717    316       C  
ATOM   8085  CE2 PHE C 286      88.036 -16.905-182.082  1.00 49.55           C  
ANISOU 8085  CE2 PHE C 286     7052   6800   4976    231    846    227       C  
ATOM   8086  CZ  PHE C 286      88.512 -17.235-183.341  1.00 50.56           C  
ANISOU 8086  CZ  PHE C 286     7123   6873   5216    236    743    243       C  
ATOM   8087  N   ASP C 287      83.124 -21.705-180.613  1.00 54.93           N  
ANISOU 8087  N   ASP C 287     7580   7698   5592   -270   1313    554       N  
ATOM   8088  CA  ASP C 287      82.421 -22.804-179.954  1.00 60.67           C  
ANISOU 8088  CA  ASP C 287     8340   8454   6257   -404   1403    641       C  
ATOM   8089  C   ASP C 287      82.676 -24.106-180.713  1.00 58.79           C  
ANISOU 8089  C   ASP C 287     8130   8129   6080   -489   1293    720       C  
ATOM   8090  O   ASP C 287      82.298 -24.228-181.883  1.00 59.03           O  
ANISOU 8090  O   ASP C 287     8033   8147   6249   -494   1244    714       O  
ATOM   8091  CB  ASP C 287      80.920 -22.521-179.879  1.00 59.42           C  
ANISOU 8091  CB  ASP C 287     8011   8415   6151   -441   1567    627       C  
ATOM   8092  CG  ASP C 287      80.591 -21.299-179.031  1.00 68.26           C  
ANISOU 8092  CG  ASP C 287     9114   9621   7200   -354   1694    547       C  
ATOM   8093  OD1 ASP C 287      81.422 -20.925-178.173  1.00 63.21           O  
ANISOU 8093  OD1 ASP C 287     8635   8955   6428   -306   1679    525       O  
ATOM   8094  OD2 ASP C 287      79.494 -20.722-179.226  1.00 61.26           O  
ANISOU 8094  OD2 ASP C 287     8056   8829   6391   -331   1804    504       O  
ATOM   8095  N   VAL C 288      83.303 -25.080-180.047  1.00 61.64           N  
ANISOU 8095  N   VAL C 288     8665   8423   6332   -555   1250    794       N  
ATOM   8096  CA  VAL C 288      83.569 -26.379-180.663  1.00 58.55           C  
ANISOU 8096  CA  VAL C 288     8324   7937   5984   -634   1146    872       C  
ATOM   8097  C   VAL C 288      82.259 -27.132-180.849  1.00 59.54           C  
ANISOU 8097  C   VAL C 288     8351   8107   6164   -769   1238    930       C  
ATOM   8098  O   VAL C 288      81.446 -27.236-179.921  1.00 59.23           O  
ANISOU 8098  O   VAL C 288     8310   8146   6049   -849   1382    961       O  
ATOM   8099  CB  VAL C 288      84.557 -27.194-179.810  1.00 57.69           C  
ANISOU 8099  CB  VAL C 288     8436   7743   5740   -661   1076    936       C  
ATOM   8100  CG1 VAL C 288      84.778 -28.580-180.415  1.00 50.78           C  
ANISOU 8100  CG1 VAL C 288     7625   6762   4907   -740    973   1016       C  
ATOM   8101  CG2 VAL C 288      85.886 -26.460-179.665  1.00 51.86           C  
ANISOU 8101  CG2 VAL C 288     7781   6963   4960   -532    972    879       C  
ATOM   8102  N   LEU C 289      82.059 -27.683-182.043  1.00 50.56           N  
ANISOU 8102  N   LEU C 289     7134   6920   5155   -802   1155    945       N  
ATOM   8103  CA  LEU C 289      80.809 -28.343-182.386  1.00 51.27           C  
ANISOU 8103  CA  LEU C 289     7109   7050   5321   -932   1222    994       C  
ATOM   8104  C   LEU C 289      80.741 -29.752-181.799  1.00 59.92           C  
ANISOU 8104  C   LEU C 289     8348   8084   6335  -1080   1225   1104       C  
ATOM   8105  O   LEU C 289      81.773 -30.395-181.583  1.00 51.77           O  
ANISOU 8105  O   LEU C 289     7498   6944   5230  -1070   1122   1142       O  
ATOM   8106  CB  LEU C 289      80.655 -28.433-183.901  1.00 48.47           C  
ANISOU 8106  CB  LEU C 289     6636   6654   5126   -915   1116    969       C  
ATOM   8107  CG  LEU C 289      80.192 -27.203-184.684  1.00 48.55           C  
ANISOU 8107  CG  LEU C 289     6457   6740   5251   -813   1131    878       C  
ATOM   8108  CD1 LEU C 289      80.364 -27.440-186.172  1.00 49.77           C  
ANISOU 8108  CD1 LEU C 289     6558   6820   5532   -793    993    863       C  
ATOM   8109  CD2 LEU C 289      78.734 -26.901-184.367  1.00 59.38           C  
ANISOU 8109  CD2 LEU C 289     7655   8243   6664   -878   1284    877       C  
ATOM   8110  N   PRO C 290      79.535 -30.250-181.533  1.00 61.97           N  
ANISOU 8110  N   PRO C 290     8528   8410   6609  -1221   1341   1158       N  
ATOM   8111  CA  PRO C 290      79.372 -31.676-181.234  1.00 65.18           C  
ANISOU 8111  CA  PRO C 290     9059   8742   6965  -1382   1327   1268       C  
ATOM   8112  C   PRO C 290      79.569 -32.507-182.493  1.00 58.96           C  
ANISOU 8112  C   PRO C 290     8272   7839   6291  -1413   1172   1289       C  
ATOM   8113  O   PRO C 290      79.661 -31.987-183.605  1.00 66.83           O  
ANISOU 8113  O   PRO C 290     9155   8832   7408  -1325   1095   1222       O  
ATOM   8114  CB  PRO C 290      77.934 -31.766-180.719  1.00 61.03           C  
ANISOU 8114  CB  PRO C 290     8402   8339   6446  -1519   1506   1305       C  
ATOM   8115  CG  PRO C 290      77.233 -30.640-181.407  1.00 63.29           C  
ANISOU 8115  CG  PRO C 290     8446   8737   6864  -1434   1554   1213       C  
ATOM   8116  CD  PRO C 290      78.248 -29.532-181.523  1.00 64.37           C  
ANISOU 8116  CD  PRO C 290     8617   8859   6982  -1241   1488   1120       C  
ATOM   8117  N   LEU C 291      79.633 -33.823-182.306  1.00 62.37           N  
ANISOU 8117  N   LEU C 291     8850   8172   6677  -1540   1127   1384       N  
ATOM   8118  CA  LEU C 291      79.773 -34.766-183.413  1.00 61.87           C  
ANISOU 8118  CA  LEU C 291     8817   7987   6705  -1586    985   1412       C  
ATOM   8119  C   LEU C 291      78.417 -35.371-183.752  1.00 68.84           C  
ANISOU 8119  C   LEU C 291     9575   8909   7672  -1761   1045   1462       C  
ATOM   8120  O   LEU C 291      77.686 -35.808-182.855  1.00 72.22           O  
ANISOU 8120  O   LEU C 291    10018   9388   8034  -1903   1166   1534       O  
ATOM   8121  CB  LEU C 291      80.763 -35.882-183.074  1.00 60.83           C  
ANISOU 8121  CB  LEU C 291     8937   7699   6478  -1606    875   1482       C  
ATOM   8122  CG  LEU C 291      82.223 -35.492-182.874  1.00 60.40           C  
ANISOU 8122  CG  LEU C 291     9012   7582   6356  -1438    779   1439       C  
ATOM   8123  CD1 LEU C 291      83.080 -36.725-182.635  1.00 62.61           C  
ANISOU 8123  CD1 LEU C 291     9526   7701   6560  -1465    661   1514       C  
ATOM   8124  CD2 LEU C 291      82.721 -34.709-184.074  1.00 61.82           C  
ANISOU 8124  CD2 LEU C 291     9077   7760   6652  -1291    691   1341       C  
ATOM   8125  N   LEU C 292      78.089 -35.395-185.042  1.00 67.27           N  
ANISOU 8125  N   LEU C 292     9255   8688   7615  -1757    958   1427       N  
ATOM   8126  CA  LEU C 292      76.888 -36.053-185.556  1.00 74.08           C  
ANISOU 8126  CA  LEU C 292    10002   9569   8575  -1925    975   1473       C  
ATOM   8127  C   LEU C 292      77.339 -37.333-186.255  1.00 68.55           C  
ANISOU 8127  C   LEU C 292     9462   8692   7890  -1992    817   1524       C  
ATOM   8128  O   LEU C 292      77.708 -37.324-187.431  1.00 61.81           O  
ANISOU 8128  O   LEU C 292     8594   7769   7123  -1918    687   1474       O  
ATOM   8129  CB  LEU C 292      76.097 -35.140-186.498  1.00 72.36           C  
ANISOU 8129  CB  LEU C 292     9531   9457   8507  -1876    986   1395       C  
ATOM   8130  CG  LEU C 292      75.235 -34.074-185.816  1.00 77.27           C  
ANISOU 8130  CG  LEU C 292     9961  10261   9135  -1856   1162   1359       C  
ATOM   8131  CD1 LEU C 292      74.413 -33.293-186.836  1.00 74.52           C  
ANISOU 8131  CD1 LEU C 292     9367  10002   8947  -1812   1150   1290       C  
ATOM   8132  CD2 LEU C 292      74.334 -34.709-184.763  1.00 81.58           C  
ANISOU 8132  CD2 LEU C 292    10501  10874   9621  -2040   1312   1448       C  
ATOM   8133  N   LEU C 293      77.307 -38.436-185.513  1.00 66.24           N  
ANISOU 8133  N   LEU C 293     9335   8326   7508  -2133    832   1623       N  
ATOM   8134  CA  LEU C 293      77.758 -39.735-185.988  1.00 67.71           C  
ANISOU 8134  CA  LEU C 293     9708   8330   7688  -2201    689   1680       C  
ATOM   8135  C   LEU C 293      76.556 -40.571-186.399  1.00 74.66           C  
ANISOU 8135  C   LEU C 293    10515   9202   8649  -2412    695   1742       C  
ATOM   8136  O   LEU C 293      75.517 -40.547-185.734  1.00 84.19           O  
ANISOU 8136  O   LEU C 293    11615  10522   9853  -2552    836   1789       O  
ATOM   8137  CB  LEU C 293      78.553 -40.457-184.897  1.00 71.10           C  
ANISOU 8137  CB  LEU C 293    10391   8662   7961  -2218    683   1755       C  
ATOM   8138  CG  LEU C 293      79.610 -39.614-184.184  1.00 67.34           C  
ANISOU 8138  CG  LEU C 293     9980   8218   7386  -2040    701   1708       C  
ATOM   8139  CD1 LEU C 293      80.349 -40.448-183.148  1.00 64.38           C  
ANISOU 8139  CD1 LEU C 293     9866   7736   6859  -2069    674   1791       C  
ATOM   8140  CD2 LEU C 293      80.577 -39.013-185.203  1.00 64.80           C  
ANISOU 8140  CD2 LEU C 293     9631   7855   7135  -1843    576   1609       C  
ATOM   8141  N   GLN C 294      76.700 -41.321-187.487  1.00 68.19           N  
ANISOU 8141  N   GLN C 294     9756   8250   7902  -2438    543   1740       N  
ATOM   8142  CA  GLN C 294      75.575 -42.049-188.065  1.00 74.72           C  
ANISOU 8142  CA  GLN C 294    10502   9063   8824  -2632    522   1786       C  
ATOM   8143  C   GLN C 294      75.981 -43.493-188.322  1.00 77.58           C  
ANISOU 8143  C   GLN C 294    11107   9219   9152  -2728    388   1855       C  
ATOM   8144  O   GLN C 294      76.796 -43.764-189.210  1.00 73.83           O  
ANISOU 8144  O   GLN C 294    10740   8613   8699  -2619    239   1810       O  
ATOM   8145  CB  GLN C 294      75.105 -41.381-189.355  1.00 71.87           C  
ANISOU 8145  CB  GLN C 294     9934   8761   8613  -2573    462   1699       C  
ATOM   8146  CG  GLN C 294      73.989 -42.114-190.076  1.00 80.97           C  
ANISOU 8146  CG  GLN C 294    10999   9892   9873  -2767    412   1738       C  
ATOM   8147  CD  GLN C 294      73.871 -41.686-191.528  1.00 86.16           C  
ANISOU 8147  CD  GLN C 294    11538  10542  10657  -2685    290   1653       C  
ATOM   8148  OE1 GLN C 294      73.289 -40.648-191.837  1.00 86.47           O  
ANISOU 8148  OE1 GLN C 294    11349  10726  10780  -2626    342   1592       O  
ATOM   8149  NE2 GLN C 294      74.439 -42.482-192.426  1.00 86.17           N  
ANISOU 8149  NE2 GLN C 294    11705  10370  10665  -2675    126   1645       N  
ATOM   8150  N   ALA C 295      75.404 -44.414-187.555  1.00 83.87           N  
ANISOU 8150  N   ALA C 295    11992   9983   9893  -2930    444   1963       N  
ATOM   8151  CA  ALA C 295      75.534 -45.836-187.815  1.00 81.18           C  
ANISOU 8151  CA  ALA C 295    11867   9446   9532  -3058    322   2037       C  
ATOM   8152  C   ALA C 295      74.518 -46.255-188.877  1.00 85.71           C  
ANISOU 8152  C   ALA C 295    12316  10006  10243  -3207    256   2036       C  
ATOM   8153  O   ALA C 295      73.542 -45.542-189.122  1.00 89.60           O  
ANISOU 8153  O   ALA C 295    12550  10661  10835  -3252    335   2004       O  
ATOM   8154  CB  ALA C 295      75.333 -46.622-186.520  1.00 79.18           C  
ANISOU 8154  CB  ALA C 295    11770   9160   9155  -3222    411   2159       C  
ATOM   8155  N   PRO C 296      74.733 -47.411-189.543  1.00 83.10           N  
ANISOU 8155  N   PRO C 296    12170   9480   9924  -3280    101   2066       N  
ATOM   8156  CA  PRO C 296      73.837 -47.810-190.642  1.00 81.21           C  
ANISOU 8156  CA  PRO C 296    11828   9213   9813  -3414     13   2057       C  
ATOM   8157  C   PRO C 296      72.356 -47.803-190.284  1.00 86.34           C  
ANISOU 8157  C   PRO C 296    12268  10006  10532  -3644    132   2117       C  
ATOM   8158  O   PRO C 296      71.906 -48.574-189.429  1.00 87.52           O  
ANISOU 8158  O   PRO C 296    12502  10129  10622  -3838    201   2224       O  
ATOM   8159  CB  PRO C 296      74.314 -49.229-190.977  1.00 79.82           C  
ANISOU 8159  CB  PRO C 296    11942   8790   9595  -3489   -142   2108       C  
ATOM   8160  CG  PRO C 296      75.737 -49.249-190.573  1.00 75.75           C  
ANISOU 8160  CG  PRO C 296    11639   8176   8967  -3290   -180   2090       C  
ATOM   8161  CD  PRO C 296      75.825 -48.382-189.353  1.00 77.21           C  
ANISOU 8161  CD  PRO C 296    11737   8523   9075  -3232    -10   2104       C  
ATOM   8162  N   ASP C 297      71.621 -46.884-190.922  1.00 91.01           N  
ANISOU 8162  N   ASP C 297    12580  10753  11247  -3615    160   2048       N  
ATOM   8163  CA  ASP C 297      70.161 -46.820-190.988  1.00 96.34           C  
ANISOU 8163  CA  ASP C 297    13006  11564  12034  -3813    233   2080       C  
ATOM   8164  C   ASP C 297      69.521 -46.040-189.844  1.00101.62           C  
ANISOU 8164  C   ASP C 297    13481  12447  12682  -3844    457   2105       C  
ATOM   8165  O   ASP C 297      68.416 -45.512-190.004  1.00107.29           O  
ANISOU 8165  O   ASP C 297    13922  13330  13514  -3920    532   2091       O  
ATOM   8166  CB  ASP C 297      69.563 -48.226-191.079  1.00 99.29           C  
ANISOU 8166  CB  ASP C 297    13501  11803  12421  -4080    160   2180       C  
ATOM   8167  CG  ASP C 297      69.799 -48.860-192.435  1.00103.83           C  
ANISOU 8167  CG  ASP C 297    14189  12203  13061  -4075    -59   2139       C  
ATOM   8168  OD1 ASP C 297      68.913 -48.752-193.306  1.00108.84           O  
ANISOU 8168  OD1 ASP C 297    14639  12889  13827  -4162   -121   2111       O  
ATOM   8169  OD2 ASP C 297      70.890 -49.430-192.645  1.00104.66           O  
ANISOU 8169  OD2 ASP C 297    14562  12120  13082  -3973   -172   2129       O  
ATOM   8170  N   GLU C 298      70.186 -45.936-188.700  1.00101.17           N  
ANISOU 8170  N   GLU C 298    13562  12396  12483  -3780    563   2138       N  
ATOM   8171  CA  GLU C 298      69.636 -45.111-187.639  1.00103.07           C  
ANISOU 8171  CA  GLU C 298    13628  12841  12692  -3786    779   2148       C  
ATOM   8172  C   GLU C 298      69.855 -43.633-187.965  1.00100.62           C  
ANISOU 8172  C   GLU C 298    13127  12671  12434  -3547    814   2026       C  
ATOM   8173  O   GLU C 298      70.792 -43.280-188.691  1.00 91.17           O  
ANISOU 8173  O   GLU C 298    12007  11393  11240  -3355    688   1948       O  
ATOM   8174  CB  GLU C 298      70.279 -45.451-186.295  1.00109.24           C  
ANISOU 8174  CB  GLU C 298    14633  13580  13293  -3794    877   2220       C  
ATOM   8175  CG  GLU C 298      69.477 -44.996-185.067  1.00119.10           C  
ANISOU 8175  CG  GLU C 298    15741  15020  14491  -3888   1116   2266       C  
ATOM   8176  CD  GLU C 298      68.430 -46.013-184.625  1.00123.66           C  
ANISOU 8176  CD  GLU C 298    16306  15597  15081  -4161   1185   2374       C  
ATOM   8177  OE1 GLU C 298      68.648 -47.223-184.838  1.00124.40           O  
ANISOU 8177  OE1 GLU C 298    16601  15504  15160  -4235   1052   2418       O  
ATOM   8178  OE2 GLU C 298      67.390 -45.604-184.060  1.00125.27           O  
ANISOU 8178  OE2 GLU C 298    16287  15983  15327  -4235   1363   2380       O  
ATOM   8179  N   PRO C 299      68.980 -42.753-187.485  1.00100.17           N  
ANISOU 8179  N   PRO C 299    12816  12823  12423  -3557    984   2007       N  
ATOM   8180  CA  PRO C 299      69.295 -41.322-187.480  1.00 92.92           C  
ANISOU 8180  CA  PRO C 299    11759  12031  11516  -3323   1044   1901       C  
ATOM   8181  C   PRO C 299      70.642 -41.075-186.826  1.00 85.45           C  
ANISOU 8181  C   PRO C 299    11040  11012  10415  -3152   1044   1882       C  
ATOM   8182  O   PRO C 299      71.111 -41.891-186.018  1.00 85.24           O  
ANISOU 8182  O   PRO C 299    11239  10889  10258  -3229   1061   1963       O  
ATOM   8183  CB  PRO C 299      68.155 -40.709-186.652  1.00 93.35           C  
ANISOU 8183  CB  PRO C 299    11568  12303  11597  -3401   1262   1915       C  
ATOM   8184  CG  PRO C 299      67.044 -41.723-186.665  1.00 97.45           C  
ANISOU 8184  CG  PRO C 299    12016  12828  12183  -3678   1284   2011       C  
ATOM   8185  CD  PRO C 299      67.542 -43.002-187.284  1.00100.13           C  
ANISOU 8185  CD  PRO C 299    12594  12943  12506  -3780   1093   2066       C  
ATOM   8186  N   PRO C 300      71.310 -39.974-187.151  1.00 81.00           N  
ANISOU 8186  N   PRO C 300    10431  10487   9860  -2921   1019   1780       N  
ATOM   8187  CA  PRO C 300      72.595 -39.697-186.506  1.00 82.43           C  
ANISOU 8187  CA  PRO C 300    10812  10607   9900  -2762   1016   1760       C  
ATOM   8188  C   PRO C 300      72.391 -39.259-185.066  1.00 86.46           C  
ANISOU 8188  C   PRO C 300    11315  11242  10296  -2778   1215   1790       C  
ATOM   8189  O   PRO C 300      71.359 -38.690-184.703  1.00 96.02           O  
ANISOU 8189  O   PRO C 300    12311  12619  11552  -2830   1367   1782       O  
ATOM   8190  CB  PRO C 300      73.185 -38.572-187.363  1.00 75.74           C  
ANISOU 8190  CB  PRO C 300     9877   9782   9117  -2534    939   1641       C  
ATOM   8191  CG  PRO C 300      71.983 -37.849-187.867  1.00 72.01           C  
ANISOU 8191  CG  PRO C 300     9112   9463   8787  -2558    998   1597       C  
ATOM   8192  CD  PRO C 300      70.956 -38.933-188.132  1.00 72.91           C  
ANISOU 8192  CD  PRO C 300     9176   9554   8972  -2796    981   1679       C  
ATOM   8193  N   GLU C 301      73.391 -39.536-184.237  1.00 79.47           N  
ANISOU 8193  N   GLU C 301    10668  10271   9255  -2728   1211   1822       N  
ATOM   8194  CA  GLU C 301      73.301 -39.291-182.805  1.00 78.27           C  
ANISOU 8194  CA  GLU C 301    10566  10210   8965  -2756   1386   1862       C  
ATOM   8195  C   GLU C 301      74.301 -38.222-182.392  1.00 78.31           C  
ANISOU 8195  C   GLU C 301    10622  10243   8887  -2531   1395   1780       C  
ATOM   8196  O   GLU C 301      75.470 -38.267-182.790  1.00 77.93           O  
ANISOU 8196  O   GLU C 301    10722  10074   8816  -2398   1248   1748       O  
ATOM   8197  CB  GLU C 301      73.530 -40.582-182.018  1.00 76.59           C  
ANISOU 8197  CB  GLU C 301    10605   9873   8621  -2916   1380   1985       C  
ATOM   8198  CG  GLU C 301      72.517 -41.666-182.346  1.00 86.52           C  
ANISOU 8198  CG  GLU C 301    11824  11097   9952  -3160   1376   2073       C  
ATOM   8199  CD  GLU C 301      72.323 -42.649-181.209  1.00 94.03           C  
ANISOU 8199  CD  GLU C 301    12960  12003  10763  -3351   1464   2202       C  
ATOM   8200  OE1 GLU C 301      73.202 -42.718-180.324  1.00 96.53           O  
ANISOU 8200  OE1 GLU C 301    13495  12262  10921  -3283   1471   2228       O  
ATOM   8201  OE2 GLU C 301      71.283 -43.342-181.196  1.00101.64           O  
ANISOU 8201  OE2 GLU C 301    13852  12991  11775  -3574   1524   2279       O  
ATOM   8202  N   LEU C 302      73.834 -37.268-181.591  1.00 73.68           N  
ANISOU 8202  N   LEU C 302     9915   9820   8262  -2491   1570   1746       N  
ATOM   8203  CA  LEU C 302      74.647 -36.135-181.176  1.00 68.57           C  
ANISOU 8203  CA  LEU C 302     9295   9215   7543  -2286   1591   1662       C  
ATOM   8204  C   LEU C 302      75.541 -36.534-180.008  1.00 71.57           C  
ANISOU 8204  C   LEU C 302     9943   9522   7729  -2282   1601   1717       C  
ATOM   8205  O   LEU C 302      75.063 -37.060-178.998  1.00 70.44           O  
ANISOU 8205  O   LEU C 302     9875   9410   7478  -2426   1725   1801       O  
ATOM   8206  CB  LEU C 302      73.741 -34.968-180.784  1.00 73.04           C  
ANISOU 8206  CB  LEU C 302     9633   9979   8142  -2244   1773   1599       C  
ATOM   8207  CG  LEU C 302      74.355 -33.595-180.517  1.00 75.61           C  
ANISOU 8207  CG  LEU C 302     9935  10367   8427  -2029   1801   1493       C  
ATOM   8208  CD1 LEU C 302      74.321 -32.741-181.774  1.00 73.03           C  
ANISOU 8208  CD1 LEU C 302     9424  10061   8262  -1893   1709   1393       C  
ATOM   8209  CD2 LEU C 302      73.628 -32.911-179.365  1.00 82.78           C  
ANISOU 8209  CD2 LEU C 302    10761  11437   9253  -2042   2026   1481       C  
ATOM   8210  N   PHE C 303      76.842 -36.298-180.152  1.00 70.81           N  
ANISOU 8210  N   PHE C 303     9990   9328   7587  -2122   1468   1674       N  
ATOM   8211  CA  PHE C 303      77.817 -36.580-179.109  1.00 71.26           C  
ANISOU 8211  CA  PHE C 303    10297   9311   7468  -2090   1448   1716       C  
ATOM   8212  C   PHE C 303      78.642 -35.329-178.858  1.00 81.21           C  
ANISOU 8212  C   PHE C 303    11552  10620   8685  -1886   1442   1617       C  
ATOM   8213  O   PHE C 303      78.989 -34.609-179.798  1.00 82.78           O  
ANISOU 8213  O   PHE C 303    11636  10821   8994  -1750   1360   1528       O  
ATOM   8214  CB  PHE C 303      78.755 -37.731-179.492  1.00 69.54           C  
ANISOU 8214  CB  PHE C 303    10294   8897   7230  -2103   1261   1774       C  
ATOM   8215  CG  PHE C 303      78.084 -39.070-179.581  1.00 70.88           C  
ANISOU 8215  CG  PHE C 303    10529   8989   7412  -2311   1253   1882       C  
ATOM   8216  CD1 PHE C 303      77.518 -39.500-180.770  1.00 73.15           C  
ANISOU 8216  CD1 PHE C 303    10695   9243   7855  -2379   1183   1878       C  
ATOM   8217  CD2 PHE C 303      78.045 -39.913-178.484  1.00 67.81           C  
ANISOU 8217  CD2 PHE C 303    10338   8553   6875  -2444   1306   1991       C  
ATOM   8218  CE1 PHE C 303      76.906 -40.741-180.854  1.00 73.20           C  
ANISOU 8218  CE1 PHE C 303    10770   9169   7873  -2580   1167   1978       C  
ATOM   8219  CE2 PHE C 303      77.436 -41.155-178.562  1.00 72.11           C  
ANISOU 8219  CE2 PHE C 303    10954   9017   7429  -2647   1296   2096       C  
ATOM   8220  CZ  PHE C 303      76.866 -41.569-179.750  1.00 70.23           C  
ANISOU 8220  CZ  PHE C 303    10588   8744   7351  -2717   1225   2088       C  
ATOM   8221  N   LEU C 304      78.958 -35.078-177.591  1.00 76.60           N  
ANISOU 8221  N   LEU C 304    11101  10068   7935  -1870   1526   1634       N  
ATOM   8222  CA  LEU C 304      79.781 -33.941-177.205  1.00 73.72           C  
ANISOU 8222  CA  LEU C 304    10761   9740   7509  -1691   1516   1547       C  
ATOM   8223  C   LEU C 304      81.198 -34.421-176.921  1.00 66.53           C  
ANISOU 8223  C   LEU C 304    10091   8686   6501  -1620   1355   1574       C  
ATOM   8224  O   LEU C 304      81.392 -35.407-176.204  1.00 62.71           O  
ANISOU 8224  O   LEU C 304     9804   8123   5900  -1719   1339   1671       O  
ATOM   8225  CB  LEU C 304      79.199 -33.229-175.982  1.00 83.03           C  
ANISOU 8225  CB  LEU C 304    11925  11057   8565  -1707   1714   1534       C  
ATOM   8226  CG  LEU C 304      78.104 -32.178-176.207  1.00 86.04           C  
ANISOU 8226  CG  LEU C 304    12046  11604   9042  -1679   1869   1456       C  
ATOM   8227  CD1 LEU C 304      76.842 -32.784-176.807  1.00 86.36           C  
ANISOU 8227  CD1 LEU C 304    11912  11693   9210  -1833   1937   1503       C  
ATOM   8228  CD2 LEU C 304      77.786 -31.460-174.898  1.00 89.52           C  
ANISOU 8228  CD2 LEU C 304    12520  12161   9333  -1665   2053   1435       C  
ATOM   8229  N   LEU C 305      82.176 -33.742-177.500  1.00 65.21           N  
ANISOU 8229  N   LEU C 305     9906   8485   6387  -1452   1233   1491       N  
ATOM   8230  CA  LEU C 305      83.567 -34.089-177.240  1.00 67.49           C  
ANISOU 8230  CA  LEU C 305    10397   8651   6596  -1367   1077   1507       C  
ATOM   8231  C   LEU C 305      83.961 -33.605-175.851  1.00 72.38           C  
ANISOU 8231  C   LEU C 305    11154   9312   7036  -1335   1139   1509       C  
ATOM   8232  O   LEU C 305      83.693 -32.447-175.510  1.00 71.24           O  
ANISOU 8232  O   LEU C 305    10912   9283   6872  -1269   1242   1433       O  
ATOM   8233  CB  LEU C 305      84.486 -33.467-178.286  1.00 57.12           C  
ANISOU 8233  CB  LEU C 305     9007   7299   5397  -1203    939   1416       C  
ATOM   8234  CG  LEU C 305      84.418 -34.029-179.709  1.00 60.08           C  
ANISOU 8234  CG  LEU C 305     9297   7601   5932  -1211    838   1412       C  
ATOM   8235  CD1 LEU C 305      85.127 -33.110-180.675  1.00 56.85           C  
ANISOU 8235  CD1 LEU C 305     8778   7195   5628  -1050    751   1310       C  
ATOM   8236  CD2 LEU C 305      85.024 -35.424-179.763  1.00 61.05           C  
ANISOU 8236  CD2 LEU C 305     9609   7566   6021  -1262    710   1497       C  
ATOM   8237  N   PRO C 306      84.573 -34.452-175.025  1.00 74.24           N  
ANISOU 8237  N   PRO C 306    11622   9453   7133  -1377   1076   1592       N  
ATOM   8238  CA  PRO C 306      85.071 -33.994-173.724  1.00 76.96           C  
ANISOU 8238  CA  PRO C 306    12119   9826   7297  -1337   1108   1591       C  
ATOM   8239  C   PRO C 306      86.033 -32.836-173.907  1.00 84.16           C  
ANISOU 8239  C   PRO C 306    12984  10757   8234  -1156   1026   1483       C  
ATOM   8240  O   PRO C 306      87.037 -32.966-174.622  1.00 89.86           O  
ANISOU 8240  O   PRO C 306    13718  11390   9035  -1058    857   1459       O  
ATOM   8241  CB  PRO C 306      85.784 -35.232-173.157  1.00 75.61           C  
ANISOU 8241  CB  PRO C 306    12205   9512   7013  -1390    988   1699       C  
ATOM   8242  CG  PRO C 306      85.193 -36.384-173.887  1.00 75.76           C  
ANISOU 8242  CG  PRO C 306    12204   9457   7123  -1514    970   1773       C  
ATOM   8243  CD  PRO C 306      84.859 -35.878-175.257  1.00 71.99           C  
ANISOU 8243  CD  PRO C 306    11484   9021   6847  -1459    960   1689       C  
ATOM   8244  N   PRO C 307      85.737 -31.675-173.303  1.00 85.51           N  
ANISOU 8244  N   PRO C 307    13100  11046   8346  -1108   1145   1413       N  
ATOM   8245  CA  PRO C 307      86.571 -30.482-173.518  1.00 83.53           C  
ANISOU 8245  CA  PRO C 307    12793  10816   8127   -945   1073   1305       C  
ATOM   8246  C   PRO C 307      88.068 -30.748-173.408  1.00 79.58           C  
ANISOU 8246  C   PRO C 307    12446  10202   7587   -856    873   1314       C  
ATOM   8247  O   PRO C 307      88.858 -30.217-174.202  1.00 68.90           O  
ANISOU 8247  O   PRO C 307    11012   8825   6342   -739    758   1245       O  
ATOM   8248  CB  PRO C 307      86.084 -29.527-172.421  1.00 86.01           C  
ANISOU 8248  CB  PRO C 307    13126  11245   8310   -939   1230   1261       C  
ATOM   8249  CG  PRO C 307      84.639 -29.896-172.240  1.00 87.99           C  
ANISOU 8249  CG  PRO C 307    13296  11578   8557  -1077   1422   1308       C  
ATOM   8250  CD  PRO C 307      84.558 -31.390-172.465  1.00 88.86           C  
ANISOU 8250  CD  PRO C 307    13493  11590   8679  -1203   1361   1425       C  
ATOM   8251  N   GLU C 308      88.462 -31.605-172.460  1.00 77.46           N  
ANISOU 8251  N   GLU C 308    12399   9863   7170   -913    826   1402       N  
ATOM   8252  CA  GLU C 308      89.872 -31.919-172.253  1.00 75.98           C  
ANISOU 8252  CA  GLU C 308    12362   9568   6938   -828    630   1418       C  
ATOM   8253  C   GLU C 308      90.462 -32.779-173.365  1.00 71.50           C  
ANISOU 8253  C   GLU C 308    11768   8888   6511   -797    477   1443       C  
ATOM   8254  O   GLU C 308      91.688 -32.935-173.418  1.00 61.76           O  
ANISOU 8254  O   GLU C 308    10611   7574   5280   -701    309   1438       O  
ATOM   8255  CB  GLU C 308      90.066 -32.605-170.896  1.00 81.64           C  
ANISOU 8255  CB  GLU C 308    13334  10239   7448   -898    620   1510       C  
ATOM   8256  CG  GLU C 308      90.372 -34.100-170.959  1.00 96.56           C  
ANISOU 8256  CG  GLU C 308    15374  11990   9323   -963    507   1623       C  
ATOM   8257  CD  GLU C 308      89.129 -34.969-170.921  1.00110.87           C  
ANISOU 8257  CD  GLU C 308    17196  13809  11121  -1133    644   1709       C  
ATOM   8258  OE1 GLU C 308      88.008 -34.416-170.969  1.00112.45           O  
ANISOU 8258  OE1 GLU C 308    17252  14128  11345  -1197    827   1678       O  
ATOM   8259  OE2 GLU C 308      89.276 -36.209-170.834  1.00116.94           O  
ANISOU 8259  OE2 GLU C 308    18116  14461  11856  -1205    566   1810       O  
ATOM   8260  N   LEU C 309      89.634 -33.336-174.251  1.00 67.43           N  
ANISOU 8260  N   LEU C 309    11143   8366   6111   -873    529   1466       N  
ATOM   8261  CA  LEU C 309      90.168 -34.039-175.407  1.00 61.71           C  
ANISOU 8261  CA  LEU C 309    10384   7539   5525   -832    392   1473       C  
ATOM   8262  C   LEU C 309      90.559 -33.100-176.534  1.00 55.74           C  
ANISOU 8262  C   LEU C 309     9436   6819   4922   -709    350   1365       C  
ATOM   8263  O   LEU C 309      91.348 -33.497-177.395  1.00 52.24           O  
ANISOU 8263  O   LEU C 309     8981   6292   4576   -637    217   1354       O  
ATOM   8264  CB  LEU C 309      89.161 -35.044-175.962  1.00 61.46           C  
ANISOU 8264  CB  LEU C 309    10325   7472   5555   -967    447   1540       C  
ATOM   8265  CG  LEU C 309      89.078 -36.447-175.360  1.00 74.14           C  
ANISOU 8265  CG  LEU C 309    12140   8968   7062  -1082    412   1664       C  
ATOM   8266  CD1 LEU C 309      88.733 -37.437-176.461  1.00 76.39           C  
ANISOU 8266  CD1 LEU C 309    12388   9164   7473  -1142    362   1699       C  
ATOM   8267  CD2 LEU C 309      90.366 -36.842-174.645  1.00 77.86           C  
ANISOU 8267  CD2 LEU C 309    12819   9338   7425  -1002    258   1699       C  
ATOM   8268  N   VAL C 310      90.030 -31.881-176.549  1.00 54.54           N  
ANISOU 8268  N   VAL C 310     9142   6788   4794   -683    463   1287       N  
ATOM   8269  CA  VAL C 310      90.146 -30.980-177.698  1.00 54.78           C  
ANISOU 8269  CA  VAL C 310     8980   6857   4975   -590    447   1191       C  
ATOM   8270  C   VAL C 310      91.192 -29.928-177.347  1.00 52.80           C  
ANISOU 8270  C   VAL C 310     8741   6629   4690   -465    381   1118       C  
ATOM   8271  O   VAL C 310      90.895 -28.892-176.749  1.00 58.63           O  
ANISOU 8271  O   VAL C 310     9449   7458   5371   -447    471   1066       O  
ATOM   8272  CB  VAL C 310      88.803 -30.355-178.061  1.00 52.84           C  
ANISOU 8272  CB  VAL C 310     8560   6721   4794   -644    606   1154       C  
ATOM   8273  CG1 VAL C 310      88.897 -29.619-179.373  1.00 50.46           C  
ANISOU 8273  CG1 VAL C 310     8080   6440   4654   -557    570   1070       C  
ATOM   8274  CG2 VAL C 310      87.726 -31.423-178.115  1.00 61.02           C  
ANISOU 8274  CG2 VAL C 310     9604   7745   5837   -792    680   1237       C  
ATOM   8275  N   LEU C 311      92.434 -30.189-177.749  1.00 49.70           N  
ANISOU 8275  N   LEU C 311     8390   6154   4339   -377    222   1112       N  
ATOM   8276  CA  LEU C 311      93.526 -29.260-177.492  1.00 50.87           C  
ANISOU 8276  CA  LEU C 311     8542   6317   4470   -266    140   1047       C  
ATOM   8277  C   LEU C 311      93.400 -28.035-178.388  1.00 52.45           C  
ANISOU 8277  C   LEU C 311     8555   6585   4787   -200    179    948       C  
ATOM   8278  O   LEU C 311      93.301 -28.165-179.609  1.00 44.67           O  
ANISOU 8278  O   LEU C 311     7454   5581   3937   -181    160    928       O  
ATOM   8279  CB  LEU C 311      94.869 -29.953-177.732  1.00 56.08           C  
ANISOU 8279  CB  LEU C 311     9278   6873   5156   -192    -40   1071       C  
ATOM   8280  CG  LEU C 311      96.105 -29.151-177.340  1.00 57.34           C  
ANISOU 8280  CG  LEU C 311     9455   7040   5290    -89   -144   1018       C  
ATOM   8281  CD1 LEU C 311      96.056 -28.759-175.854  1.00 54.39           C  
ANISOU 8281  CD1 LEU C 311     9219   6704   4742   -118   -113   1032       C  
ATOM   8282  CD2 LEU C 311      97.364 -29.941-177.644  1.00 59.05           C  
ANISOU 8282  CD2 LEU C 311     9727   7159   5550    -15   -316   1046       C  
ATOM   8283  N   GLU C 312      93.406 -26.844-177.786  1.00 47.48           N  
ANISOU 8283  N   GLU C 312     7909   6029   4102   -163    229    885       N  
ATOM   8284  CA  GLU C 312      93.324 -25.598-178.536  1.00 46.91           C  
ANISOU 8284  CA  GLU C 312     7680   6015   4129    -98    261    791       C  
ATOM   8285  C   GLU C 312      94.501 -24.697-178.196  1.00 49.10           C  
ANISOU 8285  C   GLU C 312     7987   6290   4379     -9    165    734       C  
ATOM   8286  O   GLU C 312      95.116 -24.814-177.131  1.00 48.26           O  
ANISOU 8286  O   GLU C 312     8021   6165   4151     -6    109    756       O  
ATOM   8287  CB  GLU C 312      92.020 -24.845-178.259  1.00 50.66           C  
ANISOU 8287  CB  GLU C 312     8080   6586   4581   -138    429    757       C  
ATOM   8288  CG  GLU C 312      90.796 -25.428-178.918  1.00 56.90           C  
ANISOU 8288  CG  GLU C 312     8773   7398   5449   -215    524    790       C  
ATOM   8289  CD  GLU C 312      89.553 -24.636-178.579  1.00 65.66           C  
ANISOU 8289  CD  GLU C 312     9796   8611   6540   -242    691    752       C  
ATOM   8290  OE1 GLU C 312      88.824 -25.031-177.641  1.00 66.14           O  
ANISOU 8290  OE1 GLU C 312     9925   8711   6496   -323    796    798       O  
ATOM   8291  OE2 GLU C 312      89.316 -23.604-179.231  1.00 60.44           O  
ANISOU 8291  OE2 GLU C 312     9002   7994   5967   -179    718    675       O  
ATOM   8292  N   VAL C 313      94.791 -23.777-179.112  1.00 50.94           N  
ANISOU 8292  N   VAL C 313     8090   6541   4724     58    145    660       N  
ATOM   8293  CA  VAL C 313      95.949 -22.896-178.989  1.00 48.41           C  
ANISOU 8293  CA  VAL C 313     7774   6215   4404    135     47    603       C  
ATOM   8294  C   VAL C 313      95.491 -21.444-179.040  1.00 49.91           C  
ANISOU 8294  C   VAL C 313     7884   6471   4608    164    128    517       C  
ATOM   8295  O   VAL C 313      95.097 -20.965-180.109  1.00 48.44           O  
ANISOU 8295  O   VAL C 313     7564   6302   4539    185    165    477       O  
ATOM   8296  CB  VAL C 313      96.979 -23.183-180.095  1.00 47.83           C  
ANISOU 8296  CB  VAL C 313     7630   6087   4457    192    -73    597       C  
ATOM   8297  CG1 VAL C 313      98.179 -22.244-179.977  1.00 46.05           C  
ANISOU 8297  CG1 VAL C 313     7394   5862   4241    261   -171    540       C  
ATOM   8298  CG2 VAL C 313      97.424 -24.638-180.044  1.00 44.84           C  
ANISOU 8298  CG2 VAL C 313     7337   5633   4066    176   -155    678       C  
ATOM   8299  N   PRO C 314      95.542 -20.702-177.940  1.00 47.11           N  
ANISOU 8299  N   PRO C 314     7616   6148   4136    170    152    484       N  
ATOM   8300  CA  PRO C 314      95.223 -19.273-178.011  1.00 41.16           C  
ANISOU 8300  CA  PRO C 314     6798   5443   3398    210    213    395       C  
ATOM   8301  C   PRO C 314      96.321 -18.566-178.777  1.00 37.94           C  
ANISOU 8301  C   PRO C 314     6323   5005   3088    273     98    345       C  
ATOM   8302  O   PRO C 314      97.499 -18.898-178.633  1.00 41.21           O  
ANISOU 8302  O   PRO C 314     6786   5375   3495    290    -31    364       O  
ATOM   8303  CB  PRO C 314      95.187 -18.835-176.533  1.00 40.82           C  
ANISOU 8303  CB  PRO C 314     6900   5425   3184    200    245    379       C  
ATOM   8304  CG  PRO C 314      95.258 -20.113-175.737  1.00 54.70           C  
ANISOU 8304  CG  PRO C 314     8790   7157   4837    141    224    470       C  
ATOM   8305  CD  PRO C 314      95.988 -21.090-176.590  1.00 46.50           C  
ANISOU 8305  CD  PRO C 314     7712   6055   3901    147    108    523       C  
ATOM   8306  N   LEU C 315      95.936 -17.629-179.645  1.00 37.21           N  
ANISOU 8306  N   LEU C 315     6112   4935   3093    306    144    283       N  
ATOM   8307  CA  LEU C 315      96.914 -17.016-180.526  1.00 32.83           C  
ANISOU 8307  CA  LEU C 315     5485   4350   2640    353     48    244       C  
ATOM   8308  C   LEU C 315      97.441 -15.712-179.947  1.00 38.13           C  
ANISOU 8308  C   LEU C 315     6200   5027   3262    384     14    173       C  
ATOM   8309  O   LEU C 315      96.666 -14.823-179.582  1.00 42.01           O  
ANISOU 8309  O   LEU C 315     6700   5551   3711    395    104    120       O  
ATOM   8310  CB  LEU C 315      96.320 -16.776-181.920  1.00 40.81           C  
ANISOU 8310  CB  LEU C 315     6352   5366   3787    368     96    224       C  
ATOM   8311  CG  LEU C 315      95.870 -18.048-182.654  1.00 41.31           C  
ANISOU 8311  CG  LEU C 315     6369   5414   3912    335    112    289       C  
ATOM   8312  CD1 LEU C 315      95.327 -17.724-184.044  1.00 40.44           C  
ANISOU 8312  CD1 LEU C 315     6128   5307   3930    351    146    264       C  
ATOM   8313  CD2 LEU C 315      97.003 -19.068-182.749  1.00 41.86           C  
ANISOU 8313  CD2 LEU C 315     6483   5430   3992    337     -5    340       C  
ATOM   8314  N   GLU C 316      98.767 -15.610-179.870  1.00 39.67           N  
ANISOU 8314  N   GLU C 316     6420   5188   3465    400   -118    169       N  
ATOM   8315  CA AGLU C 316      99.452 -14.392-179.467  0.60 42.30           C  
ANISOU 8315  CA AGLU C 316     6787   5516   3770    421   -177    103       C  
ATOM   8316  CA BGLU C 316      99.442 -14.386-179.480  0.40 42.00           C  
ANISOU 8316  CA BGLU C 316     6748   5478   3733    422   -176    103       C  
ATOM   8317  C   GLU C 316     100.530 -14.082-180.496  1.00 39.47           C  
ANISOU 8317  C   GLU C 316     6331   5130   3537    442   -275     89       C  
ATOM   8318  O   GLU C 316     100.907 -14.934-181.304  1.00 39.84           O  
ANISOU 8318  O   GLU C 316     6307   5160   3668    446   -311    133       O  
ATOM   8319  CB AGLU C 316     100.075 -14.513-178.053  0.60 42.76           C  
ANISOU 8319  CB AGLU C 316     6996   5567   3686    407   -252    113       C  
ATOM   8320  CB BGLU C 316     100.044 -14.500-178.073  0.40 43.12           C  
ANISOU 8320  CB BGLU C 316     7039   5612   3732    407   -248    113       C  
ATOM   8321  CG AGLU C 316     101.368 -15.327-177.972  0.60 42.83           C  
ANISOU 8321  CG AGLU C 316     7021   5541   3709    407   -402    163       C  
ATOM   8322  CG BGLU C 316      99.015 -14.898-177.039  0.40 45.56           C  
ANISOU 8322  CG BGLU C 316     7456   5950   3905    380   -143    135       C  
ATOM   8323  CD AGLU C 316     101.965 -15.371-176.564  0.60 51.37           C  
ANISOU 8323  CD AGLU C 316     8259   6613   4646    394   -490    172       C  
ATOM   8324  CD BGLU C 316      99.601 -15.141-175.662  0.40 48.61           C  
ANISOU 8324  CD BGLU C 316     8009   6325   4137    361   -219    154       C  
ATOM   8325  OE1AGLU C 316     101.201 -15.588-175.597  0.60 46.42           O  
ANISOU 8325  OE1AGLU C 316     7750   6002   3885    370   -417    186       O  
ATOM   8326  OE1BGLU C 316     100.449 -14.341-175.211  0.40 47.71           O  
ANISOU 8326  OE1BGLU C 316     7946   6193   3987    375   -316    107       O  
ATOM   8327  OE2AGLU C 316     103.200 -15.189-176.425  0.60 48.49           O  
ANISOU 8327  OE2AGLU C 316     7897   6227   4301    405   -634    164       O  
ATOM   8328  OE2BGLU C 316      99.208 -16.145-175.041  0.40 46.13           O  
ANISOU 8328  OE2BGLU C 316     7778   6014   3736    329   -186    218       O  
ATOM   8329  N   HIS C 317     101.025 -12.857-180.447  1.00 39.04           N  
ANISOU 8329  N   HIS C 317     6277   5067   3489    454   -316     26       N  
ATOM   8330  CA  HIS C 317     102.083 -12.446-181.341  1.00 38.71           C  
ANISOU 8330  CA  HIS C 317     6145   5003   3558    462   -403     10       C  
ATOM   8331  C   HIS C 317     103.356 -12.140-180.556  1.00 38.68           C  
ANISOU 8331  C   HIS C 317     6201   4985   3510    451   -539     -2       C  
ATOM   8332  O   HIS C 317     103.282 -11.627-179.430  1.00 40.93           O  
ANISOU 8332  O   HIS C 317     6602   5271   3680    441   -553    -32       O  
ATOM   8333  CB  HIS C 317     101.635 -11.215-182.137  1.00 41.72           C  
ANISOU 8333  CB  HIS C 317     6464   5380   4006    475   -346    -51       C  
ATOM   8334  CG  HIS C 317     102.552 -10.848-183.256  1.00 37.77           C  
ANISOU 8334  CG  HIS C 317     5863   4860   3627    475   -408    -59       C  
ATOM   8335  ND1 HIS C 317     103.732 -10.166-183.057  1.00 39.02           N  
ANISOU 8335  ND1 HIS C 317     6027   5002   3797    459   -513    -85       N  
ATOM   8336  CD2 HIS C 317     102.457 -11.062-184.592  1.00 35.11           C  
ANISOU 8336  CD2 HIS C 317     5420   4520   3402    485   -378    -43       C  
ATOM   8337  CE1 HIS C 317     104.328  -9.974-184.222  1.00 43.07           C  
ANISOU 8337  CE1 HIS C 317     6435   5506   4425    456   -535    -84       C  
ATOM   8338  NE2 HIS C 317     103.576 -10.509-185.170  1.00 36.31           N  
ANISOU 8338  NE2 HIS C 317     5515   4655   3626    475   -453    -59       N  
ATOM   8339  N   PRO C 318     104.534 -12.471-181.098  1.00 43.29           N  
ANISOU 8339  N   PRO C 318     6709   5558   4181    454   -641     20       N  
ATOM   8340  CA  PRO C 318     105.770 -12.297-180.315  1.00 45.06           C  
ANISOU 8340  CA  PRO C 318     6977   5773   4369    442   -783     16       C  
ATOM   8341  C   PRO C 318     106.081 -10.861-179.934  1.00 47.33           C  
ANISOU 8341  C   PRO C 318     7303   6051   4630    419   -821    -54       C  
ATOM   8342  O   PRO C 318     106.778 -10.638-178.938  1.00 47.16           O  
ANISOU 8342  O   PRO C 318     7364   6021   4533    401   -927    -65       O  
ATOM   8343  CB  PRO C 318     106.857 -12.872-181.236  1.00 46.40           C  
ANISOU 8343  CB  PRO C 318     7020   5941   4667    457   -859     47       C  
ATOM   8344  CG  PRO C 318     106.241 -12.897-182.619  1.00 45.80           C  
ANISOU 8344  CG  PRO C 318     6839   5868   4695    470   -753     47       C  
ATOM   8345  CD  PRO C 318     104.782 -13.155-182.382  1.00 43.49           C  
ANISOU 8345  CD  PRO C 318     6610   5581   4333    471   -632     54       C  
ATOM   8346  N   THR C 319     105.621  -9.881-180.702  1.00 45.55           N  
ANISOU 8346  N   THR C 319     7026   5817   4462    417   -749   -101       N  
ATOM   8347  CA  THR C 319     105.954  -8.486-180.452  1.00 47.91           C  
ANISOU 8347  CA  THR C 319     7365   6094   4746    393   -791   -167       C  
ATOM   8348  C   THR C 319     104.760  -7.542-180.467  1.00 58.50           C  
ANISOU 8348  C   THR C 319     8757   7423   6048    409   -676   -222       C  
ATOM   8349  O   THR C 319     104.877  -6.433-179.933  1.00 53.00           O  
ANISOU 8349  O   THR C 319     8141   6698   5300    394   -707   -282       O  
ATOM   8350  CB  THR C 319     106.985  -7.980-181.475  1.00 46.84           C  
ANISOU 8350  CB  THR C 319     7107   5948   4744    369   -855   -175       C  
ATOM   8351  OG1 THR C 319     106.484  -8.159-182.811  1.00 50.13           O  
ANISOU 8351  OG1 THR C 319     7416   6369   5263    389   -761   -159       O  
ATOM   8352  CG2 THR C 319     108.312  -8.711-181.316  1.00 46.18           C  
ANISOU 8352  CG2 THR C 319     6968   5878   4698    358   -984   -133       C  
ATOM   8353  N   LEU C 320     103.632  -7.926-181.067  1.00 52.18           N  
ANISOU 8353  N   LEU C 320     7912   6638   5274    439   -551   -207       N  
ATOM   8354  CA  LEU C 320     102.425  -7.098-181.081  1.00 43.19           C  
ANISOU 8354  CA  LEU C 320     6809   5495   4107    466   -439   -258       C  
ATOM   8355  C   LEU C 320     101.578  -7.505-179.881  1.00 43.91           C  
ANISOU 8355  C   LEU C 320     7011   5612   4060    480   -372   -258       C  
ATOM   8356  O   LEU C 320     100.835  -8.487-179.937  1.00 40.60           O  
ANISOU 8356  O   LEU C 320     6567   5226   3634    489   -294   -211       O  
ATOM   8357  CB  LEU C 320     101.671  -7.270-182.400  1.00 41.54           C  
ANISOU 8357  CB  LEU C 320     6483   5293   4006    490   -350   -241       C  
ATOM   8358  CG  LEU C 320     102.410  -6.844-183.673  1.00 44.76           C  
ANISOU 8358  CG  LEU C 320     6790   5676   4542    475   -398   -241       C  
ATOM   8359  CD1 LEU C 320     101.666  -7.350-184.891  1.00 38.11           C  
ANISOU 8359  CD1 LEU C 320     5847   4845   3788    498   -317   -210       C  
ATOM   8360  CD2 LEU C 320     102.560  -5.316-183.739  1.00 48.63           C  
ANISOU 8360  CD2 LEU C 320     7319   6120   5037    469   -420   -308       C  
ATOM   8361  N   GLU C 321     101.681  -6.733-178.791  1.00 41.78           N  
ANISOU 8361  N   GLU C 321     6871   5326   3678    477   -399   -311       N  
ATOM   8362  CA  GLU C 321     101.101  -7.155-177.518  1.00 43.11           C  
ANISOU 8362  CA  GLU C 321     7166   5520   3695    481   -349   -308       C  
ATOM   8363  C   GLU C 321      99.581  -7.213-177.575  1.00 47.99           C  
ANISOU 8363  C   GLU C 321     7769   6173   4292    518   -180   -319       C  
ATOM   8364  O   GLU C 321      98.964  -7.983-176.829  1.00 46.58           O  
ANISOU 8364  O   GLU C 321     7648   6031   4019    514   -110   -287       O  
ATOM   8365  CB  GLU C 321     101.546  -6.214-176.393  1.00 57.91           C  
ANISOU 8365  CB  GLU C 321     9192   7363   5448    472   -417   -372       C  
ATOM   8366  CG  GLU C 321     102.996  -6.364-175.977  1.00 74.63           C  
ANISOU 8366  CG  GLU C 321    11345   9457   7552    428   -592   -353       C  
ATOM   8367  CD  GLU C 321     103.254  -5.818-174.571  1.00 93.91           C  
ANISOU 8367  CD  GLU C 321    13973  11879   9831    414   -653   -401       C  
ATOM   8368  OE1 GLU C 321     103.292  -4.581-174.405  1.00 97.73           O  
ANISOU 8368  OE1 GLU C 321    14519  12322  10292    417   -669   -479       O  
ATOM   8369  OE2 GLU C 321     103.402  -6.628-173.630  1.00 99.63           O  
ANISOU 8369  OE2 GLU C 321    14791  12620  10443    401   -687   -361       O  
ATOM   8370  N   TRP C 322      98.962  -6.418-178.451  1.00 39.22           N  
ANISOU 8370  N   TRP C 322     6580   5052   3270    553   -115   -360       N  
ATOM   8371  CA  TRP C 322      97.509  -6.367-178.541  1.00 43.60           C  
ANISOU 8371  CA  TRP C 322     7103   5643   3819    595     40   -377       C  
ATOM   8372  C   TRP C 322      96.914  -7.550-179.301  1.00 43.82           C  
ANISOU 8372  C   TRP C 322     7012   5712   3927    585    102   -304       C  
ATOM   8373  O   TRP C 322      95.685  -7.694-179.325  1.00 37.77           O  
ANISOU 8373  O   TRP C 322     6206   4986   3157    609    229   -306       O  
ATOM   8374  CB  TRP C 322      97.073  -5.064-179.220  1.00 42.76           C  
ANISOU 8374  CB  TRP C 322     6961   5504   3783    644     72   -449       C  
ATOM   8375  CG  TRP C 322      97.835  -4.796-180.491  1.00 41.10           C  
ANISOU 8375  CG  TRP C 322     6653   5252   3711    628    -16   -435       C  
ATOM   8376  CD1 TRP C 322      98.855  -3.917-180.646  1.00 42.76           C  
ANISOU 8376  CD1 TRP C 322     6896   5405   3944    608   -124   -468       C  
ATOM   8377  CD2 TRP C 322      97.657  -5.437-181.770  1.00 43.64           C  
ANISOU 8377  CD2 TRP C 322     6834   5587   4159    624      0   -381       C  
ATOM   8378  NE1 TRP C 322      99.333  -3.964-181.929  1.00 42.23           N  
ANISOU 8378  NE1 TRP C 322     6716   5320   4008    590   -168   -438       N  
ATOM   8379  CE2 TRP C 322      98.614  -4.886-182.645  1.00 42.73           C  
ANISOU 8379  CE2 TRP C 322     6677   5424   4134    604    -95   -386       C  
ATOM   8380  CE3 TRP C 322      96.787  -6.429-182.254  1.00 35.50           C  
ANISOU 8380  CE3 TRP C 322     5714   4603   3172    629     82   -330       C  
ATOM   8381  CZ2 TRP C 322      98.712  -5.265-183.990  1.00 42.10           C  
ANISOU 8381  CZ2 TRP C 322     6477   5342   4176    596   -101   -345       C  
ATOM   8382  CZ3 TRP C 322      96.896  -6.825-183.584  1.00 38.35           C  
ANISOU 8382  CZ3 TRP C 322     5958   4955   3656    621     63   -291       C  
ATOM   8383  CH2 TRP C 322      97.858  -6.244-184.437  1.00 42.47           C  
ANISOU 8383  CH2 TRP C 322     6449   5430   4257    608    -25   -300       C  
ATOM   8384  N   PHE C 323      97.743  -8.385-179.932  1.00 40.79           N  
ANISOU 8384  N   PHE C 323     6565   5317   3615    550     16   -242       N  
ATOM   8385  CA  PHE C 323      97.194  -9.467-180.750  1.00 46.61           C  
ANISOU 8385  CA  PHE C 323     7197   6081   4432    540     67   -178       C  
ATOM   8386  C   PHE C 323      96.442 -10.472-179.893  1.00 39.05           C  
ANISOU 8386  C   PHE C 323     6290   5167   3380    518    148   -132       C  
ATOM   8387  O   PHE C 323      95.374 -10.956-180.289  1.00 41.62           O  
ANISOU 8387  O   PHE C 323     6544   5527   3743    517    249   -108       O  
ATOM   8388  CB  PHE C 323      98.302 -10.158-181.542  1.00 44.10           C  
ANISOU 8388  CB  PHE C 323     6817   5737   4201    516    -42   -127       C  
ATOM   8389  CG  PHE C 323      97.796 -11.014-182.686  1.00 42.35           C  
ANISOU 8389  CG  PHE C 323     6482   5526   4083    513      0    -78       C  
ATOM   8390  CD1 PHE C 323      97.326 -12.306-182.457  1.00 38.34           C  
ANISOU 8390  CD1 PHE C 323     5979   5041   3548    487     39    -13       C  
ATOM   8391  CD2 PHE C 323      97.803 -10.526-183.980  1.00 44.01           C  
ANISOU 8391  CD2 PHE C 323     6594   5717   4412    530     -5    -95       C  
ATOM   8392  CE1 PHE C 323      96.868 -13.091-183.494  1.00 42.80           C  
ANISOU 8392  CE1 PHE C 323     6450   5607   4203    479     68     28       C  
ATOM   8393  CE2 PHE C 323      97.342 -11.308-185.035  1.00 39.99           C  
ANISOU 8393  CE2 PHE C 323     5993   5213   3989    527     26    -53       C  
ATOM   8394  CZ  PHE C 323      96.877 -12.588-184.796  1.00 37.21           C  
ANISOU 8394  CZ  PHE C 323     5644   4882   3611    501     59      6       C  
ATOM   8395  N   ALA C 324      96.972 -10.789-178.706  1.00 37.68           N  
ANISOU 8395  N   ALA C 324     6244   4993   3082    494    103   -118       N  
ATOM   8396  CA  ALA C 324      96.268 -11.696-177.812  1.00 39.96           C  
ANISOU 8396  CA  ALA C 324     6602   5319   3263    465    184    -72       C  
ATOM   8397  C   ALA C 324      94.858 -11.206-177.518  1.00 42.30           C  
ANISOU 8397  C   ALA C 324     6887   5664   3521    488    346   -113       C  
ATOM   8398  O   ALA C 324      93.935 -12.012-177.342  1.00 40.04           O  
ANISOU 8398  O   ALA C 324     6580   5422   3211    460    450    -68       O  
ATOM   8399  CB  ALA C 324      97.052 -11.863-176.506  1.00 42.77           C  
ANISOU 8399  CB  ALA C 324     7119   5661   3472    442    107    -62       C  
ATOM   8400  N   ALA C 325      94.677  -9.886-177.424  1.00 40.40           N  
ANISOU 8400  N   ALA C 325     6662   5416   3272    538    371   -199       N  
ATOM   8401  CA  ALA C 325      93.369  -9.380-177.021  1.00 43.42           C  
ANISOU 8401  CA  ALA C 325     7041   5848   3610    573    527   -245       C  
ATOM   8402  C   ALA C 325      92.317  -9.565-178.107  1.00 40.94           C  
ANISOU 8402  C   ALA C 325     6561   5567   3429    590    615   -232       C  
ATOM   8403  O   ALA C 325      91.120  -9.427-177.824  1.00 43.37           O  
ANISOU 8403  O   ALA C 325     6834   5930   3714    612    754   -253       O  
ATOM   8404  CB  ALA C 325      93.461  -7.905-176.618  1.00 46.04           C  
ANISOU 8404  CB  ALA C 325     7447   6152   3896    633    524   -346       C  
ATOM   8405  N   LEU C 326      92.725  -9.890-179.331  1.00 41.33           N  
ANISOU 8405  N   LEU C 326     6504   5587   3612    579    537   -197       N  
ATOM   8406  CA  LEU C 326      91.732 -10.183-180.350  1.00 41.62           C  
ANISOU 8406  CA  LEU C 326     6393   5654   3767    586    608   -178       C  
ATOM   8407  C   LEU C 326      90.936 -11.438-180.036  1.00 47.18           C  
ANISOU 8407  C   LEU C 326     7072   6411   4442    529    695   -107       C  
ATOM   8408  O   LEU C 326      89.868 -11.627-180.623  1.00 45.67           O  
ANISOU 8408  O   LEU C 326     6764   6260   4328    531    778    -98       O  
ATOM   8409  CB  LEU C 326      92.401 -10.316-181.726  1.00 42.54           C  
ANISOU 8409  CB  LEU C 326     6422   5722   4019    582    503   -154       C  
ATOM   8410  CG  LEU C 326      93.021  -9.019-182.252  1.00 42.97           C  
ANISOU 8410  CG  LEU C 326     6478   5725   4123    631    431   -220       C  
ATOM   8411  CD1 LEU C 326      93.710  -9.258-183.603  1.00 44.49           C  
ANISOU 8411  CD1 LEU C 326     6589   5877   4439    618    339   -188       C  
ATOM   8412  CD2 LEU C 326      91.968  -7.935-182.380  1.00 42.56           C  
ANISOU 8412  CD2 LEU C 326     6386   5688   4096    698    519   -289       C  
ATOM   8413  N   GLY C 327      91.410 -12.277-179.114  1.00 47.54           N  
ANISOU 8413  N   GLY C 327     7229   6456   4377    476    674    -56       N  
ATOM   8414  CA  GLY C 327      90.678 -13.459-178.704  1.00 43.69           C  
ANISOU 8414  CA  GLY C 327     6742   6013   3847    411    758     15       C  
ATOM   8415  C   GLY C 327      90.723 -14.609-179.684  1.00 45.31           C  
ANISOU 8415  C   GLY C 327     6864   6197   4155    362    710     90       C  
ATOM   8416  O   GLY C 327      89.924 -15.547-179.567  1.00 42.19           O  
ANISOU 8416  O   GLY C 327     6443   5837   3752    303    786    148       O  
ATOM   8417  N   LEU C 328      91.622 -14.558-180.660  1.00 45.08           N  
ANISOU 8417  N   LEU C 328     6794   6112   4221    382    589     91       N  
ATOM   8418  CA  LEU C 328      91.716 -15.619-181.646  1.00 50.62           C  
ANISOU 8418  CA  LEU C 328     7428   6788   5019    345    539    154       C  
ATOM   8419  C   LEU C 328      92.267 -16.896-181.023  1.00 49.17           C  
ANISOU 8419  C   LEU C 328     7346   6577   4758    287    491    232       C  
ATOM   8420  O   LEU C 328      93.084 -16.865-180.098  1.00 43.09           O  
ANISOU 8420  O   LEU C 328     6696   5788   3887    289    435    234       O  
ATOM   8421  CB  LEU C 328      92.608 -15.176-182.803  1.00 43.89           C  
ANISOU 8421  CB  LEU C 328     6518   5884   4275    386    431    129       C  
ATOM   8422  CG  LEU C 328      92.222 -13.831-183.424  1.00 43.77           C  
ANISOU 8422  CG  LEU C 328     6424   5877   4328    447    458     53       C  
ATOM   8423  CD1 LEU C 328      93.180 -13.494-184.556  1.00 38.01           C  
ANISOU 8423  CD1 LEU C 328     5653   5094   3695    473    351     40       C  
ATOM   8424  CD2 LEU C 328      90.785 -13.863-183.930  1.00 41.05           C  
ANISOU 8424  CD2 LEU C 328     5970   5580   4048    445    562     52       C  
ATOM   8425  N   ARG C 329      91.799 -18.030-181.538  1.00 37.56           N  
ANISOU 8425  N   ARG C 329     5833   5100   3338    234    505    297       N  
ATOM   8426  CA  ARG C 329      92.343 -19.324-181.157  1.00 42.85           C  
ANISOU 8426  CA  ARG C 329     6597   5727   3955    183    444    376       C  
ATOM   8427  C   ARG C 329      92.195 -20.267-182.334  1.00 43.02           C  
ANISOU 8427  C   ARG C 329     6544   5713   4090    156    409    421       C  
ATOM   8428  O   ARG C 329      91.500 -19.967-183.311  1.00 44.22           O  
ANISOU 8428  O   ARG C 329     6575   5884   4344    164    447    397       O  
ATOM   8429  CB  ARG C 329      91.658 -19.903-179.906  1.00 50.92           C  
ANISOU 8429  CB  ARG C 329     7717   6785   4846    117    535    423       C  
ATOM   8430  CG  ARG C 329      90.134 -19.875-179.941  1.00 61.15           C  
ANISOU 8430  CG  ARG C 329     8924   8152   6161     75    688    423       C  
ATOM   8431  CD  ARG C 329      89.529 -19.696-178.542  1.00 62.33           C  
ANISOU 8431  CD  ARG C 329     9161   8359   6161     44    807    424       C  
ATOM   8432  NE  ARG C 329      89.783 -20.843-177.680  1.00 68.41           N  
ANISOU 8432  NE  ARG C 329    10075   9101   6817    -31    790    508       N  
ATOM   8433  CZ  ARG C 329      90.496 -20.799-176.555  1.00 76.18           C  
ANISOU 8433  CZ  ARG C 329    11220  10066   7658    -26    751    515       C  
ATOM   8434  NH1 ARG C 329      91.025 -19.656-176.137  1.00 82.90           N  
ANISOU 8434  NH1 ARG C 329    12109  10927   8462     46    726    439       N  
ATOM   8435  NH2 ARG C 329      90.670 -21.900-175.840  1.00 67.47           N  
ANISOU 8435  NH2 ARG C 329    10250   8930   6454    -95    731    599       N  
ATOM   8436  N   TRP C 330      92.884 -21.403-182.247  1.00 39.71           N  
ANISOU 8436  N   TRP C 330     6204   5235   3648    129    327    485       N  
ATOM   8437  CA  TRP C 330      92.623 -22.495-183.175  1.00 43.39           C  
ANISOU 8437  CA  TRP C 330     6631   5660   4197     91    304    536       C  
ATOM   8438  C   TRP C 330      92.975 -23.805-182.491  1.00 45.96           C  
ANISOU 8438  C   TRP C 330     7087   5932   4443     41    258    617       C  
ATOM   8439  O   TRP C 330      93.586 -23.828-181.421  1.00 39.75           O  
ANISOU 8439  O   TRP C 330     6417   5138   3549     47    224    632       O  
ATOM   8440  CB  TRP C 330      93.380 -22.329-184.507  1.00 38.40           C  
ANISOU 8440  CB  TRP C 330     5923   4984   3685    150    214    505       C  
ATOM   8441  CG  TRP C 330      92.673 -23.038-185.626  1.00 39.08           C  
ANISOU 8441  CG  TRP C 330     5935   5049   3865    114    227    530       C  
ATOM   8442  CD1 TRP C 330      92.980 -24.262-186.162  1.00 41.99           C  
ANISOU 8442  CD1 TRP C 330     6342   5348   4265     91    163    582       C  
ATOM   8443  CD2 TRP C 330      91.497 -22.583-186.313  1.00 40.62           C  
ANISOU 8443  CD2 TRP C 330     6011   5290   4131     95    306    504       C  
ATOM   8444  NE1 TRP C 330      92.079 -24.582-187.153  1.00 36.88           N  
ANISOU 8444  NE1 TRP C 330     5613   4699   3700     53    194    588       N  
ATOM   8445  CE2 TRP C 330      91.159 -23.570-187.265  1.00 38.01           C  
ANISOU 8445  CE2 TRP C 330     5655   4916   3873     54    278    543       C  
ATOM   8446  CE3 TRP C 330      90.695 -21.441-186.211  1.00 38.15           C  
ANISOU 8446  CE3 TRP C 330     5617   5049   3830    114    391    451       C  
ATOM   8447  CZ2 TRP C 330      90.059 -23.444-188.108  1.00 37.90           C  
ANISOU 8447  CZ2 TRP C 330     5531   4930   3940     25    325    531       C  
ATOM   8448  CZ3 TRP C 330      89.607 -21.316-187.063  1.00 40.46           C  
ANISOU 8448  CZ3 TRP C 330     5793   5371   4211     95    439    440       C  
ATOM   8449  CH2 TRP C 330      89.300 -22.307-187.992  1.00 37.48           C  
ANISOU 8449  CH2 TRP C 330     5386   4951   3902     48    403    481       C  
ATOM   8450  N   TYR C 331      92.552 -24.899-183.103  1.00 43.49           N  
ANISOU 8450  N   TYR C 331     6766   5579   4181    -12    252    671       N  
ATOM   8451  CA  TYR C 331      92.699 -26.214-182.505  1.00 47.26           C  
ANISOU 8451  CA  TYR C 331     7374   5998   4587    -71    216    755       C  
ATOM   8452  C   TYR C 331      93.914 -26.936-183.073  1.00 49.39           C  
ANISOU 8452  C   TYR C 331     7690   6175   4901    -17     76    773       C  
ATOM   8453  O   TYR C 331      94.375 -26.661-184.188  1.00 45.48           O  
ANISOU 8453  O   TYR C 331     7107   5662   4510     43     27    731       O  
ATOM   8454  CB  TYR C 331      91.433 -27.050-182.716  1.00 43.25           C  
ANISOU 8454  CB  TYR C 331     6842   5494   4097   -176    298    810       C  
ATOM   8455  CG  TYR C 331      90.930 -27.096-184.145  1.00 43.91           C  
ANISOU 8455  CG  TYR C 331     6794   5570   4319   -177    297    786       C  
ATOM   8456  CD1 TYR C 331      91.398 -28.048-185.039  1.00 43.03           C  
ANISOU 8456  CD1 TYR C 331     6707   5370   4273   -172    202    814       C  
ATOM   8457  CD2 TYR C 331      89.963 -26.200-184.590  1.00 40.08           C  
ANISOU 8457  CD2 TYR C 331     6167   5164   3896   -179    387    736       C  
ATOM   8458  CE1 TYR C 331      90.928 -28.095-186.356  1.00 45.41           C  
ANISOU 8458  CE1 TYR C 331     6902   5660   4690   -176    197    791       C  
ATOM   8459  CE2 TYR C 331      89.480 -26.255-185.905  1.00 39.69           C  
ANISOU 8459  CE2 TYR C 331     6006   5105   3969   -183    374    718       C  
ATOM   8460  CZ  TYR C 331      89.968 -27.205-186.771  1.00 45.08           C  
ANISOU 8460  CZ  TYR C 331     6725   5699   4706   -185    279    746       C  
ATOM   8461  OH  TYR C 331      89.495 -27.253-188.071  1.00 48.20           O  
ANISOU 8461  OH  TYR C 331     7023   6081   5210   -189    262    726       O  
ATOM   8462  N   ALA C 332      94.409 -27.895-182.290  1.00 41.39           N  
ANISOU 8462  N   ALA C 332     6822   5103   3803    -38     15    839       N  
ATOM   8463  CA  ALA C 332      95.677 -28.547-182.601  1.00 41.64           C  
ANISOU 8463  CA  ALA C 332     6909   5049   3863     31   -125    854       C  
ATOM   8464  C   ALA C 332      95.542 -29.551-183.744  1.00 45.81           C  
ANISOU 8464  C   ALA C 332     7416   5504   4485     20   -159    880       C  
ATOM   8465  O   ALA C 332      96.463 -29.703-184.552  1.00 46.61           O  
ANISOU 8465  O   ALA C 332     7489   5559   4663    100   -246    855       O  
ATOM   8466  CB  ALA C 332      96.210 -29.252-181.349  1.00 42.10           C  
ANISOU 8466  CB  ALA C 332     7139   5061   3795     17   -188    919       C  
ATOM   8467  N   LEU C 333      94.415 -30.249-183.828  1.00 39.74           N  
ANISOU 8467  N   LEU C 333     6662   4724   3711    -80    -91    927       N  
ATOM   8468  CA  LEU C 333      94.351 -31.479-184.610  1.00 41.25           C  
ANISOU 8468  CA  LEU C 333     6893   4821   3957   -105   -143    970       C  
ATOM   8469  C   LEU C 333      93.548 -31.299-185.888  1.00 46.53           C  
ANISOU 8469  C   LEU C 333     7433   5510   4738   -130    -96    934       C  
ATOM   8470  O   LEU C 333      92.313 -31.186-185.822  1.00 46.11           O  
ANISOU 8470  O   LEU C 333     7326   5509   4685   -222      2    947       O  
ATOM   8471  CB  LEU C 333      93.741 -32.598-183.765  1.00 46.02           C  
ANISOU 8471  CB  LEU C 333     7638   5378   4471   -214   -124   1063       C  
ATOM   8472  CG  LEU C 333      93.862 -33.984-184.376  1.00 47.83           C  
ANISOU 8472  CG  LEU C 333     7954   5483   4737   -236   -203   1115       C  
ATOM   8473  CD1 LEU C 333      95.331 -34.386-184.492  1.00 49.91           C  
ANISOU 8473  CD1 LEU C 333     8291   5663   5010   -114   -341   1108       C  
ATOM   8474  CD2 LEU C 333      93.084 -34.994-183.539  1.00 49.75           C  
ANISOU 8474  CD2 LEU C 333     8330   5684   4889   -367   -167   1210       C  
ATOM   8475  N   PRO C 334      94.190 -31.292-187.074  1.00 41.49           N  
ANISOU 8475  N   PRO C 334     6740   4831   4194    -52   -161    890       N  
ATOM   8476  CA  PRO C 334      93.444 -31.329-188.341  1.00 41.36           C  
ANISOU 8476  CA  PRO C 334     6630   4811   4273    -81   -135    866       C  
ATOM   8477  C   PRO C 334      93.067 -32.764-188.675  1.00 45.41           C  
ANISOU 8477  C   PRO C 334     7237   5225   4794   -151   -174    927       C  
ATOM   8478  O   PRO C 334      93.923 -33.588-189.011  1.00 46.19           O  
ANISOU 8478  O   PRO C 334     7422   5226   4902    -96   -266    939       O  
ATOM   8479  CB  PRO C 334      94.444 -30.740-189.349  1.00 38.67           C  
ANISOU 8479  CB  PRO C 334     6219   4464   4008     36   -192    796       C  
ATOM   8480  CG  PRO C 334      95.784 -31.122-188.813  1.00 41.86           C  
ANISOU 8480  CG  PRO C 334     6715   4816   4373    116   -280    809       C  
ATOM   8481  CD  PRO C 334      95.648 -31.239-187.290  1.00 43.24           C  
ANISOU 8481  CD  PRO C 334     6982   5010   4435     67   -262    861       C  
ATOM   8482  N   ALA C 335      91.776 -33.071-188.565  1.00 40.21           N  
ANISOU 8482  N   ALA C 335     6559   4587   4130   -273   -104    965       N  
ATOM   8483  CA  ALA C 335      91.274 -34.440-188.646  1.00 43.04           C  
ANISOU 8483  CA  ALA C 335     7020   4852   4480   -371   -132   1035       C  
ATOM   8484  C   ALA C 335      90.048 -34.443-189.547  1.00 45.10           C  
ANISOU 8484  C   ALA C 335     7177   5139   4820   -458    -86   1025       C  
ATOM   8485  O   ALA C 335      88.934 -34.168-189.093  1.00 46.61           O  
ANISOU 8485  O   ALA C 335     7301   5410   5001   -557      8   1046       O  
ATOM   8486  CB  ALA C 335      90.943 -34.987-187.256  1.00 46.32           C  
ANISOU 8486  CB  ALA C 335     7550   5264   4785   -462    -94   1115       C  
ATOM   8487  N   VAL C 336      90.257 -34.776-190.814  1.00 46.42           N  
ANISOU 8487  N   VAL C 336     7334   5240   5064   -422   -154    993       N  
ATOM   8488  CA  VAL C 336      89.194 -34.741-191.812  1.00 44.94           C  
ANISOU 8488  CA  VAL C 336     7048   5071   4957   -492   -134    976       C  
ATOM   8489  C   VAL C 336      88.386 -36.031-191.750  1.00 46.05           C  
ANISOU 8489  C   VAL C 336     7276   5134   5089   -634   -150   1050       C  
ATOM   8490  O   VAL C 336      88.942 -37.135-191.755  1.00 45.51           O  
ANISOU 8490  O   VAL C 336     7358   4942   4992   -633   -228   1088       O  
ATOM   8491  CB  VAL C 336      89.789 -34.495-193.205  1.00 45.04           C  
ANISOU 8491  CB  VAL C 336     7026   5045   5044   -393   -200    908       C  
ATOM   8492  CG1 VAL C 336      88.809 -34.861-194.322  1.00 43.23           C  
ANISOU 8492  CG1 VAL C 336     6750   4789   4885   -472   -219    903       C  
ATOM   8493  CG2 VAL C 336      90.172 -33.049-193.286  1.00 42.58           C  
ANISOU 8493  CG2 VAL C 336     6594   4834   4751   -295   -160    840       C  
ATOM   8494  N   SER C 337      87.060 -35.888-191.709  1.00 46.03           N  
ANISOU 8494  N   SER C 337     7173   5202   5116   -755    -78   1070       N  
ATOM   8495  CA  SER C 337      86.161 -36.985-191.382  1.00 45.81           C  
ANISOU 8495  CA  SER C 337     7209   5125   5071   -917    -68   1150       C  
ATOM   8496  C   SER C 337      85.062 -37.188-192.414  1.00 50.67           C  
ANISOU 8496  C   SER C 337     7730   5744   5780  -1014    -80   1143       C  
ATOM   8497  O   SER C 337      84.151 -37.986-192.173  1.00 57.81           O  
ANISOU 8497  O   SER C 337     8655   6626   6683  -1168    -63   1208       O  
ATOM   8498  CB  SER C 337      85.529 -36.755-190.001  1.00 50.96           C  
ANISOU 8498  CB  SER C 337     7841   5871   5651  -1005     48   1203       C  
ATOM   8499  OG  SER C 337      84.925 -35.467-189.917  1.00 45.14           O  
ANISOU 8499  OG  SER C 337     6921   5281   4947   -981    145   1152       O  
ATOM   8500  N   ASN C 338      85.111 -36.499-193.554  1.00 47.13           N  
ANISOU 8500  N   ASN C 338     7179   5319   5408   -934   -113   1068       N  
ATOM   8501  CA  ASN C 338      84.016 -36.574-194.510  1.00 50.07           C  
ANISOU 8501  CA  ASN C 338     7449   5705   5868  -1023   -131   1058       C  
ATOM   8502  C   ASN C 338      84.438 -37.137-195.863  1.00 45.11           C  
ANISOU 8502  C   ASN C 338     6898   4960   5283   -983   -250   1024       C  
ATOM   8503  O   ASN C 338      83.640 -37.111-196.802  1.00 54.25           O  
ANISOU 8503  O   ASN C 338     7976   6123   6512  -1038   -283   1004       O  
ATOM   8504  CB  ASN C 338      83.366 -35.194-194.683  1.00 47.63           C  
ANISOU 8504  CB  ASN C 338     6936   5544   5617   -987    -58   1004       C  
ATOM   8505  CG  ASN C 338      84.262 -34.203-195.401  1.00 49.79           C  
ANISOU 8505  CG  ASN C 338     7177   5831   5910   -821    -90    922       C  
ATOM   8506  OD1 ASN C 338      85.454 -34.442-195.604  1.00 50.15           O  
ANISOU 8506  OD1 ASN C 338     7338   5795   5920   -725   -148    904       O  
ATOM   8507  ND2 ASN C 338      83.688 -33.067-195.777  1.00 60.45           N  
ANISOU 8507  ND2 ASN C 338     8366   7284   7318   -787    -50    873       N  
ATOM   8508  N   MET C 339      85.659 -37.642-195.992  1.00 47.21           N  
ANISOU 8508  N   MET C 339     7313   5119   5505   -885   -317   1014       N  
ATOM   8509  CA  MET C 339      86.114 -38.231-197.243  1.00 47.18           C  
ANISOU 8509  CA  MET C 339     7397   4997   5530   -839   -421    978       C  
ATOM   8510  C   MET C 339      85.955 -39.746-197.207  1.00 50.91           C  
ANISOU 8510  C   MET C 339     8039   5326   5979   -942   -490   1039       C  
ATOM   8511  O   MET C 339      85.736 -40.347-196.151  1.00 51.19           O  
ANISOU 8511  O   MET C 339     8142   5344   5964  -1031   -461   1112       O  
ATOM   8512  CB  MET C 339      87.566 -37.844-197.527  1.00 52.35           C  
ANISOU 8512  CB  MET C 339     8103   5625   6163   -658   -449    921       C  
ATOM   8513  CG  MET C 339      87.740 -36.353-197.835  1.00 44.60           C  
ANISOU 8513  CG  MET C 339     6967   4765   5214   -561   -398    854       C  
ATOM   8514  SD  MET C 339      89.415 -35.942-198.339  1.00 49.66           S  
ANISOU 8514  SD  MET C 339     7656   5372   5839   -368   -433    788       S  
ATOM   8515  CE  MET C 339      89.441 -36.594-200.003  1.00 43.19           C  
ANISOU 8515  CE  MET C 339     6909   4443   5060   -353   -521    746       C  
ATOM   8516  N   LEU C 340      86.037 -40.359-198.387  1.00 45.45           N  
ANISOU 8516  N   LEU C 340     7424   4527   5318   -935   -583   1009       N  
ATOM   8517  CA  LEU C 340      85.827 -41.793-198.550  1.00 46.16           C  
ANISOU 8517  CA  LEU C 340     7682   4464   5392  -1034   -663   1057       C  
ATOM   8518  C   LEU C 340      87.149 -42.459-198.911  1.00 40.88           C  
ANISOU 8518  C   LEU C 340     7190   3657   4685   -897   -738   1028       C  
ATOM   8519  O   LEU C 340      87.867 -41.984-199.792  1.00 48.23           O  
ANISOU 8519  O   LEU C 340     8104   4588   5634   -761   -761    953       O  
ATOM   8520  CB  LEU C 340      84.772 -42.057-199.626  1.00 54.79           C  
ANISOU 8520  CB  LEU C 340     8735   5533   6551  -1147   -718   1044       C  
ATOM   8521  CG  LEU C 340      84.348 -43.484-199.990  1.00 57.99           C  
ANISOU 8521  CG  LEU C 340     9304   5779   6953  -1275   -813   1086       C  
ATOM   8522  CD1 LEU C 340      82.853 -43.503-200.243  1.00 53.40           C  
ANISOU 8522  CD1 LEU C 340     8603   5252   6436  -1461   -813   1115       C  
ATOM   8523  CD2 LEU C 340      85.095 -43.971-201.223  1.00 54.61           C  
ANISOU 8523  CD2 LEU C 340     9013   5216   6522  -1171   -915   1021       C  
ATOM   8524  N   LEU C 341      87.489 -43.523-198.194  1.00 47.80           N  
ANISOU 8524  N   LEU C 341     8233   4421   5506   -928   -773   1089       N  
ATOM   8525  CA  LEU C 341      88.697 -44.299-198.446  1.00 49.27           C  
ANISOU 8525  CA  LEU C 341     8598   4464   5659   -799   -851   1069       C  
ATOM   8526  C   LEU C 341      88.344 -45.487-199.333  1.00 52.52           C  
ANISOU 8526  C   LEU C 341     9161   4712   6081   -871   -950   1071       C  
ATOM   8527  O   LEU C 341      87.436 -46.260-199.007  1.00 57.71           O  
ANISOU 8527  O   LEU C 341     9881   5313   6734  -1043   -970   1140       O  
ATOM   8528  CB  LEU C 341      89.314 -44.789-197.130  1.00 48.88           C  
ANISOU 8528  CB  LEU C 341     8658   4373   5539   -779   -846   1136       C  
ATOM   8529  CG  LEU C 341      90.432 -45.835-197.182  1.00 47.76           C  
ANISOU 8529  CG  LEU C 341     8722   4063   5360   -667   -938   1136       C  
ATOM   8530  CD1 LEU C 341      91.616 -45.361-198.023  1.00 43.43           C  
ANISOU 8530  CD1 LEU C 341     8145   3518   4837   -461   -957   1042       C  
ATOM   8531  CD2 LEU C 341      90.903 -46.200-195.765  1.00 48.41           C  
ANISOU 8531  CD2 LEU C 341     8899   4123   5371   -662   -933   1212       C  
ATOM   8532  N   GLU C 342      89.064 -45.639-200.441  1.00 49.43           N  
ANISOU 8532  N   GLU C 342     8835   4243   5702   -744  -1009    996       N  
ATOM   8533  CA  GLU C 342      88.816 -46.718-201.390  1.00 49.61           C  
ANISOU 8533  CA  GLU C 342     9016   4103   5730   -792  -1107    982       C  
ATOM   8534  C   GLU C 342      90.060 -47.577-201.549  1.00 49.56           C  
ANISOU 8534  C   GLU C 342     9203   3943   5685   -641  -1173    957       C  
ATOM   8535  O   GLU C 342      91.133 -47.065-201.886  1.00 48.24           O  
ANISOU 8535  O   GLU C 342     9004   3808   5518   -458  -1154    891       O  
ATOM   8536  CB  GLU C 342      88.387 -46.183-202.759  1.00 53.50           C  
ANISOU 8536  CB  GLU C 342     9425   4632   6270   -788  -1125    907       C  
ATOM   8537  CG  GLU C 342      88.054 -47.310-203.738  1.00 67.80           C  
ANISOU 8537  CG  GLU C 342    11411   6270   8078   -852  -1234    891       C  
ATOM   8538  CD  GLU C 342      89.165 -47.577-204.743  1.00 83.97           C  
ANISOU 8538  CD  GLU C 342    13582   8218  10104   -670  -1279    805       C  
ATOM   8539  OE1 GLU C 342      89.416 -48.761-205.067  1.00 85.78           O  
ANISOU 8539  OE1 GLU C 342    14020   8268  10305   -665  -1364    802       O  
ATOM   8540  OE2 GLU C 342      89.782 -46.597-205.220  1.00 87.87           O  
ANISOU 8540  OE2 GLU C 342    13967   8812  10609   -534  -1227    738       O  
ATOM   8541  N   ILE C 343      89.899 -48.883-201.330  1.00 46.38           N  
ANISOU 8541  N   ILE C 343     8999   3372   5253   -718  -1251   1009       N  
ATOM   8542  CA  ILE C 343      90.996 -49.851-201.359  1.00 50.82           C  
ANISOU 8542  CA  ILE C 343     9766   3768   5778   -582  -1322    996       C  
ATOM   8543  C   ILE C 343      90.500 -51.110-202.052  1.00 51.72           C  
ANISOU 8543  C   ILE C 343    10081   3688   5883   -676  -1426   1001       C  
ATOM   8544  O   ILE C 343      89.559 -51.753-201.572  1.00 55.51           O  
ANISOU 8544  O   ILE C 343    10626   4112   6355   -868  -1455   1081       O  
ATOM   8545  CB  ILE C 343      91.499 -50.211-199.948  1.00 50.85           C  
ANISOU 8545  CB  ILE C 343     9839   3748   5734   -564  -1317   1075       C  
ATOM   8546  CG1 ILE C 343      91.911 -48.964-199.166  1.00 46.96           C  
ANISOU 8546  CG1 ILE C 343     9155   3446   5243   -490  -1219   1074       C  
ATOM   8547  CG2 ILE C 343      92.648 -51.195-200.040  1.00 48.62           C  
ANISOU 8547  CG2 ILE C 343     9758   3294   5422   -405  -1400   1054       C  
ATOM   8548  CD1 ILE C 343      92.137 -49.249-197.673  1.00 50.44           C  
ANISOU 8548  CD1 ILE C 343     9657   3880   5628   -517  -1211   1164       C  
ATOM   8549  N   GLY C 344      91.137 -51.474-203.160  1.00 55.23           N  
ANISOU 8549  N   GLY C 344    10630   4028   6327   -546  -1481    917       N  
ATOM   8550  CA  GLY C 344      90.788 -52.717-203.834  1.00 54.83           C  
ANISOU 8550  CA  GLY C 344    10734   3839   6260   -607  -1568    888       C  
ATOM   8551  C   GLY C 344      89.323 -52.844-204.184  1.00 56.86           C  
ANISOU 8551  C   GLY C 344    10975   4088   6543   -842  -1601    927       C  
ATOM   8552  O   GLY C 344      88.764 -53.946-204.130  1.00 58.92           O  
ANISOU 8552  O   GLY C 344    11345   4257   6785   -964  -1664    953       O  
ATOM   8553  N   GLY C 345      88.682 -51.734-204.549  1.00 51.29           N  
ANISOU 8553  N   GLY C 345    10103   3504   5881   -905  -1556    922       N  
ATOM   8554  CA  GLY C 345      87.268 -51.751-204.846  1.00 54.20           C  
ANISOU 8554  CA  GLY C 345    10407   3899   6286  -1126  -1583    954       C  
ATOM   8555  C   GLY C 345      86.358 -51.678-203.642  1.00 60.78           C  
ANISOU 8555  C   GLY C 345    11141   4818   7134  -1313  -1531   1061       C  
ATOM   8556  O   GLY C 345      85.141 -51.549-203.817  1.00 61.14           O  
ANISOU 8556  O   GLY C 345    11087   4919   7223  -1498  -1537   1090       O  
ATOM   8557  N   LEU C 346      86.892 -51.783-202.427  1.00 54.80           N  
ANISOU 8557  N   LEU C 346    10410   4071   6339  -1274  -1483   1122       N  
ATOM   8558  CA  LEU C 346      86.090 -51.577-201.235  1.00 54.78           C  
ANISOU 8558  CA  LEU C 346    10304   4172   6340  -1438  -1411   1220       C  
ATOM   8559  C   LEU C 346      86.056 -50.096-200.882  1.00 56.65           C  
ANISOU 8559  C   LEU C 346    10280   4641   6604  -1378  -1290   1198       C  
ATOM   8560  O   LEU C 346      86.985 -49.342-201.184  1.00 53.06           O  
ANISOU 8560  O   LEU C 346     9763   4249   6149  -1186  -1259   1126       O  
ATOM   8561  CB  LEU C 346      86.648 -52.380-200.061  1.00 49.11           C  
ANISOU 8561  CB  LEU C 346     9753   3352   5556  -1430  -1419   1300       C  
ATOM   8562  CG  LEU C 346      86.872 -53.867-200.336  1.00 52.17           C  
ANISOU 8562  CG  LEU C 346    10338   3574   5910  -1424  -1518   1279       C  
ATOM   8563  CD1 LEU C 346      87.424 -54.547-199.078  1.00 56.33           C  
ANISOU 8563  CD1 LEU C 346    10963   4067   6373  -1393  -1507   1336       C  
ATOM   8564  CD2 LEU C 346      85.588 -54.531-200.781  1.00 52.20           C  
ANISOU 8564  CD2 LEU C 346    10358   3533   5941  -1647  -1569   1304       C  
ATOM   8565  N   GLU C 347      84.978 -49.684-200.225  1.00 53.82           N  
ANISOU 8565  N   GLU C 347     9771   4408   6271  -1546  -1219   1260       N  
ATOM   8566  CA  GLU C 347      84.746 -48.275-199.950  1.00 57.65           C  
ANISOU 8566  CA  GLU C 347    10006   5109   6788  -1508  -1108   1237       C  
ATOM   8567  C   GLU C 347      84.403 -48.098-198.479  1.00 55.13           C  
ANISOU 8567  C   GLU C 347     9627   4883   6435  -1598  -1010   1325       C  
ATOM   8568  O   GLU C 347      83.514 -48.778-197.950  1.00 55.73           O  
ANISOU 8568  O   GLU C 347     9742   4927   6507  -1793  -1007   1408       O  
ATOM   8569  CB  GLU C 347      83.642 -47.728-200.866  1.00 61.69           C  
ANISOU 8569  CB  GLU C 347    10353   5709   7378  -1607  -1114   1202       C  
ATOM   8570  CG  GLU C 347      84.019 -47.828-202.359  1.00 68.89           C  
ANISOU 8570  CG  GLU C 347    11333   6532   8308  -1509  -1209   1110       C  
ATOM   8571  CD  GLU C 347      82.881 -47.489-203.311  1.00 80.45           C  
ANISOU 8571  CD  GLU C 347    12672   8051   9842  -1623  -1247   1083       C  
ATOM   8572  OE1 GLU C 347      81.701 -47.632-202.917  1.00 77.08           O  
ANISOU 8572  OE1 GLU C 347    12155   7676   9456  -1817  -1233   1146       O  
ATOM   8573  OE2 GLU C 347      83.171 -47.085-204.463  1.00 85.44           O  
ANISOU 8573  OE2 GLU C 347    13297   8677  10489  -1520  -1291   1000       O  
ATOM   8574  N   PHE C 348      85.132 -47.203-197.824  1.00 50.56           N  
ANISOU 8574  N   PHE C 348     8965   4416   5830  -1460   -931   1307       N  
ATOM   8575  CA  PHE C 348      84.943 -46.906-196.411  1.00 56.20           C  
ANISOU 8575  CA  PHE C 348     9629   5227   6498  -1517   -832   1378       C  
ATOM   8576  C   PHE C 348      84.477 -45.465-196.283  1.00 50.12           C  
ANISOU 8576  C   PHE C 348     8606   4668   5769  -1497   -722   1341       C  
ATOM   8577  O   PHE C 348      85.300 -44.537-196.332  1.00 51.62           O  
ANISOU 8577  O   PHE C 348     8724   4934   5955  -1327   -692   1279       O  
ATOM   8578  CB  PHE C 348      86.246 -47.138-195.637  1.00 58.78           C  
ANISOU 8578  CB  PHE C 348    10097   5491   6747  -1371   -846   1391       C  
ATOM   8579  CG  PHE C 348      86.791 -48.534-195.789  1.00 60.91           C  
ANISOU 8579  CG  PHE C 348    10622   5543   6979  -1363   -961   1421       C  
ATOM   8580  CD1 PHE C 348      87.640 -48.854-196.838  1.00 55.07           C  
ANISOU 8580  CD1 PHE C 348     9975   4691   6258  -1214  -1052   1345       C  
ATOM   8581  CD2 PHE C 348      86.435 -49.533-194.893  1.00 61.94           C  
ANISOU 8581  CD2 PHE C 348    10906   5576   7051  -1505   -976   1524       C  
ATOM   8582  CE1 PHE C 348      88.131 -50.140-196.988  1.00 57.52           C  
ANISOU 8582  CE1 PHE C 348    10526   4796   6535  -1195  -1158   1366       C  
ATOM   8583  CE2 PHE C 348      86.926 -50.834-195.032  1.00 63.38           C  
ANISOU 8583  CE2 PHE C 348    11338   5544   7198  -1495  -1091   1552       C  
ATOM   8584  CZ  PHE C 348      87.775 -51.137-196.076  1.00 55.30           C  
ANISOU 8584  CZ  PHE C 348    10403   4409   6198  -1334  -1183   1471       C  
ATOM   8585  N   PRO C 349      83.169 -45.218-196.171  1.00 51.00           N  
ANISOU 8585  N   PRO C 349     8573   4879   5926  -1662   -663   1374       N  
ATOM   8586  CA  PRO C 349      82.679 -43.832-196.143  1.00 51.20           C  
ANISOU 8586  CA  PRO C 349     8356   5099   5999  -1631   -565   1331       C  
ATOM   8587  C   PRO C 349      82.959 -43.110-194.832  1.00 53.66           C  
ANISOU 8587  C   PRO C 349     8610   5529   6251  -1585   -448   1355       C  
ATOM   8588  O   PRO C 349      82.799 -41.884-194.779  1.00 49.21           O  
ANISOU 8588  O   PRO C 349     7868   5115   5716  -1519   -371   1308       O  
ATOM   8589  CB  PRO C 349      81.168 -43.989-196.380  1.00 54.82           C  
ANISOU 8589  CB  PRO C 349     8691   5612   6528  -1832   -548   1366       C  
ATOM   8590  CG  PRO C 349      80.971 -45.409-196.841  1.00 59.67           C  
ANISOU 8590  CG  PRO C 349     9488   6044   7139  -1954   -660   1409       C  
ATOM   8591  CD  PRO C 349      82.072 -46.197-196.222  1.00 55.69           C  
ANISOU 8591  CD  PRO C 349     9213   5404   6542  -1882   -696   1443       C  
ATOM   8592  N   ALA C 350      83.349 -43.827-193.775  1.00 48.49           N  
ANISOU 8592  N   ALA C 350     8110   4806   5509  -1620   -438   1428       N  
ATOM   8593  CA  ALA C 350      83.783 -43.222-192.515  1.00 50.43           C  
ANISOU 8593  CA  ALA C 350     8341   5142   5678  -1563   -345   1450       C  
ATOM   8594  C   ALA C 350      85.172 -43.778-192.228  1.00 51.62           C  
ANISOU 8594  C   ALA C 350     8691   5165   5756  -1431   -424   1454       C  
ATOM   8595  O   ALA C 350      85.326 -44.954-191.884  1.00 51.93           O  
ANISOU 8595  O   ALA C 350     8922   5065   5745  -1497   -484   1522       O  
ATOM   8596  CB  ALA C 350      82.812 -43.524-191.376  1.00 51.12           C  
ANISOU 8596  CB  ALA C 350     8418   5287   5720  -1746   -245   1544       C  
ATOM   8597  N   ALA C 351      86.184 -42.934-192.395  1.00 50.30           N  
ANISOU 8597  N   ALA C 351     8479   5043   5589  -1243   -430   1381       N  
ATOM   8598  CA  ALA C 351      87.577 -43.320-192.164  1.00 57.98           C  
ANISOU 8598  CA  ALA C 351     9607   5914   6508  -1096   -506   1375       C  
ATOM   8599  C   ALA C 351      88.373 -42.057-191.871  1.00 54.91           C  
ANISOU 8599  C   ALA C 351     9107   5645   6111   -939   -459   1313       C  
ATOM   8600  O   ALA C 351      89.209 -41.617-192.673  1.00 52.29           O  
ANISOU 8600  O   ALA C 351     8740   5308   5821   -791   -503   1236       O  
ATOM   8601  CB  ALA C 351      88.141 -44.064-193.374  1.00 47.75           C  
ANISOU 8601  CB  ALA C 351     8415   4472   5257  -1022   -624   1332       C  
ATOM   8602  N   PRO C 352      88.122 -41.428-190.725  1.00 49.67           N  
ANISOU 8602  N   PRO C 352     8388   5093   5390   -973   -365   1343       N  
ATOM   8603  CA  PRO C 352      88.735 -40.126-190.461  1.00 45.83           C  
ANISOU 8603  CA  PRO C 352     7785   4728   4900   -842   -317   1280       C  
ATOM   8604  C   PRO C 352      90.238 -40.260-190.280  1.00 45.32           C  
ANISOU 8604  C   PRO C 352     7827   4593   4799   -682   -400   1261       C  
ATOM   8605  O   PRO C 352      90.726 -41.220-189.677  1.00 49.40           O  
ANISOU 8605  O   PRO C 352     8516   5002   5252   -685   -461   1320       O  
ATOM   8606  CB  PRO C 352      88.050 -39.671-189.165  1.00 51.88           C  
ANISOU 8606  CB  PRO C 352     8511   5605   5597   -935   -203   1329       C  
ATOM   8607  CG  PRO C 352      87.707 -40.967-188.471  1.00 49.93           C  
ANISOU 8607  CG  PRO C 352     8437   5255   5280  -1069   -222   1432       C  
ATOM   8608  CD  PRO C 352      87.328 -41.909-189.579  1.00 50.60           C  
ANISOU 8608  CD  PRO C 352     8565   5224   5436  -1133   -300   1438       C  
ATOM   8609  N   PHE C 353      90.971 -39.276-190.800  1.00 41.13           N  
ANISOU 8609  N   PHE C 353     7191   4126   4312   -541   -403   1178       N  
ATOM   8610  CA  PHE C 353      92.426 -39.266-190.737  1.00 44.27           C  
ANISOU 8610  CA  PHE C 353     7650   4476   4693   -381   -478   1148       C  
ATOM   8611  C   PHE C 353      92.905 -37.893-190.284  1.00 43.24           C  
ANISOU 8611  C   PHE C 353     7398   4477   4554   -296   -425   1099       C  
ATOM   8612  O   PHE C 353      92.244 -36.878-190.515  1.00 46.96           O  
ANISOU 8612  O   PHE C 353     7722   5060   5060   -323   -346   1059       O  
ATOM   8613  CB  PHE C 353      93.053 -39.632-192.094  1.00 43.69           C  
ANISOU 8613  CB  PHE C 353     7591   4317   4693   -284   -555   1091       C  
ATOM   8614  CG  PHE C 353      92.539 -38.799-193.265  1.00 47.95           C  
ANISOU 8614  CG  PHE C 353     7975   4930   5314   -281   -514   1020       C  
ATOM   8615  CD1 PHE C 353      93.142 -37.596-193.597  1.00 41.30           C  
ANISOU 8615  CD1 PHE C 353     7006   4181   4504   -171   -486    948       C  
ATOM   8616  CD2 PHE C 353      91.476 -39.245-194.035  1.00 48.60           C  
ANISOU 8616  CD2 PHE C 353     8048   4980   5438   -391   -513   1028       C  
ATOM   8617  CE1 PHE C 353      92.675 -36.829-194.687  1.00 45.12           C  
ANISOU 8617  CE1 PHE C 353     7362   4724   5056   -167   -455    887       C  
ATOM   8618  CE2 PHE C 353      91.005 -38.496-195.117  1.00 43.31           C  
ANISOU 8618  CE2 PHE C 353     7245   4371   4838   -385   -488    966       C  
ATOM   8619  CZ  PHE C 353      91.611 -37.291-195.436  1.00 39.39           C  
ANISOU 8619  CZ  PHE C 353     6632   3966   4369   -271   -458    897       C  
ATOM   8620  N   SER C 354      94.063 -37.866-189.634  1.00 46.47           N  
ANISOU 8620  N   SER C 354     7872   4867   4918   -192   -478   1100       N  
ATOM   8621  CA  SER C 354      94.575 -36.621-189.086  1.00 43.19           C  
ANISOU 8621  CA  SER C 354     7361   4565   4485   -120   -441   1058       C  
ATOM   8622  C   SER C 354      96.085 -36.599-189.230  1.00 44.19           C  
ANISOU 8622  C   SER C 354     7511   4652   4626     34   -531   1022       C  
ATOM   8623  O   SER C 354      96.732 -37.648-189.269  1.00 41.07           O  
ANISOU 8623  O   SER C 354     7239   4142   4224     81   -620   1051       O  
ATOM   8624  CB  SER C 354      94.175 -36.440-187.615  1.00 39.15           C  
ANISOU 8624  CB  SER C 354     6900   4108   3869   -196   -387   1114       C  
ATOM   8625  OG  SER C 354      94.705 -37.496-186.821  1.00 46.85           O  
ANISOU 8625  OG  SER C 354     8052   4981   4768   -197   -463   1184       O  
ATOM   8626  N   GLY C 355      96.637 -35.394-189.334  1.00 46.53           N  
ANISOU 8626  N   GLY C 355     7686   5042   4950    114   -509    958       N  
ATOM   8627  CA  GLY C 355      98.074 -35.216-189.290  1.00 43.27           C  
ANISOU 8627  CA  GLY C 355     7272   4616   4550    251   -586    926       C  
ATOM   8628  C   GLY C 355      98.427 -34.106-188.326  1.00 44.04           C  
ANISOU 8628  C   GLY C 355     7316   4815   4602    271   -562    909       C  
ATOM   8629  O   GLY C 355      98.065 -34.155-187.144  1.00 45.69           O  
ANISOU 8629  O   GLY C 355     7598   5041   4719    208   -544    959       O  
ATOM   8630  N   TRP C 356      99.155 -33.111-188.817  1.00 45.17           N  
ANISOU 8630  N   TRP C 356     7341   5020   4801    357   -563    840       N  
ATOM   8631  CA  TRP C 356      99.307 -31.837-188.136  1.00 41.32           C  
ANISOU 8631  CA  TRP C 356     6780   4635   4283    363   -527    808       C  
ATOM   8632  C   TRP C 356      99.205 -30.715-189.158  1.00 41.07           C  
ANISOU 8632  C   TRP C 356     6599   4673   4332    387   -471    734       C  
ATOM   8633  O   TRP C 356      99.225 -30.937-190.379  1.00 37.54           O  
ANISOU 8633  O   TRP C 356     6109   4195   3960    414   -472    706       O  
ATOM   8634  CB  TRP C 356     100.627 -31.732-187.383  1.00 38.39           C  
ANISOU 8634  CB  TRP C 356     6443   4261   3884    450   -618    808       C  
ATOM   8635  CG  TRP C 356     101.840 -32.050-188.191  1.00 43.43           C  
ANISOU 8635  CG  TRP C 356     7045   4855   4602    566   -697    776       C  
ATOM   8636  CD1 TRP C 356     102.517 -31.209-189.028  1.00 45.06           C  
ANISOU 8636  CD1 TRP C 356     7122   5111   4889    635   -690    708       C  
ATOM   8637  CD2 TRP C 356     102.557 -33.290-188.203  1.00 44.96           C  
ANISOU 8637  CD2 TRP C 356     7336   4947   4801    631   -793    811       C  
ATOM   8638  NE1 TRP C 356     103.602 -31.855-189.575  1.00 44.93           N  
ANISOU 8638  NE1 TRP C 356     7104   5037   4929    738   -765    697       N  
ATOM   8639  CE2 TRP C 356     103.648 -33.135-189.087  1.00 49.43           C  
ANISOU 8639  CE2 TRP C 356     7812   5512   5457    744   -832    757       C  
ATOM   8640  CE3 TRP C 356     102.368 -34.523-187.573  1.00 43.45           C  
ANISOU 8640  CE3 TRP C 356     7302   4659   4547    604   -847    884       C  
ATOM   8641  CZ2 TRP C 356     104.552 -34.169-189.350  1.00 48.34           C  
ANISOU 8641  CZ2 TRP C 356     7729   5286   5352    843   -921    768       C  
ATOM   8642  CZ3 TRP C 356     103.270 -35.544-187.822  1.00 47.33           C  
ANISOU 8642  CZ3 TRP C 356     7860   5053   5069    701   -946    898       C  
ATOM   8643  CH2 TRP C 356     104.352 -35.362-188.702  1.00 47.49           C  
ANISOU 8643  CH2 TRP C 356     7781   5080   5184    825   -982    837       C  
ATOM   8644  N   TYR C 357      99.105 -29.496-188.646  1.00 35.90           N  
ANISOU 8644  N   TYR C 357     5879   4108   3654    379   -426    701       N  
ATOM   8645  CA  TYR C 357      98.801 -28.345-189.489  1.00 36.09           C  
ANISOU 8645  CA  TYR C 357     5774   4197   3741    386   -365    638       C  
ATOM   8646  C   TYR C 357     100.051 -27.761-190.134  1.00 39.93           C  
ANISOU 8646  C   TYR C 357     6188   4694   4291    481   -412    585       C  
ATOM   8647  O   TYR C 357     101.130 -27.737-189.539  1.00 37.18           O  
ANISOU 8647  O   TYR C 357     5860   4343   3924    537   -480    585       O  
ATOM   8648  CB  TYR C 357      98.122 -27.251-188.666  1.00 37.13           C  
ANISOU 8648  CB  TYR C 357     5873   4415   3821    339   -292    622       C  
ATOM   8649  CG  TYR C 357      96.612 -27.238-188.728  1.00 42.90           C  
ANISOU 8649  CG  TYR C 357     6582   5175   4545    250   -199    636       C  
ATOM   8650  CD1 TYR C 357      95.951 -26.983-189.919  1.00 35.60           C  
ANISOU 8650  CD1 TYR C 357     5568   4259   3700    239   -161    606       C  
ATOM   8651  CD2 TYR C 357      95.846 -27.449-187.581  1.00 41.42           C  
ANISOU 8651  CD2 TYR C 357     6458   5011   4270    177   -148    680       C  
ATOM   8652  CE1 TYR C 357      94.567 -26.943-189.978  1.00 41.65           C  
ANISOU 8652  CE1 TYR C 357     6296   5058   4470    160    -84    618       C  
ATOM   8653  CE2 TYR C 357      94.454 -27.418-187.633  1.00 39.98           C  
ANISOU 8653  CE2 TYR C 357     6234   4866   4089     95    -56    692       C  
ATOM   8654  CZ  TYR C 357      93.824 -27.162-188.831  1.00 39.42           C  
ANISOU 8654  CZ  TYR C 357     6062   4806   4110     88    -28    660       C  
ATOM   8655  OH  TYR C 357      92.449 -27.123-188.886  1.00 41.09           O  
ANISOU 8655  OH  TYR C 357     6217   5060   4333      8     56    672       O  
ATOM   8656  N   MET C 358      99.890 -27.285-191.374  1.00 36.13           N  
ANISOU 8656  N   MET C 358     5619   4225   3884    496   -378    540       N  
ATOM   8657  CA  MET C 358     100.802 -26.308-191.948  1.00 38.56           C  
ANISOU 8657  CA  MET C 358     5835   4570   4245    559   -387    483       C  
ATOM   8658  C   MET C 358     100.256 -24.922-191.619  1.00 35.22           C  
ANISOU 8658  C   MET C 358     5352   4224   3806    524   -328    450       C  
ATOM   8659  O   MET C 358      99.043 -24.704-191.651  1.00 33.50           O  
ANISOU 8659  O   MET C 358     5125   4027   3577    465   -264    453       O  
ATOM   8660  CB  MET C 358     100.942 -26.489-193.465  1.00 34.40           C  
ANISOU 8660  CB  MET C 358     5262   4015   3795    592   -378    454       C  
ATOM   8661  CG  MET C 358     101.962 -25.546-194.072  1.00 44.22           C  
ANISOU 8661  CG  MET C 358     6417   5296   5090    652   -382    402       C  
ATOM   8662  SD  MET C 358     102.357 -25.924-195.797  1.00 46.20           S  
ANISOU 8662  SD  MET C 358     6635   5506   5414    702   -372    371       S  
ATOM   8663  CE  MET C 358     100.799 -25.547-196.597  1.00 41.46           C  
ANISOU 8663  CE  MET C 358     6023   4911   4819    628   -306    363       C  
ATOM   8664  N   SER C 359     101.145 -24.002-191.244  1.00 33.85           N  
ANISOU 8664  N   SER C 359     5139   4090   3633    560   -354    418       N  
ATOM   8665  CA  SER C 359     100.671 -22.779-190.601  1.00 34.72           C  
ANISOU 8665  CA  SER C 359     5227   4261   3707    529   -310    390       C  
ATOM   8666  C   SER C 359      99.785 -21.949-191.515  1.00 35.55           C  
ANISOU 8666  C   SER C 359     5261   4391   3857    508   -239    354       C  
ATOM   8667  O   SER C 359      98.876 -21.265-191.030  1.00 34.26           O  
ANISOU 8667  O   SER C 359     5091   4266   3660    472   -183    342       O  
ATOM   8668  CB  SER C 359     101.842 -21.943-190.105  1.00 40.57           C  
ANISOU 8668  CB  SER C 359     5943   5029   4443    566   -362    360       C  
ATOM   8669  OG  SER C 359     102.846 -21.857-191.083  1.00 39.24           O  
ANISOU 8669  OG  SER C 359     5707   4850   4352    616   -395    336       O  
ATOM   8670  N   THR C 360     100.000 -22.018-192.839  1.00 34.18           N  
ANISOU 8670  N   THR C 360     5038   4195   3755    533   -239    336       N  
ATOM   8671  CA  THR C 360      99.186 -21.199-193.729  1.00 36.56           C  
ANISOU 8671  CA  THR C 360     5281   4516   4096    516   -185    304       C  
ATOM   8672  C   THR C 360      97.742 -21.667-193.779  1.00 32.45           C  
ANISOU 8672  C   THR C 360     4771   3993   3564    463   -138    328       C  
ATOM   8673  O   THR C 360      96.869 -20.871-194.122  1.00 36.19           O  
ANISOU 8673  O   THR C 360     5196   4496   4057    446    -92    303       O  
ATOM   8674  CB  THR C 360      99.759 -21.186-195.150  1.00 35.33           C  
ANISOU 8674  CB  THR C 360     5084   4335   4007    551   -197    281       C  
ATOM   8675  OG1 THR C 360      99.953 -22.537-195.580  1.00 37.25           O  
ANISOU 8675  OG1 THR C 360     5370   4525   4261    564   -225    311       O  
ATOM   8676  CG2 THR C 360     101.086 -20.446-195.182  1.00 33.40           C  
ANISOU 8676  CG2 THR C 360     4801   4108   3783    592   -226    252       C  
ATOM   8677  N   GLU C 361      97.464 -22.931-193.455  1.00 31.93           N  
ANISOU 8677  N   GLU C 361     4766   3892   3473    435   -152    376       N  
ATOM   8678  CA  GLU C 361      96.070 -23.367-193.407  1.00 38.39           C  
ANISOU 8678  CA  GLU C 361     5587   4715   4284    369   -105    403       C  
ATOM   8679  C   GLU C 361      95.293 -22.558-192.387  1.00 35.17           C  
ANISOU 8679  C   GLU C 361     5160   4371   3830    338    -44    395       C  
ATOM   8680  O   GLU C 361      94.152 -22.150-192.646  1.00 35.36           O  
ANISOU 8680  O   GLU C 361     5129   4429   3877    307     11    384       O  
ATOM   8681  CB  GLU C 361      95.971 -24.866-193.080  1.00 36.36           C  
ANISOU 8681  CB  GLU C 361     5415   4403   3998    334   -133    461       C  
ATOM   8682  CG  GLU C 361      96.729 -25.784-194.035  1.00 38.14           C  
ANISOU 8682  CG  GLU C 361     5675   4554   4263    373   -193    466       C  
ATOM   8683  CD  GLU C 361      96.641 -27.253-193.613  1.00 44.46           C  
ANISOU 8683  CD  GLU C 361     6576   5288   5030    341   -228    525       C  
ATOM   8684  OE1 GLU C 361      95.586 -27.867-193.875  1.00 43.63           O  
ANISOU 8684  OE1 GLU C 361     6487   5161   4931    271   -207    553       O  
ATOM   8685  OE2 GLU C 361      97.600 -27.788-193.002  1.00 40.63           O  
ANISOU 8685  OE2 GLU C 361     6155   4769   4513    382   -281    546       O  
ATOM   8686  N   ILE C 362      95.907 -22.306-191.229  1.00 33.33           N  
ANISOU 8686  N   ILE C 362     4974   4158   3533    352    -55    397       N  
ATOM   8687  CA  ILE C 362      95.255 -21.556-190.157  1.00 32.30           C  
ANISOU 8687  CA  ILE C 362     4844   4085   3342    329      7    386       C  
ATOM   8688  C   ILE C 362      95.368 -20.053-190.389  1.00 32.89           C  
ANISOU 8688  C   ILE C 362     4857   4197   3442    371     24    321       C  
ATOM   8689  O   ILE C 362      94.368 -19.328-190.368  1.00 36.47           O  
ANISOU 8689  O   ILE C 362     5262   4691   3902    361     90    296       O  
ATOM   8690  CB  ILE C 362      95.858 -21.940-188.790  1.00 34.73           C  
ANISOU 8690  CB  ILE C 362     5248   4390   3556    324    -20    416       C  
ATOM   8691  CG1 ILE C 362      95.848 -23.444-188.583  1.00 35.22           C  
ANISOU 8691  CG1 ILE C 362     5389   4401   3593    287    -50    484       C  
ATOM   8692  CG2 ILE C 362      95.100 -21.217-187.678  1.00 39.61           C  
ANISOU 8692  CG2 ILE C 362     5882   5069   4101    298     56    402       C  
ATOM   8693  CD1 ILE C 362      96.747 -23.900-187.434  1.00 35.35           C  
ANISOU 8693  CD1 ILE C 362     5510   4396   3526    299   -110    516       C  
ATOM   8694  N   GLY C 363      96.591 -19.551-190.575  1.00 32.13           N  
ANISOU 8694  N   GLY C 363     4762   4086   3361    417    -34    294       N  
ATOM   8695  CA  GLY C 363      96.797 -18.105-190.556  1.00 31.72           C  
ANISOU 8695  CA  GLY C 363     4675   4062   3316    447    -24    237       C  
ATOM   8696  C   GLY C 363      96.342 -17.427-191.836  1.00 32.55           C  
ANISOU 8696  C   GLY C 363     4704   4164   3498    461     -3    205       C  
ATOM   8697  O   GLY C 363      95.877 -16.291-191.819  1.00 39.18           O  
ANISOU 8697  O   GLY C 363     5516   5028   4344    475     30    164       O  
ATOM   8698  N   THR C 364      96.473 -18.103-192.961  1.00 35.46           N  
ANISOU 8698  N   THR C 364     5051   4498   3924    463    -27    222       N  
ATOM   8699  CA  THR C 364      96.044 -17.495-194.216  1.00 32.01           C  
ANISOU 8699  CA  THR C 364     4556   4054   3552    475    -15    195       C  
ATOM   8700  C   THR C 364      94.632 -17.916-194.608  1.00 33.32           C  
ANISOU 8700  C   THR C 364     4690   4228   3741    443     25    212       C  
ATOM   8701  O   THR C 364      93.769 -17.060-194.812  1.00 39.73           O  
ANISOU 8701  O   THR C 364     5456   5066   4575    449     60    184       O  
ATOM   8702  CB  THR C 364      97.030 -17.832-195.339  1.00 34.71           C  
ANISOU 8702  CB  THR C 364     4893   4355   3940    498    -61    196       C  
ATOM   8703  OG1 THR C 364      98.366 -17.499-194.926  1.00 31.41           O  
ANISOU 8703  OG1 THR C 364     4487   3938   3509    523    -99    184       O  
ATOM   8704  CG2 THR C 364      96.675 -17.021-196.586  1.00 34.06           C  
ANISOU 8704  CG2 THR C 364     4766   4264   3910    510    -51    167       C  
ATOM   8705  N   ARG C 365      94.358 -19.218-194.694  1.00 32.94           N  
ANISOU 8705  N   ARG C 365     4668   4158   3692    408     16    256       N  
ATOM   8706  CA  ARG C 365      93.054 -19.635-195.205  1.00 32.35           C  
ANISOU 8706  CA  ARG C 365     4553   4087   3650    367     43    273       C  
ATOM   8707  C   ARG C 365      91.953 -19.499-194.148  1.00 32.15           C  
ANISOU 8707  C   ARG C 365     4507   4118   3592    331    110    282       C  
ATOM   8708  O   ARG C 365      90.961 -18.793-194.358  1.00 35.63           O  
ANISOU 8708  O   ARG C 365     4878   4596   4065    334    149    258       O  
ATOM   8709  CB  ARG C 365      93.132 -21.071-195.740  1.00 32.34           C  
ANISOU 8709  CB  ARG C 365     4595   4033   3661    335      6    315       C  
ATOM   8710  CG  ARG C 365      94.129 -21.291-196.918  1.00 29.26           C  
ANISOU 8710  CG  ARG C 365     4224   3588   3304    376    -49    302       C  
ATOM   8711  CD  ARG C 365      93.927 -20.321-198.109  1.00 31.59           C  
ANISOU 8711  CD  ARG C 365     4469   3886   3648    402    -51    262       C  
ATOM   8712  NE  ARG C 365      92.540 -20.346-198.530  1.00 35.79           N  
ANISOU 8712  NE  ARG C 365     4956   4430   4211    363    -36    268       N  
ATOM   8713  CZ  ARG C 365      92.002 -21.332-199.239  1.00 35.11           C  
ANISOU 8713  CZ  ARG C 365     4885   4308   4148    325    -62    292       C  
ATOM   8714  NH1 ARG C 365      92.748 -22.366-199.611  1.00 34.57           N  
ANISOU 8714  NH1 ARG C 365     4885   4180   4069    328   -100    310       N  
ATOM   8715  NH2 ARG C 365      90.716 -21.295-199.556  1.00 37.96           N  
ANISOU 8715  NH2 ARG C 365     5192   4688   4543    285    -55    297       N  
ATOM   8716  N   ASN C 366      92.107 -20.157-192.990  1.00 34.02           N  
ANISOU 8716  N   ASN C 366     4802   4363   3762    301    126    316       N  
ATOM   8717  CA  ASN C 366      90.985 -20.203-192.055  1.00 32.98           C  
ANISOU 8717  CA  ASN C 366     4651   4286   3595    256    203    332       C  
ATOM   8718  C   ASN C 366      90.716 -18.835-191.438  1.00 35.17           C  
ANISOU 8718  C   ASN C 366     4894   4618   3849    297    257    280       C  
ATOM   8719  O   ASN C 366      89.551 -18.466-191.229  1.00 34.96           O  
ANISOU 8719  O   ASN C 366     4803   4644   3835    284    327    269       O  
ATOM   8720  CB  ASN C 366      91.238 -21.261-190.967  1.00 33.73           C  
ANISOU 8720  CB  ASN C 366     4836   4368   3611    208    207    387       C  
ATOM   8721  CG  ASN C 366      91.462 -22.651-191.549  1.00 37.34           C  
ANISOU 8721  CG  ASN C 366     5340   4759   4089    170    151    437       C  
ATOM   8722  OD1 ASN C 366      91.142 -22.904-192.716  1.00 36.45           O  
ANISOU 8722  OD1 ASN C 366     5185   4619   4047    164    124    434       O  
ATOM   8723  ND2 ASN C 366      92.025 -23.548-190.753  1.00 35.80           N  
ANISOU 8723  ND2 ASN C 366     5243   4532   3830    149    125    483       N  
ATOM   8724  N   LEU C 367      91.769 -18.055-191.161  1.00 33.07           N  
ANISOU 8724  N   LEU C 367     4669   4341   3555    349    224    246       N  
ATOM   8725  CA  LEU C 367      91.574 -16.760-190.519  1.00 35.42           C  
ANISOU 8725  CA  LEU C 367     4956   4679   3824    388    268    193       C  
ATOM   8726  C   LEU C 367      91.427 -15.601-191.502  1.00 38.49           C  
ANISOU 8726  C   LEU C 367     5281   5060   4282    439    256    141       C  
ATOM   8727  O   LEU C 367      90.724 -14.635-191.185  1.00 38.61           O  
ANISOU 8727  O   LEU C 367     5263   5111   4296    470    308    100       O  
ATOM   8728  CB  LEU C 367      92.729 -16.468-189.549  1.00 34.19           C  
ANISOU 8728  CB  LEU C 367     4887   4512   3590    407    235    182       C  
ATOM   8729  CG  LEU C 367      92.741 -17.373-188.309  1.00 40.30           C  
ANISOU 8729  CG  LEU C 367     5741   5300   4272    363    255    228       C  
ATOM   8730  CD1 LEU C 367      93.957 -17.088-187.425  1.00 31.83           C  
ANISOU 8730  CD1 LEU C 367     4757   4212   3126    385    200    217       C  
ATOM   8731  CD2 LEU C 367      91.451 -17.193-187.520  1.00 33.08           C  
ANISOU 8731  CD2 LEU C 367     4808   4447   3314    339    363    224       C  
ATOM   8732  N   CYS C 368      92.023 -15.670-192.701  1.00 35.75           N  
ANISOU 8732  N   CYS C 368     4921   4667   3995    452    192    142       N  
ATOM   8733  CA  CYS C 368      92.014 -14.511-193.604  1.00 30.81           C  
ANISOU 8733  CA  CYS C 368     4256   4026   3423    497    174     97       C  
ATOM   8734  C   CYS C 368      91.157 -14.657-194.853  1.00 33.96           C  
ANISOU 8734  C   CYS C 368     4589   4416   3897    494    165    103       C  
ATOM   8735  O   CYS C 368      90.983 -13.661-195.565  1.00 33.47           O  
ANISOU 8735  O   CYS C 368     4500   4341   3876    533    151     69       O  
ATOM   8736  CB  CYS C 368      93.437 -14.148-194.057  1.00 35.66           C  
ANISOU 8736  CB  CYS C 368     4910   4597   4041    518    110     84       C  
ATOM   8737  SG  CYS C 368      94.498 -13.601-192.692  1.00 42.70           S  
ANISOU 8737  SG  CYS C 368     5872   5498   4855    528     98     63       S  
ATOM   8738  N   ASP C 369      90.627 -15.835-195.149  1.00 35.87           N  
ANISOU 8738  N   ASP C 369     4814   4657   4158    447    165    147       N  
ATOM   8739  CA  ASP C 369      89.749 -15.944-196.311  1.00 36.47           C  
ANISOU 8739  CA  ASP C 369     4828   4724   4303    439    146    150       C  
ATOM   8740  C   ASP C 369      88.545 -15.030-196.122  1.00 41.97           C  
ANISOU 8740  C   ASP C 369     5447   5469   5030    466    193    119       C  
ATOM   8741  O   ASP C 369      88.024 -14.920-195.011  1.00 36.56           O  
ANISOU 8741  O   ASP C 369     4745   4836   4310    462    260    114       O  
ATOM   8742  CB  ASP C 369      89.248 -17.373-196.519  1.00 34.75           C  
ANISOU 8742  CB  ASP C 369     4606   4498   4098    373    139    201       C  
ATOM   8743  CG  ASP C 369      90.168 -18.213-197.395  1.00 35.68           C  
ANISOU 8743  CG  ASP C 369     4785   4551   4222    363     74    223       C  
ATOM   8744  OD1 ASP C 369      91.211 -17.717-197.873  1.00 39.79           O  
ANISOU 8744  OD1 ASP C 369     5339   5039   4739    405     41    200       O  
ATOM   8745  OD2 ASP C 369      89.827 -19.389-197.589  1.00 38.31           O  
ANISOU 8745  OD2 ASP C 369     5131   4863   4560    311     59    262       O  
ATOM   8746  N   PRO C 370      88.069 -14.376-197.184  1.00 36.64           N  
ANISOU 8746  N   PRO C 370     4726   4779   4416    499    160     97       N  
ATOM   8747  CA  PRO C 370      86.903 -13.493-197.038  1.00 33.90           C  
ANISOU 8747  CA  PRO C 370     4298   4476   4107    538    197     65       C  
ATOM   8748  C   PRO C 370      85.644 -14.227-196.626  1.00 33.05           C  
ANISOU 8748  C   PRO C 370     4105   4429   4024    493    248     91       C  
ATOM   8749  O   PRO C 370      84.768 -13.625-195.986  1.00 38.14           O  
ANISOU 8749  O   PRO C 370     4682   5132   4679    523    312     64       O  
ATOM   8750  CB  PRO C 370      86.762 -12.861-198.435  1.00 37.72           C  
ANISOU 8750  CB  PRO C 370     4765   4916   4651    575    128     48       C  
ATOM   8751  CG  PRO C 370      87.492 -13.792-199.349  1.00 41.42           C  
ANISOU 8751  CG  PRO C 370     5288   5332   5118    531     68     83       C  
ATOM   8752  CD  PRO C 370      88.594 -14.408-198.563  1.00 36.53           C  
ANISOU 8752  CD  PRO C 370     4739   4704   4435    505     86    100       C  
ATOM   8753  N   HIS C 371      85.527 -15.507-196.969  1.00 34.37           N  
ANISOU 8753  N   HIS C 371     4274   4585   4202    419    224    140       N  
ATOM   8754  CA  HIS C 371      84.374 -16.320-196.611  1.00 35.00           C  
ANISOU 8754  CA  HIS C 371     4275   4717   4306    354    269    173       C  
ATOM   8755  C   HIS C 371      84.632 -17.194-195.389  1.00 38.25           C  
ANISOU 8755  C   HIS C 371     4738   5151   4645    294    330    210       C  
ATOM   8756  O   HIS C 371      83.835 -18.094-195.110  1.00 41.32           O  
ANISOU 8756  O   HIS C 371     5084   5572   5045    217    363    251       O  
ATOM   8757  CB  HIS C 371      83.950 -17.193-197.793  1.00 37.77           C  
ANISOU 8757  CB  HIS C 371     4602   5034   4717    299    195    206       C  
ATOM   8758  CG  HIS C 371      85.054 -18.041-198.349  1.00 42.69           C  
ANISOU 8758  CG  HIS C 371     5334   5578   5307    271    131    232       C  
ATOM   8759  ND1 HIS C 371      86.149 -17.510-199.003  1.00 43.03           N  
ANISOU 8759  ND1 HIS C 371     5450   5566   5335    327     81    207       N  
ATOM   8760  CD2 HIS C 371      85.218 -19.384-198.374  1.00 43.77           C  
ANISOU 8760  CD2 HIS C 371     5521   5682   5426    196    111    279       C  
ATOM   8761  CE1 HIS C 371      86.943 -18.491-199.398  1.00 41.11           C  
ANISOU 8761  CE1 HIS C 371     5287   5265   5067    294     39    235       C  
ATOM   8762  NE2 HIS C 371      86.403 -19.637-199.025  1.00 41.40           N  
ANISOU 8762  NE2 HIS C 371     5319   5310   5102    219     52    278       N  
ATOM   8763  N   ARG C 372      85.734 -16.966-194.670  1.00 33.77           N  
ANISOU 8763  N   ARG C 372     4266   4563   4001    320    339    200       N  
ATOM   8764  CA  ARG C 372      85.928 -17.625-193.385  1.00 34.05           C  
ANISOU 8764  CA  ARG C 372     4357   4623   3956    274    397    231       C  
ATOM   8765  C   ARG C 372      85.917 -16.539-192.302  1.00 36.63           C  
ANISOU 8765  C   ARG C 372     4690   4998   4228    330    469    186       C  
ATOM   8766  O   ARG C 372      85.052 -15.651-192.332  1.00 40.90           O  
ANISOU 8766  O   ARG C 372     5146   5585   4809    375    514    145       O  
ATOM   8767  CB  ARG C 372      87.219 -18.430-193.378  1.00 35.54           C  
ANISOU 8767  CB  ARG C 372     4661   4746   4096    255    336    263       C  
ATOM   8768  CG  ARG C 372      87.277 -19.512-194.476  1.00 38.03           C  
ANISOU 8768  CG  ARG C 372     4987   5004   4459    208    265    301       C  
ATOM   8769  CD  ARG C 372      86.297 -20.667-194.203  1.00 38.61           C  
ANISOU 8769  CD  ARG C 372     5036   5096   4540    113    296    356       C  
ATOM   8770  NE  ARG C 372      86.594 -21.383-192.958  1.00 39.10           N  
ANISOU 8770  NE  ARG C 372     5176   5164   4517     67    338    397       N  
ATOM   8771  CZ  ARG C 372      87.574 -22.270-192.831  1.00 40.20           C  
ANISOU 8771  CZ  ARG C 372     5425   5239   4612     52    286    431       C  
ATOM   8772  NH1 ARG C 372      88.364 -22.551-193.860  1.00 35.80           N  
ANISOU 8772  NH1 ARG C 372     4904   4611   4086     82    202    425       N  
ATOM   8773  NH2 ARG C 372      87.775 -22.870-191.670  1.00 42.22           N  
ANISOU 8773  NH2 ARG C 372     5757   5498   4786     12    319    471       N  
ATOM   8774  N   TYR C 373      86.876 -16.567-191.361  1.00 39.86           N  
ANISOU 8774  N   TYR C 373     5202   5394   4548    334    475    188       N  
ATOM   8775  CA  TYR C 373      86.849 -15.581-190.280  1.00 37.90           C  
ANISOU 8775  CA  TYR C 373     4976   5187   4236    382    541    142       C  
ATOM   8776  C   TYR C 373      87.103 -14.164-190.783  1.00 41.29           C  
ANISOU 8776  C   TYR C 373     5390   5598   4701    470    511     75       C  
ATOM   8777  O   TYR C 373      86.611 -13.214-190.168  1.00 42.84           O  
ANISOU 8777  O   TYR C 373     5569   5833   4877    521    574     26       O  
ATOM   8778  CB  TYR C 373      87.841 -15.968-189.183  1.00 35.68           C  
ANISOU 8778  CB  TYR C 373     4819   4891   3848    362    537    161       C  
ATOM   8779  CG  TYR C 373      87.245 -17.005-188.258  1.00 39.54           C  
ANISOU 8779  CG  TYR C 373     5328   5419   4276    285    608    216       C  
ATOM   8780  CD1 TYR C 373      87.272 -18.356-188.584  1.00 37.02           C  
ANISOU 8780  CD1 TYR C 373     5027   5070   3971    209    573    284       C  
ATOM   8781  CD2 TYR C 373      86.593 -16.622-187.090  1.00 48.15           C  
ANISOU 8781  CD2 TYR C 373     6423   6576   5295    286    715    198       C  
ATOM   8782  CE1 TYR C 373      86.692 -19.309-187.743  1.00 39.46           C  
ANISOU 8782  CE1 TYR C 373     5361   5409   4223    128    639    340       C  
ATOM   8783  CE2 TYR C 373      86.014 -17.562-186.245  1.00 44.27           C  
ANISOU 8783  CE2 TYR C 373     5954   6124   4744    206    791    253       C  
ATOM   8784  CZ  TYR C 373      86.068 -18.903-186.576  1.00 40.89           C  
ANISOU 8784  CZ  TYR C 373     5546   5661   4330    123    750    326       C  
ATOM   8785  OH  TYR C 373      85.495 -19.841-185.753  1.00 42.59           O  
ANISOU 8785  OH  TYR C 373     5792   5908   4484     33    823    386       O  
ATOM   8786  N   ASN C 374      87.867 -13.995-191.873  1.00 36.01           N  
ANISOU 8786  N   ASN C 374     4736   4867   4080    490    421     71       N  
ATOM   8787  CA  ASN C 374      87.954 -12.713-192.584  1.00 34.00           C  
ANISOU 8787  CA  ASN C 374     4460   4586   3872    561    387     17       C  
ATOM   8788  C   ASN C 374      88.486 -11.605-191.667  1.00 37.26           C  
ANISOU 8788  C   ASN C 374     4939   4998   4221    612    408    -36       C  
ATOM   8789  O   ASN C 374      87.930 -10.508-191.588  1.00 38.17           O  
ANISOU 8789  O   ASN C 374     5027   5124   4351    674    438    -88       O  
ATOM   8790  CB  ASN C 374      86.583 -12.335-193.168  1.00 35.73           C  
ANISOU 8790  CB  ASN C 374     4567   4840   4170    588    416      0       C  
ATOM   8791  CG  ASN C 374      86.641 -11.128-194.076  1.00 39.92           C  
ANISOU 8791  CG  ASN C 374     5086   5330   4754    659    365    -45       C  
ATOM   8792  OD1 ASN C 374      87.682 -10.826-194.653  1.00 36.91           O  
ANISOU 8792  OD1 ASN C 374     4768   4888   4369    667    298    -50       O  
ATOM   8793  ND2 ASN C 374      85.514 -10.425-194.209  1.00 40.20           N  
ANISOU 8793  ND2 ASN C 374     5037   5397   4840    712    398    -78       N  
ATOM   8794  N   ILE C 375      89.570 -11.908-190.944  1.00 39.66           N  
ANISOU 8794  N   ILE C 375     5334   5284   4451    588    385    -23       N  
ATOM   8795  CA  ILE C 375      90.060 -10.988-189.915  1.00 40.69           C  
ANISOU 8795  CA  ILE C 375     5539   5415   4506    623    401    -70       C  
ATOM   8796  C   ILE C 375      91.137 -10.052-190.428  1.00 39.66           C  
ANISOU 8796  C   ILE C 375     5453   5225   4392    653    323   -103       C  
ATOM   8797  O   ILE C 375      91.726  -9.314-189.633  1.00 32.66           O  
ANISOU 8797  O   ILE C 375     4639   4327   3444    671    315   -140       O  
ATOM   8798  CB  ILE C 375      90.662 -11.731-188.708  1.00 36.99           C  
ANISOU 8798  CB  ILE C 375     5155   4961   3939    579    410    -40       C  
ATOM   8799  CG1 ILE C 375      91.980 -12.372-189.130  1.00 36.22           C  
ANISOU 8799  CG1 ILE C 375     5100   4815   3847    549    316     -4       C  
ATOM   8800  CG2 ILE C 375      89.711 -12.769-188.169  1.00 46.03           C  
ANISOU 8800  CG2 ILE C 375     6272   6159   5057    531    487      4       C  
ATOM   8801  CD1 ILE C 375      92.706 -12.992-187.977  1.00 42.38           C  
ANISOU 8801  CD1 ILE C 375     5971   5599   4533    517    301     23       C  
ATOM   8802  N   LEU C 376      91.446 -10.082-191.727  1.00 32.37           N  
ANISOU 8802  N   LEU C 376     4494   4261   3543    651    264    -89       N  
ATOM   8803  CA  LEU C 376      92.617  -9.371-192.219  1.00 30.69           C  
ANISOU 8803  CA  LEU C 376     4325   3995   3341    661    193   -108       C  
ATOM   8804  C   LEU C 376      92.546  -7.885-191.885  1.00 33.32           C  
ANISOU 8804  C   LEU C 376     4693   4307   3658    711    199   -172       C  
ATOM   8805  O   LEU C 376      93.524  -7.291-191.412  1.00 34.35           O  
ANISOU 8805  O   LEU C 376     4893   4410   3749    706    161   -195       O  
ATOM   8806  CB  LEU C 376      92.729  -9.570-193.735  1.00 35.97           C  
ANISOU 8806  CB  LEU C 376     4950   4628   4088    654    148    -86       C  
ATOM   8807  CG  LEU C 376      94.045  -9.387-194.472  1.00 47.01           C  
ANISOU 8807  CG  LEU C 376     6378   5979   5505    640     81    -80       C  
ATOM   8808  CD1 LEU C 376      95.135 -10.248-193.867  1.00 41.25           C  
ANISOU 8808  CD1 LEU C 376     5682   5256   4735    604     56    -51       C  
ATOM   8809  CD2 LEU C 376      93.815  -9.754-195.947  1.00 38.81           C  
ANISOU 8809  CD2 LEU C 376     5298   4915   4532    635     58    -55       C  
ATOM   8810  N   GLU C 377      91.397  -7.259-192.153  1.00 32.87           N  
ANISOU 8810  N   GLU C 377     4591   4260   3638    760    239   -201       N  
ATOM   8811  CA  GLU C 377      91.311  -5.824-191.950  1.00 38.03           C  
ANISOU 8811  CA  GLU C 377     5287   4880   4283    817    237   -264       C  
ATOM   8812  C   GLU C 377      91.349  -5.461-190.476  1.00 34.35           C  
ANISOU 8812  C   GLU C 377     4889   4437   3726    832    282   -303       C  
ATOM   8813  O   GLU C 377      91.869  -4.396-190.122  1.00 33.10           O  
ANISOU 8813  O   GLU C 377     4807   4234   3535    856    254   -351       O  
ATOM   8814  CB  GLU C 377      90.051  -5.260-192.592  1.00 41.75           C  
ANISOU 8814  CB  GLU C 377     5690   5354   4820    880    264   -288       C  
ATOM   8815  CG  GLU C 377      90.308  -3.887-193.169  1.00 63.85           C  
ANISOU 8815  CG  GLU C 377     8535   8079   7644    927    213   -331       C  
ATOM   8816  CD  GLU C 377      89.050  -3.164-193.570  1.00 80.44           C  
ANISOU 8816  CD  GLU C 377    10583  10179   9800   1008    236   -365       C  
ATOM   8817  OE1 GLU C 377      88.954  -1.952-193.289  1.00 88.48           O  
ANISOU 8817  OE1 GLU C 377    11658  11155  10807   1071    232   -422       O  
ATOM   8818  OE2 GLU C 377      88.164  -3.798-194.180  1.00 85.91           O  
ANISOU 8818  OE2 GLU C 377    11181  10909  10552   1011    249   -335       O  
ATOM   8819  N   ASP C 378      90.787  -6.320-189.620  1.00 32.07           N  
ANISOU 8819  N   ASP C 378     4583   4213   3391    815    351   -283       N  
ATOM   8820  CA  ASP C 378      90.889  -6.126-188.170  1.00 37.23           C  
ANISOU 8820  CA  ASP C 378     5317   4890   3939    820    396   -314       C  
ATOM   8821  C   ASP C 378      92.341  -6.018-187.729  1.00 38.08           C  
ANISOU 8821  C   ASP C 378     5522   4956   3989    781    317   -313       C  
ATOM   8822  O   ASP C 378      92.721  -5.073-187.021  1.00 38.96           O  
ANISOU 8822  O   ASP C 378     5721   5041   4042    804    303   -366       O  
ATOM   8823  CB  ASP C 378      90.193  -7.275-187.443  1.00 39.22           C  
ANISOU 8823  CB  ASP C 378     5539   5216   4148    785    477   -274       C  
ATOM   8824  CG  ASP C 378      88.692  -7.283-187.680  1.00 51.96           C  
ANISOU 8824  CG  ASP C 378     7047   6882   5814    822    566   -282       C  
ATOM   8825  OD1 ASP C 378      88.062  -6.217-187.544  1.00 51.32           O  
ANISOU 8825  OD1 ASP C 378     6957   6801   5741    898    606   -345       O  
ATOM   8826  OD2 ASP C 378      88.147  -8.349-188.015  1.00 53.81           O  
ANISOU 8826  OD2 ASP C 378     7205   7156   6086    777    591   -227       O  
ATOM   8827  N   VAL C 379      93.170  -6.974-188.155  1.00 35.93           N  
ANISOU 8827  N   VAL C 379     5236   4679   3738    723    259   -254       N  
ATOM   8828  CA  VAL C 379      94.586  -6.961-187.793  1.00 38.19           C  
ANISOU 8828  CA  VAL C 379     5593   4933   3984    687    176   -249       C  
ATOM   8829  C   VAL C 379      95.282  -5.730-188.364  1.00 37.53           C  
ANISOU 8829  C   VAL C 379     5534   4788   3938    700    112   -290       C  
ATOM   8830  O   VAL C 379      96.083  -5.081-187.677  1.00 34.40           O  
ANISOU 8830  O   VAL C 379     5217   4364   3488    689     65   -322       O  
ATOM   8831  CB  VAL C 379      95.260  -8.267-188.254  1.00 38.25           C  
ANISOU 8831  CB  VAL C 379     5565   4947   4021    637    133   -179       C  
ATOM   8832  CG1 VAL C 379      96.764  -8.232-187.991  1.00 33.85           C  
ANISOU 8832  CG1 VAL C 379     5058   4362   3442    606     40   -174       C  
ATOM   8833  CG2 VAL C 379      94.624  -9.454-187.571  1.00 39.52           C  
ANISOU 8833  CG2 VAL C 379     5725   5157   4134    615    189   -136       C  
ATOM   8834  N   ALA C 380      94.976  -5.363-189.621  1.00 35.12           N  
ANISOU 8834  N   ALA C 380     5169   4456   3721    718    105   -289       N  
ATOM   8835  CA  ALA C 380      95.663  -4.225-190.223  1.00 32.18           C  
ANISOU 8835  CA  ALA C 380     4827   4018   3381    720     45   -319       C  
ATOM   8836  C   ALA C 380      95.320  -2.908-189.521  1.00 37.00           C  
ANISOU 8836  C   ALA C 380     5515   4596   3946    765     57   -390       C  
ATOM   8837  O   ALA C 380      96.181  -2.032-189.378  1.00 37.67           O  
ANISOU 8837  O   ALA C 380     5669   4628   4015    746     -3   -420       O  
ATOM   8838  CB  ALA C 380      95.341  -4.137-191.727  1.00 30.67           C  
ANISOU 8838  CB  ALA C 380     4570   3802   3282    729     36   -299       C  
ATOM   8839  N   VAL C 381      94.068  -2.743-189.086  1.00 34.40           N  
ANISOU 8839  N   VAL C 381     5177   4296   3599    825    136   -421       N  
ATOM   8840  CA  VAL C 381      93.696  -1.571-188.291  1.00 36.78           C  
ANISOU 8840  CA  VAL C 381     5560   4568   3845    881    159   -495       C  
ATOM   8841  C   VAL C 381      94.480  -1.532-186.976  1.00 41.87           C  
ANISOU 8841  C   VAL C 381     6308   5215   4385    849    137   -517       C  
ATOM   8842  O   VAL C 381      94.911  -0.461-186.526  1.00 40.16           O  
ANISOU 8842  O   VAL C 381     6189   4942   4127    859     97   -572       O  
ATOM   8843  CB  VAL C 381      92.172  -1.560-188.042  1.00 40.49           C  
ANISOU 8843  CB  VAL C 381     5979   5085   4318    957    261   -521       C  
ATOM   8844  CG1 VAL C 381      91.802  -0.569-186.941  1.00 47.51           C  
ANISOU 8844  CG1 VAL C 381     6964   5960   5128   1020    304   -601       C  
ATOM   8845  CG2 VAL C 381      91.423  -1.238-189.347  1.00 38.04           C  
ANISOU 8845  CG2 VAL C 381     5585   4754   4115   1002    258   -515       C  
ATOM   8846  N   CYS C 382      94.668  -2.688-186.333  1.00 41.80           N  
ANISOU 8846  N   CYS C 382     6291   5266   4327    808    154   -473       N  
ATOM   8847  CA  CYS C 382      95.442  -2.702-185.092  1.00 44.08           C  
ANISOU 8847  CA  CYS C 382     6684   5554   4509    776    120   -489       C  
ATOM   8848  C   CYS C 382      96.911  -2.401-185.343  1.00 42.58           C  
ANISOU 8848  C   CYS C 382     6527   5313   4337    717      0   -480       C  
ATOM   8849  O   CYS C 382      97.583  -1.837-184.472  1.00 42.24           O  
ANISOU 8849  O   CYS C 382     6586   5242   4221    699    -53   -517       O  
ATOM   8850  CB  CYS C 382      95.307  -4.044-184.377  1.00 40.96           C  
ANISOU 8850  CB  CYS C 382     6280   5228   4055    744    159   -436       C  
ATOM   8851  SG  CYS C 382      93.656  -4.460-183.798  1.00 44.49           S  
ANISOU 8851  SG  CYS C 382     6697   5748   4461    792    310   -444       S  
ATOM   8852  N   MET C 383      97.426  -2.767-186.517  1.00 37.23           N  
ANISOU 8852  N   MET C 383     5765   4626   3756    685    -42   -432       N  
ATOM   8853  CA  MET C 383      98.788  -2.422-186.909  1.00 34.96           C  
ANISOU 8853  CA  MET C 383     5486   4297   3502    628   -144   -423       C  
ATOM   8854  C   MET C 383      98.905  -0.996-187.430  1.00 40.87           C  
ANISOU 8854  C   MET C 383     6274   4970   4284    636   -175   -472       C  
ATOM   8855  O   MET C 383      99.997  -0.602-187.856  1.00 43.34           O  
ANISOU 8855  O   MET C 383     6587   5246   4633    581   -253   -464       O  
ATOM   8856  CB  MET C 383      99.300  -3.389-187.988  1.00 36.65           C  
ANISOU 8856  CB  MET C 383     5595   4531   3801    594   -164   -356       C  
ATOM   8857  CG  MET C 383      99.419  -4.831-187.534  1.00 41.60           C  
ANISOU 8857  CG  MET C 383     6192   5214   4399    578   -156   -303       C  
ATOM   8858  SD  MET C 383      99.763  -5.969-188.900  1.00 43.23           S  
ANISOU 8858  SD  MET C 383     6283   5436   4704    559   -162   -233       S  
ATOM   8859  CE  MET C 383     101.412  -5.455-189.386  1.00 37.73           C  
ANISOU 8859  CE  MET C 383     5572   4708   4057    507   -260   -232       C  
ATOM   8860  N   ASP C 384      97.815  -0.226-187.420  1.00 41.36           N  
ANISOU 8860  N   ASP C 384     6367   5009   4339    704   -117   -520       N  
ATOM   8861  CA  ASP C 384      97.808   1.157-187.914  1.00 44.23           C  
ANISOU 8861  CA  ASP C 384     6783   5289   4732    722   -147   -567       C  
ATOM   8862  C   ASP C 384      98.308   1.256-189.359  1.00 48.41           C  
ANISOU 8862  C   ASP C 384     7248   5786   5360    683   -188   -525       C  
ATOM   8863  O   ASP C 384      99.052   2.169-189.719  1.00 51.87           O  
ANISOU 8863  O   ASP C 384     7735   6156   5819    643   -252   -539       O  
ATOM   8864  CB  ASP C 384      98.619   2.078-186.997  1.00 48.46           C  
ANISOU 8864  CB  ASP C 384     7443   5770   5198    690   -217   -619       C  
ATOM   8865  CG  ASP C 384      98.131   2.046-185.555  1.00 67.42           C  
ANISOU 8865  CG  ASP C 384     9931   8200   7487    730   -175   -666       C  
ATOM   8866  OD1 ASP C 384      98.907   1.634-184.666  1.00 74.73           O  
ANISOU 8866  OD1 ASP C 384    10902   9148   8346    680   -223   -659       O  
ATOM   8867  OD2 ASP C 384      96.964   2.420-185.315  1.00 77.91           O  
ANISOU 8867  OD2 ASP C 384    11281   9529   8792    814    -94   -710       O  
ATOM   8868  N   LEU C 385      97.892   0.321-190.201  1.00 44.65           N  
ANISOU 8868  N   LEU C 385     6670   5355   4941    691   -149   -472       N  
ATOM   8869  CA  LEU C 385      98.267   0.351-191.609  1.00 41.35           C  
ANISOU 8869  CA  LEU C 385     6197   4909   4605    660   -176   -433       C  
ATOM   8870  C   LEU C 385      97.306   1.234-192.400  1.00 48.53           C  
ANISOU 8870  C   LEU C 385     7120   5765   5554    721   -157   -457       C  
ATOM   8871  O   LEU C 385      96.168   1.468-191.999  1.00 47.99           O  
ANISOU 8871  O   LEU C 385     7061   5704   5469    797   -106   -493       O  
ATOM   8872  CB  LEU C 385      98.283  -1.066-192.199  1.00 38.72           C  
ANISOU 8872  CB  LEU C 385     5763   4640   4310    643   -151   -369       C  
ATOM   8873  CG  LEU C 385      99.177  -2.086-191.485  1.00 41.82           C  
ANISOU 8873  CG  LEU C 385     6136   5085   4670    596   -174   -338       C  
ATOM   8874  CD1 LEU C 385      99.055  -3.488-192.097  1.00 38.19           C  
ANISOU 8874  CD1 LEU C 385     5588   4675   4246    590   -147   -279       C  
ATOM   8875  CD2 LEU C 385     100.618  -1.621-191.470  1.00 42.35           C  
ANISOU 8875  CD2 LEU C 385     6227   5123   4744    528   -251   -338       C  
ATOM   8876  N   ASP C 386      97.776   1.711-193.550  1.00 56.22           N  
ANISOU 8876  N   ASP C 386     8094   6686   6582    687   -196   -435       N  
ATOM   8877  CA  ASP C 386      96.950   2.520-194.448  1.00 51.77           C  
ANISOU 8877  CA  ASP C 386     7549   6062   6060    740   -193   -448       C  
ATOM   8878  C   ASP C 386      96.091   1.588-195.294  1.00 48.58           C  
ANISOU 8878  C   ASP C 386     7049   5707   5702    774   -153   -406       C  
ATOM   8879  O   ASP C 386      96.549   1.047-196.303  1.00 54.50           O  
ANISOU 8879  O   ASP C 386     7755   6464   6491    728   -167   -356       O  
ATOM   8880  CB  ASP C 386      97.825   3.410-195.324  1.00 65.86           C  
ANISOU 8880  CB  ASP C 386     9387   7764   7871    680   -253   -435       C  
ATOM   8881  CG  ASP C 386      97.016   4.291-196.269  1.00 70.36           C  
ANISOU 8881  CG  ASP C 386     9996   8259   8476    734   -263   -444       C  
ATOM   8882  OD1 ASP C 386      95.773   4.349-196.136  1.00 70.55           O  
ANISOU 8882  OD1 ASP C 386    10005   8293   8508    829   -230   -470       O  
ATOM   8883  OD2 ASP C 386      97.634   4.921-197.154  1.00 76.81           O  
ANISOU 8883  OD2 ASP C 386    10858   9010   9316    681   -305   -422       O  
ATOM   8884  N   THR C 387      94.827   1.420-194.916  1.00 43.18           N  
ANISOU 8884  N   THR C 387     6332   5058   5017    853   -103   -429       N  
ATOM   8885  CA  THR C 387      93.966   0.475-195.612  1.00 41.42           C  
ANISOU 8885  CA  THR C 387     6012   4886   4839    877    -70   -391       C  
ATOM   8886  C   THR C 387      93.134   1.119-196.713  1.00 52.20           C  
ANISOU 8886  C   THR C 387     7373   6201   6261    932    -90   -393       C  
ATOM   8887  O   THR C 387      92.292   0.437-197.307  1.00 58.10           O  
ANISOU 8887  O   THR C 387     8040   6986   7048    957    -73   -367       O  
ATOM   8888  CB  THR C 387      93.031  -0.224-194.628  1.00 45.96           C  
ANISOU 8888  CB  THR C 387     6533   5540   5389    919      0   -405       C  
ATOM   8889  OG1 THR C 387      92.022   0.700-194.209  1.00 50.08           O  
ANISOU 8889  OG1 THR C 387     7077   6043   5908   1009     28   -463       O  
ATOM   8890  CG2 THR C 387      93.810  -0.730-193.409  1.00 46.36           C  
ANISOU 8890  CG2 THR C 387     6615   5631   5370    873     13   -407       C  
ATOM   8891  N   ARG C 388      93.333   2.404-196.998  1.00 40.56           N  
ANISOU 8891  N   ARG C 388     5986   4637   4788    949   -134   -422       N  
ATOM   8892  CA  ARG C 388      92.546   3.047-198.044  1.00 53.08           C  
ANISOU 8892  CA  ARG C 388     7579   6166   6422   1007   -166   -421       C  
ATOM   8893  C   ARG C 388      93.218   3.007-199.414  1.00 54.95           C  
ANISOU 8893  C   ARG C 388     7836   6358   6684    943   -215   -367       C  
ATOM   8894  O   ARG C 388      92.606   3.441-200.394  1.00 49.81           O  
ANISOU 8894  O   ARG C 388     7198   5658   6068    983   -249   -357       O  
ATOM   8895  CB  ARG C 388      92.200   4.489-197.657  1.00 65.57           C  
ANISOU 8895  CB  ARG C 388     9257   7664   7993   1078   -188   -482       C  
ATOM   8896  CG  ARG C 388      90.924   4.558-196.802  1.00 76.05           C  
ANISOU 8896  CG  ARG C 388    10538   9035   9322   1187   -132   -535       C  
ATOM   8897  CD  ARG C 388      90.364   5.966-196.603  1.00 77.18           C  
ANISOU 8897  CD  ARG C 388    10768   9091   9467   1286   -154   -599       C  
ATOM   8898  NE  ARG C 388      90.752   6.518-195.305  1.00 81.09           N  
ANISOU 8898  NE  ARG C 388    11348   9570   9894   1294   -131   -660       N  
ATOM   8899  CZ  ARG C 388      90.027   7.382-194.598  1.00 77.45           C  
ANISOU 8899  CZ  ARG C 388    10936   9076   9417   1400   -108   -733       C  
ATOM   8900  NH1 ARG C 388      88.850   7.801-195.048  1.00 87.49           N  
ANISOU 8900  NH1 ARG C 388    12167  10331  10744   1515   -104   -755       N  
ATOM   8901  NH2 ARG C 388      90.478   7.820-193.430  1.00 66.13           N  
ANISOU 8901  NH2 ARG C 388     9593   7624   7909   1395    -90   -787       N  
ATOM   8902  N   THR C 389      94.436   2.478-199.518  1.00 45.72           N  
ANISOU 8902  N   THR C 389     6667   5206   5497    848   -217   -333       N  
ATOM   8903  CA  THR C 389      95.024   2.175-200.816  1.00 47.80           C  
ANISOU 8903  CA  THR C 389     6930   5450   5780    788   -241   -279       C  
ATOM   8904  C   THR C 389      95.586   0.757-200.821  1.00 39.35           C  
ANISOU 8904  C   THR C 389     5781   4462   4708    734   -209   -240       C  
ATOM   8905  O   THR C 389      96.228   0.328-199.856  1.00 44.15           O  
ANISOU 8905  O   THR C 389     6370   5114   5290    702   -190   -248       O  
ATOM   8906  CB  THR C 389      96.119   3.183-201.194  1.00 56.89           C  
ANISOU 8906  CB  THR C 389     8176   6521   6917    721   -281   -275       C  
ATOM   8907  OG1 THR C 389      96.675   2.828-202.467  1.00 63.45           O  
ANISOU 8907  OG1 THR C 389     9004   7343   7761    662   -288   -222       O  
ATOM   8908  CG2 THR C 389      97.223   3.224-200.156  1.00 59.02           C  
ANISOU 8908  CG2 THR C 389     8458   6812   7157    659   -276   -292       C  
ATOM   8909  N   THR C 390      95.348   0.026-201.916  1.00 34.10           N  
ANISOU 8909  N   THR C 390     5078   3810   4067    726   -210   -199       N  
ATOM   8910  CA  THR C 390      95.901  -1.324-202.007  1.00 34.17           C  
ANISOU 8910  CA  THR C 390     5024   3885   4075    680   -183   -164       C  
ATOM   8911  C   THR C 390      97.420  -1.303-202.131  1.00 30.88           C  
ANISOU 8911  C   THR C 390     4628   3462   3643    603   -185   -147       C  
ATOM   8912  O   THR C 390      98.083  -2.278-201.753  1.00 35.08           O  
ANISOU 8912  O   THR C 390     5111   4049   4170    572   -165   -131       O  
ATOM   8913  CB  THR C 390      95.310  -2.071-203.206  1.00 44.04           C  
ANISOU 8913  CB  THR C 390     6245   5141   5349    689   -188   -129       C  
ATOM   8914  OG1 THR C 390      95.496  -1.275-204.382  1.00 43.74           O  
ANISOU 8914  OG1 THR C 390     6275   5032   5313    675   -223   -115       O  
ATOM   8915  CG2 THR C 390      93.836  -2.325-202.995  1.00 53.18           C  
ANISOU 8915  CG2 THR C 390     7352   6324   6530    756   -186   -142       C  
ATOM   8916  N   SER C 391      97.988  -0.215-202.661  1.00 31.74           N  
ANISOU 8916  N   SER C 391     4806   3504   3749    569   -211   -148       N  
ATOM   8917  CA  SER C 391      99.414  -0.220-202.957  1.00 33.88           C  
ANISOU 8917  CA  SER C 391     5081   3776   4016    487   -207   -125       C  
ATOM   8918  C   SER C 391     100.284  -0.081-201.716  1.00 35.60           C  
ANISOU 8918  C   SER C 391     5286   4018   4220    452   -213   -148       C  
ATOM   8919  O   SER C 391     101.508  -0.218-201.832  1.00 36.26           O  
ANISOU 8919  O   SER C 391     5348   4119   4310    384   -211   -130       O  
ATOM   8920  CB  SER C 391      99.751   0.871-203.986  1.00 34.46           C  
ANISOU 8920  CB  SER C 391     5236   3769   4088    447   -229   -111       C  
ATOM   8921  OG  SER C 391      99.272   2.152-203.608  1.00 41.67           O  
ANISOU 8921  OG  SER C 391     6229   4611   4995    473   -266   -144       O  
ATOM   8922  N   SER C 392      99.695   0.145-200.532  1.00 37.04           N  
ANISOU 8922  N   SER C 392     5480   4209   4384    497   -220   -187       N  
ATOM   8923  CA  SER C 392     100.480   0.051-199.301  1.00 44.07           C  
ANISOU 8923  CA  SER C 392     6360   5133   5252    467   -230   -207       C  
ATOM   8924  C   SER C 392     100.797  -1.386-198.926  1.00 39.05           C  
ANISOU 8924  C   SER C 392     5643   4578   4616    464   -208   -182       C  
ATOM   8925  O   SER C 392     101.591  -1.610-197.995  1.00 36.29           O  
ANISOU 8925  O   SER C 392     5280   4261   4249    435   -225   -190       O  
ATOM   8926  CB  SER C 392      99.741   0.710-198.134  1.00 32.99           C  
ANISOU 8926  CB  SER C 392     5008   3712   3815    518   -238   -259       C  
ATOM   8927  OG  SER C 392      98.594  -0.059-197.788  1.00 38.92           O  
ANISOU 8927  OG  SER C 392     5716   4511   4560    587   -200   -263       O  
ATOM   8928  N   LEU C 393     100.171  -2.349-199.606  1.00 32.96           N  
ANISOU 8928  N   LEU C 393     4827   3836   3862    495   -178   -155       N  
ATOM   8929  CA  LEU C 393     100.328  -3.776-199.314  1.00 30.71           C  
ANISOU 8929  CA  LEU C 393     4477   3615   3575    499   -158   -130       C  
ATOM   8930  C   LEU C 393      99.976  -4.078-197.858  1.00 32.99           C  
ANISOU 8930  C   LEU C 393     4767   3941   3827    524   -155   -152       C  
ATOM   8931  O   LEU C 393     100.590  -4.935-197.215  1.00 30.65           O  
ANISOU 8931  O   LEU C 393     4441   3687   3517    509   -161   -137       O  
ATOM   8932  CB  LEU C 393     101.740  -4.264-199.656  1.00 32.99           C  
ANISOU 8932  CB  LEU C 393     4728   3926   3882    447   -165   -104       C  
ATOM   8933  CG  LEU C 393     102.119  -4.004-201.135  1.00 37.16           C  
ANISOU 8933  CG  LEU C 393     5261   4423   4437    418   -152    -81       C  
ATOM   8934  CD1 LEU C 393     103.387  -4.752-201.486  1.00 35.43           C  
ANISOU 8934  CD1 LEU C 393     4983   4241   4237    382   -140    -56       C  
ATOM   8935  CD2 LEU C 393     100.983  -4.382-202.070  1.00 33.52           C  
ANISOU 8935  CD2 LEU C 393     4810   3946   3981    459   -133    -68       C  
ATOM   8936  N   TRP C 394      98.944  -3.393-197.351  1.00 31.16           N  
ANISOU 8936  N   TRP C 394     4571   3692   3576    568   -145   -186       N  
ATOM   8937  CA  TRP C 394      98.490  -3.632-195.986  1.00 34.35           C  
ANISOU 8937  CA  TRP C 394     4984   4132   3934    594   -128   -209       C  
ATOM   8938  C   TRP C 394      97.941  -5.042-195.807  1.00 33.80           C  
ANISOU 8938  C   TRP C 394     4860   4120   3861    608    -94   -177       C  
ATOM   8939  O   TRP C 394      98.118  -5.637-194.736  1.00 33.65           O  
ANISOU 8939  O   TRP C 394     4846   4139   3801    601    -88   -174       O  
ATOM   8940  CB  TRP C 394      97.440  -2.590-195.580  1.00 34.74           C  
ANISOU 8940  CB  TRP C 394     5079   4153   3968    648   -113   -256       C  
ATOM   8941  CG  TRP C 394      96.157  -2.586-196.410  1.00 32.47           C  
ANISOU 8941  CG  TRP C 394     4759   3859   3719    700    -85   -252       C  
ATOM   8942  CD1 TRP C 394      95.886  -1.812-197.510  1.00 35.47           C  
ANISOU 8942  CD1 TRP C 394     5158   4182   4138    716   -108   -254       C  
ATOM   8943  CD2 TRP C 394      94.968  -3.343-196.151  1.00 34.69           C  
ANISOU 8943  CD2 TRP C 394     4984   4191   4004    741    -38   -247       C  
ATOM   8944  NE1 TRP C 394      94.608  -2.071-197.970  1.00 36.20           N  
ANISOU 8944  NE1 TRP C 394     5205   4289   4261    769    -86   -250       N  
ATOM   8945  CE2 TRP C 394      94.026  -3.003-197.150  1.00 34.28           C  
ANISOU 8945  CE2 TRP C 394     4908   4114   4001    782    -40   -246       C  
ATOM   8946  CE3 TRP C 394      94.615  -4.289-195.181  1.00 38.12           C  
ANISOU 8946  CE3 TRP C 394     5389   4689   4404    741      4   -238       C  
ATOM   8947  CZ2 TRP C 394      92.753  -3.572-197.199  1.00 35.64           C  
ANISOU 8947  CZ2 TRP C 394     5014   4330   4198    821     -4   -240       C  
ATOM   8948  CZ3 TRP C 394      93.354  -4.863-195.236  1.00 36.91           C  
ANISOU 8948  CZ3 TRP C 394     5175   4578   4272    772     50   -229       C  
ATOM   8949  CH2 TRP C 394      92.437  -4.498-196.228  1.00 39.34           C  
ANISOU 8949  CH2 TRP C 394     5445   4865   4637    811     45   -231       C  
ATOM   8950  N   LYS C 395      97.268  -5.590-196.821  1.00 33.52           N  
ANISOU 8950  N   LYS C 395     4783   4086   3866    621    -76   -151       N  
ATOM   8951  CA  LYS C 395      96.785  -6.966-196.709  1.00 36.03           C  
ANISOU 8951  CA  LYS C 395     5057   4451   4184    622    -49   -117       C  
ATOM   8952  C   LYS C 395      97.941  -7.943-196.578  1.00 34.04           C  
ANISOU 8952  C   LYS C 395     4794   4216   3924    586    -70    -85       C  
ATOM   8953  O   LYS C 395      97.880  -8.881-195.776  1.00 34.91           O  
ANISOU 8953  O   LYS C 395     4899   4361   4004    582    -59    -67       O  
ATOM   8954  CB  LYS C 395      95.932  -7.353-197.920  1.00 30.14           C  
ANISOU 8954  CB  LYS C 395     4274   3695   3483    636    -41    -96       C  
ATOM   8955  CG  LYS C 395      94.687  -6.488-198.149  1.00 36.78           C  
ANISOU 8955  CG  LYS C 395     5109   4520   4344    682    -29   -124       C  
ATOM   8956  CD  LYS C 395      93.954  -6.936-199.449  1.00 38.81           C  
ANISOU 8956  CD  LYS C 395     5332   4766   4648    688    -40    -98       C  
ATOM   8957  CE  LYS C 395      92.510  -6.422-199.483  1.00 44.53           C  
ANISOU 8957  CE  LYS C 395     6023   5496   5400    740    -29   -119       C  
ATOM   8958  NZ  LYS C 395      91.649  -7.216-200.413  1.00 51.65           N  
ANISOU 8958  NZ  LYS C 395     6874   6407   6343    737    -41    -90       N  
ATOM   8959  N   ASP C 396      99.005  -7.729-197.354  1.00 32.65           N  
ANISOU 8959  N   ASP C 396     4616   4016   3773    561    -98    -77       N  
ATOM   8960  CA  ASP C 396     100.163  -8.614-197.323  1.00 28.89           C  
ANISOU 8960  CA  ASP C 396     4117   3559   3302    538   -117    -51       C  
ATOM   8961  C   ASP C 396     100.866  -8.548-195.973  1.00 28.15           C  
ANISOU 8961  C   ASP C 396     4042   3487   3168    526   -146    -62       C  
ATOM   8962  O   ASP C 396     101.233  -9.583-195.411  1.00 30.58           O  
ANISOU 8962  O   ASP C 396     4339   3821   3459    526   -158    -38       O  
ATOM   8963  CB  ASP C 396     101.135  -8.227-198.424  1.00 26.48           C  
ANISOU 8963  CB  ASP C 396     3799   3231   3034    514   -129    -45       C  
ATOM   8964  CG  ASP C 396     100.427  -8.009-199.772  1.00 34.60           C  
ANISOU 8964  CG  ASP C 396     4832   4226   4087    523   -109    -39       C  
ATOM   8965  OD1 ASP C 396      99.679  -7.010-199.916  1.00 36.16           O  
ANISOU 8965  OD1 ASP C 396     5060   4395   4284    535   -108    -61       O  
ATOM   8966  OD2 ASP C 396     100.615  -8.850-200.665  1.00 37.11           O  
ANISOU 8966  OD2 ASP C 396     5132   4546   4424    523    -98    -15       O  
ATOM   8967  N   LYS C 397     101.089  -7.334-195.462  1.00 28.12           N  
ANISOU 8967  N   LYS C 397     4073   3464   3145    515   -165    -97       N  
ATOM   8968  CA  LYS C 397     101.767  -7.187-194.169  1.00 30.12           C  
ANISOU 8968  CA  LYS C 397     4357   3735   3355    499   -204   -112       C  
ATOM   8969  C   LYS C 397     100.947  -7.783-193.031  1.00 35.48           C  
ANISOU 8969  C   LYS C 397     5066   4442   3973    523   -181   -112       C  
ATOM   8970  O   LYS C 397     101.497  -8.447-192.138  1.00 35.09           O  
ANISOU 8970  O   LYS C 397     5030   4417   3887    514   -211    -97       O  
ATOM   8971  CB  LYS C 397     102.038  -5.712-193.884  1.00 33.97           C  
ANISOU 8971  CB  LYS C 397     4892   4185   3829    480   -231   -155       C  
ATOM   8972  CG  LYS C 397     102.853  -4.981-194.924  1.00 37.83           C  
ANISOU 8972  CG  LYS C 397     5362   4642   4371    441   -251   -154       C  
ATOM   8973  CD  LYS C 397     103.036  -3.544-194.469  1.00 52.00           C  
ANISOU 8973  CD  LYS C 397     7222   6392   6145    417   -284   -197       C  
ATOM   8974  CE  LYS C 397     103.637  -2.686-195.543  1.00 67.43           C  
ANISOU 8974  CE  LYS C 397     9173   8303   8146    373   -295   -194       C  
ATOM   8975  NZ  LYS C 397     103.565  -1.252-195.132  1.00 78.33           N  
ANISOU 8975  NZ  LYS C 397    10636   9622   9502    355   -326   -238       N  
ATOM   8976  N   ALA C 398      99.639  -7.535-193.026  1.00 28.76           N  
ANISOU 8976  N   ALA C 398     4228   3591   3111    554   -129   -127       N  
ATOM   8977  CA  ALA C 398      98.798  -8.109-191.980  1.00 33.65           C  
ANISOU 8977  CA  ALA C 398     4870   4245   3672    570    -90   -124       C  
ATOM   8978  C   ALA C 398      98.770  -9.639-192.055  1.00 35.23           C  
ANISOU 8978  C   ALA C 398     5039   4471   3876    560    -83    -71       C  
ATOM   8979  O   ALA C 398      98.826 -10.322-191.025  1.00 34.28           O  
ANISOU 8979  O   ALA C 398     4952   4375   3699    553    -85    -54       O  
ATOM   8980  CB  ALA C 398      97.390  -7.524-192.069  1.00 33.21           C  
ANISOU 8980  CB  ALA C 398     4811   4189   3617    608    -30   -152       C  
ATOM   8981  N   ALA C 399      98.680 -10.197-193.262  1.00 30.75           N  
ANISOU 8981  N   ALA C 399     4421   3893   3369    560    -78    -44       N  
ATOM   8982  CA  ALA C 399      98.645 -11.648-193.406  1.00 28.80           C  
ANISOU 8982  CA  ALA C 399     4157   3658   3127    552    -75      4       C  
ATOM   8983  C   ALA C 399      99.916 -12.290-192.874  1.00 34.09           C  
ANISOU 8983  C   ALA C 399     4842   4331   3779    542   -130     25       C  
ATOM   8984  O   ALA C 399      99.863 -13.327-192.204  1.00 36.92           O  
ANISOU 8984  O   ALA C 399     5225   4702   4102    537   -135     57       O  
ATOM   8985  CB  ALA C 399      98.436 -12.015-194.893  1.00 29.73           C  
ANISOU 8985  CB  ALA C 399     4230   3754   3311    555    -68     20       C  
ATOM   8986  N   VAL C 400     101.066 -11.671-193.127  1.00 32.99           N  
ANISOU 8986  N   VAL C 400     4690   4181   3665    536   -175      9       N  
ATOM   8987  CA  VAL C 400     102.319 -12.241-192.650  1.00 32.96           C  
ANISOU 8987  CA  VAL C 400     4683   4185   3655    532   -235     27       C  
ATOM   8988  C   VAL C 400     102.339 -12.279-191.129  1.00 37.11           C  
ANISOU 8988  C   VAL C 400     5271   4727   4102    526   -261     24       C  
ATOM   8989  O   VAL C 400     102.686 -13.299-190.521  1.00 35.90           O  
ANISOU 8989  O   VAL C 400     5139   4581   3920    530   -293     58       O  
ATOM   8990  CB  VAL C 400     103.521 -11.457-193.206  1.00 35.53           C  
ANISOU 8990  CB  VAL C 400     4968   4503   4030    518   -273      8       C  
ATOM   8991  CG1 VAL C 400     104.793 -11.904-192.516  1.00 39.16           C  
ANISOU 8991  CG1 VAL C 400     5415   4979   4485    515   -345     21       C  
ATOM   8992  CG2 VAL C 400     103.642 -11.674-194.719  1.00 37.38           C  
ANISOU 8992  CG2 VAL C 400     5149   4722   4330    524   -244     18       C  
ATOM   8993  N   GLU C 401     101.932 -11.181-190.489  1.00 36.00           N  
ANISOU 8993  N   GLU C 401     5172   4587   3919    519   -249    -15       N  
ATOM   8994  CA  GLU C 401     101.972 -11.150-189.033  1.00 35.61           C  
ANISOU 8994  CA  GLU C 401     5197   4553   3782    513   -273    -23       C  
ATOM   8995  C   GLU C 401     100.963 -12.116-188.415  1.00 31.63           C  
ANISOU 8995  C   GLU C 401     4731   4067   3220    517   -221      9       C  
ATOM   8996  O   GLU C 401     101.217 -12.647-187.332  1.00 35.71           O  
ANISOU 8996  O   GLU C 401     5310   4594   3665    510   -251     28       O  
ATOM   8997  CB  GLU C 401     101.737  -9.724-188.527  1.00 35.28           C  
ANISOU 8997  CB  GLU C 401     5202   4500   3702    509   -266    -80       C  
ATOM   8998  CG  GLU C 401     102.829  -8.729-188.919  1.00 36.75           C  
ANISOU 8998  CG  GLU C 401     5367   4662   3932    487   -329   -108       C  
ATOM   8999  CD  GLU C 401     104.250  -9.209-188.640  1.00 46.61           C  
ANISOU 8999  CD  GLU C 401     6593   5921   5195    466   -419    -85       C  
ATOM   9000  OE1 GLU C 401     104.496  -9.922-187.638  1.00 42.29           O  
ANISOU 9000  OE1 GLU C 401     6089   5391   4589    469   -459    -65       O  
ATOM   9001  OE2 GLU C 401     105.145  -8.869-189.439  1.00 47.02           O  
ANISOU 9001  OE2 GLU C 401     6581   5965   5319    447   -452    -86       O  
ATOM   9002  N   ILE C 402      99.828 -12.376-189.081  1.00 36.12           N  
ANISOU 9002  N   ILE C 402     5267   4640   3818    524   -147     18       N  
ATOM   9003  CA  ILE C 402      98.912 -13.403-188.578  1.00 34.19           C  
ANISOU 9003  CA  ILE C 402     5047   4414   3529    515    -98     55       C  
ATOM   9004  C   ILE C 402      99.563 -14.776-188.651  1.00 40.89           C  
ANISOU 9004  C   ILE C 402     5901   5250   4385    507   -146    111       C  
ATOM   9005  O   ILE C 402      99.411 -15.602-187.736  1.00 36.52           O  
ANISOU 9005  O   ILE C 402     5408   4703   3764    492   -148    147       O  
ATOM   9006  CB  ILE C 402      97.572 -13.375-189.336  1.00 31.31           C  
ANISOU 9006  CB  ILE C 402     4630   4059   3207    518    -19     53       C  
ATOM   9007  CG1 ILE C 402      96.761 -12.124-188.985  1.00 32.36           C  
ANISOU 9007  CG1 ILE C 402     4770   4209   3318    538     36     -1       C  
ATOM   9008  CG2 ILE C 402      96.742 -14.603-189.024  1.00 31.34           C  
ANISOU 9008  CG2 ILE C 402     4645   4080   3184    493     25    102       C  
ATOM   9009  CD1 ILE C 402      95.819 -11.689-190.134  1.00 32.96           C  
ANISOU 9009  CD1 ILE C 402     4773   4281   3471    557     78    -17       C  
ATOM   9010  N   ASN C 403     100.309 -15.042-189.730  1.00 32.80           N  
ANISOU 9010  N   ASN C 403     4821   4203   3439    520   -185    119       N  
ATOM   9011  CA  ASN C 403     100.996 -16.326-189.841  1.00 33.95           C  
ANISOU 9011  CA  ASN C 403     4973   4330   3598    527   -234    166       C  
ATOM   9012  C   ASN C 403     102.140 -16.440-188.837  1.00 34.35           C  
ANISOU 9012  C   ASN C 403     5065   4382   3604    534   -316    173       C  
ATOM   9013  O   ASN C 403     102.375 -17.524-188.289  1.00 34.72           O  
ANISOU 9013  O   ASN C 403     5160   4416   3617    538   -353    216       O  
ATOM   9014  CB  ASN C 403     101.497 -16.539-191.272  1.00 31.89           C  
ANISOU 9014  CB  ASN C 403     4642   4047   3428    547   -244    165       C  
ATOM   9015  CG  ASN C 403     100.387 -17.008-192.204  1.00 33.49           C  
ANISOU 9015  CG  ASN C 403     4824   4237   3663    538   -186    178       C  
ATOM   9016  OD1 ASN C 403     100.288 -18.191-192.521  1.00 38.53           O  
ANISOU 9016  OD1 ASN C 403     5476   4852   4312    539   -192    215       O  
ATOM   9017  ND2 ASN C 403      99.540 -16.080-192.634  1.00 43.86           N  
ANISOU 9017  ND2 ASN C 403     6110   5562   4993    531   -136    148       N  
ATOM   9018  N   VAL C 404     102.870 -15.341-188.598  1.00 33.66           N  
ANISOU 9018  N   VAL C 404     4966   4306   3520    534   -355    133       N  
ATOM   9019  CA  VAL C 404     103.859 -15.293-187.512  1.00 37.01           C  
ANISOU 9019  CA  VAL C 404     5434   4735   3893    534   -441    134       C  
ATOM   9020  C   VAL C 404     103.208 -15.649-186.179  1.00 39.30           C  
ANISOU 9020  C   VAL C 404     5831   5032   4070    518   -430    153       C  
ATOM   9021  O   VAL C 404     103.742 -16.444-185.394  1.00 34.49           O  
ANISOU 9021  O   VAL C 404     5278   4416   3413    523   -496    189       O  
ATOM   9022  CB  VAL C 404     104.529 -13.900-187.444  1.00 34.51           C  
ANISOU 9022  CB  VAL C 404     5096   4426   3592    521   -477     82       C  
ATOM   9023  CG1 VAL C 404     105.358 -13.746-186.154  1.00 36.51           C  
ANISOU 9023  CG1 VAL C 404     5410   4685   3776    512   -571     79       C  
ATOM   9024  CG2 VAL C 404     105.394 -13.635-188.659  1.00 35.36           C  
ANISOU 9024  CG2 VAL C 404     5101   4529   3804    528   -496     73       C  
ATOM   9025  N   ALA C 405     102.045 -15.057-185.897  1.00 39.31           N  
ANISOU 9025  N   ALA C 405     5863   5049   4025    502   -345    129       N  
ATOM   9026  CA  ALA C 405     101.368 -15.322-184.629  1.00 38.27           C  
ANISOU 9026  CA  ALA C 405     5833   4931   3777    484   -314    144       C  
ATOM   9027  C   ALA C 405     101.007 -16.798-184.485  1.00 38.11           C  
ANISOU 9027  C   ALA C 405     5846   4900   3734    473   -303    212       C  
ATOM   9028  O   ALA C 405     101.141 -17.382-183.401  1.00 37.37           O  
ANISOU 9028  O   ALA C 405     5849   4804   3548    459   -335    245       O  
ATOM   9029  CB  ALA C 405     100.119 -14.450-184.522  1.00 34.85           C  
ANISOU 9029  CB  ALA C 405     5404   4522   3316    478   -208    103       C  
ATOM   9030  N   VAL C 406     100.545 -17.417-185.571  1.00 34.66           N  
ANISOU 9030  N   VAL C 406     5342   4450   3375    474   -263    233       N  
ATOM   9031  CA  VAL C 406     100.185 -18.831-185.556  1.00 34.04           C  
ANISOU 9031  CA  VAL C 406     5299   4350   3284    458   -257    297       C  
ATOM   9032  C   VAL C 406     101.401 -19.679-185.218  1.00 38.03           C  
ANISOU 9032  C   VAL C 406     5847   4821   3780    482   -367    334       C  
ATOM   9033  O   VAL C 406     101.367 -20.527-184.309  1.00 34.87           O  
ANISOU 9033  O   VAL C 406     5544   4406   3301    466   -393    382       O  
ATOM   9034  CB  VAL C 406      99.583 -19.237-186.918  1.00 37.02           C  
ANISOU 9034  CB  VAL C 406     5597   4714   3756    457   -209    304       C  
ATOM   9035  CG1 VAL C 406      99.548 -20.773-187.067  1.00 33.52           C  
ANISOU 9035  CG1 VAL C 406     5193   4229   3315    446   -233    368       C  
ATOM   9036  CG2 VAL C 406      98.197 -18.622-187.094  1.00 34.07           C  
ANISOU 9036  CG2 VAL C 406     5187   4374   3383    432   -104    280       C  
ATOM   9037  N   LEU C 407     102.497 -19.467-185.948  1.00 32.25           N  
ANISOU 9037  N   LEU C 407     5044   4079   3131    521   -434    313       N  
ATOM   9038  CA  LEU C 407     103.702 -20.255-185.703  1.00 35.99           C  
ANISOU 9038  CA  LEU C 407     5536   4524   3612    557   -542    344       C  
ATOM   9039  C   LEU C 407     104.204 -20.051-184.275  1.00 39.09           C  
ANISOU 9039  C   LEU C 407     6019   4926   3906    550   -615    350       C  
ATOM   9040  O   LEU C 407     104.484 -21.018-183.557  1.00 39.27           O  
ANISOU 9040  O   LEU C 407     6127   4921   3873    558   -676    401       O  
ATOM   9041  CB  LEU C 407     104.773 -19.888-186.725  1.00 32.92           C  
ANISOU 9041  CB  LEU C 407     5037   4138   3332    599   -585    313       C  
ATOM   9042  CG  LEU C 407     104.507 -20.473-188.145  1.00 29.69           C  
ANISOU 9042  CG  LEU C 407     4563   3705   3012    618   -537    319       C  
ATOM   9043  CD1 LEU C 407     105.247 -19.714-189.238  1.00 35.72           C  
ANISOU 9043  CD1 LEU C 407     5216   4485   3870    641   -536    275       C  
ATOM   9044  CD2 LEU C 407     104.883 -21.954-188.195  1.00 30.65           C  
ANISOU 9044  CD2 LEU C 407     4724   3779   3141    653   -588    369       C  
ATOM   9045  N   HIS C 408     104.316 -18.793-183.847  1.00 34.50           N  
ANISOU 9045  N   HIS C 408     5434   4378   3298    536   -614    300       N  
ATOM   9046  CA  HIS C 408     104.777 -18.503-182.482  1.00 33.84           C  
ANISOU 9046  CA  HIS C 408     5448   4301   3110    525   -687    299       C  
ATOM   9047  C   HIS C 408     103.881 -19.149-181.439  1.00 39.81           C  
ANISOU 9047  C   HIS C 408     6336   5051   3739    493   -645    341       C  
ATOM   9048  O   HIS C 408     104.369 -19.671-180.424  1.00 39.31           O  
ANISOU 9048  O   HIS C 408     6374   4971   3591    494   -728    377       O  
ATOM   9049  CB  HIS C 408     104.835 -16.988-182.283  1.00 37.37           C  
ANISOU 9049  CB  HIS C 408     5879   4776   3545    509   -677    231       C  
ATOM   9050  CG  HIS C 408     104.931 -16.562-180.852  1.00 39.98           C  
ANISOU 9050  CG  HIS C 408     6332   5112   3745    488   -722    220       C  
ATOM   9051  ND1 HIS C 408     106.134 -16.442-180.190  1.00 45.95           N  
ANISOU 9051  ND1 HIS C 408     7116   5862   4480    496   -860    218       N  
ATOM   9052  CD2 HIS C 408     103.973 -16.213-179.961  1.00 47.16           C  
ANISOU 9052  CD2 HIS C 408     7345   6036   4537    461   -648    207       C  
ATOM   9053  CE1 HIS C 408     105.911 -16.047-178.947  1.00 49.59           C  
ANISOU 9053  CE1 HIS C 408     7707   6327   4807    472   -875    205       C  
ATOM   9054  NE2 HIS C 408     104.608 -15.901-178.782  1.00 45.17           N  
ANISOU 9054  NE2 HIS C 408     7197   5780   4184    452   -741    197       N  
ATOM   9055  N   SER C 409     102.568 -19.118-181.663  1.00 37.02           N  
ANISOU 9055  N   SER C 409     5983   4713   3370    463   -516    341       N  
ATOM   9056  CA  SER C 409     101.626 -19.572-180.645  1.00 40.53           C  
ANISOU 9056  CA  SER C 409     6545   5165   3691    421   -452    376       C  
ATOM   9057  C   SER C 409     101.641 -21.088-180.503  1.00 42.69           C  
ANISOU 9057  C   SER C 409     6883   5396   3943    411   -486    456       C  
ATOM   9058  O   SER C 409     101.618 -21.616-179.380  1.00 39.96           O  
ANISOU 9058  O   SER C 409     6668   5036   3478    388   -512    500       O  
ATOM   9059  CB  SER C 409     100.223 -19.071-180.978  1.00 36.23           C  
ANISOU 9059  CB  SER C 409     5958   4656   3151    393   -304    350       C  
ATOM   9060  OG  SER C 409     100.180 -17.657-180.892  1.00 43.20           O  
ANISOU 9060  OG  SER C 409     6814   5569   4031    406   -278    276       O  
ATOM   9061  N   TYR C 410     101.685 -21.804-181.631  1.00 37.35           N  
ANISOU 9061  N   TYR C 410     6128   4690   3374    429   -487    477       N  
ATOM   9062  CA  TYR C 410     101.798 -23.255-181.586  1.00 37.05           C  
ANISOU 9062  CA  TYR C 410     6156   4596   3325    427   -532    550       C  
ATOM   9063  C   TYR C 410     103.129 -23.689-180.993  1.00 36.58           C  
ANISOU 9063  C   TYR C 410     6155   4501   3242    475   -681    574       C  
ATOM   9064  O   TYR C 410     103.177 -24.627-180.185  1.00 40.68           O  
ANISOU 9064  O   TYR C 410     6799   4981   3677    462   -729    636       O  
ATOM   9065  CB  TYR C 410     101.608 -23.838-182.998  1.00 34.55           C  
ANISOU 9065  CB  TYR C 410     5744   4251   3131    443   -506    555       C  
ATOM   9066  CG  TYR C 410     100.153 -24.013-183.338  1.00 38.19           C  
ANISOU 9066  CG  TYR C 410     6193   4727   3591    381   -381    568       C  
ATOM   9067  CD1 TYR C 410      99.611 -25.278-183.522  1.00 35.97           C  
ANISOU 9067  CD1 TYR C 410     5963   4397   3307    346   -367    630       C  
ATOM   9068  CD2 TYR C 410      99.307 -22.914-183.418  1.00 41.23           C  
ANISOU 9068  CD2 TYR C 410     6517   5172   3976    357   -281    518       C  
ATOM   9069  CE1 TYR C 410      98.266 -25.439-183.806  1.00 37.25           C  
ANISOU 9069  CE1 TYR C 410     6103   4577   3472    279   -257    643       C  
ATOM   9070  CE2 TYR C 410      97.971 -23.063-183.692  1.00 40.11           C  
ANISOU 9070  CE2 TYR C 410     6349   5051   3839    304   -171    529       C  
ATOM   9071  CZ  TYR C 410      97.455 -24.320-183.883  1.00 39.60           C  
ANISOU 9071  CZ  TYR C 410     6325   4946   3777    260   -159    592       C  
ATOM   9072  OH  TYR C 410      96.109 -24.450-184.143  1.00 39.10           O  
ANISOU 9072  OH  TYR C 410     6223   4909   3725    198    -53    604       O  
ATOM   9073  N   GLN C 411     104.218 -23.011-181.366  1.00 38.49           N  
ANISOU 9073  N   GLN C 411     6308   4757   3557    526   -758    527       N  
ATOM   9074  CA  GLN C 411     105.527 -23.383-180.840  1.00 36.33           C  
ANISOU 9074  CA  GLN C 411     6067   4458   3277    576   -909    547       C  
ATOM   9075  C   GLN C 411     105.608 -23.127-179.342  1.00 44.70           C  
ANISOU 9075  C   GLN C 411     7264   5526   4193    548   -961    560       C  
ATOM   9076  O   GLN C 411     106.204 -23.921-178.604  1.00 48.51           O  
ANISOU 9076  O   GLN C 411     7845   5969   4618    569  -1071    610       O  
ATOM   9077  CB  GLN C 411     106.622 -22.623-181.579  1.00 43.69           C  
ANISOU 9077  CB  GLN C 411     6859   5417   4326    625   -968    492       C  
ATOM   9078  CG  GLN C 411     106.809 -23.119-183.026  1.00 49.47           C  
ANISOU 9078  CG  GLN C 411     7474   6129   5192    668   -940    487       C  
ATOM   9079  CD  GLN C 411     107.683 -22.201-183.868  1.00 62.13           C  
ANISOU 9079  CD  GLN C 411     8930   7770   6908    698   -958    429       C  
ATOM   9080  OE1 GLN C 411     108.144 -21.156-183.402  1.00 69.92           O  
ANISOU 9080  OE1 GLN C 411     9894   8793   7878    682   -995    391       O  
ATOM   9081  NE2 GLN C 411     107.903 -22.587-185.123  1.00 55.28           N  
ANISOU 9081  NE2 GLN C 411     7966   6889   6147    737   -930    422       N  
ATOM   9082  N   LEU C 412     104.995 -22.038-178.874  1.00 46.19           N  
ANISOU 9082  N   LEU C 412     7473   5762   4316    505   -886    515       N  
ATOM   9083  CA  LEU C 412     105.008 -21.749-177.442  1.00 48.07           C  
ANISOU 9083  CA  LEU C 412     7856   6007   4401    476   -926    522       C  
ATOM   9084  C   LEU C 412     104.185 -22.774-176.669  1.00 50.41           C  
ANISOU 9084  C   LEU C 412     8303   6277   4576    433   -879    594       C  
ATOM   9085  O   LEU C 412     104.528 -23.130-175.537  1.00 47.88           O  
ANISOU 9085  O   LEU C 412     8125   5933   4133    425   -961    632       O  
ATOM   9086  CB  LEU C 412     104.488 -20.331-177.193  1.00 49.06           C  
ANISOU 9086  CB  LEU C 412     7970   6184   4486    447   -844    449       C  
ATOM   9087  CG  LEU C 412     104.675 -19.737-175.797  1.00 60.95           C  
ANISOU 9087  CG  LEU C 412     9617   7701   5841    425   -894    432       C  
ATOM   9088  CD1 LEU C 412     106.153 -19.670-175.458  1.00 63.86           C  
ANISOU 9088  CD1 LEU C 412     9987   8050   6227    461  -1081    429       C  
ATOM   9089  CD2 LEU C 412     104.041 -18.355-175.716  1.00 69.08           C  
ANISOU 9089  CD2 LEU C 412    10631   8773   6844    405   -795    353       C  
ATOM   9090  N   ALA C 413     103.093 -23.262-177.262  1.00 43.64           N  
ANISOU 9090  N   ALA C 413     7418   5419   3747    399   -752    617       N  
ATOM   9091  CA  ALA C 413     102.255 -24.263-176.617  1.00 47.59           C  
ANISOU 9091  CA  ALA C 413     8050   5893   4141    343   -696    690       C  
ATOM   9092  C   ALA C 413     102.749 -25.681-176.837  1.00 46.04           C  
ANISOU 9092  C   ALA C 413     7899   5619   3974    366   -789    765       C  
ATOM   9093  O   ALA C 413     102.093 -26.614-176.372  1.00 51.72           O  
ANISOU 9093  O   ALA C 413     8736   6304   4613    313   -752    834       O  
ATOM   9094  CB  ALA C 413     100.806 -24.153-177.101  1.00 42.96           C  
ANISOU 9094  CB  ALA C 413     7409   5342   3571    286   -519    683       C  
ATOM   9095  N   LYS C 414     103.882 -25.858-177.523  1.00 50.60           N  
ANISOU 9095  N   LYS C 414     8392   6168   4666    443   -907    752       N  
ATOM   9096  CA  LYS C 414     104.447 -27.182-177.797  1.00 49.13           C  
ANISOU 9096  CA  LYS C 414     8244   5903   4521    485  -1003    813       C  
ATOM   9097  C   LYS C 414     103.458 -28.056-178.561  1.00 50.79           C  
ANISOU 9097  C   LYS C 414     8448   6078   4772    445   -904    850       C  
ATOM   9098  O   LYS C 414     103.275 -29.235-178.254  1.00 50.48           O  
ANISOU 9098  O   LYS C 414     8529   5969   4684    425   -933    924       O  
ATOM   9099  CB  LYS C 414     104.900 -27.876-176.506  1.00 51.24           C  
ANISOU 9099  CB  LYS C 414     8694   6120   4654    485  -1118    880       C  
ATOM   9100  CG  LYS C 414     105.849 -27.060-175.662  1.00 69.09           C  
ANISOU 9100  CG  LYS C 414    10977   8412   6861    517  -1231    846       C  
ATOM   9101  CD  LYS C 414     107.223 -26.968-176.292  1.00 80.53           C  
ANISOU 9101  CD  LYS C 414    12298   9855   8446    613  -1367    814       C  
ATOM   9102  CE  LYS C 414     108.201 -26.276-175.349  1.00 91.68           C  
ANISOU 9102  CE  LYS C 414    13743  11290   9799    635  -1503    791       C  
ATOM   9103  NZ  LYS C 414     109.550 -26.110-175.961  1.00 95.82           N  
ANISOU 9103  NZ  LYS C 414    14119  11822  10466    722  -1630    757       N  
ATOM   9104  N   VAL C 415     102.790 -27.466-179.547  1.00 42.32           N  
ANISOU 9104  N   VAL C 415     7244   5050   3787    426   -790    801       N  
ATOM   9105  CA  VAL C 415     101.906 -28.188-180.453  1.00 44.92           C  
ANISOU 9105  CA  VAL C 415     7541   5349   4176    390   -707    825       C  
ATOM   9106  C   VAL C 415     102.572 -28.246-181.821  1.00 49.26           C  
ANISOU 9106  C   VAL C 415     7959   5880   4878    465   -745    785       C  
ATOM   9107  O   VAL C 415     103.047 -27.221-182.329  1.00 37.48           O  
ANISOU 9107  O   VAL C 415     6346   4439   3455    505   -744    718       O  
ATOM   9108  CB  VAL C 415     100.528 -27.514-180.550  1.00 49.92           C  
ANISOU 9108  CB  VAL C 415     8128   6048   4791    311   -547    800       C  
ATOM   9109  CG1 VAL C 415      99.633 -28.267-181.520  1.00 41.03           C  
ANISOU 9109  CG1 VAL C 415     6962   4892   3735    269   -476    825       C  
ATOM   9110  CG2 VAL C 415      99.899 -27.432-179.177  1.00 42.66           C  
ANISOU 9110  CG2 VAL C 415     7339   5155   3716    241   -496    835       C  
ATOM   9111  N   THR C 416     102.614 -29.445-182.407  1.00 43.63           N  
ANISOU 9111  N   THR C 416     7278   5089   4210    482   -778    827       N  
ATOM   9112  CA  THR C 416     103.292 -29.646-183.679  1.00 49.42           C  
ANISOU 9112  CA  THR C 416     7906   5796   5075    560   -814    792       C  
ATOM   9113  C   THR C 416     102.689 -28.752-184.757  1.00 42.13           C  
ANISOU 9113  C   THR C 416     6843   4931   4232    540   -708    730       C  
ATOM   9114  O   THR C 416     101.471 -28.688-184.922  1.00 40.71           O  
ANISOU 9114  O   THR C 416     6663   4770   4036    463   -607    737       O  
ATOM   9115  CB  THR C 416     103.195 -31.111-184.093  1.00 50.42           C  
ANISOU 9115  CB  THR C 416     8116   5822   5220    570   -850    847       C  
ATOM   9116  OG1 THR C 416     103.813 -31.929-183.098  1.00 47.45           O  
ANISOU 9116  OG1 THR C 416     7877   5383   4770    598   -961    907       O  
ATOM   9117  CG2 THR C 416     103.881 -31.343-185.452  1.00 42.57           C  
ANISOU 9117  CG2 THR C 416     7020   4799   4356    657   -877    805       C  
ATOM   9118  N   ILE C 417     103.550 -28.037-185.474  1.00 34.13           N  
ANISOU 9118  N   ILE C 417     5710   3950   3307    608   -734    671       N  
ATOM   9119  CA  ILE C 417     103.139 -27.228-186.623  1.00 30.90           C  
ANISOU 9119  CA  ILE C 417     5176   3585   2981    600   -650    614       C  
ATOM   9120  C   ILE C 417     104.340 -27.084-187.542  1.00 36.65           C  
ANISOU 9120  C   ILE C 417     5804   4310   3810    688   -704    573       C  
ATOM   9121  O   ILE C 417     105.490 -27.171-187.111  1.00 41.16           O  
ANISOU 9121  O   ILE C 417     6374   4877   4388    750   -798    574       O  
ATOM   9122  CB  ILE C 417     102.614 -25.842-186.175  1.00 31.90           C  
ANISOU 9122  CB  ILE C 417     5258   3792   3070    554   -581    574       C  
ATOM   9123  CG1 ILE C 417     101.920 -25.116-187.336  1.00 40.90           C  
ANISOU 9123  CG1 ILE C 417     6291   4965   4284    536   -490    526       C  
ATOM   9124  CG2 ILE C 417     103.739 -24.995-185.589  1.00 41.27           C  
ANISOU 9124  CG2 ILE C 417     6417   5015   4248    597   -655    541       C  
ATOM   9125  CD1 ILE C 417     100.682 -24.415-186.902  1.00 42.26           C  
ANISOU 9125  CD1 ILE C 417     6466   5187   4405    468   -393    517       C  
ATOM   9126  N   VAL C 418     104.073 -26.855-188.828  1.00 39.63           N  
ANISOU 9126  N   VAL C 418     6097   4693   4267    694   -643    537       N  
ATOM   9127  CA  VAL C 418     105.133 -26.732-189.814  1.00 38.69           C  
ANISOU 9127  CA  VAL C 418     5883   4575   4242    772   -672    498       C  
ATOM   9128  C   VAL C 418     104.842 -25.514-190.683  1.00 37.34           C  
ANISOU 9128  C   VAL C 418     5606   4461   4120    749   -594    443       C  
ATOM   9129  O   VAL C 418     103.698 -25.303-191.111  1.00 37.11           O  
ANISOU 9129  O   VAL C 418     5578   4437   4084    693   -517    439       O  
ATOM   9130  CB  VAL C 418     105.278 -28.013-190.666  1.00 41.13           C  
ANISOU 9130  CB  VAL C 418     6225   4807   4595    820   -690    516       C  
ATOM   9131  CG1 VAL C 418     104.017 -28.321-191.483  1.00 32.35           C  
ANISOU 9131  CG1 VAL C 418     5136   3667   3488    760   -610    520       C  
ATOM   9132  CG2 VAL C 418     106.492 -27.920-191.560  1.00 36.97           C  
ANISOU 9132  CG2 VAL C 418     5601   4287   4157    911   -716    474       C  
ATOM   9133  N   ASP C 419     105.862 -24.690-190.908  1.00 30.88           N  
ANISOU 9133  N   ASP C 419     4696   3685   3351    788   -618    402       N  
ATOM   9134  CA  ASP C 419     105.626 -23.529-191.747  1.00 34.60           C  
ANISOU 9134  CA  ASP C 419     5080   4201   3865    764   -549    354       C  
ATOM   9135  C   ASP C 419     105.705 -23.928-193.223  1.00 35.02           C  
ANISOU 9135  C   ASP C 419     5089   4227   3989    797   -511    337       C  
ATOM   9136  O   ASP C 419     106.194 -25.004-193.589  1.00 33.50           O  
ANISOU 9136  O   ASP C 419     4918   3988   3822    853   -544    352       O  
ATOM   9137  CB  ASP C 419     106.612 -22.408-191.407  1.00 32.08           C  
ANISOU 9137  CB  ASP C 419     4687   3935   3565    773   -584    320       C  
ATOM   9138  CG  ASP C 419     108.041 -22.717-191.845  1.00 46.19           C  
ANISOU 9138  CG  ASP C 419     6401   5725   5425    845   -641    310       C  
ATOM   9139  OD1 ASP C 419     108.316 -22.703-193.060  1.00 48.20           O  
ANISOU 9139  OD1 ASP C 419     6588   5978   5746    872   -598    286       O  
ATOM   9140  OD2 ASP C 419     108.901 -22.951-190.975  1.00 48.95           O  
ANISOU 9140  OD2 ASP C 419     6756   6080   5765    877   -730    324       O  
ATOM   9141  N   HIS C 420     105.199 -23.042-194.089  1.00 37.70           N  
ANISOU 9141  N   HIS C 420     5377   4592   4355    766   -442    304       N  
ATOM   9142  CA  HIS C 420     105.089 -23.389-195.509  1.00 36.39           C  
ANISOU 9142  CA  HIS C 420     5189   4399   4239    787   -401    288       C  
ATOM   9143  C   HIS C 420     106.443 -23.493-196.210  1.00 38.65           C  
ANISOU 9143  C   HIS C 420     5407   4690   4588    857   -418    264       C  
ATOM   9144  O   HIS C 420     106.546 -24.179-197.233  1.00 39.04           O  
ANISOU 9144  O   HIS C 420     5463   4702   4667    895   -397    257       O  
ATOM   9145  CB  HIS C 420     104.183 -22.382-196.227  1.00 33.28           C  
ANISOU 9145  CB  HIS C 420     4765   4028   3853    737   -332    261       C  
ATOM   9146  CG  HIS C 420     104.594 -20.951-196.061  1.00 36.94           C  
ANISOU 9146  CG  HIS C 420     5163   4545   4326    720   -322    229       C  
ATOM   9147  ND1 HIS C 420     104.466 -20.269-194.866  1.00 33.85           N  
ANISOU 9147  ND1 HIS C 420     4784   4185   3891    690   -341    229       N  
ATOM   9148  CD2 HIS C 420     105.097 -20.059-196.950  1.00 34.61           C  
ANISOU 9148  CD2 HIS C 420     4804   4272   4076    723   -294    195       C  
ATOM   9149  CE1 HIS C 420     104.892 -19.027-195.020  1.00 34.96           C  
ANISOU 9149  CE1 HIS C 420     4870   4360   4053    677   -331    195       C  
ATOM   9150  NE2 HIS C 420     105.276 -18.871-196.276  1.00 35.68           N  
ANISOU 9150  NE2 HIS C 420     4913   4447   4199    693   -302    177       N  
ATOM   9151  N   HIS C 421     107.489 -22.847-195.693  1.00 33.52           N  
ANISOU 9151  N   HIS C 421     4691   4086   3958    875   -455    251       N  
ATOM   9152  CA  HIS C 421     108.813 -23.025-196.283  1.00 35.70           C  
ANISOU 9152  CA  HIS C 421     4889   4376   4301    943   -470    231       C  
ATOM   9153  C   HIS C 421     109.361 -24.408-195.982  1.00 39.26           C  
ANISOU 9153  C   HIS C 421     5378   4781   4758   1020   -531    256       C  
ATOM   9154  O   HIS C 421     109.877 -25.090-196.871  1.00 34.06           O  
ANISOU 9154  O   HIS C 421     4701   4098   4144   1087   -515    243       O  
ATOM   9155  CB  HIS C 421     109.782 -21.954-195.777  1.00 35.69           C  
ANISOU 9155  CB  HIS C 421     4796   4438   4325    932   -501    212       C  
ATOM   9156  CG  HIS C 421     109.327 -20.554-196.037  1.00 38.21           C  
ANISOU 9156  CG  HIS C 421     5087   4792   4638    859   -449    187       C  
ATOM   9157  ND1 HIS C 421     109.202 -20.033-197.307  1.00 36.76           N  
ANISOU 9157  ND1 HIS C 421     4867   4615   4487    845   -374    162       N  
ATOM   9158  CD2 HIS C 421     108.976 -19.561-195.187  1.00 34.38           C  
ANISOU 9158  CD2 HIS C 421     4617   4332   4114    801   -465    181       C  
ATOM   9159  CE1 HIS C 421     108.786 -18.782-197.229  1.00 37.37           C  
ANISOU 9159  CE1 HIS C 421     4936   4715   4549    782   -351    145       C  
ATOM   9160  NE2 HIS C 421     108.635 -18.474-195.952  1.00 40.43           N  
ANISOU 9160  NE2 HIS C 421     5354   5114   4895    757   -403    154       N  
ATOM   9161  N   ALA C 422     109.302 -24.826-194.716  1.00 36.96           N  
ANISOU 9161  N   ALA C 422     5149   4475   4420   1018   -604    291       N  
ATOM   9162  CA  ALA C 422     109.780 -26.161-194.378  1.00 33.54           C  
ANISOU 9162  CA  ALA C 422     4770   3986   3988   1093   -673    321       C  
ATOM   9163  C   ALA C 422     108.964 -27.231-195.093  1.00 34.93           C  
ANISOU 9163  C   ALA C 422     5038   4085   4150   1100   -638    335       C  
ATOM   9164  O   ALA C 422     109.517 -28.220-195.574  1.00 36.94           O  
ANISOU 9164  O   ALA C 422     5308   4290   4438   1182   -661    333       O  
ATOM   9165  CB  ALA C 422     109.730 -26.363-192.859  1.00 36.63           C  
ANISOU 9165  CB  ALA C 422     5234   4370   4315   1074   -758    362       C  
ATOM   9166  N   ALA C 423     107.644 -27.039-195.192  1.00 34.16           N  
ANISOU 9166  N   ALA C 423     4999   3975   4006   1017   -585    345       N  
ATOM   9167  CA  ALA C 423     106.796 -28.085-195.756  1.00 36.23           C  
ANISOU 9167  CA  ALA C 423     5354   4160   4251   1008   -566    364       C  
ATOM   9168  C   ALA C 423     107.052 -28.265-197.246  1.00 33.91           C  
ANISOU 9168  C   ALA C 423     5027   3847   4010   1054   -517    324       C  
ATOM   9169  O   ALA C 423     107.170 -29.400-197.724  1.00 36.63           O  
ANISOU 9169  O   ALA C 423     5436   4118   4363   1108   -535    329       O  
ATOM   9170  CB  ALA C 423     105.328 -27.764-195.506  1.00 34.68           C  
ANISOU 9170  CB  ALA C 423     5207   3967   4003    903   -521    384       C  
ATOM   9171  N   THR C 424     107.150 -27.161-197.993  1.00 33.72           N  
ANISOU 9171  N   THR C 424     4914   3883   4016   1034   -456    285       N  
ATOM   9172  CA  THR C 424     107.387 -27.292-199.432  1.00 37.15           C  
ANISOU 9172  CA  THR C 424     5327   4301   4487   1074   -402    247       C  
ATOM   9173  C   THR C 424     108.786 -27.819-199.713  1.00 34.59           C  
ANISOU 9173  C   THR C 424     4954   3975   4214   1184   -422    227       C  
ATOM   9174  O   THR C 424     108.990 -28.562-200.677  1.00 36.79           O  
ANISOU 9174  O   THR C 424     5264   4206   4509   1243   -398    206       O  
ATOM   9175  CB  THR C 424     107.162 -25.950-200.134  1.00 38.90           C  
ANISOU 9175  CB  THR C 424     5475   4583   4721   1022   -334    216       C  
ATOM   9176  OG1 THR C 424     108.017 -24.961-199.560  1.00 34.15           O  
ANISOU 9176  OG1 THR C 424     4777   4054   4143   1022   -344    205       O  
ATOM   9177  CG2 THR C 424     105.726 -25.503-199.975  1.00 35.19           C  
ANISOU 9177  CG2 THR C 424     5050   4111   4209    929   -314    232       C  
ATOM   9178  N   ALA C 425     109.759 -27.474-198.870  1.00 35.07           N  
ANISOU 9178  N   ALA C 425     4939   4085   4300   1216   -469    231       N  
ATOM   9179  CA  ALA C 425     111.085 -28.065-199.016  1.00 39.64           C  
ANISOU 9179  CA  ALA C 425     5461   4664   4935   1329   -498    214       C  
ATOM   9180  C   ALA C 425     111.046 -29.579-198.806  1.00 38.62           C  
ANISOU 9180  C   ALA C 425     5442   4439   4792   1401   -557    238       C  
ATOM   9181  O   ALA C 425     111.732 -30.328-199.517  1.00 37.35           O  
ANISOU 9181  O   ALA C 425     5276   4246   4671   1501   -548    212       O  
ATOM   9182  CB  ALA C 425     112.061 -27.395-198.046  1.00 39.86           C  
ANISOU 9182  CB  ALA C 425     5386   4765   4994   1339   -555    218       C  
ATOM   9183  N   SER C 426     110.237 -30.057-197.849  1.00 36.19           N  
ANISOU 9183  N   SER C 426     5243   4083   4425   1351   -614    286       N  
ATOM   9184  CA ASER C 426     110.125 -31.501-197.644  0.64 35.54           C  
ANISOU 9184  CA ASER C 426     5285   3897   4323   1407   -674    315       C  
ATOM   9185  CA BSER C 426     110.131 -31.501-197.654  0.36 36.42           C  
ANISOU 9185  CA BSER C 426     5395   4007   4434   1407   -673    314       C  
ATOM   9186  C   SER C 426     109.389 -32.166-198.806  1.00 42.32           C  
ANISOU 9186  C   SER C 426     6229   4681   5170   1400   -621    298       C  
ATOM   9187  O   SER C 426     109.712 -33.299-199.186  1.00 38.91           O  
ANISOU 9187  O   SER C 426     5870   4166   4750   1486   -649    293       O  
ATOM   9188  CB ASER C 426     109.421 -31.805-196.316  0.64 35.80           C  
ANISOU 9188  CB ASER C 426     5418   3897   4287   1340   -741    376       C  
ATOM   9189  CB BSER C 426     109.433 -31.814-196.333  0.36 35.88           C  
ANISOU 9189  CB BSER C 426     5428   3906   4298   1341   -740    376       C  
ATOM   9190  OG ASER C 426     108.008 -31.661-196.409  0.64 37.81           O  
ANISOU 9190  OG ASER C 426     5742   4134   4488   1225   -692    396       O  
ATOM   9191  OG BSER C 426     110.252 -31.449-195.244  0.36 31.88           O  
ANISOU 9191  OG BSER C 426     4868   3449   3796   1368   -811    391       O  
ATOM   9192  N   PHE C 427     108.398 -31.484-199.377  1.00 40.80           N  
ANISOU 9192  N   PHE C 427     6036   4513   4955   1304   -552    288       N  
ATOM   9193  CA  PHE C 427     107.703 -32.072-200.516  1.00 35.45           C  
ANISOU 9193  CA  PHE C 427     5439   3766   4265   1293   -513    270       C  
ATOM   9194  C   PHE C 427     108.639 -32.213-201.704  1.00 39.04           C  
ANISOU 9194  C   PHE C 427     5849   4220   4764   1395   -467    214       C  
ATOM   9195  O   PHE C 427     108.543 -33.182-202.468  1.00 38.85           O  
ANISOU 9195  O   PHE C 427     5917   4110   4732   1443   -465    197       O  
ATOM   9196  CB  PHE C 427     106.480 -31.240-200.899  1.00 36.64           C  
ANISOU 9196  CB  PHE C 427     5585   3950   4388   1174   -457    271       C  
ATOM   9197  CG  PHE C 427     105.654 -31.873-201.982  1.00 37.87           C  
ANISOU 9197  CG  PHE C 427     5834   4031   4525   1149   -435    258       C  
ATOM   9198  CD1 PHE C 427     104.836 -32.954-201.701  1.00 42.07           C  
ANISOU 9198  CD1 PHE C 427     6493   4470   5023   1109   -482    295       C  
ATOM   9199  CD2 PHE C 427     105.707 -31.395-203.287  1.00 35.66           C  
ANISOU 9199  CD2 PHE C 427     5523   3769   4259   1160   -371    210       C  
ATOM   9200  CE1 PHE C 427     104.076 -33.554-202.705  1.00 42.22           C  
ANISOU 9200  CE1 PHE C 427     6601   4415   5026   1079   -474    282       C  
ATOM   9201  CE2 PHE C 427     104.950 -31.982-204.298  1.00 32.97           C  
ANISOU 9201  CE2 PHE C 427     5277   3355   3894   1135   -361    196       C  
ATOM   9202  CZ  PHE C 427     104.141 -33.063-204.012  1.00 38.42           C  
ANISOU 9202  CZ  PHE C 427     6089   3953   4556   1095   -416    230       C  
ATOM   9203  N   MET C 428     109.554 -31.261-201.881  1.00 38.92           N  
ANISOU 9203  N   MET C 428     5697   4299   4793   1426   -426    183       N  
ATOM   9204  CA  MET C 428     110.548 -31.411-202.936  1.00 40.88           C  
ANISOU 9204  CA  MET C 428     5891   4557   5085   1527   -372    131       C  
ATOM   9205  C   MET C 428     111.388 -32.667-202.719  1.00 43.68           C  
ANISOU 9205  C   MET C 428     6285   4846   5467   1659   -429    128       C  
ATOM   9206  O   MET C 428     111.700 -33.385-203.674  1.00 41.92           O  
ANISOU 9206  O   MET C 428     6106   4570   5252   1743   -395     89       O  
ATOM   9207  CB  MET C 428     111.421 -30.162-203.013  1.00 38.90           C  
ANISOU 9207  CB  MET C 428     5476   4423   4880   1525   -323    107       C  
ATOM   9208  CG  MET C 428     110.637 -28.899-203.417  1.00 37.69           C  
ANISOU 9208  CG  MET C 428     5295   4324   4701   1407   -262    104       C  
ATOM   9209  SD  MET C 428     109.930 -28.992-205.093  1.00 41.23           S  
ANISOU 9209  SD  MET C 428     5823   4727   5114   1387   -176     68       S  
ATOM   9210  CE  MET C 428     111.411 -29.150-206.087  1.00 39.48           C  
ANISOU 9210  CE  MET C 428     5519   4539   4941   1508   -101     14       C  
ATOM   9211  N   LYS C 429     111.752 -32.958-201.466  1.00 41.37           N  
ANISOU 9211  N   LYS C 429     5986   4549   5183   1684   -519    167       N  
ATOM   9212  CA  LYS C 429     112.448 -34.209-201.175  1.00 42.52           C  
ANISOU 9212  CA  LYS C 429     6188   4617   5351   1811   -591    171       C  
ATOM   9213  C   LYS C 429     111.563 -35.408-201.487  1.00 37.76           C  
ANISOU 9213  C   LYS C 429     5771   3878   4697   1805   -616    185       C  
ATOM   9214  O   LYS C 429     112.035 -36.421-202.022  1.00 38.61           O  
ANISOU 9214  O   LYS C 429     5943   3906   4821   1920   -627    158       O  
ATOM   9215  CB  LYS C 429     112.885 -34.234-199.712  1.00 42.57           C  
ANISOU 9215  CB  LYS C 429     6169   4641   5363   1822   -696    218       C  
ATOM   9216  CG  LYS C 429     113.953 -35.267-199.432  1.00 54.16           C  
ANISOU 9216  CG  LYS C 429     7644   6058   6878   1978   -773    215       C  
ATOM   9217  CD  LYS C 429     115.294 -34.741-199.916  1.00 70.41           C  
ANISOU 9217  CD  LYS C 429     9516   8212   9024   2077   -730    163       C  
ATOM   9218  CE  LYS C 429     115.951 -35.701-200.885  1.00 75.57           C  
ANISOU 9218  CE  LYS C 429    10187   8808   9719   2227   -697    113       C  
ATOM   9219  NZ  LYS C 429     116.353 -36.959-200.194  1.00 73.04           N  
ANISOU 9219  NZ  LYS C 429     9958   8386   9408   2345   -816    138       N  
ATOM   9220  N   HIS C 430     110.264 -35.300-201.177  1.00 41.41           N  
ANISOU 9220  N   HIS C 430     6322   4313   5098   1671   -624    226       N  
ATOM   9221  CA  HIS C 430     109.330 -36.380-201.481  1.00 43.81           C  
ANISOU 9221  CA  HIS C 430     6799   4491   5355   1640   -650    243       C  
ATOM   9222  C   HIS C 430     109.238 -36.630-202.986  1.00 38.34           C  
ANISOU 9222  C   HIS C 430     6144   3759   4664   1675   -580    184       C  
ATOM   9223  O   HIS C 430     109.191 -37.781-203.428  1.00 38.40           O  
ANISOU 9223  O   HIS C 430     6282   3651   4659   1735   -609    172       O  
ATOM   9224  CB  HIS C 430     107.944 -36.060-200.906  1.00 39.71           C  
ANISOU 9224  CB  HIS C 430     6335   3974   4781   1479   -657    295       C  
ATOM   9225  CG  HIS C 430     106.905 -37.083-201.254  1.00 46.68           C  
ANISOU 9225  CG  HIS C 430     7381   4735   5619   1423   -681    315       C  
ATOM   9226  ND1 HIS C 430     106.898 -38.351-200.709  1.00 41.75           N  
ANISOU 9226  ND1 HIS C 430     6898   3993   4975   1455   -763    354       N  
ATOM   9227  CD2 HIS C 430     105.859 -37.040-202.116  1.00 39.51           C  
ANISOU 9227  CD2 HIS C 430     6524   3802   4688   1335   -640    303       C  
ATOM   9228  CE1 HIS C 430     105.885 -39.038-201.204  1.00 45.15           C  
ANISOU 9228  CE1 HIS C 430     7456   4330   5370   1381   -770    365       C  
ATOM   9229  NE2 HIS C 430     105.240 -38.268-202.064  1.00 39.71           N  
ANISOU 9229  NE2 HIS C 430     6711   3698   4680   1308   -698    333       N  
ATOM   9230  N   LEU C 431     109.201 -35.563-203.788  1.00 40.71           N  
ANISOU 9230  N   LEU C 431     6346   4149   4975   1637   -491    147       N  
ATOM   9231  CA  LEU C 431     109.162 -35.741-205.235  1.00 39.01           C  
ANISOU 9231  CA  LEU C 431     6172   3901   4750   1670   -422     90       C  
ATOM   9232  C   LEU C 431     110.387 -36.506-205.721  1.00 40.79           C  
ANISOU 9232  C   LEU C 431     6396   4090   5012   1838   -411     42       C  
ATOM   9233  O   LEU C 431     110.277 -37.409-206.558  1.00 39.99           O  
ANISOU 9233  O   LEU C 431     6417   3891   4887   1893   -404      8       O  
ATOM   9234  CB  LEU C 431     109.062 -34.377-205.928  1.00 38.33           C  
ANISOU 9234  CB  LEU C 431     5974   3924   4667   1606   -331     63       C  
ATOM   9235  CG  LEU C 431     107.721 -33.662-205.774  1.00 41.05           C  
ANISOU 9235  CG  LEU C 431     6335   4291   4973   1452   -332     97       C  
ATOM   9236  CD1 LEU C 431     107.716 -32.284-206.481  1.00 43.06           C  
ANISOU 9236  CD1 LEU C 431     6485   4644   5232   1403   -249     70       C  
ATOM   9237  CD2 LEU C 431     106.596 -34.538-206.303  1.00 36.68           C  
ANISOU 9237  CD2 LEU C 431     5939   3627   4372   1398   -362    104       C  
ATOM   9238  N   GLU C 432     111.558 -36.177-205.174  1.00 44.40           N  
ANISOU 9238  N   GLU C 432     6717   4624   5527   1923   -414     37       N  
ATOM   9239  CA  GLU C 432     112.789 -36.871-205.530  1.00 44.75           C  
ANISOU 9239  CA  GLU C 432     6734   4649   5621   2094   -405     -9       C  
ATOM   9240  C   GLU C 432     112.735 -38.346-205.131  1.00 45.49           C  
ANISOU 9240  C   GLU C 432     6986   4598   5702   2176   -501      8       C  
ATOM   9241  O   GLU C 432     113.102 -39.228-205.921  1.00 46.41           O  
ANISOU 9241  O   GLU C 432     7182   4633   5820   2290   -483    -40       O  
ATOM   9242  CB  GLU C 432     113.965 -36.163-204.861  1.00 49.10           C  
ANISOU 9242  CB  GLU C 432     7092   5318   6244   2149   -407     -8       C  
ATOM   9243  CG  GLU C 432     115.308 -36.323-205.533  1.00 66.25           C  
ANISOU 9243  CG  GLU C 432     9156   7533   8483   2305   -345    -69       C  
ATOM   9244  CD  GLU C 432     116.319 -35.321-205.000  1.00 86.16           C  
ANISOU 9244  CD  GLU C 432    11463  10196  11078   2314   -334    -66       C  
ATOM   9245  OE1 GLU C 432     117.533 -35.623-205.005  1.00 89.28           O  
ANISOU 9245  OE1 GLU C 432    11750  10626  11547   2453   -332    -96       O  
ATOM   9246  OE2 GLU C 432     115.886 -34.228-204.565  1.00 92.56           O  
ANISOU 9246  OE2 GLU C 432    12211  11083  11874   2181   -330    -35       O  
ATOM   9247  N   ASN C 433     112.272 -38.630-203.904  1.00 46.74           N  
ANISOU 9247  N   ASN C 433     7201   4717   5842   2117   -603     76       N  
ATOM   9248  CA  ASN C 433     112.177 -40.013-203.430  1.00 44.73           C  
ANISOU 9248  CA  ASN C 433     7110   4317   5570   2180   -704    104       C  
ATOM   9249  C   ASN C 433     111.214 -40.821-204.278  1.00 43.64           C  
ANISOU 9249  C   ASN C 433     7157   4051   5373   2137   -696     90       C  
ATOM   9250  O   ASN C 433     111.458 -41.998-204.558  1.00 47.58           O  
ANISOU 9250  O   ASN C 433     7788   4423   5869   2241   -738     70       O  
ATOM   9251  CB  ASN C 433     111.693 -40.064-201.981  1.00 45.45           C  
ANISOU 9251  CB  ASN C 433     7241   4394   5633   2093   -803    187       C  
ATOM   9252  CG  ASN C 433     112.652 -39.429-201.015  1.00 44.92           C  
ANISOU 9252  CG  ASN C 433     7021   4431   5615   2140   -840    205       C  
ATOM   9253  OD1 ASN C 433     113.838 -39.267-201.299  1.00 51.09           O  
ANISOU 9253  OD1 ASN C 433     7676   5271   6465   2268   -818    160       O  
ATOM   9254  ND2 ASN C 433     112.137 -39.060-199.857  1.00 46.18           N  
ANISOU 9254  ND2 ASN C 433     7190   4617   5740   2033   -896    270       N  
ATOM   9255  N   GLU C 434     110.086 -40.216-204.655  1.00 43.48           N  
ANISOU 9255  N   GLU C 434     7156   4057   5309   1982   -652    101       N  
ATOM   9256  CA  GLU C 434     109.086 -40.949-205.411  1.00 45.77           C  
ANISOU 9256  CA  GLU C 434     7618   4227   5544   1922   -659     93       C  
ATOM   9257  C   GLU C 434     109.522 -41.163-206.848  1.00 48.20           C  
ANISOU 9257  C   GLU C 434     7954   4509   5851   2018   -584      9       C  
ATOM   9258  O   GLU C 434     109.139 -42.163-207.465  1.00 49.87           O  
ANISOU 9258  O   GLU C 434     8337   4587   6026   2038   -611    -12       O  
ATOM   9259  CB  GLU C 434     107.753 -40.214-205.368  1.00 46.89           C  
ANISOU 9259  CB  GLU C 434     7756   4413   5646   1732   -641    130       C  
ATOM   9260  CG  GLU C 434     107.096 -40.265-204.014  1.00 49.66           C  
ANISOU 9260  CG  GLU C 434     8130   4760   5980   1627   -713    213       C  
ATOM   9261  CD  GLU C 434     106.601 -41.652-203.656  1.00 53.25           C  
ANISOU 9261  CD  GLU C 434     8779   5055   6400   1613   -804    253       C  
ATOM   9262  OE1 GLU C 434     105.408 -41.932-203.902  1.00 50.64           O  
ANISOU 9262  OE1 GLU C 434     8546   4666   6030   1485   -816    276       O  
ATOM   9263  OE2 GLU C 434     107.397 -42.461-203.131  1.00 54.99           O  
ANISOU 9263  OE2 GLU C 434     9054   5205   6636   1728   -868    263       O  
ATOM   9264  N   GLN C 435     110.306 -40.234-207.397  1.00 49.54           N  
ANISOU 9264  N   GLN C 435     7967   4802   6055   2071   -489    -38       N  
ATOM   9265  CA  GLN C 435     110.863 -40.461-208.724  1.00 53.92           C  
ANISOU 9265  CA  GLN C 435     8546   5338   6604   2177   -406   -119       C  
ATOM   9266  C   GLN C 435     111.650 -41.761-208.753  1.00 52.39           C  
ANISOU 9266  C   GLN C 435     8448   5028   6428   2350   -449   -151       C  
ATOM   9267  O   GLN C 435     111.489 -42.572-209.671  1.00 48.85           O  
ANISOU 9267  O   GLN C 435     8150   4470   5940   2403   -437   -200       O  
ATOM   9268  CB  GLN C 435     111.743 -39.287-209.143  1.00 45.65           C  
ANISOU 9268  CB  GLN C 435     7301   4447   5598   2213   -296   -156       C  
ATOM   9269  CG  GLN C 435     112.044 -39.249-210.644  1.00 46.39           C  
ANISOU 9269  CG  GLN C 435     7422   4541   5663   2274   -185   -235       C  
ATOM   9270  CD  GLN C 435     110.784 -39.168-211.497  1.00 48.42           C  
ANISOU 9270  CD  GLN C 435     7815   4742   5839   2147   -176   -239       C  
ATOM   9271  OE1 GLN C 435     109.814 -38.482-211.142  1.00 44.88           O  
ANISOU 9271  OE1 GLN C 435     7350   4330   5373   1995   -204   -189       O  
ATOM   9272  NE2 GLN C 435     110.789 -39.877-212.631  1.00 46.13           N  
ANISOU 9272  NE2 GLN C 435     7665   4362   5501   2214   -141   -301       N  
ATOM   9273  N   LYS C 436     112.470 -42.003-207.727  1.00 61.15           N  
ANISOU 9273  N   LYS C 436     9485   6153   7596   2441   -510   -124       N  
ATOM   9274  CA  LYS C 436     113.239 -43.245-207.684  1.00 61.87           C  
ANISOU 9274  CA  LYS C 436     9666   6130   7712   2619   -562   -152       C  
ATOM   9275  C   LYS C 436     112.355 -44.436-207.336  1.00 58.68           C  
ANISOU 9275  C   LYS C 436     9496   5546   7255   2575   -675   -112       C  
ATOM   9276  O   LYS C 436     112.525 -45.524-207.895  1.00 61.30           O  
ANISOU 9276  O   LYS C 436     9948   5775   7568   2641   -686   -153       O  
ATOM   9277  CB  LYS C 436     114.382 -43.115-206.683  1.00 59.89           C  
ANISOU 9277  CB  LYS C 436     9263   5952   7542   2730   -606   -132       C  
ATOM   9278  CG  LYS C 436     115.312 -41.956-206.977  1.00 61.89           C  
ANISOU 9278  CG  LYS C 436     9275   6384   7855   2766   -501   -169       C  
ATOM   9279  CD  LYS C 436     116.033 -41.528-205.718  1.00 66.76           C  
ANISOU 9279  CD  LYS C 436     9737   7089   8539   2789   -571   -122       C  
ATOM   9280  CE  LYS C 436     117.183 -40.591-206.017  1.00 70.10           C  
ANISOU 9280  CE  LYS C 436     9920   7675   9039   2856   -478   -164       C  
ATOM   9281  NZ  LYS C 436     117.808 -40.126-204.751  1.00 76.95           N  
ANISOU 9281  NZ  LYS C 436    10642   8628   9969   2859   -562   -115       N  
ATOM   9282  N   ALA C 437     111.398 -44.246-206.427  1.00 53.49           N  
ANISOU 9282  N   ALA C 437     8873   4883   6569   2414   -743    -30       N  
ATOM   9283  CA  ALA C 437     110.603 -45.371-205.944  1.00 56.99           C  
ANISOU 9283  CA  ALA C 437     9528   5160   6966   2360   -853     21       C  
ATOM   9284  C   ALA C 437     109.599 -45.846-206.990  1.00 64.11           C  
ANISOU 9284  C   ALA C 437    10594   5960   7804   2273   -836     -7       C  
ATOM   9285  O   ALA C 437     109.396 -47.056-207.151  1.00 60.90           O  
ANISOU 9285  O   ALA C 437    10339   5433   7367   2268   -891    -14       O  
ATOM   9286  CB  ALA C 437     109.891 -44.989-204.644  1.00 50.74           C  
ANISOU 9286  CB  ALA C 437     8713   4406   6158   2207   -917    118       C  
ATOM   9287  N   ARG C 438     108.959 -44.916-207.713  1.00 56.26           N  
ANISOU 9287  N   ARG C 438     9537   5053   6787   2161   -756    -26       N  
ATOM   9288  CA  ARG C 438     107.864 -45.264-208.614  1.00 52.36           C  
ANISOU 9288  CA  ARG C 438     9195   4469   6231   2055   -758    -43       C  
ATOM   9289  C   ARG C 438     107.933 -44.606-209.988  1.00 49.65           C  
ANISOU 9289  C   ARG C 438     8806   4190   5867   2068   -650   -119       C  
ATOM   9290  O   ARG C 438     107.033 -44.841-210.801  1.00 50.58           O  
ANISOU 9290  O   ARG C 438     9049   4237   5931   1979   -657   -137       O  
ATOM   9291  CB  ARG C 438     106.503 -44.894-207.990  1.00 60.68           C  
ANISOU 9291  CB  ARG C 438    10256   5542   7258   1838   -801     37       C  
ATOM   9292  CG  ARG C 438     106.183 -45.535-206.665  1.00 65.04           C  
ANISOU 9292  CG  ARG C 438    10878   6025   7810   1784   -902    122       C  
ATOM   9293  CD  ARG C 438     104.674 -45.613-206.445  1.00 57.59           C  
ANISOU 9293  CD  ARG C 438    10013   5043   6824   1575   -942    184       C  
ATOM   9294  NE  ARG C 438     104.077 -44.324-206.129  1.00 50.27           N  
ANISOU 9294  NE  ARG C 438     8920   4274   5906   1447   -887    214       N  
ATOM   9295  CZ  ARG C 438     102.808 -44.164-205.768  1.00 47.08           C  
ANISOU 9295  CZ  ARG C 438     8532   3878   5480   1267   -908    272       C  
ATOM   9296  NH1 ARG C 438     102.017 -45.224-205.668  1.00 50.32           N  
ANISOU 9296  NH1 ARG C 438     9113   4149   5859   1181   -984    309       N  
ATOM   9297  NH2 ARG C 438     102.335 -42.955-205.487  1.00 45.41           N  
ANISOU 9297  NH2 ARG C 438     8163   3812   5279   1173   -854    292       N  
ATOM   9298  N   GLY C 439     108.927 -43.760-210.256  1.00 48.47           N  
ANISOU 9298  N   GLY C 439     8483   4174   5757   2162   -554   -161       N  
ATOM   9299  CA  GLY C 439     109.000 -43.068-211.532  1.00 46.86           C  
ANISOU 9299  CA  GLY C 439     8240   4039   5527   2164   -445   -226       C  
ATOM   9300  C   GLY C 439     108.098 -41.862-211.672  1.00 50.54           C  
ANISOU 9300  C   GLY C 439     8618   4610   5973   1993   -411   -195       C  
ATOM   9301  O   GLY C 439     107.824 -41.434-212.803  1.00 48.72           O  
ANISOU 9301  O   GLY C 439     8412   4401   5700   1962   -346   -240       O  
ATOM   9302  N   GLY C 440     107.633 -41.291-210.571  1.00 46.15           N  
ANISOU 9302  N   GLY C 440     7969   4122   5444   1885   -453   -122       N  
ATOM   9303  CA  GLY C 440     106.747 -40.147-210.640  1.00 47.39           C  
ANISOU 9303  CA  GLY C 440     8042   4376   5587   1731   -425    -93       C  
ATOM   9304  C   GLY C 440     105.971 -39.982-209.351  1.00 49.42           C  
ANISOU 9304  C   GLY C 440     8268   4652   5858   1609   -496    -10       C  
ATOM   9305  O   GLY C 440     106.122 -40.741-208.400  1.00 54.97           O  
ANISOU 9305  O   GLY C 440     9020   5293   6575   1635   -567     30       O  
ATOM   9306  N   CYS C 441     105.126 -38.967-209.350  1.00 52.46           N  
ANISOU 9306  N   CYS C 441     8576   5121   6234   1477   -473     15       N  
ATOM   9307  CA  CYS C 441     104.334 -38.633-208.178  1.00 45.69           C  
ANISOU 9307  CA  CYS C 441     7672   4302   5386   1356   -520     89       C  
ATOM   9308  C   CYS C 441     103.179 -37.741-208.604  1.00 39.85           C  
ANISOU 9308  C   CYS C 441     6893   3620   4628   1217   -497     99       C  
ATOM   9309  O   CYS C 441     103.422 -36.653-209.139  1.00 39.79           O  
ANISOU 9309  O   CYS C 441     6780   3710   4627   1221   -428     69       O  
ATOM   9310  CB  CYS C 441     105.206 -37.934-207.128  1.00 47.92           C  
ANISOU 9310  CB  CYS C 441     7803   4692   5713   1404   -502    111       C  
ATOM   9311  SG  CYS C 441     104.314 -37.299-205.719  1.00 46.80           S  
ANISOU 9311  SG  CYS C 441     7593   4618   5570   1263   -537    191       S  
ATOM   9312  N   PRO C 442     101.923 -38.146-208.402  1.00 38.24           N  
ANISOU 9312  N   PRO C 442     6766   3360   4403   1091   -555    140       N  
ATOM   9313  CA  PRO C 442     100.814 -37.250-208.759  1.00 42.87           C  
ANISOU 9313  CA  PRO C 442     7295   4010   4982    966   -539    150       C  
ATOM   9314  C   PRO C 442     100.772 -36.061-207.810  1.00 39.22           C  
ANISOU 9314  C   PRO C 442     6673   3680   4549    924   -503    184       C  
ATOM   9315  O   PRO C 442     100.821 -36.218-206.581  1.00 34.21           O  
ANISOU 9315  O   PRO C 442     6013   3059   3925    908   -528    232       O  
ATOM   9316  CB  PRO C 442      99.573 -38.134-208.621  1.00 41.43           C  
ANISOU 9316  CB  PRO C 442     7227   3732   4781    848   -615    191       C  
ATOM   9317  CG  PRO C 442      99.967 -39.149-207.574  1.00 38.40           C  
ANISOU 9317  CG  PRO C 442     6914   3275   4400    881   -664    231       C  
ATOM   9318  CD  PRO C 442     101.446 -39.415-207.818  1.00 39.95           C  
ANISOU 9318  CD  PRO C 442     7120   3454   4605   1053   -638    183       C  
ATOM   9319  N   ALA C 443     100.699 -34.869-208.391  1.00 35.13           N  
ANISOU 9319  N   ALA C 443     6059   3252   4036    909   -448    158       N  
ATOM   9320  CA  ALA C 443     100.723 -33.647-207.602  1.00 33.51           C  
ANISOU 9320  CA  ALA C 443     5709   3168   3856    878   -411    180       C  
ATOM   9321  C   ALA C 443      99.884 -32.582-208.287  1.00 41.29           C  
ANISOU 9321  C   ALA C 443     6639   4211   4838    803   -385    169       C  
ATOM   9322  O   ALA C 443      99.924 -32.439-209.509  1.00 35.71           O  
ANISOU 9322  O   ALA C 443     5970   3485   4112    823   -366    128       O  
ATOM   9323  CB  ALA C 443     102.156 -33.144-207.385  1.00 36.41           C  
ANISOU 9323  CB  ALA C 443     5989   3598   4247    987   -364    155       C  
ATOM   9324  N   ASP C 444      99.145 -31.838-207.480  1.00 38.28           N  
ANISOU 9324  N   ASP C 444     6174   3900   4472    724   -384    205       N  
ATOM   9325  CA  ASP C 444      98.204 -30.824-207.928  1.00 37.15           C  
ANISOU 9325  CA  ASP C 444     5972   3811   4333    651   -371    202       C  
ATOM   9326  C   ASP C 444      98.818 -29.467-207.578  1.00 32.54           C  
ANISOU 9326  C   ASP C 444     5266   3330   3767    681   -315    191       C  
ATOM   9327  O   ASP C 444      98.747 -29.021-206.427  1.00 31.36           O  
ANISOU 9327  O   ASP C 444     5047   3237   3632    659   -308    219       O  
ATOM   9328  CB  ASP C 444      96.850 -31.066-207.262  1.00 34.21           C  
ANISOU 9328  CB  ASP C 444     5595   3435   3967    541   -410    249       C  
ATOM   9329  CG  ASP C 444      95.763 -30.123-207.748  1.00 48.02           C  
ANISOU 9329  CG  ASP C 444     7281   5234   5729    471   -408    245       C  
ATOM   9330  OD1 ASP C 444      96.080 -29.001-208.204  1.00 48.05           O  
ANISOU 9330  OD1 ASP C 444     7223   5297   5738    503   -370    217       O  
ATOM   9331  OD2 ASP C 444      94.577 -30.515-207.652  1.00 42.60           O  
ANISOU 9331  OD2 ASP C 444     6606   4528   5051    381   -448    273       O  
ATOM   9332  N   TRP C 445      99.435 -28.831-208.581  1.00 32.53           N  
ANISOU 9332  N   TRP C 445     5252   3349   3760    729   -274    150       N  
ATOM   9333  CA  TRP C 445     100.241 -27.624-208.374  1.00 30.76           C  
ANISOU 9333  CA  TRP C 445     4925   3209   3552    763   -220    136       C  
ATOM   9334  C   TRP C 445      99.476 -26.547-207.616  1.00 32.39           C  
ANISOU 9334  C   TRP C 445     5047   3485   3775    697   -219    160       C  
ATOM   9335  O   TRP C 445     100.002 -25.946-206.670  1.00 33.57           O  
ANISOU 9335  O   TRP C 445     5123   3693   3941    710   -201    168       O  
ATOM   9336  CB  TRP C 445     100.705 -27.090-209.736  1.00 33.05           C  
ANISOU 9336  CB  TRP C 445     5231   3502   3824    796   -176     95       C  
ATOM   9337  CG  TRP C 445     101.747 -25.998-209.689  1.00 29.70           C  
ANISOU 9337  CG  TRP C 445     4716   3154   3417    832   -116     79       C  
ATOM   9338  CD1 TRP C 445     103.098 -26.157-209.824  1.00 32.26           C  
ANISOU 9338  CD1 TRP C 445     5014   3493   3752    911    -72     56       C  
ATOM   9339  CD2 TRP C 445     101.524 -24.586-209.526  1.00 28.35           C  
ANISOU 9339  CD2 TRP C 445     4465   3048   3256    789    -95     84       C  
ATOM   9340  NE1 TRP C 445     103.726 -24.930-209.776  1.00 30.66           N  
ANISOU 9340  NE1 TRP C 445     4719   3365   3566    907    -24     49       N  
ATOM   9341  CE2 TRP C 445     102.784 -23.951-209.598  1.00 29.79           C  
ANISOU 9341  CE2 TRP C 445     4585   3282   3454    834    -40     65       C  
ATOM   9342  CE3 TRP C 445     100.383 -23.799-209.330  1.00 30.72           C  
ANISOU 9342  CE3 TRP C 445     4743   3370   3560    721   -118    101       C  
ATOM   9343  CZ2 TRP C 445     102.945 -22.564-209.437  1.00 26.75           C  
ANISOU 9343  CZ2 TRP C 445     4125   2958   3081    803    -12     66       C  
ATOM   9344  CZ3 TRP C 445     100.531 -22.410-209.162  1.00 29.71           C  
ANISOU 9344  CZ3 TRP C 445     4543   3302   3444    704    -90     98       C  
ATOM   9345  CH2 TRP C 445     101.806 -21.803-209.231  1.00 28.78           C  
ANISOU 9345  CH2 TRP C 445     4375   3224   3335    740    -40     81       C  
ATOM   9346  N   ALA C 446      98.215 -26.315-208.000  1.00 28.00           N  
ANISOU 9346  N   ALA C 446     4502   2921   3215    628   -243    168       N  
ATOM   9347  CA  ALA C 446      97.393 -25.278-207.381  1.00 30.65           C  
ANISOU 9347  CA  ALA C 446     4757   3320   3569    575   -238    184       C  
ATOM   9348  C   ALA C 446      97.233 -25.487-205.870  1.00 33.02           C  
ANISOU 9348  C   ALA C 446     5019   3651   3877    553   -242    218       C  
ATOM   9349  O   ALA C 446      97.078 -24.512-205.125  1.00 32.04           O  
ANISOU 9349  O   ALA C 446     4822   3590   3762    539   -220    222       O  
ATOM   9350  CB  ALA C 446      96.015 -25.242-208.049  1.00 32.35           C  
ANISOU 9350  CB  ALA C 446     4989   3515   3786    512   -275    189       C  
ATOM   9351  N   TRP C 447      97.232 -26.738-205.410  1.00 28.20           N  
ANISOU 9351  N   TRP C 447     4469   2989   3256    547   -271    242       N  
ATOM   9352  CA  TRP C 447      97.091 -27.026-203.984  1.00 30.69           C  
ANISOU 9352  CA  TRP C 447     4768   3325   3566    521   -275    280       C  
ATOM   9353  C   TRP C 447      98.427 -27.190-203.270  1.00 31.90           C  
ANISOU 9353  C   TRP C 447     4920   3486   3714    591   -272    280       C  
ATOM   9354  O   TRP C 447      98.511 -26.908-202.065  1.00 35.27           O  
ANISOU 9354  O   TRP C 447     5314   3955   4131    580   -267    301       O  
ATOM   9355  CB  TRP C 447      96.233 -28.276-203.785  1.00 30.01           C  
ANISOU 9355  CB  TRP C 447     4755   3176   3471    460   -314    317       C  
ATOM   9356  CG  TRP C 447      94.759 -28.023-203.992  1.00 37.35           C  
ANISOU 9356  CG  TRP C 447     5652   4124   4415    372   -320    329       C  
ATOM   9357  CD1 TRP C 447      94.146 -27.600-205.155  1.00 42.85           C  
ANISOU 9357  CD1 TRP C 447     6337   4817   5128    355   -332    305       C  
ATOM   9358  CD2 TRP C 447      93.711 -28.188-203.029  1.00 42.15           C  
ANISOU 9358  CD2 TRP C 447     6231   4761   5025    291   -314    371       C  
ATOM   9359  NE1 TRP C 447      92.789 -27.496-204.957  1.00 36.79           N  
ANISOU 9359  NE1 TRP C 447     5523   4074   4381    272   -342    327       N  
ATOM   9360  CE2 TRP C 447      92.497 -27.846-203.665  1.00 43.93           C  
ANISOU 9360  CE2 TRP C 447     6411   5003   5278    230   -324    367       C  
ATOM   9361  CE3 TRP C 447      93.676 -28.612-201.692  1.00 58.09           C  
ANISOU 9361  CE3 TRP C 447     8259   6792   7020    261   -302    412       C  
ATOM   9362  CZ2 TRP C 447      91.264 -27.905-203.008  1.00 58.32           C  
ANISOU 9362  CZ2 TRP C 447     8181   6862   7115    143   -313    401       C  
ATOM   9363  CZ3 TRP C 447      92.448 -28.664-201.038  1.00 63.93           C  
ANISOU 9363  CZ3 TRP C 447     8960   7566   7764    170   -284    447       C  
ATOM   9364  CH2 TRP C 447      91.261 -28.309-201.701  1.00 56.40           C  
ANISOU 9364  CH2 TRP C 447     7945   6637   6847    113   -286    440       C  
ATOM   9365  N   ILE C 448      99.483 -27.547-203.987  1.00 31.28           N  
ANISOU 9365  N   ILE C 448     4871   3375   3641    665   -272    253       N  
ATOM   9366  CA  ILE C 448     100.786 -27.746-203.360  1.00 34.17           C  
ANISOU 9366  CA  ILE C 448     5222   3751   4012    738   -276    251       C  
ATOM   9367  C   ILE C 448     101.462 -26.408-203.074  1.00 37.45           C  
ANISOU 9367  C   ILE C 448     5537   4250   4443    756   -242    231       C  
ATOM   9368  O   ILE C 448     102.058 -26.215-202.008  1.00 33.99           O  
ANISOU 9368  O   ILE C 448     5063   3847   4005    774   -255    244       O  
ATOM   9369  CB  ILE C 448     101.646 -28.660-204.258  1.00 36.85           C  
ANISOU 9369  CB  ILE C 448     5620   4025   4355    818   -283    226       C  
ATOM   9370  CG1 ILE C 448     101.064 -30.077-204.311  1.00 38.35           C  
ANISOU 9370  CG1 ILE C 448     5927   4118   4526    800   -330    249       C  
ATOM   9371  CG2 ILE C 448     103.110 -28.695-203.793  1.00 33.74           C  
ANISOU 9371  CG2 ILE C 448     5182   3655   3982    908   -282    215       C  
ATOM   9372  CD1 ILE C 448     101.156 -30.840-202.957  1.00 35.94           C  
ANISOU 9372  CD1 ILE C 448     5659   3789   4210    797   -375    296       C  
ATOM   9373  N   VAL C 449     101.349 -25.452-203.994  1.00 31.63           N  
ANISOU 9373  N   VAL C 449     4760   3541   3715    746   -204    201       N  
ATOM   9374  CA  VAL C 449     101.886 -24.106-203.798  1.00 26.37           C  
ANISOU 9374  CA  VAL C 449     4009   2946   3063    749   -174    184       C  
ATOM   9375  C   VAL C 449     101.115 -23.386-202.690  1.00 32.19           C  
ANISOU 9375  C   VAL C 449     4713   3727   3791    694   -179    203       C  
ATOM   9376  O   VAL C 449      99.878 -23.283-202.751  1.00 32.36           O  
ANISOU 9376  O   VAL C 449     4748   3744   3803    640   -179    214       O  
ATOM   9377  CB  VAL C 449     101.866 -23.316-205.128  1.00 28.17           C  
ANISOU 9377  CB  VAL C 449     4227   3181   3297    746   -135    153       C  
ATOM   9378  CG1 VAL C 449     102.406 -21.914-204.903  1.00 30.06           C  
ANISOU 9378  CG1 VAL C 449     4387   3483   3549    739   -107    138       C  
ATOM   9379  CG2 VAL C 449     102.708 -24.043-206.166  1.00 29.29           C  
ANISOU 9379  CG2 VAL C 449     4406   3284   3438    807   -117    130       C  
ATOM   9380  N   PRO C 450     101.800 -22.901-201.652  1.00 31.51           N  
ANISOU 9380  N   PRO C 450     4583   3685   3705    706   -186    206       N  
ATOM   9381  CA  PRO C 450     101.122 -22.263-200.504  1.00 35.49           C  
ANISOU 9381  CA  PRO C 450     5068   4229   4188    660   -188    220       C  
ATOM   9382  C   PRO C 450     100.354 -21.015-200.903  1.00 35.70           C  
ANISOU 9382  C   PRO C 450     5059   4286   4221    624   -156    200       C  
ATOM   9383  O   PRO C 450     100.690 -20.361-201.908  1.00 35.41           O  
ANISOU 9383  O   PRO C 450     5000   4249   4203    637   -136    174       O  
ATOM   9384  CB  PRO C 450     102.280 -21.908-199.558  1.00 36.77           C  
ANISOU 9384  CB  PRO C 450     5195   4426   4349    690   -208    218       C  
ATOM   9385  CG  PRO C 450     103.455 -22.698-200.041  1.00 48.21           C  
ANISOU 9385  CG  PRO C 450     6644   5850   5822    754   -226    213       C  
ATOM   9386  CD  PRO C 450     103.257 -22.994-201.503  1.00 29.07           C  
ANISOU 9386  CD  PRO C 450     4240   3390   3415    766   -196    195       C  
ATOM   9387  N   PRO C 451      99.340 -20.632-200.117  1.00 32.51           N  
ANISOU 9387  N   PRO C 451     4648   3905   3797    583   -148    210       N  
ATOM   9388  CA  PRO C 451      98.508 -19.469-200.460  1.00 31.20           C  
ANISOU 9388  CA  PRO C 451     4450   3764   3642    560   -122    189       C  
ATOM   9389  C   PRO C 451      99.115 -18.112-200.131  1.00 32.46           C  
ANISOU 9389  C   PRO C 451     4571   3959   3803    571   -112    161       C  
ATOM   9390  O   PRO C 451      98.481 -17.093-200.419  1.00 40.46           O  
ANISOU 9390  O   PRO C 451     5566   4984   4825    560    -95    142       O  
ATOM   9391  CB  PRO C 451      97.250 -19.707-199.628  1.00 35.07           C  
ANISOU 9391  CB  PRO C 451     4942   4270   4113    519   -111    210       C  
ATOM   9392  CG  PRO C 451      97.816 -20.342-198.329  1.00 31.33           C  
ANISOU 9392  CG  PRO C 451     4497   3804   3602    522   -125    235       C  
ATOM   9393  CD  PRO C 451      98.929 -21.251-198.830  1.00 33.85           C  
ANISOU 9393  CD  PRO C 451     4846   4082   3933    560   -158    242       C  
ATOM   9394  N   ILE C 452     100.286 -18.050-199.508  1.00 31.86           N  
ANISOU 9394  N   ILE C 452     4486   3897   3720    592   -128    158       N  
ATOM   9395  CA  ILE C 452     101.053 -16.816-199.431  1.00 34.29           C  
ANISOU 9395  CA  ILE C 452     4761   4230   4038    595   -126    131       C  
ATOM   9396  C   ILE C 452     102.462 -17.148-199.879  1.00 38.82           C  
ANISOU 9396  C   ILE C 452     5313   4801   4637    624   -139    129       C  
ATOM   9397  O   ILE C 452     102.917 -18.292-199.754  1.00 34.29           O  
ANISOU 9397  O   ILE C 452     4752   4213   4064    651   -158    147       O  
ATOM   9398  CB  ILE C 452     101.078 -16.163-198.022  1.00 31.15           C  
ANISOU 9398  CB  ILE C 452     4364   3865   3608    583   -138    124       C  
ATOM   9399  CG1 ILE C 452     101.519 -17.176-196.956  1.00 33.58           C  
ANISOU 9399  CG1 ILE C 452     4696   4177   3887    592   -171    151       C  
ATOM   9400  CG2 ILE C 452      99.736 -15.517-197.718  1.00 35.22           C  
ANISOU 9400  CG2 ILE C 452     4887   4390   4105    563   -110    114       C  
ATOM   9401  CD1 ILE C 452     101.886 -16.542-195.620  1.00 40.39           C  
ANISOU 9401  CD1 ILE C 452     5568   5069   4710    584   -195    142       C  
ATOM   9402  N   SER C 453     103.136 -16.144-200.449  1.00 40.09           N  
ANISOU 9402  N   SER C 453     5440   4972   4819    618   -126    106       N  
ATOM   9403  CA  SER C 453     104.549 -16.263-200.810  1.00 40.57           C  
ANISOU 9403  CA  SER C 453     5458   5046   4910    640   -128    100       C  
ATOM   9404  C   SER C 453     104.806 -17.449-201.745  1.00 31.39           C  
ANISOU 9404  C   SER C 453     4308   3857   3761    680   -113    109       C  
ATOM   9405  O   SER C 453     105.836 -18.120-201.650  1.00 34.69           O  
ANISOU 9405  O   SER C 453     4697   4283   4200    719   -125    111       O  
ATOM   9406  CB  SER C 453     105.409 -16.370-199.556  1.00 43.54           C  
ANISOU 9406  CB  SER C 453     5806   5451   5284    650   -174    105       C  
ATOM   9407  OG  SER C 453     105.223 -15.215-198.749  1.00 45.33           O  
ANISOU 9407  OG  SER C 453     6034   5697   5493    613   -188     91       O  
ATOM   9408  N   GLY C 454     103.863 -17.711-202.646  1.00 33.51           N  
ANISOU 9408  N   GLY C 454     4621   4092   4019    673    -91    110       N  
ATOM   9409  CA  GLY C 454     103.998 -18.824-203.575  1.00 28.71           C  
ANISOU 9409  CA  GLY C 454     4046   3449   3415    708    -78    113       C  
ATOM   9410  C   GLY C 454     105.391 -19.028-204.153  1.00 29.15           C  
ANISOU 9410  C   GLY C 454     4062   3518   3497    750    -54     99       C  
ATOM   9411  O   GLY C 454     105.994 -20.095-203.972  1.00 32.57           O  
ANISOU 9411  O   GLY C 454     4495   3940   3941    801    -69    104       O  
ATOM   9412  N   SER C 455     105.929 -17.998-204.816  1.00 29.43           N  
ANISOU 9412  N   SER C 455     4060   3577   3545    730    -15     82       N  
ATOM   9413  CA  SER C 455     107.156 -18.151-205.588  1.00 29.54           C  
ANISOU 9413  CA  SER C 455     4031   3609   3583    763     28     67       C  
ATOM   9414  C   SER C 455     108.403 -18.091-204.731  1.00 29.83           C  
ANISOU 9414  C   SER C 455     3978   3694   3660    784      8     66       C  
ATOM   9415  O   SER C 455     109.497 -18.363-205.245  1.00 32.34           O  
ANISOU 9415  O   SER C 455     4241   4036   4010    821     43     54       O  
ATOM   9416  CB  SER C 455     107.237 -17.093-206.704  1.00 32.06           C  
ANISOU 9416  CB  SER C 455     4354   3933   3895    723     83     56       C  
ATOM   9417  OG  SER C 455     107.504 -15.799-206.198  1.00 29.92           O  
ANISOU 9417  OG  SER C 455     4036   3694   3637    671     77     55       O  
ATOM   9418  N   LEU C 456     108.262 -17.766-203.436  1.00 32.57           N  
ANISOU 9418  N   LEU C 456     4310   4059   4007    762    -48     78       N  
ATOM   9419  CA  LEU C 456     109.351 -17.897-202.482  1.00 31.01           C  
ANISOU 9419  CA  LEU C 456     4039   3900   3843    785    -91     80       C  
ATOM   9420  C   LEU C 456     109.585 -19.347-202.063  1.00 38.79           C  
ANISOU 9420  C   LEU C 456     5042   4865   4833    858   -130     93       C  
ATOM   9421  O   LEU C 456     110.559 -19.619-201.353  1.00 37.80           O  
ANISOU 9421  O   LEU C 456     4855   4767   4738    893   -174     96       O  
ATOM   9422  CB  LEU C 456     109.067 -17.039-201.225  1.00 29.20           C  
ANISOU 9422  CB  LEU C 456     3809   3689   3596    735   -144     86       C  
ATOM   9423  CG  LEU C 456     108.578 -15.594-201.459  1.00 31.64           C  
ANISOU 9423  CG  LEU C 456     4129   4002   3892    666   -120     73       C  
ATOM   9424  CD1 LEU C 456     108.569 -14.808-200.136  1.00 29.67           C  
ANISOU 9424  CD1 LEU C 456     3875   3770   3627    629   -175     71       C  
ATOM   9425  CD2 LEU C 456     109.434 -14.899-202.504  1.00 33.56           C  
ANISOU 9425  CD2 LEU C 456     4316   4266   4169    643    -67     60       C  
ATOM   9426  N   THR C 457     108.708 -20.272-202.461  1.00 33.49           N  
ANISOU 9426  N   THR C 457     4455   4140   4132    879   -123    101       N  
ATOM   9427  CA  THR C 457     108.856 -21.682-202.147  1.00 33.88           C  
ANISOU 9427  CA  THR C 457     4542   4151   4180    945   -161    115       C  
ATOM   9428  C   THR C 457     109.279 -22.448-203.399  1.00 36.29           C  
ANISOU 9428  C   THR C 457     4859   4429   4502   1006   -112     95       C  
ATOM   9429  O   THR C 457     109.000 -22.017-204.525  1.00 37.02           O  
ANISOU 9429  O   THR C 457     4966   4517   4583    983    -50     77       O  
ATOM   9430  CB  THR C 457     107.559 -22.278-201.569  1.00 37.65           C  
ANISOU 9430  CB  THR C 457     5116   4580   4609    917   -195    142       C  
ATOM   9431  OG1 THR C 457     106.524 -22.275-202.552  1.00 40.91           O  
ANISOU 9431  OG1 THR C 457     5587   4957   4999    886   -154    136       O  
ATOM   9432  CG2 THR C 457     107.080 -21.475-200.326  1.00 32.19           C  
ANISOU 9432  CG2 THR C 457     4419   3919   3891    859   -229    157       C  
ATOM   9433  N   PRO C 458     110.011 -23.553-203.243  1.00 32.41           N  
ANISOU 9433  N   PRO C 458     4363   3918   4032   1090   -138     95       N  
ATOM   9434  CA  PRO C 458     110.567 -24.230-204.426  1.00 36.39           C  
ANISOU 9434  CA  PRO C 458     4872   4401   4553   1161    -83     67       C  
ATOM   9435  C   PRO C 458     109.533 -24.968-205.258  1.00 36.13           C  
ANISOU 9435  C   PRO C 458     4964   4290   4473   1158    -66     64       C  
ATOM   9436  O   PRO C 458     109.795 -25.235-206.443  1.00 39.49           O  
ANISOU 9436  O   PRO C 458     5410   4699   4895   1196     -5     35       O  
ATOM   9437  CB  PRO C 458     111.591 -25.202-203.829  1.00 39.43           C  
ANISOU 9437  CB  PRO C 458     5221   4782   4980   1260   -132     68       C  
ATOM   9438  CG  PRO C 458     111.142 -25.405-202.395  1.00 37.85           C  
ANISOU 9438  CG  PRO C 458     5056   4566   4759   1234   -225    107       C  
ATOM   9439  CD  PRO C 458     110.519 -24.111-201.978  1.00 34.36           C  
ANISOU 9439  CD  PRO C 458     4594   4168   4295   1129   -219    117       C  
ATOM   9440  N   VAL C 459     108.372 -25.302-204.688  1.00 35.48           N  
ANISOU 9440  N   VAL C 459     4965   4162   4354   1110   -116     93       N  
ATOM   9441  CA  VAL C 459     107.353 -26.008-205.459  1.00 34.96           C  
ANISOU 9441  CA  VAL C 459     5012   4023   4248   1095   -111     92       C  
ATOM   9442  C   VAL C 459     106.774 -25.116-206.549  1.00 34.51           C  
ANISOU 9442  C   VAL C 459     4963   3978   4169   1039    -54     74       C  
ATOM   9443  O   VAL C 459     106.303 -25.614-207.577  1.00 34.80           O  
ANISOU 9443  O   VAL C 459     5082   3962   4178   1044    -36     59       O  
ATOM   9444  CB  VAL C 459     106.250 -26.555-204.536  1.00 30.86           C  
ANISOU 9444  CB  VAL C 459     4565   3459   3700   1046   -175    132       C  
ATOM   9445  CG1 VAL C 459     106.801 -27.713-203.682  1.00 30.32           C  
ANISOU 9445  CG1 VAL C 459     4528   3351   3640   1111   -235    152       C  
ATOM   9446  CG2 VAL C 459     105.687 -25.461-203.639  1.00 30.07           C  
ANISOU 9446  CG2 VAL C 459     4416   3415   3592    967   -184    152       C  
ATOM   9447  N   PHE C 460     106.813 -23.796-206.360  1.00 35.75           N  
ANISOU 9447  N   PHE C 460     5049   4199   4337    986    -33     75       N  
ATOM   9448  CA  PHE C 460     106.283 -22.882-207.376  1.00 31.94           C  
ANISOU 9448  CA  PHE C 460     4581   3723   3831    934     13     61       C  
ATOM   9449  C   PHE C 460     106.967 -23.087-208.713  1.00 34.77           C  
ANISOU 9449  C   PHE C 460     4957   4072   4182    979     78     30       C  
ATOM   9450  O   PHE C 460     106.320 -23.017-209.763  1.00 32.92           O  
ANISOU 9450  O   PHE C 460     4796   3802   3909    956    100     19       O  
ATOM   9451  CB  PHE C 460     106.453 -21.439-206.910  1.00 29.98           C  
ANISOU 9451  CB  PHE C 460     4253   3539   3600    881     24     65       C  
ATOM   9452  CG  PHE C 460     105.878 -20.415-207.864  1.00 32.59           C  
ANISOU 9452  CG  PHE C 460     4607   3869   3906    828     60     57       C  
ATOM   9453  CD1 PHE C 460     106.626 -19.940-208.929  1.00 33.18           C  
ANISOU 9453  CD1 PHE C 460     4668   3961   3979    835    126     37       C  
ATOM   9454  CD2 PHE C 460     104.601 -19.915-207.659  1.00 29.76           C  
ANISOU 9454  CD2 PHE C 460     4282   3495   3528    772     29     71       C  
ATOM   9455  CE1 PHE C 460     106.103 -18.995-209.798  1.00 38.57           C  
ANISOU 9455  CE1 PHE C 460     5387   4636   4632    784    152     35       C  
ATOM   9456  CE2 PHE C 460     104.080 -18.956-208.535  1.00 31.41           C  
ANISOU 9456  CE2 PHE C 460     4518   3700   3718    731     51     65       C  
ATOM   9457  CZ  PHE C 460     104.830 -18.513-209.594  1.00 31.61           C  
ANISOU 9457  CZ  PHE C 460     4544   3732   3733    736    108     49       C  
ATOM   9458  N   HIS C 461     108.274 -23.318-208.700  1.00 30.87           N  
ANISOU 9458  N   HIS C 461     4395   3611   3723   1045    111     13       N  
ATOM   9459  CA  HIS C 461     109.046 -23.473-209.926  1.00 35.37           C  
ANISOU 9459  CA  HIS C 461     4969   4184   4285   1093    191    -21       C  
ATOM   9460  C   HIS C 461     109.104 -24.907-210.443  1.00 39.85           C  
ANISOU 9460  C   HIS C 461     5624   4683   4835   1176    190    -41       C  
ATOM   9461  O   HIS C 461     109.809 -25.158-211.422  1.00 40.89           O  
ANISOU 9461  O   HIS C 461     5764   4817   4958   1232    263    -75       O  
ATOM   9462  CB  HIS C 461     110.461 -22.949-209.696  1.00 37.10           C  
ANISOU 9462  CB  HIS C 461     5053   4483   4559   1122    237    -31       C  
ATOM   9463  CG  HIS C 461     110.483 -21.618-209.021  1.00 40.85           C  
ANISOU 9463  CG  HIS C 461     5449   5017   5056   1042    222    -11       C  
ATOM   9464  ND1 HIS C 461     110.260 -20.439-209.699  1.00 39.83           N  
ANISOU 9464  ND1 HIS C 461     5322   4907   4904    968    270    -11       N  
ATOM   9465  CD2 HIS C 461     110.648 -21.281-207.720  1.00 42.39           C  
ANISOU 9465  CD2 HIS C 461     5576   5245   5286   1022    159      9       C  
ATOM   9466  CE1 HIS C 461     110.306 -19.430-208.846  1.00 39.37           C  
ANISOU 9466  CE1 HIS C 461     5200   4890   4871    909    237      6       C  
ATOM   9467  NE2 HIS C 461     110.538 -19.915-207.638  1.00 41.56           N  
ANISOU 9467  NE2 HIS C 461     5434   5178   5181    939    171     17       N  
ATOM   9468  N   GLN C 462     108.375 -25.835-209.827  1.00 35.67           N  
ANISOU 9468  N   GLN C 462     5167   4091   4297   1182    114    -23       N  
ATOM   9469  CA  GLN C 462     108.382 -27.247-210.199  1.00 34.16           C  
ANISOU 9469  CA  GLN C 462     5073   3818   4087   1257     97    -40       C  
ATOM   9470  C   GLN C 462     107.148 -27.573-211.037  1.00 34.11           C  
ANISOU 9470  C   GLN C 462     5202   3737   4021   1206     80    -43       C  
ATOM   9471  O   GLN C 462     106.015 -27.424-210.566  1.00 34.30           O  
ANISOU 9471  O   GLN C 462     5257   3742   4033   1127     22    -11       O  
ATOM   9472  CB  GLN C 462     108.410 -28.108-208.933  1.00 33.51           C  
ANISOU 9472  CB  GLN C 462     4993   3706   4032   1289     15    -12       C  
ATOM   9473  CG  GLN C 462     108.416 -29.604-209.183  1.00 33.90           C  
ANISOU 9473  CG  GLN C 462     5155   3658   4066   1366    -16    -25       C  
ATOM   9474  CD  GLN C 462     109.583 -30.030-210.009  1.00 42.37           C  
ANISOU 9474  CD  GLN C 462     6212   4733   5154   1480     51    -74       C  
ATOM   9475  OE1 GLN C 462     110.725 -29.937-209.576  1.00 38.05           O  
ANISOU 9475  OE1 GLN C 462     5554   4242   4660   1550     67    -82       O  
ATOM   9476  NE2 GLN C 462     109.310 -30.482-211.233  1.00 38.10           N  
ANISOU 9476  NE2 GLN C 462     5779   4133   4564   1500     91   -110       N  
ATOM   9477  N   GLU C 463     107.353 -28.018-212.271  1.00 39.56           N  
ANISOU 9477  N   GLU C 463     5972   4386   4673   1251    129    -82       N  
ATOM   9478  CA  GLU C 463     106.224 -28.541-213.028  1.00 35.98           C  
ANISOU 9478  CA  GLU C 463     5660   3848   4161   1211     94    -87       C  
ATOM   9479  C   GLU C 463     105.730 -29.839-212.390  1.00 35.97           C  
ANISOU 9479  C   GLU C 463     5741   3761   4164   1226     10    -70       C  
ATOM   9480  O   GLU C 463     106.509 -30.622-211.844  1.00 35.52           O  
ANISOU 9480  O   GLU C 463     5672   3686   4137   1309     -1    -75       O  
ATOM   9481  CB  GLU C 463     106.615 -28.763-214.488  1.00 32.87           C  
ANISOU 9481  CB  GLU C 463     5350   3426   3715   1259    164   -136       C  
ATOM   9482  CG  GLU C 463     106.870 -27.450-215.224  1.00 33.29           C  
ANISOU 9482  CG  GLU C 463     5351   3551   3748   1218    243   -143       C  
ATOM   9483  CD  GLU C 463     107.349 -27.662-216.644  1.00 40.79           C  
ANISOU 9483  CD  GLU C 463     6386   4477   4635   1268    326   -192       C  
ATOM   9484  OE1 GLU C 463     107.735 -28.812-216.974  1.00 43.44           O  
ANISOU 9484  OE1 GLU C 463     6798   4753   4955   1355    336   -227       O  
ATOM   9485  OE2 GLU C 463     107.333 -26.681-217.423  1.00 45.13           O  
ANISOU 9485  OE2 GLU C 463     6937   5065   5147   1220    382   -194       O  
ATOM   9486  N   MET C 464     104.418 -30.055-212.443  1.00 35.59           N  
ANISOU 9486  N   MET C 464     5775   3660   4088   1143    -54    -48       N  
ATOM   9487  CA  MET C 464     103.811 -31.227-211.836  1.00 39.19           C  
ANISOU 9487  CA  MET C 464     6314   4032   4544   1131   -135    -24       C  
ATOM   9488  C   MET C 464     102.825 -31.873-212.796  1.00 45.37           C  
ANISOU 9488  C   MET C 464     7241   4722   5276   1087   -176    -38       C  
ATOM   9489  O   MET C 464     102.317 -31.238-213.720  1.00 48.03           O  
ANISOU 9489  O   MET C 464     7599   5070   5579   1040   -160    -53       O  
ATOM   9490  CB  MET C 464     103.117 -30.861-210.513  1.00 41.06           C  
ANISOU 9490  CB  MET C 464     6482   4308   4813   1051   -186     32       C  
ATOM   9491  CG  MET C 464     104.081 -30.324-209.482  1.00 40.12           C  
ANISOU 9491  CG  MET C 464     6237   4268   4737   1093   -163     45       C  
ATOM   9492  SD  MET C 464     103.279 -29.725-207.976  1.00 40.37           S  
ANISOU 9492  SD  MET C 464     6196   4354   4789    999   -208    103       S  
ATOM   9493  CE  MET C 464     104.669 -28.883-207.206  1.00 37.44           C  
ANISOU 9493  CE  MET C 464     5686   4080   4461   1060   -172     98       C  
ATOM   9494  N   VAL C 465     102.576 -33.163-212.566  1.00 38.72           N  
ANISOU 9494  N   VAL C 465     6505   3781   4426   1100   -238    -32       N  
ATOM   9495  CA  VAL C 465     101.594 -33.945-213.313  1.00 39.50           C  
ANISOU 9495  CA  VAL C 465     6751   3777   4481   1047   -297    -40       C  
ATOM   9496  C   VAL C 465     100.547 -34.448-212.328  1.00 40.60           C  
ANISOU 9496  C   VAL C 465     6904   3880   4640    951   -381     18       C  
ATOM   9497  O   VAL C 465     100.892 -35.060-211.310  1.00 37.74           O  
ANISOU 9497  O   VAL C 465     6538   3499   4304    979   -405     46       O  
ATOM   9498  CB  VAL C 465     102.253 -35.126-214.048  1.00 40.35           C  
ANISOU 9498  CB  VAL C 465     6997   3780   4553   1148   -294    -90       C  
ATOM   9499  CG1 VAL C 465     101.266 -35.795-214.992  1.00 43.42           C  
ANISOU 9499  CG1 VAL C 465     7547   4064   4887   1088   -356   -107       C  
ATOM   9500  CG2 VAL C 465     103.477 -34.667-214.775  1.00 41.33           C  
ANISOU 9500  CG2 VAL C 465     7081   3957   4667   1256   -193   -142       C  
ATOM   9501  N   ASN C 466      99.277 -34.212-212.639  1.00 37.62           N  
ANISOU 9501  N   ASN C 466     6547   3496   4252    839   -427     36       N  
ATOM   9502  CA  ASN C 466      98.170 -34.603-211.779  1.00 36.82           C  
ANISOU 9502  CA  ASN C 466     6445   3374   4172    731   -495     92       C  
ATOM   9503  C   ASN C 466      97.398 -35.757-212.401  1.00 42.27           C  
ANISOU 9503  C   ASN C 466     7290   3939   4832    678   -573     87       C  
ATOM   9504  O   ASN C 466      97.034 -35.695-213.586  1.00 42.72           O  
ANISOU 9504  O   ASN C 466     7417   3963   4854    662   -589     51       O  
ATOM   9505  CB  ASN C 466      97.238 -33.421-211.519  1.00 39.92           C  
ANISOU 9505  CB  ASN C 466     6716   3863   4589    638   -490    120       C  
ATOM   9506  CG  ASN C 466      96.247 -33.710-210.414  1.00 46.38           C  
ANISOU 9506  CG  ASN C 466     7501   4686   5435    537   -535    180       C  
ATOM   9507  OD1 ASN C 466      96.380 -34.699-209.699  1.00 46.05           O  
ANISOU 9507  OD1 ASN C 466     7519   4585   5395    536   -564    207       O  
ATOM   9508  ND2 ASN C 466      95.251 -32.852-210.269  1.00 53.97           N  
ANISOU 9508  ND2 ASN C 466     8369   5717   6419    453   -538    201       N  
ATOM   9509  N   TYR C 467      97.171 -36.816-211.608  1.00 37.95           N  
ANISOU 9509  N   TYR C 467     6808   3319   4294    648   -626    124       N  
ATOM   9510  CA  TYR C 467      96.452 -38.006-212.063  1.00 38.18           C  
ANISOU 9510  CA  TYR C 467     6992   3216   4297    586   -710    126       C  
ATOM   9511  C   TYR C 467      96.009 -38.815-210.848  1.00 44.56           C  
ANISOU 9511  C   TYR C 467     7824   3980   5128    516   -759    191       C  
ATOM   9512  O   TYR C 467      96.501 -38.617-209.738  1.00 41.34           O  
ANISOU 9512  O   TYR C 467     7339   3627   4743    547   -727    224       O  
ATOM   9513  CB  TYR C 467      97.309 -38.860-213.001  1.00 41.19           C  
ANISOU 9513  CB  TYR C 467     7527   3490   4634    698   -711     64       C  
ATOM   9514  CG  TYR C 467      98.709 -39.154-212.498  1.00 43.66           C  
ANISOU 9514  CG  TYR C 467     7832   3801   4957    844   -661     47       C  
ATOM   9515  CD1 TYR C 467      99.740 -38.244-212.696  1.00 42.40           C  
ANISOU 9515  CD1 TYR C 467     7564   3740   4806    946   -571     13       C  
ATOM   9516  CD2 TYR C 467      99.007 -40.352-211.854  1.00 43.87           C  
ANISOU 9516  CD2 TYR C 467     7960   3723   4985    878   -710     67       C  
ATOM   9517  CE1 TYR C 467     101.020 -38.504-212.270  1.00 41.73           C  
ANISOU 9517  CE1 TYR C 467     7456   3661   4739   1078   -531     -3       C  
ATOM   9518  CE2 TYR C 467     100.294 -40.621-211.404  1.00 47.55           C  
ANISOU 9518  CE2 TYR C 467     8412   4188   5466   1021   -675     52       C  
ATOM   9519  CZ  TYR C 467     101.295 -39.693-211.608  1.00 47.90           C  
ANISOU 9519  CZ  TYR C 467     8332   4342   5527   1121   -586     16       C  
ATOM   9520  OH  TYR C 467     102.578 -39.943-211.177  1.00 41.54           O  
ANISOU 9520  OH  TYR C 467     7494   3543   4745   1262   -555     -1       O  
ATOM   9521  N   PHE C 468      95.084 -39.747-211.079  1.00 43.25           N  
ANISOU 9521  N   PHE C 468     7773   3711   4950    416   -840    209       N  
ATOM   9522  CA  PHE C 468      94.400 -40.470-210.015  1.00 49.60           C  
ANISOU 9522  CA  PHE C 468     8600   4473   5770    310   -888    280       C  
ATOM   9523  C   PHE C 468      94.911 -41.905-209.944  1.00 47.24           C  
ANISOU 9523  C   PHE C 468     8486   4018   5444    358   -943    278       C  
ATOM   9524  O   PHE C 468      94.736 -42.682-210.890  1.00 40.89           O  
ANISOU 9524  O   PHE C 468     7831   3095   4610    353   -999    242       O  
ATOM   9525  CB  PHE C 468      92.884 -40.459-210.231  1.00 57.65           C  
ANISOU 9525  CB  PHE C 468     9602   5496   6807    141   -943    312       C  
ATOM   9526  CG  PHE C 468      92.111 -41.292-209.222  1.00 67.72           C  
ANISOU 9526  CG  PHE C 468    10912   6723   8097     13   -989    387       C  
ATOM   9527  CD1 PHE C 468      91.532 -40.698-208.108  1.00 61.78           C  
ANISOU 9527  CD1 PHE C 468    10017   6080   7378    -68   -948    446       C  
ATOM   9528  CD2 PHE C 468      91.953 -42.668-209.397  1.00 72.32           C  
ANISOU 9528  CD2 PHE C 468    11677   7145   8655    -29  -1070    397       C  
ATOM   9529  CE1 PHE C 468      90.820 -41.456-207.188  1.00 62.61           C  
ANISOU 9529  CE1 PHE C 468    10156   6144   7489   -192   -979    519       C  
ATOM   9530  CE2 PHE C 468      91.251 -43.430-208.474  1.00 68.77           C  
ANISOU 9530  CE2 PHE C 468    11266   6647   8215   -157  -1109    472       C  
ATOM   9531  CZ  PHE C 468      90.680 -42.823-207.374  1.00 59.31           C  
ANISOU 9531  CZ  PHE C 468     9920   5568   7048   -241  -1059    534       C  
ATOM   9532  N   LEU C 469      95.506 -42.264-208.811  1.00 43.12           N  
ANISOU 9532  N   LEU C 469     7964   3488   4929    401   -933    319       N  
ATOM   9533  CA  LEU C 469      95.866 -43.645-208.536  1.00 51.42           C  
ANISOU 9533  CA  LEU C 469     9192   4386   5960    433   -996    333       C  
ATOM   9534  C   LEU C 469      94.980 -44.185-207.422  1.00 53.59           C  
ANISOU 9534  C   LEU C 469     9490   4631   6241    286  -1040    423       C  
ATOM   9535  O   LEU C 469      94.405 -43.430-206.631  1.00 53.76           O  
ANISOU 9535  O   LEU C 469     9371   4771   6284    199  -1002    471       O  
ATOM   9536  CB  LEU C 469      97.340 -43.774-208.131  1.00 50.24           C  
ANISOU 9536  CB  LEU C 469     9047   4232   5810    613   -964    310       C  
ATOM   9537  CG  LEU C 469      98.392 -43.280-209.116  1.00 49.14           C  
ANISOU 9537  CG  LEU C 469     8875   4128   5667    770   -904    225       C  
ATOM   9538  CD1 LEU C 469      99.787 -43.446-208.555  1.00 44.56           C  
ANISOU 9538  CD1 LEU C 469     8277   3553   5101    936   -878    212       C  
ATOM   9539  CD2 LEU C 469      98.251 -44.032-210.450  1.00 49.06           C  
ANISOU 9539  CD2 LEU C 469     9031   3991   5618    791   -942    163       C  
ATOM   9540  N   SER C 470      94.874 -45.507-207.370  1.00 48.65           N  
ANISOU 9540  N   SER C 470     9050   3842   5591    258  -1119    443       N  
ATOM   9541  CA  SER C 470      94.159 -46.185-206.306  1.00 44.24           C  
ANISOU 9541  CA  SER C 470     8544   3234   5030    122  -1162    533       C  
ATOM   9542  C   SER C 470      95.114 -47.112-205.560  1.00 47.79           C  
ANISOU 9542  C   SER C 470     9125   3575   5457    224  -1197    557       C  
ATOM   9543  O   SER C 470      96.063 -47.616-206.162  1.00 45.23           O  
ANISOU 9543  O   SER C 470     8905   3160   5121    376  -1218    497       O  
ATOM   9544  CB  SER C 470      92.979 -46.991-206.863  1.00 58.60           C  
ANISOU 9544  CB  SER C 470    10480   4943   6843    -41  -1241    551       C  
ATOM   9545  OG  SER C 470      92.187 -47.540-205.827  1.00 57.03           O  
ANISOU 9545  OG  SER C 470    10310   4714   6644   -197  -1269    644       O  
ATOM   9546  N   PRO C 471      94.935 -47.321-204.229  1.00 41.78           N  
ANISOU 9546  N   PRO C 471     8361   2824   4688    156  -1201    642       N  
ATOM   9547  CA  PRO C 471      93.998 -46.767-203.237  1.00 47.20           C  
ANISOU 9547  CA  PRO C 471     8929   3624   5383     -1  -1160    719       C  
ATOM   9548  C   PRO C 471      93.959 -45.242-203.217  1.00 44.15           C  
ANISOU 9548  C   PRO C 471     8315   3435   5025     19  -1067    692       C  
ATOM   9549  O   PRO C 471      94.957 -44.613-203.578  1.00 45.85           O  
ANISOU 9549  O   PRO C 471     8464   3707   5251    173  -1030    631       O  
ATOM   9550  CB  PRO C 471      94.546 -47.289-201.898  1.00 45.44           C  
ANISOU 9550  CB  PRO C 471     8777   3359   5129     28  -1178    788       C  
ATOM   9551  CG  PRO C 471      95.240 -48.556-202.255  1.00 50.52           C  
ANISOU 9551  CG  PRO C 471     9634   3811   5751    123  -1264    770       C  
ATOM   9552  CD  PRO C 471      95.848 -48.300-203.622  1.00 45.33           C  
ANISOU 9552  CD  PRO C 471     8962   3148   5113    261  -1254    664       C  
ATOM   9553  N   ALA C 472      92.841 -44.665-202.780  1.00 44.61           N  
ANISOU 9553  N   ALA C 472     8256   3594   5098   -133  -1029    737       N  
ATOM   9554  CA  ALA C 472      92.664 -43.224-202.854  1.00 38.88           C  
ANISOU 9554  CA  ALA C 472     7325   3043   4402   -121   -948    707       C  
ATOM   9555  C   ALA C 472      91.707 -42.749-201.771  1.00 43.69           C  
ANISOU 9555  C   ALA C 472     7825   3759   5016   -260   -897    777       C  
ATOM   9556  O   ALA C 472      90.844 -43.490-201.294  1.00 45.80           O  
ANISOU 9556  O   ALA C 472     8156   3973   5273   -405   -922    843       O  
ATOM   9557  CB  ALA C 472      92.131 -42.797-204.229  1.00 41.38           C  
ANISOU 9557  CB  ALA C 472     7596   3378   4748   -141   -956    646       C  
ATOM   9558  N   PHE C 473      91.866 -41.487-201.406  1.00 41.22           N  
ANISOU 9558  N   PHE C 473     7348   3597   4717   -215   -821    760       N  
ATOM   9559  CA  PHE C 473      90.849 -40.733-200.687  1.00 48.13           C  
ANISOU 9559  CA  PHE C 473     8084   4599   5605   -332   -756    799       C  
ATOM   9560  C   PHE C 473      90.028 -39.957-201.708  1.00 48.32           C  
ANISOU 9560  C   PHE C 473     7986   4693   5679   -374   -743    755       C  
ATOM   9561  O   PHE C 473      90.592 -39.299-202.591  1.00 44.62           O  
ANISOU 9561  O   PHE C 473     7476   4251   5226   -267   -738    687       O  
ATOM   9562  CB  PHE C 473      91.485 -39.793-199.659  1.00 42.34           C  
ANISOU 9562  CB  PHE C 473     7254   3979   4853   -256   -686    804       C  
ATOM   9563  CG  PHE C 473      92.117 -40.519-198.495  1.00 45.18           C  
ANISOU 9563  CG  PHE C 473     7728   4281   5159   -237   -705    860       C  
ATOM   9564  CD1 PHE C 473      91.326 -41.115-197.536  1.00 41.49           C  
ANISOU 9564  CD1 PHE C 473     7312   3794   4658   -374   -697    942       C  
ATOM   9565  CD2 PHE C 473      93.495 -40.600-198.363  1.00 44.98           C  
ANISOU 9565  CD2 PHE C 473     7756   4220   5115    -83   -731    834       C  
ATOM   9566  CE1 PHE C 473      91.893 -41.787-196.450  1.00 46.91           C  
ANISOU 9566  CE1 PHE C 473     8119   4420   5284   -360   -720   1000       C  
ATOM   9567  CE2 PHE C 473      94.074 -41.276-197.286  1.00 45.18           C  
ANISOU 9567  CE2 PHE C 473     7890   4186   5090    -60   -763    889       C  
ATOM   9568  CZ  PHE C 473      93.270 -41.870-196.335  1.00 42.49           C  
ANISOU 9568  CZ  PHE C 473     7617   3819   4707   -198   -760    973       C  
ATOM   9569  N   ARG C 474      88.703 -40.075-201.615  1.00 45.29           N  
ANISOU 9569  N   ARG C 474     7551   4336   5320   -531   -741    795       N  
ATOM   9570  CA  ARG C 474      87.786 -39.417-202.533  1.00 54.25           C  
ANISOU 9570  CA  ARG C 474     8569   5534   6508   -583   -744    761       C  
ATOM   9571  C   ARG C 474      86.820 -38.524-201.773  1.00 53.20           C  
ANISOU 9571  C   ARG C 474     8261   5549   6406   -666   -665    791       C  
ATOM   9572  O   ARG C 474      86.485 -38.785-200.619  1.00 53.48           O  
ANISOU 9572  O   ARG C 474     8290   5610   6419   -743   -621    853       O  
ATOM   9573  CB  ARG C 474      86.947 -40.419-203.326  1.00 50.91           C  
ANISOU 9573  CB  ARG C 474     8235   5004   6104   -704   -830    773       C  
ATOM   9574  CG  ARG C 474      87.691 -41.384-204.199  1.00 58.46           C  
ANISOU 9574  CG  ARG C 474     9378   5803   7031   -637   -914    739       C  
ATOM   9575  CD  ARG C 474      86.646 -42.218-204.931  1.00 68.36           C  
ANISOU 9575  CD  ARG C 474    10700   6968   8307   -782  -1001    752       C  
ATOM   9576  NE  ARG C 474      87.186 -43.411-205.563  1.00 84.42           N  
ANISOU 9576  NE  ARG C 474    12948   8824  10305   -751  -1088    734       N  
ATOM   9577  CZ  ARG C 474      86.508 -44.548-205.679  1.00 96.79           C  
ANISOU 9577  CZ  ARG C 474    14637  10270  11870   -887  -1167    772       C  
ATOM   9578  NH1 ARG C 474      85.278 -44.636-205.185  1.00 92.06           N  
ANISOU 9578  NH1 ARG C 474    13952   9718  11307  -1069  -1164    836       N  
ATOM   9579  NH2 ARG C 474      87.059 -45.597-206.277  1.00106.02           N  
ANISOU 9579  NH2 ARG C 474    16011  11269  13001   -843  -1247    747       N  
ATOM   9580  N   TYR C 475      86.334 -37.490-202.446  1.00 43.80           N  
ANISOU 9580  N   TYR C 475     6932   4449   5261   -650   -649    746       N  
ATOM   9581  CA  TYR C 475      85.215 -36.761-201.884  1.00 46.90           C  
ANISOU 9581  CA  TYR C 475     7157   4970   5694   -738   -586    771       C  
ATOM   9582  C   TYR C 475      83.936 -37.561-202.100  1.00 45.71           C  
ANISOU 9582  C   TYR C 475     6998   4786   5582   -909   -632    815       C  
ATOM   9583  O   TYR C 475      83.866 -38.432-202.967  1.00 51.64           O  
ANISOU 9583  O   TYR C 475     7861   5422   6337   -948   -724    809       O  
ATOM   9584  CB  TYR C 475      85.096 -35.368-202.510  1.00 46.27           C  
ANISOU 9584  CB  TYR C 475     6933   4994   5655   -659   -561    711       C  
ATOM   9585  CG  TYR C 475      86.337 -34.515-202.361  1.00 48.13           C  
ANISOU 9585  CG  TYR C 475     7167   5262   5857   -503   -518    667       C  
ATOM   9586  CD1 TYR C 475      86.788 -34.119-201.109  1.00 56.40           C  
ANISOU 9586  CD1 TYR C 475     8187   6373   6871   -468   -442    688       C  
ATOM   9587  CD2 TYR C 475      87.037 -34.071-203.481  1.00 60.26           C  
ANISOU 9587  CD2 TYR C 475     8728   6772   7396   -397   -554    605       C  
ATOM   9588  CE1 TYR C 475      87.915 -33.330-200.968  1.00 64.35           C  
ANISOU 9588  CE1 TYR C 475     9188   7411   7853   -336   -412    648       C  
ATOM   9589  CE2 TYR C 475      88.166 -33.277-203.349  1.00 67.76           C  
ANISOU 9589  CE2 TYR C 475     9668   7757   8322   -267   -512    568       C  
ATOM   9590  CZ  TYR C 475      88.598 -32.910-202.089  1.00 72.85           C  
ANISOU 9590  CZ  TYR C 475    10279   8462   8940   -239   -446    589       C  
ATOM   9591  OH  TYR C 475      89.718 -32.124-201.945  1.00 81.46           O  
ANISOU 9591  OH  TYR C 475    11355   9587  10011   -120   -413    553       O  
ATOM   9592  N   GLN C 476      82.924 -37.279-201.287  1.00 48.59           N  
ANISOU 9592  N   GLN C 476     7234   5253   5976  -1014   -564    859       N  
ATOM   9593  CA  GLN C 476      81.675 -38.017-201.388  1.00 49.81           C  
ANISOU 9593  CA  GLN C 476     7361   5391   6175  -1191   -599    907       C  
ATOM   9594  C   GLN C 476      80.532 -37.065-201.089  1.00 46.17           C  
ANISOU 9594  C   GLN C 476     6676   5087   5780  -1246   -528    911       C  
ATOM   9595  O   GLN C 476      80.746 -36.005-200.495  1.00 51.90           O  
ANISOU 9595  O   GLN C 476     7300   5921   6497  -1158   -438    890       O  
ATOM   9596  CB  GLN C 476      81.646 -39.216-200.430  1.00 48.20           C  
ANISOU 9596  CB  GLN C 476     7281   5110   5923  -1303   -588    987       C  
ATOM   9597  CG  GLN C 476      81.746 -38.841-198.981  1.00 46.82           C  
ANISOU 9597  CG  GLN C 476     7059   5026   5703  -1302   -470   1029       C  
ATOM   9598  CD  GLN C 476      81.829 -40.059-198.070  1.00 53.01           C  
ANISOU 9598  CD  GLN C 476     7997   5719   6426  -1406   -468   1111       C  
ATOM   9599  OE1 GLN C 476      81.304 -41.128-198.388  1.00 51.39           O  
ANISOU 9599  OE1 GLN C 476     7876   5415   6234  -1537   -536   1152       O  
ATOM   9600  NE2 GLN C 476      82.499 -39.900-196.929  1.00 49.75           N  
ANISOU 9600  NE2 GLN C 476     7630   5332   5940  -1350   -398   1137       N  
ATOM   9601  N   PRO C 477      79.317 -37.394-201.516  1.00 58.83           N  
ANISOU 9601  N   PRO C 477     8196   6704   7452  -1385   -570    933       N  
ATOM   9602  CA  PRO C 477      78.186 -36.519-201.205  1.00 58.83           C  
ANISOU 9602  CA  PRO C 477     7968   6859   7524  -1433   -499    936       C  
ATOM   9603  C   PRO C 477      77.961 -36.459-199.706  1.00 58.95           C  
ANISOU 9603  C   PRO C 477     7930   6962   7507  -1485   -364    991       C  
ATOM   9604  O   PRO C 477      78.313 -37.379-198.967  1.00 63.99           O  
ANISOU 9604  O   PRO C 477     8704   7528   8079  -1548   -346   1047       O  
ATOM   9605  CB  PRO C 477      77.008 -37.188-201.924  1.00 65.34           C  
ANISOU 9605  CB  PRO C 477     8741   7658   8427  -1594   -588    960       C  
ATOM   9606  CG  PRO C 477      77.633 -38.032-202.990  1.00 59.17           C  
ANISOU 9606  CG  PRO C 477     8155   6711   7615  -1579   -723    938       C  
ATOM   9607  CD  PRO C 477      78.938 -38.493-202.425  1.00 61.75           C  
ANISOU 9607  CD  PRO C 477     8669   6948   7843  -1492   -694    946       C  
ATOM   9608  N   ASP C 478      77.396 -35.343-199.257  1.00 61.16           N  
ANISOU 9608  N   ASP C 478     8021   7393   7825  -1450   -269    971       N  
ATOM   9609  CA  ASP C 478      76.980 -35.227-197.871  1.00 72.45           C  
ANISOU 9609  CA  ASP C 478     9379   8920   9226  -1510   -131   1019       C  
ATOM   9610  C   ASP C 478      75.918 -36.284-197.562  1.00 73.83           C  
ANISOU 9610  C   ASP C 478     9531   9089   9433  -1721   -124   1097       C  
ATOM   9611  O   ASP C 478      75.190 -36.725-198.457  1.00 73.92           O  
ANISOU 9611  O   ASP C 478     9498   9068   9522  -1815   -217   1101       O  
ATOM   9612  CB  ASP C 478      76.431 -33.827-197.593  1.00 73.71           C  
ANISOU 9612  CB  ASP C 478     9331   9242   9435  -1433    -36    975       C  
ATOM   9613  CG  ASP C 478      77.508 -32.758-197.635  1.00 77.97           C  
ANISOU 9613  CG  ASP C 478     9903   9792   9929  -1240    -22    908       C  
ATOM   9614  OD1 ASP C 478      78.353 -32.727-196.714  1.00 74.61           O  
ANISOU 9614  OD1 ASP C 478     9578   9358   9415  -1186     41    919       O  
ATOM   9615  OD2 ASP C 478      77.518 -31.960-198.597  1.00 83.66           O  
ANISOU 9615  OD2 ASP C 478    10556  10527  10704  -1146    -80    847       O  
ATOM   9616  N   PRO C 479      75.821 -36.725-196.303  1.00 62.89           N  
ANISOU 9616  N   PRO C 479     8183   7728   7985  -1805    -19   1163       N  
ATOM   9617  CA  PRO C 479      74.800 -37.737-195.976  1.00 66.83           C  
ANISOU 9617  CA  PRO C 479     8660   8221   8512  -2021     -4   1244       C  
ATOM   9618  C   PRO C 479      73.387 -37.236-196.203  1.00 73.66           C  
ANISOU 9618  C   PRO C 479     9267   9226   9495  -2107     36   1240       C  
ATOM   9619  O   PRO C 479      72.561 -37.959-196.775  1.00 79.28           O  
ANISOU 9619  O   PRO C 479     9937   9905  10279  -2259    -39   1272       O  
ATOM   9620  CB  PRO C 479      75.078 -38.055-194.498  1.00 62.02           C  
ANISOU 9620  CB  PRO C 479     8139   7630   7796  -2065    121   1309       C  
ATOM   9621  CG  PRO C 479      76.484 -37.592-194.255  1.00 60.56           C  
ANISOU 9621  CG  PRO C 479     8091   7398   7520  -1878    115   1265       C  
ATOM   9622  CD  PRO C 479      76.675 -36.405-195.149  1.00 64.77           C  
ANISOU 9622  CD  PRO C 479     8506   7988   8117  -1718     79   1171       C  
ATOM   9623  N   TRP C 480      73.085 -36.011-195.787  1.00 80.34           N  
ANISOU 9623  N   TRP C 480     9936  10224  10366  -2011    144   1197       N  
ATOM   9624  CA  TRP C 480      71.761 -35.449-196.029  1.00 87.53           C  
ANISOU 9624  CA  TRP C 480    10585  11274  11399  -2067    180   1185       C  
ATOM   9625  C   TRP C 480      71.583 -35.118-197.518  1.00 88.42           C  
ANISOU 9625  C   TRP C 480    10635  11352  11608  -2009     26   1125       C  
ATOM   9626  O   TRP C 480      71.333 -36.011-198.332  1.00 87.11           O  
ANISOU 9626  O   TRP C 480    10529  11088  11480  -2119   -102   1147       O  
ATOM   9627  CB  TRP C 480      71.524 -34.214-195.142  1.00 88.45           C  
ANISOU 9627  CB  TRP C 480    10544  11555  11510  -1964    342   1150       C  
ATOM   9628  CG  TRP C 480      72.531 -33.086-195.280  1.00 90.57           C  
ANISOU 9628  CG  TRP C 480    10857  11822  11732  -1741    338   1070       C  
ATOM   9629  CD1 TRP C 480      72.377 -31.934-196.001  1.00 87.90           C  
ANISOU 9629  CD1 TRP C 480    10387  11544  11468  -1606    304    993       C  
ATOM   9630  CD2 TRP C 480      73.820 -32.993-194.655  1.00 92.58           C  
ANISOU 9630  CD2 TRP C 480    11300  12014  11861  -1636    367   1062       C  
ATOM   9631  NE1 TRP C 480      73.493 -31.142-195.878  1.00 86.85           N  
ANISOU 9631  NE1 TRP C 480    10352  11387  11262  -1432    313    939       N  
ATOM   9632  CE2 TRP C 480      74.393 -31.768-195.056  1.00 88.20           C  
ANISOU 9632  CE2 TRP C 480    10712  11487  11313  -1448    351    979       C  
ATOM   9633  CE3 TRP C 480      74.549 -33.829-193.805  1.00 91.30           C  
ANISOU 9633  CE3 TRP C 480    11334  11774  11583  -1685    397   1119       C  
ATOM   9634  CZ2 TRP C 480      75.658 -31.361-194.634  1.00 80.67           C  
ANISOU 9634  CZ2 TRP C 480     9902  10489  10259  -1315    365    950       C  
ATOM   9635  CZ3 TRP C 480      75.807 -33.421-193.388  1.00 83.31           C  
ANISOU 9635  CZ3 TRP C 480    10462  10719  10472  -1543    405   1089       C  
ATOM   9636  CH2 TRP C 480      76.347 -32.200-193.802  1.00 78.80           C  
ANISOU 9636  CH2 TRP C 480     9842  10182   9915  -1364    390   1005       C  
ATOM   9637  OXT TRP C 480      71.684 -33.975-197.965  1.00 90.64           O  
ANISOU 9637  OXT TRP C 480    10820  11695  11926  -1857     18   1053       O  
TER    9638      TRP C 480                                                      
ATOM   9639  N   PHE D  68      78.899 -28.467-220.799  1.00 61.08           N  
ANISOU 9639  N   PHE D  68     7728   8139   7339  -1950   -715    774       N  
ATOM   9640  CA  PHE D  68      79.676 -27.264-220.505  1.00 54.02           C  
ANISOU 9640  CA  PHE D  68     6758   7245   6524  -1682   -651    731       C  
ATOM   9641  C   PHE D  68      80.187 -27.259-219.071  1.00 54.37           C  
ANISOU 9641  C   PHE D  68     6824   7253   6580  -1619   -589    754       C  
ATOM   9642  O   PHE D  68      79.419 -27.515-218.146  1.00 59.90           O  
ANISOU 9642  O   PHE D  68     7442   8088   7229  -1743   -567    815       O  
ATOM   9643  CB  PHE D  68      78.836 -26.016-220.740  1.00 53.52           C  
ANISOU 9643  CB  PHE D  68     6437   7426   6471  -1593   -629    734       C  
ATOM   9644  CG  PHE D  68      78.325 -25.883-222.139  1.00 61.46           C  
ANISOU 9644  CG  PHE D  68     7403   8487   7463  -1635   -694    716       C  
ATOM   9645  CD1 PHE D  68      76.972 -25.984-222.406  1.00 65.64           C  
ANISOU 9645  CD1 PHE D  68     7771   9240   7931  -1794   -731    764       C  
ATOM   9646  CD2 PHE D  68      79.199 -25.654-223.190  1.00 58.23           C  
ANISOU 9646  CD2 PHE D  68     7110   7919   7094  -1520   -717    653       C  
ATOM   9647  CE1 PHE D  68      76.496 -25.857-223.695  1.00 64.22           C  
ANISOU 9647  CE1 PHE D  68     7551   9118   7731  -1835   -798    751       C  
ATOM   9648  CE2 PHE D  68      78.730 -25.521-224.482  1.00 58.40           C  
ANISOU 9648  CE2 PHE D  68     7102   7995   7095  -1561   -778    638       C  
ATOM   9649  CZ  PHE D  68      77.377 -25.621-224.736  1.00 58.98           C  
ANISOU 9649  CZ  PHE D  68     7018   8284   7107  -1718   -823    688       C  
ATOM   9650  N   PRO D  69      81.468 -26.937-218.881  1.00 45.17           N  
ANISOU 9650  N   PRO D  69     5760   5925   5477  -1432   -560    706       N  
ATOM   9651  CA  PRO D  69      82.041 -26.969-217.524  1.00 41.83           C  
ANISOU 9651  CA  PRO D  69     5373   5460   5061  -1372   -510    727       C  
ATOM   9652  C   PRO D  69      81.354 -25.985-216.591  1.00 44.30           C  
ANISOU 9652  C   PRO D  69     5468   5999   5367  -1318   -444    753       C  
ATOM   9653  O   PRO D  69      81.200 -24.805-216.905  1.00 45.13           O  
ANISOU 9653  O   PRO D  69     5425   6213   5507  -1175   -416    719       O  
ATOM   9654  CB  PRO D  69      83.511 -26.580-217.741  1.00 41.25           C  
ANISOU 9654  CB  PRO D  69     5407   5207   5059  -1164   -496    661       C  
ATOM   9655  CG  PRO D  69      83.766 -26.722-219.187  1.00 46.21           C  
ANISOU 9655  CG  PRO D  69     6110   5742   5705  -1153   -543    611       C  
ATOM   9656  CD  PRO D  69      82.452 -26.511-219.885  1.00 40.50           C  
ANISOU 9656  CD  PRO D  69     5247   5198   4945  -1272   -571    633       C  
ATOM   9657  N   ARG D  70      80.957 -26.481-215.427  1.00 43.25           N  
ANISOU 9657  N   ARG D  70     5327   5927   5180  -1430   -419    812       N  
ATOM   9658  CA  ARG D  70      80.523 -25.627-214.333  1.00 44.21           C  
ANISOU 9658  CA  ARG D  70     5274   6235   5286  -1361   -345    829       C  
ATOM   9659  C   ARG D  70      81.736 -25.027-213.636  1.00 50.11           C  
ANISOU 9659  C   ARG D  70     6085   6870   6086  -1162   -303    789       C  
ATOM   9660  O   ARG D  70      82.730 -25.716-213.389  1.00 59.07           O  
ANISOU 9660  O   ARG D  70     7402   7808   7232  -1155   -324    789       O  
ATOM   9661  CB  ARG D  70      79.693 -26.430-213.331  1.00 51.84           C  
ANISOU 9661  CB  ARG D  70     6219   7313   6164  -1568   -331    909       C  
ATOM   9662  CG  ARG D  70      78.680 -25.618-212.573  1.00 64.12           C  
ANISOU 9662  CG  ARG D  70     7534   9148   7680  -1554   -261    931       C  
ATOM   9663  CD  ARG D  70      78.874 -25.774-211.094  1.00 77.98           C  
ANISOU 9663  CD  ARG D  70     9314  10925   9391  -1570   -205    967       C  
ATOM   9664  NE  ARG D  70      78.946 -27.177-210.709  1.00 85.85           N  
ANISOU 9664  NE  ARG D  70    10489  11803  10327  -1785   -246   1034       N  
ATOM   9665  CZ  ARG D  70      79.608 -27.613-209.645  1.00 89.41           C  
ANISOU 9665  CZ  ARG D  70    11071  12148  10754  -1790   -230   1064       C  
ATOM   9666  NH1 ARG D  70      80.256 -26.750-208.871  1.00 75.34           N  
ANISOU 9666  NH1 ARG D  70     9253  10372   9000  -1599   -173   1028       N  
ATOM   9667  NH2 ARG D  70      79.629 -28.910-209.363  1.00 96.77           N  
ANISOU 9667  NH2 ARG D  70    12181  12960  11627  -1988   -276   1130       N  
ATOM   9668  N   VAL D  71      81.639 -23.743-213.298  1.00 41.41           N  
ANISOU 9668  N   VAL D  71     4830   5894   5008  -1002   -245    757       N  
ATOM   9669  CA  VAL D  71      82.756 -22.948-212.798  1.00 39.64           C  
ANISOU 9669  CA  VAL D  71     4647   5581   4835   -807   -208    709       C  
ATOM   9670  C   VAL D  71      82.266 -22.198-211.563  1.00 39.23           C  
ANISOU 9670  C   VAL D  71     4460   5701   4747   -756   -134    720       C  
ATOM   9671  O   VAL D  71      81.319 -21.406-211.653  1.00 38.73           O  
ANISOU 9671  O   VAL D  71     4220   5826   4670   -718   -101    713       O  
ATOM   9672  CB  VAL D  71      83.261 -21.954-213.862  1.00 44.59           C  
ANISOU 9672  CB  VAL D  71     5252   6158   5532   -640   -218    641       C  
ATOM   9673  CG1 VAL D  71      84.504 -21.247-213.398  1.00 42.33           C  
ANISOU 9673  CG1 VAL D  71     5027   5765   5292   -470   -188    594       C  
ATOM   9674  CG2 VAL D  71      83.492 -22.642-215.221  1.00 44.83           C  
ANISOU 9674  CG2 VAL D  71     5387   6062   5584   -703   -286    628       C  
ATOM   9675  N   LYS D  72      82.900 -22.427-210.419  1.00 39.61           N  
ANISOU 9675  N   LYS D  72     4586   5690   4772   -746   -107    734       N  
ATOM   9676  CA  LYS D  72      82.436 -21.850-209.169  1.00 35.11           C  
ANISOU 9676  CA  LYS D  72     3908   5282   4152   -717    -35    745       C  
ATOM   9677  C   LYS D  72      83.409 -20.803-208.642  1.00 33.08           C  
ANISOU 9677  C   LYS D  72     3671   4967   3933   -522      2    686       C  
ATOM   9678  O   LYS D  72      84.627 -20.953-208.751  1.00 34.78           O  
ANISOU 9678  O   LYS D  72     4023   5001   4191   -460    -30    663       O  
ATOM   9679  CB  LYS D  72      82.238 -22.943-208.101  1.00 40.91           C  
ANISOU 9679  CB  LYS D  72     4710   6027   4806   -889    -30    820       C  
ATOM   9680  CG  LYS D  72      81.723 -22.428-206.766  1.00 40.66           C  
ANISOU 9680  CG  LYS D  72     4568   6177   4706   -876     50    833       C  
ATOM   9681  CD  LYS D  72      81.267 -23.586-205.894  1.00 51.78           C  
ANISOU 9681  CD  LYS D  72     6028   7627   6021  -1088     51    921       C  
ATOM   9682  CE  LYS D  72      80.573 -23.103-204.624  1.00 67.42           C  
ANISOU 9682  CE  LYS D  72     7876   9825   7916  -1096    139    937       C  
ATOM   9683  NZ  LYS D  72      79.119 -22.842-204.868  1.00 82.34           N  
ANISOU 9683  NZ  LYS D  72     9550  11973   9760  -1167    179    951       N  
ATOM   9684  N   ASN D  73      82.863 -19.742-208.066  1.00 39.07           N  
ANISOU 9684  N   ASN D  73     4292   5884   4668   -426     67    659       N  
ATOM   9685  CA  ASN D  73      83.624 -18.833-207.226  1.00 38.79           C  
ANISOU 9685  CA  ASN D  73     4281   5818   4639   -279    111    611       C  
ATOM   9686  C   ASN D  73      83.375 -19.235-205.779  1.00 38.12           C  
ANISOU 9686  C   ASN D  73     4193   5824   4467   -360    157    653       C  
ATOM   9687  O   ASN D  73      82.221 -19.279-205.336  1.00 38.54           O  
ANISOU 9687  O   ASN D  73     4119   6070   4454   -432    204    683       O  
ATOM   9688  CB  ASN D  73      83.236 -17.370-207.449  1.00 38.98           C  
ANISOU 9688  CB  ASN D  73     4185   5940   4684   -111    154    548       C  
ATOM   9689  CG  ASN D  73      84.075 -16.437-206.597  1.00 48.17           C  
ANISOU 9689  CG  ASN D  73     5399   7054   5848     27    193    494       C  
ATOM   9690  OD1 ASN D  73      83.863 -16.316-205.379  1.00 45.83           O  
ANISOU 9690  OD1 ASN D  73     5078   6850   5485     22    248    498       O  
ATOM   9691  ND2 ASN D  73      85.069 -15.820-207.212  1.00 37.89           N  
ANISOU 9691  ND2 ASN D  73     4176   5606   4613    135    163    444       N  
ATOM   9692  N   TRP D  74      84.445 -19.545-205.049  1.00 37.38           N  
ANISOU 9692  N   TRP D  74     4233   5602   4367   -351    144    658       N  
ATOM   9693  CA  TRP D  74      84.272 -20.054-203.689  1.00 40.64           C  
ANISOU 9693  CA  TRP D  74     4667   6086   4690   -444    178    708       C  
ATOM   9694  C   TRP D  74      84.181 -18.946-202.657  1.00 46.49           C  
ANISOU 9694  C   TRP D  74     5335   6945   5385   -331    255    662       C  
ATOM   9695  O   TRP D  74      83.726 -19.198-201.535  1.00 43.42           O  
ANISOU 9695  O   TRP D  74     4920   6672   4904   -406    302    698       O  
ATOM   9696  CB  TRP D  74      85.405 -21.028-203.325  1.00 37.07           C  
ANISOU 9696  CB  TRP D  74     4400   5448   4239   -496    119    748       C  
ATOM   9697  CG  TRP D  74      85.263 -22.278-204.090  1.00 39.31           C  
ANISOU 9697  CG  TRP D  74     4765   5636   4535   -635     54    804       C  
ATOM   9698  CD1 TRP D  74      85.728 -22.519-205.360  1.00 41.01           C  
ANISOU 9698  CD1 TRP D  74     5041   5711   4831   -605     -6    779       C  
ATOM   9699  CD2 TRP D  74      84.538 -23.445-203.699  1.00 46.20           C  
ANISOU 9699  CD2 TRP D  74     5673   6549   5333   -836     42    890       C  
ATOM   9700  NE1 TRP D  74      85.341 -23.772-205.766  1.00 45.71           N  
ANISOU 9700  NE1 TRP D  74     5715   6250   5404   -769    -55    840       N  
ATOM   9701  CE2 TRP D  74      84.628 -24.366-204.758  1.00 48.94           C  
ANISOU 9701  CE2 TRP D  74     6116   6760   5719   -918    -30    912       C  
ATOM   9702  CE3 TRP D  74      83.845 -23.813-202.539  1.00 51.22           C  
ANISOU 9702  CE3 TRP D  74     6278   7321   5863   -963     85    953       C  
ATOM   9703  CZ2 TRP D  74      84.043 -25.628-204.700  1.00 51.88           C  
ANISOU 9703  CZ2 TRP D  74     6564   7116   6031  -1127    -65    993       C  
ATOM   9704  CZ3 TRP D  74      83.265 -25.070-202.483  1.00 57.59           C  
ANISOU 9704  CZ3 TRP D  74     7151   8121   6609  -1178     53   1040       C  
ATOM   9705  CH2 TRP D  74      83.367 -25.960-203.559  1.00 56.14           C  
ANISOU 9705  CH2 TRP D  74     7074   7789   6469  -1259    -24   1059       C  
ATOM   9706  N   GLU D  75      84.584 -17.730-203.015  1.00 40.47           N  
ANISOU 9706  N   GLU D  75     4548   6153   4678   -158    269    582       N  
ATOM   9707  CA  GLU D  75      84.428 -16.607-202.105  1.00 44.68           C  
ANISOU 9707  CA  GLU D  75     5022   6790   5164    -42    342    526       C  
ATOM   9708  C   GLU D  75      82.959 -16.235-201.962  1.00 47.32           C  
ANISOU 9708  C   GLU D  75     5181   7354   5445    -43    412    526       C  
ATOM   9709  O   GLU D  75      82.454 -16.054-200.845  1.00 46.40           O  
ANISOU 9709  O   GLU D  75     5008   7383   5238    -53    483    527       O  
ATOM   9710  CB  GLU D  75      85.251 -15.419-202.601  1.00 39.58           C  
ANISOU 9710  CB  GLU D  75     4417   6034   4590    130    331    443       C  
ATOM   9711  CG  GLU D  75      85.008 -14.144-201.797  1.00 49.71           C  
ANISOU 9711  CG  GLU D  75     5651   7410   5825    263    404    374       C  
ATOM   9712  CD  GLU D  75      85.961 -13.015-202.152  1.00 53.04           C  
ANISOU 9712  CD  GLU D  75     6149   7698   6304    408    387    297       C  
ATOM   9713  OE1 GLU D  75      86.938 -13.251-202.903  1.00 48.58           O  
ANISOU 9713  OE1 GLU D  75     5671   6976   5810    400    320    300       O  
ATOM   9714  OE2 GLU D  75      85.732 -11.881-201.667  1.00 54.97           O  
ANISOU 9714  OE2 GLU D  75     6371   7998   6518    527    440    232       O  
ATOM   9715  N   VAL D  76      82.252 -16.181-203.087  1.00 43.80           N  
ANISOU 9715  N   VAL D  76     4643   6955   5045    -40    392    528       N  
ATOM   9716  CA  VAL D  76      80.882 -15.692-203.166  1.00 51.51           C  
ANISOU 9716  CA  VAL D  76     5431   8156   5983     -7    449    521       C  
ATOM   9717  C   VAL D  76      79.859 -16.819-203.290  1.00 53.90           C  
ANISOU 9717  C   VAL D  76     5643   8601   6237   -207    443    604       C  
ATOM   9718  O   VAL D  76      78.690 -16.626-202.919  1.00 54.88           O  
ANISOU 9718  O   VAL D  76     5597   8960   6293   -221    506    614       O  
ATOM   9719  CB  VAL D  76      80.782 -14.715-204.362  1.00 57.63           C  
ANISOU 9719  CB  VAL D  76     6159   8896   6840    149    425    465       C  
ATOM   9720  CG1 VAL D  76      79.365 -14.585-204.895  1.00 63.06           C  
ANISOU 9720  CG1 VAL D  76     6653   9798   7509    148    445    481       C  
ATOM   9721  CG2 VAL D  76      81.343 -13.357-203.973  1.00 63.17           C  
ANISOU 9721  CG2 VAL D  76     6907   9541   7556    350    461    379       C  
ATOM   9722  N   GLY D  77      80.261 -17.989-203.782  1.00 54.85           N  
ANISOU 9722  N   GLY D  77     5870   8589   6381   -363    370    663       N  
ATOM   9723  CA  GLY D  77      79.350 -19.090-204.004  1.00 49.46           C  
ANISOU 9723  CA  GLY D  77     5129   8013   5651   -572    351    742       C  
ATOM   9724  C   GLY D  77      78.726 -19.127-205.381  1.00 58.43           C  
ANISOU 9724  C   GLY D  77     6180   9183   6839   -591    302    745       C  
ATOM   9725  O   GLY D  77      77.961 -20.056-205.668  1.00 72.91           O  
ANISOU 9725  O   GLY D  77     7968  11103   8633   -782    276    810       O  
ATOM   9726  N   SER D  78      79.043 -18.167-206.247  1.00 51.60           N  
ANISOU 9726  N   SER D  78     5303   8248   6054   -413    283    680       N  
ATOM   9727  CA  SER D  78      78.374 -18.037-207.535  1.00 49.45           C  
ANISOU 9727  CA  SER D  78     4933   8032   5822   -409    239    679       C  
ATOM   9728  C   SER D  78      78.893 -19.058-208.543  1.00 49.71           C  
ANISOU 9728  C   SER D  78     5105   7883   5900   -539    147    710       C  
ATOM   9729  O   SER D  78      80.041 -19.510-208.478  1.00 43.69           O  
ANISOU 9729  O   SER D  78     4524   6906   5171   -548    114    706       O  
ATOM   9730  CB  SER D  78      78.561 -16.622-208.086  1.00 48.04           C  
ANISOU 9730  CB  SER D  78     4714   7832   5706   -170    248    603       C  
ATOM   9731  OG  SER D  78      79.925 -16.240-208.046  1.00 44.38           O  
ANISOU 9731  OG  SER D  78     4421   7142   5300    -66    232    556       O  
ATOM   9732  N   ILE D  79      78.041 -19.382-209.512  1.00 48.47           N  
ANISOU 9732  N   ILE D  79     4857   7818   5743   -629    105    737       N  
ATOM   9733  CA  ILE D  79      78.275 -20.468-210.450  1.00 46.48           C  
ANISOU 9733  CA  ILE D  79     4723   7427   5510   -785     21    771       C  
ATOM   9734  C   ILE D  79      78.020 -19.964-211.867  1.00 50.92           C  
ANISOU 9734  C   ILE D  79     5228   7992   6126   -713    -30    741       C  
ATOM   9735  O   ILE D  79      77.004 -19.311-212.129  1.00 48.58           O  
ANISOU 9735  O   ILE D  79     4743   7901   5813   -662    -13    739       O  
ATOM   9736  CB  ILE D  79      77.379 -21.679-210.127  1.00 52.15           C  
ANISOU 9736  CB  ILE D  79     5408   8263   6143  -1046     10    852       C  
ATOM   9737  CG1 ILE D  79      77.948 -22.443-208.924  1.00 55.61           C  
ANISOU 9737  CG1 ILE D  79     5984   8610   6535  -1140     33    890       C  
ATOM   9738  CG2 ILE D  79      77.227 -22.582-211.339  1.00 48.00           C  
ANISOU 9738  CG2 ILE D  79     4954   7653   5630  -1200    -79    877       C  
ATOM   9739  CD1 ILE D  79      77.081 -23.583-208.462  1.00 65.27           C  
ANISOU 9739  CD1 ILE D  79     7189   9950   7663  -1406     29    976       C  
ATOM   9740  N   THR D  80      78.946 -20.252-212.773  1.00 44.58           N  
ANISOU 9740  N   THR D  80     4586   6971   5383   -700    -91    717       N  
ATOM   9741  CA  THR D  80      78.765 -19.979-214.189  1.00 41.07           C  
ANISOU 9741  CA  THR D  80     4117   6509   4979   -667   -149    697       C  
ATOM   9742  C   THR D  80      79.102 -21.238-214.978  1.00 43.96           C  
ANISOU 9742  C   THR D  80     4639   6721   5344   -838   -224    719       C  
ATOM   9743  O   THR D  80      79.624 -22.217-214.437  1.00 41.79           O  
ANISOU 9743  O   THR D  80     4506   6322   5050   -947   -231    743       O  
ATOM   9744  CB  THR D  80      79.636 -18.799-214.647  1.00 48.65           C  
ANISOU 9744  CB  THR D  80     5119   7353   6010   -441   -143    629       C  
ATOM   9745  OG1 THR D  80      81.019 -19.105-214.428  1.00 49.73           O  
ANISOU 9745  OG1 THR D  80     5445   7265   6185   -413   -147    604       O  
ATOM   9746  CG2 THR D  80      79.286 -17.532-213.866  1.00 51.96           C  
ANISOU 9746  CG2 THR D  80     5409   7909   6426   -268    -72    601       C  
ATOM   9747  N   TYR D  81      78.777 -21.214-216.267  1.00 40.44           N  
ANISOU 9747  N   TYR D  81     4171   6280   4913   -858   -283    710       N  
ATOM   9748  CA  TYR D  81      79.126 -22.276-217.202  1.00 43.87           C  
ANISOU 9748  CA  TYR D  81     4764   6558   5348   -995   -356    714       C  
ATOM   9749  C   TYR D  81      79.965 -21.681-218.315  1.00 43.31           C  
ANISOU 9749  C   TYR D  81     4771   6344   5341   -850   -385    655       C  
ATOM   9750  O   TYR D  81      79.581 -20.673-218.916  1.00 39.80           O  
ANISOU 9750  O   TYR D  81     4209   5997   4915   -735   -387    635       O  
ATOM   9751  CB  TYR D  81      77.878 -22.962-217.776  1.00 45.02           C  
ANISOU 9751  CB  TYR D  81     4821   6855   5431  -1201   -407    763       C  
ATOM   9752  CG  TYR D  81      77.152 -23.762-216.719  1.00 55.24           C  
ANISOU 9752  CG  TYR D  81     6071   8268   6651  -1389   -384    829       C  
ATOM   9753  CD1 TYR D  81      76.167 -23.174-215.933  1.00 57.86           C  
ANISOU 9753  CD1 TYR D  81     6182   8859   6943  -1373   -326    857       C  
ATOM   9754  CD2 TYR D  81      77.481 -25.090-216.476  1.00 52.85           C  
ANISOU 9754  CD2 TYR D  81     5954   7814   6313  -1575   -416    861       C  
ATOM   9755  CE1 TYR D  81      75.516 -23.893-214.945  1.00 63.81           C  
ANISOU 9755  CE1 TYR D  81     6890   9735   7619  -1555   -297    920       C  
ATOM   9756  CE2 TYR D  81      76.832 -25.816-215.494  1.00 57.57           C  
ANISOU 9756  CE2 TYR D  81     6524   8515   6835  -1760   -395    928       C  
ATOM   9757  CZ  TYR D  81      75.852 -25.212-214.729  1.00 62.82           C  
ANISOU 9757  CZ  TYR D  81     6958   9454   7457  -1756   -333    958       C  
ATOM   9758  OH  TYR D  81      75.205 -25.925-213.746  1.00 68.18           O  
ANISOU 9758  OH  TYR D  81     7604  10250   8050  -1951   -306   1028       O  
ATOM   9759  N   ASP D  82      81.120 -22.282-218.575  1.00 41.18           N  
ANISOU 9759  N   ASP D  82     4698   5848   5099   -847   -405    627       N  
ATOM   9760  CA  ASP D  82      81.987 -21.784-219.640  1.00 40.87           C  
ANISOU 9760  CA  ASP D  82     4739   5679   5112   -723   -427    570       C  
ATOM   9761  C   ASP D  82      81.559 -22.453-220.942  1.00 44.95           C  
ANISOU 9761  C   ASP D  82     5300   6176   5602   -850   -500    572       C  
ATOM   9762  O   ASP D  82      82.041 -23.525-221.307  1.00 55.75           O  
ANISOU 9762  O   ASP D  82     6835   7390   6957   -949   -536    564       O  
ATOM   9763  CB  ASP D  82      83.453 -22.037-219.318  1.00 39.33           C  
ANISOU 9763  CB  ASP D  82     4712   5275   4956   -642   -410    533       C  
ATOM   9764  CG  ASP D  82      84.393 -21.301-220.269  1.00 49.20           C  
ANISOU 9764  CG  ASP D  82     6014   6423   6256   -497   -414    474       C  
ATOM   9765  OD1 ASP D  82      84.276 -21.496-221.496  1.00 59.66           O  
ANISOU 9765  OD1 ASP D  82     7375   7719   7575   -536   -461    458       O  
ATOM   9766  OD2 ASP D  82      85.229 -20.511-219.786  1.00 55.85           O  
ANISOU 9766  OD2 ASP D  82     6860   7222   7137   -353   -372    444       O  
ATOM   9767  N   THR D  83      80.627 -21.815-221.649  1.00 42.92           N  
ANISOU 9767  N   THR D  83     4898   6077   5331   -843   -524    581       N  
ATOM   9768  CA  THR D  83      80.228 -22.310-222.959  1.00 43.93           C  
ANISOU 9768  CA  THR D  83     5062   6199   5430   -954   -598    579       C  
ATOM   9769  C   THR D  83      81.233 -21.960-224.046  1.00 44.88           C  
ANISOU 9769  C   THR D  83     5302   6164   5588   -843   -616    521       C  
ATOM   9770  O   THR D  83      81.233 -22.607-225.103  1.00 47.89           O  
ANISOU 9770  O   THR D  83     5777   6478   5940   -941   -673    506       O  
ATOM   9771  CB  THR D  83      78.858 -21.761-223.349  1.00 51.69           C  
ANISOU 9771  CB  THR D  83     5838   7424   6379   -985   -626    616       C  
ATOM   9772  OG1 THR D  83      78.923 -20.331-223.414  1.00 49.24           O  
ANISOU 9772  OG1 THR D  83     5419   7180   6111   -772   -595    596       O  
ATOM   9773  CG2 THR D  83      77.806 -22.184-222.330  1.00 42.45           C  
ANISOU 9773  CG2 THR D  83     4535   6436   5159  -1117   -606    676       C  
ATOM   9774  N   LEU D  84      82.090 -20.962-223.818  1.00 38.23           N  
ANISOU 9774  N   LEU D  84     4462   5264   4800   -653   -567    486       N  
ATOM   9775  CA  LEU D  84      83.030 -20.550-224.863  1.00 39.45           C  
ANISOU 9775  CA  LEU D  84     4714   5292   4982   -555   -579    434       C  
ATOM   9776  C   LEU D  84      84.122 -21.596-225.102  1.00 38.06           C  
ANISOU 9776  C   LEU D  84     4738   4914   4808   -599   -585    396       C  
ATOM   9777  O   LEU D  84      84.648 -21.699-226.217  1.00 40.10           O  
ANISOU 9777  O   LEU D  84     5091   5084   5062   -587   -611    357       O  
ATOM   9778  CB  LEU D  84      83.647 -19.195-224.498  1.00 37.50           C  
ANISOU 9778  CB  LEU D  84     4420   5042   4785   -359   -527    411       C  
ATOM   9779  CG  LEU D  84      84.677 -18.621-225.460  1.00 38.82           C  
ANISOU 9779  CG  LEU D  84     4679   5093   4978   -257   -528    363       C  
ATOM   9780  CD1 LEU D  84      84.042 -18.333-226.826  1.00 36.08           C  
ANISOU 9780  CD1 LEU D  84     4300   4808   4600   -284   -587    369       C  
ATOM   9781  CD2 LEU D  84      85.311 -17.371-224.865  1.00 33.98           C  
ANISOU 9781  CD2 LEU D  84     4034   4469   4408    -91   -475    345       C  
ATOM   9782  N   SER D  85      84.453 -22.399-224.083  1.00 31.85           N  
ANISOU 9782  N   SER D  85     4021   4058   4023   -646   -563    409       N  
ATOM   9783  CA  SER D  85      85.498 -23.405-224.248  1.00 32.07           C  
ANISOU 9783  CA  SER D  85     4242   3891   4052   -664   -570    373       C  
ATOM   9784  C   SER D  85      85.144 -24.444-225.302  1.00 43.75           C  
ANISOU 9784  C   SER D  85     5832   5310   5481   -810   -634    363       C  
ATOM   9785  O   SER D  85      86.047 -25.080-225.854  1.00 46.20           O  
ANISOU 9785  O   SER D  85     6305   5458   5790   -791   -643    315       O  
ATOM   9786  CB  SER D  85      85.774 -24.101-222.908  1.00 37.16           C  
ANISOU 9786  CB  SER D  85     4941   4481   4699   -694   -545    402       C  
ATOM   9787  OG  SER D  85      84.637 -24.837-222.485  1.00 46.82           O  
ANISOU 9787  OG  SER D  85     6133   5786   5871   -871   -573    459       O  
ATOM   9788  N   ALA D  86      83.855 -24.644-225.584  1.00 49.42           N  
ANISOU 9788  N   ALA D  86     6465   6159   6151   -957   -678    405       N  
ATOM   9789  CA  ALA D  86      83.474 -25.599-226.620  1.00 54.98           C  
ANISOU 9789  CA  ALA D  86     7279   6811   6798  -1113   -746    394       C  
ATOM   9790  C   ALA D  86      83.978 -25.187-227.994  1.00 53.95           C  
ANISOU 9790  C   ALA D  86     7200   6630   6669  -1037   -764    336       C  
ATOM   9791  O   ALA D  86      83.989 -26.015-228.910  1.00 62.93           O  
ANISOU 9791  O   ALA D  86     8472   7679   7758  -1139   -812    306       O  
ATOM   9792  CB  ALA D  86      81.954 -25.771-226.658  1.00 53.02           C  
ANISOU 9792  CB  ALA D  86     6902   6748   6495  -1291   -793    454       C  
ATOM   9793  N   GLN D  87      84.409 -23.937-228.156  1.00 51.77           N  
ANISOU 9793  N   GLN D  87     6831   6402   6438   -868   -726    319       N  
ATOM   9794  CA  GLN D  87      84.898 -23.424-229.430  1.00 50.39           C  
ANISOU 9794  CA  GLN D  87     6696   6192   6258   -796   -738    272       C  
ATOM   9795  C   GLN D  87      86.416 -23.443-229.532  1.00 51.37           C  
ANISOU 9795  C   GLN D  87     6948   6154   6416   -667   -690    210       C  
ATOM   9796  O   GLN D  87      86.967 -22.898-230.492  1.00 49.95           O  
ANISOU 9796  O   GLN D  87     6794   5952   6233   -592   -685    170       O  
ATOM   9797  CB  GLN D  87      84.380 -22.004-229.647  1.00 50.99           C  
ANISOU 9797  CB  GLN D  87     6599   6422   6351   -701   -735    298       C  
ATOM   9798  CG  GLN D  87      82.919 -21.865-229.280  1.00 64.37           C  
ANISOU 9798  CG  GLN D  87     8129   8306   8021   -791   -768    364       C  
ATOM   9799  CD  GLN D  87      82.266 -20.691-229.954  1.00 71.22           C  
ANISOU 9799  CD  GLN D  87     8859   9318   8884   -717   -795    385       C  
ATOM   9800  OE1 GLN D  87      82.604 -20.343-231.087  1.00 78.55           O  
ANISOU 9800  OE1 GLN D  87     9842  10207   9796   -681   -820    358       O  
ATOM   9801  NE2 GLN D  87      81.320 -20.069-229.263  1.00 71.76           N  
ANISOU 9801  NE2 GLN D  87     8749   9556   8960   -689   -788    435       N  
ATOM   9802  N   ALA D  88      87.102 -24.046-228.563  1.00 43.05           N  
ANISOU 9802  N   ALA D  88     5969   4998   5388   -639   -656    203       N  
ATOM   9803  CA  ALA D  88      88.557 -24.113-228.601  1.00 48.01           C  
ANISOU 9803  CA  ALA D  88     6703   5492   6047   -511   -613    146       C  
ATOM   9804  C   ALA D  88      89.011 -24.875-229.844  1.00 61.56           C  
ANISOU 9804  C   ALA D  88     8575   7097   7719   -543   -638     84       C  
ATOM   9805  O   ALA D  88      88.642 -26.037-230.038  1.00 55.55           O  
ANISOU 9805  O   ALA D  88     7933   6259   6912   -665   -681     79       O  
ATOM   9806  CB  ALA D  88      89.080 -24.779-227.325  1.00 41.99           C  
ANISOU 9806  CB  ALA D  88     5997   4645   5311   -489   -587    159       C  
ATOM   9807  N   GLN D  89      89.795 -24.212-230.695  1.00 93.30           N  
ANISOU 9807  N   GLN D  89    12600  11107  11742   -440   -611     37       N  
ATOM   9808  CA  GLN D  89      90.167 -24.750-231.999  1.00110.43           C  
ANISOU 9808  CA  GLN D  89    14900  13200  13858   -464   -629    -26       C  
ATOM   9809  C   GLN D  89      91.643 -25.149-232.060  1.00106.20           C  
ANISOU 9809  C   GLN D  89    14477  12540  13336   -340   -578    -95       C  
ATOM   9810  O   GLN D  89      92.263 -25.114-233.126  1.00110.78           O  
ANISOU 9810  O   GLN D  89    15121  13090  13882   -298   -563   -155       O  
ATOM   9811  CB  GLN D  89      89.822 -23.749-233.104  1.00113.58           C  
ANISOU 9811  CB  GLN D  89    15223  13703  14230   -461   -643    -26       C  
ATOM   9812  CG  GLN D  89      89.632 -24.365-234.503  1.00112.64           C  
ANISOU 9812  CG  GLN D  89    15222  13545  14032   -550   -687    -72       C  
ATOM   9813  CD  GLN D  89      88.502 -25.385-234.569  1.00116.48           C  
ANISOU 9813  CD  GLN D  89    15763  14027  14469   -729   -759    -48       C  
ATOM   9814  OE1 GLN D  89      87.524 -25.301-233.824  1.00115.80           O  
ANISOU 9814  OE1 GLN D  89    15571  14029  14397   -805   -787     19       O  
ATOM   9815  NE2 GLN D  89      88.635 -26.357-235.468  1.00121.49           N  
ANISOU 9815  NE2 GLN D  89    16566  14561  15036   -803   -789   -106       N  
ATOM   9816  N   GLN D  90      92.217 -25.522-230.918  1.00 84.49           N  
ANISOU 9816  N   GLN D  90    11744   9728  10630   -276   -551    -86       N  
ATOM   9817  CA  GLN D  90      93.509 -26.194-230.885  1.00 73.37           C  
ANISOU 9817  CA  GLN D  90    10455   8196   9227   -166   -516   -147       C  
ATOM   9818  C   GLN D  90      93.645 -26.903-229.549  1.00 69.65           C  
ANISOU 9818  C   GLN D  90    10023   7653   8788   -154   -520   -113       C  
ATOM   9819  O   GLN D  90      93.031 -26.514-228.551  1.00 55.05           O  
ANISOU 9819  O   GLN D  90     8072   5875   6968   -193   -525    -47       O  
ATOM   9820  CB  GLN D  90      94.682 -25.234-231.096  1.00 78.83           C  
ANISOU 9820  CB  GLN D  90    11071   8933   9946    -18   -453   -183       C  
ATOM   9821  CG  GLN D  90      95.706 -25.742-232.101  1.00 90.97           C  
ANISOU 9821  CG  GLN D  90    12723  10396  11445     57   -425   -270       C  
ATOM   9822  CD  GLN D  90      97.031 -25.015-232.004  1.00 91.35           C  
ANISOU 9822  CD  GLN D  90    12697  10487  11523    204   -358   -301       C  
ATOM   9823  OE1 GLN D  90      97.695 -25.045-230.966  1.00 94.74           O  
ANISOU 9823  OE1 GLN D  90    13093  10905  11999    289   -335   -289       O  
ATOM   9824  NE2 GLN D  90      97.423 -24.352-233.089  1.00 87.77           N  
ANISOU 9824  NE2 GLN D  90    12218  10094  11036    225   -328   -339       N  
ATOM   9825  N   ASP D  91      94.477 -27.936-229.543  1.00 63.50           N  
ANISOU 9825  N   ASP D  91     9396   6732   7997    -90   -517   -161       N  
ATOM   9826  CA  ASP D  91      94.557 -28.862-228.431  1.00 52.81           C  
ANISOU 9826  CA  ASP D  91     8131   5278   6657    -93   -536   -129       C  
ATOM   9827  C   ASP D  91      95.621 -28.436-227.430  1.00 58.38           C  
ANISOU 9827  C   ASP D  91     8763   6001   7418     62   -491   -121       C  
ATOM   9828  O   ASP D  91      96.717 -28.007-227.805  1.00 55.67           O  
ANISOU 9828  O   ASP D  91     8386   5675   7090    200   -446   -173       O  
ATOM   9829  CB  ASP D  91      94.845 -30.270-228.931  1.00 56.45           C  
ANISOU 9829  CB  ASP D  91     8820   5560   7070    -99   -567   -181       C  
ATOM   9830  CG  ASP D  91      93.601 -30.965-229.426  1.00 58.20           C  
ANISOU 9830  CG  ASP D  91     9139   5742   7232   -300   -631   -164       C  
ATOM   9831  OD1 ASP D  91      92.507 -30.368-229.333  1.00 59.90           O  
ANISOU 9831  OD1 ASP D  91     9227   6087   7446   -429   -651   -105       O  
ATOM   9832  OD2 ASP D  91      93.713 -32.111-229.905  1.00 66.03           O  
ANISOU 9832  OD2 ASP D  91    10337   6576   8174   -329   -663   -209       O  
ATOM   9833  N   GLY D  92      95.281 -28.553-226.153  1.00 50.19           N  
ANISOU 9833  N   GLY D  92     7695   4969   6404     29   -504    -53       N  
ATOM   9834  CA  GLY D  92      96.237 -28.365-225.096  1.00 45.00           C  
ANISOU 9834  CA  GLY D  92     6996   4313   5789    159   -475    -40       C  
ATOM   9835  C   GLY D  92      96.901 -29.673-224.720  1.00 41.67           C  
ANISOU 9835  C   GLY D  92     6751   3726   5354    223   -501    -53       C  
ATOM   9836  O   GLY D  92      96.748 -30.695-225.391  1.00 40.11           O  
ANISOU 9836  O   GLY D  92     6723   3401   5115    183   -533    -87       O  
ATOM   9837  N   PRO D  93      97.646 -29.660-223.610  1.00 40.29           N  
ANISOU 9837  N   PRO D  93     6549   3548   5211    326   -490    -26       N  
ATOM   9838  CA  PRO D  93      98.459 -30.822-223.227  1.00 40.34           C  
ANISOU 9838  CA  PRO D  93     6718   3402   5209    428   -515    -39       C  
ATOM   9839  C   PRO D  93      97.774 -31.860-222.349  1.00 36.79           C  
ANISOU 9839  C   PRO D  93     6409   2837   4733    323   -572     30       C  
ATOM   9840  O   PRO D  93      98.366 -32.924-222.128  1.00 43.45           O  
ANISOU 9840  O   PRO D  93     7423   3527   5561    403   -603     21       O  
ATOM   9841  CB  PRO D  93      99.609 -30.165-222.448  1.00 47.23           C  
ANISOU 9841  CB  PRO D  93     7467   4356   6124    588   -480    -37       C  
ATOM   9842  CG  PRO D  93      98.937 -29.003-221.771  1.00 40.21           C  
ANISOU 9842  CG  PRO D  93     6404   3618   5258    500   -461     19       C  
ATOM   9843  CD  PRO D  93      97.987 -28.459-222.825  1.00 40.67           C  
ANISOU 9843  CD  PRO D  93     6412   3738   5301    383   -451      1       C  
ATOM   9844  N   CYS D  94      96.578 -31.591-221.834  1.00 42.63           N  
ANISOU 9844  N   CYS D  94     7088   3648   5462    151   -586    100       N  
ATOM   9845  CA  CYS D  94      95.941 -32.474-220.870  1.00 40.67           C  
ANISOU 9845  CA  CYS D  94     6953   3317   5183     36   -634    177       C  
ATOM   9846  C   CYS D  94      95.134 -33.551-221.560  1.00 46.88           C  
ANISOU 9846  C   CYS D  94     7926   3972   5912   -117   -685    173       C  
ATOM   9847  O   CYS D  94      94.669 -33.382-222.688  1.00 45.90           O  
ANISOU 9847  O   CYS D  94     7793   3876   5772   -184   -684    128       O  
ATOM   9848  CB  CYS D  94      95.012 -31.706-219.934  1.00 35.27           C  
ANISOU 9848  CB  CYS D  94     6108   2788   4503    -83   -619    254       C  
ATOM   9849  SG  CYS D  94      95.757 -30.327-219.096  1.00 41.21           S  
ANISOU 9849  SG  CYS D  94     6646   3702   5311     59   -561    259       S  
ATOM   9850  N   THR D  95      94.946 -34.654-220.847  1.00 40.36           N  
ANISOU 9850  N   THR D  95     7279   3006   5052   -185   -736    226       N  
ATOM   9851  CA  THR D  95      94.082 -35.744-221.282  1.00 46.45           C  
ANISOU 9851  CA  THR D  95     8247   3643   5758   -369   -794    240       C  
ATOM   9852  C   THR D  95      93.251 -36.183-220.086  1.00 50.41           C  
ANISOU 9852  C   THR D  95     8784   4145   6225   -540   -827    348       C  
ATOM   9853  O   THR D  95      93.553 -35.783-218.951  1.00 43.30           O  
ANISOU 9853  O   THR D  95     7789   3313   5349   -477   -806    401       O  
ATOM   9854  CB  THR D  95      94.891 -36.919-221.841  1.00 50.06           C  
ANISOU 9854  CB  THR D  95     8968   3862   6191   -262   -830    178       C  
ATOM   9855  OG1 THR D  95      95.627 -37.533-220.781  1.00 48.33           O  
ANISOU 9855  OG1 THR D  95     8828   3558   5974   -148   -845    217       O  
ATOM   9856  CG2 THR D  95      95.855 -36.454-222.928  1.00 48.24           C  
ANISOU 9856  CG2 THR D  95     8687   3652   5991    -70   -785     69       C  
ATOM   9857  N   PRO D  96      92.193 -36.977-220.288  1.00 48.56           N  
ANISOU 9857  N   PRO D  96     8679   3846   5926   -769   -877    385       N  
ATOM   9858  CA  PRO D  96      91.464 -37.522-219.134  1.00 47.45           C  
ANISOU 9858  CA  PRO D  96     8595   3694   5739   -943   -909    492       C  
ATOM   9859  C   PRO D  96      92.347 -38.284-218.170  1.00 50.34           C  
ANISOU 9859  C   PRO D  96     9135   3891   6102   -826   -937    528       C  
ATOM   9860  O   PRO D  96      91.985 -38.406-216.997  1.00 52.30           O  
ANISOU 9860  O   PRO D  96     9373   4174   6325   -916   -945    621       O  
ATOM   9861  CB  PRO D  96      90.424 -38.447-219.781  1.00 50.22           C  
ANISOU 9861  CB  PRO D  96     9112   3956   6012  -1193   -969    504       C  
ATOM   9862  CG  PRO D  96      90.195 -37.858-221.114  1.00 47.16           C  
ANISOU 9862  CG  PRO D  96     8621   3657   5639  -1190   -951    423       C  
ATOM   9863  CD  PRO D  96      91.504 -37.270-221.558  1.00 46.86           C  
ANISOU 9863  CD  PRO D  96     8531   3606   5670   -905   -904    336       C  
ATOM   9864  N   ARG D  97      93.496 -38.786-218.614  1.00 50.73           N  
ANISOU 9864  N   ARG D  97     9275   3833   6168   -608   -934    448       N  
ATOM   9865  CA  ARG D  97      94.339 -39.583-217.736  1.00 51.37           C  
ANISOU 9865  CA  ARG D  97     9457   3824   6238   -475   -950    469       C  
ATOM   9866  C   ARG D  97      95.322 -38.753-216.914  1.00 44.88           C  
ANISOU 9866  C   ARG D  97     8500   3074   5480   -274   -917    484       C  
ATOM   9867  O   ARG D  97      95.741 -39.206-215.842  1.00 48.68           O  
ANISOU 9867  O   ARG D  97     9027   3523   5948   -220   -935    538       O  
ATOM   9868  CB  ARG D  97      95.098 -40.630-218.552  1.00 53.91           C  
ANISOU 9868  CB  ARG D  97     9942   4005   6537   -341   -965    383       C  
ATOM   9869  CG  ARG D  97      95.247 -41.946-217.798  1.00 67.65           C  
ANISOU 9869  CG  ARG D  97    11870   5615   8219   -351  -1014    426       C  
ATOM   9870  CD  ARG D  97      95.155 -43.143-218.719  1.00 75.23           C  
ANISOU 9870  CD  ARG D  97    13035   6431   9116   -384  -1049    368       C  
ATOM   9871  NE  ARG D  97      96.471 -43.697-219.013  1.00 84.39           N  
ANISOU 9871  NE  ARG D  97    14273   7498  10292   -126  -1043    297       N  
ATOM   9872  CZ  ARG D  97      96.681 -44.697-219.859  1.00 93.73           C  
ANISOU 9872  CZ  ARG D  97    15635   8552  11427    -89  -1065    232       C  
ATOM   9873  NH1 ARG D  97      95.658 -45.246-220.498  1.00 96.82           N  
ANISOU 9873  NH1 ARG D  97    16149   8887  11750   -300  -1098    229       N  
ATOM   9874  NH2 ARG D  97      97.912 -45.147-220.072  1.00 96.95           N  
ANISOU 9874  NH2 ARG D  97    16093   8892  11850    155  -1054    171       N  
ATOM   9875  N   ARG D  98      95.687 -37.554-217.366  1.00 41.61           N  
ANISOU 9875  N   ARG D  98     7922   2758   5128   -169   -873    439       N  
ATOM   9876  CA  ARG D  98      96.654 -36.746-216.623  1.00 47.57           C  
ANISOU 9876  CA  ARG D  98     8534   3604   5937     20   -841    446       C  
ATOM   9877  C   ARG D  98      96.563 -35.291-217.052  1.00 46.85           C  
ANISOU 9877  C   ARG D  98     8168   3738   5894     43   -770    401       C  
ATOM   9878  O   ARG D  98      96.484 -34.996-218.245  1.00 37.79           O  
ANISOU 9878  O   ARG D  98     6985   2615   4759     47   -748    328       O  
ATOM   9879  CB  ARG D  98      98.079 -37.244-216.857  1.00 44.65           C  
ANISOU 9879  CB  ARG D  98     8206   3173   5586    268   -835    375       C  
ATOM   9880  CG  ARG D  98      98.269 -37.628-218.315  1.00 61.87           C  
ANISOU 9880  CG  ARG D  98    10452   5296   7760    310   -822    272       C  
ATOM   9881  CD  ARG D  98      99.634 -37.260-218.770  1.00 63.54           C  
ANISOU 9881  CD  ARG D  98    10568   5559   8015    557   -780    190       C  
ATOM   9882  NE  ARG D  98      99.780 -37.348-220.211  1.00 46.48           N  
ANISOU 9882  NE  ARG D  98     8435   3377   5847    593   -755     91       N  
ATOM   9883  CZ  ARG D  98      99.335 -36.428-221.066  1.00 46.58           C  
ANISOU 9883  CZ  ARG D  98     8359   3461   5878    534   -725     53       C  
ATOM   9884  NH1 ARG D  98      98.657 -35.381-220.634  1.00 44.32           N  
ANISOU 9884  NH1 ARG D  98     7935   3285   5618    431   -715    105       N  
ATOM   9885  NH2 ARG D  98      99.530 -36.578-222.364  1.00 63.72           N  
ANISOU 9885  NH2 ARG D  98    10567   5611   8033    571   -703    -38       N  
ATOM   9886  N   CYS D  99      96.628 -34.391-216.075  1.00 37.28           N  
ANISOU 9886  N   CYS D  99     6777   2683   4705     63   -737    444       N  
ATOM   9887  CA  CYS D  99      96.601 -32.950-216.295  1.00 42.40           C  
ANISOU 9887  CA  CYS D  99     7178   3535   5398     95   -672    410       C  
ATOM   9888  C   CYS D  99      98.029 -32.415-216.316  1.00 41.28           C  
ANISOU 9888  C   CYS D  99     6957   3424   5304    322   -646    355       C  
ATOM   9889  O   CYS D  99      98.834 -32.726-215.428  1.00 41.39           O  
ANISOU 9889  O   CYS D  99     7011   3397   5319    431   -667    385       O  
ATOM   9890  CB  CYS D  99      95.776 -32.255-215.202  1.00 40.46           C  
ANISOU 9890  CB  CYS D  99     6790   3442   5139    -23   -649    483       C  
ATOM   9891  SG  CYS D  99      95.837 -30.458-215.131  1.00 36.98           S  
ANISOU 9891  SG  CYS D  99     6071   3233   4747     39   -576    451       S  
ATOM   9892  N   LEU D 100      98.345 -31.631-217.344  1.00 33.94           N  
ANISOU 9892  N   LEU D 100     5916   2572   4406    387   -603    279       N  
ATOM   9893  CA  LEU D 100      99.645 -30.975-217.477  1.00 38.43           C  
ANISOU 9893  CA  LEU D 100     6381   3205   5015    576   -569    224       C  
ATOM   9894  C   LEU D 100      99.500 -29.463-217.459  1.00 39.15           C  
ANISOU 9894  C   LEU D 100     6254   3485   5136    558   -514    214       C  
ATOM   9895  O   LEU D 100     100.322 -28.738-218.038  1.00 37.29           O  
ANISOU 9895  O   LEU D 100     5920   3320   4928    664   -477    154       O  
ATOM   9896  CB  LEU D 100     100.359 -31.425-218.758  1.00 42.46           C  
ANISOU 9896  CB  LEU D 100     6973   3633   5529    687   -564    137       C  
ATOM   9897  CG  LEU D 100     100.714 -32.912-218.856  1.00 45.33           C  
ANISOU 9897  CG  LEU D 100     7570   3791   5862    751   -617    130       C  
ATOM   9898  CD1 LEU D 100     101.292 -33.224-220.239  1.00 45.77           C  
ANISOU 9898  CD1 LEU D 100     7692   3785   5914    853   -598     30       C  
ATOM   9899  CD2 LEU D 100     101.691 -33.319-217.751  1.00 40.09           C  
ANISOU 9899  CD2 LEU D 100     6939   3088   5205    899   -645    167       C  
ATOM   9900  N   GLY D 101      98.454 -28.975-216.799  1.00 36.48           N  
ANISOU 9900  N   GLY D 101     5843   3231   4787    424   -507    270       N  
ATOM   9901  CA  GLY D 101      98.223 -27.543-216.749  1.00 35.95           C  
ANISOU 9901  CA  GLY D 101     5589   3327   4743    411   -459    260       C  
ATOM   9902  C   GLY D 101      99.384 -26.749-216.179  1.00 38.08           C  
ANISOU 9902  C   GLY D 101     5757   3673   5040    543   -434    243       C  
ATOM   9903  O   GLY D 101      99.535 -25.570-216.486  1.00 38.90           O  
ANISOU 9903  O   GLY D 101     5731   3884   5166    564   -394    210       O  
ATOM   9904  N   SER D 102     100.226 -27.374-215.353  1.00 33.16           N  
ANISOU 9904  N   SER D 102     5195   2995   4411    630   -463    266       N  
ATOM   9905  CA  SER D 102     101.322 -26.637-214.730  1.00 33.15           C  
ANISOU 9905  CA  SER D 102     5087   3081   4427    742   -448    254       C  
ATOM   9906  C   SER D 102     102.553 -26.479-215.632  1.00 42.60           C  
ANISOU 9906  C   SER D 102     6249   4289   5647    879   -431    182       C  
ATOM   9907  O   SER D 102     103.481 -25.754-215.255  1.00 34.19           O  
ANISOU 9907  O   SER D 102     5078   3319   4595    957   -415    167       O  
ATOM   9908  CB  SER D 102     101.713 -27.312-213.385  1.00 30.16           C  
ANISOU 9908  CB  SER D 102     4773   2662   4024    778   -491    317       C  
ATOM   9909  OG  SER D 102     102.560 -28.422-213.563  1.00 39.08           O  
ANISOU 9909  OG  SER D 102     6023   3673   5151    895   -533    308       O  
ATOM   9910  N   LEU D 103     102.579 -27.087-216.822  1.00 41.40           N  
ANISOU 9910  N   LEU D 103     6178   4056   5496    902   -430    135       N  
ATOM   9911  CA  LEU D 103     103.763 -26.992-217.677  1.00 36.24           C  
ANISOU 9911  CA  LEU D 103     5488   3425   4855   1036   -407     64       C  
ATOM   9912  C   LEU D 103     103.874 -25.607-218.328  1.00 34.48           C  
ANISOU 9912  C   LEU D 103     5115   3337   4648   1009   -352     23       C  
ATOM   9913  O   LEU D 103     102.879 -25.032-218.780  1.00 34.86           O  
ANISOU 9913  O   LEU D 103     5139   3410   4696    896   -335     27       O  
ATOM   9914  CB  LEU D 103     103.740 -28.096-218.735  1.00 43.35           C  
ANISOU 9914  CB  LEU D 103     6538   4194   5742   1072   -421     20       C  
ATOM   9915  CG  LEU D 103     104.484 -29.380-218.312  1.00 48.40           C  
ANISOU 9915  CG  LEU D 103     7312   4709   6368   1203   -467     26       C  
ATOM   9916  CD1 LEU D 103     103.999 -29.905-216.959  1.00 56.46           C  
ANISOU 9916  CD1 LEU D 103     8408   5668   7376   1148   -519    115       C  
ATOM   9917  CD2 LEU D 103     104.361 -30.455-219.355  1.00 51.40           C  
ANISOU 9917  CD2 LEU D 103     7862   4940   6726   1231   -480    -23       C  
ATOM   9918  N   VAL D 104     105.101 -25.066-218.349  1.00 29.27           N  
ANISOU 9918  N   VAL D 104     4354   2769   3998   1112   -329    -11       N  
ATOM   9919  CA  VAL D 104     105.338 -23.724-218.875  1.00 30.72           C  
ANISOU 9919  CA  VAL D 104     4405   3077   4189   1080   -281    -43       C  
ATOM   9920  C   VAL D 104     105.138 -23.704-220.382  1.00 33.80           C  
ANISOU 9920  C   VAL D 104     4822   3449   4571   1062   -251    -98       C  
ATOM   9921  O   VAL D 104     104.496 -22.800-220.926  1.00 34.46           O  
ANISOU 9921  O   VAL D 104     4860   3579   4655    971   -227   -102       O  
ATOM   9922  CB  VAL D 104     106.747 -23.233-218.493  1.00 39.10           C  
ANISOU 9922  CB  VAL D 104     5354   4249   5253   1177   -268    -62       C  
ATOM   9923  CG1 VAL D 104     107.081 -21.943-219.233  1.00 37.73           C  
ANISOU 9923  CG1 VAL D 104     5068   4190   5078   1136   -218   -100       C  
ATOM   9924  CG2 VAL D 104     106.836 -22.990-216.990  1.00 39.42           C  
ANISOU 9924  CG2 VAL D 104     5357   4328   5294   1168   -298     -6       C  
ATOM   9925  N   PHE D 105     105.695 -24.689-221.076  1.00 34.75           N  
ANISOU 9925  N   PHE D 105     5021   3503   4679   1155   -253   -143       N  
ATOM   9926  CA  PHE D 105     105.471 -24.865-222.510  1.00 44.33           C  
ANISOU 9926  CA  PHE D 105     6287   4685   5873   1138   -228   -199       C  
ATOM   9927  C   PHE D 105     104.650 -26.121-222.739  1.00 50.72           C  
ANISOU 9927  C   PHE D 105     7268   5337   6667   1107   -268   -193       C  
ATOM   9928  O   PHE D 105     105.193 -27.231-222.667  1.00 54.40           O  
ANISOU 9928  O   PHE D 105     7837   5710   7123   1213   -290   -212       O  
ATOM   9929  CB  PHE D 105     106.805 -24.973-223.247  1.00 41.71           C  
ANISOU 9929  CB  PHE D 105     5913   4410   5526   1270   -189   -268       C  
ATOM   9930  CG  PHE D 105     107.630 -23.747-223.181  1.00 40.31           C  
ANISOU 9930  CG  PHE D 105     5569   4393   5352   1275   -149   -276       C  
ATOM   9931  CD1 PHE D 105     107.305 -22.644-223.940  1.00 50.86           C  
ANISOU 9931  CD1 PHE D 105     6844   5802   6679   1176   -113   -287       C  
ATOM   9932  CD2 PHE D 105     108.742 -23.696-222.385  1.00 47.59           C  
ANISOU 9932  CD2 PHE D 105     6404   5395   6282   1373   -151   -271       C  
ATOM   9933  CE1 PHE D 105     108.076 -21.511-223.892  1.00 57.71           C  
ANISOU 9933  CE1 PHE D 105     7577   6806   7542   1165    -78   -292       C  
ATOM   9934  CE2 PHE D 105     109.511 -22.559-222.332  1.00 53.09           C  
ANISOU 9934  CE2 PHE D 105     6951   6245   6974   1356   -117   -278       C  
ATOM   9935  CZ  PHE D 105     109.188 -21.471-223.096  1.00 60.33           C  
ANISOU 9935  CZ  PHE D 105     7821   7222   7881   1248    -79   -289       C  
ATOM   9936  N   PRO D 106     103.347 -26.012-222.989  1.00 57.14           N  
ANISOU 9936  N   PRO D 106     8121   6116   7473    965   -283   -166       N  
ATOM   9937  CA  PRO D 106     102.610 -27.201-223.439  1.00 78.02           C  
ANISOU 9937  CA  PRO D 106    10936   8618  10092    916   -321   -171       C  
ATOM   9938  C   PRO D 106     103.242 -27.799-224.684  1.00 85.13           C  
ANISOU 9938  C   PRO D 106    11918   9465  10962   1001   -301   -254       C  
ATOM   9939  O   PRO D 106     103.508 -29.006-224.742  1.00 86.41           O  
ANISOU 9939  O   PRO D 106    12229   9496  11106   1072   -328   -278       O  
ATOM   9940  CB  PRO D 106     101.195 -26.660-223.707  1.00 75.39           C  
ANISOU 9940  CB  PRO D 106    10577   8315   9752    746   -330   -135       C  
ATOM   9941  CG  PRO D 106     101.122 -25.345-222.998  1.00 66.60           C  
ANISOU 9941  CG  PRO D 106     9302   7335   8668    722   -306    -97       C  
ATOM   9942  CD  PRO D 106     102.516 -24.796-222.965  1.00 62.38           C  
ANISOU 9942  CD  PRO D 106     8680   6875   8147    849   -268   -134       C  
ATOM   9943  N   ARG D 107     103.549 -26.956-225.659  1.00 85.22           N  
ANISOU 9943  N   ARG D 107    11840   9576  10965   1003   -253   -301       N  
ATOM   9944  CA  ARG D 107     104.032 -27.380-226.963  1.00 80.00           C  
ANISOU 9944  CA  ARG D 107    11245   8887  10263   1064   -225   -384       C  
ATOM   9945  C   ARG D 107     105.536 -27.165-227.151  1.00 84.01           C  
ANISOU 9945  C   ARG D 107    11666   9485  10769   1225   -173   -439       C  
ATOM   9946  O   ARG D 107     106.357 -27.855-226.545  1.00 87.70           O  
ANISOU 9946  O   ARG D 107    12159   9917  11247   1362   -182   -447       O  
ATOM   9947  CB  ARG D 107     103.250 -26.628-228.032  1.00 75.63           C  
ANISOU 9947  CB  ARG D 107    10661   8390   9686    938   -209   -395       C  
ATOM   9948  CG  ARG D 107     101.746 -26.752-227.820  1.00 76.06           C  
ANISOU 9948  CG  ARG D 107    10769   8392   9741    777   -262   -336       C  
ATOM   9949  CD  ARG D 107     101.005 -25.428-227.904  1.00 82.05           C  
ANISOU 9949  CD  ARG D 107    11396   9269  10512    671   -253   -293       C  
ATOM   9950  NE  ARG D 107      99.852 -25.400-227.007  1.00 90.64           N  
ANISOU 9950  NE  ARG D 107    12472  10348  11620    563   -295   -218       N  
ATOM   9951  CZ  ARG D 107      98.686 -24.826-227.290  1.00 92.26           C  
ANISOU 9951  CZ  ARG D 107    12633  10604  11818    442   -313   -183       C  
ATOM   9952  NH1 ARG D 107      98.510 -24.241-228.466  1.00 92.76           N  
ANISOU 9952  NH1 ARG D 107    12673  10718  11854    410   -301   -212       N  
ATOM   9953  NH2 ARG D 107      97.691 -24.844-226.412  1.00 92.01           N  
ANISOU 9953  NH2 ARG D 107    12578  10582  11801    355   -345   -117       N  
ATOM   9954  N   ALA D 119      98.402 -26.338-247.887  1.00 74.70           N  
ANISOU 9954  N   ALA D 119    11562   8514   8307   -135   -234  -1035       N  
ATOM   9955  CA  ALA D 119      97.676 -25.885-246.703  1.00 74.42           C  
ANISOU 9955  CA  ALA D 119    11403   8483   8391   -171   -293   -923       C  
ATOM   9956  C   ALA D 119      96.322 -25.179-246.943  1.00 82.17           C  
ANISOU 9956  C   ALA D 119    12321   9535   9363   -327   -391   -824       C  
ATOM   9957  O   ALA D 119      95.734 -24.679-245.982  1.00 85.22           O  
ANISOU 9957  O   ALA D 119    12588   9947   9844   -344   -431   -732       O  
ATOM   9958  CB  ALA D 119      98.581 -24.956-245.905  1.00 67.58           C  
ANISOU 9958  CB  ALA D 119    10371   7693   7612    -53   -220   -883       C  
ATOM   9959  N   PRO D 120      95.810 -25.153-248.187  1.00 74.43           N  
ANISOU 9959  N   PRO D 120    11419   8594   8268   -433   -432   -842       N  
ATOM   9960  CA  PRO D 120      94.795 -24.133-248.514  1.00 70.49           C  
ANISOU 9960  CA  PRO D 120    10821   8205   7757   -540   -509   -740       C  
ATOM   9961  C   PRO D 120      93.493 -24.291-247.748  1.00 70.72           C  
ANISOU 9961  C   PRO D 120    10795   8225   7851   -635   -610   -658       C  
ATOM   9962  O   PRO D 120      92.960 -23.295-247.241  1.00 60.47           O  
ANISOU 9962  O   PRO D 120     9347   7012   6617   -638   -642   -558       O  
ATOM   9963  CB  PRO D 120      94.584 -24.317-250.028  1.00 69.33           C  
ANISOU 9963  CB  PRO D 120    10797   8088   7459   -633   -535   -790       C  
ATOM   9964  CG  PRO D 120      95.656 -25.277-250.476  1.00 68.23           C  
ANISOU 9964  CG  PRO D 120    10805   7864   7255   -554   -450   -925       C  
ATOM   9965  CD  PRO D 120      95.917 -26.128-249.285  1.00 70.98           C  
ANISOU 9965  CD  PRO D 120    11172   8093   7704   -475   -432   -949       C  
ATOM   9966  N   GLU D 121      92.957 -25.513-247.656  1.00 65.94           N  
ANISOU 9966  N   GLU D 121    10310   7521   7222   -715   -661   -698       N  
ATOM   9967  CA  GLU D 121      91.699 -25.718-246.942  1.00 63.08           C  
ANISOU 9967  CA  GLU D 121     9891   7168   6909   -825   -755   -620       C  
ATOM   9968  C   GLU D 121      91.819 -25.381-245.464  1.00 59.94           C  
ANISOU 9968  C   GLU D 121     9360   6767   6649   -739   -726   -558       C  
ATOM   9969  O   GLU D 121      90.863 -24.876-244.866  1.00 55.58           O  
ANISOU 9969  O   GLU D 121     8677   6291   6148   -794   -783   -464       O  
ATOM   9970  CB  GLU D 121      91.223 -27.161-247.100  1.00 63.48           C  
ANISOU 9970  CB  GLU D 121    10119   7099   6902   -940   -809   -679       C  
ATOM   9971  CG  GLU D 121      90.190 -27.349-248.190  1.00 80.10           C  
ANISOU 9971  CG  GLU D 121    12286   9257   8891  -1117   -907   -675       C  
ATOM   9972  CD  GLU D 121      90.715 -26.994-249.568  1.00 98.75           C  
ANISOU 9972  CD  GLU D 121    14719  11661  11139  -1101   -878   -734       C  
ATOM   9973  OE1 GLU D 121      89.894 -26.660-250.451  1.00106.47           O  
ANISOU 9973  OE1 GLU D 121    15686  12735  12031  -1223   -958   -699       O  
ATOM   9974  OE2 GLU D 121      91.948 -27.053-249.771  1.00104.12           O  
ANISOU 9974  OE2 GLU D 121    15461  12290  11810   -967   -777   -813       O  
ATOM   9975  N   GLN D 122      92.965 -25.666-244.851  1.00 55.41           N  
ANISOU 9975  N   GLN D 122     8812   6113   6128   -603   -639   -608       N  
ATOM   9976  CA  GLN D 122      93.106 -25.354-243.436  1.00 46.34           C  
ANISOU 9976  CA  GLN D 122     7543   4962   5101   -525   -614   -551       C  
ATOM   9977  C   GLN D 122      93.243 -23.850-243.219  1.00 46.64           C  
ANISOU 9977  C   GLN D 122     7407   5125   5190   -461   -587   -479       C  
ATOM   9978  O   GLN D 122      92.652 -23.298-242.286  1.00 52.11           O  
ANISOU 9978  O   GLN D 122     7973   5867   5960   -464   -613   -398       O  
ATOM   9979  CB  GLN D 122      94.292 -26.110-242.841  1.00 56.63           C  
ANISOU 9979  CB  GLN D 122     8925   6150   6441   -395   -539   -622       C  
ATOM   9980  CG  GLN D 122      94.483 -25.884-241.346  1.00 68.78           C  
ANISOU 9980  CG  GLN D 122    10354   7682   8098   -318   -517   -566       C  
ATOM   9981  CD  GLN D 122      93.270 -26.291-240.516  1.00 79.28           C  
ANISOU 9981  CD  GLN D 122    11662   8996   9465   -433   -594   -495       C  
ATOM   9982  OE1 GLN D 122      92.497 -27.173-240.904  1.00 86.29           O  
ANISOU 9982  OE1 GLN D 122    12662   9828  10294   -562   -659   -509       O  
ATOM   9983  NE2 GLN D 122      93.103 -25.649-239.363  1.00 74.61           N  
ANISOU 9983  NE2 GLN D 122    10927   8458   8963   -396   -586   -421       N  
ATOM   9984  N   LEU D 123      94.005 -23.170-244.079  1.00 47.71           N  
ANISOU 9984  N   LEU D 123     7541   5310   5276   -409   -536   -508       N  
ATOM   9985  CA  LEU D 123      94.086 -21.713-244.011  1.00 44.81           C  
ANISOU 9985  CA  LEU D 123     7037   5048   4941   -369   -521   -438       C  
ATOM   9986  C   LEU D 123      92.710 -21.080-244.170  1.00 46.13           C  
ANISOU 9986  C   LEU D 123     7128   5299   5102   -463   -615   -348       C  
ATOM   9987  O   LEU D 123      92.342 -20.178-243.413  1.00 42.76           O  
ANISOU 9987  O   LEU D 123     6574   4928   4747   -429   -627   -271       O  
ATOM   9988  CB  LEU D 123      95.041 -21.193-245.086  1.00 44.71           C  
ANISOU 9988  CB  LEU D 123     7060   5076   4850   -332   -459   -483       C  
ATOM   9989  CG  LEU D 123      95.177 -19.674-245.172  1.00 46.48           C  
ANISOU 9989  CG  LEU D 123     7177   5396   5089   -307   -446   -411       C  
ATOM   9990  CD1 LEU D 123      95.547 -19.099-243.801  1.00 51.66           C  
ANISOU 9990  CD1 LEU D 123     7718   6050   5862   -219   -410   -368       C  
ATOM   9991  CD2 LEU D 123      96.213 -19.280-246.203  1.00 48.82           C  
ANISOU 9991  CD2 LEU D 123     7519   5732   5298   -285   -376   -459       C  
ATOM   9992  N   LEU D 124      91.927 -21.561-245.138  1.00 45.67           N  
ANISOU 9992  N   LEU D 124     7145   5254   4952   -579   -686   -359       N  
ATOM   9993  CA  LEU D 124      90.611 -20.986-245.395  1.00 46.22           C  
ANISOU 9993  CA  LEU D 124     7133   5423   5004   -666   -783   -273       C  
ATOM   9994  C   LEU D 124      89.675 -21.130-244.200  1.00 46.93           C  
ANISOU 9994  C   LEU D 124     7118   5533   5179   -690   -828   -209       C  
ATOM   9995  O   LEU D 124      88.976 -20.177-243.841  1.00 43.49           O  
ANISOU 9995  O   LEU D 124     6549   5192   4785   -671   -865   -125       O  
ATOM   9996  CB  LEU D 124      89.990 -21.628-246.637  1.00 47.00           C  
ANISOU 9996  CB  LEU D 124     7341   5536   4982   -798   -854   -304       C  
ATOM   9997  CG  LEU D 124      90.161 -20.784-247.896  1.00 55.25           C  
ANISOU 9997  CG  LEU D 124     8406   6653   5934   -804   -862   -295       C  
ATOM   9998  CD1 LEU D 124      89.486 -21.449-249.097  1.00 60.17           C  
ANISOU 9998  CD1 LEU D 124     9139   7295   6428   -945   -941   -325       C  
ATOM   9999  CD2 LEU D 124      89.604 -19.394-247.679  1.00 51.67           C  
ANISOU 9999  CD2 LEU D 124     7806   6302   5522   -763   -900   -186       C  
ATOM  10000  N   SER D 125      89.619 -22.317-243.582  1.00 44.64           N  
ANISOU10000  N   SER D 125     6892   5157   4911   -732   -828   -247       N  
ATOM  10001  CA  SER D 125      88.723 -22.475-242.438  1.00 45.51           C  
ANISOU10001  CA  SER D 125     6902   5298   5092   -770   -866   -183       C  
ATOM  10002  C   SER D 125      89.100 -21.517-241.310  1.00 41.71           C  
ANISOU10002  C   SER D 125     6288   4845   4715   -639   -810   -136       C  
ATOM  10003  O   SER D 125      88.226 -20.930-240.667  1.00 42.80           O  
ANISOU10003  O   SER D 125     6290   5073   4898   -643   -845    -60       O  
ATOM  10004  CB  SER D 125      88.716 -23.926-241.946  1.00 57.39           C  
ANISOU10004  CB  SER D 125     8523   6687   6597   -840   -871   -230       C  
ATOM  10005  OG  SER D 125      90.022 -24.384-241.664  1.00 62.52           O  
ANISOU10005  OG  SER D 125     9270   7212   7272   -732   -787   -303       O  
ATOM  10006  N   GLN D 126      90.398 -21.324-241.078  1.00 36.92           N  
ANISOU10006  N   GLN D 126     5715   4171   4142   -523   -723   -181       N  
ATOM  10007  CA  GLN D 126      90.837 -20.357-240.078  1.00 36.48           C  
ANISOU10007  CA  GLN D 126     5545   4140   4174   -408   -672   -142       C  
ATOM  10008  C   GLN D 126      90.530 -18.929-240.507  1.00 37.63           C  
ANISOU10008  C   GLN D 126     5601   4385   4313   -374   -690    -82       C  
ATOM  10009  O   GLN D 126      90.171 -18.087-239.672  1.00 35.26           O  
ANISOU10009  O   GLN D 126     5186   4134   4076   -319   -691    -23       O  
ATOM  10010  CB  GLN D 126      92.333 -20.504-239.827  1.00 41.47           C  
ANISOU10010  CB  GLN D 126     6233   4693   4831   -303   -580   -206       C  
ATOM  10011  CG  GLN D 126      92.717 -21.721-239.012  1.00 48.00           C  
ANISOU10011  CG  GLN D 126     7128   5417   5692   -290   -558   -248       C  
ATOM  10012  CD  GLN D 126      94.208 -21.937-239.015  1.00 52.61           C  
ANISOU10012  CD  GLN D 126     7769   5938   6281   -181   -474   -319       C  
ATOM  10013  OE1 GLN D 126      94.720 -22.747-239.783  1.00 69.61           O  
ANISOU10013  OE1 GLN D 126    10045   8029   8374   -182   -458   -394       O  
ATOM  10014  NE2 GLN D 126      94.917 -21.202-238.172  1.00 49.67           N  
ANISOU10014  NE2 GLN D 126     7308   5590   5977    -84   -422   -299       N  
ATOM  10015  N   ALA D 127      90.711 -18.625-241.794  1.00 34.23           N  
ANISOU10015  N   ALA D 127     5231   3975   3801   -399   -702    -99       N  
ATOM  10016  CA  ALA D 127      90.420 -17.276-242.266  1.00 38.15           C  
ANISOU10016  CA  ALA D 127     5663   4550   4280   -369   -728    -37       C  
ATOM  10017  C   ALA D 127      88.931 -16.981-242.182  1.00 37.01           C  
ANISOU10017  C   ALA D 127     5423   4501   4138   -416   -822     40       C  
ATOM  10018  O   ALA D 127      88.538 -15.896-241.731  1.00 39.49           O  
ANISOU10018  O   ALA D 127     5638   4871   4495   -346   -835    105       O  
ATOM  10019  CB  ALA D 127      90.924 -17.087-243.702  1.00 36.61           C  
ANISOU10019  CB  ALA D 127     5565   4361   3985   -400   -724    -69       C  
ATOM  10020  N   ARG D 128      88.088 -17.932-242.613  1.00 38.41           N  
ANISOU10020  N   ARG D 128     5628   4703   4264   -533   -888     32       N  
ATOM  10021  CA  ARG D 128      86.644 -17.714-242.548  1.00 40.43           C  
ANISOU10021  CA  ARG D 128     5773   5075   4514   -586   -980    106       C  
ATOM  10022  C   ARG D 128      86.201 -17.486-241.112  1.00 44.90           C  
ANISOU10022  C   ARG D 128     6209   5674   5176   -530   -964    150       C  
ATOM  10023  O   ARG D 128      85.395 -16.587-240.834  1.00 39.46           O  
ANISOU10023  O   ARG D 128     5395   5086   4511   -479  -1002    219       O  
ATOM  10024  CB  ARG D 128      85.874 -18.896-243.134  1.00 38.39           C  
ANISOU10024  CB  ARG D 128     5568   4836   4183   -745  -1052     86       C  
ATOM  10025  CG  ARG D 128      85.988 -19.086-244.634  1.00 47.90           C  
ANISOU10025  CG  ARG D 128     6888   6039   5272   -820  -1091     51       C  
ATOM  10026  CD  ARG D 128      84.849 -19.974-245.121  1.00 50.74           C  
ANISOU10026  CD  ARG D 128     7258   6461   5560   -986  -1190     59       C  
ATOM  10027  NE  ARG D 128      85.063 -20.479-246.465  1.00 68.80           N  
ANISOU10027  NE  ARG D 128     9692   8719   7730  -1077  -1219      3       N  
ATOM  10028  CZ  ARG D 128      85.679 -21.622-246.748  1.00 80.53           C  
ANISOU10028  CZ  ARG D 128    11342  10084   9172  -1139  -1186    -90       C  
ATOM  10029  NH1 ARG D 128      86.155 -22.384-245.772  1.00 77.89           N  
ANISOU10029  NH1 ARG D 128    11046   9642   8905  -1116  -1126   -131       N  
ATOM  10030  NH2 ARG D 128      85.820 -22.003-248.015  1.00 81.21           N  
ANISOU10030  NH2 ARG D 128    11561  10153   9141  -1217  -1213   -142       N  
ATOM  10031  N   ASP D 129      86.713 -18.296-240.181  1.00 34.75           N  
ANISOU10031  N   ASP D 129     4956   4306   3943   -531   -908    109       N  
ATOM  10032  CA  ASP D 129      86.322 -18.111-238.794  1.00 36.67           C  
ANISOU10032  CA  ASP D 129     5082   4582   4267   -484   -888    149       C  
ATOM  10033  C   ASP D 129      86.692 -16.722-238.302  1.00 36.31           C  
ANISOU10033  C   ASP D 129     4963   4554   4278   -338   -846    182       C  
ATOM  10034  O   ASP D 129      85.907 -16.071-237.604  1.00 39.47           O  
ANISOU10034  O   ASP D 129     5237   5041   4716   -289   -864    238       O  
ATOM  10035  CB  ASP D 129      86.976 -19.157-237.901  1.00 37.19           C  
ANISOU10035  CB  ASP D 129     5216   4542   4374   -499   -833    102       C  
ATOM  10036  CG  ASP D 129      86.795 -18.821-236.439  1.00 46.05           C  
ANISOU10036  CG  ASP D 129     6228   5692   5578   -434   -798    140       C  
ATOM  10037  OD1 ASP D 129      85.656 -18.980-235.949  1.00 47.59           O  
ANISOU10037  OD1 ASP D 129     6323   5984   5776   -495   -841    189       O  
ATOM  10038  OD2 ASP D 129      87.764 -18.351-235.803  1.00 50.90           O  
ANISOU10038  OD2 ASP D 129     6849   6246   6245   -325   -729    122       O  
ATOM  10039  N   PHE D 130      87.883 -16.245-238.664  1.00 33.21           N  
ANISOU10039  N   PHE D 130     4650   4085   3885   -269   -790    145       N  
ATOM  10040  CA  PHE D 130      88.302 -14.926-238.219  1.00 31.11           C  
ANISOU10040  CA  PHE D 130     4336   3821   3663   -149   -753    173       C  
ATOM  10041  C   PHE D 130      87.427 -13.830-238.815  1.00 33.10           C  
ANISOU10041  C   PHE D 130     4530   4161   3886   -116   -819    239       C  
ATOM  10042  O   PHE D 130      87.018 -12.893-238.111  1.00 33.49           O  
ANISOU10042  O   PHE D 130     4494   4250   3981    -25   -820    285       O  
ATOM  10043  CB  PHE D 130      89.763 -14.675-238.573  1.00 33.03           C  
ANISOU10043  CB  PHE D 130     4674   3977   3897   -108   -683    123       C  
ATOM  10044  CG  PHE D 130      90.169 -13.253-238.351  1.00 36.86           C  
ANISOU10044  CG  PHE D 130     5135   4461   4408    -13   -658    156       C  
ATOM  10045  CD1 PHE D 130      90.284 -12.751-237.067  1.00 31.54           C  
ANISOU10045  CD1 PHE D 130     4396   3777   3809     65   -622    171       C  
ATOM  10046  CD2 PHE D 130      90.373 -12.398-239.428  1.00 33.52           C  
ANISOU10046  CD2 PHE D 130     4764   4046   3926     -9   -676    176       C  
ATOM  10047  CE1 PHE D 130      90.631 -11.429-236.856  1.00 34.23           C  
ANISOU10047  CE1 PHE D 130     4734   4106   4168    145   -603    198       C  
ATOM  10048  CE2 PHE D 130      90.720 -11.074-239.216  1.00 39.32           C  
ANISOU10048  CE2 PHE D 130     5496   4765   4678     68   -659    210       C  
ATOM  10049  CZ  PHE D 130      90.845 -10.592-237.935  1.00 38.12           C  
ANISOU10049  CZ  PHE D 130     5288   4594   4603    144   -623    219       C  
ATOM  10050  N   ILE D 131      87.146 -13.917-240.118  1.00 32.01           N  
ANISOU10050  N   ILE D 131     4443   4052   3667   -182   -875    244       N  
ATOM  10051  CA  ILE D 131      86.279 -12.920-240.737  1.00 35.53           C  
ANISOU10051  CA  ILE D 131     4837   4584   4077   -147   -950    314       C  
ATOM  10052  C   ILE D 131      84.912 -12.931-240.066  1.00 38.31           C  
ANISOU10052  C   ILE D 131     5042   5054   4459   -137  -1006    367       C  
ATOM  10053  O   ILE D 131      84.311 -11.875-239.834  1.00 35.24           O  
ANISOU10053  O   ILE D 131     4572   4728   4091    -35  -1036    424       O  
ATOM  10054  CB  ILE D 131      86.160 -13.163-242.255  1.00 34.11           C  
ANISOU10054  CB  ILE D 131     4740   4427   3794   -236  -1009    310       C  
ATOM  10055  CG1 ILE D 131      87.524 -13.012-242.935  1.00 35.42           C  
ANISOU10055  CG1 ILE D 131     5040   4496   3921   -235   -944    260       C  
ATOM  10056  CG2 ILE D 131      85.155 -12.196-242.848  1.00 34.80           C  
ANISOU10056  CG2 ILE D 131     4765   4613   3843   -196  -1100    391       C  
ATOM  10057  CD1 ILE D 131      88.103 -11.616-242.811  1.00 36.67           C  
ANISOU10057  CD1 ILE D 131     5210   4621   4101   -130   -912    295       C  
ATOM  10058  N   ASN D 132      84.406 -14.121-239.729  1.00 38.21           N  
ANISOU10058  N   ASN D 132     4995   5075   4446   -242  -1020    348       N  
ATOM  10059  CA  ASN D 132      83.147 -14.191-238.993  1.00 38.96           C  
ANISOU10059  CA  ASN D 132     4936   5300   4567   -246  -1062    398       C  
ATOM  10060  C   ASN D 132      83.258 -13.475-237.653  1.00 35.34           C  
ANISOU10060  C   ASN D 132     4397   4836   4193   -116  -1001    412       C  
ATOM  10061  O   ASN D 132      82.344 -12.734-237.267  1.00 35.62           O  
ANISOU10061  O   ASN D 132     4305   4983   4245    -34  -1032    465       O  
ATOM  10062  CB  ASN D 132      82.706 -15.643-238.807  1.00 39.46           C  
ANISOU10062  CB  ASN D 132     4998   5384   4611   -404  -1080    375       C  
ATOM  10063  CG  ASN D 132      82.292 -16.299-240.108  1.00 48.32           C  
ANISOU10063  CG  ASN D 132     6182   6540   5639   -542  -1159    368       C  
ATOM  10064  OD1 ASN D 132      81.994 -15.623-241.090  1.00 45.57           O  
ANISOU10064  OD1 ASN D 132     5829   6247   5237   -520  -1218    399       O  
ATOM  10065  ND2 ASN D 132      82.259 -17.627-240.118  1.00 49.71           N  
ANISOU10065  ND2 ASN D 132     6426   6677   5786   -689  -1166    327       N  
ATOM  10066  N   GLN D 133      84.385 -13.646-236.943  1.00 32.90           N  
ANISOU10066  N   GLN D 133     4162   4406   3934    -86   -914    364       N  
ATOM  10067  CA  GLN D 133      84.552 -12.957-235.662  1.00 37.43           C  
ANISOU10067  CA  GLN D 133     4673   4970   4579     31   -857    372       C  
ATOM  10068  C   GLN D 133      84.553 -11.453-235.859  1.00 40.48           C  
ANISOU10068  C   GLN D 133     5049   5359   4971    168   -866    407       C  
ATOM  10069  O   GLN D 133      83.938 -10.715-235.079  1.00 34.45           O  
ANISOU10069  O   GLN D 133     4189   4658   4242    270   -864    439       O  
ATOM  10070  CB  GLN D 133      85.855 -13.365-234.963  1.00 32.92           C  
ANISOU10070  CB  GLN D 133     4188   4269   4051     37   -771    315       C  
ATOM  10071  CG  GLN D 133      85.982 -14.802-234.499  1.00 38.16           C  
ANISOU10071  CG  GLN D 133     4878   4899   4719    -69   -753    281       C  
ATOM  10072  CD  GLN D 133      87.278 -15.014-233.715  1.00 41.66           C  
ANISOU10072  CD  GLN D 133     5393   5227   5210    -27   -672    234       C  
ATOM  10073  OE1 GLN D 133      87.632 -14.205-232.850  1.00 36.96           O  
ANISOU10073  OE1 GLN D 133     4762   4620   4661     71   -628    240       O  
ATOM  10074  NE2 GLN D 133      88.005 -16.075-234.041  1.00 36.78           N  
ANISOU10074  NE2 GLN D 133     4879   4522   4573    -94   -655    184       N  
ATOM  10075  N   TYR D 134      85.252 -10.981-236.896  1.00 37.62           N  
ANISOU10075  N   TYR D 134     4797   4927   4569    172   -874    399       N  
ATOM  10076  CA  TYR D 134      85.322  -9.550-237.156  1.00 36.97           C  
ANISOU10076  CA  TYR D 134     4738   4826   4484    289   -888    436       C  
ATOM  10077  C   TYR D 134      83.936  -8.965-237.413  1.00 38.44           C  
ANISOU10077  C   TYR D 134     4818   5139   4649    353   -972    503       C  
ATOM  10078  O   TYR D 134      83.570  -7.941-236.820  1.00 36.52           O  
ANISOU10078  O   TYR D 134     4527   4911   4437    488   -971    533       O  
ATOM  10079  CB  TYR D 134      86.257  -9.258-238.337  1.00 33.92           C  
ANISOU10079  CB  TYR D 134     4490   4355   4041    253   -887    423       C  
ATOM  10080  CG  TYR D 134      86.227  -7.790-238.703  1.00 32.53           C  
ANISOU10080  CG  TYR D 134     4357   4155   3849    358   -915    472       C  
ATOM  10081  CD1 TYR D 134      86.929  -6.851-237.952  1.00 38.77           C  
ANISOU10081  CD1 TYR D 134     5189   4859   4683    447   -860    466       C  
ATOM  10082  CD2 TYR D 134      85.449  -7.337-239.756  1.00 37.00           C  
ANISOU10082  CD2 TYR D 134     4924   4782   4352    368  -1004    528       C  
ATOM  10083  CE1 TYR D 134      86.881  -5.500-238.260  1.00 41.48           C  
ANISOU10083  CE1 TYR D 134     5594   5161   5007    539   -890    513       C  
ATOM  10084  CE2 TYR D 134      85.399  -5.993-240.075  1.00 40.03           C  
ANISOU10084  CE2 TYR D 134     5363   5130   4718    470  -1037    580       C  
ATOM  10085  CZ  TYR D 134      86.120  -5.084-239.326  1.00 38.20           C  
ANISOU10085  CZ  TYR D 134     5189   4795   4530    554   -979    571       C  
ATOM  10086  OH  TYR D 134      86.072  -3.751-239.627  1.00 42.50           O  
ANISOU10086  OH  TYR D 134     5812   5285   5053    651  -1015    623       O  
ATOM  10087  N   TYR D 135      83.158  -9.589-238.314  1.00 36.86           N  
ANISOU10087  N   TYR D 135     4582   5033   4391    261  -1047    524       N  
ATOM  10088  CA  TYR D 135      81.855  -9.028-238.653  1.00 42.83           C  
ANISOU10088  CA  TYR D 135     5226   5929   5119    324  -1137    592       C  
ATOM  10089  C   TYR D 135      80.856  -9.182-237.515  1.00 43.54           C  
ANISOU10089  C   TYR D 135     5143   6145   5254    370  -1131    609       C  
ATOM  10090  O   TYR D 135      79.934  -8.370-237.391  1.00 41.67           O  
ANISOU10090  O   TYR D 135     4801   6013   5018    492  -1177    660       O  
ATOM  10091  CB  TYR D 135      81.321  -9.630-239.967  1.00 44.07           C  
ANISOU10091  CB  TYR D 135     5392   6162   5191    202  -1226    612       C  
ATOM  10092  CG  TYR D 135      81.873  -8.853-241.136  1.00 42.25           C  
ANISOU10092  CG  TYR D 135     5294   5856   4902    228  -1257    630       C  
ATOM  10093  CD1 TYR D 135      81.278  -7.665-241.548  1.00 35.57           C  
ANISOU10093  CD1 TYR D 135     4427   5055   4035    354  -1326    700       C  
ATOM  10094  CD2 TYR D 135      83.046  -9.254-241.768  1.00 39.61           C  
ANISOU10094  CD2 TYR D 135     5112   5402   4535    138  -1212    579       C  
ATOM  10095  CE1 TYR D 135      81.815  -6.915-242.579  1.00 42.72           C  
ANISOU10095  CE1 TYR D 135     5470   5881   4882    372  -1354    724       C  
ATOM  10096  CE2 TYR D 135      83.589  -8.511-242.799  1.00 37.69           C  
ANISOU10096  CE2 TYR D 135     4991   5097   4232    153  -1232    598       C  
ATOM  10097  CZ  TYR D 135      82.974  -7.345-243.196  1.00 40.38           C  
ANISOU10097  CZ  TYR D 135     5318   5475   4548    262  -1304    674       C  
ATOM  10098  OH  TYR D 135      83.511  -6.613-244.217  1.00 48.33           O  
ANISOU10098  OH  TYR D 135     6459   6415   5487    265  -1327    700       O  
ATOM  10099  N   SER D 136      81.032 -10.185-236.659  1.00 43.15           N  
ANISOU10099  N   SER D 136     5065   6091   5240    282  -1075    569       N  
ATOM  10100  CA  SER D 136      80.210 -10.248-235.457  1.00 47.44           C  
ANISOU10100  CA  SER D 136     5452   6749   5823    328  -1053    584       C  
ATOM  10101  C   SER D 136      80.510  -9.071-234.537  1.00 42.93           C  
ANISOU10101  C   SER D 136     4879   6124   5306    510   -996    582       C  
ATOM  10102  O   SER D 136      79.589  -8.454-233.987  1.00 49.05           O  
ANISOU10102  O   SER D 136     5525   7018   6095    627  -1008    615       O  
ATOM  10103  CB  SER D 136      80.436 -11.582-234.742  1.00 59.61           C  
ANISOU10103  CB  SER D 136     6991   8275   7383    185  -1004    545       C  
ATOM  10104  OG  SER D 136      79.858 -11.573-233.447  1.00 74.40           O  
ANISOU10104  OG  SER D 136     8734  10239   9295    231   -963    555       O  
ATOM  10105  N   SER D 137      81.793  -8.726-234.381  1.00 37.29           N  
ANISOU10105  N   SER D 137     4310   5239   4620    536   -934    542       N  
ATOM  10106  CA  SER D 137      82.179  -7.684-233.434  1.00 42.06           C  
ANISOU10106  CA  SER D 137     4933   5776   5271    685   -877    532       C  
ATOM  10107  C   SER D 137      81.595  -6.322-233.791  1.00 50.38           C  
ANISOU10107  C   SER D 137     5976   6855   6310    848   -928    577       C  
ATOM  10108  O   SER D 137      81.337  -5.513-232.894  1.00 48.21           O  
ANISOU10108  O   SER D 137     5663   6588   6067    990   -898    578       O  
ATOM  10109  CB  SER D 137      83.699  -7.585-233.343  1.00 45.11           C  
ANISOU10109  CB  SER D 137     5475   5985   5677    659   -812    484       C  
ATOM  10110  OG  SER D 137      84.251  -6.861-234.433  1.00 42.05           O  
ANISOU10110  OG  SER D 137     5210   5514   5254    675   -843    497       O  
ATOM  10111  N   ILE D 138      81.408  -6.026-235.079  1.00 47.17           N  
ANISOU10111  N   ILE D 138     5617   6453   5851    838  -1004    615       N  
ATOM  10112  CA  ILE D 138      80.811  -4.756-235.480  1.00 50.19           C  
ANISOU10112  CA  ILE D 138     6001   6855   6214   1000  -1065    667       C  
ATOM  10113  C   ILE D 138      79.325  -4.897-235.776  1.00 57.02           C  
ANISOU10113  C   ILE D 138     6691   7924   7049   1038  -1147    720       C  
ATOM  10114  O   ILE D 138      78.735  -4.002-236.392  1.00 56.70           O  
ANISOU10114  O   ILE D 138     6647   7919   6978   1160  -1222    772       O  
ATOM  10115  CB  ILE D 138      81.540  -4.134-236.686  1.00 50.47           C  
ANISOU10115  CB  ILE D 138     6209   6765   6203    986  -1103    687       C  
ATOM  10116  CG1 ILE D 138      81.531  -5.095-237.879  1.00 42.95           C  
ANISOU10116  CG1 ILE D 138     5271   5858   5191    820  -1154    693       C  
ATOM  10117  CG2 ILE D 138      82.958  -3.714-236.295  1.00 49.32           C  
ANISOU10117  CG2 ILE D 138     6222   6435   6085    977  -1022    641       C  
ATOM  10118  CD1 ILE D 138      81.920  -4.427-239.205  1.00 43.42           C  
ANISOU10118  CD1 ILE D 138     5473   5842   5184    816  -1211    729       C  
ATOM  10119  N   LYS D 139      78.712  -6.017-235.382  1.00 53.07           N  
ANISOU10119  N   LYS D 139     6049   7564   6553    927  -1141    711       N  
ATOM  10120  CA  LYS D 139      77.262  -6.210-235.494  1.00 56.71           C  
ANISOU10120  CA  LYS D 139     6311   8250   6984    948  -1212    759       C  
ATOM  10121  C   LYS D 139      76.793  -6.155-236.946  1.00 58.02           C  
ANISOU10121  C   LYS D 139     6486   8477   7080    909  -1325    811       C  
ATOM  10122  O   LYS D 139      75.764  -5.556-237.261  1.00 56.91           O  
ANISOU10122  O   LYS D 139     6232   8478   6913   1027  -1402    868       O  
ATOM  10123  CB  LYS D 139      76.492  -5.189-234.646  1.00 63.60           C  
ANISOU10123  CB  LYS D 139     7069   9210   7885   1170  -1201    779       C  
ATOM  10124  CG  LYS D 139      76.519  -5.445-233.138  1.00 68.30           C  
ANISOU10124  CG  LYS D 139     7587   9831   8532   1191  -1100    736       C  
ATOM  10125  CD  LYS D 139      77.871  -5.117-232.517  1.00 71.09           C  
ANISOU10125  CD  LYS D 139     8120   9960   8931   1207  -1012    680       C  
ATOM  10126  CE  LYS D 139      77.904  -5.460-231.033  1.00 74.07           C  
ANISOU10126  CE  LYS D 139     8424  10368   9350   1211   -918    638       C  
ATOM  10127  NZ  LYS D 139      79.265  -5.247-230.458  1.00 73.26           N  
ANISOU10127  NZ  LYS D 139     8490  10058   9285   1203   -840    585       N  
ATOM  10128  N   ARG D 140      77.543  -6.795-237.843  1.00 59.14           N  
ANISOU10128  N   ARG D 140     6762   8522   7187    748  -1337    792       N  
ATOM  10129  CA  ARG D 140      77.132  -6.840-239.243  1.00 61.13           C  
ANISOU10129  CA  ARG D 140     7033   8833   7360    689  -1444    837       C  
ATOM  10130  C   ARG D 140      77.244  -8.245-239.819  1.00 62.03           C  
ANISOU10130  C   ARG D 140     7167   8972   7430    453  -1460    808       C  
ATOM  10131  O   ARG D 140      77.515  -8.404-241.013  1.00 57.70           O  
ANISOU10131  O   ARG D 140     6723   8385   6816    367  -1515    815       O  
ATOM  10132  CB  ARG D 140      77.945  -5.857-240.094  1.00 59.92           C  
ANISOU10132  CB  ARG D 140     7068   8518   7180    761  -1462    852       C  
ATOM  10133  CG  ARG D 140      77.470  -4.413-240.013  1.00 66.29           C  
ANISOU10133  CG  ARG D 140     7864   9330   7995    991  -1503    908       C  
ATOM  10134  CD  ARG D 140      77.868  -3.653-241.278  1.00 88.01           C  
ANISOU10134  CD  ARG D 140    10778  11981  10679   1013  -1571    951       C  
ATOM  10135  NE  ARG D 140      79.296  -3.340-241.308  1.00 95.71           N  
ANISOU10135  NE  ARG D 140    11958  12740  11667    976  -1494    910       N  
ATOM  10136  CZ  ARG D 140      79.970  -2.971-242.395  1.00 88.26           C  
ANISOU10136  CZ  ARG D 140    11182  11692  10660    926  -1523    930       C  
ATOM  10137  NH1 ARG D 140      79.357  -2.873-243.568  1.00 89.50           N  
ANISOU10137  NH1 ARG D 140    11340  11930  10736    908  -1633    991       N  
ATOM  10138  NH2 ARG D 140      81.267  -2.700-242.307  1.00 79.51           N  
ANISOU10138  NH2 ARG D 140    10236  10409   9564    887  -1444    891       N  
ATOM  10139  N   SER D 141      77.038  -9.269-238.992  1.00 64.05           N  
ANISOU10139  N   SER D 141     7337   9286   7715    344  -1414    775       N  
ATOM  10140  CA ASER D 141      77.086 -10.638-239.484  0.31 60.04           C  
ANISOU10140  CA ASER D 141     6862   8789   7161    119  -1433    746       C  
ATOM  10141  CA BSER D 141      77.081 -10.640-239.483  0.69 60.39           C  
ANISOU10141  CA BSER D 141     6905   8834   7205    119  -1434    746       C  
ATOM  10142  C   SER D 141      76.002 -10.862-240.533  1.00 60.91           C  
ANISOU10142  C   SER D 141     6882   9073   7187     39  -1558    799       C  
ATOM  10143  O   SER D 141      74.888 -10.341-240.424  1.00 64.57           O  
ANISOU10143  O   SER D 141     7172   9719   7642    131  -1619    858       O  
ATOM  10144  CB ASER D 141      76.921 -11.623-238.326  0.31 57.83           C  
ANISOU10144  CB ASER D 141     6501   8547   6923     24  -1371    715       C  
ATOM  10145  CB BSER D 141      76.897 -11.626-238.330  0.69 57.93           C  
ANISOU10145  CB BSER D 141     6511   8564   6935     24  -1372    716       C  
ATOM  10146  OG ASER D 141      77.065 -12.963-238.769  0.31 56.56           O  
ANISOU10146  OG ASER D 141     6410   8363   6719   -192  -1387    681       O  
ATOM  10147  OG BSER D 141      78.007 -11.595-237.458  0.69 54.66           O  
ANISOU10147  OG BSER D 141     6199   7980   6588     69  -1264    663       O  
ATOM  10148  N   GLY D 142      76.334 -11.647-241.556  1.00 58.57           N  
ANISOU10148  N   GLY D 142     6704   8726   6823   -129  -1596    775       N  
ATOM  10149  CA  GLY D 142      75.397 -11.915-242.626  1.00 53.96           C  
ANISOU10149  CA  GLY D 142     6057   8298   6148   -227  -1720    820       C  
ATOM  10150  C   GLY D 142      75.147 -10.760-243.571  1.00 55.12           C  
ANISOU10150  C   GLY D 142     6214   8480   6249    -94  -1802    881       C  
ATOM  10151  O   GLY D 142      74.324 -10.901-244.486  1.00 61.14           O  
ANISOU10151  O   GLY D 142     6915   9386   6929   -164  -1916    927       O  
ATOM  10152  N   SER D 143      75.820  -9.623-243.388  1.00 47.42           N  
ANISOU10152  N   SER D 143     5322   7376   5318     89  -1755    888       N  
ATOM  10153  CA  SER D 143      75.632  -8.489-244.283  1.00 50.49           C  
ANISOU10153  CA  SER D 143     5749   7775   5660    218  -1836    952       C  
ATOM  10154  C   SER D 143      76.249  -8.781-245.649  1.00 49.57           C  
ANISOU10154  C   SER D 143     5810   7573   5452     88  -1877    939       C  
ATOM  10155  O   SER D 143      77.020  -9.729-245.816  1.00 44.32           O  
ANISOU10155  O   SER D 143     5259   6809   4772    -69  -1821    869       O  
ATOM  10156  CB  SER D 143      76.256  -7.226-243.686  1.00 47.10           C  
ANISOU10156  CB  SER D 143     5391   7207   5298    429  -1771    958       C  
ATOM  10157  OG  SER D 143      77.661  -7.373-243.507  1.00 38.42           O  
ANISOU10157  OG  SER D 143     4471   5898   4228    381  -1666    891       O  
ATOM  10158  N   GLN D 144      75.905  -7.942-246.637  1.00 42.87           N  
ANISOU10158  N   GLN D 144     4990   6764   4534    163  -1975   1008       N  
ATOM  10159  CA  GLN D 144      76.580  -8.020-247.931  1.00 43.63           C  
ANISOU10159  CA  GLN D 144     5271   6769   4536     61  -2005   1001       C  
ATOM  10160  C   GLN D 144      78.091  -7.864-247.772  1.00 41.70           C  
ANISOU10160  C   GLN D 144     5219   6299   4325     61  -1882    937       C  
ATOM  10161  O   GLN D 144      78.868  -8.614-248.375  1.00 46.17           O  
ANISOU10161  O   GLN D 144     5916   6786   4842    -88  -1846    877       O  
ATOM  10162  CB  GLN D 144      76.022  -6.957-248.895  1.00 53.47           C  
ANISOU10162  CB  GLN D 144     6528   8079   5708    171  -2126   1096       C  
ATOM  10163  CG  GLN D 144      74.874  -7.417-249.801  1.00 56.56           C  
ANISOU10163  CG  GLN D 144     6811   8677   6000     73  -2270   1148       C  
ATOM  10164  CD  GLN D 144      74.503  -6.383-250.898  1.00 69.15           C  
ANISOU10164  CD  GLN D 144     8456  10310   7507    174  -2393   1244       C  
ATOM  10165  OE1 GLN D 144      74.936  -5.222-250.860  1.00 67.59           O  
ANISOU10165  OE1 GLN D 144     8356   9994   7332    342  -2378   1282       O  
ATOM  10166  NE2 GLN D 144      73.701  -6.811-251.872  1.00 63.82           N  
ANISOU10166  NE2 GLN D 144     7725   9797   6726     64  -2521   1284       N  
ATOM  10167  N   ALA D 145      78.528  -6.909-246.943  1.00 36.72           N  
ANISOU10167  N   ALA D 145     4606   5571   3776    226  -1816    945       N  
ATOM  10168  CA  ALA D 145      79.956  -6.682-246.755  1.00 35.29           C  
ANISOU10168  CA  ALA D 145     4592   5194   3624    223  -1704    890       C  
ATOM  10169  C   ALA D 145      80.633  -7.926-246.193  1.00 46.33           C  
ANISOU10169  C   ALA D 145     6002   6539   5061     91  -1605    795       C  
ATOM  10170  O   ALA D 145      81.759  -8.267-246.581  1.00 37.42           O  
ANISOU10170  O   ALA D 145     5016   5293   3908      8  -1538    738       O  
ATOM  10171  CB  ALA D 145      80.176  -5.487-245.819  1.00 38.62           C  
ANISOU10171  CB  ALA D 145     5014   5533   4127    415  -1657    914       C  
ATOM  10172  N   HIS D 146      79.955  -8.611-245.273  1.00 44.06           N  
ANISOU10172  N   HIS D 146     5566   6342   4831     73  -1595    779       N  
ATOM  10173  CA  HIS D 146      80.491  -9.836-244.686  1.00 39.05           C  
ANISOU10173  CA  HIS D 146     4947   5657   4234    -49  -1513    697       C  
ATOM  10174  C   HIS D 146      80.692 -10.912-245.747  1.00 34.65           C  
ANISOU10174  C   HIS D 146     4484   5096   3585   -233  -1542    654       C  
ATOM  10175  O   HIS D 146      81.779 -11.494-245.855  1.00 36.33           O  
ANISOU10175  O   HIS D 146     4827   5184   3794   -302  -1463    581       O  
ATOM  10176  CB  HIS D 146      79.539 -10.322-243.599  1.00 34.89           C  
ANISOU10176  CB  HIS D 146     4239   5250   3766    -46  -1516    705       C  
ATOM  10177  CG  HIS D 146      80.027 -11.521-242.856  1.00 44.01           C  
ANISOU10177  CG  HIS D 146     5414   6345   4962   -158  -1436    632       C  
ATOM  10178  ND1 HIS D 146      79.227 -12.228-241.983  1.00 47.51           N  
ANISOU10178  ND1 HIS D 146     5718   6894   5440   -211  -1438    635       N  
ATOM  10179  CD2 HIS D 146      81.238 -12.127-242.835  1.00 48.45           C  
ANISOU10179  CD2 HIS D 146     6119   6756   5534   -222  -1353    558       C  
ATOM  10180  CE1 HIS D 146      79.925 -13.219-241.456  1.00 45.57           C  
ANISOU10180  CE1 HIS D 146     5544   6548   5223   -304  -1364    569       C  
ATOM  10181  NE2 HIS D 146      81.150 -13.177-241.949  1.00 44.25           N  
ANISOU10181  NE2 HIS D 146     5544   6225   5044   -302  -1312    520       N  
ATOM  10182  N   GLU D 147      79.640 -11.192-246.533  1.00 37.04           N  
ANISOU10182  N   GLU D 147     4722   5540   3810   -311  -1656    697       N  
ATOM  10183  CA  GLU D 147      79.719 -12.194-247.604  1.00 45.18           C  
ANISOU10183  CA  GLU D 147     5851   6575   4740   -493  -1696    656       C  
ATOM  10184  C   GLU D 147      80.789 -11.835-248.623  1.00 45.96           C  
ANISOU10184  C   GLU D 147     6136   6555   4770   -500  -1667    631       C  
ATOM  10185  O   GLU D 147      81.532 -12.705-249.086  1.00 39.79           O  
ANISOU10185  O   GLU D 147     5483   5693   3944   -615  -1621    554       O  
ATOM  10186  CB  GLU D 147      78.383 -12.338-248.344  1.00 52.37           C  
ANISOU10186  CB  GLU D 147     6657   7672   5567   -567  -1838    719       C  
ATOM  10187  CG  GLU D 147      77.126 -12.167-247.540  1.00 74.88           C  
ANISOU10187  CG  GLU D 147     9285  10696   8468   -511  -1891    780       C  
ATOM  10188  CD  GLU D 147      76.934 -13.240-246.493  1.00 99.04           C  
ANISOU10188  CD  GLU D 147    12271  13773  11587   -608  -1838    734       C  
ATOM  10189  OE1 GLU D 147      77.442 -14.365-246.685  1.00107.77           O  
ANISOU10189  OE1 GLU D 147    13493  14792  12664   -767  -1805    662       O  
ATOM  10190  OE2 GLU D 147      76.271 -12.955-245.475  1.00106.42           O  
ANISOU10190  OE2 GLU D 147    13037  14806  12593   -523  -1828    770       O  
ATOM  10191  N   GLN D 148      80.851 -10.568-249.024  1.00 37.97           N  
ANISOU10191  N   GLN D 148     5148   5538   3743   -379  -1697    697       N  
ATOM  10192  CA  GLN D 148      81.815 -10.188-250.050  1.00 37.35           C  
ANISOU10192  CA  GLN D 148     5244   5364   3584   -402  -1674    683       C  
ATOM  10193  C   GLN D 148      83.248 -10.307-249.548  1.00 35.41           C  
ANISOU10193  C   GLN D 148     5101   4963   3391   -389  -1532    605       C  
ATOM  10194  O   GLN D 148      84.152 -10.631-250.329  1.00 36.11           O  
ANISOU10194  O   GLN D 148     5327   4984   3407   -468  -1486    552       O  
ATOM  10195  CB  GLN D 148      81.534  -8.762-250.542  1.00 36.58           C  
ANISOU10195  CB  GLN D 148     5159   5286   3454   -279  -1743    781       C  
ATOM  10196  CG  GLN D 148      80.219  -8.622-251.224  1.00 44.14           C  
ANISOU10196  CG  GLN D 148     6026   6404   4341   -287  -1891    860       C  
ATOM  10197  CD  GLN D 148      79.942  -7.187-251.614  1.00 40.17           C  
ANISOU10197  CD  GLN D 148     5545   5905   3814   -139  -1961    961       C  
ATOM  10198  OE1 GLN D 148      80.833  -6.342-251.570  1.00 43.09           O  
ANISOU10198  OE1 GLN D 148     6032   6143   4198    -65  -1900    968       O  
ATOM  10199  NE2 GLN D 148      78.707  -6.901-251.959  1.00 40.86           N  
ANISOU10199  NE2 GLN D 148     5518   6145   3863    -94  -2093   1042       N  
ATOM  10200  N   ARG D 149      83.483 -10.073-248.256  1.00 32.78           N  
ANISOU10200  N   ARG D 149     4698   4581   3175   -292  -1460    595       N  
ATOM  10201  CA  ARG D 149      84.848 -10.183-247.767  1.00 36.79           C  
ANISOU10201  CA  ARG D 149     5293   4957   3730   -281  -1333    525       C  
ATOM  10202  C   ARG D 149      85.268 -11.651-247.668  1.00 37.67           C  
ANISOU10202  C   ARG D 149     5439   5036   3838   -398  -1279    430       C  
ATOM  10203  O   ARG D 149      86.420 -11.994-247.964  1.00 37.42           O  
ANISOU10203  O   ARG D 149     5519   4918   3782   -432  -1197    361       O  
ATOM  10204  CB  ARG D 149      84.976  -9.458-246.427  1.00 39.06           C  
ANISOU10204  CB  ARG D 149     5505   5203   4135   -145  -1279    543       C  
ATOM  10205  CG  ARG D 149      86.311  -9.594-245.762  1.00 36.90           C  
ANISOU10205  CG  ARG D 149     5293   4811   3917   -133  -1155    475       C  
ATOM  10206  CD  ARG D 149      87.443  -9.110-246.648  1.00 35.17           C  
ANISOU10206  CD  ARG D 149     5215   4520   3628   -159  -1111    460       C  
ATOM  10207  NE  ARG D 149      88.706  -9.188-245.909  1.00 37.07           N  
ANISOU10207  NE  ARG D 149     5489   4670   3927   -140   -993    399       N  
ATOM  10208  CZ  ARG D 149      89.886  -9.329-246.500  1.00 34.61           C  
ANISOU10208  CZ  ARG D 149     5278   4311   3562   -193   -923    349       C  
ATOM  10209  NH1 ARG D 149      89.932  -9.415-247.832  1.00 36.00           N  
ANISOU10209  NH1 ARG D 149     5541   4515   3622   -272   -956    351       N  
ATOM  10210  NH2 ARG D 149      90.994  -9.421-245.780  1.00 35.50           N  
ANISOU10210  NH2 ARG D 149     5398   4361   3728   -171   -822    296       N  
ATOM  10211  N   LEU D 150      84.336 -12.537-247.305  1.00 37.72           N  
ANISOU10211  N   LEU D 150     5356   5115   3860   -462  -1327    425       N  
ATOM  10212  CA  LEU D 150      84.627 -13.974-247.325  1.00 41.55           C  
ANISOU10212  CA  LEU D 150     5902   5558   4327   -584  -1294    339       C  
ATOM  10213  C   LEU D 150      84.965 -14.442-248.737  1.00 41.77           C  
ANISOU10213  C   LEU D 150     6070   5573   4228   -692  -1317    297       C  
ATOM  10214  O   LEU D 150      85.940 -15.174-248.938  1.00 40.54           O  
ANISOU10214  O   LEU D 150     6030   5324   4049   -733  -1240    210       O  
ATOM  10215  CB  LEU D 150      83.443 -14.779-246.779  1.00 39.72           C  
ANISOU10215  CB  LEU D 150     5557   5417   4117   -659  -1358    355       C  
ATOM  10216  CG  LEU D 150      83.056 -14.655-245.304  1.00 41.53           C  
ANISOU10216  CG  LEU D 150     5648   5670   4463   -582  -1327    381       C  
ATOM  10217  CD1 LEU D 150      81.660 -15.243-245.067  1.00 41.24           C  
ANISOU10217  CD1 LEU D 150     5481   5775   4415   -673  -1414    420       C  
ATOM  10218  CD2 LEU D 150      84.100 -15.341-244.415  1.00 41.18           C  
ANISOU10218  CD2 LEU D 150     5666   5495   4486   -574  -1216    306       C  
ATOM  10219  N   GLN D 151      84.167 -14.023-249.733  1.00 35.86           N  
ANISOU10219  N   GLN D 151     5314   4922   3390   -732  -1422    357       N  
ATOM  10220  CA  GLN D 151      84.459 -14.383-251.124  1.00 37.25           C  
ANISOU10220  CA  GLN D 151     5628   5095   3430   -836  -1448    321       C  
ATOM  10221  C   GLN D 151      85.807 -13.821-251.555  1.00 43.89           C  
ANISOU10221  C   GLN D 151     6588   5844   4244   -784  -1353    288       C  
ATOM  10222  O   GLN D 151      86.569 -14.484-252.266  1.00 43.11           O  
ANISOU10222  O   GLN D 151     6618   5696   4068   -855  -1303    207       O  
ATOM  10223  CB  GLN D 151      83.346 -13.880-252.055  1.00 45.81           C  
ANISOU10223  CB  GLN D 151     6671   6310   4424   -874  -1586    406       C  
ATOM  10224  CG  GLN D 151      82.054 -14.686-251.948  1.00 63.77           C  
ANISOU10224  CG  GLN D 151     8846   8701   6684   -980  -1688    423       C  
ATOM  10225  CD  GLN D 151      80.839 -13.966-252.513  1.00 81.53           C  
ANISOU10225  CD  GLN D 151    10990  11109   8878   -970  -1828    529       C  
ATOM  10226  OE1 GLN D 151      80.904 -13.334-253.570  1.00 88.14           O  
ANISOU10226  OE1 GLN D 151    11899  11969   9621   -965  -1879    568       O  
ATOM  10227  NE2 GLN D 151      79.717 -14.063-251.804  1.00 84.21           N  
ANISOU10227  NE2 GLN D 151    11156  11568   9273   -964  -1892    580       N  
ATOM  10228  N   GLU D 152      86.133 -12.614-251.095  1.00 42.25           N  
ANISOU10228  N   GLU D 152     6340   5614   4097   -661  -1322    346       N  
ATOM  10229  CA  GLU D 152      87.396 -11.982-251.457  1.00 41.31           C  
ANISOU10229  CA  GLU D 152     6324   5422   3949   -625  -1234    326       C  
ATOM  10230  C   GLU D 152      88.589 -12.746-250.888  1.00 46.43           C  
ANISOU10230  C   GLU D 152     7015   5980   4646   -623  -1105    222       C  
ATOM  10231  O   GLU D 152      89.597 -12.947-251.576  1.00 37.09           O  
ANISOU10231  O   GLU D 152     5940   4763   3392   -658  -1035    162       O  
ATOM  10232  CB  GLU D 152      87.394 -10.544-250.957  1.00 45.51           C  
ANISOU10232  CB  GLU D 152     6808   5941   4541   -503  -1239    413       C  
ATOM  10233  CG  GLU D 152      88.507  -9.668-251.496  1.00 46.35           C  
ANISOU10233  CG  GLU D 152     7023   5991   4595   -489  -1176    421       C  
ATOM  10234  CD  GLU D 152      88.318  -8.231-251.063  1.00 43.83           C  
ANISOU10234  CD  GLU D 152     6679   5650   4325   -378  -1205    516       C  
ATOM  10235  OE1 GLU D 152      88.639  -7.908-249.898  1.00 41.70           O  
ANISOU10235  OE1 GLU D 152     6353   5326   4165   -295  -1146    509       O  
ATOM  10236  OE2 GLU D 152      87.803  -7.432-251.876  1.00 41.20           O  
ANISOU10236  OE2 GLU D 152     6388   5350   3915   -372  -1292    598       O  
ATOM  10237  N   VAL D 153      88.510 -13.152-249.614  1.00 36.23           N  
ANISOU10237  N   VAL D 153     5637   4656   3473   -573  -1070    203       N  
ATOM  10238  CA  VAL D 153      89.584 -13.947-249.023  1.00 37.81           C  
ANISOU10238  CA  VAL D 153     5874   4773   3721   -561   -959    109       C  
ATOM  10239  C   VAL D 153      89.727 -15.276-249.746  1.00 38.31           C  
ANISOU10239  C   VAL D 153     6037   4816   3701   -662   -954     19       C  
ATOM  10240  O   VAL D 153      90.839 -15.726-250.042  1.00 41.76           O  
ANISOU10240  O   VAL D 153     6563   5201   4105   -660   -865    -63       O  
ATOM  10241  CB  VAL D 153      89.331 -14.151-247.524  1.00 37.35           C  
ANISOU10241  CB  VAL D 153     5706   4689   3794   -497   -939    116       C  
ATOM  10242  CG1 VAL D 153      90.306 -15.187-246.943  1.00 42.44           C  
ANISOU10242  CG1 VAL D 153     6395   5250   4480   -491   -843     20       C  
ATOM  10243  CG2 VAL D 153      89.451 -12.820-246.826  1.00 37.22           C  
ANISOU10243  CG2 VAL D 153     5619   4671   3850   -388   -923    184       C  
ATOM  10244  N   GLU D 154      88.603 -15.934-250.017  1.00 38.13           N  
ANISOU10244  N   GLU D 154     6003   4841   3643   -750  -1049     31       N  
ATOM  10245  CA  GLU D 154      88.664 -17.243-250.652  1.00 48.16           C  
ANISOU10245  CA  GLU D 154     7387   6078   4833   -855  -1052    -58       C  
ATOM  10246  C   GLU D 154      89.294 -17.148-252.036  1.00 45.69           C  
ANISOU10246  C   GLU D 154     7204   5772   4385   -899  -1032    -99       C  
ATOM  10247  O   GLU D 154      90.047 -18.039-252.446  1.00 46.61           O  
ANISOU10247  O   GLU D 154     7437   5828   4446   -926   -968   -202       O  
ATOM  10248  CB  GLU D 154      87.263 -17.853-250.716  1.00 56.95           C  
ANISOU10248  CB  GLU D 154     8460   7256   5924   -965  -1171    -25       C  
ATOM  10249  CG  GLU D 154      87.245 -19.319-251.128  1.00 77.54           C  
ANISOU10249  CG  GLU D 154    11194   9805   8462  -1084  -1179   -120       C  
ATOM  10250  CD  GLU D 154      85.945 -20.006-250.770  1.00 88.12           C  
ANISOU10250  CD  GLU D 154    12474  11196   9811  -1196  -1280    -88       C  
ATOM  10251  OE1 GLU D 154      85.150 -19.412-250.007  1.00 91.98           O  
ANISOU10251  OE1 GLU D 154    12803  11766  10378  -1161  -1324      1       O  
ATOM  10252  OE2 GLU D 154      85.721 -21.139-251.250  1.00 91.07           O  
ANISOU10252  OE2 GLU D 154    12963  11532  10108  -1323  -1313   -152       O  
ATOM  10253  N   ALA D 155      89.024 -16.057-252.759  1.00 47.03           N  
ANISOU10253  N   ALA D 155     7359   6014   4494   -897  -1082    -21       N  
ATOM  10254  CA  ALA D 155      89.620 -15.885-254.080  1.00 49.41           C  
ANISOU10254  CA  ALA D 155     7783   6333   4656   -945  -1061    -51       C  
ATOM  10255  C   ALA D 155      91.114 -15.608-253.982  1.00 50.00           C  
ANISOU10255  C   ALA D 155     7902   6356   4742   -873   -923   -106       C  
ATOM  10256  O   ALA D 155      91.896 -16.113-254.793  1.00 49.76           O  
ANISOU10256  O   ALA D 155     7982   6314   4612   -909   -859   -190       O  
ATOM  10257  CB  ALA D 155      88.915 -14.761-254.847  1.00 49.10           C  
ANISOU10257  CB  ALA D 155     7725   6382   4548   -963  -1160     59       C  
ATOM  10258  N   GLU D 156      91.538 -14.812-252.997  1.00 47.62           N  
ANISOU10258  N   GLU D 156     7510   6031   4554   -773   -873    -62       N  
ATOM  10259  CA  GLU D 156      92.964 -14.526-252.870  1.00 43.04           C  
ANISOU10259  CA  GLU D 156     6954   5419   3981   -717   -745   -110       C  
ATOM  10260  C   GLU D 156      93.746 -15.774-252.453  1.00 44.36           C  
ANISOU10260  C   GLU D 156     7154   5524   4177   -691   -655   -230       C  
ATOM  10261  O   GLU D 156      94.889 -15.969-252.882  1.00 40.78           O  
ANISOU10261  O   GLU D 156     6759   5068   3666   -676   -555   -304       O  
ATOM  10262  CB  GLU D 156      93.201 -13.378-251.877  1.00 43.86           C  
ANISOU10262  CB  GLU D 156     6961   5508   4194   -627   -722    -35       C  
ATOM  10263  CG  GLU D 156      94.611 -12.814-251.983  1.00 50.42           C  
ANISOU10263  CG  GLU D 156     7819   6336   5003   -600   -607    -60       C  
ATOM  10264  CD  GLU D 156      94.909 -11.684-251.007  1.00 59.53           C  
ANISOU10264  CD  GLU D 156     8896   7468   6257   -528   -585      7       C  
ATOM  10265  OE1 GLU D 156      93.964 -11.113-250.423  1.00 51.66           O  
ANISOU10265  OE1 GLU D 156     7838   6461   5329   -491   -665     87       O  
ATOM  10266  OE2 GLU D 156      96.105 -11.377-250.819  1.00 57.56           O  
ANISOU10266  OE2 GLU D 156     8645   7214   6010   -508   -486    -22       O  
ATOM  10267  N   VAL D 157      93.170 -16.611-251.588  1.00 38.04           N  
ANISOU10267  N   VAL D 157     6315   4675   3461   -681   -686   -249       N  
ATOM  10268  CA  VAL D 157      93.876 -17.823-251.183  1.00 42.13           C  
ANISOU10268  CA  VAL D 157     6884   5119   4005   -649   -611   -358       C  
ATOM  10269  C   VAL D 157      93.972 -18.783-252.362  1.00 52.55           C  
ANISOU10269  C   VAL D 157     8349   6429   5190   -724   -610   -449       C  
ATOM  10270  O   VAL D 157      94.989 -19.457-252.557  1.00 44.73           O  
ANISOU10270  O   VAL D 157     7433   5399   4165   -681   -517   -551       O  
ATOM  10271  CB  VAL D 157      93.180 -18.469-249.972  1.00 44.36           C  
ANISOU10271  CB  VAL D 157     7105   5348   4403   -635   -652   -345       C  
ATOM  10272  CG1 VAL D 157      93.751 -19.868-249.681  1.00 48.84           C  
ANISOU10272  CG1 VAL D 157     7759   5820   4978   -614   -597   -455       C  
ATOM  10273  CG2 VAL D 157      93.344 -17.587-248.765  1.00 36.83           C  
ANISOU10273  CG2 VAL D 157     6021   4398   3576   -544   -626   -278       C  
ATOM  10274  N   ALA D 158      92.918 -18.844-253.172  1.00 49.95           N  
ANISOU10274  N   ALA D 158     8063   6141   4776   -833   -715   -416       N  
ATOM  10275  CA  ALA D 158      92.916 -19.722-254.338  1.00 57.27           C  
ANISOU10275  CA  ALA D 158     9140   7059   5561   -919   -726   -502       C  
ATOM  10276  C   ALA D 158      93.991 -19.317-255.336  1.00 59.21           C  
ANISOU10276  C   ALA D 158     9454   7348   5694   -901   -636   -549       C  
ATOM  10277  O   ALA D 158      94.666 -20.174-255.918  1.00 74.70           O  
ANISOU10277  O   ALA D 158    11535   9277   7572   -900   -570   -664       O  
ATOM  10278  CB  ALA D 158      91.537 -19.700-254.995  1.00 53.32           C  
ANISOU10278  CB  ALA D 158     8652   6619   4989  -1047   -867   -440       C  
ATOM  10279  N   ALA D 159      94.173 -18.009-255.532  1.00 54.79           N  
ANISOU10279  N   ALA D 159     8828   6861   5128   -886   -631   -461       N  
ATOM  10280  CA  ALA D 159      95.109 -17.493-256.523  1.00 55.96           C  
ANISOU10280  CA  ALA D 159     9036   7069   5157   -895   -554   -486       C  
ATOM  10281  C   ALA D 159      96.552 -17.547-256.035  1.00 61.39           C  
ANISOU10281  C   ALA D 159     9695   7743   5889   -792   -406   -555       C  
ATOM  10282  O   ALA D 159      97.468 -17.815-256.820  1.00 58.51           O  
ANISOU10282  O   ALA D 159     9402   7413   5415   -791   -315   -639       O  
ATOM  10283  CB  ALA D 159      94.740 -16.051-256.874  1.00 50.31           C  
ANISOU10283  CB  ALA D 159     8273   6425   4417   -926   -611   -356       C  
ATOM  10284  N   THR D 160      96.772 -17.271-254.752  1.00 48.59           N  
ANISOU10284  N   THR D 160     7959   6085   4418   -706   -381   -521       N  
ATOM  10285  CA  THR D 160      98.104 -17.017-254.226  1.00 46.91           C  
ANISOU10285  CA  THR D 160     7687   5885   4251   -615   -256   -557       C  
ATOM  10286  C   THR D 160      98.501 -17.942-253.087  1.00 51.01           C  
ANISOU10286  C   THR D 160     8168   6327   4887   -514   -209   -625       C  
ATOM  10287  O   THR D 160      99.668 -17.920-252.677  1.00 53.94           O  
ANISOU10287  O   THR D 160     8490   6716   5289   -431   -104   -670       O  
ATOM  10288  CB  THR D 160      98.217 -15.564-253.727  1.00 56.12           C  
ANISOU10288  CB  THR D 160     8753   7090   5480   -604   -260   -443       C  
ATOM  10289  OG1 THR D 160      97.487 -15.412-252.498  1.00 50.26           O  
ANISOU10289  OG1 THR D 160     7922   6291   4885   -560   -324   -380       O  
ATOM  10290  CG2 THR D 160      97.662 -14.596-254.767  1.00 57.56           C  
ANISOU10290  CG2 THR D 160     8984   7331   5556   -699   -329   -356       C  
ATOM  10291  N   GLY D 161      97.581 -18.748-252.562  1.00 44.80           N  
ANISOU10291  N   GLY D 161     7400   5460   4161   -524   -286   -629       N  
ATOM  10292  CA  GLY D 161      97.875 -19.544-251.394  1.00 47.53           C  
ANISOU10292  CA  GLY D 161     7714   5724   4622   -434   -255   -673       C  
ATOM  10293  C   GLY D 161      97.873 -18.798-250.074  1.00 49.64           C  
ANISOU10293  C   GLY D 161     7842   5988   5033   -375   -257   -591       C  
ATOM  10294  O   GLY D 161      98.061 -19.431-249.030  1.00 47.71           O  
ANISOU10294  O   GLY D 161     7566   5677   4883   -304   -239   -617       O  
ATOM  10295  N   THR D 162      97.678 -17.481-250.075  1.00 41.94           N  
ANISOU10295  N   THR D 162     6792   5075   4069   -399   -281   -494       N  
ATOM  10296  CA  THR D 162      97.607 -16.715-248.827  1.00 44.95           C  
ANISOU10296  CA  THR D 162     7053   5447   4578   -345   -288   -418       C  
ATOM  10297  C   THR D 162      96.700 -15.505-249.045  1.00 39.74           C  
ANISOU10297  C   THR D 162     6357   4828   3913   -397   -371   -304       C  
ATOM  10298  O   THR D 162      96.035 -15.386-250.076  1.00 40.36           O  
ANISOU10298  O   THR D 162     6497   4939   3898   -474   -434   -281       O  
ATOM  10299  CB  THR D 162      99.006 -16.311-248.343  1.00 43.93           C  
ANISOU10299  CB  THR D 162     6864   5344   4482   -268   -178   -445       C  
ATOM  10300  OG1 THR D 162      98.910 -15.759-247.015  1.00 42.92           O  
ANISOU10300  OG1 THR D 162     6634   5194   4482   -215   -189   -385       O  
ATOM  10301  CG2 THR D 162      99.612 -15.275-249.261  1.00 43.68           C  
ANISOU10301  CG2 THR D 162     6844   5396   4356   -314   -138   -418       C  
ATOM  10302  N   TYR D 163      96.641 -14.608-248.054  1.00 37.20           N  
ANISOU10302  N   TYR D 163     5942   4502   3690   -349   -377   -233       N  
ATOM  10303  CA  TYR D 163      95.815 -13.421-248.222  1.00 35.86           C  
ANISOU10303  CA  TYR D 163     5748   4360   3516   -374   -455   -128       C  
ATOM  10304  C   TYR D 163      96.346 -12.314-247.330  1.00 39.95           C  
ANISOU10304  C   TYR D 163     6199   4870   4112   -315   -417    -77       C  
ATOM  10305  O   TYR D 163      97.303 -12.503-246.577  1.00 35.65           O  
ANISOU10305  O   TYR D 163     5614   4308   3622   -266   -337   -122       O  
ATOM  10306  CB  TYR D 163      94.338 -13.717-247.940  1.00 34.97           C  
ANISOU10306  CB  TYR D 163     5601   4243   3441   -392   -564    -81       C  
ATOM  10307  CG  TYR D 163      93.984 -13.928-246.474  1.00 36.96           C  
ANISOU10307  CG  TYR D 163     5759   4459   3826   -328   -568    -67       C  
ATOM  10308  CD1 TYR D 163      94.269 -15.123-245.841  1.00 31.41           C  
ANISOU10308  CD1 TYR D 163     5059   3708   3169   -312   -530   -139       C  
ATOM  10309  CD2 TYR D 163      93.316 -12.944-245.755  1.00 33.22           C  
ANISOU10309  CD2 TYR D 163     5204   3997   3421   -282   -614     19       C  
ATOM  10310  CE1 TYR D 163      93.924 -15.336-244.506  1.00 33.92           C  
ANISOU10310  CE1 TYR D 163     5295   3996   3596   -264   -536   -121       C  
ATOM  10311  CE2 TYR D 163      92.962 -13.140-244.424  1.00 32.10           C  
ANISOU10311  CE2 TYR D 163     4976   3833   3389   -228   -615     29       C  
ATOM  10312  CZ  TYR D 163      93.275 -14.336-243.809  1.00 36.16           C  
ANISOU10312  CZ  TYR D 163     5491   4306   3944   -226   -575    -38       C  
ATOM  10313  OH  TYR D 163      92.929 -14.549-242.493  1.00 32.93           O  
ANISOU10313  OH  TYR D 163     5002   3877   3633   -182   -576    -23       O  
ATOM  10314  N   GLN D 164      95.738 -11.137-247.464  1.00 36.54           N  
ANISOU10314  N   GLN D 164     5761   4448   3673   -322   -480     17       N  
ATOM  10315  CA  GLN D 164      96.123  -9.960-246.694  1.00 33.69           C  
ANISOU10315  CA  GLN D 164     5362   4066   3373   -275   -459     71       C  
ATOM  10316  C   GLN D 164      94.950  -9.495-245.848  1.00 36.75           C  
ANISOU10316  C   GLN D 164     5686   4431   3846   -217   -539    140       C  
ATOM  10317  O   GLN D 164      93.811  -9.435-246.327  1.00 34.51           O  
ANISOU10317  O   GLN D 164     5406   4171   3534   -230   -631    188       O  
ATOM  10318  CB  GLN D 164      96.580  -8.812-247.609  1.00 39.66           C  
ANISOU10318  CB  GLN D 164     6193   4841   4035   -327   -454    123       C  
ATOM  10319  CG  GLN D 164      97.787  -9.152-248.480  1.00 48.33           C  
ANISOU10319  CG  GLN D 164     7343   5985   5034   -390   -364     57       C  
ATOM  10320  CD  GLN D 164      99.073  -9.240-247.678  1.00 50.51           C  
ANISOU10320  CD  GLN D 164     7564   6266   5363   -360   -257      3       C  
ATOM  10321  OE1 GLN D 164      99.253  -8.522-246.692  1.00 58.49           O  
ANISOU10321  OE1 GLN D 164     8527   7243   6452   -323   -251     40       O  
ATOM  10322  NE2 GLN D 164      99.973 -10.117-248.099  1.00 51.41           N  
ANISOU10322  NE2 GLN D 164     7682   6425   5426   -371   -175    -87       N  
ATOM  10323  N   LEU D 165      95.235  -9.168-244.587  1.00 28.84           N  
ANISOU10323  N   LEU D 165     4622   3394   2944   -151   -505    144       N  
ATOM  10324  CA  LEU D 165      94.233  -8.539-243.744  1.00 29.13           C  
ANISOU10324  CA  LEU D 165     4600   3414   3055    -84   -568    208       C  
ATOM  10325  C   LEU D 165      93.979  -7.104-244.167  1.00 33.33           C  
ANISOU10325  C   LEU D 165     5184   3930   3548    -70   -615    291       C  
ATOM  10326  O   LEU D 165      94.904  -6.372-244.535  1.00 35.63           O  
ANISOU10326  O   LEU D 165     5545   4200   3794   -104   -572    299       O  
ATOM  10327  CB  LEU D 165      94.692  -8.556-242.281  1.00 26.70           C  
ANISOU10327  CB  LEU D 165     4223   3070   2851    -21   -513    184       C  
ATOM  10328  CG  LEU D 165      94.970  -9.946-241.728  1.00 29.24           C  
ANISOU10328  CG  LEU D 165     4501   3393   3216    -22   -470    110       C  
ATOM  10329  CD1 LEU D 165      95.524  -9.763-240.306  1.00 33.18           C  
ANISOU10329  CD1 LEU D 165     4941   3860   3807     40   -418     97       C  
ATOM  10330  CD2 LEU D 165      93.721 -10.806-241.689  1.00 30.91           C  
ANISOU10330  CD2 LEU D 165     4676   3628   3442    -32   -537    116       C  
ATOM  10331  N   ARG D 166      92.715  -6.693-244.107  1.00 32.55           N  
ANISOU10331  N   ARG D 166     5055   3845   3465    -19   -705    355       N  
ATOM  10332  CA  ARG D 166      92.435  -5.266-244.098  1.00 28.97           C  
ANISOU10332  CA  ARG D 166     4647   3353   3006     37   -750    434       C  
ATOM  10333  C   ARG D 166      93.047  -4.641-242.843  1.00 29.99           C  
ANISOU10333  C   ARG D 166     4761   3418   3217     95   -692    424       C  
ATOM  10334  O   ARG D 166      93.274  -5.311-241.833  1.00 34.01           O  
ANISOU10334  O   ARG D 166     5192   3929   3801    118   -642    372       O  
ATOM  10335  CB  ARG D 166      90.933  -5.015-244.114  1.00 30.70           C  
ANISOU10335  CB  ARG D 166     4814   3612   3238    108   -855    498       C  
ATOM  10336  CG  ARG D 166      90.254  -5.413-245.454  1.00 31.44           C  
ANISOU10336  CG  ARG D 166     4935   3776   3236     45   -933    524       C  
ATOM  10337  CD  ARG D 166      88.748  -5.256-245.342  1.00 34.05           C  
ANISOU10337  CD  ARG D 166     5180   4172   3585    120  -1038    584       C  
ATOM  10338  NE  ARG D 166      88.082  -5.471-246.639  1.00 35.94           N  
ANISOU10338  NE  ARG D 166     5448   4483   3725     60  -1126    621       N  
ATOM  10339  CZ  ARG D 166      86.769  -5.643-246.760  1.00 41.40           C  
ANISOU10339  CZ  ARG D 166     6049   5267   4413     92  -1223    665       C  
ATOM  10340  NH1 ARG D 166      86.010  -5.621-245.667  1.00 38.70           N  
ANISOU10340  NH1 ARG D 166     5581   4961   4161    185  -1235    675       N  
ATOM  10341  NH2 ARG D 166      86.219  -5.828-247.960  1.00 37.17           N  
ANISOU10341  NH2 ARG D 166     5544   4802   3779     27  -1308    698       N  
ATOM  10342  N   GLU D 167      93.309  -3.339-242.918  1.00 31.12           N  
ANISOU10342  N   GLU D 167     4990   3499   3337    115   -703    477       N  
ATOM  10343  CA  GLU D 167      93.818  -2.625-241.746  1.00 33.32           C  
ANISOU10343  CA  GLU D 167     5270   3709   3682    165   -660    471       C  
ATOM  10344  C   GLU D 167      92.908  -2.814-240.537  1.00 32.00           C  
ANISOU10344  C   GLU D 167     4998   3550   3611    276   -679    466       C  
ATOM  10345  O   GLU D 167      93.380  -3.104-239.432  1.00 31.50           O  
ANISOU10345  O   GLU D 167     4879   3474   3615    293   -620    420       O  
ATOM  10346  CB  GLU D 167      93.988  -1.137-242.066  1.00 43.00           C  
ANISOU10346  CB  GLU D 167     6628   4851   4861    172   -691    539       C  
ATOM  10347  CG  GLU D 167      95.028  -0.866-243.159  1.00 72.77           C  
ANISOU10347  CG  GLU D 167    10504   8616   8528     43   -658    547       C  
ATOM  10348  CD  GLU D 167      95.204   0.616-243.473  1.00 88.21           C  
ANISOU10348  CD  GLU D 167    12611  10476  10429     33   -694    622       C  
ATOM  10349  OE1 GLU D 167      94.654   1.455-242.727  1.00 96.33           O  
ANISOU10349  OE1 GLU D 167    13669  11427  11506    135   -735    657       O  
ATOM  10350  OE2 GLU D 167      95.890   0.940-244.468  1.00 89.72           O  
ANISOU10350  OE2 GLU D 167    12901  10668  10522    -79   -680    645       O  
ATOM  10351  N   SER D 168      91.595  -2.662-240.726  1.00 38.05           N  
ANISOU10351  N   SER D 168     5728   4351   4379    351   -763    515       N  
ATOM  10352  CA ASER D 168      90.665  -2.787-239.606  0.14 35.75           C  
ANISOU10352  CA ASER D 168     5326   4090   4169    457   -779    514       C  
ATOM  10353  CA BSER D 168      90.660  -2.791-239.607  0.86 33.02           C  
ANISOU10353  CA BSER D 168     4979   3744   3822    457   -779    514       C  
ATOM  10354  C   SER D 168      90.690  -4.192-239.011  1.00 34.73           C  
ANISOU10354  C   SER D 168     5085   4022   4088    415   -734    451       C  
ATOM  10355  O   SER D 168      90.532  -4.366-237.787  1.00 34.50           O  
ANISOU10355  O   SER D 168     4981   3997   4132    470   -703    428       O  
ATOM  10356  CB ASER D 168      89.252  -2.416-240.058  0.14 37.37           C  
ANISOU10356  CB ASER D 168     5497   4350   4354    541   -880    580       C  
ATOM  10357  CB BSER D 168      89.247  -2.446-240.083  0.86 38.87           C  
ANISOU10357  CB BSER D 168     5685   4541   4542    538   -880    580       C  
ATOM  10358  OG ASER D 168      88.306  -2.693-239.043  0.14 38.80           O  
ANISOU10358  OG ASER D 168     5547   4593   4604    632   -890    575       O  
ATOM  10359  OG BSER D 168      88.877  -3.314-241.151  0.86 37.96           O  
ANISOU10359  OG BSER D 168     5547   4507   4370    454   -922    583       O  
ATOM  10360  N   GLU D 169      90.894  -5.212-239.857  1.00 30.37           N  
ANISOU10360  N   GLU D 169     4534   3514   3491    316   -732    423       N  
ATOM  10361  CA  GLU D 169      91.005  -6.581-239.373  1.00 30.19           C  
ANISOU10361  CA  GLU D 169     4437   3527   3506    271   -692    362       C  
ATOM  10362  C   GLU D 169      92.283  -6.793-238.575  1.00 28.85           C  
ANISOU10362  C   GLU D 169     4279   3304   3377    257   -600    305       C  
ATOM  10363  O   GLU D 169      92.281  -7.545-237.601  1.00 31.23           O  
ANISOU10363  O   GLU D 169     4512   3615   3738    270   -568    270       O  
ATOM  10364  CB  GLU D 169      90.948  -7.569-240.542  1.00 29.48           C  
ANISOU10364  CB  GLU D 169     4373   3481   3347    173   -714    340       C  
ATOM  10365  CG  GLU D 169      89.619  -7.567-241.242  1.00 32.26           C  
ANISOU10365  CG  GLU D 169     4693   3907   3660    173   -812    393       C  
ATOM  10366  CD  GLU D 169      89.687  -8.193-242.652  1.00 37.98           C  
ANISOU10366  CD  GLU D 169     5483   4661   4288     69   -842    380       C  
ATOM  10367  OE1 GLU D 169      90.792  -8.544-243.122  1.00 34.20           O  
ANISOU10367  OE1 GLU D 169     5081   4143   3770      7   -779    328       O  
ATOM  10368  OE2 GLU D 169      88.616  -8.352-243.248  1.00 34.93           O  
ANISOU10368  OE2 GLU D 169     5065   4346   3862     51   -927    418       O  
ATOM  10369  N   LEU D 170      93.397  -6.186-238.999  1.00 30.73           N  
ANISOU10369  N   LEU D 170     4602   3497   3577    222   -558    297       N  
ATOM  10370  CA  LEU D 170      94.619  -6.280-238.202  1.00 31.25           C  
ANISOU10370  CA  LEU D 170     4665   3531   3679    211   -476    248       C  
ATOM  10371  C   LEU D 170      94.400  -5.711-236.797  1.00 33.75           C  
ANISOU10371  C   LEU D 170     4937   3815   4071    292   -467    258       C  
ATOM  10372  O   LEU D 170      94.796  -6.321-235.795  1.00 31.95           O  
ANISOU10372  O   LEU D 170     4652   3590   3898    304   -422    217       O  
ATOM  10373  CB  LEU D 170      95.764  -5.550-238.903  1.00 32.95           C  
ANISOU10373  CB  LEU D 170     4970   3720   3831    150   -438    249       C  
ATOM  10374  CG  LEU D 170      97.130  -5.660-238.212  1.00 31.46           C  
ANISOU10374  CG  LEU D 170     4765   3522   3665    125   -354    199       C  
ATOM  10375  CD1 LEU D 170      97.593  -7.104-238.149  1.00 34.04           C  
ANISOU10375  CD1 LEU D 170     5035   3891   4006    110   -309    130       C  
ATOM  10376  CD2 LEU D 170      98.172  -4.782-238.895  1.00 38.50           C  
ANISOU10376  CD2 LEU D 170     5738   4405   4487     50   -321    211       C  
ATOM  10377  N   VAL D 171      93.767  -4.539-236.703  1.00 29.89           N  
ANISOU10377  N   VAL D 171     4482   3294   3581    354   -513    312       N  
ATOM  10378  CA  VAL D 171      93.545  -3.922-235.391  1.00 33.16           C  
ANISOU10378  CA  VAL D 171     4868   3675   4057    439   -503    315       C  
ATOM  10379  C   VAL D 171      92.682  -4.831-234.516  1.00 32.54           C  
ANISOU10379  C   VAL D 171     4670   3656   4037    485   -507    299       C  
ATOM  10380  O   VAL D 171      93.035  -5.147-233.370  1.00 30.45           O  
ANISOU10380  O   VAL D 171     4360   3386   3823    501   -461    265       O  
ATOM  10381  CB  VAL D 171      92.919  -2.527-235.558  1.00 32.93           C  
ANISOU10381  CB  VAL D 171     4910   3593   4007    514   -557    374       C  
ATOM  10382  CG1 VAL D 171      92.614  -1.930-234.170  1.00 34.49           C  
ANISOU10382  CG1 VAL D 171     5083   3757   4263    614   -543    367       C  
ATOM  10383  CG2 VAL D 171      93.868  -1.609-236.300  1.00 32.42           C  
ANISOU10383  CG2 VAL D 171     4980   3457   3880    449   -549    393       C  
ATOM  10384  N   PHE D 172      91.562  -5.306-235.070  1.00 33.73           N  
ANISOU10384  N   PHE D 172     4770   3872   4174    493   -564    326       N  
ATOM  10385  CA  PHE D 172      90.668  -6.196-234.336  1.00 35.89           C  
ANISOU10385  CA  PHE D 172     4930   4217   4491    513   -572    318       C  
ATOM  10386  C   PHE D 172      91.378  -7.484-233.929  1.00 37.71           C  
ANISOU10386  C   PHE D 172     5136   4448   4744    440   -519    263       C  
ATOM  10387  O   PHE D 172      91.230  -7.963-232.790  1.00 32.32           O  
ANISOU10387  O   PHE D 172     4388   3781   4111    461   -493    246       O  
ATOM  10388  CB  PHE D 172      89.445  -6.500-235.202  1.00 35.38           C  
ANISOU10388  CB  PHE D 172     4818   4233   4391    504   -648    358       C  
ATOM  10389  CG  PHE D 172      88.594  -7.610-234.679  1.00 35.08           C  
ANISOU10389  CG  PHE D 172     4669   4280   4380    479   -659    350       C  
ATOM  10390  CD1 PHE D 172      87.677  -7.377-233.665  1.00 41.48           C  
ANISOU10390  CD1 PHE D 172     5379   5151   5231    558   -665    370       C  
ATOM  10391  CD2 PHE D 172      88.714  -8.891-235.189  1.00 31.83           C  
ANISOU10391  CD2 PHE D 172     4260   3889   3947    371   -661    322       C  
ATOM  10392  CE1 PHE D 172      86.899  -8.413-233.164  1.00 42.42           C  
ANISOU10392  CE1 PHE D 172     5394   5359   5367    514   -672    368       C  
ATOM  10393  CE2 PHE D 172      87.926  -9.923-234.716  1.00 34.87           C  
ANISOU10393  CE2 PHE D 172     4558   4343   4348    327   -675    319       C  
ATOM  10394  CZ  PHE D 172      87.015  -9.685-233.697  1.00 44.01           C  
ANISOU10394  CZ  PHE D 172     5607   5570   5544    391   -681    346       C  
ATOM  10395  N   GLY D 173      92.146  -8.070-234.860  1.00 28.90           N  
ANISOU10395  N   GLY D 173     4078   3316   3587    361   -505    235       N  
ATOM  10396  CA  GLY D 173      92.831  -9.322-234.570  1.00 29.24           C  
ANISOU10396  CA  GLY D 173     4111   3351   3645    310   -459    180       C  
ATOM  10397  C   GLY D 173      93.859  -9.196-233.454  1.00 31.36           C  
ANISOU10397  C   GLY D 173     4375   3581   3961    338   -395    149       C  
ATOM  10398  O   GLY D 173      94.003 -10.106-232.631  1.00 27.65           O  
ANISOU10398  O   GLY D 173     3865   3112   3527    337   -370    122       O  
ATOM  10399  N   ALA D 174      94.627  -8.097-233.437  1.00 27.48           N  
ANISOU10399  N   ALA D 174     3930   3053   3460    355   -371    154       N  
ATOM  10400  CA  ALA D 174      95.609  -7.926-232.358  1.00 31.83           C  
ANISOU10400  CA  ALA D 174     4471   3577   4047    372   -316    125       C  
ATOM  10401  C   ALA D 174      94.917  -7.807-231.000  1.00 30.24           C  
ANISOU10401  C   ALA D 174     4208   3381   3900    436   -320    137       C  
ATOM  10402  O   ALA D 174      95.363  -8.399-229.999  1.00 26.92           O  
ANISOU10402  O   ALA D 174     3751   2961   3516    442   -286    110       O  
ATOM  10403  CB  ALA D 174      96.480  -6.690-232.618  1.00 26.92           C  
ANISOU10403  CB  ALA D 174     3916   2918   3394    358   -297    134       C  
ATOM  10404  N   LYS D 175      93.829  -7.031-230.944  1.00 30.59           N  
ANISOU10404  N   LYS D 175     4241   3434   3946    490   -362    178       N  
ATOM  10405  CA  LYS D 175      93.055  -6.913-229.708  1.00 33.07           C  
ANISOU10405  CA  LYS D 175     4491   3772   4303    557   -362    187       C  
ATOM  10406  C   LYS D 175      92.462  -8.254-229.291  1.00 34.37           C  
ANISOU10406  C   LYS D 175     4576   3994   4490    530   -364    180       C  
ATOM  10407  O   LYS D 175      92.427  -8.576-228.097  1.00 27.82           O  
ANISOU10407  O   LYS D 175     3700   3176   3693    550   -337    169       O  
ATOM  10408  CB  LYS D 175      91.948  -5.872-229.875  1.00 26.96           C  
ANISOU10408  CB  LYS D 175     3714   3011   3519    636   -407    231       C  
ATOM  10409  CG  LYS D 175      92.456  -4.432-229.961  1.00 30.22           C  
ANISOU10409  CG  LYS D 175     4225   3345   3913    676   -406    240       C  
ATOM  10410  CD  LYS D 175      91.305  -3.473-230.242  1.00 33.80           C  
ANISOU10410  CD  LYS D 175     4687   3803   4352    773   -460    285       C  
ATOM  10411  CE  LYS D 175      91.825  -2.085-230.562  1.00 38.70           C  
ANISOU10411  CE  LYS D 175     5439   4322   4942    798   -470    301       C  
ATOM  10412  NZ  LYS D 175      90.723  -1.165-230.960  1.00 49.13           N  
ANISOU10412  NZ  LYS D 175     6785   5637   6244    908   -531    349       N  
ATOM  10413  N   GLN D 176      91.978  -9.047-230.257  1.00 27.07           N  
ANISOU10413  N   GLN D 176     3644   3101   3539    476   -399    188       N  
ATOM  10414  CA  GLN D 176      91.439 -10.365-229.929  1.00 26.80           C  
ANISOU10414  CA  GLN D 176     3556   3109   3517    427   -406    183       C  
ATOM  10415  C   GLN D 176      92.503 -11.302-229.386  1.00 27.86           C  
ANISOU10415  C   GLN D 176     3718   3198   3671    395   -361    140       C  
ATOM  10416  O   GLN D 176      92.220 -12.112-228.482  1.00 28.19           O  
ANISOU10416  O   GLN D 176     3721   3254   3737    381   -353    140       O  
ATOM  10417  CB  GLN D 176      90.782 -11.007-231.153  1.00 32.92           C  
ANISOU10417  CB  GLN D 176     4337   3918   4250    361   -457    195       C  
ATOM  10418  CG  GLN D 176      89.476 -10.419-231.495  1.00 49.96           C  
ANISOU10418  CG  GLN D 176     6437   6154   6393    391   -514    244       C  
ATOM  10419  CD  GLN D 176      88.406 -10.769-230.503  1.00 43.00           C  
ANISOU10419  CD  GLN D 176     5447   5353   5536    403   -522    267       C  
ATOM  10420  OE1 GLN D 176      88.010  -9.940-229.700  1.00 41.87           O  
ANISOU10420  OE1 GLN D 176     5252   5239   5416    490   -509    283       O  
ATOM  10421  NE2 GLN D 176      87.896 -11.987-230.583  1.00 51.69           N  
ANISOU10421  NE2 GLN D 176     6519   6496   6626    310   -543    267       N  
ATOM  10422  N   ALA D 177      93.728 -11.214-229.914  1.00 28.15           N  
ANISOU10422  N   ALA D 177     3819   3185   3693    383   -332    108       N  
ATOM  10423  CA  ALA D 177      94.789 -12.092-229.425  1.00 28.09           C  
ANISOU10423  CA  ALA D 177     3828   3143   3701    372   -291     67       C  
ATOM  10424  C   ALA D 177      95.114 -11.783-227.966  1.00 27.59           C  
ANISOU10424  C   ALA D 177     3728   3076   3678    417   -261     67       C  
ATOM  10425  O   ALA D 177      95.356 -12.696-227.167  1.00 28.34           O  
ANISOU10425  O   ALA D 177     3812   3162   3795    414   -248     55       O  
ATOM  10426  CB  ALA D 177      96.036 -11.934-230.284  1.00 25.33           C  
ANISOU10426  CB  ALA D 177     3534   2768   3321    359   -261     32       C  
ATOM  10427  N   TRP D 178      95.166 -10.498-227.626  1.00 25.22           N  
ANISOU10427  N   TRP D 178     3424   2775   3382    458   -253     81       N  
ATOM  10428  CA  TRP D 178      95.324 -10.105-226.215  1.00 19.74           C  
ANISOU10428  CA  TRP D 178     2701   2082   2718    499   -229     80       C  
ATOM  10429  C   TRP D 178      94.152 -10.618-225.385  1.00 26.05           C  
ANISOU10429  C   TRP D 178     3438   2924   3535    511   -243    104       C  
ATOM  10430  O   TRP D 178      94.333 -11.253-224.334  1.00 27.29           O  
ANISOU10430  O   TRP D 178     3573   3085   3711    509   -225     98       O  
ATOM  10431  CB  TRP D 178      95.439  -8.578-226.150  1.00 21.43           C  
ANISOU10431  CB  TRP D 178     2945   2276   2923    537   -226     89       C  
ATOM  10432  CG  TRP D 178      95.670  -8.019-224.774  1.00 23.85           C  
ANISOU10432  CG  TRP D 178     3239   2574   3247    576   -202     81       C  
ATOM  10433  CD1 TRP D 178      95.971  -8.731-223.643  1.00 27.97           C  
ANISOU10433  CD1 TRP D 178     3725   3112   3790    576   -180     67       C  
ATOM  10434  CD2 TRP D 178      95.678  -6.641-224.407  1.00 24.92           C  
ANISOU10434  CD2 TRP D 178     3416   2679   3375    616   -199     83       C  
ATOM  10435  NE1 TRP D 178      96.136  -7.866-222.574  1.00 28.60           N  
ANISOU10435  NE1 TRP D 178     3812   3182   3872    611   -163     60       N  
ATOM  10436  CE2 TRP D 178      95.947  -6.581-223.013  1.00 24.72           C  
ANISOU10436  CE2 TRP D 178     3371   2657   3363    638   -173     66       C  
ATOM  10437  CE3 TRP D 178      95.441  -5.445-225.106  1.00 27.03           C  
ANISOU10437  CE3 TRP D 178     3746   2907   3617    639   -220    100       C  
ATOM  10438  CZ2 TRP D 178      96.011  -5.375-222.319  1.00 25.59           C  
ANISOU10438  CZ2 TRP D 178     3527   2733   3463    677   -165     57       C  
ATOM  10439  CZ3 TRP D 178      95.505  -4.245-224.416  1.00 30.08           C  
ANISOU10439  CZ3 TRP D 178     4185   3247   3996    683   -213     94       C  
ATOM  10440  CH2 TRP D 178      95.790  -4.222-223.026  1.00 30.39           C  
ANISOU10440  CH2 TRP D 178     4207   3291   4049    700   -185     69       C  
ATOM  10441  N   ARG D 179      92.936 -10.364-225.857  1.00 25.76           N  
ANISOU10441  N   ARG D 179     3369   2929   3487    519   -277    135       N  
ATOM  10442  CA  ARG D 179      91.737 -10.820-225.163  1.00 31.40           C  
ANISOU10442  CA  ARG D 179     4009   3712   4211    520   -290    161       C  
ATOM  10443  C   ARG D 179      91.760 -12.325-224.907  1.00 32.53           C  
ANISOU10443  C   ARG D 179     4148   3856   4357    446   -291    157       C  
ATOM  10444  O   ARG D 179      91.279 -12.797-223.864  1.00 30.67           O  
ANISOU10444  O   ARG D 179     3866   3658   4131    436   -280    172       O  
ATOM  10445  CB  ARG D 179      90.518 -10.428-225.983  1.00 26.77           C  
ANISOU10445  CB  ARG D 179     3381   3186   3604    531   -334    194       C  
ATOM  10446  CG  ARG D 179      89.176 -10.716-225.371  1.00 32.23           C  
ANISOU10446  CG  ARG D 179     3971   3979   4295    534   -348    225       C  
ATOM  10447  CD  ARG D 179      88.106 -10.548-226.467  1.00 32.11           C  
ANISOU10447  CD  ARG D 179     3914   4033   4254    528   -404    258       C  
ATOM  10448  NE  ARG D 179      86.769 -10.421-225.890  1.00 33.98           N  
ANISOU10448  NE  ARG D 179     4031   4393   4486    561   -415    291       N  
ATOM  10449  CZ  ARG D 179      85.662 -10.206-226.596  1.00 36.21           C  
ANISOU10449  CZ  ARG D 179     4243   4772   4745    573   -466    325       C  
ATOM  10450  NH1 ARG D 179      85.710 -10.096-227.929  1.00 35.21           N  
ANISOU10450  NH1 ARG D 179     4164   4621   4594    548   -515    335       N  
ATOM  10451  NH2 ARG D 179      84.501 -10.099-225.968  1.00 33.54           N  
ANISOU10451  NH2 ARG D 179     3778   4564   4401    609   -467    352       N  
ATOM  10452  N   ASN D 180      92.303 -13.096-225.846  1.00 27.48           N  
ANISOU10452  N   ASN D 180     3566   3171   3704    395   -303    138       N  
ATOM  10453  CA  ASN D 180      92.340 -14.551-225.745  1.00 27.62           C  
ANISOU10453  CA  ASN D 180     3610   3166   3719    328   -311    132       C  
ATOM  10454  C   ASN D 180      93.530 -15.088-224.946  1.00 26.64           C  
ANISOU10454  C   ASN D 180     3526   2981   3614    349   -277    105       C  
ATOM  10455  O   ASN D 180      93.609 -16.299-224.760  1.00 30.25           O  
ANISOU10455  O   ASN D 180     4021   3403   4068    307   -286    101       O  
ATOM  10456  CB  ASN D 180      92.343 -15.165-227.165  1.00 24.71           C  
ANISOU10456  CB  ASN D 180     3300   2771   3319    272   -341    116       C  
ATOM  10457  CG  ASN D 180      91.015 -14.993-227.868  1.00 27.69           C  
ANISOU10457  CG  ASN D 180     3632   3220   3670    231   -390    150       C  
ATOM  10458  OD1 ASN D 180      90.004 -14.765-227.212  1.00 29.44           O  
ANISOU10458  OD1 ASN D 180     3771   3517   3899    233   -401    186       O  
ATOM  10459  ND2 ASN D 180      90.999 -15.116-229.220  1.00 27.68           N  
ANISOU10459  ND2 ASN D 180     3678   3208   3633    192   -420    138       N  
ATOM  10460  N   ALA D 181      94.442 -14.245-224.473  1.00 28.62           N  
ANISOU10460  N   ALA D 181     3775   3220   3880    408   -244     88       N  
ATOM  10461  CA  ALA D 181      95.671 -14.729-223.843  1.00 26.02           C  
ANISOU10461  CA  ALA D 181     3475   2849   3564    431   -219     62       C  
ATOM  10462  C   ALA D 181      95.418 -15.266-222.428  1.00 26.06           C  
ANISOU10462  C   ALA D 181     3457   2862   3582    430   -215     84       C  
ATOM  10463  O   ALA D 181      95.212 -14.463-221.517  1.00 25.95           O  
ANISOU10463  O   ALA D 181     3400   2885   3574    459   -199     97       O  
ATOM  10464  CB  ALA D 181      96.697 -13.591-223.778  1.00 24.67           C  
ANISOU10464  CB  ALA D 181     3300   2678   3395    475   -190     41       C  
ATOM  10465  N   PRO D 182      95.468 -16.581-222.197  1.00 27.98           N  
ANISOU10465  N   PRO D 182     3741   3068   3823    399   -228     89       N  
ATOM  10466  CA  PRO D 182      94.997 -17.120-220.897  1.00 29.06           C  
ANISOU10466  CA  PRO D 182     3862   3218   3961    378   -230    123       C  
ATOM  10467  C   PRO D 182      95.838 -16.717-219.703  1.00 27.00           C  
ANISOU10467  C   PRO D 182     3585   2962   3711    432   -206    119       C  
ATOM  10468  O   PRO D 182      95.302 -16.674-218.591  1.00 26.60           O  
ANISOU10468  O   PRO D 182     3503   2950   3655    420   -199    148       O  
ATOM  10469  CB  PRO D 182      95.041 -18.646-221.103  1.00 28.86           C  
ANISOU10469  CB  PRO D 182     3916   3123   3925    330   -257    126       C  
ATOM  10470  CG  PRO D 182      95.071 -18.850-222.604  1.00 35.22           C  
ANISOU10470  CG  PRO D 182     4765   3898   4719    312   -272     96       C  
ATOM  10471  CD  PRO D 182      95.792 -17.653-223.163  1.00 25.51           C  
ANISOU10471  CD  PRO D 182     3502   2693   3498    373   -246     65       C  
ATOM  10472  N   ARG D 183      97.125 -16.431-219.885  1.00 26.37           N  
ANISOU10472  N   ARG D 183     3521   2858   3640    483   -192     85       N  
ATOM  10473  CA  ARG D 183      98.001 -16.119-218.764  1.00 28.82           C  
ANISOU10473  CA  ARG D 183     3815   3181   3954    524   -177     81       C  
ATOM  10474  C   ARG D 183      98.107 -14.626-218.455  1.00 30.05           C  
ANISOU10474  C   ARG D 183     3928   3380   4108    546   -155     70       C  
ATOM  10475  O   ARG D 183      98.893 -14.251-217.575  1.00 31.88           O  
ANISOU10475  O   ARG D 183     4150   3628   4337    570   -145     63       O  
ATOM  10476  CB  ARG D 183      99.392 -16.698-219.024  1.00 27.25           C  
ANISOU10476  CB  ARG D 183     3647   2948   3760    567   -178     52       C  
ATOM  10477  CG  ARG D 183      99.379 -18.216-219.030  1.00 28.93           C  
ANISOU10477  CG  ARG D 183     3925   3097   3971    565   -203     63       C  
ATOM  10478  CD  ARG D 183     100.688 -18.820-219.561  1.00 30.51           C  
ANISOU10478  CD  ARG D 183     4156   3263   4173    630   -202     25       C  
ATOM  10479  NE  ARG D 183     100.743 -20.248-219.288  1.00 34.70           N  
ANISOU10479  NE  ARG D 183     4767   3719   4700    647   -231     37       N  
ATOM  10480  CZ  ARG D 183     101.758 -21.050-219.590  1.00 35.76           C  
ANISOU10480  CZ  ARG D 183     4945   3810   4833    723   -237      8       C  
ATOM  10481  NH1 ARG D 183     102.835 -20.568-220.203  1.00 32.49           N  
ANISOU10481  NH1 ARG D 183     4483   3441   4419    782   -210    -37       N  
ATOM  10482  NH2 ARG D 183     101.697 -22.341-219.260  1.00 34.97           N  
ANISOU10482  NH2 ARG D 183     4939   3622   4726    739   -269     26       N  
ATOM  10483  N   CYS D 184      97.316 -13.770-219.107  1.00 25.55           N  
ANISOU10483  N   CYS D 184     3342   2829   3535    538   -151     71       N  
ATOM  10484  CA  CYS D 184      97.409 -12.322-218.908  1.00 23.49           C  
ANISOU10484  CA  CYS D 184     3069   2588   3270    563   -135     59       C  
ATOM  10485  C   CYS D 184      96.339 -11.863-217.935  1.00 26.41           C  
ANISOU10485  C   CYS D 184     3406   2998   3631    578   -126     79       C  
ATOM  10486  O   CYS D 184      95.147 -11.942-218.236  1.00 27.55           O  
ANISOU10486  O   CYS D 184     3522   3173   3773    571   -134    100       O  
ATOM  10487  CB  CYS D 184      97.262 -11.559-220.240  1.00 26.64           C  
ANISOU10487  CB  CYS D 184     3483   2974   3664    561   -139     49       C  
ATOM  10488  SG  CYS D 184      97.423  -9.747-220.039  1.00 25.29           S  
ANISOU10488  SG  CYS D 184     3331   2799   3480    590   -125     36       S  
ATOM  10489  N   VAL D 185      96.770 -11.342-216.776  1.00 27.02           N  
ANISOU10489  N   VAL D 185     3482   3087   3697    598   -109     69       N  
ATOM  10490  CA  VAL D 185      95.830 -10.776-215.812  1.00 26.95           C  
ANISOU10490  CA  VAL D 185     3446   3122   3670    623    -92     78       C  
ATOM  10491  C   VAL D 185      95.408  -9.354-216.168  1.00 28.54           C  
ANISOU10491  C   VAL D 185     3661   3318   3866    669    -83     60       C  
ATOM  10492  O   VAL D 185      94.485  -8.812-215.544  1.00 28.98           O  
ANISOU10492  O   VAL D 185     3693   3414   3906    711    -67     62       O  
ATOM  10493  CB  VAL D 185      96.489 -10.833-214.418  1.00 29.82           C  
ANISOU10493  CB  VAL D 185     3818   3497   4015    623    -79     71       C  
ATOM  10494  CG1 VAL D 185      97.621  -9.831-214.370  1.00 26.70           C  
ANISOU10494  CG1 VAL D 185     3460   3071   3612    634    -76     36       C  
ATOM  10495  CG2 VAL D 185      95.465 -10.569-213.312  1.00 29.57           C  
ANISOU10495  CG2 VAL D 185     3756   3524   3956    643    -55     81       C  
ATOM  10496  N   GLY D 186      96.033  -8.735-217.174  1.00 28.22           N  
ANISOU10496  N   GLY D 186     3662   3230   3831    667    -94     44       N  
ATOM  10497  CA  GLY D 186      95.752  -7.362-217.538  1.00 30.97           C  
ANISOU10497  CA  GLY D 186     4048   3550   4168    709    -93     32       C  
ATOM  10498  C   GLY D 186      94.658  -7.140-218.570  1.00 26.26           C  
ANISOU10498  C   GLY D 186     3436   2964   3577    738   -111     53       C  
ATOM  10499  O   GLY D 186      94.461  -6.000-219.009  1.00 28.37           O  
ANISOU10499  O   GLY D 186     3750   3196   3834    781   -119     48       O  
ATOM  10500  N   ARG D 187      93.866  -8.166-218.878  1.00 31.05           N  
ANISOU10500  N   ARG D 187     3983   3622   4194    718   -123     80       N  
ATOM  10501  CA  ARG D 187      92.989  -8.104-220.048  1.00 30.29           C  
ANISOU10501  CA  ARG D 187     3867   3543   4098    726   -152    102       C  
ATOM  10502  C   ARG D 187      91.763  -7.220-219.865  1.00 29.35           C  
ANISOU10502  C   ARG D 187     3712   3470   3968    809   -154    114       C  
ATOM  10503  O   ARG D 187      91.025  -7.037-220.843  1.00 32.37           O  
ANISOU10503  O   ARG D 187     4077   3874   4348    828   -184    136       O  
ATOM  10504  CB  ARG D 187      92.551  -9.510-220.446  1.00 26.89           C  
ANISOU10504  CB  ARG D 187     3390   3151   3674    661   -169    125       C  
ATOM  10505  CG  ARG D 187      93.631 -10.302-221.175  1.00 24.47           C  
ANISOU10505  CG  ARG D 187     3132   2790   3375    602   -178    112       C  
ATOM  10506  CD  ARG D 187      93.127 -11.717-221.457  1.00 22.15           C  
ANISOU10506  CD  ARG D 187     2815   2518   3082    539   -197    130       C  
ATOM  10507  NE  ARG D 187      93.251 -12.596-220.282  1.00 26.22           N  
ANISOU10507  NE  ARG D 187     3319   3043   3602    515   -183    137       N  
ATOM  10508  CZ  ARG D 187      92.708 -13.811-220.214  1.00 26.74           C  
ANISOU10508  CZ  ARG D 187     3374   3124   3661    453   -199    160       C  
ATOM  10509  NH1 ARG D 187      91.984 -14.283-221.237  1.00 30.17           N  
ANISOU10509  NH1 ARG D 187     3804   3573   4087    404   -230    174       N  
ATOM  10510  NH2 ARG D 187      92.891 -14.574-219.139  1.00 26.43           N  
ANISOU10510  NH2 ARG D 187     3340   3081   3620    430   -189    172       N  
ATOM  10511  N   ILE D 188      91.528  -6.635-218.674  1.00 29.51           N  
ANISOU10511  N   ILE D 188     3725   3510   3978    868   -123     97       N  
ATOM  10512  CA  ILE D 188      90.483  -5.608-218.608  1.00 32.04           C  
ANISOU10512  CA  ILE D 188     4027   3862   4284    975   -123     99       C  
ATOM  10513  C   ILE D 188      90.748  -4.509-219.635  1.00 30.43           C  
ANISOU10513  C   ILE D 188     3912   3572   4076   1016   -153     97       C  
ATOM  10514  O   ILE D 188      89.817  -3.853-220.111  1.00 33.16           O  
ANISOU10514  O   ILE D 188     4244   3941   4414   1101   -174    113       O  
ATOM  10515  CB  ILE D 188      90.360  -5.011-217.182  1.00 32.37           C  
ANISOU10515  CB  ILE D 188     4073   3920   4305   1041    -80     68       C  
ATOM  10516  CG1 ILE D 188      89.068  -4.211-217.043  1.00 34.35           C  
ANISOU10516  CG1 ILE D 188     4277   4235   4539   1167    -74     69       C  
ATOM  10517  CG2 ILE D 188      91.540  -4.090-216.891  1.00 32.52           C  
ANISOU10517  CG2 ILE D 188     4216   3827   4315   1042    -73     30       C  
ATOM  10518  CD1 ILE D 188      87.817  -5.035-216.985  1.00 37.36           C  
ANISOU10518  CD1 ILE D 188     4514   4764   4917   1164    -71    103       C  
ATOM  10519  N   GLN D 189      92.010  -4.308-220.013  1.00 29.14           N  
ANISOU10519  N   GLN D 189     3839   3318   3914    956   -156     82       N  
ATOM  10520  CA  GLN D 189      92.409  -3.231-220.914  1.00 33.20           C  
ANISOU10520  CA  GLN D 189     4457   3744   4415    972   -181     83       C  
ATOM  10521  C   GLN D 189      92.312  -3.602-222.402  1.00 29.21           C  
ANISOU10521  C   GLN D 189     3948   3240   3910    928   -220    115       C  
ATOM  10522  O   GLN D 189      92.656  -2.762-223.238  1.00 32.28           O  
ANISOU10522  O   GLN D 189     4427   3558   4281    929   -242    123       O  
ATOM  10523  CB  GLN D 189      93.860  -2.820-220.597  1.00 32.83           C  
ANISOU10523  CB  GLN D 189     4501   3615   4357    907   -164     52       C  
ATOM  10524  CG  GLN D 189      94.042  -2.126-219.251  1.00 38.64           C  
ANISOU10524  CG  GLN D 189     5278   4325   5078    948   -136     17       C  
ATOM  10525  CD  GLN D 189      93.544  -0.688-219.275  1.00 48.30           C  
ANISOU10525  CD  GLN D 189     6599   5475   6276   1044   -147      8       C  
ATOM  10526  OE1 GLN D 189      93.591  -0.009-220.313  1.00 42.78           O  
ANISOU10526  OE1 GLN D 189     5979   4709   5566   1049   -180     28       O  
ATOM  10527  NE2 GLN D 189      93.073  -0.211-218.131  1.00 40.10           N  
ANISOU10527  NE2 GLN D 189     5569   4443   5223   1125   -122    -22       N  
ATOM  10528  N   TRP D 190      91.854  -4.824-222.737  1.00 28.94           N  
ANISOU10528  N   TRP D 190     3825   3283   3890    882   -229    133       N  
ATOM  10529  CA  TRP D 190      92.140  -5.396-224.061  1.00 28.46           C  
ANISOU10529  CA  TRP D 190     3776   3213   3823    810   -257    149       C  
ATOM  10530  C   TRP D 190      91.615  -4.526-225.188  1.00 29.81           C  
ANISOU10530  C   TRP D 190     3992   3363   3971    852   -300    178       C  
ATOM  10531  O   TRP D 190      92.166  -4.558-226.296  1.00 37.71           O  
ANISOU10531  O   TRP D 190     5047   4328   4953    794   -318    185       O  
ATOM  10532  CB  TRP D 190      91.572  -6.819-224.203  1.00 28.42           C  
ANISOU10532  CB  TRP D 190     3684   3286   3829    755   -266    162       C  
ATOM  10533  CG  TRP D 190      90.075  -6.898-224.270  1.00 31.69           C  
ANISOU10533  CG  TRP D 190     4010   3792   4239    799   -294    195       C  
ATOM  10534  CD1 TRP D 190      89.215  -7.008-223.221  1.00 34.74           C  
ANISOU10534  CD1 TRP D 190     4311   4258   4631    843   -275    200       C  
ATOM  10535  CD2 TRP D 190      89.265  -6.881-225.452  1.00 31.84           C  
ANISOU10535  CD2 TRP D 190     4007   3852   4240    799   -345    227       C  
ATOM  10536  NE1 TRP D 190      87.920  -7.056-223.661  1.00 33.63           N  
ANISOU10536  NE1 TRP D 190     4084   4214   4478    872   -310    234       N  
ATOM  10537  CE2 TRP D 190      87.923  -6.975-225.035  1.00 32.79           C  
ANISOU10537  CE2 TRP D 190     4016   4084   4358    846   -358    252       C  
ATOM  10538  CE3 TRP D 190      89.546  -6.803-226.824  1.00 32.31           C  
ANISOU10538  CE3 TRP D 190     4126   3875   4277    760   -382    239       C  
ATOM  10539  CZ2 TRP D 190      86.867  -7.007-225.930  1.00 35.25           C  
ANISOU10539  CZ2 TRP D 190     4267   4476   4650    855   -412    290       C  
ATOM  10540  CZ3 TRP D 190      88.488  -6.814-227.721  1.00 35.60           C  
ANISOU10540  CZ3 TRP D 190     4496   4358   4671    769   -437    276       C  
ATOM  10541  CH2 TRP D 190      87.162  -6.909-227.271  1.00 36.50           C  
ANISOU10541  CH2 TRP D 190     4492   4588   4787    818   -455    302       C  
ATOM  10542  N   GLY D 191      90.564  -3.746-224.933  1.00 31.77           N  
ANISOU10542  N   GLY D 191     4219   3636   4215    959   -318    195       N  
ATOM  10543  CA  GLY D 191      90.022  -2.896-225.981  1.00 37.48           C  
ANISOU10543  CA  GLY D 191     4990   4336   4914   1015   -368    229       C  
ATOM  10544  C   GLY D 191      90.780  -1.608-226.217  1.00 43.77           C  
ANISOU10544  C   GLY D 191     5933   5008   5688   1036   -372    224       C  
ATOM  10545  O   GLY D 191      90.502  -0.900-227.194  1.00 36.27           O  
ANISOU10545  O   GLY D 191     5050   4020   4711   1069   -418    258       O  
ATOM  10546  N   LYS D 192      91.727  -1.283-225.342  1.00 34.32           N  
ANISOU10546  N   LYS D 192     4796   3749   4496   1011   -330    187       N  
ATOM  10547  CA  LYS D 192      92.540  -0.074-225.453  1.00 37.63           C  
ANISOU10547  CA  LYS D 192     5364   4045   4887   1004   -332    180       C  
ATOM  10548  C   LYS D 192      93.949  -0.521-225.836  1.00 40.15           C  
ANISOU10548  C   LYS D 192     5716   4343   5198    861   -309    165       C  
ATOM  10549  O   LYS D 192      94.789  -0.837-224.987  1.00 38.39           O  
ANISOU10549  O   LYS D 192     5478   4123   4987    809   -269    129       O  
ATOM  10550  CB  LYS D 192      92.519   0.739-224.154  1.00 39.30           C  
ANISOU10550  CB  LYS D 192     5624   4208   5099   1080   -306    145       C  
ATOM  10551  CG  LYS D 192      91.476   1.856-224.143  1.00 64.22           C  
ANISOU10551  CG  LYS D 192     8838   7322   8241   1234   -337    160       C  
ATOM  10552  CD  LYS D 192      90.536   1.781-222.932  1.00 77.66           C  
ANISOU10552  CD  LYS D 192    10450   9097   9959   1354   -308    133       C  
ATOM  10553  CE  LYS D 192      89.398   0.788-223.161  1.00 83.26           C  
ANISOU10553  CE  LYS D 192    10985   9960  10690   1387   -318    161       C  
ATOM  10554  NZ  LYS D 192      88.880   0.222-221.877  1.00 79.28           N  
ANISOU10554  NZ  LYS D 192    10364   9559  10201   1424   -270    133       N  
ATOM  10555  N   LEU D 193      94.200  -0.555-227.135  1.00 37.16           N  
ANISOU10555  N   LEU D 193     5375   3953   4792    801   -335    192       N  
ATOM  10556  CA  LEU D 193      95.448  -1.077-227.667  1.00 30.84           C  
ANISOU10556  CA  LEU D 193     4584   3157   3976    674   -309    178       C  
ATOM  10557  C   LEU D 193      95.752  -0.267-228.912  1.00 34.42           C  
ANISOU10557  C   LEU D 193     5151   3551   4377    628   -339    212       C  
ATOM  10558  O   LEU D 193      94.937  -0.248-229.834  1.00 34.74           O  
ANISOU10558  O   LEU D 193     5195   3604   4400    662   -382    250       O  
ATOM  10559  CB  LEU D 193      95.337  -2.571-228.007  1.00 29.29           C  
ANISOU10559  CB  LEU D 193     4276   3052   3800    636   -300    170       C  
ATOM  10560  CG  LEU D 193      96.605  -3.223-228.565  1.00 28.38           C  
ANISOU10560  CG  LEU D 193     4162   2954   3668    529   -268    147       C  
ATOM  10561  CD1 LEU D 193      97.733  -3.121-227.565  1.00 28.29           C  
ANISOU10561  CD1 LEU D 193     4150   2932   3666    493   -225    112       C  
ATOM  10562  CD2 LEU D 193      96.371  -4.679-228.959  1.00 24.71           C  
ANISOU10562  CD2 LEU D 193     3613   2557   3218    508   -266    137       C  
ATOM  10563  N   GLN D 194      96.887   0.421-228.918  1.00 32.82           N  
ANISOU10563  N   GLN D 194     5040   3290   4142    545   -319    203       N  
ATOM  10564  CA  GLN D 194      97.340   1.150-230.101  1.00 33.87           C  
ANISOU10564  CA  GLN D 194     5285   3370   4212    470   -340    238       C  
ATOM  10565  C   GLN D 194      98.055   0.178-231.033  1.00 32.71           C  
ANISOU10565  C   GLN D 194     5080   3304   4044    370   -314    229       C  
ATOM  10566  O   GLN D 194      99.039  -0.449-230.637  1.00 30.26           O  
ANISOU10566  O   GLN D 194     4708   3046   3745    306   -265    190       O  
ATOM  10567  CB  GLN D 194      98.280   2.280-229.681  1.00 33.35           C  
ANISOU10567  CB  GLN D 194     5344   3216   4112    402   -328    232       C  
ATOM  10568  CG  GLN D 194      98.797   3.076-230.854  1.00 47.13           C  
ANISOU10568  CG  GLN D 194     7218   4905   5784    305   -348    274       C  
ATOM  10569  CD  GLN D 194      97.688   3.832-231.550  1.00 48.31           C  
ANISOU10569  CD  GLN D 194     7467   4978   5911    396   -414    329       C  
ATOM  10570  OE1 GLN D 194      96.696   4.211-230.927  1.00 53.49           O  
ANISOU10570  OE1 GLN D 194     8133   5591   6599    534   -443    332       O  
ATOM  10571  NE2 GLN D 194      97.842   4.046-232.844  1.00 53.09           N  
ANISOU10571  NE2 GLN D 194     8141   5575   6455    326   -438    374       N  
ATOM  10572  N   VAL D 195      97.575   0.046-232.271  1.00 30.55           N  
ANISOU10572  N   VAL D 195     4826   3045   3736    363   -347    264       N  
ATOM  10573  CA  VAL D 195      98.121  -0.923-233.215  1.00 31.97           C  
ANISOU10573  CA  VAL D 195     4956   3302   3888    281   -323    250       C  
ATOM  10574  C   VAL D 195      98.877  -0.142-234.279  1.00 36.77           C  
ANISOU10574  C   VAL D 195     5675   3880   4415    177   -322    279       C  
ATOM  10575  O   VAL D 195      98.274   0.628-235.039  1.00 34.51           O  
ANISOU10575  O   VAL D 195     5486   3540   4087    192   -374    333       O  
ATOM  10576  CB  VAL D 195      97.018  -1.798-233.829  1.00 31.09           C  
ANISOU10576  CB  VAL D 195     4781   3244   3788    333   -359    262       C  
ATOM  10577  CG1 VAL D 195      97.605  -2.799-234.824  1.00 29.57           C  
ANISOU10577  CG1 VAL D 195     4558   3118   3557    251   -332    238       C  
ATOM  10578  CG2 VAL D 195      96.276  -2.542-232.714  1.00 34.76           C  
ANISOU10578  CG2 VAL D 195     5138   3744   4326    417   -357    239       C  
ATOM  10579  N   PHE D 196     100.197  -0.317-234.319  1.00 30.70           N  
ANISOU10579  N   PHE D 196     4891   3153   3619     73   -265    248       N  
ATOM  10580  CA  PHE D 196     101.032   0.263-235.359  1.00 32.80           C  
ANISOU10580  CA  PHE D 196     5242   3422   3798    -49   -251    272       C  
ATOM  10581  C   PHE D 196     101.197  -0.748-236.496  1.00 32.72           C  
ANISOU10581  C   PHE D 196     5178   3504   3749    -87   -228    256       C  
ATOM  10582  O   PHE D 196     101.655  -1.868-236.280  1.00 31.85           O  
ANISOU10582  O   PHE D 196     4961   3474   3667    -81   -182    201       O  
ATOM  10583  CB  PHE D 196     102.384   0.660-234.782  1.00 31.24           C  
ANISOU10583  CB  PHE D 196     5044   3242   3583   -150   -198    247       C  
ATOM  10584  CG  PHE D 196     102.296   1.777-233.756  1.00 27.72           C  
ANISOU10584  CG  PHE D 196     4683   2692   3157   -135   -223    261       C  
ATOM  10585  CD1 PHE D 196     101.915   3.048-234.140  1.00 31.35           C  
ANISOU10585  CD1 PHE D 196     5307   3036   3570   -151   -272    317       C  
ATOM  10586  CD2 PHE D 196     102.580   1.537-232.409  1.00 29.23           C  
ANISOU10586  CD2 PHE D 196     4802   2896   3408   -100   -200    218       C  
ATOM  10587  CE1 PHE D 196     101.832   4.079-233.221  1.00 42.73           C  
ANISOU10587  CE1 PHE D 196     6846   4366   5021   -132   -296    324       C  
ATOM  10588  CE2 PHE D 196     102.501   2.560-231.481  1.00 35.00           C  
ANISOU10588  CE2 PHE D 196     5623   3530   4147    -89   -221    223       C  
ATOM  10589  CZ  PHE D 196     102.118   3.829-231.878  1.00 37.95           C  
ANISOU10589  CZ  PHE D 196     6166   3779   4473   -101   -268    273       C  
ATOM  10590  N   ASP D 197     100.836  -0.348-237.700  1.00 31.48           N  
ANISOU10590  N   ASP D 197     5108   3330   3522   -123   -263    302       N  
ATOM  10591  CA  ASP D 197     100.884  -1.244-238.856  1.00 27.32           C  
ANISOU10591  CA  ASP D 197     4550   2884   2945   -159   -248    287       C  
ATOM  10592  C   ASP D 197     102.261  -1.071-239.493  1.00 31.60           C  
ANISOU10592  C   ASP D 197     5111   3490   3405   -293   -182    273       C  
ATOM  10593  O   ASP D 197     102.526  -0.074-240.171  1.00 35.41           O  
ANISOU10593  O   ASP D 197     5706   3940   3809   -382   -195    325       O  
ATOM  10594  CB  ASP D 197      99.756  -0.895-239.825  1.00 31.35           C  
ANISOU10594  CB  ASP D 197     5141   3357   3413   -130   -325    347       C  
ATOM  10595  CG  ASP D 197      99.671  -1.848-241.004  1.00 36.76           C  
ANISOU10595  CG  ASP D 197     5803   4122   4041   -166   -319    328       C  
ATOM  10596  OD1 ASP D 197     100.530  -2.741-241.142  1.00 34.89           O  
ANISOU10596  OD1 ASP D 197     5500   3964   3793   -209   -249    266       O  
ATOM  10597  OD2 ASP D 197      98.723  -1.694-241.791  1.00 34.65           O  
ANISOU10597  OD2 ASP D 197     5588   3840   3738   -145   -387    375       O  
ATOM  10598  N   ALA D 198     103.137  -2.048-239.302  1.00 27.63           N  
ANISOU10598  N   ALA D 198     4501   3084   2915   -307   -112    205       N  
ATOM  10599  CA  ALA D 198     104.464  -2.014-239.904  1.00 31.17           C  
ANISOU10599  CA  ALA D 198     4935   3626   3283   -423    -39    183       C  
ATOM  10600  C   ALA D 198     104.614  -3.091-240.983  1.00 33.29           C  
ANISOU10600  C   ALA D 198     5165   3987   3498   -427     -2    140       C  
ATOM  10601  O   ALA D 198     105.723  -3.553-241.270  1.00 32.64           O  
ANISOU10601  O   ALA D 198     5017   4013   3371   -476     75     91       O  
ATOM  10602  CB  ALA D 198     105.549  -2.146-238.827  1.00 32.51           C  
ANISOU10602  CB  ALA D 198     5007   3851   3495   -437     18    138       C  
ATOM  10603  N   ARG D 199     103.502  -3.481-241.616  1.00 30.83           N  
ANISOU10603  N   ARG D 199     4894   3639   3181   -376    -58    156       N  
ATOM  10604  CA  ARG D 199     103.558  -4.547-242.621  1.00 33.04           C  
ANISOU10604  CA  ARG D 199     5154   3993   3407   -379    -29    108       C  
ATOM  10605  C   ARG D 199     104.280  -4.138-243.898  1.00 40.05           C  
ANISOU10605  C   ARG D 199     6103   4952   4164   -499     12    121       C  
ATOM  10606  O   ARG D 199     104.565  -5.012-244.725  1.00 37.68           O  
ANISOU10606  O   ARG D 199     5784   4729   3804   -507     55     68       O  
ATOM  10607  CB  ARG D 199     102.144  -5.041-242.946  1.00 31.10           C  
ANISOU10607  CB  ARG D 199     4937   3696   3183   -312   -108    125       C  
ATOM  10608  CG  ARG D 199     101.520  -5.871-241.768  1.00 28.71           C  
ANISOU10608  CG  ARG D 199     4551   3359   2999   -201   -129     92       C  
ATOM  10609  CD  ARG D 199     100.069  -6.234-242.063  1.00 33.58           C  
ANISOU10609  CD  ARG D 199     5188   3939   3632   -154   -212    119       C  
ATOM  10610  NE  ARG D 199      99.257  -5.035-242.246  1.00 35.58           N  
ANISOU10610  NE  ARG D 199     5512   4136   3870   -153   -286    204       N  
ATOM  10611  CZ  ARG D 199      98.058  -4.995-242.826  1.00 33.04           C  
ANISOU10611  CZ  ARG D 199     5223   3801   3529   -131   -367    249       C  
ATOM  10612  NH1 ARG D 199      97.499  -6.094-243.312  1.00 32.91           N  
ANISOU10612  NH1 ARG D 199     5179   3824   3500   -128   -388    216       N  
ATOM  10613  NH2 ARG D 199      97.418  -3.830-242.931  1.00 34.37           N  
ANISOU10613  NH2 ARG D 199     5457   3916   3685   -111   -433    327       N  
ATOM  10614  N   ASP D 200     104.604  -2.857-244.078  1.00 34.54           N  
ANISOU10614  N   ASP D 200     5485   4227   3411   -595      3    187       N  
ATOM  10615  CA  ASP D 200     105.384  -2.430-245.241  1.00 44.33           C  
ANISOU10615  CA  ASP D 200     6782   5546   4516   -729     50    204       C  
ATOM  10616  C   ASP D 200     106.877  -2.343-244.938  1.00 43.52           C  
ANISOU10616  C   ASP D 200     6596   5554   4385   -811    147    165       C  
ATOM  10617  O   ASP D 200     107.648  -1.865-245.776  1.00 42.48           O  
ANISOU10617  O   ASP D 200     6499   5503   4137   -942    196    183       O  
ATOM  10618  CB  ASP D 200     104.874  -1.083-245.764  1.00 64.54           C  
ANISOU10618  CB  ASP D 200     9496   8012   7012   -806    -21    308       C  
ATOM  10619  CG  ASP D 200     103.754  -1.233-246.779  1.00 95.74           C  
ANISOU10619  CG  ASP D 200    13532  11929  10916   -777    -95    345       C  
ATOM  10620  OD1 ASP D 200     103.934  -1.972-247.775  1.00103.29           O  
ANISOU10620  OD1 ASP D 200    14478  12975  11793   -809    -59    307       O  
ATOM  10621  OD2 ASP D 200     102.689  -0.613-246.575  1.00105.41           O  
ANISOU10621  OD2 ASP D 200    14831  13042  12179   -718   -190    411       O  
ATOM  10622  N   CYS D 201     107.288  -2.785-243.753  1.00 36.35           N  
ANISOU10622  N   CYS D 201     5574   4662   3573   -741    175    116       N  
ATOM  10623  CA  CYS D 201     108.689  -2.730-243.357  1.00 39.06           C  
ANISOU10623  CA  CYS D 201     5819   5127   3897   -808    260     79       C  
ATOM  10624  C   CYS D 201     109.535  -3.580-244.291  1.00 42.67           C  
ANISOU10624  C   CYS D 201     6200   5744   4266   -828    351     13       C  
ATOM  10625  O   CYS D 201     109.132  -4.675-244.689  1.00 44.26           O  
ANISOU10625  O   CYS D 201     6381   5956   4478   -731    357    -43       O  
ATOM  10626  CB  CYS D 201     108.833  -3.237-241.918  1.00 33.98           C  
ANISOU10626  CB  CYS D 201     5064   4470   3377   -702    261     36       C  
ATOM  10627  SG  CYS D 201     110.441  -2.883-241.231  1.00 41.85           S  
ANISOU10627  SG  CYS D 201     5942   5603   4354   -793    337     13       S  
ATOM  10628  N   ARG D 202     110.724  -3.086-244.636  1.00 43.91           N  
ANISOU10628  N   ARG D 202     6319   6033   4332   -959    424     15       N  
ATOM  10629  CA  ARG D 202     111.539  -3.790-245.614  1.00 54.04           C  
ANISOU10629  CA  ARG D 202     7533   7484   5514   -982    518    -47       C  
ATOM  10630  C   ARG D 202     113.003  -3.968-245.235  1.00 53.31           C  
ANISOU10630  C   ARG D 202     7278   7578   5398  -1016    616    -98       C  
ATOM  10631  O   ARG D 202     113.749  -4.557-246.019  1.00 46.02           O  
ANISOU10631  O   ARG D 202     6283   6815   4388  -1022    705   -157       O  
ATOM  10632  CB  ARG D 202     111.449  -3.090-246.976  1.00 62.31           C  
ANISOU10632  CB  ARG D 202     8705   8552   6418  -1126    522      9       C  
ATOM  10633  CG  ARG D 202     110.279  -3.594-247.815  1.00 77.26           C  
ANISOU10633  CG  ARG D 202    10702  10356   8295  -1057    466     11       C  
ATOM  10634  CD  ARG D 202     110.178  -2.877-249.145  1.00 90.95           C  
ANISOU10634  CD  ARG D 202    12566  12109   9880  -1200    461     74       C  
ATOM  10635  NE  ARG D 202     110.170  -1.430-248.969  1.00100.51           N  
ANISOU10635  NE  ARG D 202    13881  13243  11066  -1333    412    179       N  
ATOM  10636  CZ  ARG D 202     111.133  -0.619-249.396  1.00104.94           C  
ANISOU10636  CZ  ARG D 202    14458  13900  11513  -1510    468    218       C  
ATOM  10637  NH1 ARG D 202     112.183  -1.113-250.041  1.00108.20           N  
ANISOU10637  NH1 ARG D 202    14772  14514  11826  -1571    581    158       N  
ATOM  10638  NH2 ARG D 202     111.043   0.688-249.186  1.00100.54           N  
ANISOU10638  NH2 ARG D 202    14022  13242  10936  -1629    412    315       N  
ATOM  10639  N   SER D 203     113.437  -3.511-244.064  1.00 40.94           N  
ANISOU10639  N   SER D 203     5647   6006   3902  -1033    603    -82       N  
ATOM  10640  CA  SER D 203     114.842  -3.660-243.708  1.00 38.97           C  
ANISOU10640  CA  SER D 203     5228   5953   3624  -1071    689   -127       C  
ATOM  10641  C   SER D 203     114.960  -3.697-242.193  1.00 38.73           C  
ANISOU10641  C   SER D 203     5117   5880   3717  -1000    652   -134       C  
ATOM  10642  O   SER D 203     114.037  -3.301-241.477  1.00 36.41           O  
ANISOU10642  O   SER D 203     4917   5407   3509   -965    566    -91       O  
ATOM  10643  CB  SER D 203     115.692  -2.521-244.274  1.00 44.56           C  
ANISOU10643  CB  SER D 203     5953   6775   4204  -1299    732    -70       C  
ATOM  10644  OG  SER D 203     115.375  -1.297-243.629  1.00 40.37           O  
ANISOU10644  OG  SER D 203     5531   6107   3699  -1410    656     14       O  
ATOM  10645  N   ALA D 204     116.110  -4.175-241.705  1.00 37.94           N  
ANISOU10645  N   ALA D 204     4839   5956   3619   -972    718   -189       N  
ATOM  10646  CA  ALA D 204     116.307  -4.157-240.252  1.00 39.98           C  
ANISOU10646  CA  ALA D 204     5020   6188   3982   -919    681   -191       C  
ATOM  10647  C   ALA D 204     116.434  -2.732-239.738  1.00 40.62           C  
ANISOU10647  C   ALA D 204     5172   6218   4046  -1100    637   -113       C  
ATOM  10648  O   ALA D 204     116.069  -2.450-238.586  1.00 39.32           O  
ANISOU10648  O   ALA D 204     5029   5939   3970  -1066    573    -94       O  
ATOM  10649  CB  ALA D 204     117.538  -4.972-239.858  1.00 43.99           C  
ANISOU10649  CB  ALA D 204     5315   6908   4490   -845    754   -262       C  
ATOM  10650  N   GLN D 205     116.952  -1.824-240.573  1.00 43.95           N  
ANISOU10650  N   GLN D 205     5639   6716   4344  -1297    671    -68       N  
ATOM  10651  CA  GLN D 205     117.025  -0.421-240.179  1.00 46.63           C  
ANISOU10651  CA  GLN D 205     6083   6979   4653  -1484    623     10       C  
ATOM  10652  C   GLN D 205     115.630   0.178-240.020  1.00 50.45           C  
ANISOU10652  C   GLN D 205     6777   7195   5195  -1448    523     67       C  
ATOM  10653  O   GLN D 205     115.366   0.903-239.051  1.00 43.91           O  
ANISOU10653  O   GLN D 205     6018   6243   4420  -1476    461    100       O  
ATOM  10654  CB  GLN D 205     117.857   0.361-241.194  1.00 46.78           C  
ANISOU10654  CB  GLN D 205     6120   7138   4518  -1712    681     49       C  
ATOM  10655  CG  GLN D 205     117.864   1.869-240.989  1.00 51.98           C  
ANISOU10655  CG  GLN D 205     6935   7689   5126  -1928    627    138       C  
ATOM  10656  CD  GLN D 205     118.507   2.297-239.678  1.00 54.41           C  
ANISOU10656  CD  GLN D 205     7168   8027   5478  -1990    605    137       C  
ATOM  10657  OE1 GLN D 205     117.842   2.837-238.791  1.00 58.28           O  
ANISOU10657  OE1 GLN D 205     7776   8323   6044  -1964    522    164       O  
ATOM  10658  NE2 GLN D 205     119.809   2.064-239.554  1.00 52.84           N  
ANISOU10658  NE2 GLN D 205     6770   8082   5226  -2072    678    103       N  
ATOM  10659  N   GLU D 206     114.724  -0.116-240.956  1.00 43.91           N  
ANISOU10659  N   GLU D 206     6050   6282   4353  -1382    507     76       N  
ATOM  10660  CA  GLU D 206     113.338   0.323-240.813  1.00 41.27           C  
ANISOU10660  CA  GLU D 206     5889   5713   4078  -1317    411    126       C  
ATOM  10661  C   GLU D 206     112.670  -0.329-239.605  1.00 42.79           C  
ANISOU10661  C   GLU D 206     6032   5812   4415  -1132    365     89       C  
ATOM  10662  O   GLU D 206     111.867   0.312-238.912  1.00 40.21           O  
ANISOU10662  O   GLU D 206     5811   5319   4148  -1105    290    129       O  
ATOM  10663  CB  GLU D 206     112.556   0.015-242.088  1.00 42.36           C  
ANISOU10663  CB  GLU D 206     6119   5811   4165  -1281    402    139       C  
ATOM  10664  CG  GLU D 206     111.409   0.971-242.351  1.00 57.79           C  
ANISOU10664  CG  GLU D 206     8277   7564   6115  -1302    309    223       C  
ATOM  10665  CD  GLU D 206     110.627   0.613-243.609  1.00 67.75           C  
ANISOU10665  CD  GLU D 206     9619   8801   7322  -1266    292    237       C  
ATOM  10666  OE1 GLU D 206     109.458   1.044-243.728  1.00 69.34           O  
ANISOU10666  OE1 GLU D 206     9954   8842   7549  -1213    205    291       O  
ATOM  10667  OE2 GLU D 206     111.182  -0.105-244.471  1.00 66.24           O  
ANISOU10667  OE2 GLU D 206     9352   8758   7058  -1284    366    192       O  
ATOM  10668  N   MET D 207     112.985  -1.602-239.337  1.00 36.29           N  
ANISOU10668  N   MET D 207     5055   5092   3643  -1001    409     13       N  
ATOM  10669  CA  MET D 207     112.499  -2.261-238.124  1.00 38.49           C  
ANISOU10669  CA  MET D 207     5278   5299   4048   -843    372    -19       C  
ATOM  10670  C   MET D 207     112.829  -1.433-236.884  1.00 36.92           C  
ANISOU10670  C   MET D 207     5078   5064   3887   -904    340      5       C  
ATOM  10671  O   MET D 207     111.990  -1.240-235.996  1.00 35.23           O  
ANISOU10671  O   MET D 207     4924   4707   3755   -828    277     20       O  
ATOM  10672  CB  MET D 207     113.139  -3.642-237.986  1.00 50.35           C  
ANISOU10672  CB  MET D 207     6614   6940   5579   -723    431   -101       C  
ATOM  10673  CG  MET D 207     112.416  -4.822-238.595  1.00 63.01           C  
ANISOU10673  CG  MET D 207     8227   8508   7206   -582    433   -143       C  
ATOM  10674  SD  MET D 207     113.011  -6.329-237.766  1.00 64.65           S  
ANISOU10674  SD  MET D 207     8268   8805   7490   -407    470   -230       S  
ATOM  10675  CE  MET D 207     111.679  -6.658-236.630  1.00 46.48           C  
ANISOU10675  CE  MET D 207     6030   6312   5320   -284    381   -212       C  
ATOM  10676  N   PHE D 208     114.071  -0.955-236.809  1.00 36.49           N  
ANISOU10676  N   PHE D 208     4949   5150   3766  -1044    386      5       N  
ATOM  10677  CA  PHE D 208     114.533  -0.224-235.636  1.00 44.62           C  
ANISOU10677  CA  PHE D 208     5968   6167   4818  -1119    358     20       C  
ATOM  10678  C   PHE D 208     113.766   1.083-235.454  1.00 41.34           C  
ANISOU10678  C   PHE D 208     5756   5556   4396  -1202    286     87       C  
ATOM  10679  O   PHE D 208     113.431   1.464-234.330  1.00 36.98           O  
ANISOU10679  O   PHE D 208     5245   4899   3907  -1170    236     92       O  
ATOM  10680  CB  PHE D 208     116.034   0.029-235.769  1.00 44.01           C  
ANISOU10680  CB  PHE D 208     5765   6304   4653  -1277    422     11       C  
ATOM  10681  CG  PHE D 208     116.628   0.780-234.618  1.00 48.69           C  
ANISOU10681  CG  PHE D 208     6340   6907   5253  -1382    394     25       C  
ATOM  10682  CD1 PHE D 208     116.657   0.219-233.357  1.00 52.67           C  
ANISOU10682  CD1 PHE D 208     6750   7415   5849  -1261    370    -12       C  
ATOM  10683  CD2 PHE D 208     117.179   2.033-234.805  1.00 54.24           C  
ANISOU10683  CD2 PHE D 208     7128   7619   5861  -1612    389     76       C  
ATOM  10684  CE1 PHE D 208     117.218   0.898-232.293  1.00 55.37           C  
ANISOU10684  CE1 PHE D 208     7076   7773   6188  -1363    340     -2       C  
ATOM  10685  CE2 PHE D 208     117.740   2.719-233.742  1.00 55.47           C  
ANISOU10685  CE2 PHE D 208     7276   7784   6016  -1722    358     85       C  
ATOM  10686  CZ  PHE D 208     117.759   2.149-232.493  1.00 52.52           C  
ANISOU10686  CZ  PHE D 208     6802   7420   5733  -1596    334     43       C  
ATOM  10687  N   THR D 209     113.480   1.783-236.556  1.00 39.08           N  
ANISOU10687  N   THR D 209     5607   5213   4028  -1302    279    139       N  
ATOM  10688  CA  THR D 209     112.703   3.016-236.477  1.00 39.75           C  
ANISOU10688  CA  THR D 209     5905   5096   4102  -1360    206    205       C  
ATOM  10689  C   THR D 209     111.297   2.760-235.954  1.00 37.34           C  
ANISOU10689  C   THR D 209     5666   4620   3902  -1168    141    204       C  
ATOM  10690  O   THR D 209     110.806   3.494-235.084  1.00 38.52           O  
ANISOU10690  O   THR D 209     5916   4627   4091  -1150     85    223       O  
ATOM  10691  CB  THR D 209     112.637   3.666-237.861  1.00 45.91           C  
ANISOU10691  CB  THR D 209     6817   5856   4770  -1486    209    264       C  
ATOM  10692  OG1 THR D 209     113.965   3.944-238.299  1.00 45.38           O  
ANISOU10692  OG1 THR D 209     6682   5963   4597  -1682    275    268       O  
ATOM  10693  CG2 THR D 209     111.831   4.944-237.802  1.00 45.71           C  
ANISOU10693  CG2 THR D 209     7027   5610   4730  -1529    127    336       C  
ATOM  10694  N   TYR D 210     110.636   1.721-236.480  1.00 34.83           N  
ANISOU10694  N   TYR D 210     5292   4319   3622  -1027    148    179       N  
ATOM  10695  CA  TYR D 210     109.323   1.330-235.972  1.00 32.79           C  
ANISOU10695  CA  TYR D 210     5064   3934   3462   -850     92    174       C  
ATOM  10696  C   TYR D 210     109.374   1.022-234.478  1.00 33.94           C  
ANISOU10696  C   TYR D 210     5127   4070   3700   -767     84    135       C  
ATOM  10697  O   TYR D 210     108.461   1.384-233.727  1.00 30.73           O  
ANISOU10697  O   TYR D 210     4793   3532   3353   -684     29    149       O  
ATOM  10698  CB  TYR D 210     108.811   0.111-236.730  1.00 31.46           C  
ANISOU10698  CB  TYR D 210     4826   3816   3311   -739    109    144       C  
ATOM  10699  CG  TYR D 210     108.061   0.453-237.996  1.00 35.79           C  
ANISOU10699  CG  TYR D 210     5498   4303   3798   -760     78    193       C  
ATOM  10700  CD1 TYR D 210     106.865   1.157-237.935  1.00 40.57           C  
ANISOU10700  CD1 TYR D 210     6237   4750   4428   -704     -2    246       C  
ATOM  10701  CD2 TYR D 210     108.544   0.081-239.239  1.00 39.43           C  
ANISOU10701  CD2 TYR D 210     5941   4871   4172   -828    126    186       C  
ATOM  10702  CE1 TYR D 210     106.161   1.487-239.067  1.00 42.25           C  
ANISOU10702  CE1 TYR D 210     6561   4911   4582   -716    -41    297       C  
ATOM  10703  CE2 TYR D 210     107.828   0.401-240.418  1.00 39.78           C  
ANISOU10703  CE2 TYR D 210     6104   4859   4149   -851     90    235       C  
ATOM  10704  CZ  TYR D 210     106.641   1.107-240.310  1.00 42.85           C  
ANISOU10704  CZ  TYR D 210     6624   5089   4568   -795      2    294       C  
ATOM  10705  OH  TYR D 210     105.914   1.465-241.425  1.00 44.30           O  
ANISOU10705  OH  TYR D 210     6926   5220   4687   -810    -45    350       O  
ATOM  10706  N   ILE D 211     110.419   0.324-234.039  1.00 31.60           N  
ANISOU10706  N   ILE D 211     4675   3922   3411   -780    137     86       N  
ATOM  10707  CA  ILE D 211     110.512  -0.063-232.629  1.00 29.53           C  
ANISOU10707  CA  ILE D 211     4328   3662   3229   -699    127     51       C  
ATOM  10708  C   ILE D 211     110.741   1.156-231.747  1.00 39.33           C  
ANISOU10708  C   ILE D 211     5657   4828   4457   -797     93     75       C  
ATOM  10709  O   ILE D 211     110.137   1.281-230.675  1.00 37.03           O  
ANISOU10709  O   ILE D 211     5397   4443   4230   -715     54     69       O  
ATOM  10710  CB  ILE D 211     111.618  -1.120-232.435  1.00 33.03           C  
ANISOU10710  CB  ILE D 211     4583   4288   3677   -679    186     -4       C  
ATOM  10711  CG1 ILE D 211     111.156  -2.476-232.967  1.00 32.16           C  
ANISOU10711  CG1 ILE D 211     4408   4207   3606   -536    206    -40       C  
ATOM  10712  CG2 ILE D 211     111.971  -1.274-230.920  1.00 34.67           C  
ANISOU10712  CG2 ILE D 211     4713   4515   3946   -638    171    -29       C  
ATOM  10713  CD1 ILE D 211     112.273  -3.489-233.114  1.00 33.70           C  
ANISOU10713  CD1 ILE D 211     4440   4580   3785   -508    271    -94       C  
ATOM  10714  N   CYS D 212     111.636   2.053-232.163  1.00 34.67           N  
ANISOU10714  N   CYS D 212     5112   4283   3776   -980    110    101       N  
ATOM  10715  CA  CYS D 212     111.867   3.276-231.399  1.00 38.54           C  
ANISOU10715  CA  CYS D 212     5716   4687   4240  -1095     73    125       C  
ATOM  10716  C   CYS D 212     110.594   4.101-231.291  1.00 37.83           C  
ANISOU10716  C   CYS D 212     5824   4377   4173  -1030      7    162       C  
ATOM  10717  O   CYS D 212     110.286   4.638-230.218  1.00 35.70           O  
ANISOU10717  O   CYS D 212     5624   4004   3937  -1003    -31    155       O  
ATOM  10718  CB  CYS D 212     112.998   4.095-232.028  1.00 38.94           C  
ANISOU10718  CB  CYS D 212     5797   4822   4176  -1325    100    154       C  
ATOM  10719  SG  CYS D 212     114.627   3.340-231.815  1.00 45.42           S  
ANISOU10719  SG  CYS D 212     6368   5925   4966  -1408    173    107       S  
ATOM  10720  N   ASN D 213     109.828   4.194-232.380  1.00 35.05           N  
ANISOU10720  N   ASN D 213     5561   3956   3801   -994     -8    199       N  
ATOM  10721  CA  ASN D 213     108.547   4.896-232.327  1.00 36.05           C  
ANISOU10721  CA  ASN D 213     5857   3888   3952   -902    -74    235       C  
ATOM  10722  C   ASN D 213     107.586   4.212-231.363  1.00 34.94           C  
ANISOU10722  C   ASN D 213     5650   3707   3918   -705    -94    199       C  
ATOM  10723  O   ASN D 213     106.824   4.883-230.654  1.00 38.40           O  
ANISOU10723  O   ASN D 213     6197   4007   4385   -634   -140    207       O  
ATOM  10724  CB  ASN D 213     107.917   4.968-233.723  1.00 43.05           C  
ANISOU10724  CB  ASN D 213     6825   4737   4795   -891    -90    283       C  
ATOM  10725  CG  ASN D 213     108.724   5.825-234.704  1.00 63.83           C  
ANISOU10725  CG  ASN D 213     9562   7383   7307  -1095    -78    332       C  
ATOM  10726  OD1 ASN D 213     109.774   6.371-234.365  1.00 62.31           O  
ANISOU10726  OD1 ASN D 213     9377   7234   7063  -1256    -56    330       O  
ATOM  10727  ND2 ASN D 213     108.233   5.923-235.937  1.00 69.41           N  
ANISOU10727  ND2 ASN D 213    10348   8061   7964  -1097    -93    378       N  
ATOM  10728  N   HIS D 214     107.588   2.872-231.341  1.00 32.26           N  
ANISOU10728  N   HIS D 214     5140   3485   3631   -614    -59    160       N  
ATOM  10729  CA  HIS D 214     106.742   2.132-230.408  1.00 28.04           C  
ANISOU10729  CA  HIS D 214     4536   2928   3192   -448    -74    129       C  
ATOM  10730  C   HIS D 214     107.111   2.477-228.969  1.00 31.90           C  
ANISOU10730  C   HIS D 214     5015   3398   3706   -456    -80    102       C  
ATOM  10731  O   HIS D 214     106.250   2.848-228.169  1.00 31.05           O  
ANISOU10731  O   HIS D 214     4972   3186   3639   -364   -114    101       O  
ATOM  10732  CB  HIS D 214     106.874   0.623-230.669  1.00 29.82           C  
ANISOU10732  CB  HIS D 214     4596   3280   3455   -377    -36     92       C  
ATOM  10733  CG  HIS D 214     106.079  -0.244-229.736  1.00 30.75           C  
ANISOU10733  CG  HIS D 214     4640   3384   3661   -229    -49     65       C  
ATOM  10734  ND1 HIS D 214     105.239  -1.242-230.186  1.00 27.73           N  
ANISOU10734  ND1 HIS D 214     4208   3012   3317   -127    -54     61       N  
ATOM  10735  CD2 HIS D 214     106.016  -0.284-228.376  1.00 28.45           C  
ANISOU10735  CD2 HIS D 214     4316   3076   3418   -179    -57     43       C  
ATOM  10736  CE1 HIS D 214     104.688  -1.849-229.149  1.00 33.31           C  
ANISOU10736  CE1 HIS D 214     4857   3709   4092    -26    -64     41       C  
ATOM  10737  NE2 HIS D 214     105.137  -1.282-228.039  1.00 31.57           N  
ANISOU10737  NE2 HIS D 214     4645   3473   3879    -51    -65     30       N  
ATOM  10738  N   ILE D 215     108.402   2.386-228.645  1.00 31.03           N  
ANISOU10738  N   ILE D 215     4824   3399   3566   -569    -45     79       N  
ATOM  10739  CA  ILE D 215     108.878   2.655-227.290  1.00 32.94           C  
ANISOU10739  CA  ILE D 215     5047   3646   3823   -593    -53     51       C  
ATOM  10740  C   ILE D 215     108.527   4.070-226.864  1.00 37.63           C  
ANISOU10740  C   ILE D 215     5832   4080   4383   -645    -96     72       C  
ATOM  10741  O   ILE D 215     108.113   4.306-225.719  1.00 34.26           O  
ANISOU10741  O   ILE D 215     5441   3585   3991   -579   -119     50       O  
ATOM  10742  CB  ILE D 215     110.393   2.392-227.208  1.00 31.11           C  
ANISOU10742  CB  ILE D 215     4690   3583   3549   -722    -13     31       C  
ATOM  10743  CG1 ILE D 215     110.674   0.898-227.397  1.00 34.80           C  
ANISOU10743  CG1 ILE D 215     4971   4193   4059   -626     27      0       C  
ATOM  10744  CG2 ILE D 215     110.984   2.887-225.842  1.00 34.25           C  
ANISOU10744  CG2 ILE D 215     5087   3985   3940   -785    -31      9       C  
ATOM  10745  CD1 ILE D 215     112.143   0.578-227.503  1.00 34.13           C  
ANISOU10745  CD1 ILE D 215     4746   4295   3929   -729     70    -20       C  
ATOM  10746  N   LYS D 216     108.670   5.034-227.775  1.00 36.97           N  
ANISOU10746  N   LYS D 216     5889   3930   4229   -760   -109    114       N  
ATOM  10747  CA  LYS D 216     108.394   6.418-227.410  1.00 40.64           C  
ANISOU10747  CA  LYS D 216     6564   4225   4654   -812   -155    134       C  
ATOM  10748  C   LYS D 216     106.906   6.618-227.132  1.00 41.28           C  
ANISOU10748  C   LYS D 216     6738   4156   4789   -623   -195    139       C  
ATOM  10749  O   LYS D 216     106.527   7.206-226.109  1.00 38.37           O  
ANISOU10749  O   LYS D 216     6460   3685   4434   -572   -220    117       O  
ATOM  10750  CB  LYS D 216     108.895   7.359-228.517  1.00 42.64           C  
ANISOU10750  CB  LYS D 216     6956   4435   4810   -985   -163    187       C  
ATOM  10751  CG  LYS D 216     108.565   8.820-228.324  1.00 56.08           C  
ANISOU10751  CG  LYS D 216     8913   5933   6462  -1039   -217    215       C  
ATOM  10752  CD  LYS D 216     109.433   9.703-229.239  1.00 73.92           C  
ANISOU10752  CD  LYS D 216    11296   8181   8610  -1270   -219    266       C  
ATOM  10753  CE  LYS D 216     109.680   9.063-230.609  1.00 79.50           C  
ANISOU10753  CE  LYS D 216    11902   9016   9287  -1310   -181    298       C  
ATOM  10754  NZ  LYS D 216     110.668   9.845-231.417  1.00 88.62           N  
ANISOU10754  NZ  LYS D 216    13150  10197  10323  -1559   -171    345       N  
ATOM  10755  N   TYR D 217     106.048   6.114-228.023  1.00 33.57           N  
ANISOU10755  N   TYR D 217     5736   3179   3840   -515   -200    164       N  
ATOM  10756  CA  TYR D 217     104.602   6.201-227.813  1.00 34.13           C  
ANISOU10756  CA  TYR D 217     5862   3144   3963   -328   -236    171       C  
ATOM  10757  C   TYR D 217     104.184   5.495-226.520  1.00 31.53           C  
ANISOU10757  C   TYR D 217     5417   2855   3709   -203   -223    121       C  
ATOM  10758  O   TYR D 217     103.397   6.027-225.727  1.00 34.07           O  
ANISOU10758  O   TYR D 217     5818   3077   4051    -98   -248    108       O  
ATOM  10759  CB  TYR D 217     103.852   5.585-229.002  1.00 33.76           C  
ANISOU10759  CB  TYR D 217     5768   3130   3930   -251   -243    205       C  
ATOM  10760  CG  TYR D 217     102.356   5.446-228.720  1.00 31.88           C  
ANISOU10760  CG  TYR D 217     5531   2832   3752    -54   -278    208       C  
ATOM  10761  CD1 TYR D 217     101.475   6.482-229.033  1.00 38.58           C  
ANISOU10761  CD1 TYR D 217     6545   3537   4577     20   -331    248       C  
ATOM  10762  CD2 TYR D 217     101.832   4.285-228.131  1.00 30.03           C  
ANISOU10762  CD2 TYR D 217     5132   2688   3591     58   -257    174       C  
ATOM  10763  CE1 TYR D 217     100.122   6.371-228.770  1.00 35.36           C  
ANISOU10763  CE1 TYR D 217     6117   3098   4218    206   -361    250       C  
ATOM  10764  CE2 TYR D 217     100.485   4.182-227.838  1.00 32.68           C  
ANISOU10764  CE2 TYR D 217     5455   2990   3973    222   -285    179       C  
ATOM  10765  CZ  TYR D 217      99.635   5.227-228.164  1.00 33.57           C  
ANISOU10765  CZ  TYR D 217     5713   2980   4062    299   -335    215       C  
ATOM  10766  OH  TYR D 217      98.290   5.121-227.889  1.00 47.32           O  
ANISOU10766  OH  TYR D 217     7422   4713   5846    470   -360    220       O  
ATOM  10767  N   ALA D 218     104.657   4.270-226.327  1.00 31.04           N  
ANISOU10767  N   ALA D 218     5170   2939   3684   -203   -184     93       N  
ATOM  10768  CA  ALA D 218     104.143   3.462-225.230  1.00 29.73           C  
ANISOU10768  CA  ALA D 218     4894   2814   3586    -80   -174     57       C  
ATOM  10769  C   ALA D 218     104.629   4.003-223.893  1.00 34.45           C  
ANISOU10769  C   ALA D 218     5530   3384   4174   -117   -175     22       C  
ATOM  10770  O   ALA D 218     103.896   3.966-222.897  1.00 35.03           O  
ANISOU10770  O   ALA D 218     5604   3422   4283     -7   -182     -1       O  
ATOM  10771  CB  ALA D 218     104.561   2.008-225.401  1.00 25.02           C  
ANISOU10771  CB  ALA D 218     4116   2365   3027    -70   -139     39       C  
ATOM  10772  N   THR D 219     105.868   4.490-223.854  1.00 29.17           N  
ANISOU10772  N   THR D 219     4889   2744   3450   -279   -168     17       N  
ATOM  10773  CA  THR D 219     106.424   5.025-222.614  1.00 34.93           C  
ANISOU10773  CA  THR D 219     5660   3455   4158   -338   -174    -17       C  
ATOM  10774  C   THR D 219     105.738   6.329-222.230  1.00 35.88           C  
ANISOU10774  C   THR D 219     5990   3395   4249   -308   -211    -17       C  
ATOM  10775  O   THR D 219     105.304   6.504-221.078  1.00 34.26           O  
ANISOU10775  O   THR D 219     5815   3144   4060   -230   -217    -53       O  
ATOM  10776  CB  THR D 219     107.931   5.246-222.761  1.00 36.96           C  
ANISOU10776  CB  THR D 219     5887   3802   4353   -537   -162    -17       C  
ATOM  10777  OG1 THR D 219     108.573   4.001-223.056  1.00 34.10           O  
ANISOU10777  OG1 THR D 219     5325   3614   4018   -537   -126    -24       O  
ATOM  10778  CG2 THR D 219     108.520   5.811-221.454  1.00 36.44           C  
ANISOU10778  CG2 THR D 219     5865   3724   4256   -613   -177    -52       C  
ATOM  10779  N   ASN D 220     105.669   7.274-223.171  1.00 34.71           N  
ANISOU10779  N   ASN D 220     5998   3139   4051   -369   -235     21       N  
ATOM  10780  CA  ASN D 220     104.885   8.482-222.988  1.00 36.69           C  
ANISOU10780  CA  ASN D 220     6466   3199   4276   -308   -274     26       C  
ATOM  10781  C   ASN D 220     105.286   9.180-221.682  1.00 39.22           C  
ANISOU10781  C   ASN D 220     6883   3455   4563   -359   -284    -22       C  
ATOM  10782  O   ASN D 220     104.448   9.581-220.883  1.00 36.56           O  
ANISOU10782  O   ASN D 220     6630   3019   4240   -226   -296    -53       O  
ATOM  10783  CB  ASN D 220     103.394   8.132-223.026  1.00 34.55           C  
ANISOU10783  CB  ASN D 220     6168   2893   4068    -82   -282     30       C  
ATOM  10784  CG  ASN D 220     102.507   9.345-223.067  1.00 38.65           C  
ANISOU10784  CG  ASN D 220     6903   3223   4561     13   -325     42       C  
ATOM  10785  OD1 ASN D 220     102.897  10.392-223.578  1.00 42.65           O  
ANISOU10785  OD1 ASN D 220     7597   3607   5001    -90   -355     69       O  
ATOM  10786  ND2 ASN D 220     101.289   9.205-222.560  1.00 35.22           N  
ANISOU10786  ND2 ASN D 220     6444   2764   4172    215   -328     24       N  
ATOM  10787  N   ARG D 221     106.606   9.286-221.484  1.00 39.33           N  
ANISOU10787  N   ARG D 221     6874   3542   4528   -557   -276    -31       N  
ATOM  10788  CA  ARG D 221     107.314   9.805-220.312  1.00 43.74           C  
ANISOU10788  CA  ARG D 221     7492   4085   5042   -663   -287    -75       C  
ATOM  10789  C   ARG D 221     106.730   9.367-218.967  1.00 42.48           C  
ANISOU10789  C   ARG D 221     7272   3942   4928   -516   -277   -129       C  
ATOM  10790  O   ARG D 221     106.655  10.159-218.017  1.00 40.76           O  
ANISOU10790  O   ARG D 221     7198   3619   4672   -523   -297   -169       O  
ATOM  10791  CB  ARG D 221     107.421  11.334-220.391  1.00 64.15           C  
ANISOU10791  CB  ARG D 221    10358   6473   7544   -770   -329    -68       C  
ATOM  10792  CG  ARG D 221     106.128  12.119-220.352  1.00 69.70           C  
ANISOU10792  CG  ARG D 221    11258   6970   8254   -593   -358    -71       C  
ATOM  10793  CD  ARG D 221     106.367  13.547-220.845  1.00 78.01           C  
ANISOU10793  CD  ARG D 221    12597   7825   9219   -720   -403    -44       C  
ATOM  10794  NE  ARG D 221     106.549  13.562-222.285  1.00 74.56           N  
ANISOU10794  NE  ARG D 221    12165   7401   8763   -798   -409     28       N  
ATOM  10795  CZ  ARG D 221     105.553  13.710-223.154  1.00 83.98           C  
ANISOU10795  CZ  ARG D 221    13425   8504   9977   -653   -428     71       C  
ATOM  10796  NH1 ARG D 221     104.310  13.871-222.715  1.00 85.82           N  
ANISOU10796  NH1 ARG D 221    13718   8636  10256   -417   -442     48       N  
ATOM  10797  NH2 ARG D 221     105.798  13.700-224.460  1.00 78.05           N  
ANISOU10797  NH2 ARG D 221    12679   7778   9199   -742   -432    137       N  
ATOM  10798  N   GLY D 222     106.363   8.097-218.859  1.00 41.86           N  
ANISOU10798  N   GLY D 222     6987   3995   4922   -395   -247   -131       N  
ATOM  10799  CA  GLY D 222     105.880   7.514-217.622  1.00 39.85           C  
ANISOU10799  CA  GLY D 222     6649   3784   4706   -273   -233   -173       C  
ATOM  10800  C   GLY D 222     104.393   7.246-217.603  1.00 38.39           C  
ANISOU10800  C   GLY D 222     6459   3550   4579    -57   -224   -173       C  
ATOM  10801  O   GLY D 222     103.938   6.436-216.795  1.00 38.84           O  
ANISOU10801  O   GLY D 222     6397   3684   4677     45   -203   -195       O  
ATOM  10802  N   ASN D 223     103.615   7.904-218.463  1.00 33.86           N  
ANISOU10802  N   ASN D 223     6007   2858   4003     12   -242   -145       N  
ATOM  10803  CA  ASN D 223     102.179   7.654-218.506  1.00 30.95           C  
ANISOU10803  CA  ASN D 223     5612   2465   3684    219   -237   -141       C  
ATOM  10804  C   ASN D 223     101.929   6.588-219.570  1.00 35.89           C  
ANISOU10804  C   ASN D 223     6078   3197   4361    247   -226    -96       C  
ATOM  10805  O   ASN D 223     101.538   6.869-220.709  1.00 35.92           O  
ANISOU10805  O   ASN D 223     6135   3151   4363    267   -246    -53       O  
ATOM  10806  CB  ASN D 223     101.413   8.935-218.793  1.00 39.51           C  
ANISOU10806  CB  ASN D 223     6911   3366   4734    302   -270   -136       C  
ATOM  10807  CG  ASN D 223      99.926   8.724-218.761  1.00 52.23           C  
ANISOU10807  CG  ASN D 223     8480   4974   6392    525   -265   -134       C  
ATOM  10808  OD1 ASN D 223      99.447   7.760-218.164  1.00 48.67           O  
ANISOU10808  OD1 ASN D 223     7862   4643   5988    608   -234   -151       O  
ATOM  10809  ND2 ASN D 223      99.180   9.615-219.412  1.00 66.78           N  
ANISOU10809  ND2 ASN D 223    10470   6685   8217    621   -299   -110       N  
ATOM  10810  N   LEU D 224     102.166   5.337-219.182  1.00 34.59           N  
ANISOU10810  N   LEU D 224     5726   3177   4239    249   -198   -105       N  
ATOM  10811  CA  LEU D 224     102.304   4.246-220.149  1.00 30.91           C  
ANISOU10811  CA  LEU D 224     5116   2818   3810    233   -186    -71       C  
ATOM  10812  C   LEU D 224     100.999   3.952-220.886  1.00 31.85           C  
ANISOU10812  C   LEU D 224     5210   2926   3968    369   -195    -41       C  
ATOM  10813  O   LEU D 224      99.905   4.033-220.318  1.00 32.44           O  
ANISOU10813  O   LEU D 224     5286   2976   4064    505   -196    -52       O  
ATOM  10814  CB  LEU D 224     102.794   2.977-219.438  1.00 31.36           C  
ANISOU10814  CB  LEU D 224     5000   3014   3902    222   -158    -91       C  
ATOM  10815  CG  LEU D 224     104.309   2.770-219.330  1.00 43.24           C  
ANISOU10815  CG  LEU D 224     6452   4599   5378     72   -150   -100       C  
ATOM  10816  CD1 LEU D 224     105.018   4.036-218.903  1.00 35.98           C  
ANISOU10816  CD1 LEU D 224     5675   3603   4392    -44   -168   -118       C  
ATOM  10817  CD2 LEU D 224     104.625   1.668-218.335  1.00 49.17           C  
ANISOU10817  CD2 LEU D 224     7060   5462   6159     97   -134   -121       C  
ATOM  10818  N   ARG D 225     101.129   3.597-222.170  1.00 30.55           N  
ANISOU10818  N   ARG D 225     5013   2791   3805    328   -201     -4       N  
ATOM  10819  CA  ARG D 225     100.009   3.265-223.046  1.00 30.07           C  
ANISOU10819  CA  ARG D 225     4921   2733   3771    430   -217     30       C  
ATOM  10820  C   ARG D 225     100.275   1.939-223.749  1.00 28.70           C  
ANISOU10820  C   ARG D 225     4604   2678   3625    394   -199     41       C  
ATOM  10821  O   ARG D 225     101.372   1.722-224.277  1.00 33.63           O  
ANISOU10821  O   ARG D 225     5209   3344   4225    277   -184     42       O  
ATOM  10822  CB  ARG D 225      99.796   4.356-224.127  1.00 33.31           C  
ANISOU10822  CB  ARG D 225     5486   3034   4137    417   -255     70       C  
ATOM  10823  CG  ARG D 225      99.631   5.754-223.629  1.00 35.44           C  
ANISOU10823  CG  ARG D 225     5938   3159   4368    444   -279     62       C  
ATOM  10824  CD  ARG D 225      99.424   6.716-224.811  1.00 37.01           C  
ANISOU10824  CD  ARG D 225     6295   3246   4521    431   -323    113       C  
ATOM  10825  NE  ARG D 225     100.685   7.216-225.344  1.00 42.46           N  
ANISOU10825  NE  ARG D 225     7076   3905   5151    241   -322    128       N  
ATOM  10826  CZ  ARG D 225     100.838   8.431-225.864  1.00 46.34           C  
ANISOU10826  CZ  ARG D 225     7770   4256   5580    186   -359    159       C  
ATOM  10827  NH1 ARG D 225      99.805   9.263-225.911  1.00 43.63           N  
ANISOU10827  NH1 ARG D 225     7563   3782   5231    327   -402    177       N  
ATOM  10828  NH2 ARG D 225     102.022   8.819-226.328  1.00 40.83           N  
ANISOU10828  NH2 ARG D 225     7140   3552   4821     -9   -354    175       N  
ATOM  10829  N   SER D 226      99.275   1.058-223.770  1.00 29.75           N  
ANISOU10829  N   SER D 226     4636   2865   3801    492   -200     48       N  
ATOM  10830  CA  SER D 226      99.459  -0.248-224.383  1.00 30.07           C  
ANISOU10830  CA  SER D 226     4559   3001   3866    463   -186     53       C  
ATOM  10831  C   SER D 226      99.587  -0.117-225.903  1.00 26.69           C  
ANISOU10831  C   SER D 226     4173   2564   3406    411   -202     85       C  
ATOM  10832  O   SER D 226      98.882   0.675-226.529  1.00 31.87           O  
ANISOU10832  O   SER D 226     4915   3154   4041    450   -237    117       O  
ATOM  10833  CB  SER D 226      98.285  -1.166-224.046  1.00 30.08           C  
ANISOU10833  CB  SER D 226     4461   3056   3913    562   -189     57       C  
ATOM  10834  OG  SER D 226      98.170  -1.347-222.624  1.00 34.08           O  
ANISOU10834  OG  SER D 226     4927   3582   4441    604   -170     30       O  
ATOM  10835  N   ALA D 227     100.495  -0.893-226.495  1.00 27.31           N  
ANISOU10835  N   ALA D 227     4193   2711   3475    329   -178     76       N  
ATOM  10836  CA  ALA D 227     100.689  -0.803-227.947  1.00 26.67           C  
ANISOU10836  CA  ALA D 227     4151   2632   3351    270   -186    102       C  
ATOM  10837  C   ALA D 227     101.258  -2.099-228.496  1.00 30.64           C  
ANISOU10837  C   ALA D 227     4553   3230   3858    235   -155     81       C  
ATOM  10838  O   ALA D 227     101.878  -2.888-227.780  1.00 29.94           O  
ANISOU10838  O   ALA D 227     4380   3198   3797    233   -126     47       O  
ATOM  10839  CB  ALA D 227     101.615   0.364-228.312  1.00 28.69           C  
ANISOU10839  CB  ALA D 227     4518   2838   3545    162   -184    115       C  
ATOM  10840  N   ILE D 228     101.043  -2.314-229.801  1.00 29.53           N  
ANISOU10840  N   ILE D 228     4432   3103   3686    212   -165    100       N  
ATOM  10841  CA  ILE D 228     101.653  -3.434-230.503  1.00 27.15           C  
ANISOU10841  CA  ILE D 228     4061   2881   3373    176   -134     75       C  
ATOM  10842  C   ILE D 228     102.045  -2.917-231.881  1.00 30.95           C  
ANISOU10842  C   ILE D 228     4612   3366   3780     93   -132     97       C  
ATOM  10843  O   ILE D 228     101.321  -2.109-232.467  1.00 28.36           O  
ANISOU10843  O   ILE D 228     4374   2977   3426     98   -174    141       O  
ATOM  10844  CB  ILE D 228     100.699  -4.643-230.623  1.00 27.57           C  
ANISOU10844  CB  ILE D 228     4052   2959   3465    247   -150     68       C  
ATOM  10845  CG1 ILE D 228     101.380  -5.796-231.369  1.00 27.68           C  
ANISOU10845  CG1 ILE D 228     4019   3038   3460    216   -117     33       C  
ATOM  10846  CG2 ILE D 228      99.382  -4.225-231.315  1.00 28.42           C  
ANISOU10846  CG2 ILE D 228     4211   3027   3562    285   -204    112       C  
ATOM  10847  CD1 ILE D 228     100.618  -7.121-231.251  1.00 26.91           C  
ANISOU10847  CD1 ILE D 228     3870   2954   3401    273   -130     17       C  
ATOM  10848  N   THR D 229     103.221  -3.307-232.355  1.00 27.58           N  
ANISOU10848  N   THR D 229     4148   3015   3316     20    -84     69       N  
ATOM  10849  CA  THR D 229     103.654  -3.000-233.723  1.00 28.09           C  
ANISOU10849  CA  THR D 229     4266   3107   3301    -67    -71     85       C  
ATOM  10850  C   THR D 229     103.749  -4.316-234.479  1.00 30.26           C  
ANISOU10850  C   THR D 229     4476   3456   3566    -45    -44     48       C  
ATOM  10851  O   THR D 229     104.421  -5.249-234.017  1.00 30.76           O  
ANISOU10851  O   THR D 229     4449   3583   3657    -19     -4     -1       O  
ATOM  10852  CB  THR D 229     105.019  -2.304-233.737  1.00 27.38           C  
ANISOU10852  CB  THR D 229     4185   3064   3156   -184    -28     81       C  
ATOM  10853  OG1 THR D 229     104.939  -1.075-233.011  1.00 33.46           O  
ANISOU10853  OG1 THR D 229     5037   3748   3928   -212    -57    112       O  
ATOM  10854  CG2 THR D 229     105.432  -2.003-235.199  1.00 27.34           C  
ANISOU10854  CG2 THR D 229     4235   3097   3055   -283    -10    102       C  
ATOM  10855  N   VAL D 230     103.098  -4.430-235.631  1.00 30.26           N  
ANISOU10855  N   VAL D 230     4527   3446   3523    -53    -68     68       N  
ATOM  10856  CA  VAL D 230     103.105  -5.735-236.266  1.00 33.12           C  
ANISOU10856  CA  VAL D 230     4842   3864   3877    -28    -47     24       C  
ATOM  10857  C   VAL D 230     103.814  -5.637-237.607  1.00 34.92           C  
ANISOU10857  C   VAL D 230     5105   4154   4007   -114    -10     17       C  
ATOM  10858  O   VAL D 230     103.444  -4.839-238.493  1.00 27.92           O  
ANISOU10858  O   VAL D 230     4309   3241   3059   -170    -39     66       O  
ATOM  10859  CB  VAL D 230     101.709  -6.392-236.317  1.00 46.27           C  
ANISOU10859  CB  VAL D 230     6511   5487   5581     44   -103     35       C  
ATOM  10860  CG1 VAL D 230     100.574  -5.443-235.957  1.00 51.73           C  
ANISOU10860  CG1 VAL D 230     7250   6106   6300     78   -169     95       C  
ATOM  10861  CG2 VAL D 230     101.493  -7.241-237.547  1.00 30.58           C  
ANISOU10861  CG2 VAL D 230     4545   3534   3541     26   -104     13       C  
ATOM  10862  N   PHE D 231     104.908  -6.378-237.692  1.00 33.77           N  
ANISOU10862  N   PHE D 231     4890   4098   3843   -121     58    -41       N  
ATOM  10863  CA  PHE D 231     105.774  -6.397-238.849  1.00 36.96           C  
ANISOU10863  CA  PHE D 231     5302   4591   4150   -197    113    -61       C  
ATOM  10864  C   PHE D 231     105.207  -7.383-239.865  1.00 32.17           C  
ANISOU10864  C   PHE D 231     4724   3990   3509   -166    106    -92       C  
ATOM  10865  O   PHE D 231     104.195  -8.044-239.593  1.00 31.89           O  
ANISOU10865  O   PHE D 231     4696   3892   3529    -95     57    -95       O  
ATOM  10866  CB  PHE D 231     107.185  -6.730-238.372  1.00 31.39           C  
ANISOU10866  CB  PHE D 231     4492   3993   3443   -202    188   -113       C  
ATOM  10867  CG  PHE D 231     107.825  -5.615-237.585  1.00 30.28           C  
ANISOU10867  CG  PHE D 231     4337   3860   3309   -273    192    -79       C  
ATOM  10868  CD1 PHE D 231     108.334  -4.496-238.229  1.00 37.78           C  
ANISOU10868  CD1 PHE D 231     5343   4838   4173   -407    207    -38       C  
ATOM  10869  CD2 PHE D 231     107.887  -5.669-236.197  1.00 31.07           C  
ANISOU10869  CD2 PHE D 231     4380   3933   3493   -218    177    -85       C  
ATOM  10870  CE1 PHE D 231     108.910  -3.456-237.520  1.00 35.22           C  
ANISOU10870  CE1 PHE D 231     5025   4512   3847   -490    205     -7       C  
ATOM  10871  CE2 PHE D 231     108.476  -4.638-235.473  1.00 32.76           C  
ANISOU10871  CE2 PHE D 231     4591   4151   3704   -293    176    -58       C  
ATOM  10872  CZ  PHE D 231     108.985  -3.526-236.129  1.00 28.80           C  
ANISOU10872  CZ  PHE D 231     4152   3672   3117   -432    189    -20       C  
ATOM  10873  N   PRO D 232     105.803  -7.466-241.065  1.00 32.11           N  
ANISOU10873  N   PRO D 232     4739   4060   3400   -229    153   -113       N  
ATOM  10874  CA  PRO D 232     105.183  -8.250-242.139  1.00 35.87           C  
ANISOU10874  CA  PRO D 232     5270   4533   3826   -216    139   -138       C  
ATOM  10875  C   PRO D 232     104.977  -9.715-241.762  1.00 35.00           C  
ANISOU10875  C   PRO D 232     5118   4408   3772   -112    144   -207       C  
ATOM  10876  O   PRO D 232     105.766 -10.321-241.036  1.00 31.87           O  
ANISOU10876  O   PRO D 232     4643   4047   3419    -51    191   -258       O  
ATOM  10877  CB  PRO D 232     106.172  -8.099-243.304  1.00 30.42           C  
ANISOU10877  CB  PRO D 232     4591   3952   3013   -300    211   -162       C  
ATOM  10878  CG  PRO D 232     106.825  -6.752-243.067  1.00 29.04           C  
ANISOU10878  CG  PRO D 232     4418   3803   2814   -397    226   -104       C  
ATOM  10879  CD  PRO D 232     106.970  -6.702-241.552  1.00 29.06           C  
ANISOU10879  CD  PRO D 232     4344   3769   2929   -335    216   -106       C  
ATOM  10880  N   GLN D 233     103.891 -10.284-242.278  1.00 34.55           N  
ANISOU10880  N   GLN D 233     5123   4296   3708    -98     88   -206       N  
ATOM  10881  CA  GLN D 233     103.574 -11.675-242.005  1.00 33.06           C  
ANISOU10881  CA  GLN D 233     4925   4074   3562    -19     82   -267       C  
ATOM  10882  C   GLN D 233     104.548 -12.615-242.710  1.00 31.80           C  
ANISOU10882  C   GLN D 233     4765   3981   3335      6    159   -357       C  
ATOM  10883  O   GLN D 233     105.211 -12.258-243.687  1.00 32.75           O  
ANISOU10883  O   GLN D 233     4903   4183   3359    -51    211   -371       O  
ATOM  10884  CB  GLN D 233     102.148 -12.001-242.439  1.00 28.49           C  
ANISOU10884  CB  GLN D 233     4414   3431   2980    -33     -2   -240       C  
ATOM  10885  CG  GLN D 233     101.965 -11.996-243.985  1.00 29.25           C  
ANISOU10885  CG  GLN D 233     4595   3562   2957   -105     -8   -247       C  
ATOM  10886  CD  GLN D 233     100.527 -11.756-244.387  1.00 41.42           C  
ANISOU10886  CD  GLN D 233     6189   5059   4490   -141   -108   -186       C  
ATOM  10887  OE1 GLN D 233      99.887 -10.814-243.900  1.00 39.94           O  
ANISOU10887  OE1 GLN D 233     5985   4843   4347   -142   -162   -109       O  
ATOM  10888  NE2 GLN D 233     100.001 -12.605-245.279  1.00 39.90           N  
ANISOU10888  NE2 GLN D 233     6060   4864   4234   -167   -135   -221       N  
ATOM  10889  N   ARG D 234     104.627 -13.831-242.167  1.00 33.95           N  
ANISOU10889  N   ARG D 234     5023   4219   3659     96    169   -417       N  
ATOM  10890  CA  ARG D 234     105.347 -14.926-242.793  1.00 35.43           C  
ANISOU10890  CA  ARG D 234     5231   4443   3789    150    231   -512       C  
ATOM  10891  C   ARG D 234     104.789 -15.216-244.176  1.00 35.33           C  
ANISOU10891  C   ARG D 234     5325   4425   3675     91    215   -534       C  
ATOM  10892  O   ARG D 234     103.576 -15.187-244.398  1.00 36.36           O  
ANISOU10892  O   ARG D 234     5518   4488   3810     42    133   -491       O  
ATOM  10893  CB  ARG D 234     105.225 -16.178-241.918  1.00 32.77           C  
ANISOU10893  CB  ARG D 234     4895   4028   3529    255    216   -558       C  
ATOM  10894  CG  ARG D 234     105.847 -17.423-242.473  1.00 35.53           C  
ANISOU10894  CG  ARG D 234     5290   4382   3826    335    269   -660       C  
ATOM  10895  CD  ARG D 234     105.812 -18.501-241.386  1.00 40.62           C  
ANISOU10895  CD  ARG D 234     5938   4938   4559    442    248   -688       C  
ATOM  10896  NE  ARG D 234     106.750 -18.197-240.309  1.00 38.25           N  
ANISOU10896  NE  ARG D 234     5517   4694   4322    511    284   -676       N  
ATOM  10897  CZ  ARG D 234     106.704 -18.746-239.093  1.00 42.99           C  
ANISOU10897  CZ  ARG D 234     6095   5229   5011    587    256   -667       C  
ATOM  10898  NH1 ARG D 234     105.738 -19.605-238.785  1.00 38.97           N  
ANISOU10898  NH1 ARG D 234     5676   4594   4538    594    193   -664       N  
ATOM  10899  NH2 ARG D 234     107.608 -18.424-238.182  1.00 40.23           N  
ANISOU10899  NH2 ARG D 234     5633   4945   4706    643    287   -657       N  
ATOM  10900  N   CYS D 235     105.676 -15.527-245.106  1.00 34.81           N  
ANISOU10900  N   CYS D 235     5274   4442   3512     98    293   -604       N  
ATOM  10901  CA  CYS D 235     105.193 -15.897-246.428  1.00 44.61           C  
ANISOU10901  CA  CYS D 235     6625   5679   4646     44    281   -635       C  
ATOM  10902  C   CYS D 235     106.195 -16.837-247.083  1.00 47.55           C  
ANISOU10902  C   CYS D 235     7016   6113   4938    115    374   -750       C  
ATOM  10903  O   CYS D 235     107.399 -16.753-246.804  1.00 43.38           O  
ANISOU10903  O   CYS D 235     6394   5680   4409    173    459   -785       O  
ATOM  10904  CB  CYS D 235     104.944 -14.655-247.296  1.00 59.93           C  
ANISOU10904  CB  CYS D 235     8591   7676   6505    -81    263   -562       C  
ATOM  10905  SG  CYS D 235     106.397 -13.680-247.655  1.00 70.74           S  
ANISOU10905  SG  CYS D 235     9882   9197   7798   -128    369   -559       S  
ATOM  10906  N   PRO D 236     105.736 -17.748-247.936  1.00 47.34           N  
ANISOU10906  N   PRO D 236     7108   6038   4841    115    359   -814       N  
ATOM  10907  CA  PRO D 236     106.662 -18.718-248.535  1.00 50.55           C  
ANISOU10907  CA  PRO D 236     7546   6490   5169    205    450   -935       C  
ATOM  10908  C   PRO D 236     107.669 -18.021-249.436  1.00 47.18           C  
ANISOU10908  C   PRO D 236     7071   6230   4628    163    547   -953       C  
ATOM  10909  O   PRO D 236     107.365 -17.010-250.070  1.00 47.68           O  
ANISOU10909  O   PRO D 236     7146   6342   4629     35    528   -883       O  
ATOM  10910  CB  PRO D 236     105.741 -19.652-249.331  1.00 55.35           C  
ANISOU10910  CB  PRO D 236     8316   6999   5714    177    395   -985       C  
ATOM  10911  CG  PRO D 236     104.493 -18.868-249.566  1.00 55.02           C  
ANISOU10911  CG  PRO D 236     8308   6924   5674     39    292   -882       C  
ATOM  10912  CD  PRO D 236     104.342 -17.967-248.356  1.00 49.12           C  
ANISOU10912  CD  PRO D 236     7442   6169   5052     38    257   -781       C  
ATOM  10913  N   GLY D 237     108.889 -18.555-249.463  1.00 46.35           N  
ANISOU10913  N   GLY D 237     6906   6216   4490    273    652  -1044       N  
ATOM  10914  CA  GLY D 237     109.925 -18.023-250.326  1.00 52.15           C  
ANISOU10914  CA  GLY D 237     7580   7130   5104    237    758  -1073       C  
ATOM  10915  C   GLY D 237     110.670 -16.827-249.790  1.00 53.71           C  
ANISOU10915  C   GLY D 237     7627   7451   5331    179    794   -996       C  
ATOM  10916  O   GLY D 237     111.412 -16.189-250.548  1.00 55.81           O  
ANISOU10916  O   GLY D 237     7847   7871   5487    104    873   -997       O  
ATOM  10917  N   ARG D 238     110.484 -16.493-248.514  1.00 48.76           N  
ANISOU10917  N   ARG D 238     6927   6759   4839    199    739   -930       N  
ATOM  10918  CA  ARG D 238     111.143 -15.360-247.888  1.00 45.55           C  
ANISOU10918  CA  ARG D 238     6390   6451   4465    136    762   -858       C  
ATOM  10919  C   ARG D 238     111.312 -15.694-246.413  1.00 42.17           C  
ANISOU10919  C   ARG D 238     5876   5968   4180    246    734   -851       C  
ATOM  10920  O   ARG D 238     110.433 -16.317-245.816  1.00 38.04           O  
ANISOU10920  O   ARG D 238     5419   5292   3744    304    657   -846       O  
ATOM  10921  CB  ARG D 238     110.321 -14.072-248.070  1.00 51.91           C  
ANISOU10921  CB  ARG D 238     7248   7210   5264    -28    688   -739       C  
ATOM  10922  CG  ARG D 238     110.881 -12.846-247.375  1.00 65.43           C  
ANISOU10922  CG  ARG D 238     8859   8990   7012   -108    696   -659       C  
ATOM  10923  CD  ARG D 238     109.962 -11.630-247.521  1.00 81.90           C  
ANISOU10923  CD  ARG D 238    11026  10996   9097   -246    611   -544       C  
ATOM  10924  NE  ARG D 238     110.246 -10.845-248.726  1.00 92.34           N  
ANISOU10924  NE  ARG D 238    12397  12412  10278   -384    649   -514       N  
ATOM  10925  CZ  ARG D 238     109.454 -10.776-249.795  1.00 94.08           C  
ANISOU10925  CZ  ARG D 238    12743  12590  10414   -448    608   -494       C  
ATOM  10926  NH1 ARG D 238     108.305 -11.440-249.831  1.00 90.28           N  
ANISOU10926  NH1 ARG D 238    12346  11981   9977   -393    527   -502       N  
ATOM  10927  NH2 ARG D 238     109.809 -10.031-250.834  1.00 97.14           N  
ANISOU10927  NH2 ARG D 238    13173  13071  10666   -579    646   -461       N  
ATOM  10928  N   GLY D 239     112.445 -15.302-245.842  1.00 39.41           N  
ANISOU10928  N   GLY D 239     5379   5751   3844    266    796   -851       N  
ATOM  10929  CA  GLY D 239     112.658 -15.473-244.416  1.00 37.57           C  
ANISOU10929  CA  GLY D 239     5056   5481   3736    355    765   -833       C  
ATOM  10930  C   GLY D 239     111.733 -14.606-243.573  1.00 39.18           C  
ANISOU10930  C   GLY D 239     5287   5567   4033    267    668   -727       C  
ATOM  10931  O   GLY D 239     111.103 -13.656-244.040  1.00 42.47           O  
ANISOU10931  O   GLY D 239     5766   5954   4416    133    630   -658       O  
ATOM  10932  N   ASP D 240     111.654 -14.946-242.288  1.00 37.95           N  
ANISOU10932  N   ASP D 240     5085   5343   3991    353    627   -716       N  
ATOM  10933  CA  ASP D 240     110.863 -14.174-241.333  1.00 37.90           C  
ANISOU10933  CA  ASP D 240     5088   5236   4074    291    544   -625       C  
ATOM  10934  C   ASP D 240     111.591 -12.916-240.872  1.00 40.41           C  
ANISOU10934  C   ASP D 240     5309   5655   4389    195    565   -569       C  
ATOM  10935  O   ASP D 240     112.818 -12.890-240.741  1.00 41.84           O  
ANISOU10935  O   ASP D 240     5372   5985   4541    214    634   -601       O  
ATOM  10936  CB  ASP D 240     110.551 -14.988-240.068  1.00 35.22           C  
ANISOU10936  CB  ASP D 240     4736   4797   3850    410    495   -632       C  
ATOM  10937  CG  ASP D 240     109.643 -16.181-240.317  1.00 45.95           C  
ANISOU10937  CG  ASP D 240     6212   6023   5225    481    454   -671       C  
ATOM  10938  OD1 ASP D 240     108.841 -16.161-241.276  1.00 42.02           O  
ANISOU10938  OD1 ASP D 240     5816   5476   4674    414    429   -667       O  
ATOM  10939  OD2 ASP D 240     109.726 -17.136-239.508  1.00 45.57           O  
ANISOU10939  OD2 ASP D 240     6157   5916   5241    598    439   -702       O  
ATOM  10940  N   PHE D 241     110.809 -11.887-240.556  1.00 32.36           N  
ANISOU10940  N   PHE D 241     4341   4554   3401     96    499   -484       N  
ATOM  10941  CA  PHE D 241     111.269 -10.854-239.643  1.00 33.93           C  
ANISOU10941  CA  PHE D 241     4470   4787   3635     31    491   -430       C  
ATOM  10942  C   PHE D 241     111.274 -11.431-238.229  1.00 35.49           C  
ANISOU10942  C   PHE D 241     4605   4937   3941    141    460   -439       C  
ATOM  10943  O   PHE D 241     110.320 -12.099-237.825  1.00 34.62           O  
ANISOU10943  O   PHE D 241     4555   4701   3898    215    405   -439       O  
ATOM  10944  CB  PHE D 241     110.336  -9.636-239.680  1.00 37.64           C  
ANISOU10944  CB  PHE D 241     5036   5158   4109    -83    424   -342       C  
ATOM  10945  CG  PHE D 241     110.501  -8.764-240.875  1.00 39.09           C  
ANISOU10945  CG  PHE D 241     5276   5394   4180   -217    449   -311       C  
ATOM  10946  CD1 PHE D 241     109.823  -9.050-242.058  1.00 39.86           C  
ANISOU10946  CD1 PHE D 241     5471   5458   4215   -231    439   -317       C  
ATOM  10947  CD2 PHE D 241     111.327  -7.656-240.830  1.00 42.75           C  
ANISOU10947  CD2 PHE D 241     5706   5943   4595   -341    479   -272       C  
ATOM  10948  CE1 PHE D 241     109.959  -8.234-243.160  1.00 37.33           C  
ANISOU10948  CE1 PHE D 241     5214   5187   3785   -359    457   -281       C  
ATOM  10949  CE2 PHE D 241     111.485  -6.844-241.958  1.00 46.49           C  
ANISOU10949  CE2 PHE D 241     6246   6462   4955   -479    501   -235       C  
ATOM  10950  CZ  PHE D 241     110.793  -7.136-243.114  1.00 39.30           C  
ANISOU10950  CZ  PHE D 241     5433   5515   3983   -482    490   -238       C  
ATOM  10951  N   ARG D 242     112.346 -11.183-237.474  1.00 34.15           N  
ANISOU10951  N   ARG D 242     4317   4875   3785    144    492   -444       N  
ATOM  10952  CA  ARG D 242     112.394 -11.600-236.073  1.00 32.89           C  
ANISOU10952  CA  ARG D 242     4099   4677   3720    236    457   -443       C  
ATOM  10953  C   ARG D 242     113.111 -10.557-235.236  1.00 34.22           C  
ANISOU10953  C   ARG D 242     4185   4922   3895    150    456   -403       C  
ATOM  10954  O   ARG D 242     114.075  -9.933-235.679  1.00 32.76           O  
ANISOU10954  O   ARG D 242     3932   4878   3637     58    509   -404       O  
ATOM  10955  CB  ARG D 242     113.128 -12.944-235.863  1.00 34.46           C  
ANISOU10955  CB  ARG D 242     4222   4938   3934    394    494   -517       C  
ATOM  10956  CG  ARG D 242     112.427 -14.155-236.463  1.00 38.53           C  
ANISOU10956  CG  ARG D 242     4835   5353   4453    495    485   -565       C  
ATOM  10957  CD  ARG D 242     111.102 -14.446-235.748  1.00 39.70           C  
ANISOU10957  CD  ARG D 242     5078   5321   4685    516    401   -526       C  
ATOM  10958  NE  ARG D 242     111.266 -14.772-234.328  1.00 38.67           N  
ANISOU10958  NE  ARG D 242     4891   5164   4636    593    368   -513       N  
ATOM  10959  CZ  ARG D 242     111.453 -16.003-233.851  1.00 43.98           C  
ANISOU10959  CZ  ARG D 242     5563   5802   5346    730    362   -553       C  
ATOM  10960  NH1 ARG D 242     111.519 -17.034-234.678  1.00 44.26           N  
ANISOU10960  NH1 ARG D 242     5654   5818   5344    812    389   -618       N  
ATOM  10961  NH2 ARG D 242     111.574 -16.202-232.537  1.00 43.92           N  
ANISOU10961  NH2 ARG D 242     5510   5772   5406    787    326   -530       N  
ATOM  10962  N   ILE D 243     112.642 -10.402-234.005  1.00 33.58           N  
ANISOU10962  N   ILE D 243     4111   4752   3895    173    397   -369       N  
ATOM  10963  CA  ILE D 243     113.372  -9.711-232.949  1.00 38.55           C  
ANISOU10963  CA  ILE D 243     4656   5450   4542    124    390   -345       C  
ATOM  10964  C   ILE D 243     113.956 -10.789-232.044  1.00 33.68           C  
ANISOU10964  C   ILE D 243     3938   4882   3976    266    392   -384       C  
ATOM  10965  O   ILE D 243     113.217 -11.604-231.492  1.00 32.41           O  
ANISOU10965  O   ILE D 243     3825   4608   3882    371    351   -388       O  
ATOM  10966  CB  ILE D 243     112.453  -8.760-232.166  1.00 35.36           C  
ANISOU10966  CB  ILE D 243     4339   4912   4184     58    323   -284       C  
ATOM  10967  CG1 ILE D 243     111.861  -7.716-233.114  1.00 39.38           C  
ANISOU10967  CG1 ILE D 243     4960   5362   4639    -63    315   -242       C  
ATOM  10968  CG2 ILE D 243     113.206  -8.107-231.001  1.00 31.97           C  
ANISOU10968  CG2 ILE D 243     3835   4545   3768      6    311   -266       C  
ATOM  10969  CD1 ILE D 243     110.697  -6.949-232.533  1.00 39.43           C  
ANISOU10969  CD1 ILE D 243     5075   5215   4693    -85    248   -189       C  
ATOM  10970  N   TRP D 244     115.284 -10.847-231.949  1.00 29.61           N  
ANISOU10970  N   TRP D 244     3284   4544   3423    271    438   -412       N  
ATOM  10971  CA  TRP D 244     115.905 -11.945-231.225  1.00 30.86           C  
ANISOU10971  CA  TRP D 244     3345   4761   3621    428    440   -450       C  
ATOM  10972  C   TRP D 244     115.767 -11.757-229.718  1.00 39.89           C  
ANISOU10972  C   TRP D 244     4471   5855   4832    438    376   -413       C  
ATOM  10973  O   TRP D 244     115.673 -12.746-228.981  1.00 35.92           O  
ANISOU10973  O   TRP D 244     3957   5306   4384    577    347   -426       O  
ATOM  10974  CB  TRP D 244     117.381 -12.072-231.613  1.00 30.47           C  
ANISOU10974  CB  TRP D 244     3134   4940   3505    443    509   -492       C  
ATOM  10975  CG  TRP D 244     117.645 -12.724-232.983  1.00 33.92           C  
ANISOU10975  CG  TRP D 244     3571   5441   3876    502    582   -553       C  
ATOM  10976  CD1 TRP D 244     116.859 -12.678-234.089  1.00 37.96           C  
ANISOU10976  CD1 TRP D 244     4208   5862   4354    457    596   -558       C  
ATOM  10977  CD2 TRP D 244     118.769 -13.545-233.321  1.00 37.06           C  
ANISOU10977  CD2 TRP D 244     3836   6012   4233    628    646   -619       C  
ATOM  10978  NE1 TRP D 244     117.437 -13.406-235.123  1.00 35.58           N  
ANISOU10978  NE1 TRP D 244     3869   5663   3985    537    669   -627       N  
ATOM  10979  CE2 TRP D 244     118.617 -13.939-234.671  1.00 39.63           C  
ANISOU10979  CE2 TRP D 244     4223   6341   4495    649    705   -668       C  
ATOM  10980  CE3 TRP D 244     119.904 -13.968-232.614  1.00 37.41           C  
ANISOU10980  CE3 TRP D 244     3712   6220   4283    731    659   -642       C  
ATOM  10981  CZ2 TRP D 244     119.545 -14.755-235.319  1.00 45.88           C  
ANISOU10981  CZ2 TRP D 244     4919   7286   5229    777    782   -745       C  
ATOM  10982  CZ3 TRP D 244     120.828 -14.762-233.255  1.00 43.46           C  
ANISOU10982  CZ3 TRP D 244     4373   7145   4997    865    732   -714       C  
ATOM  10983  CH2 TRP D 244     120.648 -15.152-234.602  1.00 48.62           C  
ANISOU10983  CH2 TRP D 244     5094   7792   5586    890    797   -769       C  
ATOM  10984  N   ASN D 245     115.737 -10.507-229.253  1.00 32.63           N  
ANISOU10984  N   ASN D 245     3561   4935   3902    292    353   -366       N  
ATOM  10985  CA  ASN D 245     115.554 -10.217-227.830  1.00 31.89           C  
ANISOU10985  CA  ASN D 245     3465   4790   3862    288    294   -333       C  
ATOM  10986  C   ASN D 245     114.167 -10.655-227.377  1.00 39.42           C  
ANISOU10986  C   ASN D 245     4542   5549   4885    358    243   -314       C  
ATOM  10987  O   ASN D 245     113.183 -10.536-228.115  1.00 32.32           O  
ANISOU10987  O   ASN D 245     3752   4540   3987    336    240   -305       O  
ATOM  10988  CB  ASN D 245     115.716  -8.721-227.551  1.00 31.28           C  
ANISOU10988  CB  ASN D 245     3407   4730   3749    108    280   -292       C  
ATOM  10989  CG  ASN D 245     116.961  -8.143-228.162  1.00 45.02           C  
ANISOU10989  CG  ASN D 245     5040   6659   5405     -6    332   -302       C  
ATOM  10990  OD1 ASN D 245     117.147  -8.170-229.392  1.00 47.00           O  
ANISOU10990  OD1 ASN D 245     5292   6965   5602    -35    385   -319       O  
ATOM  10991  ND2 ASN D 245     117.816  -7.583-227.317  1.00 40.49           N  
ANISOU10991  ND2 ASN D 245     4376   6196   4812    -86    317   -289       N  
ATOM  10992  N   SER D 246     114.085 -11.150-226.135  1.00 32.00           N  
ANISOU10992  N   SER D 246     3581   4577   3998    437    200   -305       N  
ATOM  10993  CA  SER D 246     112.789 -11.579-225.624  1.00 26.53           C  
ANISOU10993  CA  SER D 246     2995   3719   3365    492    155   -284       C  
ATOM  10994  C   SER D 246     111.909 -10.400-225.235  1.00 28.06           C  
ANISOU10994  C   SER D 246     3273   3820   3567    386    124   -242       C  
ATOM  10995  O   SER D 246     110.680 -10.522-225.218  1.00 28.32           O  
ANISOU10995  O   SER D 246     3399   3728   3634    406     99   -224       O  
ATOM  10996  CB  SER D 246     112.984 -12.517-224.431  1.00 36.04           C  
ANISOU10996  CB  SER D 246     4158   4920   4614    606    120   -283       C  
ATOM  10997  OG  SER D 246     113.546 -11.801-223.354  1.00 37.56           O  
ANISOU10997  OG  SER D 246     4289   5179   4801    549     97   -262       O  
ATOM  10998  N   GLN D 247     112.513  -9.272-224.859  1.00 30.32           N  
ANISOU10998  N   GLN D 247     3530   4169   3820    277    124   -228       N  
ATOM  10999  CA  GLN D 247     111.798  -8.028-224.631  1.00 27.22           C  
ANISOU10999  CA  GLN D 247     3233   3686   3422    177    100   -195       C  
ATOM  11000  C   GLN D 247     112.588  -6.893-225.257  1.00 29.05           C  
ANISOU11000  C   GLN D 247     3459   3995   3586     33    125   -190       C  
ATOM  11001  O   GLN D 247     113.803  -6.988-225.449  1.00 33.33           O  
ANISOU11001  O   GLN D 247     3891   4685   4087      0    156   -208       O  
ATOM  11002  CB  GLN D 247     111.586  -7.713-223.132  1.00 28.66           C  
ANISOU11002  CB  GLN D 247     3426   3831   3634    179     57   -178       C  
ATOM  11003  CG  GLN D 247     110.690  -8.677-222.408  1.00 25.63           C  
ANISOU11003  CG  GLN D 247     3065   3365   3309    295     30   -172       C  
ATOM  11004  CD  GLN D 247     110.495  -8.262-220.941  1.00 36.27           C  
ANISOU11004  CD  GLN D 247     4426   4685   4670    286     -6   -157       C  
ATOM  11005  OE1 GLN D 247     110.566  -7.088-220.606  1.00 37.75           O  
ANISOU11005  OE1 GLN D 247     4654   4861   4830    193    -15   -149       O  
ATOM  11006  NE2 GLN D 247     110.236  -9.227-220.088  1.00 36.41           N  
ANISOU11006  NE2 GLN D 247     4423   4687   4724    377    -28   -152       N  
ATOM  11007  N   LEU D 248     111.899  -5.788-225.528  1.00 29.11           N  
ANISOU11007  N   LEU D 248     3583   3903   3576    -54    110   -161       N  
ATOM  11008  CA  LEU D 248     112.609  -4.652-226.110  1.00 33.73           C  
ANISOU11008  CA  LEU D 248     4187   4541   4088   -209    128   -149       C  
ATOM  11009  C   LEU D 248     113.612  -4.051-225.129  1.00 33.78           C  
ANISOU11009  C   LEU D 248     4134   4635   4066   -300    117   -149       C  
ATOM  11010  O   LEU D 248     114.683  -3.592-225.545  1.00 33.40           O  
ANISOU11010  O   LEU D 248     4025   4712   3953   -419    144   -151       O  
ATOM  11011  CB  LEU D 248     111.619  -3.596-226.579  1.00 30.50           C  
ANISOU11011  CB  LEU D 248     3937   3987   3664   -269    105   -114       C  
ATOM  11012  CG  LEU D 248     110.698  -4.018-227.715  1.00 33.68           C  
ANISOU11012  CG  LEU D 248     4398   4323   4076   -209    112   -107       C  
ATOM  11013  CD1 LEU D 248     109.893  -2.814-228.118  1.00 31.57           C  
ANISOU11013  CD1 LEU D 248     4282   3929   3783   -275     82    -66       C  
ATOM  11014  CD2 LEU D 248     111.521  -4.597-228.897  1.00 32.70           C  
ANISOU11014  CD2 LEU D 248     4197   4324   3902   -230    166   -129       C  
ATOM  11015  N   VAL D 249     113.313  -4.075-223.834  1.00 29.42           N  
ANISOU11015  N   VAL D 249     3591   4033   3555   -255     77   -149       N  
ATOM  11016  CA  VAL D 249     114.229  -3.580-222.807  1.00 38.29           C  
ANISOU11016  CA  VAL D 249     4659   5241   4650   -339     57   -152       C  
ATOM  11017  C   VAL D 249     114.548  -4.740-221.870  1.00 36.29           C  
ANISOU11017  C   VAL D 249     4286   5061   4440   -213     44   -169       C  
ATOM  11018  O   VAL D 249     113.636  -5.344-221.292  1.00 33.55           O  
ANISOU11018  O   VAL D 249     3980   4617   4152    -96     22   -167       O  
ATOM  11019  CB  VAL D 249     113.645  -2.379-222.040  1.00 38.99           C  
ANISOU11019  CB  VAL D 249     4890   5197   4727   -418     17   -136       C  
ATOM  11020  CG1 VAL D 249     114.655  -1.837-221.013  1.00 32.67           C  
ANISOU11020  CG1 VAL D 249     4040   4490   3884   -527     -7   -142       C  
ATOM  11021  CG2 VAL D 249     113.241  -1.281-223.022  1.00 39.69           C  
ANISOU11021  CG2 VAL D 249     5118   5188   4773   -521     23   -113       C  
ATOM  11022  N   ARG D 250     115.836  -5.074-221.764  1.00 34.04           N  
ANISOU11022  N   ARG D 250     3853   4957   4124   -235     58   -183       N  
ATOM  11023  CA  ARG D 250     116.335  -6.170-220.945  1.00 32.66           C  
ANISOU11023  CA  ARG D 250     3556   4873   3981   -112     41   -196       C  
ATOM  11024  C   ARG D 250     117.708  -5.785-220.425  1.00 37.86           C  
ANISOU11024  C   ARG D 250     4083   5718   4583   -210     31   -199       C  
ATOM  11025  O   ARG D 250     118.482  -5.128-221.122  1.00 33.02           O  
ANISOU11025  O   ARG D 250     3424   5214   3907   -342     61   -200       O  
ATOM  11026  CB  ARG D 250     116.481  -7.486-221.719  1.00 42.86           C  
ANISOU11026  CB  ARG D 250     4769   6215   5299     36     77   -218       C  
ATOM  11027  CG  ARG D 250     115.207  -8.039-222.314  1.00 50.35           C  
ANISOU11027  CG  ARG D 250     5831   7002   6297    129     84   -218       C  
ATOM  11028  CD  ARG D 250     114.706  -9.181-221.483  1.00 48.52           C  
ANISOU11028  CD  ARG D 250     5602   6707   6126    281     52   -217       C  
ATOM  11029  NE  ARG D 250     114.134  -8.695-220.244  1.00 55.39           N  
ANISOU11029  NE  ARG D 250     6534   7497   7015    252      6   -193       N  
ATOM  11030  CZ  ARG D 250     113.743  -9.477-219.247  1.00 61.32           C  
ANISOU11030  CZ  ARG D 250     7291   8203   7806    351    -28   -183       C  
ATOM  11031  NH1 ARG D 250     113.882 -10.793-219.347  1.00 58.98           N  
ANISOU11031  NH1 ARG D 250     6952   7919   7537    485    -28   -192       N  
ATOM  11032  NH2 ARG D 250     113.225  -8.937-218.147  1.00 59.74           N  
ANISOU11032  NH2 ARG D 250     7149   7939   7610    314    -63   -165       N  
ATOM  11033  N   TYR D 251     118.023  -6.235-219.211  1.00 32.15           N  
ANISOU11033  N   TYR D 251     3295   5043   3876   -149    -12   -197       N  
ATOM  11034  CA  TYR D 251     119.337  -5.992-218.645  1.00 33.54           C  
ANISOU11034  CA  TYR D 251     3329   5417   4000   -230    -31   -198       C  
ATOM  11035  C   TYR D 251     120.283  -7.122-219.012  1.00 31.38           C  
ANISOU11035  C   TYR D 251     2871   5323   3728   -102     -7   -216       C  
ATOM  11036  O   TYR D 251     119.883  -8.290-219.061  1.00 40.06           O  
ANISOU11036  O   TYR D 251     3969   6369   4883     82     -4   -224       O  
ATOM  11037  CB  TYR D 251     119.253  -5.864-217.117  1.00 31.29           C  
ANISOU11037  CB  TYR D 251     3064   5106   3720   -232    -97   -186       C  
ATOM  11038  CG  TYR D 251     118.513  -4.634-216.666  1.00 34.39           C  
ANISOU11038  CG  TYR D 251     3628   5347   4094   -365   -120   -178       C  
ATOM  11039  CD1 TYR D 251     118.912  -3.386-217.090  1.00 37.09           C  
ANISOU11039  CD1 TYR D 251     4014   5707   4369   -562   -111   -177       C  
ATOM  11040  CD2 TYR D 251     117.429  -4.721-215.807  1.00 32.28           C  
ANISOU11040  CD2 TYR D 251     3480   4917   3867   -293   -149   -173       C  
ATOM  11041  CE1 TYR D 251     118.258  -2.252-216.698  1.00 40.34           C  
ANISOU11041  CE1 TYR D 251     4601   5966   4759   -671   -133   -174       C  
ATOM  11042  CE2 TYR D 251     116.759  -3.583-215.400  1.00 34.56           C  
ANISOU11042  CE2 TYR D 251     3926   5070   4134   -395   -165   -173       C  
ATOM  11043  CZ  TYR D 251     117.187  -2.344-215.849  1.00 37.18           C  
ANISOU11043  CZ  TYR D 251     4315   5410   4403   -578   -159   -175       C  
ATOM  11044  OH  TYR D 251     116.554  -1.178-215.466  1.00 38.72           O  
ANISOU11044  OH  TYR D 251     4686   5454   4570   -673   -178   -179       O  
ATOM  11045  N   ALA D 252     121.551  -6.773-219.229  1.00 32.32           N  
ANISOU11045  N   ALA D 252     2838   5660   3781   -201      8   -221       N  
ATOM  11046  CA  ALA D 252     122.539  -7.770-219.595  1.00 39.97           C  
ANISOU11046  CA  ALA D 252     3616   6828   4743    -73     35   -242       C  
ATOM  11047  C   ALA D 252     122.776  -8.767-218.461  1.00 49.79           C  
ANISOU11047  C   ALA D 252     4783   8109   6025     97    -22   -236       C  
ATOM  11048  O   ALA D 252     122.712  -8.429-217.277  1.00 44.03           O  
ANISOU11048  O   ALA D 252     4080   7355   5293     48    -85   -214       O  
ATOM  11049  CB  ALA D 252     123.856  -7.096-219.972  1.00 43.71           C  
ANISOU11049  CB  ALA D 252     3926   7554   5129   -231     61   -246       C  
ATOM  11050  N   GLY D 253     123.064 -10.009-218.841  1.00 47.76           N  
ANISOU11050  N   GLY D 253     4441   7909   5798    299      0   -257       N  
ATOM  11051  CA  GLY D 253     123.488 -11.013-217.884  1.00 43.84           C  
ANISOU11051  CA  GLY D 253     3856   7475   5326    472    -54   -249       C  
ATOM  11052  C   GLY D 253     124.814 -11.622-218.291  1.00 45.56           C  
ANISOU11052  C   GLY D 253     3852   7949   5508    576    -28   -273       C  
ATOM  11053  O   GLY D 253     124.882 -12.386-219.261  1.00 41.80           O  
ANISOU11053  O   GLY D 253     3354   7485   5044    712     28   -308       O  
ATOM  11054  N   TYR D 254     125.878 -11.291-217.569  1.00 45.43           N  
ANISOU11054  N   TYR D 254     3669   8150   5442    515    -69   -258       N  
ATOM  11055  CA  TYR D 254     127.230 -11.722-217.919  1.00 55.26           C  
ANISOU11055  CA  TYR D 254     4670   9684   6641    596    -45   -279       C  
ATOM  11056  C   TYR D 254     127.588 -12.980-217.128  1.00 62.64           C  
ANISOU11056  C   TYR D 254     5529  10660   7612    851   -104   -271       C  
ATOM  11057  O   TYR D 254     127.730 -12.930-215.898  1.00 53.68           O  
ANISOU11057  O   TYR D 254     4377   9544   6475    841   -188   -234       O  
ATOM  11058  CB  TYR D 254     128.243 -10.614-217.643  1.00 52.21           C  
ANISOU11058  CB  TYR D 254     4128   9540   6171    368    -59   -264       C  
ATOM  11059  CG  TYR D 254     127.896  -9.261-218.224  1.00 51.74           C  
ANISOU11059  CG  TYR D 254     4171   9419   6067     92    -20   -260       C  
ATOM  11060  CD1 TYR D 254     127.903  -9.051-219.599  1.00 45.81           C  
ANISOU11060  CD1 TYR D 254     3423   8693   5291     42     71   -287       C  
ATOM  11061  CD2 TYR D 254     127.587  -8.182-217.395  1.00 50.29           C  
ANISOU11061  CD2 TYR D 254     4093   9153   5861   -117    -76   -230       C  
ATOM  11062  CE1 TYR D 254     127.594  -7.811-220.136  1.00 48.76           C  
ANISOU11062  CE1 TYR D 254     3905   9002   5619   -209    100   -275       C  
ATOM  11063  CE2 TYR D 254     127.282  -6.934-217.923  1.00 45.03           C  
ANISOU11063  CE2 TYR D 254     3542   8416   5152   -361    -46   -225       C  
ATOM  11064  CZ  TYR D 254     127.288  -6.757-219.297  1.00 51.32           C  
ANISOU11064  CZ  TYR D 254     4341   9232   5925   -406     40   -244       C  
ATOM  11065  OH  TYR D 254     126.989  -5.526-219.833  1.00 48.89           O  
ANISOU11065  OH  TYR D 254     4161   8844   5570   -645     64   -231       O  
ATOM  11066  N   ARG D 255     127.743 -14.102-217.835  1.00 61.20           N  
ANISOU11066  N   ARG D 255     5311  10487   7454   1080    -61   -307       N  
ATOM  11067  CA  ARG D 255     128.296 -15.307-217.227  1.00 68.05           C  
ANISOU11067  CA  ARG D 255     6088  11426   8344   1339   -113   -303       C  
ATOM  11068  C   ARG D 255     129.668 -14.998-216.660  1.00 70.49           C  
ANISOU11068  C   ARG D 255     6202  11995   8588   1278   -147   -282       C  
ATOM  11069  O   ARG D 255     130.575 -14.602-217.395  1.00 68.66           O  
ANISOU11069  O   ARG D 255     5835  11959   8295   1197    -88   -306       O  
ATOM  11070  CB  ARG D 255     128.403 -16.438-218.247  1.00 80.57           C  
ANISOU11070  CB  ARG D 255     7714  12951   9948   1550    -49   -350       C  
ATOM  11071  CG  ARG D 255     127.105 -17.146-218.553  1.00 87.79           C  
ANISOU11071  CG  ARG D 255     8840  13584  10932   1671    -41   -364       C  
ATOM  11072  CD  ARG D 255     126.584 -17.958-217.376  1.00 95.13           C  
ANISOU11072  CD  ARG D 255     9900  14331  11914   1796   -134   -318       C  
ATOM  11073  NE  ARG D 255     127.045 -19.343-217.415  1.00103.92           N  
ANISOU11073  NE  ARG D 255    11067  15376  13043   2013   -145   -327       N  
ATOM  11074  CZ  ARG D 255     127.983 -19.844-216.618  1.00109.24           C  
ANISOU11074  CZ  ARG D 255    11661  16145  13700   2101   -201   -298       C  
ATOM  11075  NH1 ARG D 255     128.559 -19.072-215.707  1.00113.41           N  
ANISOU11075  NH1 ARG D 255    12055  16843  14194   1985   -254   -259       N  
ATOM  11076  NH2 ARG D 255     128.342 -21.118-216.729  1.00106.58           N  
ANISOU11076  NH2 ARG D 255    11385  15733  13378   2302   -208   -310       N  
ATOM  11077  N   GLN D 256     129.812 -15.159-215.356  1.00 71.86           N  
ANISOU11077  N   GLN D 256     6374  12162   8766   1303   -243   -236       N  
ATOM  11078  CA  GLN D 256     131.097 -14.968-214.710  1.00 85.02           C  
ANISOU11078  CA  GLN D 256     7877  14054  10371   1257   -286   -212       C  
ATOM  11079  C   GLN D 256     131.891 -16.268-214.744  1.00 96.40           C  
ANISOU11079  C   GLN D 256     9281  15523  11822   1509   -290   -219       C  
ATOM  11080  O   GLN D 256     131.355 -17.350-214.998  1.00 93.82           O  
ANISOU11080  O   GLN D 256     9086  15007  11553   1712   -281   -233       O  
ATOM  11081  CB  GLN D 256     130.911 -14.489-213.269  1.00 81.60           C  
ANISOU11081  CB  GLN D 256     7462  13613   9930   1154   -391   -159       C  
ATOM  11082  CG  GLN D 256     130.317 -13.092-213.166  1.00 81.60           C  
ANISOU11082  CG  GLN D 256     7484  13618   9903    878   -396   -155       C  
ATOM  11083  CD  GLN D 256     131.237 -12.030-213.748  1.00 83.61           C  
ANISOU11083  CD  GLN D 256     7594  14098  10076    648   -349   -170       C  
ATOM  11084  OE1 GLN D 256     132.450 -12.068-213.546  1.00 88.19           O  
ANISOU11084  OE1 GLN D 256     8032  14877  10600    639   -360   -161       O  
ATOM  11085  NE2 GLN D 256     130.663 -11.082-214.480  1.00 79.78           N  
ANISOU11085  NE2 GLN D 256     7173  13560   9580    452   -292   -188       N  
ATOM  11086  N   GLN D 257     133.194 -16.150-214.494  1.00107.07           N  
ANISOU11086  N   GLN D 257    10456  17114  13111   1487   -305   -210       N  
ATOM  11087  CA  GLN D 257     134.024 -17.344-214.532  1.00111.13           C  
ANISOU11087  CA  GLN D 257    10921  17677  13629   1728   -309   -219       C  
ATOM  11088  C   GLN D 257     133.838 -18.220-213.301  1.00116.87           C  
ANISOU11088  C   GLN D 257    11735  18274  14397   1885   -409   -172       C  
ATOM  11089  O   GLN D 257     134.171 -19.409-213.350  1.00119.48           O  
ANISOU11089  O   GLN D 257    12094  18553  14751   2114   -417   -178       O  
ATOM  11090  CB  GLN D 257     135.492 -16.968-214.711  1.00106.28           C  
ANISOU11090  CB  GLN D 257    10079  17374  12930   1666   -290   -226       C  
ATOM  11091  CG  GLN D 257     135.965 -17.057-216.163  1.00100.34           C  
ANISOU11091  CG  GLN D 257     9253  16728  12144   1696   -180   -285       C  
ATOM  11092  CD  GLN D 257     136.020 -18.490-216.696  1.00 93.15           C  
ANISOU11092  CD  GLN D 257     8410  15709  11275   1991   -152   -321       C  
ATOM  11093  OE1 GLN D 257     135.097 -19.282-216.509  1.00 92.24           O  
ANISOU11093  OE1 GLN D 257     8479  15335  11232   2131   -177   -318       O  
ATOM  11094  NE2 GLN D 257     137.110 -18.821-217.364  1.00 89.62           N  
ANISOU11094  NE2 GLN D 257     7817  15459  10775   2079   -102   -355       N  
ATOM  11095  N   ASP D 258     133.287 -17.674-212.214  1.00118.65           N  
ANISOU11095  N   ASP D 258    12016  18437  14629   1764   -486   -124       N  
ATOM  11096  CA  ASP D 258     132.906 -18.467-211.045  1.00113.62           C  
ANISOU11096  CA  ASP D 258    11494  17648  14030   1895   -581    -75       C  
ATOM  11097  C   ASP D 258     131.722 -19.390-211.316  1.00110.89           C  
ANISOU11097  C   ASP D 258    11370  17002  13761   2046   -568    -81       C  
ATOM  11098  O   ASP D 258     131.219 -20.003-210.362  1.00113.24           O  
ANISOU11098  O   ASP D 258    11793  17145  14089   2129   -644    -35       O  
ATOM  11099  CB  ASP D 258     132.562 -17.543-209.876  1.00105.58           C  
ANISOU11099  CB  ASP D 258    10484  16646  12987   1705   -661    -27       C  
ATOM  11100  CG  ASP D 258     133.561 -16.424-209.704  1.00107.19           C  
ANISOU11100  CG  ASP D 258    10496  17123  13108   1495   -667    -26       C  
ATOM  11101  OD1 ASP D 258     134.743 -16.719-209.424  1.00109.80           O  
ANISOU11101  OD1 ASP D 258    10681  17640  13396   1556   -692    -14       O  
ATOM  11102  OD2 ASP D 258     133.165 -15.249-209.862  1.00104.74           O  
ANISOU11102  OD2 ASP D 258    10185  16840  12771   1263   -648    -35       O  
ATOM  11103  N   GLY D 259     131.269 -19.512-212.564  1.00 99.62           N  
ANISOU11103  N   GLY D 259    10001  15493  12359   2074   -478   -134       N  
ATOM  11104  CA  GLY D 259     129.980 -20.100-212.851  1.00 88.91           C  
ANISOU11104  CA  GLY D 259     8862  13852  11067   2150   -464   -141       C  
ATOM  11105  C   GLY D 259     128.801 -19.221-212.496  1.00 84.95           C  
ANISOU11105  C   GLY D 259     8454  13239  10583   1985   -481   -121       C  
ATOM  11106  O   GLY D 259     127.658 -19.613-212.755  1.00 78.81           O  
ANISOU11106  O   GLY D 259     7855  12232   9857   2030   -467   -126       O  
ATOM  11107  N   SER D 260     129.041 -18.045-211.916  1.00 87.57           N  
ANISOU11107  N   SER D 260     8674  13727  10870   1790   -513   -100       N  
ATOM  11108  CA  SER D 260     127.990 -17.143-211.470  1.00 82.53           C  
ANISOU11108  CA  SER D 260     8115  13003  10238   1629   -539    -82       C  
ATOM  11109  C   SER D 260     127.586 -16.207-212.611  1.00 81.32           C  
ANISOU11109  C   SER D 260     7949  12867  10081   1475   -451   -129       C  
ATOM  11110  O   SER D 260     127.946 -16.414-213.774  1.00 77.53           O  
ANISOU11110  O   SER D 260     7413  12446   9600   1527   -371   -175       O  
ATOM  11111  CB  SER D 260     128.456 -16.367-210.239  1.00 69.19           C  
ANISOU11111  CB  SER D 260     6337  11459   8494   1482   -624    -39       C  
ATOM  11112  OG  SER D 260     129.618 -15.611-210.534  1.00 66.49           O  
ANISOU11112  OG  SER D 260     5803  11373   8089   1348   -599    -57       O  
ATOM  11113  N   VAL D 261     126.823 -15.164-212.286  1.00 72.26           N  
ANISOU11113  N   VAL D 261     6927  11600   8928   1247   -452   -116       N  
ATOM  11114  CA  VAL D 261     126.319 -14.214-213.275  1.00 55.31           C  
ANISOU11114  CA  VAL D 261     4850   9386   6777   1062   -369   -149       C  
ATOM  11115  C   VAL D 261     126.284 -12.831-212.642  1.00 58.65           C  
ANISOU11115  C   VAL D 261     5293   9840   7152    796   -397   -131       C  
ATOM  11116  O   VAL D 261     125.877 -12.676-211.487  1.00 58.40           O  
ANISOU11116  O   VAL D 261     5347   9725   7119    756   -465    -97       O  
ATOM  11117  CB  VAL D 261     124.916 -14.613-213.790  1.00 52.57           C  
ANISOU11117  CB  VAL D 261     4734   8744   6498   1113   -329   -159       C  
ATOM  11118  CG1 VAL D 261     124.307 -13.488-214.620  1.00 46.17           C  
ANISOU11118  CG1 VAL D 261     4012   7854   5678    906   -262   -181       C  
ATOM  11119  CG2 VAL D 261     124.973 -15.895-214.621  1.00 53.42           C  
ANISOU11119  CG2 VAL D 261     4839   8816   6642   1350   -292   -188       C  
ATOM  11120  N   ARG D 262     126.713 -11.822-213.398  1.00 58.14           N  
ANISOU11120  N   ARG D 262     5159   9891   7040    610   -343   -154       N  
ATOM  11121  CA  ARG D 262     126.512 -10.428-213.026  1.00 59.58           C  
ANISOU11121  CA  ARG D 262     5414  10048   7177    342   -357   -145       C  
ATOM  11122  C   ARG D 262     125.433  -9.834-213.920  1.00 56.53           C  
ANISOU11122  C   ARG D 262     5214   9446   6818    247   -289   -164       C  
ATOM  11123  O   ARG D 262     125.548  -9.877-215.151  1.00 53.32           O  
ANISOU11123  O   ARG D 262     4776   9072   6412    255   -215   -191       O  
ATOM  11124  CB  ARG D 262     127.801  -9.613-213.137  1.00 60.68           C  
ANISOU11124  CB  ARG D 262     5353  10473   7229    167   -359   -149       C  
ATOM  11125  CG  ARG D 262     127.694  -8.244-212.469  1.00 62.43           C  
ANISOU11125  CG  ARG D 262     5660  10667   7393   -107   -398   -135       C  
ATOM  11126  CD  ARG D 262     129.056  -7.601-212.275  1.00 72.97           C  
ANISOU11126  CD  ARG D 262     6786  12307   8635   -276   -426   -130       C  
ATOM  11127  NE  ARG D 262     129.095  -6.822-211.043  1.00 82.91           N  
ANISOU11127  NE  ARG D 262     8102  13559   9842   -445   -510   -109       N  
ATOM  11128  CZ  ARG D 262     128.911  -5.508-210.974  1.00 83.75           C  
ANISOU11128  CZ  ARG D 262     8329  13600   9894   -710   -512   -114       C  
ATOM  11129  NH1 ARG D 262     128.688  -4.807-212.072  1.00 83.27           N  
ANISOU11129  NH1 ARG D 262     8339  13476   9822   -841   -438   -131       N  
ATOM  11130  NH2 ARG D 262     128.954  -4.894-209.803  1.00 87.48           N  
ANISOU11130  NH2 ARG D 262     8861  14062  10315   -845   -591   -102       N  
ATOM  11131  N   GLY D 263     124.391  -9.286-213.299  1.00 48.37           N  
ANISOU11131  N   GLY D 263     4373   8204   5803    163   -315   -150       N  
ATOM  11132  CA  GLY D 263     123.232  -8.819-214.036  1.00 48.14           C  
ANISOU11132  CA  GLY D 263     4530   7955   5806    107   -262   -163       C  
ATOM  11133  C   GLY D 263     122.083  -9.801-213.950  1.00 46.35           C  
ANISOU11133  C   GLY D 263     4435   7518   5657    288   -261   -157       C  
ATOM  11134  O   GLY D 263     121.926 -10.498-212.940  1.00 41.08           O  
ANISOU11134  O   GLY D 263     3780   6818   5011    398   -317   -134       O  
ATOM  11135  N   ASP D 264     121.271  -9.875-215.004  1.00 33.36           N  
ANISOU11135  N   ASP D 264     2892   5733   4048    312   -202   -174       N  
ATOM  11136  CA  ASP D 264     120.063 -10.684-214.977  1.00 35.16           C  
ANISOU11136  CA  ASP D 264     3259   5756   4344    446   -201   -167       C  
ATOM  11137  C   ASP D 264     120.374 -12.051-215.569  1.00 46.54           C  
ANISOU11137  C   ASP D 264     4633   7232   5818    646   -182   -181       C  
ATOM  11138  O   ASP D 264     120.651 -12.141-216.779  1.00 42.77           O  
ANISOU11138  O   ASP D 264     4113   6804   5334    659   -122   -211       O  
ATOM  11139  CB  ASP D 264     118.947  -9.993-215.767  1.00 33.16           C  
ANISOU11139  CB  ASP D 264     3160   5332   4109    358   -157   -175       C  
ATOM  11140  CG  ASP D 264     117.597 -10.660-215.596  1.00 35.58           C  
ANISOU11140  CG  ASP D 264     3609   5434   4475    461   -163   -164       C  
ATOM  11141  OD1 ASP D 264     117.543 -11.831-215.167  1.00 36.92           O  
ANISOU11141  OD1 ASP D 264     3766   5583   4677    611   -188   -153       O  
ATOM  11142  OD2 ASP D 264     116.576 -10.012-215.911  1.00 37.63           O  
ANISOU11142  OD2 ASP D 264     3996   5555   4748    390   -144   -163       O  
ATOM  11143  N   PRO D 265     120.346 -13.130-214.779  1.00 41.34           N  
ANISOU11143  N   PRO D 265     3973   6545   5188    804   -230   -161       N  
ATOM  11144  CA  PRO D 265     120.653 -14.461-215.338  1.00 37.85           C  
ANISOU11144  CA  PRO D 265     3491   6118   4774   1008   -216   -178       C  
ATOM  11145  C   PRO D 265     119.670 -14.927-216.397  1.00 37.39           C  
ANISOU11145  C   PRO D 265     3563   5888   4757   1057   -164   -201       C  
ATOM  11146  O   PRO D 265     120.009 -15.818-217.186  1.00 45.21           O  
ANISOU11146  O   PRO D 265     4521   6901   5756   1196   -134   -231       O  
ATOM  11147  CB  PRO D 265     120.616 -15.379-214.103  1.00 39.14           C  
ANISOU11147  CB  PRO D 265     3675   6240   4956   1139   -291   -139       C  
ATOM  11148  CG  PRO D 265     120.823 -14.460-212.939  1.00 34.43           C  
ANISOU11148  CG  PRO D 265     3050   5711   4322   1000   -343   -109       C  
ATOM  11149  CD  PRO D 265     120.161 -13.174-213.313  1.00 39.59           C  
ANISOU11149  CD  PRO D 265     3786   6292   4963    803   -303   -122       C  
ATOM  11150  N   ALA D 266     118.464 -14.358-216.454  1.00 37.02           N  
ANISOU11150  N   ALA D 266     3661   5674   4730    952   -155   -190       N  
ATOM  11151  CA  ALA D 266     117.527 -14.757-217.494  1.00 42.89           C  
ANISOU11151  CA  ALA D 266     4519   6272   5506    985   -112   -209       C  
ATOM  11152  C   ALA D 266     118.028 -14.389-218.885  1.00 43.61           C  
ANISOU11152  C   ALA D 266     4550   6452   5566    944    -43   -251       C  
ATOM  11153  O   ALA D 266     117.556 -14.962-219.874  1.00 42.05           O  
ANISOU11153  O   ALA D 266     4419   6173   5386   1005     -7   -276       O  
ATOM  11154  CB  ALA D 266     116.163 -14.117-217.248  1.00 40.21           C  
ANISOU11154  CB  ALA D 266     4326   5765   5188    878   -118   -186       C  
ATOM  11155  N   ASN D 267     118.977 -13.460-218.986  1.00 36.48           N  
ANISOU11155  N   ASN D 267     3527   5721   4614    832    -26   -257       N  
ATOM  11156  CA  ASN D 267     119.375 -12.896-220.271  1.00 42.82           C  
ANISOU11156  CA  ASN D 267     4284   6611   5376    749     41   -288       C  
ATOM  11157  C   ASN D 267     120.805 -13.268-220.653  1.00 47.06           C  
ANISOU11157  C   ASN D 267     4632   7381   5870    818     72   -318       C  
ATOM  11158  O   ASN D 267     121.450 -12.556-221.423  1.00 43.36           O  
ANISOU11158  O   ASN D 267     4078   7050   5345    707    121   -335       O  
ATOM  11159  CB  ASN D 267     119.198 -11.381-220.238  1.00 38.53           C  
ANISOU11159  CB  ASN D 267     3778   6065   4797    531     44   -269       C  
ATOM  11160  CG  ASN D 267     117.772 -10.988-219.938  1.00 36.83           C  
ANISOU11160  CG  ASN D 267     3741   5631   4620    483     20   -244       C  
ATOM  11161  OD1 ASN D 267     116.834 -11.621-220.421  1.00 35.20           O  
ANISOU11161  OD1 ASN D 267     3634   5286   4454    563     31   -249       O  
ATOM  11162  ND2 ASN D 267     117.595  -9.964-219.122  1.00 35.60           N  
ANISOU11162  ND2 ASN D 267     3626   5450   4449    356    -13   -220       N  
ATOM  11163  N   VAL D 268     121.297 -14.396-220.135  1.00 37.86           N  
ANISOU11163  N   VAL D 268     3399   6262   4724   1006     42   -324       N  
ATOM  11164  CA  VAL D 268     122.666 -14.831-220.406  1.00 43.88           C  
ANISOU11164  CA  VAL D 268     3966   7260   5447   1105     67   -353       C  
ATOM  11165  C   VAL D 268     122.856 -15.135-221.891  1.00 46.10           C  
ANISOU11165  C   VAL D 268     4228   7584   5702   1154    153   -408       C  
ATOM  11166  O   VAL D 268     123.857 -14.747-222.508  1.00 41.89           O  
ANISOU11166  O   VAL D 268     3538   7269   5108   1106    206   -433       O  
ATOM  11167  CB  VAL D 268     123.002 -16.056-219.541  1.00 46.14           C  
ANISOU11167  CB  VAL D 268     4218   7549   5766   1325      9   -344       C  
ATOM  11168  CG1 VAL D 268     124.146 -16.821-220.139  1.00 52.25           C  
ANISOU11168  CG1 VAL D 268     4830   8513   6510   1497     47   -390       C  
ATOM  11169  CG2 VAL D 268     123.333 -15.624-218.121  1.00 50.48           C  
ANISOU11169  CG2 VAL D 268     4708   8164   6308   1263    -70   -295       C  
ATOM  11170  N   GLU D 269     121.904 -15.848-222.482  1.00 41.01           N  
ANISOU11170  N   GLU D 269     3742   6743   5096   1242    169   -427       N  
ATOM  11171  CA  GLU D 269     122.085 -16.317-223.852  1.00 47.46           C  
ANISOU11171  CA  GLU D 269     4554   7594   5884   1315    247   -486       C  
ATOM  11172  C   GLU D 269     122.045 -15.152-224.838  1.00 45.60           C  
ANISOU11172  C   GLU D 269     4312   7418   5594   1110    308   -491       C  
ATOM  11173  O   GLU D 269     122.895 -15.055-225.731  1.00 52.22           O  
ANISOU11173  O   GLU D 269     5031   8439   6371   1105    378   -530       O  
ATOM  11174  CB  GLU D 269     121.020 -17.364-224.180  1.00 46.48           C  
ANISOU11174  CB  GLU D 269     4618   7232   5809   1442    237   -503       C  
ATOM  11175  CG  GLU D 269     121.278 -18.146-225.461  1.00 66.35           C  
ANISOU11175  CG  GLU D 269     7141   9773   8294   1567    308   -574       C  
ATOM  11176  CD  GLU D 269     120.365 -19.352-225.602  1.00 78.29           C  
ANISOU11176  CD  GLU D 269     8841  11055   9852   1709    284   -592       C  
ATOM  11177  OE1 GLU D 269     119.469 -19.530-224.747  1.00 82.89           O  
ANISOU11177  OE1 GLU D 269     9543  11462  10489   1692    215   -544       O  
ATOM  11178  OE2 GLU D 269     120.548 -20.123-226.568  1.00 80.48           O  
ANISOU11178  OE2 GLU D 269     9147  11329  10103   1832    334   -656       O  
ATOM  11179  N   ILE D 270     121.071 -14.250-224.682  1.00 38.61           N  
ANISOU11179  N   ILE D 270     3558   6386   4727    941    284   -450       N  
ATOM  11180  CA  ILE D 270     120.972 -13.114-225.593  1.00 40.83           C  
ANISOU11180  CA  ILE D 270     3859   6698   4954    746    332   -446       C  
ATOM  11181  C   ILE D 270     122.143 -12.158-225.389  1.00 44.89           C  
ANISOU11181  C   ILE D 270     4207   7446   5404    602    346   -433       C  
ATOM  11182  O   ILE D 270     122.614 -11.521-226.340  1.00 38.90           O  
ANISOU11182  O   ILE D 270     3397   6808   4576    481    408   -445       O  
ATOM  11183  CB  ILE D 270     119.612 -12.411-225.428  1.00 40.34           C  
ANISOU11183  CB  ILE D 270     3984   6414   4929    626    294   -405       C  
ATOM  11184  CG1 ILE D 270     119.417 -11.353-226.512  1.00 48.63           C  
ANISOU11184  CG1 ILE D 270     5085   7469   5922    450    341   -399       C  
ATOM  11185  CG2 ILE D 270     119.487 -11.777-224.037  1.00 47.01           C  
ANISOU11185  CG2 ILE D 270     4835   7227   5799    550    225   -358       C  
ATOM  11186  CD1 ILE D 270     119.403 -11.934-227.949  1.00 38.67           C  
ANISOU11186  CD1 ILE D 270     3842   6226   4626    512    409   -446       C  
ATOM  11187  N   THR D 271     122.642 -12.050-224.153  1.00 40.18           N  
ANISOU11187  N   THR D 271     3525   6922   4821    602    288   -407       N  
ATOM  11188  CA  THR D 271     123.810 -11.215-223.904  1.00 39.37           C  
ANISOU11188  CA  THR D 271     3252   7058   4651    460    294   -395       C  
ATOM  11189  C   THR D 271     125.022 -11.740-224.669  1.00 46.34           C  
ANISOU11189  C   THR D 271     3935   8196   5476    547    363   -440       C  
ATOM  11190  O   THR D 271     125.784 -10.961-225.251  1.00 44.07           O  
ANISOU11190  O   THR D 271     3537   8097   5109    389    412   -442       O  
ATOM  11191  CB  THR D 271     124.109 -11.156-222.396  1.00 39.17           C  
ANISOU11191  CB  THR D 271     3171   7065   4648    465    211   -361       C  
ATOM  11192  OG1 THR D 271     123.001 -10.564-221.699  1.00 38.15           O  
ANISOU11192  OG1 THR D 271     3223   6713   4560    373    157   -324       O  
ATOM  11193  CG2 THR D 271     125.353 -10.328-222.120  1.00 46.86           C  
ANISOU11193  CG2 THR D 271     3960   8301   5545    308    210   -349       C  
ATOM  11194  N   GLU D 272     125.222 -13.060-224.672  1.00 40.08           N  
ANISOU11194  N   GLU D 272     3097   7416   4717    798    367   -477       N  
ATOM  11195  CA  GLU D 272     126.370 -13.621-225.376  1.00 43.80           C  
ANISOU11195  CA  GLU D 272     3374   8135   5132    915    436   -528       C  
ATOM  11196  C   GLU D 272     126.202 -13.517-226.886  1.00 47.01           C  
ANISOU11196  C   GLU D 272     3828   8546   5489    871    531   -569       C  
ATOM  11197  O   GLU D 272     127.191 -13.373-227.608  1.00 49.71           O  
ANISOU11197  O   GLU D 272     4001   9135   5752    846    605   -601       O  
ATOM  11198  CB  GLU D 272     126.587 -15.074-224.965  1.00 58.00           C  
ANISOU11198  CB  GLU D 272     5139   9919   6979   1214    410   -558       C  
ATOM  11199  CG  GLU D 272     126.996 -15.235-223.510  1.00 75.66           C  
ANISOU11199  CG  GLU D 272     7294  12208   9247   1271    318   -516       C  
ATOM  11200  CD  GLU D 272     127.004 -16.683-223.060  1.00 94.69           C  
ANISOU11200  CD  GLU D 272     9725  14543  11710   1566    279   -535       C  
ATOM  11201  OE1 GLU D 272     126.575 -17.556-223.848  1.00 97.28           O  
ANISOU11201  OE1 GLU D 272    10160  14745  12056   1719    320   -582       O  
ATOM  11202  OE2 GLU D 272     127.436 -16.946-221.915  1.00101.70           O  
ANISOU11202  OE2 GLU D 272    10551  15476  12616   1632    201   -498       O  
ATOM  11203  N   LEU D 273     124.966 -13.581-227.381  1.00 42.84           N  
ANISOU11203  N   LEU D 273     3519   7760   4998    857    531   -569       N  
ATOM  11204  CA  LEU D 273     124.749 -13.363-228.809  1.00 49.15           C  
ANISOU11204  CA  LEU D 273     4376   8559   5741    789    614   -601       C  
ATOM  11205  C   LEU D 273     125.011 -11.912-229.189  1.00 54.04           C  
ANISOU11205  C   LEU D 273     4965   9280   6287    507    640   -562       C  
ATOM  11206  O   LEU D 273     125.538 -11.642-230.272  1.00 57.22           O  
ANISOU11206  O   LEU D 273     5300   9835   6605    435    723   -588       O  
ATOM  11207  CB  LEU D 273     123.330 -13.779-229.200  1.00 45.43           C  
ANISOU11207  CB  LEU D 273     4143   7792   5325    836    594   -604       C  
ATOM  11208  CG  LEU D 273     123.048 -15.281-229.108  1.00 43.62           C  
ANISOU11208  CG  LEU D 273     3973   7451   5151   1099    580   -649       C  
ATOM  11209  CD1 LEU D 273     121.548 -15.537-229.114  1.00 47.75           C  
ANISOU11209  CD1 LEU D 273     4729   7675   5737   1099    534   -631       C  
ATOM  11210  CD2 LEU D 273     123.720 -16.025-230.258  1.00 45.38           C  
ANISOU11210  CD2 LEU D 273     4124   7808   5312   1235    671   -728       C  
ATOM  11211  N   CYS D 274     124.674 -10.966-228.311  1.00 51.68           N  
ANISOU11211  N   CYS D 274     4724   8900   6010    344    572   -502       N  
ATOM  11212  CA  CYS D 274     124.988  -9.567-228.589  1.00 52.81           C  
ANISOU11212  CA  CYS D 274     4854   9131   6078     70    589   -463       C  
ATOM  11213  C   CYS D 274     126.496  -9.346-228.653  1.00 56.38           C  
ANISOU11213  C   CYS D 274     5055   9920   6445      4    635   -475       C  
ATOM  11214  O   CYS D 274     126.995  -8.644-229.543  1.00 51.33           O  
ANISOU11214  O   CYS D 274     4365   9425   5713   -166    700   -472       O  
ATOM  11215  CB  CYS D 274     124.357  -8.660-227.530  1.00 52.53           C  
ANISOU11215  CB  CYS D 274     4940   8935   6084    -70    503   -404       C  
ATOM  11216  SG  CYS D 274     122.567  -8.405-227.734  1.00 48.37           S  
ANISOU11216  SG  CYS D 274     4706   8050   5624    -83    465   -379       S  
ATOM  11217  N   ILE D 275     127.239  -9.938-227.712  1.00 50.64           N  
ANISOU11217  N   ILE D 275     4165   9334   5744    134    599   -484       N  
ATOM  11218  CA  ILE D 275     128.701  -9.834-227.731  1.00 55.75           C  
ANISOU11218  CA  ILE D 275     4542  10330   6310     96    639   -497       C  
ATOM  11219  C   ILE D 275     129.245 -10.394-229.034  1.00 61.30           C  
ANISOU11219  C   ILE D 275     5141  11204   6948    190    749   -557       C  
ATOM  11220  O   ILE D 275     130.015  -9.744-229.752  1.00 63.73           O  
ANISOU11220  O   ILE D 275     5324  11737   7153     22    819   -557       O  
ATOM  11221  CB  ILE D 275     129.320 -10.583-226.536  1.00 55.29           C  
ANISOU11221  CB  ILE D 275     4331  10380   6296    275    575   -500       C  
ATOM  11222  CG1 ILE D 275     128.661 -10.191-225.219  1.00 64.68           C  
ANISOU11222  CG1 ILE D 275     5647  11377   7552    214    466   -448       C  
ATOM  11223  CG2 ILE D 275     130.822 -10.347-226.488  1.00 51.31           C  
ANISOU11223  CG2 ILE D 275     3537  10253   5703    211    605   -505       C  
ATOM  11224  CD1 ILE D 275     128.629  -8.746-224.993  1.00 69.69           C  
ANISOU11224  CD1 ILE D 275     6336  12006   8137    -94    442   -399       C  
ATOM  11225  N   GLN D 276     128.858 -11.631-229.335  1.00 59.17           N  
ANISOU11225  N   GLN D 276     4923  10826   6730    459    767   -610       N  
ATOM  11226  CA  GLN D 276     129.330 -12.349-230.507  1.00 63.10           C  
ANISOU11226  CA  GLN D 276     5338  11465   7171    597    871   -681       C  
ATOM  11227  C   GLN D 276     128.970 -11.634-231.806  1.00 63.35           C  
ANISOU11227  C   GLN D 276     5473  11471   7127    408    946   -681       C  
ATOM  11228  O   GLN D 276     129.619 -11.869-232.832  1.00 66.46           O  
ANISOU11228  O   GLN D 276     5769  12044   7439    437   1039   -729       O  
ATOM  11229  CB  GLN D 276     128.761 -13.769-230.416  1.00 66.06           C  
ANISOU11229  CB  GLN D 276     5817  11655   7630    907    851   -730       C  
ATOM  11230  CG  GLN D 276     128.496 -14.524-231.687  1.00 82.35           C  
ANISOU11230  CG  GLN D 276     7969  13657   9664   1038    931   -800       C  
ATOM  11231  CD  GLN D 276     127.879 -15.877-231.387  1.00 90.82           C  
ANISOU11231  CD  GLN D 276     9181  14501  10825   1314    885   -835       C  
ATOM  11232  OE1 GLN D 276     127.888 -16.332-230.238  1.00 92.15           O  
ANISOU11232  OE1 GLN D 276     9348  14598  11067   1424    799   -807       O  
ATOM  11233  NE2 GLN D 276     127.330 -16.521-232.411  1.00 92.93           N  
ANISOU11233  NE2 GLN D 276     9585  14647  11079   1412    938   -894       N  
ATOM  11234  N   HIS D 277     127.987 -10.732-231.775  1.00 56.43           N  
ANISOU11234  N   HIS D 277     4802  10368   6272    212    900   -625       N  
ATOM  11235  CA  HIS D 277     127.605  -9.940-232.936  1.00 56.01           C  
ANISOU11235  CA  HIS D 277     4863  10274   6144     16    956   -610       C  
ATOM  11236  C   HIS D 277     128.137  -8.512-232.884  1.00 62.46           C  
ANISOU11236  C   HIS D 277     5627  11225   6879   -299    956   -548       C  
ATOM  11237  O   HIS D 277     127.687  -7.667-233.664  1.00 66.88           O  
ANISOU11237  O   HIS D 277     6324  11703   7384   -493    978   -515       O  
ATOM  11238  CB  HIS D 277     126.086  -9.934-233.095  1.00 52.55           C  
ANISOU11238  CB  HIS D 277     4704   9485   5776     24    905   -590       C  
ATOM  11239  CG  HIS D 277     125.558 -11.150-233.783  1.00 58.81           C  
ANISOU11239  CG  HIS D 277     5578  10168   6597    253    939   -655       C  
ATOM  11240  ND1 HIS D 277     125.189 -12.291-233.104  1.00 58.42           N  
ANISOU11240  ND1 HIS D 277     5564   9991   6644    495    890   -685       N  
ATOM  11241  CD2 HIS D 277     125.367 -11.416-235.097  1.00 62.22           C  
ANISOU11241  CD2 HIS D 277     6073  10603   6966    270   1014   -698       C  
ATOM  11242  CE1 HIS D 277     124.781 -13.203-233.968  1.00 60.93           C  
ANISOU11242  CE1 HIS D 277     5968  10225   6956    646    933   -745       C  
ATOM  11243  NE2 HIS D 277     124.879 -12.697-235.184  1.00 62.12           N  
ANISOU11243  NE2 HIS D 277     6134  10456   7011    517   1009   -757       N  
ATOM  11244  N   GLY D 278     129.079  -8.225-231.984  1.00 64.17           N  
ANISOU11244  N   GLY D 278     5658  11642   7083   -358    927   -529       N  
ATOM  11245  CA  GLY D 278     129.849  -6.997-232.042  1.00 63.95           C  
ANISOU11245  CA  GLY D 278     5538  11807   6953   -658    943   -481       C  
ATOM  11246  C   GLY D 278     129.600  -5.996-230.936  1.00 63.49           C  
ANISOU11246  C   GLY D 278     5568  11630   6924   -848    842   -414       C  
ATOM  11247  O   GLY D 278     130.294  -4.975-230.888  1.00 68.28           O  
ANISOU11247  O   GLY D 278     6103  12396   7443  -1110    845   -374       O  
ATOM  11248  N   TRP D 279     128.641  -6.239-230.048  1.00 58.04           N  
ANISOU11248  N   TRP D 279     5036  10671   6347   -736    755   -402       N  
ATOM  11249  CA  TRP D 279     128.379  -5.299-228.968  1.00 61.37           C  
ANISOU11249  CA  TRP D 279     5552  10975   6792   -904    662   -346       C  
ATOM  11250  C   TRP D 279     129.557  -5.251-228.007  1.00 58.84           C  
ANISOU11250  C   TRP D 279     4998  10916   6442   -945    630   -341       C  
ATOM  11251  O   TRP D 279     130.081  -6.291-227.598  1.00 60.32           O  
ANISOU11251  O   TRP D 279     5012  11241   6665   -723    630   -377       O  
ATOM  11252  CB  TRP D 279     127.109  -5.693-228.217  1.00 54.99           C  
ANISOU11252  CB  TRP D 279     4941   9846   6106   -750    585   -341       C  
ATOM  11253  CG  TRP D 279     126.750  -4.750-227.111  1.00 54.52           C  
ANISOU11253  CG  TRP D 279     4996   9650   6068   -903    495   -292       C  
ATOM  11254  CD1 TRP D 279     126.609  -3.396-227.204  1.00 57.25           C  
ANISOU11254  CD1 TRP D 279     5472   9927   6356  -1172    477   -247       C  
ATOM  11255  CD2 TRP D 279     126.466  -5.090-225.743  1.00 53.31           C  
ANISOU11255  CD2 TRP D 279     4857   9404   5995   -794    411   -287       C  
ATOM  11256  NE1 TRP D 279     126.257  -2.873-225.981  1.00 52.63           N  
ANISOU11256  NE1 TRP D 279     4979   9208   5808  -1229    389   -221       N  
ATOM  11257  CE2 TRP D 279     126.162  -3.892-225.069  1.00 52.97           C  
ANISOU11257  CE2 TRP D 279     4949   9242   5935  -1004    349   -244       C  
ATOM  11258  CE3 TRP D 279     126.428  -6.291-225.029  1.00 51.07           C  
ANISOU11258  CE3 TRP D 279     4498   9117   5789   -540    381   -313       C  
ATOM  11259  CZ2 TRP D 279     125.836  -3.859-223.710  1.00 51.30           C  
ANISOU11259  CZ2 TRP D 279     4788   8925   5779   -967    265   -232       C  
ATOM  11260  CZ3 TRP D 279     126.105  -6.260-223.680  1.00 53.24           C  
ANISOU11260  CZ3 TRP D 279     4822   9288   6119   -512    293   -292       C  
ATOM  11261  CH2 TRP D 279     125.817  -5.052-223.034  1.00 48.84           C  
ANISOU11261  CH2 TRP D 279     4389   8629   5540   -725    239   -254       C  
ATOM  11262  N   THR D 280     129.980  -4.045-227.655  1.00 59.67           N  
ANISOU11262  N   THR D 280     5105  11087   6478  -1230    599   -295       N  
ATOM  11263  CA  THR D 280     130.953  -3.885-226.583  1.00 63.09           C  
ANISOU11263  CA  THR D 280     5349  11735   6886  -1296    546   -282       C  
ATOM  11264  C   THR D 280     130.218  -3.939-225.252  1.00 63.91           C  
ANISOU11264  C   THR D 280     5587  11609   7086  -1218    439   -266       C  
ATOM  11265  O   THR D 280     129.430  -3.035-224.947  1.00 66.36           O  
ANISOU11265  O   THR D 280     6124  11681   7407  -1369    390   -233       O  
ATOM  11266  CB  THR D 280     131.713  -2.568-226.710  1.00 67.38           C  
ANISOU11266  CB  THR D 280     5852  12443   7308  -1655    550   -239       C  
ATOM  11267  OG1 THR D 280     132.308  -2.482-228.011  1.00 67.35           O  
ANISOU11267  OG1 THR D 280     5787  12592   7210  -1718    640   -249       O  
ATOM  11268  CG2 THR D 280     132.799  -2.484-225.645  1.00 68.15           C  
ANISOU11268  CG2 THR D 280     5788  12733   7373  -1691    479   -229       C  
ATOM  11269  N   PRO D 281     130.440  -4.969-224.440  1.00 59.42           N  
ANISOU11269  N   PRO D 281     4894  11101   6582   -981    401   -288       N  
ATOM  11270  CA  PRO D 281     129.645  -5.131-223.218  1.00 61.24           C  
ANISOU11270  CA  PRO D 281     5264  11101   6902   -889    306   -274       C  
ATOM  11271  C   PRO D 281     130.049  -4.140-222.140  1.00 69.13           C  
ANISOU11271  C   PRO D 281     6258  12150   7856  -1114    227   -237       C  
ATOM  11272  O   PRO D 281     131.094  -3.489-222.190  1.00 70.46           O  
ANISOU11272  O   PRO D 281     6275  12569   7929  -1321    234   -223       O  
ATOM  11273  CB  PRO D 281     129.955  -6.564-222.781  1.00 57.61           C  
ANISOU11273  CB  PRO D 281     4652  10734   6505   -578    295   -305       C  
ATOM  11274  CG  PRO D 281     131.322  -6.819-223.316  1.00 60.37           C  
ANISOU11274  CG  PRO D 281     4714  11450   6774   -574    355   -327       C  
ATOM  11275  CD  PRO D 281     131.396  -6.075-224.624  1.00 56.72           C  
ANISOU11275  CD  PRO D 281     4285  11034   6232   -770    444   -329       C  
ATOM  11276  N   GLY D 282     129.183  -4.042-221.138  1.00 67.08           N  
ANISOU11276  N   GLY D 282     6173  11650   7663  -1076    150   -223       N  
ATOM  11277  CA  GLY D 282     129.496  -3.379-219.899  1.00 59.04           C  
ANISOU11277  CA  GLY D 282     5154  10662   6615  -1223     63   -198       C  
ATOM  11278  C   GLY D 282     129.909  -4.367-218.831  1.00 65.67           C  
ANISOU11278  C   GLY D 282     5841  11614   7498  -1020      3   -204       C  
ATOM  11279  O   GLY D 282     130.256  -5.521-219.111  1.00 68.73           O  
ANISOU11279  O   GLY D 282     6075  12120   7920   -784     33   -226       O  
ATOM  11280  N   ASN D 283     129.875  -3.906-217.580  1.00 62.14           N  
ANISOU11280  N   ASN D 283     5446  11123   7042  -1110    -86   -184       N  
ATOM  11281  CA  ASN D 283     130.112  -4.810-216.464  1.00 66.78           C  
ANISOU11281  CA  ASN D 283     5927  11776   7670   -918   -155   -180       C  
ATOM  11282  C   ASN D 283     129.206  -4.472-215.286  1.00 63.93           C  
ANISOU11282  C   ASN D 283     5775  11171   7344   -940   -233   -166       C  
ATOM  11283  O   ASN D 283     129.538  -4.770-214.134  1.00 60.77           O  
ANISOU11283  O   ASN D 283     5305  10844   6940   -891   -311   -153       O  
ATOM  11284  CB  ASN D 283     131.588  -4.806-216.044  1.00 72.00           C  
ANISOU11284  CB  ASN D 283     6302  12803   8251   -991   -189   -171       C  
ATOM  11285  CG  ASN D 283     132.058  -3.453-215.533  1.00 79.26           C  
ANISOU11285  CG  ASN D 283     7243  13799   9074  -1327   -238   -150       C  
ATOM  11286  OD1 ASN D 283     131.431  -2.422-215.779  1.00 84.41           O  
ANISOU11286  OD1 ASN D 283     8112  14254   9705  -1526   -227   -145       O  
ATOM  11287  ND2 ASN D 283     133.184  -3.454-214.825  1.00 79.10           N  
ANISOU11287  ND2 ASN D 283     7054  14010   8989  -1371   -289   -134       N  
ATOM  11288  N   GLY D 284     128.052  -3.859-215.564  1.00 53.35           N  
ANISOU11288  N   GLY D 284     4691   9545   6034  -1005   -213   -168       N  
ATOM  11289  CA  GLY D 284     127.102  -3.500-214.537  1.00 51.31           C  
ANISOU11289  CA  GLY D 284     4640   9051   5806  -1018   -273   -160       C  
ATOM  11290  C   GLY D 284     126.016  -4.545-214.365  1.00 58.51           C  
ANISOU11290  C   GLY D 284     5651   9758   6820   -756   -269   -165       C  
ATOM  11291  O   GLY D 284     125.927  -5.531-215.098  1.00 54.34           O  
ANISOU11291  O   GLY D 284     5061   9244   6345   -568   -221   -175       O  
ATOM  11292  N   ARG D 285     125.176  -4.310-213.356  1.00 47.47           N  
ANISOU11292  N   ARG D 285     4420   8172   5445   -753   -320   -158       N  
ATOM  11293  CA  ARG D 285     124.037  -5.173-213.075  1.00 42.85           C  
ANISOU11293  CA  ARG D 285     3951   7383   4948   -541   -321   -157       C  
ATOM  11294  C   ARG D 285     122.787  -4.763-213.835  1.00 38.74           C  
ANISOU11294  C   ARG D 285     3634   6616   4468   -550   -270   -166       C  
ATOM  11295  O   ARG D 285     121.854  -5.572-213.960  1.00 39.66           O  
ANISOU11295  O   ARG D 285     3824   6585   4658   -375   -254   -166       O  
ATOM  11296  CB  ARG D 285     123.717  -5.169-211.569  1.00 44.06           C  
ANISOU11296  CB  ARG D 285     4173   7471   5097   -528   -397   -144       C  
ATOM  11297  CG  ARG D 285     124.891  -5.488-210.667  1.00 56.79           C  
ANISOU11297  CG  ARG D 285     5598   9319   6659   -531   -465   -129       C  
ATOM  11298  CD  ARG D 285     124.485  -6.453-209.544  1.00 62.39           C  
ANISOU11298  CD  ARG D 285     6329   9970   7408   -349   -522   -109       C  
ATOM  11299  NE  ARG D 285     123.520  -5.917-208.589  1.00 64.42           N  
ANISOU11299  NE  ARG D 285     6782  10035   7660   -407   -553   -108       N  
ATOM  11300  CZ  ARG D 285     122.799  -6.662-207.744  1.00 71.15           C  
ANISOU11300  CZ  ARG D 285     7709  10776   8550   -262   -583    -91       C  
ATOM  11301  NH1 ARG D 285     122.905  -7.987-207.742  1.00 67.70           N  
ANISOU11301  NH1 ARG D 285     7186  10376   8162    -54   -592    -68       N  
ATOM  11302  NH2 ARG D 285     121.956  -6.085-206.900  1.00 70.41           N  
ANISOU11302  NH2 ARG D 285     7784  10529   8439   -326   -602    -96       N  
ATOM  11303  N   PHE D 286     122.738  -3.533-214.335  1.00 39.02           N  
ANISOU11303  N   PHE D 286     3767   6604   4455   -751   -250   -170       N  
ATOM  11304  CA  PHE D 286     121.563  -3.027-215.029  1.00 46.04           C  
ANISOU11304  CA  PHE D 286     4854   7263   5375   -763   -211   -174       C  
ATOM  11305  C   PHE D 286     121.956  -2.352-216.343  1.00 51.46           C  
ANISOU11305  C   PHE D 286     5537   7999   6017   -904   -158   -174       C  
ATOM  11306  O   PHE D 286     121.577  -1.213-216.626  1.00 47.72           O  
ANISOU11306  O   PHE D 286     5221   7403   5506  -1061   -154   -170       O  
ATOM  11307  CB  PHE D 286     120.791  -2.095-214.106  1.00 40.92           C  
ANISOU11307  CB  PHE D 286     4399   6435   4712   -850   -253   -176       C  
ATOM  11308  CG  PHE D 286     120.401  -2.737-212.806  1.00 44.35           C  
ANISOU11308  CG  PHE D 286     4839   6831   5178   -723   -301   -174       C  
ATOM  11309  CD1 PHE D 286     119.276  -3.542-212.724  1.00 45.81           C  
ANISOU11309  CD1 PHE D 286     5095   6868   5441   -538   -288   -171       C  
ATOM  11310  CD2 PHE D 286     121.168  -2.552-211.670  1.00 44.25           C  
ANISOU11310  CD2 PHE D 286     4760   6942   5111   -800   -362   -173       C  
ATOM  11311  CE1 PHE D 286     118.915  -4.149-211.520  1.00 46.64           C  
ANISOU11311  CE1 PHE D 286     5210   6943   5566   -434   -330   -164       C  
ATOM  11312  CE2 PHE D 286     120.818  -3.155-210.464  1.00 40.22           C  
ANISOU11312  CE2 PHE D 286     4260   6400   4621   -688   -408   -167       C  
ATOM  11313  CZ  PHE D 286     119.693  -3.953-210.389  1.00 41.92           C  
ANISOU11313  CZ  PHE D 286     4552   6464   4912   -506   -390   -161       C  
ATOM  11314  N   ASP D 287     122.716  -3.071-217.173  1.00 50.22           N  
ANISOU11314  N   ASP D 287     5204   8020   5856   -843   -113   -179       N  
ATOM  11315  CA  ASP D 287     123.122  -2.592-218.493  1.00 50.19           C  
ANISOU11315  CA  ASP D 287     5177   8088   5804   -962    -53   -179       C  
ATOM  11316  C   ASP D 287     122.054  -2.966-219.517  1.00 49.06           C  
ANISOU11316  C   ASP D 287     5152   7769   5719   -843     -3   -184       C  
ATOM  11317  O   ASP D 287     121.797  -4.155-219.747  1.00 41.60           O  
ANISOU11317  O   ASP D 287     4148   6822   4834   -638     18   -198       O  
ATOM  11318  CB  ASP D 287     124.467  -3.191-218.912  1.00 55.27           C  
ANISOU11318  CB  ASP D 287     5563   9028   6407   -947    -21   -188       C  
ATOM  11319  CG  ASP D 287     125.620  -2.734-218.036  1.00 60.98           C  
ANISOU11319  CG  ASP D 287     6148   9964   7060  -1095    -71   -179       C  
ATOM  11320  OD1 ASP D 287     125.493  -1.676-217.384  1.00 57.45           O  
ANISOU11320  OD1 ASP D 287     5824   9435   6571  -1278   -118   -167       O  
ATOM  11321  OD2 ASP D 287     126.661  -3.433-218.015  1.00 55.01           O  
ANISOU11321  OD2 ASP D 287     5158   9460   6285  -1025    -65   -186       O  
ATOM  11322  N   VAL D 288     121.440  -1.959-220.137  1.00 44.22           N  
ANISOU11322  N   VAL D 288     4713   7007   5081   -973     11   -171       N  
ATOM  11323  CA  VAL D 288     120.426  -2.240-221.148  1.00 44.26           C  
ANISOU11323  CA  VAL D 288     4829   6856   5131   -874     51   -171       C  
ATOM  11324  C   VAL D 288     121.084  -2.897-222.353  1.00 40.76           C  
ANISOU11324  C   VAL D 288     4245   6576   4666   -834    119   -185       C  
ATOM  11325  O   VAL D 288     122.130  -2.447-222.840  1.00 40.52           O  
ANISOU11325  O   VAL D 288     4111   6729   4557   -983    148   -182       O  
ATOM  11326  CB  VAL D 288     119.674  -0.959-221.539  1.00 42.60           C  
ANISOU11326  CB  VAL D 288     4836   6457   4891  -1019     44   -150       C  
ATOM  11327  CG1 VAL D 288     118.608  -1.281-222.577  1.00 33.80           C  
ANISOU11327  CG1 VAL D 288     3825   5196   3821   -910     77   -146       C  
ATOM  11328  CG2 VAL D 288     119.048  -0.314-220.291  1.00 41.54           C  
ANISOU11328  CG2 VAL D 288     4843   6168   4773  -1042    -18   -147       C  
ATOM  11329  N   LEU D 289     120.483  -3.975-222.829  1.00 43.92           N  
ANISOU11329  N   LEU D 289     4642   6916   5129   -638    145   -202       N  
ATOM  11330  CA  LEU D 289     120.983  -4.694-223.984  1.00 44.33           C  
ANISOU11330  CA  LEU D 289     4582   7099   5162   -572    212   -225       C  
ATOM  11331  C   LEU D 289     120.653  -3.959-225.279  1.00 40.21           C  
ANISOU11331  C   LEU D 289     4170   6519   4590   -695    256   -212       C  
ATOM  11332  O   LEU D 289     119.639  -3.263-225.365  1.00 36.83           O  
ANISOU11332  O   LEU D 289     3929   5888   4176   -747    231   -187       O  
ATOM  11333  CB  LEU D 289     120.374  -6.083-224.038  1.00 46.80           C  
ANISOU11333  CB  LEU D 289     4889   7338   5553   -328    217   -250       C  
ATOM  11334  CG  LEU D 289     120.912  -7.099-223.037  1.00 36.52           C  
ANISOU11334  CG  LEU D 289     3453   6133   4291   -173    187   -265       C  
ATOM  11335  CD1 LEU D 289     120.090  -8.351-223.199  1.00 35.10           C  
ANISOU11335  CD1 LEU D 289     3329   5824   4185     41    189   -283       C  
ATOM  11336  CD2 LEU D 289     122.362  -7.347-223.380  1.00 35.03           C  
ANISOU11336  CD2 LEU D 289     3048   6220   4041   -182    227   -286       C  
ATOM  11337  N   PRO D 290     121.487  -4.112-226.301  1.00 40.71           N  
ANISOU11337  N   PRO D 290     4117   6761   4589   -737    322   -226       N  
ATOM  11338  CA  PRO D 290     121.107  -3.651-227.640  1.00 40.41           C  
ANISOU11338  CA  PRO D 290     4183   6667   4503   -822    368   -215       C  
ATOM  11339  C   PRO D 290     120.096  -4.611-228.250  1.00 43.56           C  
ANISOU11339  C   PRO D 290     4659   6928   4965   -631    383   -237       C  
ATOM  11340  O   PRO D 290     119.863  -5.714-227.748  1.00 42.61           O  
ANISOU11340  O   PRO D 290     4492   6784   4917   -438    369   -265       O  
ATOM  11341  CB  PRO D 290     122.437  -3.651-228.403  1.00 41.12           C  
ANISOU11341  CB  PRO D 290     4093   7032   4498   -915    439   -230       C  
ATOM  11342  CG  PRO D 290     123.193  -4.778-227.768  1.00 45.90           C  
ANISOU11342  CG  PRO D 290     4494   7806   5139   -742    443   -270       C  
ATOM  11343  CD  PRO D 290     122.809  -4.762-226.298  1.00 43.79           C  
ANISOU11343  CD  PRO D 290     4269   7426   4943   -694    359   -255       C  
ATOM  11344  N   LEU D 291     119.482  -4.178-229.352  1.00 38.00           N  
ANISOU11344  N   LEU D 291     4083   6128   4228   -695    406   -221       N  
ATOM  11345  CA  LEU D 291     118.538  -5.026-230.069  1.00 40.35           C  
ANISOU11345  CA  LEU D 291     4456   6307   4569   -542    419   -241       C  
ATOM  11346  C   LEU D 291     119.247  -5.766-231.191  1.00 41.20           C  
ANISOU11346  C   LEU D 291     4451   6583   4621   -493    499   -283       C  
ATOM  11347  O   LEU D 291     120.062  -5.184-231.913  1.00 38.86           O  
ANISOU11347  O   LEU D 291     4098   6438   4230   -639    550   -277       O  
ATOM  11348  CB  LEU D 291     117.385  -4.201-230.639  1.00 42.27           C  
ANISOU11348  CB  LEU D 291     4904   6351   4807   -619    391   -199       C  
ATOM  11349  CG  LEU D 291     116.522  -3.454-229.630  1.00 47.78           C  
ANISOU11349  CG  LEU D 291     5733   6863   5557   -644    317   -162       C  
ATOM  11350  CD1 LEU D 291     115.442  -2.659-230.325  1.00 44.62           C  
ANISOU11350  CD1 LEU D 291     5524   6286   5144   -700    293   -122       C  
ATOM  11351  CD2 LEU D 291     115.917  -4.432-228.631  1.00 53.24           C  
ANISOU11351  CD2 LEU D 291     6402   7479   6348   -459    280   -184       C  
ATOM  11352  N   LEU D 292     118.951  -7.061-231.318  1.00 34.66           N  
ANISOU11352  N   LEU D 292     3595   5729   3843   -291    511   -328       N  
ATOM  11353  CA  LEU D 292     119.386  -7.863-232.459  1.00 40.07           C  
ANISOU11353  CA  LEU D 292     4215   6531   4480   -213    586   -379       C  
ATOM  11354  C   LEU D 292     118.164  -8.059-233.336  1.00 37.65           C  
ANISOU11354  C   LEU D 292     4078   6042   4183   -181    579   -377       C  
ATOM  11355  O   LEU D 292     117.220  -8.749-232.937  1.00 37.47           O  
ANISOU11355  O   LEU D 292     4136   5858   4241    -52    533   -383       O  
ATOM  11356  CB  LEU D 292     119.976  -9.200-232.022  1.00 41.28           C  
ANISOU11356  CB  LEU D 292     4231   6782   4673     -5    603   -437       C  
ATOM  11357  CG  LEU D 292     121.467  -9.180-231.691  1.00 46.75           C  
ANISOU11357  CG  LEU D 292     4707   7740   5316    -22    642   -455       C  
ATOM  11358  CD1 LEU D 292     121.859 -10.531-231.144  1.00 47.48           C  
ANISOU11358  CD1 LEU D 292     4695   7885   5462    217    639   -506       C  
ATOM  11359  CD2 LEU D 292     122.288  -8.832-232.928  1.00 49.37           C  
ANISOU11359  CD2 LEU D 292     4955   8269   5532   -128    733   -475       C  
ATOM  11360  N   LEU D 293     118.172  -7.430-234.515  1.00 40.75           N  
ANISOU11360  N   LEU D 293     4528   6466   4490   -309    619   -362       N  
ATOM  11361  CA  LEU D 293     117.007  -7.375-235.384  1.00 38.86           C  
ANISOU11361  CA  LEU D 293     4456   6061   4246   -314    601   -346       C  
ATOM  11362  C   LEU D 293     117.302  -8.124-236.672  1.00 39.04           C  
ANISOU11362  C   LEU D 293     4455   6181   4198   -260    676   -401       C  
ATOM  11363  O   LEU D 293     118.347  -7.909-237.306  1.00 38.55           O  
ANISOU11363  O   LEU D 293     4291   6314   4042   -338    750   -419       O  
ATOM  11364  CB  LEU D 293     116.614  -5.928-235.690  1.00 44.44           C  
ANISOU11364  CB  LEU D 293     5289   6691   4905   -510    572   -274       C  
ATOM  11365  CG  LEU D 293     116.298  -5.064-234.470  1.00 43.14           C  
ANISOU11365  CG  LEU D 293     5174   6419   4798   -571    501   -225       C  
ATOM  11366  CD1 LEU D 293     115.859  -3.691-234.919  1.00 38.83           C  
ANISOU11366  CD1 LEU D 293     4780   5775   4198   -746    472   -158       C  
ATOM  11367  CD2 LEU D 293     115.235  -5.721-233.580  1.00 36.70           C  
ANISOU11367  CD2 LEU D 293     4411   5437   4097   -412    438   -231       C  
ATOM  11368  N   GLN D 294     116.373  -8.986-237.062  1.00 40.83           N  
ANISOU11368  N   GLN D 294     4775   6276   4461   -137    657   -428       N  
ATOM  11369  CA  GLN D 294     116.556  -9.884-238.197  1.00 37.91           C  
ANISOU11369  CA  GLN D 294     4401   5973   4031    -57    721   -494       C  
ATOM  11370  C   GLN D 294     115.562  -9.505-239.286  1.00 35.94           C  
ANISOU11370  C   GLN D 294     4314   5610   3734   -139    703   -465       C  
ATOM  11371  O   GLN D 294     114.345  -9.601-239.086  1.00 36.92           O  
ANISOU11371  O   GLN D 294     4559   5549   3921   -106    630   -438       O  
ATOM  11372  CB  GLN D 294     116.362 -11.331-237.752  1.00 44.07           C  
ANISOU11372  CB  GLN D 294     5165   6695   4884    157    710   -557       C  
ATOM  11373  CG  GLN D 294     116.483 -12.377-238.843  1.00 48.91           C  
ANISOU11373  CG  GLN D 294     5797   7346   5439    262    770   -636       C  
ATOM  11374  CD  GLN D 294     116.107 -13.763-238.330  1.00 49.04           C  
ANISOU11374  CD  GLN D 294     5845   7254   5535    463    740   -688       C  
ATOM  11375  OE1 GLN D 294     116.875 -14.393-237.622  1.00 48.46           O  
ANISOU11375  OE1 GLN D 294     5662   7256   5495    589    755   -724       O  
ATOM  11376  NE2 GLN D 294     114.917 -14.232-238.687  1.00 55.71           N  
ANISOU11376  NE2 GLN D 294     6843   7921   6403    487    693   -689       N  
ATOM  11377  N   ALA D 295     116.078  -9.049-240.417  1.00 36.37           N  
ANISOU11377  N   ALA D 295     4365   5785   3670   -251    767   -467       N  
ATOM  11378  CA  ALA D 295     115.261  -8.899-241.610  1.00 40.12           C  
ANISOU11378  CA  ALA D 295     4984   6179   4081   -308    759   -451       C  
ATOM  11379  C   ALA D 295     115.293 -10.198-242.411  1.00 43.05           C  
ANISOU11379  C   ALA D 295     5355   6584   4416   -172    810   -542       C  
ATOM  11380  O   ALA D 295     116.185 -11.032-242.217  1.00 43.80           O  
ANISOU11380  O   ALA D 295     5329   6802   4512    -54    871   -615       O  
ATOM  11381  CB  ALA D 295     115.776  -7.727-242.454  1.00 36.77           C  
ANISOU11381  CB  ALA D 295     4576   5861   3535   -511    799   -402       C  
ATOM  11382  N   PRO D 296     114.326 -10.414-243.309  1.00 45.63           N  
ANISOU11382  N   PRO D 296     5824   6802   4710   -179    782   -541       N  
ATOM  11383  CA  PRO D 296     114.269 -11.685-244.045  1.00 43.31           C  
ANISOU11383  CA  PRO D 296     5558   6516   4380    -52    821   -632       C  
ATOM  11384  C   PRO D 296     115.591 -12.056-244.707  1.00 41.55           C  
ANISOU11384  C   PRO D 296     5219   6513   4055    -24    941   -709       C  
ATOM  11385  O   PRO D 296     116.186 -11.263-245.446  1.00 42.51           O  
ANISOU11385  O   PRO D 296     5310   6775   4067   -163   1000   -687       O  
ATOM  11386  CB  PRO D 296     113.178 -11.428-245.086  1.00 47.59           C  
ANISOU11386  CB  PRO D 296     6264   6952   4865   -135    777   -599       C  
ATOM  11387  CG  PRO D 296     112.262 -10.502-244.418  1.00 47.30           C  
ANISOU11387  CG  PRO D 296     6292   6776   4905   -211    679   -501       C  
ATOM  11388  CD  PRO D 296     113.155  -9.573-243.610  1.00 40.20           C  
ANISOU11388  CD  PRO D 296     5284   5966   4023   -286    701   -458       C  
ATOM  11389  N   ASP D 297     116.061 -13.275-244.401  1.00 44.69           N  
ANISOU11389  N   ASP D 297     5550   6944   4486    163    978   -799       N  
ATOM  11390  CA  ASP D 297     117.187 -13.925-245.076  1.00 47.22           C  
ANISOU11390  CA  ASP D 297     5770   7459   4712    248   1092   -895       C  
ATOM  11391  C   ASP D 297     118.501 -13.187-244.859  1.00 54.94           C  
ANISOU11391  C   ASP D 297     6559   8675   5640    171   1166   -878       C  
ATOM  11392  O   ASP D 297     119.396 -13.224-245.704  1.00 55.82           O  
ANISOU11392  O   ASP D 297     6587   8989   5634    155   1270   -929       O  
ATOM  11393  CB  ASP D 297     116.892 -14.106-246.574  1.00 46.18           C  
ANISOU11393  CB  ASP D 297     5753   7342   4452    202   1138   -936       C  
ATOM  11394  CG  ASP D 297     115.546 -14.755-246.798  1.00 50.27           C  
ANISOU11394  CG  ASP D 297     6457   7631   5011    248   1054   -944       C  
ATOM  11395  OD1 ASP D 297     115.378 -15.906-246.337  1.00 53.43           O  
ANISOU11395  OD1 ASP D 297     6882   7938   5480    420   1035  -1008       O  
ATOM  11396  OD2 ASP D 297     114.648 -14.104-247.372  1.00 53.22           O  
ANISOU11396  OD2 ASP D 297     6952   7916   5351    111   1000   -880       O  
ATOM  11397  N   GLU D 298     118.617 -12.522-243.719  1.00 48.87           N  
ANISOU11397  N   GLU D 298     5720   7891   4956    117   1113   -809       N  
ATOM  11398  CA  GLU D 298     119.800 -11.793-243.302  1.00 51.73           C  
ANISOU11398  CA  GLU D 298     5903   8466   5286     28   1161   -784       C  
ATOM  11399  C   GLU D 298     120.167 -12.229-241.892  1.00 53.19           C  
ANISOU11399  C   GLU D 298     5974   8649   5587    160   1122   -791       C  
ATOM  11400  O   GLU D 298     119.283 -12.562-241.100  1.00 47.07           O  
ANISOU11400  O   GLU D 298     5291   7668   4924    236   1033   -770       O  
ATOM  11401  CB  GLU D 298     119.546 -10.277-243.312  1.00 54.87           C  
ANISOU11401  CB  GLU D 298     6356   8838   5654   -222   1122   -676       C  
ATOM  11402  CG  GLU D 298     119.162  -9.694-244.665  1.00 61.75           C  
ANISOU11402  CG  GLU D 298     7352   9705   6405   -373   1148   -649       C  
ATOM  11403  CD  GLU D 298     120.370  -9.291-245.494  1.00 74.24           C  
ANISOU11403  CD  GLU D 298     8810  11559   7839   -491   1263   -667       C  
ATOM  11404  OE1 GLU D 298     120.184  -8.772-246.619  1.00 79.80           O  
ANISOU11404  OE1 GLU D 298     9609  12284   8428   -631   1292   -641       O  
ATOM  11405  OE2 GLU D 298     121.508  -9.489-245.017  1.00 75.31           O  
ANISOU11405  OE2 GLU D 298     8750  11897   7969   -447   1323   -703       O  
ATOM  11406  N   PRO D 299     121.453 -12.250-241.552  1.00 51.15           N  
ANISOU11406  N   PRO D 299     5512   8625   5299    188   1185   -818       N  
ATOM  11407  CA  PRO D 299     121.835 -12.406-240.148  1.00 47.42           C  
ANISOU11407  CA  PRO D 299     4927   8163   4927    272   1134   -803       C  
ATOM  11408  C   PRO D 299     121.346 -11.219-239.337  1.00 47.65           C  
ANISOU11408  C   PRO D 299     5011   8085   5010     90   1050   -701       C  
ATOM  11409  O   PRO D 299     121.045 -10.150-239.892  1.00 45.46           O  
ANISOU11409  O   PRO D 299     4816   7783   4672   -113   1047   -642       O  
ATOM  11410  CB  PRO D 299     123.371 -12.469-240.192  1.00 52.26           C  
ANISOU11410  CB  PRO D 299     5297   9093   5465    297   1227   -846       C  
ATOM  11411  CG  PRO D 299     123.753 -11.932-241.524  1.00 51.42           C  
ANISOU11411  CG  PRO D 299     5180   9143   5215    149   1320   -855       C  
ATOM  11412  CD  PRO D 299     122.621 -12.254-242.448  1.00 56.68           C  
ANISOU11412  CD  PRO D 299     6066   9604   5867    164   1306   -871       C  
ATOM  11413  N   PRO D 300     121.216 -11.369-238.025  1.00 50.06           N  
ANISOU11413  N   PRO D 300     5288   8309   5422    162    977   -678       N  
ATOM  11414  CA  PRO D 300     120.705 -10.260-237.218  1.00 50.80           C  
ANISOU11414  CA  PRO D 300     5449   8288   5565      3    897   -590       C  
ATOM  11415  C   PRO D 300     121.659  -9.078-237.234  1.00 45.77           C  
ANISOU11415  C   PRO D 300     4703   7841   4845   -209    930   -547       C  
ATOM  11416  O   PRO D 300     122.872  -9.227-237.409  1.00 45.71           O  
ANISOU11416  O   PRO D 300     4510   8086   4771   -206   1002   -583       O  
ATOM  11417  CB  PRO D 300     120.580 -10.864-235.814  1.00 48.33           C  
ANISOU11417  CB  PRO D 300     5101   7895   5369    149    828   -591       C  
ATOM  11418  CG  PRO D 300     121.554 -11.994-235.807  1.00 47.79           C  
ANISOU11418  CG  PRO D 300     4876   7994   5290    341    884   -668       C  
ATOM  11419  CD  PRO D 300     121.519 -12.556-237.210  1.00 49.80           C  
ANISOU11419  CD  PRO D 300     5176   8281   5467    395    962   -731       C  
ATOM  11420  N   GLU D 301     121.082  -7.890-237.076  1.00 41.91           N  
ANISOU11420  N   GLU D 301     4337   7231   4357   -397    875   -470       N  
ATOM  11421  CA  GLU D 301     121.821  -6.637-236.986  1.00 47.41           C  
ANISOU11421  CA  GLU D 301     4978   8056   4979   -630    887   -416       C  
ATOM  11422  C   GLU D 301     121.668  -6.039-235.592  1.00 38.32           C  
ANISOU11422  C   GLU D 301     3842   6813   3906   -679    800   -368       C  
ATOM  11423  O   GLU D 301     120.588  -6.094-234.998  1.00 45.82           O  
ANISOU11423  O   GLU D 301     4927   7533   4947   -610    725   -347       O  
ATOM  11424  CB  GLU D 301     121.324  -5.628-238.024  1.00 53.22           C  
ANISOU11424  CB  GLU D 301     5875   8716   5630   -825    893   -362       C  
ATOM  11425  CG  GLU D 301     122.131  -5.555-239.297  1.00 67.89           C  
ANISOU11425  CG  GLU D 301     7658  10788   7350   -920    996   -383       C  
ATOM  11426  CD  GLU D 301     121.592  -4.507-240.257  1.00 82.97           C  
ANISOU11426  CD  GLU D 301     9747  12603   9173  -1121    989   -317       C  
ATOM  11427  OE1 GLU D 301     121.707  -3.298-239.955  1.00 89.43           O  
ANISOU11427  OE1 GLU D 301    10625  13393   9961  -1327    952   -244       O  
ATOM  11428  OE2 GLU D 301     121.038  -4.898-241.308  1.00 89.12           O  
ANISOU11428  OE2 GLU D 301    10621  13328   9913  -1073   1015   -336       O  
ATOM  11429  N   LEU D 302     122.748  -5.431-235.100  1.00 43.18           N  
ANISOU11429  N   LEU D 302     4317   7616   4473   -812    814   -351       N  
ATOM  11430  CA  LEU D 302     122.805  -4.837-233.769  1.00 46.26           C  
ANISOU11430  CA  LEU D 302     4704   7956   4916   -878    738   -312       C  
ATOM  11431  C   LEU D 302     122.419  -3.360-233.817  1.00 41.65           C  
ANISOU11431  C   LEU D 302     4286   7249   4289  -1123    696   -239       C  
ATOM  11432  O   LEU D 302     122.949  -2.601-234.642  1.00 43.27           O  
ANISOU11432  O   LEU D 302     4492   7564   4383  -1318    742   -212       O  
ATOM  11433  CB  LEU D 302     124.220  -4.989-233.225  1.00 56.22           C  
ANISOU11433  CB  LEU D 302     5720   9501   6141   -898    768   -334       C  
ATOM  11434  CG  LEU D 302     124.430  -4.966-231.717  1.00 59.72           C  
ANISOU11434  CG  LEU D 302     6100   9938   6654   -867    694   -322       C  
ATOM  11435  CD1 LEU D 302     123.940  -6.259-231.122  1.00 57.62           C  
ANISOU11435  CD1 LEU D 302     5822   9574   6497   -587    664   -364       C  
ATOM  11436  CD2 LEU D 302     125.901  -4.772-231.464  1.00 67.66           C  
ANISOU11436  CD2 LEU D 302     6867  11256   7583   -966    728   -328       C  
ATOM  11437  N   PHE D 303     121.490  -2.957-232.954  1.00 42.96           N  
ANISOU11437  N   PHE D 303     4602   7187   4536  -1110    610   -207       N  
ATOM  11438  CA  PHE D 303     121.074  -1.564-232.836  1.00 43.88           C  
ANISOU11438  CA  PHE D 303     4895   7158   4619  -1313    560   -142       C  
ATOM  11439  C   PHE D 303     121.054  -1.158-231.367  1.00 46.31           C  
ANISOU11439  C   PHE D 303     5214   7397   4986  -1330    486   -128       C  
ATOM  11440  O   PHE D 303     120.442  -1.844-230.541  1.00 43.69           O  
ANISOU11440  O   PHE D 303     4886   6959   4753  -1150    445   -150       O  
ATOM  11441  CB  PHE D 303     119.691  -1.345-233.448  1.00 41.67           C  
ANISOU11441  CB  PHE D 303     4837   6628   4368  -1271    528   -114       C  
ATOM  11442  CG  PHE D 303     119.640  -1.546-234.945  1.00 42.20           C  
ANISOU11442  CG  PHE D 303     4929   6745   4360  -1289    590   -118       C  
ATOM  11443  CD1 PHE D 303     119.450  -2.808-235.482  1.00 41.48           C  
ANISOU11443  CD1 PHE D 303     4769   6694   4299  -1099    632   -174       C  
ATOM  11444  CD2 PHE D 303     119.781  -0.472-235.810  1.00 45.88           C  
ANISOU11444  CD2 PHE D 303     5502   7211   4719  -1503    605    -65       C  
ATOM  11445  CE1 PHE D 303     119.401  -2.995-236.867  1.00 44.31           C  
ANISOU11445  CE1 PHE D 303     5158   7099   4578  -1119    690   -183       C  
ATOM  11446  CE2 PHE D 303     119.735  -0.653-237.194  1.00 48.34           C  
ANISOU11446  CE2 PHE D 303     5841   7574   4952  -1526    662    -66       C  
ATOM  11447  CZ  PHE D 303     119.540  -1.920-237.716  1.00 44.99           C  
ANISOU11447  CZ  PHE D 303     5342   7197   4557  -1331    706   -128       C  
ATOM  11448  N   LEU D 304     121.698  -0.035-231.054  1.00 49.33           N  
ANISOU11448  N   LEU D 304     5613   7834   5297  -1558    469    -92       N  
ATOM  11449  CA  LEU D 304     121.709   0.493-229.696  1.00 49.98           C  
ANISOU11449  CA  LEU D 304     5728   7848   5415  -1606    398    -80       C  
ATOM  11450  C   LEU D 304     120.468   1.339-229.459  1.00 49.78           C  
ANISOU11450  C   LEU D 304     5965   7525   5425  -1628    332    -43       C  
ATOM  11451  O   LEU D 304     120.143   2.209-230.269  1.00 49.40           O  
ANISOU11451  O   LEU D 304     6077   7378   5317  -1760    333     -2       O  
ATOM  11452  CB  LEU D 304     122.959   1.336-229.464  1.00 53.75           C  
ANISOU11452  CB  LEU D 304     6115   8515   5791  -1856    404    -60       C  
ATOM  11453  CG  LEU D 304     124.301   0.645-229.699  1.00 61.68           C  
ANISOU11453  CG  LEU D 304     6838   9854   6744  -1857    471    -92       C  
ATOM  11454  CD1 LEU D 304     125.445   1.600-229.409  1.00 59.93           C  
ANISOU11454  CD1 LEU D 304     6539   9815   6417  -2134    466    -63       C  
ATOM  11455  CD2 LEU D 304     124.411  -0.606-228.843  1.00 64.12           C  
ANISOU11455  CD2 LEU D 304     6983  10231   7147  -1607    458   -141       C  
ATOM  11456  N   LEU D 305     119.765   1.077-228.364  1.00 47.59           N  
ANISOU11456  N   LEU D 305     5733   7109   5241  -1490    276    -57       N  
ATOM  11457  CA  LEU D 305     118.651   1.940-227.990  1.00 52.70           C  
ANISOU11457  CA  LEU D 305     6614   7493   5916  -1504    214    -28       C  
ATOM  11458  C   LEU D 305     119.197   3.265-227.473  1.00 54.18           C  
ANISOU11458  C   LEU D 305     6895   7662   6029  -1739    177      0       C  
ATOM  11459  O   LEU D 305     120.145   3.261-226.685  1.00 54.98           O  
ANISOU11459  O   LEU D 305     6868   7914   6106  -1816    170    -15       O  
ATOM  11460  CB  LEU D 305     117.786   1.271-226.917  1.00 43.89           C  
ANISOU11460  CB  LEU D 305     5506   6258   4910  -1298    171    -54       C  
ATOM  11461  CG  LEU D 305     116.960   0.082-227.412  1.00 43.39           C  
ANISOU11461  CG  LEU D 305     5411   6151   4922  -1078    193    -75       C  
ATOM  11462  CD1 LEU D 305     116.425  -0.709-226.228  1.00 50.86           C  
ANISOU11462  CD1 LEU D 305     6320   7042   5964   -901    158   -100       C  
ATOM  11463  CD2 LEU D 305     115.825   0.550-228.315  1.00 47.33           C  
ANISOU11463  CD2 LEU D 305     6094   6468   5421  -1068    183    -44       C  
ATOM  11464  N   PRO D 306     118.665   4.404-227.914  1.00 53.11           N  
ANISOU11464  N   PRO D 306     6984   7348   5847  -1861    150     43       N  
ATOM  11465  CA  PRO D 306     119.091   5.693-227.355  1.00 52.99           C  
ANISOU11465  CA  PRO D 306     7099   7275   5759  -2083    106     67       C  
ATOM  11466  C   PRO D 306     118.766   5.771-225.876  1.00 58.43           C  
ANISOU11466  C   PRO D 306     7824   7870   6509  -2009     48     39       C  
ATOM  11467  O   PRO D 306     117.608   5.565-225.483  1.00 57.16           O  
ANISOU11467  O   PRO D 306     7760   7529   6429  -1826     20     27       O  
ATOM  11468  CB  PRO D 306     118.271   6.717-228.153  1.00 60.85           C  
ANISOU11468  CB  PRO D 306     8360   8045   6715  -2152     82    117       C  
ATOM  11469  CG  PRO D 306     117.901   6.015-229.418  1.00 56.42           C  
ANISOU11469  CG  PRO D 306     7750   7523   6165  -2049    132    126       C  
ATOM  11470  CD  PRO D 306     117.702   4.573-229.015  1.00 55.46           C  
ANISOU11470  CD  PRO D 306     7433   7495   6145  -1809    156     73       C  
ATOM  11471  N   PRO D 307     119.762   6.042-225.028  1.00 59.67           N  
ANISOU11471  N   PRO D 307     7895   8157   6621  -2151     30     26       N  
ATOM  11472  CA  PRO D 307     119.512   6.152-223.582  1.00 56.48           C  
ANISOU11472  CA  PRO D 307     7530   7672   6258  -2097    -26     -3       C  
ATOM  11473  C   PRO D 307     118.251   6.923-223.215  1.00 54.95           C  
ANISOU11473  C   PRO D 307     7605   7180   6095  -2033    -75      2       C  
ATOM  11474  O   PRO D 307     117.498   6.478-222.345  1.00 52.99           O  
ANISOU11474  O   PRO D 307     7365   6844   5926  -1851    -97    -27       O  
ATOM  11475  CB  PRO D 307     120.770   6.870-223.065  1.00 60.82           C  
ANISOU11475  CB  PRO D 307     8035   8365   6709  -2357    -48      1       C  
ATOM  11476  CG  PRO D 307     121.746   6.924-224.254  1.00 63.26           C  
ANISOU11476  CG  PRO D 307     8228   8875   6932  -2526      8     31       C  
ATOM  11477  CD  PRO D 307     121.201   6.042-225.325  1.00 58.48           C  
ANISOU11477  CD  PRO D 307     7562   8277   6382  -2341     66     32       C  
ATOM  11478  N   GLU D 308     117.986   8.051-223.881  1.00 57.50           N  
ANISOU11478  N   GLU D 308     8148   7346   6354  -2170    -90     39       N  
ATOM  11479  CA  GLU D 308     116.826   8.871-223.535  1.00 57.34           C  
ANISOU11479  CA  GLU D 308     8391   7041   6353  -2102   -138     42       C  
ATOM  11480  C   GLU D 308     115.499   8.216-223.889  1.00 56.93           C  
ANISOU11480  C   GLU D 308     8359   6873   6399  -1838   -128     40       C  
ATOM  11481  O   GLU D 308     114.446   8.723-223.485  1.00 51.27           O  
ANISOU11481  O   GLU D 308     7822   5944   5713  -1733   -165     35       O  
ATOM  11482  CB  GLU D 308     116.904  10.235-224.225  1.00 58.32           C  
ANISOU11482  CB  GLU D 308     8759   7020   6379  -2309   -163     89       C  
ATOM  11483  CG  GLU D 308     116.813  10.187-225.737  1.00 73.70           C  
ANISOU11483  CG  GLU D 308    10719   8987   8298  -2336   -126    138       C  
ATOM  11484  CD  GLU D 308     118.169  10.032-226.409  1.00 90.12           C  
ANISOU11484  CD  GLU D 308    12629  11319  10292  -2549    -78    158       C  
ATOM  11485  OE1 GLU D 308     119.155   9.709-225.707  1.00 95.76           O  
ANISOU11485  OE1 GLU D 308    13165  12229  10991  -2632    -69    129       O  
ATOM  11486  OE2 GLU D 308     118.247  10.239-227.640  1.00 93.95           O  
ANISOU11486  OE2 GLU D 308    13157  11818  10722  -2632    -49    203       O  
ATOM  11487  N   LEU D 309     115.522   7.126-224.646  1.00 47.03           N  
ANISOU11487  N   LEU D 309     6927   5754   5187  -1732    -79     42       N  
ATOM  11488  CA  LEU D 309     114.309   6.408-224.988  1.00 46.03           C  
ANISOU11488  CA  LEU D 309     6801   5540   5148  -1499    -72     40       C  
ATOM  11489  C   LEU D 309     113.912   5.384-223.932  1.00 44.04           C  
ANISOU11489  C   LEU D 309     6420   5325   4989  -1308    -74     -4       C  
ATOM  11490  O   LEU D 309     112.743   4.994-223.876  1.00 46.42           O  
ANISOU11490  O   LEU D 309     6760   5517   5361  -1125    -82     -8       O  
ATOM  11491  CB  LEU D 309     114.505   5.701-226.333  1.00 51.38           C  
ANISOU11491  CB  LEU D 309     7369   6336   5818  -1484    -20     59       C  
ATOM  11492  CG  LEU D 309     113.349   5.461-227.293  1.00 59.00           C  
ANISOU11492  CG  LEU D 309     8411   7187   6820  -1346    -19     82       C  
ATOM  11493  CD1 LEU D 309     112.779   6.775-227.793  1.00 58.93           C  
ANISOU11493  CD1 LEU D 309     8655   6980   6756  -1427    -60    129       C  
ATOM  11494  CD2 LEU D 309     113.870   4.628-228.464  1.00 61.01           C  
ANISOU11494  CD2 LEU D 309     8520   7610   7052  -1355     40     85       C  
ATOM  11495  N   VAL D 310     114.841   4.975-223.073  1.00 37.28           N  
ANISOU11495  N   VAL D 310     5415   4621   4127  -1353    -71    -32       N  
ATOM  11496  CA  VAL D 310     114.649   3.851-222.154  1.00 36.98           C  
ANISOU11496  CA  VAL D 310     5233   4651   4168  -1182    -70    -66       C  
ATOM  11497  C   VAL D 310     114.471   4.413-220.743  1.00 39.56           C  
ANISOU11497  C   VAL D 310     5647   4891   4492  -1193   -115    -89       C  
ATOM  11498  O   VAL D 310     115.444   4.707-220.046  1.00 41.22           O  
ANISOU11498  O   VAL D 310     5809   5200   4652  -1325   -133   -101       O  
ATOM  11499  CB  VAL D 310     115.818   2.870-222.228  1.00 39.68           C  
ANISOU11499  CB  VAL D 310     5336   5237   4505  -1196    -36    -79       C  
ATOM  11500  CG1 VAL D 310     115.660   1.757-221.187  1.00 42.90           C  
ANISOU11500  CG1 VAL D 310     5617   5698   4986  -1026    -45   -108       C  
ATOM  11501  CG2 VAL D 310     115.909   2.284-223.639  1.00 42.68           C  
ANISOU11501  CG2 VAL D 310     5641   5691   4882  -1166     16    -66       C  
ATOM  11502  N   LEU D 311     113.215   4.562-220.318  1.00 34.12           N  
ANISOU11502  N   LEU D 311     5083   4028   3852  -1054   -135    -96       N  
ATOM  11503  CA  LEU D 311     112.920   5.124-219.004  1.00 33.96           C  
ANISOU11503  CA  LEU D 311     5165   3915   3825  -1047   -172   -124       C  
ATOM  11504  C   LEU D 311     113.157   4.067-217.936  1.00 35.83           C  
ANISOU11504  C   LEU D 311     5234   4275   4104   -953   -172   -151       C  
ATOM  11505  O   LEU D 311     112.683   2.935-218.056  1.00 32.47           O  
ANISOU11505  O   LEU D 311     4695   3894   3749   -794   -151   -149       O  
ATOM  11506  CB  LEU D 311     111.471   5.617-218.950  1.00 36.69           C  
ANISOU11506  CB  LEU D 311     5687   4050   4203   -913   -186   -125       C  
ATOM  11507  CG  LEU D 311     110.989   6.311-217.679  1.00 37.58           C  
ANISOU11507  CG  LEU D 311     5936   4041   4300   -886   -217   -161       C  
ATOM  11508  CD1 LEU D 311     111.846   7.524-217.383  1.00 38.15           C  
ANISOU11508  CD1 LEU D 311     6148   4071   4279  -1098   -249   -169       C  
ATOM  11509  CD2 LEU D 311     109.535   6.718-217.838  1.00 40.15           C  
ANISOU11509  CD2 LEU D 311     6410   4184   4660   -728   -221   -159       C  
ATOM  11510  N   GLU D 312     113.885   4.444-216.885  1.00 37.66           N  
ANISOU11510  N   GLU D 312     5462   4558   4288  -1058   -202   -172       N  
ATOM  11511  CA  GLU D 312     114.199   3.547-215.788  1.00 38.52           C  
ANISOU11511  CA  GLU D 312     5426   4786   4423   -986   -213   -192       C  
ATOM  11512  C   GLU D 312     113.769   4.195-214.479  1.00 35.02           C  
ANISOU11512  C   GLU D 312     5116   4236   3954   -987   -248   -223       C  
ATOM  11513  O   GLU D 312     113.591   5.412-214.395  1.00 35.88           O  
ANISOU11513  O   GLU D 312     5416   4209   4009  -1085   -268   -235       O  
ATOM  11514  CB  GLU D 312     115.700   3.208-215.751  1.00 44.26           C  
ANISOU11514  CB  GLU D 312     5974   5735   5106  -1112   -217   -188       C  
ATOM  11515  CG  GLU D 312     116.144   2.227-216.839  1.00 45.64           C  
ANISOU11515  CG  GLU D 312     5975   6051   5314  -1058   -174   -168       C  
ATOM  11516  CD  GLU D 312     117.630   1.915-216.769  1.00 51.43           C  
ANISOU11516  CD  GLU D 312     6517   7024   6001  -1167   -176   -167       C  
ATOM  11517  OE1 GLU D 312     118.428   2.720-217.280  1.00 58.49           O  
ANISOU11517  OE1 GLU D 312     7422   7981   6820  -1361   -174   -156       O  
ATOM  11518  OE2 GLU D 312     118.002   0.878-216.182  1.00 55.58           O  
ANISOU11518  OE2 GLU D 312     6882   7676   6559  -1060   -183   -174       O  
ATOM  11519  N   VAL D 313     113.602   3.363-213.459  1.00 36.89           N  
ANISOU11519  N   VAL D 313     5260   4531   4224   -875   -256   -238       N  
ATOM  11520  CA  VAL D 313     113.139   3.794-212.149  1.00 35.00           C  
ANISOU11520  CA  VAL D 313     5129   4211   3960   -854   -283   -271       C  
ATOM  11521  C   VAL D 313     114.181   3.364-211.127  1.00 34.92           C  
ANISOU11521  C   VAL D 313     4991   4366   3913   -921   -316   -280       C  
ATOM  11522  O   VAL D 313     114.401   2.165-210.940  1.00 33.65           O  
ANISOU11522  O   VAL D 313     4660   4331   3797   -823   -312   -264       O  
ATOM  11523  CB  VAL D 313     111.762   3.208-211.793  1.00 34.75           C  
ANISOU11523  CB  VAL D 313     5120   4088   3995   -647   -261   -277       C  
ATOM  11524  CG1 VAL D 313     111.305   3.740-210.437  1.00 34.24           C  
ANISOU11524  CG1 VAL D 313     5172   3947   3890   -630   -281   -317       C  
ATOM  11525  CG2 VAL D 313     110.742   3.533-212.870  1.00 32.50           C  
ANISOU11525  CG2 VAL D 313     4933   3667   3749   -569   -234   -262       C  
ATOM  11526  N   PRO D 314     114.859   4.293-210.459  1.00 40.85           N  
ANISOU11526  N   PRO D 314     5823   5121   4577  -1090   -356   -303       N  
ATOM  11527  CA  PRO D 314     115.691   3.907-209.316  1.00 41.92           C  
ANISOU11527  CA  PRO D 314     5849   5407   4672  -1140   -397   -313       C  
ATOM  11528  C   PRO D 314     114.808   3.444-208.171  1.00 41.10           C  
ANISOU11528  C   PRO D 314     5780   5246   4591   -988   -400   -332       C  
ATOM  11529  O   PRO D 314     113.761   4.036-207.900  1.00 35.49           O  
ANISOU11529  O   PRO D 314     5240   4365   3880   -927   -386   -360       O  
ATOM  11530  CB  PRO D 314     116.436   5.201-208.966  1.00 48.98           C  
ANISOU11530  CB  PRO D 314     6869   6282   5460  -1372   -439   -337       C  
ATOM  11531  CG  PRO D 314     115.506   6.285-209.402  1.00 47.32           C  
ANISOU11531  CG  PRO D 314     6904   5836   5241  -1376   -422   -355       C  
ATOM  11532  CD  PRO D 314     114.828   5.753-210.658  1.00 42.97           C  
ANISOU11532  CD  PRO D 314     6307   5244   4777  -1239   -371   -322       C  
ATOM  11533  N   LEU D 315     115.231   2.377-207.496  1.00 38.84           N  
ANISOU11533  N   LEU D 315     5330   5108   4321   -923   -419   -317       N  
ATOM  11534  CA  LEU D 315     114.404   1.777-206.456  1.00 32.80           C  
ANISOU11534  CA  LEU D 315     4580   4307   3576   -780   -419   -325       C  
ATOM  11535  C   LEU D 315     114.787   2.333-205.095  1.00 33.52           C  
ANISOU11535  C   LEU D 315     4739   4420   3575   -878   -467   -358       C  
ATOM  11536  O   LEU D 315     115.966   2.350-204.733  1.00 35.56           O  
ANISOU11536  O   LEU D 315     4906   4827   3778  -1004   -516   -352       O  
ATOM  11537  CB  LEU D 315     114.524   0.252-206.453  1.00 38.31           C  
ANISOU11537  CB  LEU D 315     5090   5127   4338   -641   -415   -285       C  
ATOM  11538  CG  LEU D 315     113.968  -0.417-207.725  1.00 43.81           C  
ANISOU11538  CG  LEU D 315     5736   5785   5124   -524   -365   -258       C  
ATOM  11539  CD1 LEU D 315     113.761  -1.902-207.485  1.00 46.86           C  
ANISOU11539  CD1 LEU D 315     5997   6238   5570   -368   -363   -226       C  
ATOM  11540  CD2 LEU D 315     112.669   0.239-208.188  1.00 35.24           C  
ANISOU11540  CD2 LEU D 315     4811   4512   4065   -472   -325   -275       C  
ATOM  11541  N   GLU D 316     113.786   2.790-204.353  1.00 35.49           N  
ANISOU11541  N   GLU D 316     5146   4534   3804   -820   -454   -395       N  
ATOM  11542  CA  GLU D 316     113.976   3.211-202.973  1.00 36.59           C  
ANISOU11542  CA  GLU D 316     5363   4687   3854   -887   -494   -432       C  
ATOM  11543  C   GLU D 316     112.785   2.751-202.139  1.00 40.55           C  
ANISOU11543  C   GLU D 316     5913   5124   4372   -723   -464   -445       C  
ATOM  11544  O   GLU D 316     111.728   2.415-202.668  1.00 36.24           O  
ANISOU11544  O   GLU D 316     5377   4493   3898   -580   -412   -434       O  
ATOM  11545  CB  GLU D 316     114.168   4.730-202.872  1.00 44.82           C  
ANISOU11545  CB  GLU D 316     6607   5613   4808  -1051   -514   -484       C  
ATOM  11546  CG  GLU D 316     112.923   5.548-203.128  1.00 54.86           C  
ANISOU11546  CG  GLU D 316     8085   6666   6091   -968   -468   -523       C  
ATOM  11547  CD  GLU D 316     113.160   7.035-202.892  1.00 69.74           C  
ANISOU11547  CD  GLU D 316    10198   8423   7879  -1128   -495   -578       C  
ATOM  11548  OE1 GLU D 316     113.981   7.619-203.631  1.00 63.86           O  
ANISOU11548  OE1 GLU D 316     9471   7685   7109  -1293   -520   -565       O  
ATOM  11549  OE2 GLU D 316     112.543   7.604-201.958  1.00 71.72           O  
ANISOU11549  OE2 GLU D 316    10612   8568   8072  -1093   -493   -636       O  
ATOM  11550  N   HIS D 317     112.961   2.735-200.797  1.00 40.31           N  
ANISOU11550  N   HIS D 317     5906   5144   4265   -753   -498   -467       N  
ATOM  11551  CA  HIS D 317     111.860   2.307-199.948  1.00 39.68           C  
ANISOU11551  CA  HIS D 317     5869   5021   4186   -611   -465   -478       C  
ATOM  11552  C   HIS D 317     111.296   3.502-199.184  1.00 40.57           C  
ANISOU11552  C   HIS D 317     6198   5005   4212   -645   -454   -554       C  
ATOM  11553  O   HIS D 317     112.051   4.394-198.814  1.00 35.22           O  
ANISOU11553  O   HIS D 317     5613   4320   3448   -802   -498   -592       O  
ATOM  11554  CB  HIS D 317     112.337   1.233-198.956  1.00 37.83           C  
ANISOU11554  CB  HIS D 317     5505   4942   3929   -590   -506   -441       C  
ATOM  11555  CG  HIS D 317     111.238   0.584-198.171  1.00 38.78           C  
ANISOU11555  CG  HIS D 317     5642   5040   4053   -450   -469   -436       C  
ATOM  11556  ND1 HIS D 317     110.692   1.147-197.036  1.00 40.78           N  
ANISOU11556  ND1 HIS D 317     6030   5247   4218   -453   -458   -488       N  
ATOM  11557  CD2 HIS D 317     110.591  -0.594-198.355  1.00 38.39           C  
ANISOU11557  CD2 HIS D 317     5495   5015   4078   -311   -438   -384       C  
ATOM  11558  CE1 HIS D 317     109.754   0.349-196.558  1.00 38.79           C  
ANISOU11558  CE1 HIS D 317     5750   5004   3986   -325   -419   -466       C  
ATOM  11559  NE2 HIS D 317     109.682  -0.721-197.331  1.00 38.05           N  
ANISOU11559  NE2 HIS D 317     5518   4950   3989   -244   -410   -400       N  
ATOM  11560  N   PRO D 318     109.987   3.574-198.942  1.00 39.48           N  
ANISOU11560  N   PRO D 318     6147   4766   4088   -503   -395   -581       N  
ATOM  11561  CA  PRO D 318     109.453   4.783-198.301  1.00 37.62           C  
ANISOU11561  CA  PRO D 318     6128   4398   3768   -518   -379   -662       C  
ATOM  11562  C   PRO D 318     109.959   4.995-196.895  1.00 48.36           C  
ANISOU11562  C   PRO D 318     7545   5819   5009   -611   -421   -702       C  
ATOM  11563  O   PRO D 318     110.053   6.148-196.450  1.00 49.40           O  
ANISOU11563  O   PRO D 318     7866   5853   5051   -697   -435   -774       O  
ATOM  11564  CB  PRO D 318     107.933   4.559-198.348  1.00 39.75           C  
ANISOU11564  CB  PRO D 318     6423   4594   4086   -321   -303   -672       C  
ATOM  11565  CG  PRO D 318     107.766   3.087-198.498  1.00 35.89           C  
ANISOU11565  CG  PRO D 318     5732   4229   3675   -234   -292   -596       C  
ATOM  11566  CD  PRO D 318     108.909   2.671-199.393  1.00 35.79           C  
ANISOU11566  CD  PRO D 318     5594   4290   3714   -328   -338   -542       C  
ATOM  11567  N   THR D 319     110.316   3.929-196.178  1.00 31.07           N  
ANISOU11567  N   THR D 319     5210   3784   2811   -601   -447   -657       N  
ATOM  11568  CA  THR D 319     110.805   4.106-194.805  1.00 35.04           C  
ANISOU11568  CA  THR D 319     5767   4356   3192   -692   -493   -691       C  
ATOM  11569  C   THR D 319     112.156   3.473-194.492  1.00 50.43           C  
ANISOU11569  C   THR D 319     7563   6483   5114   -812   -578   -638       C  
ATOM  11570  O   THR D 319     112.723   3.784-193.434  1.00 33.69           O  
ANISOU11570  O   THR D 319     5496   4423   2881   -921   -631   -668       O  
ATOM  11571  CB  THR D 319     109.796   3.570-193.774  1.00 49.66           C  
ANISOU11571  CB  THR D 319     7633   6226   5010   -561   -447   -701       C  
ATOM  11572  OG1 THR D 319     109.569   2.170-193.991  1.00 47.22           O  
ANISOU11572  OG1 THR D 319     7139   6016   4786   -456   -435   -616       O  
ATOM  11573  CG2 THR D 319     108.480   4.334-193.833  1.00 48.48           C  
ANISOU11573  CG2 THR D 319     7642   5922   4857   -444   -365   -768       C  
ATOM  11574  N   LEU D 320     112.690   2.603-195.340  1.00 47.42           N  
ANISOU11574  N   LEU D 320     6997   6194   4825   -790   -594   -564       N  
ATOM  11575  CA  LEU D 320     113.995   1.992-195.089  1.00 40.80           C  
ANISOU11575  CA  LEU D 320     6000   5538   3963   -883   -675   -514       C  
ATOM  11576  C   LEU D 320     115.007   2.716-195.961  1.00 41.19           C  
ANISOU11576  C   LEU D 320     6031   5606   4012  -1039   -709   -520       C  
ATOM  11577  O   LEU D 320     115.148   2.403-197.142  1.00 42.34           O  
ANISOU11577  O   LEU D 320     6078   5757   4250  -1004   -686   -483       O  
ATOM  11578  CB  LEU D 320     113.981   0.495-195.369  1.00 37.27           C  
ANISOU11578  CB  LEU D 320     5361   5192   3607   -746   -672   -430       C  
ATOM  11579  CG  LEU D 320     112.992  -0.385-194.617  1.00 44.63           C  
ANISOU11579  CG  LEU D 320     6295   6115   4546   -600   -639   -406       C  
ATOM  11580  CD1 LEU D 320     112.844  -1.719-195.355  1.00 39.79           C  
ANISOU11580  CD1 LEU D 320     5527   5544   4047   -467   -623   -328       C  
ATOM  11581  CD2 LEU D 320     113.431  -0.595-193.172  1.00 44.83           C  
ANISOU11581  CD2 LEU D 320     6327   6247   4458   -654   -700   -402       C  
ATOM  11582  N   GLU D 321     115.725   3.679-195.370  1.00 42.72           N  
ANISOU11582  N   GLU D 321     6323   5816   4094  -1223   -764   -567       N  
ATOM  11583  CA  GLU D 321     116.535   4.580-196.181  1.00 43.04           C  
ANISOU11583  CA  GLU D 321     6391   5845   4118  -1398   -789   -582       C  
ATOM  11584  C   GLU D 321     117.763   3.889-196.757  1.00 50.13           C  
ANISOU11584  C   GLU D 321     7049   6946   5050  -1459   -837   -515       C  
ATOM  11585  O   GLU D 321     118.260   4.306-197.814  1.00 49.60           O  
ANISOU11585  O   GLU D 321     6953   6882   5011  -1550   -830   -505       O  
ATOM  11586  CB  GLU D 321     116.956   5.813-195.382  1.00 45.82           C  
ANISOU11586  CB  GLU D 321     6928   6151   4330  -1596   -839   -652       C  
ATOM  11587  CG  GLU D 321     115.932   6.930-195.365  1.00 56.98           C  
ANISOU11587  CG  GLU D 321     8614   7321   5713  -1575   -786   -731       C  
ATOM  11588  CD  GLU D 321     114.759   6.640-194.454  1.00 81.16           C  
ANISOU11588  CD  GLU D 321    11761  10312   8764  -1400   -737   -765       C  
ATOM  11589  OE1 GLU D 321     114.884   5.739-193.607  1.00 88.31           O  
ANISOU11589  OE1 GLU D 321    12548  11355   9649  -1349   -761   -733       O  
ATOM  11590  OE2 GLU D 321     113.717   7.312-194.592  1.00104.61           O  
ANISOU11590  OE2 GLU D 321    14913  13095  11740  -1311   -676   -820       O  
ATOM  11591  N   TRP D 322     118.261   2.836-196.101  1.00 41.86           N  
ANISOU11591  N   TRP D 322     5833   6075   3999  -1403   -883   -466       N  
ATOM  11592  CA  TRP D 322     119.392   2.100-196.658  1.00 44.75           C  
ANISOU11592  CA  TRP D 322     5959   6643   4401  -1424   -925   -403       C  
ATOM  11593  C   TRP D 322     119.046   1.373-197.959  1.00 43.04           C  
ANISOU11593  C   TRP D 322     5637   6399   4319  -1275   -859   -362       C  
ATOM  11594  O   TRP D 322     119.961   0.980-198.689  1.00 42.82           O  
ANISOU11594  O   TRP D 322     5431   6516   4322  -1301   -876   -324       O  
ATOM  11595  CB  TRP D 322     119.943   1.099-195.628  1.00 43.43           C  
ANISOU11595  CB  TRP D 322     5647   6658   4199  -1370   -995   -357       C  
ATOM  11596  CG  TRP D 322     118.895   0.235-195.004  1.00 43.94           C  
ANISOU11596  CG  TRP D 322     5748   6648   4298  -1176   -962   -339       C  
ATOM  11597  CD1 TRP D 322     118.322   0.400-193.762  1.00 46.84           C  
ANISOU11597  CD1 TRP D 322     6248   6966   4584  -1172   -973   -368       C  
ATOM  11598  CD2 TRP D 322     118.296  -0.938-195.569  1.00 33.46           C  
ANISOU11598  CD2 TRP D 322     4331   5297   3087   -972   -914   -287       C  
ATOM  11599  NE1 TRP D 322     117.399  -0.592-193.539  1.00 43.20           N  
ANISOU11599  NE1 TRP D 322     5776   6456   4180   -983   -931   -332       N  
ATOM  11600  CE2 TRP D 322     117.359  -1.421-194.632  1.00 40.80           C  
ANISOU11600  CE2 TRP D 322     5342   6161   3999   -862   -897   -282       C  
ATOM  11601  CE3 TRP D 322     118.442  -1.613-196.788  1.00 36.06           C  
ANISOU11601  CE3 TRP D 322     4526   5649   3525   -877   -881   -247       C  
ATOM  11602  CZ2 TRP D 322     116.587  -2.556-194.865  1.00 38.08           C  
ANISOU11602  CZ2 TRP D 322     4952   5776   3743   -677   -855   -234       C  
ATOM  11603  CZ3 TRP D 322     117.668  -2.742-197.020  1.00 39.38           C  
ANISOU11603  CZ3 TRP D 322     4910   6017   4034   -683   -840   -205       C  
ATOM  11604  CH2 TRP D 322     116.748  -3.199-196.064  1.00 43.57           C  
ANISOU11604  CH2 TRP D 322     5527   6483   4546   -592   -829   -196       C  
ATOM  11605  N   PHE D 323     117.758   1.176-198.268  1.00 39.87           N  
ANISOU11605  N   PHE D 323     5333   5826   3989  -1120   -785   -371       N  
ATOM  11606  CA  PHE D 323     117.398   0.425-199.472  1.00 37.93           C  
ANISOU11606  CA  PHE D 323     4991   5556   3864   -981   -728   -332       C  
ATOM  11607  C   PHE D 323     117.969   1.087-200.718  1.00 41.07           C  
ANISOU11607  C   PHE D 323     5368   5957   4279  -1095   -712   -338       C  
ATOM  11608  O   PHE D 323     118.462   0.404-201.623  1.00 43.46           O  
ANISOU11608  O   PHE D 323     5510   6357   4645  -1047   -700   -298       O  
ATOM  11609  CB  PHE D 323     115.875   0.299-199.582  1.00 38.10           C  
ANISOU11609  CB  PHE D 323     5138   5394   3945   -828   -655   -346       C  
ATOM  11610  CG  PHE D 323     115.409  -0.763-200.546  1.00 38.36           C  
ANISOU11610  CG  PHE D 323     5065   5417   4094   -666   -609   -300       C  
ATOM  11611  CD1 PHE D 323     115.184  -0.454-201.876  1.00 39.97           C  
ANISOU11611  CD1 PHE D 323     5280   5544   4361   -662   -561   -303       C  
ATOM  11612  CD2 PHE D 323     115.170  -2.066-200.112  1.00 37.70           C  
ANISOU11612  CD2 PHE D 323     4886   5390   4050   -523   -615   -253       C  
ATOM  11613  CE1 PHE D 323     114.752  -1.427-202.769  1.00 38.83           C  
ANISOU11613  CE1 PHE D 323     5049   5389   4315   -521   -520   -266       C  
ATOM  11614  CE2 PHE D 323     114.732  -3.045-201.006  1.00 44.32           C  
ANISOU11614  CE2 PHE D 323     5647   6206   4988   -384   -576   -215       C  
ATOM  11615  CZ  PHE D 323     114.526  -2.722-202.329  1.00 42.32           C  
ANISOU11615  CZ  PHE D 323     5401   5883   4795   -384   -528   -224       C  
ATOM  11616  N   ALA D 324     117.935   2.422-200.769  1.00 44.02           N  
ANISOU11616  N   ALA D 324     5912   6225   4590  -1251   -712   -387       N  
ATOM  11617  CA  ALA D 324     118.452   3.135-201.932  1.00 47.18           C  
ANISOU11617  CA  ALA D 324     6317   6617   4993  -1382   -698   -388       C  
ATOM  11618  C   ALA D 324     119.912   2.805-202.195  1.00 48.44           C  
ANISOU11618  C   ALA D 324     6264   7016   5127  -1496   -745   -352       C  
ATOM  11619  O   ALA D 324     120.362   2.880-203.340  1.00 40.02           O  
ANISOU11619  O   ALA D 324     5119   5996   4090  -1545   -719   -333       O  
ATOM  11620  CB  ALA D 324     118.288   4.645-201.749  1.00 45.68           C  
ANISOU11620  CB  ALA D 324     6366   6273   4718  -1550   -706   -445       C  
ATOM  11621  N   ALA D 325     120.661   2.421-201.165  1.00 41.62           N  
ANISOU11621  N   ALA D 325     5293   6317   4203  -1533   -813   -341       N  
ATOM  11622  CA  ALA D 325     122.081   2.130-201.337  1.00 38.48           C  
ANISOU11622  CA  ALA D 325     4676   6174   3772  -1637   -864   -308       C  
ATOM  11623  C   ALA D 325     122.342   0.766-201.963  1.00 44.44           C  
ANISOU11623  C   ALA D 325     5204   7060   4619  -1450   -843   -256       C  
ATOM  11624  O   ALA D 325     123.487   0.493-202.333  1.00 42.40           O  
ANISOU11624  O   ALA D 325     4747   7018   4345  -1508   -870   -229       O  
ATOM  11625  CB  ALA D 325     122.810   2.213-199.988  1.00 40.82           C  
ANISOU11625  CB  ALA D 325     4935   6612   3963  -1742   -956   -312       C  
ATOM  11626  N   LEU D 326     121.320  -0.095-202.068  1.00 40.86           N  
ANISOU11626  N   LEU D 326     4780   6489   4258  -1228   -796   -242       N  
ATOM  11627  CA  LEU D 326     121.431  -1.322-202.852  1.00 39.88           C  
ANISOU11627  CA  LEU D 326     4486   6441   4226  -1050   -765   -201       C  
ATOM  11628  C   LEU D 326     121.681  -1.030-204.324  1.00 45.07           C  
ANISOU11628  C   LEU D 326     5099   7105   4921  -1097   -709   -202       C  
ATOM  11629  O   LEU D 326     122.170  -1.906-205.046  1.00 50.06           O  
ANISOU11629  O   LEU D 326     5559   7858   5604   -996   -690   -175       O  
ATOM  11630  CB  LEU D 326     120.145  -2.155-202.729  1.00 43.03           C  
ANISOU11630  CB  LEU D 326     4964   6679   4706   -837   -724   -190       C  
ATOM  11631  CG  LEU D 326     119.969  -3.209-201.632  1.00 46.02           C  
ANISOU11631  CG  LEU D 326     5301   7097   5088   -697   -766   -158       C  
ATOM  11632  CD1 LEU D 326     120.651  -2.800-200.388  1.00 53.36           C  
ANISOU11632  CD1 LEU D 326     6225   8138   5913   -817   -846   -163       C  
ATOM  11633  CD2 LEU D 326     118.492  -3.402-201.332  1.00 45.49           C  
ANISOU11633  CD2 LEU D 326     5394   6829   5062   -582   -720   -166       C  
ATOM  11634  N   GLY D 327     121.328   0.166-204.783  1.00 38.15           N  
ANISOU11634  N   GLY D 327     4385   6093   4016  -1241   -680   -234       N  
ATOM  11635  CA  GLY D 327     121.522   0.551-206.171  1.00 44.91           C  
ANISOU11635  CA  GLY D 327     5225   6944   4894  -1306   -627   -233       C  
ATOM  11636  C   GLY D 327     120.691  -0.254-207.142  1.00 45.30           C  
ANISOU11636  C   GLY D 327     5265   6895   5049  -1111   -559   -218       C  
ATOM  11637  O   GLY D 327     121.157  -0.562-208.246  1.00 50.00           O  
ANISOU11637  O   GLY D 327     5745   7579   5673  -1101   -522   -204       O  
ATOM  11638  N   LEU D 328     119.470  -0.603-206.761  1.00 37.09           N  
ANISOU11638  N   LEU D 328     4344   5687   4063   -962   -540   -224       N  
ATOM  11639  CA  LEU D 328     118.582  -1.345-207.633  1.00 34.94           C  
ANISOU11639  CA  LEU D 328     4077   5313   3885   -789   -481   -211       C  
ATOM  11640  C   LEU D 328     117.831  -0.394-208.555  1.00 40.62           C  
ANISOU11640  C   LEU D 328     4958   5860   4615   -847   -433   -229       C  
ATOM  11641  O   LEU D 328     117.643   0.788-208.253  1.00 36.77           O  
ANISOU11641  O   LEU D 328     4627   5273   4070   -977   -446   -255       O  
ATOM  11642  CB  LEU D 328     117.584  -2.160-206.815  1.00 35.56           C  
ANISOU11642  CB  LEU D 328     4202   5300   4009   -617   -483   -203       C  
ATOM  11643  CG  LEU D 328     118.224  -3.101-205.810  1.00 39.95           C  
ANISOU11643  CG  LEU D 328     4627   6001   4549   -551   -538   -178       C  
ATOM  11644  CD1 LEU D 328     117.148  -3.766-204.987  1.00 44.65           C  
ANISOU11644  CD1 LEU D 328     5300   6490   5176   -411   -537   -168       C  
ATOM  11645  CD2 LEU D 328     119.071  -4.125-206.517  1.00 37.57           C  
ANISOU11645  CD2 LEU D 328     4132   5855   4287   -466   -536   -150       C  
ATOM  11646  N   ARG D 329     117.400  -0.926-209.691  1.00 40.92           N  
ANISOU11646  N   ARG D 329     4966   5858   4722   -746   -382   -214       N  
ATOM  11647  CA  ARG D 329     116.567  -0.159-210.601  1.00 44.26           C  
ANISOU11647  CA  ARG D 329     5540   6115   5161   -770   -341   -223       C  
ATOM  11648  C   ARG D 329     115.810  -1.145-211.469  1.00 38.56           C  
ANISOU11648  C   ARG D 329     4779   5345   4527   -598   -295   -206       C  
ATOM  11649  O   ARG D 329     116.156  -2.325-211.534  1.00 36.73           O  
ANISOU11649  O   ARG D 329     4402   5220   4334   -489   -293   -190       O  
ATOM  11650  CB  ARG D 329     117.407   0.799-211.450  1.00 52.02           C  
ANISOU11650  CB  ARG D 329     6532   7147   6086   -961   -335   -224       C  
ATOM  11651  CG  ARG D 329     118.628   0.129-212.072  1.00 58.39           C  
ANISOU11651  CG  ARG D 329     7122   8175   6886   -986   -326   -205       C  
ATOM  11652  CD  ARG D 329     119.695   1.158-212.400  1.00 62.52           C  
ANISOU11652  CD  ARG D 329     7636   8799   7321  -1225   -339   -206       C  
ATOM  11653  NE  ARG D 329     119.282   1.999-213.520  1.00 60.79           N  
ANISOU11653  NE  ARG D 329     7554   8452   7091  -1309   -301   -201       N  
ATOM  11654  CZ  ARG D 329     119.617   3.277-213.656  1.00 63.63           C  
ANISOU11654  CZ  ARG D 329     8039   8767   7371  -1524   -317   -204       C  
ATOM  11655  NH1 ARG D 329     120.365   3.868-212.735  1.00 69.66           N  
ANISOU11655  NH1 ARG D 329     8806   9605   8058  -1685   -370   -216       N  
ATOM  11656  NH2 ARG D 329     119.192   3.965-214.706  1.00 66.75           N  
ANISOU11656  NH2 ARG D 329     8568   9036   7758  -1583   -286   -192       N  
ATOM  11657  N   TRP D 330     114.746  -0.665-212.100  1.00 30.88           N  
ANISOU11657  N   TRP D 330     3944   4208   3582   -567   -264   -210       N  
ATOM  11658  CA  TRP D 330     114.091  -1.453-213.134  1.00 29.55           C  
ANISOU11658  CA  TRP D 330     3745   4000   3484   -440   -223   -194       C  
ATOM  11659  C   TRP D 330     113.632  -0.493-214.221  1.00 35.74           C  
ANISOU11659  C   TRP D 330     4654   4670   4257   -507   -198   -193       C  
ATOM  11660  O   TRP D 330     113.693   0.736-214.070  1.00 30.92           O  
ANISOU11660  O   TRP D 330     4171   3987   3591   -632   -213   -205       O  
ATOM  11661  CB  TRP D 330     112.938  -2.331-212.584  1.00 28.03           C  
ANISOU11661  CB  TRP D 330     3571   3728   3352   -270   -219   -188       C  
ATOM  11662  CG  TRP D 330     112.729  -3.557-213.472  1.00 27.45           C  
ANISOU11662  CG  TRP D 330     3406   3682   3343   -148   -191   -170       C  
ATOM  11663  CD1 TRP D 330     111.742  -3.740-214.399  1.00 29.01           C  
ANISOU11663  CD1 TRP D 330     3657   3780   3585    -79   -160   -163       C  
ATOM  11664  CD2 TRP D 330     113.562  -4.718-213.541  1.00 31.79           C  
ANISOU11664  CD2 TRP D 330     3803   4365   3909    -85   -195   -160       C  
ATOM  11665  NE1 TRP D 330     111.906  -4.953-215.037  1.00 31.20           N  
ANISOU11665  NE1 TRP D 330     3835   4115   3903     12   -144   -152       N  
ATOM  11666  CE2 TRP D 330     113.019  -5.569-214.532  1.00 30.38           C  
ANISOU11666  CE2 TRP D 330     3609   4148   3785     18   -163   -152       C  
ATOM  11667  CE3 TRP D 330     114.709  -5.136-212.842  1.00 29.22           C  
ANISOU11667  CE3 TRP D 330     3355   4190   3555    -98   -227   -157       C  
ATOM  11668  CZ2 TRP D 330     113.592  -6.800-214.859  1.00 31.28           C  
ANISOU11668  CZ2 TRP D 330     3605   4354   3925    112   -158   -147       C  
ATOM  11669  CZ3 TRP D 330     115.276  -6.366-213.171  1.00 35.93           C  
ANISOU11669  CZ3 TRP D 330     4076   5141   4436      9   -223   -148       C  
ATOM  11670  CH2 TRP D 330     114.717  -7.179-214.173  1.00 35.95           C  
ANISOU11670  CH2 TRP D 330     4082   5087   4492    115   -187   -146       C  
ATOM  11671  N   TYR D 331     113.211  -1.056-215.347  1.00 33.09           N  
ANISOU11671  N   TYR D 331     4289   4314   3968   -428   -163   -179       N  
ATOM  11672  CA  TYR D 331     112.799  -0.214-216.453  1.00 26.20           C  
ANISOU11672  CA  TYR D 331     3530   3343   3082   -487   -143   -170       C  
ATOM  11673  C   TYR D 331     111.282  -0.054-216.488  1.00 30.77           C  
ANISOU11673  C   TYR D 331     4235   3753   3704   -374   -139   -168       C  
ATOM  11674  O   TYR D 331     110.524  -0.861-215.943  1.00 28.78           O  
ANISOU11674  O   TYR D 331     3952   3481   3501   -242   -138   -169       O  
ATOM  11675  CB  TYR D 331     113.307  -0.773-217.789  1.00 31.06           C  
ANISOU11675  CB  TYR D 331     4047   4050   3706   -490   -108   -157       C  
ATOM  11676  CG  TYR D 331     113.078  -2.246-217.970  1.00 29.61           C  
ANISOU11676  CG  TYR D 331     3745   3919   3586   -331    -90   -156       C  
ATOM  11677  CD1 TYR D 331     111.875  -2.721-218.489  1.00 30.38           C  
ANISOU11677  CD1 TYR D 331     3897   3910   3738   -214    -76   -147       C  
ATOM  11678  CD2 TYR D 331     114.063  -3.165-217.648  1.00 28.47           C  
ANISOU11678  CD2 TYR D 331     3441   3933   3443   -299    -91   -162       C  
ATOM  11679  CE1 TYR D 331     111.656  -4.073-218.675  1.00 29.37           C  
ANISOU11679  CE1 TYR D 331     3681   3817   3661    -84    -64   -147       C  
ATOM  11680  CE2 TYR D 331     113.839  -4.549-217.812  1.00 34.56           C  
ANISOU11680  CE2 TYR D 331     4129   4731   4271   -145    -79   -162       C  
ATOM  11681  CZ  TYR D 331     112.638  -4.985-218.333  1.00 37.23           C  
ANISOU11681  CZ  TYR D 331     4539   4947   4658    -48    -65   -155       C  
ATOM  11682  OH  TYR D 331     112.396  -6.332-218.526  1.00 36.38           O  
ANISOU11682  OH  TYR D 331     4373   4852   4600     86    -56   -156       O  
ATOM  11683  N   ALA D 332     110.842   1.007-217.179  1.00 33.81           N  
ANISOU11683  N   ALA D 332     4763   4021   4063   -431   -138   -161       N  
ATOM  11684  CA  ALA D 332     109.426   1.361-217.130  1.00 31.32           C  
ANISOU11684  CA  ALA D 332     4572   3551   3777   -325   -140   -160       C  
ATOM  11685  C   ALA D 332     108.574   0.407-217.958  1.00 33.62           C  
ANISOU11685  C   ALA D 332     4805   3839   4132   -196   -118   -141       C  
ATOM  11686  O   ALA D 332     107.449   0.069-217.571  1.00 32.34           O  
ANISOU11686  O   ALA D 332     4659   3618   4011    -73   -118   -141       O  
ATOM  11687  CB  ALA D 332     109.235   2.795-217.615  1.00 34.98           C  
ANISOU11687  CB  ALA D 332     5218   3883   4191   -413   -153   -155       C  
ATOM  11688  N   LEU D 333     109.098  -0.050-219.086  1.00 30.07           N  
ANISOU11688  N   LEU D 333     4282   3458   3683   -228    -99   -125       N  
ATOM  11689  CA  LEU D 333     108.254  -0.590-220.154  1.00 28.20           C  
ANISOU11689  CA  LEU D 333     4042   3188   3485   -141    -84   -106       C  
ATOM  11690  C   LEU D 333     108.427  -2.096-220.324  1.00 28.77           C  
ANISOU11690  C   LEU D 333     3969   3359   3602    -59    -65   -110       C  
ATOM  11691  O   LEU D 333     109.498  -2.538-220.771  1.00 30.81           O  
ANISOU11691  O   LEU D 333     4134   3730   3842   -108    -47   -115       O  
ATOM  11692  CB  LEU D 333     108.601   0.123-221.461  1.00 29.41           C  
ANISOU11692  CB  LEU D 333     4258   3324   3594   -241    -75    -86       C  
ATOM  11693  CG  LEU D 333     107.695  -0.266-222.631  1.00 33.16           C  
ANISOU11693  CG  LEU D 333     4750   3755   4095   -165    -67    -65       C  
ATOM  11694  CD1 LEU D 333     106.268   0.236-222.399  1.00 33.15           C  
ANISOU11694  CD1 LEU D 333     4857   3620   4119    -69    -93    -53       C  
ATOM  11695  CD2 LEU D 333     108.258   0.308-223.951  1.00 32.23           C  
ANISOU11695  CD2 LEU D 333     4677   3650   3920   -279    -55    -43       C  
ATOM  11696  N   PRO D 334     107.415  -2.930-220.003  1.00 27.32           N  
ANISOU11696  N   PRO D 334     3765   3144   3472     64    -68   -107       N  
ATOM  11697  CA  PRO D 334     107.492  -4.365-220.318  1.00 22.92           C  
ANISOU11697  CA  PRO D 334     3103   2652   2952    138    -55   -108       C  
ATOM  11698  C   PRO D 334     106.998  -4.580-221.741  1.00 25.94           C  
ANISOU11698  C   PRO D 334     3507   3008   3340    152    -41    -96       C  
ATOM  11699  O   PRO D 334     105.809  -4.418-222.030  1.00 32.49           O  
ANISOU11699  O   PRO D 334     4400   3758   4189    199    -53    -80       O  
ATOM  11700  CB  PRO D 334     106.544  -4.996-219.295  1.00 25.45           C  
ANISOU11700  CB  PRO D 334     3418   2937   3315    234    -69   -104       C  
ATOM  11701  CG  PRO D 334     105.480  -3.936-219.102  1.00 29.97           C  
ANISOU11701  CG  PRO D 334     4097   3410   3882    242    -79    -97       C  
ATOM  11702  CD  PRO D 334     106.164  -2.585-219.299  1.00 31.07           C  
ANISOU11702  CD  PRO D 334     4314   3523   3969    137    -84   -103       C  
ATOM  11703  N   ALA D 335     107.900  -4.971-222.623  1.00 26.99           N  
ANISOU11703  N   ALA D 335     3583   3221   3452    116    -17   -105       N  
ATOM  11704  CA  ALA D 335     107.586  -5.010-224.057  1.00 25.21           C  
ANISOU11704  CA  ALA D 335     3389   2978   3212    105     -3    -96       C  
ATOM  11705  C   ALA D 335     108.082  -6.340-224.616  1.00 28.79           C  
ANISOU11705  C   ALA D 335     3752   3510   3675    158     22   -118       C  
ATOM  11706  O   ALA D 335     109.260  -6.476-224.953  1.00 31.71           O  
ANISOU11706  O   ALA D 335     4053   3983   4012    118     51   -137       O  
ATOM  11707  CB  ALA D 335     108.206  -3.816-224.780  1.00 29.52           C  
ANISOU11707  CB  ALA D 335     3992   3531   3694    -19      7    -86       C  
ATOM  11708  N   VAL D 336     107.194  -7.329-224.685  1.00 25.12           N  
ANISOU11708  N   VAL D 336     3289   3002   3253    249     12   -118       N  
ATOM  11709  CA  VAL D 336     107.595  -8.673-225.072  1.00 25.37           C  
ANISOU11709  CA  VAL D 336     3260   3083   3296    314     30   -144       C  
ATOM  11710  C   VAL D 336     107.718  -8.736-226.585  1.00 31.33           C  
ANISOU11710  C   VAL D 336     4034   3858   4012    285     57   -155       C  
ATOM  11711  O   VAL D 336     106.805  -8.326-227.303  1.00 29.41           O  
ANISOU11711  O   VAL D 336     3865   3550   3760    262     43   -134       O  
ATOM  11712  CB  VAL D 336     106.592  -9.701-224.554  1.00 27.52           C  
ANISOU11712  CB  VAL D 336     3546   3292   3619    400      5   -137       C  
ATOM  11713  CG1 VAL D 336     106.819 -11.060-225.218  1.00 27.84           C  
ANISOU11713  CG1 VAL D 336     3565   3349   3664    463     19   -164       C  
ATOM  11714  CG2 VAL D 336     106.798  -9.802-223.012  1.00 31.49           C  
ANISOU11714  CG2 VAL D 336     4013   3805   4148    429    -13   -131       C  
ATOM  11715  N   SER D 337     108.839  -9.260-227.070  1.00 27.20           N  
ANISOU11715  N   SER D 337     3441   3433   3459    291     95   -188       N  
ATOM  11716  CA  SER D 337     109.131  -9.169-228.493  1.00 29.28           C  
ANISOU11716  CA  SER D 337     3719   3738   3669    247    130   -202       C  
ATOM  11717  C   SER D 337     109.402 -10.510-229.163  1.00 33.77           C  
ANISOU11717  C   SER D 337     4257   4340   4233    333    157   -246       C  
ATOM  11718  O   SER D 337     109.716 -10.527-230.365  1.00 35.02           O  
ANISOU11718  O   SER D 337     4424   4545   4337    303    193   -266       O  
ATOM  11719  CB  SER D 337     110.333  -8.243-228.716  1.00 36.24           C  
ANISOU11719  CB  SER D 337     4552   4727   4491    144    163   -203       C  
ATOM  11720  OG  SER D 337     111.397  -8.590-227.846  1.00 31.35           O  
ANISOU11720  OG  SER D 337     3824   4209   3880    173    175   -223       O  
ATOM  11721  N   ASN D 338     109.286 -11.632-228.446  1.00 31.65           N  
ANISOU11721  N   ASN D 338     3967   4044   4012    437    141   -262       N  
ATOM  11722  CA  ASN D 338     109.650 -12.912-229.038  1.00 34.90           C  
ANISOU11722  CA  ASN D 338     4367   4478   4416    528    166   -309       C  
ATOM  11723  C   ASN D 338     108.454 -13.825-229.293  1.00 28.90           C  
ANISOU11723  C   ASN D 338     3699   3597   3683    575    134   -310       C  
ATOM  11724  O   ASN D 338     108.650 -14.994-229.650  1.00 33.67           O  
ANISOU11724  O   ASN D 338     4319   4189   4283    657    145   -351       O  
ATOM  11725  CB  ASN D 338     110.688 -13.621-228.155  1.00 43.42           C  
ANISOU11725  CB  ASN D 338     5354   5629   5514    620    173   -333       C  
ATOM  11726  CG  ASN D 338     110.135 -14.022-226.818  1.00 38.06           C  
ANISOU11726  CG  ASN D 338     4692   4872   4896    669    122   -304       C  
ATOM  11727  OD1 ASN D 338     109.027 -13.646-226.459  1.00 32.54           O  
ANISOU11727  OD1 ASN D 338     4058   4082   4225    626     87   -267       O  
ATOM  11728  ND2 ASN D 338     110.914 -14.796-226.059  1.00 41.53           N  
ANISOU11728  ND2 ASN D 338     5070   5357   5353    764    117   -318       N  
ATOM  11729  N   MET D 339     107.227 -13.336-229.157  1.00 29.49           N  
ANISOU11729  N   MET D 339     3838   3588   3781    525     94   -267       N  
ATOM  11730  CA  MET D 339     106.080 -14.194-229.434  1.00 26.44           C  
ANISOU11730  CA  MET D 339     3526   3106   3411    549     61   -265       C  
ATOM  11731  C   MET D 339     105.556 -13.987-230.854  1.00 30.07           C  
ANISOU11731  C   MET D 339     4048   3555   3823    495     65   -271       C  
ATOM  11732  O   MET D 339     105.834 -12.977-231.506  1.00 31.26           O  
ANISOU11732  O   MET D 339     4195   3753   3932    429     85   -260       O  
ATOM  11733  CB  MET D 339     104.967 -13.951-228.422  1.00 27.94           C  
ANISOU11733  CB  MET D 339     3735   3229   3651    537     13   -216       C  
ATOM  11734  CG  MET D 339     105.426 -14.347-226.990  1.00 28.32           C  
ANISOU11734  CG  MET D 339     3735   3283   3740    592      4   -210       C  
ATOM  11735  SD  MET D 339     104.076 -14.293-225.788  1.00 35.72           S  
ANISOU11735  SD  MET D 339     4696   4151   4725    583    -43   -159       S  
ATOM  11736  CE  MET D 339     103.101 -15.745-226.206  1.00 30.58           C  
ANISOU11736  CE  MET D 339     4117   3422   4082    600    -72   -162       C  
ATOM  11737  N   LEU D 340     104.793 -14.973-231.319  1.00 28.96           N  
ANISOU11737  N   LEU D 340     3972   3350   3682    515     42   -285       N  
ATOM  11738  CA  LEU D 340     104.202 -14.961-232.651  1.00 27.45           C  
ANISOU11738  CA  LEU D 340     3847   3144   3440    465     36   -293       C  
ATOM  11739  C   LEU D 340     102.722 -14.610-232.546  1.00 32.62           C  
ANISOU11739  C   LEU D 340     4537   3741   4115    416    -23   -239       C  
ATOM  11740  O   LEU D 340     101.983 -15.230-231.777  1.00 33.33           O  
ANISOU11740  O   LEU D 340     4634   3779   4249    435    -58   -222       O  
ATOM  11741  CB  LEU D 340     104.383 -16.323-233.324  1.00 27.41           C  
ANISOU11741  CB  LEU D 340     3898   3111   3407    514     49   -353       C  
ATOM  11742  CG  LEU D 340     103.912 -16.518-234.782  1.00 31.49           C  
ANISOU11742  CG  LEU D 340     4493   3618   3856    465     47   -376       C  
ATOM  11743  CD1 LEU D 340     104.821 -17.531-235.483  1.00 36.43           C  
ANISOU11743  CD1 LEU D 340     5149   4259   4433    531     96   -457       C  
ATOM  11744  CD2 LEU D 340     102.466 -17.008-234.802  1.00 37.45           C  
ANISOU11744  CD2 LEU D 340     5314   4289   4626    424    -21   -347       C  
ATOM  11745  N   LEU D 341     102.284 -13.653-233.353  1.00 28.76           N  
ANISOU11745  N   LEU D 341     4070   3268   3590    354    -35   -210       N  
ATOM  11746  CA  LEU D 341     100.880 -13.265-233.417  1.00 29.03           C  
ANISOU11746  CA  LEU D 341     4130   3267   3635    320    -93   -159       C  
ATOM  11747  C   LEU D 341     100.218 -14.015-234.566  1.00 30.95           C  
ANISOU11747  C   LEU D 341     4435   3492   3831    287   -119   -176       C  
ATOM  11748  O   LEU D 341     100.676 -13.916-235.705  1.00 29.50           O  
ANISOU11748  O   LEU D 341     4289   3337   3583    258    -96   -201       O  
ATOM  11749  CB  LEU D 341     100.745 -11.758-233.636  1.00 25.45           C  
ANISOU11749  CB  LEU D 341     3676   2830   3163    282   -101   -114       C  
ATOM  11750  CG  LEU D 341      99.327 -11.263-233.940  1.00 27.67           C  
ANISOU11750  CG  LEU D 341     3982   3090   3443    262   -163    -61       C  
ATOM  11751  CD1 LEU D 341      98.401 -11.544-232.759  1.00 27.73           C  
ANISOU11751  CD1 LEU D 341     3946   3074   3513    299   -195    -37       C  
ATOM  11752  CD2 LEU D 341      99.315  -9.786-234.296  1.00 30.87           C  
ANISOU11752  CD2 LEU D 341     4413   3497   3819    236   -172    -18       C  
ATOM  11753  N   GLU D 342      99.127 -14.724-234.279  1.00 29.12           N  
ANISOU11753  N   GLU D 342     4217   3222   3624    280   -167   -161       N  
ATOM  11754  CA  GLU D 342      98.407 -15.500-235.290  1.00 29.19           C  
ANISOU11754  CA  GLU D 342     4291   3213   3586    233   -203   -176       C  
ATOM  11755  C   GLU D 342      97.002 -14.937-235.458  1.00 32.84           C  
ANISOU11755  C   GLU D 342     4738   3692   4047    187   -268   -114       C  
ATOM  11756  O   GLU D 342      96.268 -14.798-234.479  1.00 30.44           O  
ANISOU11756  O   GLU D 342     4382   3388   3795    200   -295    -74       O  
ATOM  11757  CB  GLU D 342      98.346 -16.993-234.910  1.00 30.78           C  
ANISOU11757  CB  GLU D 342     4533   3357   3803    248   -209   -214       C  
ATOM  11758  CG  GLU D 342      97.691 -17.866-235.981  1.00 50.11           C  
ANISOU11758  CG  GLU D 342     7068   5778   6193    187   -246   -240       C  
ATOM  11759  CD  GLU D 342      96.244 -18.243-235.667  1.00 68.71           C  
ANISOU11759  CD  GLU D 342     9420   8121   8564    122   -317   -194       C  
ATOM  11760  OE1 GLU D 342      95.971 -18.662-234.521  1.00 65.73           O  
ANISOU11760  OE1 GLU D 342     9014   7717   8241    135   -326   -173       O  
ATOM  11761  OE2 GLU D 342      95.379 -18.136-236.574  1.00 72.15           O  
ANISOU11761  OE2 GLU D 342     9879   8583   8952     51   -365   -176       O  
ATOM  11762  N   ILE D 343      96.628 -14.597-236.695  1.00 28.46           N  
ANISOU11762  N   ILE D 343     4224   3161   3428    139   -295   -105       N  
ATOM  11763  CA  ILE D 343      95.319 -14.011-236.966  1.00 26.22           C  
ANISOU11763  CA  ILE D 343     3920   2907   3136    106   -363    -43       C  
ATOM  11764  C   ILE D 343      94.787 -14.659-238.237  1.00 30.68           C  
ANISOU11764  C   ILE D 343     4549   3482   3627     36   -405    -59       C  
ATOM  11765  O   ILE D 343      95.399 -14.509-239.299  1.00 32.83           O  
ANISOU11765  O   ILE D 343     4880   3763   3832     14   -383    -86       O  
ATOM  11766  CB  ILE D 343      95.381 -12.484-237.165  1.00 31.93           C  
ANISOU11766  CB  ILE D 343     4629   3655   3849    126   -366      5       C  
ATOM  11767  CG1 ILE D 343      95.879 -11.741-235.910  1.00 33.44           C  
ANISOU11767  CG1 ILE D 343     4770   3832   4105    186   -330     18       C  
ATOM  11768  CG2 ILE D 343      94.029 -11.952-237.636  1.00 32.91           C  
ANISOU11768  CG2 ILE D 343     4738   3814   3952    109   -444     66       C  
ATOM  11769  CD1 ILE D 343      96.187 -10.241-236.184  1.00 29.67           C  
ANISOU11769  CD1 ILE D 343     4313   3355   3606    195   -327     56       C  
ATOM  11770  N   GLY D 344      93.650 -15.352-238.145  1.00 32.42           N  
ANISOU11770  N   GLY D 344     4758   3710   3850    -10   -464    -42       N  
ATOM  11771  CA  GLY D 344      93.038 -15.918-239.343  1.00 36.03           C  
ANISOU11771  CA  GLY D 344     5277   4183   4230    -92   -516    -53       C  
ATOM  11772  C   GLY D 344      93.937 -16.844-240.135  1.00 37.61           C  
ANISOU11772  C   GLY D 344     5582   4336   4372   -114   -476   -134       C  
ATOM  11773  O   GLY D 344      93.857 -16.883-241.377  1.00 35.05           O  
ANISOU11773  O   GLY D 344     5324   4031   3963   -167   -496   -150       O  
ATOM  11774  N   GLY D 345      94.792 -17.599-239.450  1.00 33.17           N  
ANISOU11774  N   GLY D 345     5041   3715   3848    -66   -419   -186       N  
ATOM  11775  CA  GLY D 345      95.748 -18.468-240.104  1.00 36.97           C  
ANISOU11775  CA  GLY D 345     5618   4151   4277    -55   -371   -271       C  
ATOM  11776  C   GLY D 345      97.012 -17.790-240.586  1.00 37.58           C  
ANISOU11776  C   GLY D 345     5693   4261   4324     -4   -297   -301       C  
ATOM  11777  O   GLY D 345      97.970 -18.483-240.939  1.00 41.95           O  
ANISOU11777  O   GLY D 345     6304   4792   4844     33   -241   -377       O  
ATOM  11778  N   LEU D 346      97.045 -16.465-240.639  1.00 31.30           N  
ANISOU11778  N   LEU D 346     4838   3522   3533     -1   -295   -246       N  
ATOM  11779  CA  LEU D 346      98.274 -15.754-240.952  1.00 31.74           C  
ANISOU11779  CA  LEU D 346     4883   3615   3561     30   -223   -266       C  
ATOM  11780  C   LEU D 346      99.137 -15.676-239.698  1.00 36.35           C  
ANISOU11780  C   LEU D 346     5397   4190   4225    106   -170   -274       C  
ATOM  11781  O   LEU D 346      98.625 -15.617-238.585  1.00 35.09           O  
ANISOU11781  O   LEU D 346     5186   4005   4142    130   -198   -236       O  
ATOM  11782  CB  LEU D 346      97.955 -14.351-241.470  1.00 32.17           C  
ANISOU11782  CB  LEU D 346     4922   3717   3584    -10   -249   -196       C  
ATOM  11783  CG  LEU D 346      97.064 -14.366-242.729  1.00 28.78           C  
ANISOU11783  CG  LEU D 346     4558   3307   3069    -85   -312   -178       C  
ATOM  11784  CD1 LEU D 346      96.747 -12.921-243.193  1.00 29.15           C  
ANISOU11784  CD1 LEU D 346     4600   3391   3085   -110   -346    -99       C  
ATOM  11785  CD2 LEU D 346      97.732 -15.157-243.861  1.00 32.26           C  
ANISOU11785  CD2 LEU D 346     5085   3758   3415   -114   -269   -257       C  
ATOM  11786  N   GLU D 347     100.453 -15.685-239.884  1.00 36.03           N  
ANISOU11786  N   GLU D 347     5349   4181   4158    144    -94   -325       N  
ATOM  11787  CA  GLU D 347     101.395 -15.689-238.773  1.00 32.82           C  
ANISOU11787  CA  GLU D 347     4873   3782   3816    216    -45   -339       C  
ATOM  11788  C   GLU D 347     102.297 -14.475-238.876  1.00 34.55           C  
ANISOU11788  C   GLU D 347     5039   4073   4013    200      3   -319       C  
ATOM  11789  O   GLU D 347     102.814 -14.161-239.952  1.00 30.52           O  
ANISOU11789  O   GLU D 347     4556   3618   3421    161     39   -339       O  
ATOM  11790  CB  GLU D 347     102.220 -16.976-238.767  1.00 34.30           C  
ANISOU11790  CB  GLU D 347     5088   3951   3995    288      1   -422       C  
ATOM  11791  CG  GLU D 347     101.353 -18.211-238.591  1.00 40.43           C  
ANISOU11791  CG  GLU D 347     5938   4635   4790    291    -50   -440       C  
ATOM  11792  CD  GLU D 347     102.130 -19.506-238.708  1.00 46.19           C  
ANISOU11792  CD  GLU D 347     6727   5324   5500    371    -10   -526       C  
ATOM  11793  OE1 GLU D 347     102.898 -19.654-239.687  1.00 44.72           O  
ANISOU11793  OE1 GLU D 347     6572   5181   5240    391     44   -589       O  
ATOM  11794  OE2 GLU D 347     101.973 -20.371-237.817  1.00 50.06           O  
ANISOU11794  OE2 GLU D 347     7239   5738   6044    417    -32   -531       O  
ATOM  11795  N   PHE D 348     102.488 -13.795-237.755  1.00 34.63           N  
ANISOU11795  N   PHE D 348     4982   4086   4089    221      3   -281       N  
ATOM  11796  CA  PHE D 348     103.328 -12.601-237.700  1.00 32.45           C  
ANISOU11796  CA  PHE D 348     4664   3869   3795    190     41   -257       C  
ATOM  11797  C   PHE D 348     104.419 -12.905-236.685  1.00 29.96           C  
ANISOU11797  C   PHE D 348     4270   3587   3525    252     89   -290       C  
ATOM  11798  O   PHE D 348     104.217 -12.708-235.478  1.00 29.34           O  
ANISOU11798  O   PHE D 348     4152   3479   3518    280     66   -261       O  
ATOM  11799  CB  PHE D 348     102.516 -11.365-237.317  1.00 27.84           C  
ANISOU11799  CB  PHE D 348     4086   3254   3238    151    -11   -179       C  
ATOM  11800  CG  PHE D 348     101.428 -11.044-238.283  1.00 29.18           C  
ANISOU11800  CG  PHE D 348     4323   3400   3363    104    -66   -140       C  
ATOM  11801  CD1 PHE D 348     100.186 -11.634-238.161  1.00 30.39           C  
ANISOU11801  CD1 PHE D 348     4491   3510   3548    121   -128   -125       C  
ATOM  11802  CD2 PHE D 348     101.653 -10.159-239.333  1.00 31.75           C  
ANISOU11802  CD2 PHE D 348     4698   3757   3609     36    -60   -115       C  
ATOM  11803  CE1 PHE D 348      99.176 -11.353-239.076  1.00 34.50           C  
ANISOU11803  CE1 PHE D 348     5061   4026   4021     77   -187    -87       C  
ATOM  11804  CE2 PHE D 348     100.651  -9.860-240.241  1.00 32.05           C  
ANISOU11804  CE2 PHE D 348     4800   3778   3601     -2   -120    -74       C  
ATOM  11805  CZ  PHE D 348      99.407 -10.462-240.110  1.00 33.00           C  
ANISOU11805  CZ  PHE D 348     4921   3862   3754     23   -185    -61       C  
ATOM  11806  N   PRO D 349     105.580 -13.406-237.126  1.00 32.02           N  
ANISOU11806  N   PRO D 349     4503   3920   3742    281    155   -351       N  
ATOM  11807  CA  PRO D 349     106.617 -13.801-236.155  1.00 30.89           C  
ANISOU11807  CA  PRO D 349     4275   3822   3642    355    193   -382       C  
ATOM  11808  C   PRO D 349     107.267 -12.633-235.456  1.00 35.90           C  
ANISOU11808  C   PRO D 349     4836   4514   4289    310    207   -343       C  
ATOM  11809  O   PRO D 349     107.955 -12.853-234.447  1.00 33.34           O  
ANISOU11809  O   PRO D 349     4437   4222   4008    364    220   -355       O  
ATOM  11810  CB  PRO D 349     107.643 -14.561-237.003  1.00 29.62           C  
ANISOU11810  CB  PRO D 349     4101   3739   3415    402    262   -459       C  
ATOM  11811  CG  PRO D 349     106.927 -14.855-238.336  1.00 33.25           C  
ANISOU11811  CG  PRO D 349     4663   4164   3806    359    251   -476       C  
ATOM  11812  CD  PRO D 349     105.957 -13.736-238.512  1.00 31.40           C  
ANISOU11812  CD  PRO D 349     4467   3892   3570    258    196   -398       C  
ATOM  11813  N   ALA D 350     107.094 -11.404-235.952  1.00 32.00           N  
ANISOU11813  N   ALA D 350     4371   4033   3755    209    200   -296       N  
ATOM  11814  CA  ALA D 350     107.607 -10.218-235.273  1.00 32.33           C  
ANISOU11814  CA  ALA D 350     4370   4107   3804    149    204   -256       C  
ATOM  11815  C   ALA D 350     106.443  -9.264-235.058  1.00 31.53           C  
ANISOU11815  C   ALA D 350     4343   3909   3728    105    140   -190       C  
ATOM  11816  O   ALA D 350     105.933  -8.675-236.017  1.00 30.64           O  
ANISOU11816  O   ALA D 350     4304   3774   3563     44    122   -159       O  
ATOM  11817  CB  ALA D 350     108.731  -9.564-236.075  1.00 30.35           C  
ANISOU11817  CB  ALA D 350     4090   3973   3467     62    264   -265       C  
ATOM  11818  N   ALA D 351     106.006  -9.130-233.789  1.00 27.95           N  
ANISOU11818  N   ALA D 351     3871   3401   3350    145    104   -167       N  
ATOM  11819  CA  ALA D 351     104.926  -8.223-233.439  1.00 25.27           C  
ANISOU11819  CA  ALA D 351     3590   2976   3035    128     48   -111       C  
ATOM  11820  C   ALA D 351     105.043  -7.843-231.960  1.00 25.81           C  
ANISOU11820  C   ALA D 351     3620   3024   3163    153     36    -99       C  
ATOM  11821  O   ALA D 351     104.185  -8.242-231.166  1.00 28.96           O  
ANISOU11821  O   ALA D 351     4013   3370   3619    215      3    -90       O  
ATOM  11822  CB  ALA D 351     103.563  -8.871-233.695  1.00 27.79           C  
ANISOU11822  CB  ALA D 351     3947   3230   3380    175      0    -99       C  
ATOM  11823  N   PRO D 352     106.069  -7.081-231.564  1.00 30.31           N  
ANISOU11823  N   PRO D 352     4164   3640   3711     96     63    -99       N  
ATOM  11824  CA  PRO D 352     106.271  -6.778-230.127  1.00 28.30           C  
ANISOU11824  CA  PRO D 352     3874   3374   3504    115     51    -95       C  
ATOM  11825  C   PRO D 352     105.098  -6.006-229.541  1.00 26.99           C  
ANISOU11825  C   PRO D 352     3777   3108   3370    133      2    -56       C  
ATOM  11826  O   PRO D 352     104.554  -5.105-230.172  1.00 28.67           O  
ANISOU11826  O   PRO D 352     4073   3268   3553     96    -20    -21       O  
ATOM  11827  CB  PRO D 352     107.544  -5.918-230.127  1.00 24.92           C  
ANISOU11827  CB  PRO D 352     3424   3020   3025     16     83    -97       C  
ATOM  11828  CG  PRO D 352     107.524  -5.240-231.520  1.00 29.24           C  
ANISOU11828  CG  PRO D 352     4044   3565   3498    -70     93    -74       C  
ATOM  11829  CD  PRO D 352     107.078  -6.414-232.400  1.00 27.48           C  
ANISOU11829  CD  PRO D 352     3810   3354   3276     -3    102   -100       C  
ATOM  11830  N   PHE D 353     104.751  -6.312-228.282  1.00 28.46           N  
ANISOU11830  N   PHE D 353     3930   3271   3612    195    -14    -59       N  
ATOM  11831  CA  PHE D 353     103.627  -5.641-227.654  1.00 22.43           C  
ANISOU11831  CA  PHE D 353     3219   2427   2876    228    -52    -29       C  
ATOM  11832  C   PHE D 353     104.008  -5.232-226.230  1.00 25.60           C  
ANISOU11832  C   PHE D 353     3603   2827   3299    232    -52    -37       C  
ATOM  11833  O   PHE D 353     104.878  -5.833-225.598  1.00 29.62           O  
ANISOU11833  O   PHE D 353     4040   3395   3818    234    -32    -62       O  
ATOM  11834  CB  PHE D 353     102.374  -6.522-227.641  1.00 24.76           C  
ANISOU11834  CB  PHE D 353     3500   2697   3212    304    -78    -22       C  
ATOM  11835  CG  PHE D 353     102.596  -7.907-227.052  1.00 29.32           C  
ANISOU11835  CG  PHE D 353     4005   3309   3825    350    -65    -49       C  
ATOM  11836  CD1 PHE D 353     102.508  -8.120-225.682  1.00 29.65           C  
ANISOU11836  CD1 PHE D 353     4012   3349   3905    389    -70    -50       C  
ATOM  11837  CD2 PHE D 353     102.881  -8.988-227.882  1.00 31.90           C  
ANISOU11837  CD2 PHE D 353     4314   3665   4141    356    -51    -72       C  
ATOM  11838  CE1 PHE D 353     102.714  -9.397-225.140  1.00 30.80           C  
ANISOU11838  CE1 PHE D 353     4108   3516   4079    431    -65    -67       C  
ATOM  11839  CE2 PHE D 353     103.071 -10.262-227.359  1.00 34.61           C  
ANISOU11839  CE2 PHE D 353     4615   4020   4514    406    -45    -95       C  
ATOM  11840  CZ  PHE D 353     102.990 -10.469-225.983  1.00 32.07           C  
ANISOU11840  CZ  PHE D 353     4262   3692   4232    442    -55    -89       C  
ATOM  11841  N   SER D 354     103.345  -4.201-225.733  1.00 29.19           N  
ANISOU11841  N   SER D 354     4125   3211   3755    240    -76    -17       N  
ATOM  11842  CA  SER D 354     103.730  -3.706-224.409  1.00 31.21           C  
ANISOU11842  CA  SER D 354     4381   3459   4017    234    -76    -30       C  
ATOM  11843  C   SER D 354     102.527  -3.147-223.680  1.00 26.85           C  
ANISOU11843  C   SER D 354     3881   2835   3487    304   -101    -17       C  
ATOM  11844  O   SER D 354     101.578  -2.657-224.293  1.00 29.42           O  
ANISOU11844  O   SER D 354     4266   3106   3808    338   -122      7       O  
ATOM  11845  CB  SER D 354     104.810  -2.620-224.504  1.00 23.23           C  
ANISOU11845  CB  SER D 354     3422   2450   2953    125    -68    -32       C  
ATOM  11846  OG  SER D 354     104.364  -1.535-225.314  1.00 29.84           O  
ANISOU11846  OG  SER D 354     4375   3209   3756     91    -87     -3       O  
ATOM  11847  N   GLY D 355     102.589  -3.207-222.343  1.00 30.79           N  
ANISOU11847  N   GLY D 355     4356   3342   4003    330    -98    -34       N  
ATOM  11848  CA  GLY D 355     101.588  -2.563-221.525  1.00 30.08           C  
ANISOU11848  CA  GLY D 355     4314   3193   3920    396   -112    -31       C  
ATOM  11849  C   GLY D 355     102.278  -1.798-220.422  1.00 33.28           C  
ANISOU11849  C   GLY D 355     4763   3582   4301    355   -109    -55       C  
ATOM  11850  O   GLY D 355     103.116  -0.936-220.686  1.00 30.16           O  
ANISOU11850  O   GLY D 355     4434   3162   3865    268   -111    -59       O  
ATOM  11851  N   TRP D 356     101.970  -2.148-219.176  1.00 30.71           N  
ANISOU11851  N   TRP D 356     4400   3276   3991    405   -104    -70       N  
ATOM  11852  CA  TRP D 356     102.697  -1.636-218.023  1.00 26.74           C  
ANISOU11852  CA  TRP D 356     3925   2776   3461    361   -102    -97       C  
ATOM  11853  C   TRP D 356     102.807  -2.755-216.993  1.00 29.29           C  
ANISOU11853  C   TRP D 356     4149   3175   3806    392    -94   -103       C  
ATOM  11854  O   TRP D 356     102.092  -3.760-217.048  1.00 27.04           O  
ANISOU11854  O   TRP D 356     3798   2918   3556    455    -90    -87       O  
ATOM  11855  CB  TRP D 356     102.023  -0.415-217.407  1.00 27.05           C  
ANISOU11855  CB  TRP D 356     4079   2726   3473    399   -110   -112       C  
ATOM  11856  CG  TRP D 356     100.589  -0.588-217.067  1.00 25.74           C  
ANISOU11856  CG  TRP D 356     3899   2548   3333    522   -104   -107       C  
ATOM  11857  CD1 TRP D 356     100.070  -1.198-215.956  1.00 29.73           C  
ANISOU11857  CD1 TRP D 356     4343   3103   3850    580    -89   -117       C  
ATOM  11858  CD2 TRP D 356      99.471  -0.114-217.826  1.00 29.39           C  
ANISOU11858  CD2 TRP D 356     4406   2957   3804    601   -114    -88       C  
ATOM  11859  NE1 TRP D 356      98.700  -1.154-215.992  1.00 27.55           N  
ANISOU11859  NE1 TRP D 356     4058   2820   3590    684    -84   -108       N  
ATOM  11860  CE2 TRP D 356      98.304  -0.482-217.121  1.00 30.65           C  
ANISOU11860  CE2 TRP D 356     4512   3152   3983    706   -102    -90       C  
ATOM  11861  CE3 TRP D 356      99.343   0.563-219.049  1.00 35.55           C  
ANISOU11861  CE3 TRP D 356     5262   3673   4573    591   -135    -65       C  
ATOM  11862  CZ2 TRP D 356      97.028  -0.194-217.586  1.00 33.43           C  
ANISOU11862  CZ2 TRP D 356     4868   3488   4345    807   -110    -73       C  
ATOM  11863  CZ3 TRP D 356      98.058   0.872-219.510  1.00 36.13           C  
ANISOU11863  CZ3 TRP D 356     5354   3716   4657    699   -149    -45       C  
ATOM  11864  CH2 TRP D 356      96.921   0.497-218.781  1.00 37.69           C  
ANISOU11864  CH2 TRP D 356     5482   3961   4876    809   -137    -51       C  
ATOM  11865  N   TYR D 357     103.714  -2.568-216.041  1.00 30.63           N  
ANISOU11865  N   TYR D 357     4316   3376   3948    339    -98   -123       N  
ATOM  11866  CA  TYR D 357     104.038  -3.648-215.115  1.00 31.00           C  
ANISOU11866  CA  TYR D 357     4273   3499   4008    359    -98   -123       C  
ATOM  11867  C   TYR D 357     102.997  -3.828-214.026  1.00 30.32           C  
ANISOU11867  C   TYR D 357     4192   3402   3925    433    -92   -125       C  
ATOM  11868  O   TYR D 357     102.419  -2.861-213.525  1.00 31.86           O  
ANISOU11868  O   TYR D 357     4467   3544   4095    453    -87   -143       O  
ATOM  11869  CB  TYR D 357     105.379  -3.386-214.454  1.00 25.49           C  
ANISOU11869  CB  TYR D 357     3560   2855   3272    276   -111   -141       C  
ATOM  11870  CG  TYR D 357     106.548  -4.035-215.137  1.00 28.82           C  
ANISOU11870  CG  TYR D 357     3894   3358   3698    231   -112   -134       C  
ATOM  11871  CD1 TYR D 357     106.677  -5.426-215.163  1.00 29.68           C  
ANISOU11871  CD1 TYR D 357     3909   3526   3842    291   -111   -119       C  
ATOM  11872  CD2 TYR D 357     107.542  -3.265-215.739  1.00 26.59           C  
ANISOU11872  CD2 TYR D 357     3627   3098   3379    128   -113   -142       C  
ATOM  11873  CE1 TYR D 357     107.761  -6.032-215.771  1.00 29.25           C  
ANISOU11873  CE1 TYR D 357     3773   3551   3789    272   -109   -120       C  
ATOM  11874  CE2 TYR D 357     108.645  -3.867-216.352  1.00 27.38           C  
ANISOU11874  CE2 TYR D 357     3629   3298   3477     93   -107   -139       C  
ATOM  11875  CZ  TYR D 357     108.738  -5.257-216.356  1.00 30.77           C  
ANISOU11875  CZ  TYR D 357     3962   3786   3945    177   -104   -131       C  
ATOM  11876  OH  TYR D 357     109.813  -5.885-216.927  1.00 30.36           O  
ANISOU11876  OH  TYR D 357     3811   3835   3888    168    -95   -135       O  
ATOM  11877  N   MET D 358     102.786  -5.087-213.631  1.00 31.25           N  
ANISOU11877  N   MET D 358     4232   3573   4070    472    -91   -105       N  
ATOM  11878  CA  MET D 358     102.254  -5.380-212.307  1.00 28.89           C  
ANISOU11878  CA  MET D 358     3925   3296   3756    508    -86   -106       C  
ATOM  11879  C   MET D 358     103.430  -5.564-211.352  1.00 33.52           C  
ANISOU11879  C   MET D 358     4489   3936   4312    460   -104   -114       C  
ATOM  11880  O   MET D 358     104.438  -6.169-211.716  1.00 32.80           O  
ANISOU11880  O   MET D 358     4343   3889   4231    431   -119   -105       O  
ATOM  11881  CB  MET D 358     101.366  -6.620-212.349  1.00 30.87           C  
ANISOU11881  CB  MET D 358     4117   3572   4041    559    -79    -73       C  
ATOM  11882  CG  MET D 358     100.798  -7.019-210.955  1.00 37.96           C  
ANISOU11882  CG  MET D 358     5002   4506   4915    584    -71    -65       C  
ATOM  11883  SD  MET D 358      99.563  -8.317-211.063  1.00 44.82           S  
ANISOU11883  SD  MET D 358     5816   5400   5813    620    -62    -22       S  
ATOM  11884  CE  MET D 358     100.608  -9.771-211.193  1.00 39.56           C  
ANISOU11884  CE  MET D 358     5113   4749   5168    595    -92      6       C  
ATOM  11885  N   SER D 359     103.315  -5.020-210.125  1.00 30.68           N  
ANISOU11885  N   SER D 359     4170   3578   3907    454   -103   -134       N  
ATOM  11886  CA  SER D 359     104.518  -4.828-209.315  1.00 29.38           C  
ANISOU11886  CA  SER D 359     4003   3462   3700    389   -128   -149       C  
ATOM  11887  C   SER D 359     105.160  -6.144-208.898  1.00 28.88           C  
ANISOU11887  C   SER D 359     3850   3476   3648    399   -151   -117       C  
ATOM  11888  O   SER D 359     106.388  -6.206-208.745  1.00 29.82           O  
ANISOU11888  O   SER D 359     3930   3654   3748    350   -178   -120       O  
ATOM  11889  CB  SER D 359     104.205  -3.975-208.069  1.00 31.76           C  
ANISOU11889  CB  SER D 359     4381   3746   3941    380   -123   -182       C  
ATOM  11890  OG  SER D 359     102.982  -4.380-207.476  1.00 31.53           O  
ANISOU11890  OG  SER D 359     4350   3717   3914    456    -97   -172       O  
ATOM  11891  N   THR D 360     104.367  -7.204-208.705  1.00 27.38           N  
ANISOU11891  N   THR D 360     3630   3290   3484    460   -143    -86       N  
ATOM  11892  CA  THR D 360     104.969  -8.485-208.336  1.00 32.77           C  
ANISOU11892  CA  THR D 360     4250   4026   4176    478   -170    -52       C  
ATOM  11893  C   THR D 360     105.882  -9.030-209.430  1.00 31.54           C  
ANISOU11893  C   THR D 360     4039   3890   4057    481   -183    -46       C  
ATOM  11894  O   THR D 360     106.776  -9.826-209.137  1.00 29.48           O  
ANISOU11894  O   THR D 360     3725   3683   3793    497   -212    -29       O  
ATOM  11895  CB  THR D 360     103.893  -9.531-208.015  1.00 33.43           C  
ANISOU11895  CB  THR D 360     4330   4097   4277    527   -160    -15       C  
ATOM  11896  OG1 THR D 360     102.963  -9.615-209.109  1.00 33.88           O  
ANISOU11896  OG1 THR D 360     4391   4105   4376    551   -135    -11       O  
ATOM  11897  CG2 THR D 360     103.153  -9.199-206.723  1.00 30.57           C  
ANISOU11897  CG2 THR D 360     4004   3748   3864    525   -146    -16       C  
ATOM  11898  N   GLU D 361     105.693  -8.638-210.692  1.00 28.97           N  
ANISOU11898  N   GLU D 361     3722   3526   3760    475   -162    -59       N  
ATOM  11899  CA  GLU D 361     106.635  -9.118-211.695  1.00 28.29           C  
ANISOU11899  CA  GLU D 361     3580   3472   3696    476   -168    -60       C  
ATOM  11900  C   GLU D 361     108.044  -8.654-211.367  1.00 28.08           C  
ANISOU11900  C   GLU D 361     3509   3527   3633    422   -189    -76       C  
ATOM  11901  O   GLU D 361     109.006  -9.418-211.483  1.00 30.41           O  
ANISOU11901  O   GLU D 361     3730   3892   3933    448   -206    -69       O  
ATOM  11902  CB  GLU D 361     106.238  -8.641-213.092  1.00 28.29           C  
ANISOU11902  CB  GLU D 361     3605   3425   3719    463   -142    -72       C  
ATOM  11903  CG  GLU D 361     104.865  -9.103-213.524  1.00 30.64           C  
ANISOU11903  CG  GLU D 361     3933   3659   4049    510   -127    -55       C  
ATOM  11904  CD  GLU D 361     104.474  -8.508-214.875  1.00 35.40           C  
ANISOU11904  CD  GLU D 361     4566   4220   4665    494   -109    -65       C  
ATOM  11905  OE1 GLU D 361     104.886  -9.064-215.917  1.00 33.43           O  
ANISOU11905  OE1 GLU D 361     4289   3980   4432    499   -105    -66       O  
ATOM  11906  OE2 GLU D 361     103.776  -7.467-214.889  1.00 38.38           O  
ANISOU11906  OE2 GLU D 361     4997   4553   5030    481   -101    -72       O  
ATOM  11907  N   ILE D 362     108.183  -7.397-210.975  1.00 28.62           N  
ANISOU11907  N   ILE D 362     3623   3591   3660    347   -189   -100       N  
ATOM  11908  CA  ILE D 362     109.499  -6.859-210.656  1.00 26.29           C  
ANISOU11908  CA  ILE D 362     3287   3381   3321    269   -213   -114       C  
ATOM  11909  C   ILE D 362     109.913  -7.284-209.256  1.00 30.82           C  
ANISOU11909  C   ILE D 362     3831   4018   3862    279   -250   -103       C  
ATOM  11910  O   ILE D 362     111.006  -7.817-209.045  1.00 33.25           O  
ANISOU11910  O   ILE D 362     4049   4426   4157    282   -280    -92       O  
ATOM  11911  CB  ILE D 362     109.486  -5.322-210.757  1.00 24.40           C  
ANISOU11911  CB  ILE D 362     3133   3096   3040    169   -205   -144       C  
ATOM  11912  CG1 ILE D 362     109.066  -4.866-212.162  1.00 25.51           C  
ANISOU11912  CG1 ILE D 362     3315   3172   3207    158   -174   -148       C  
ATOM  11913  CG2 ILE D 362     110.852  -4.759-210.442  1.00 30.73           C  
ANISOU11913  CG2 ILE D 362     3893   3995   3788     61   -233   -158       C  
ATOM  11914  CD1 ILE D 362     108.694  -3.416-212.167  1.00 30.11           C  
ANISOU11914  CD1 ILE D 362     4019   3668   3752     89   -169   -171       C  
ATOM  11915  N   GLY D 363     109.046  -7.020-208.285  1.00 30.70           N  
ANISOU11915  N   GLY D 363     3888   3951   3825    287   -248   -104       N  
ATOM  11916  CA  GLY D 363     109.459  -7.125-206.889  1.00 27.61           C  
ANISOU11916  CA  GLY D 363     3489   3618   3382    270   -285    -98       C  
ATOM  11917  C   GLY D 363     109.628  -8.559-206.426  1.00 34.12           C  
ANISOU11917  C   GLY D 363     4250   4489   4224    352   -312    -55       C  
ATOM  11918  O   GLY D 363     110.514  -8.859-205.622  1.00 46.57           O  
ANISOU11918  O   GLY D 363     5778   6153   5765    342   -357    -41       O  
ATOM  11919  N   THR D 364     108.784  -9.462-206.918  1.00 34.62           N  
ANISOU11919  N   THR D 364     4321   4493   4339    429   -291    -30       N  
ATOM  11920  CA  THR D 364     108.823 -10.839-206.451  1.00 34.22           C  
ANISOU11920  CA  THR D 364     4243   4459   4301    503   -319     15       C  
ATOM  11921  C   THR D 364     109.605 -11.737-207.399  1.00 35.27           C  
ANISOU11921  C   THR D 364     4306   4619   4477    564   -331     26       C  
ATOM  11922  O   THR D 364     110.524 -12.435-206.977  1.00 35.44           O  
ANISOU11922  O   THR D 364     4270   4708   4485    607   -374     47       O  
ATOM  11923  CB  THR D 364     107.405 -11.381-206.268  1.00 33.87           C  
ANISOU11923  CB  THR D 364     4259   4335   4274    539   -293     39       C  
ATOM  11924  OG1 THR D 364     106.650 -10.502-205.425  1.00 33.40           O  
ANISOU11924  OG1 THR D 364     4257   4262   4170    496   -272     22       O  
ATOM  11925  CG2 THR D 364     107.457 -12.773-205.624  1.00 32.26           C  
ANISOU11925  CG2 THR D 364     4051   4137   4068    596   -329     93       C  
ATOM  11926  N   ARG D 365     109.256 -11.749-208.686  1.00 29.71           N  
ANISOU11926  N   ARG D 365     3606   3865   3818    577   -294     10       N  
ATOM  11927  CA  ARG D 365     109.944 -12.661-209.588  1.00 28.46           C  
ANISOU11927  CA  ARG D 365     3391   3729   3693    646   -300     13       C  
ATOM  11928  C   ARG D 365     111.323 -12.135-209.977  1.00 34.54           C  
ANISOU11928  C   ARG D 365     4070   4611   4444    615   -307    -13       C  
ATOM  11929  O   ARG D 365     112.340 -12.793-209.728  1.00 35.06           O  
ANISOU11929  O   ARG D 365     4059   4763   4501    672   -340     -2       O  
ATOM  11930  CB  ARG D 365     109.081 -12.903-210.840  1.00 31.48           C  
ANISOU11930  CB  ARG D 365     3814   4026   4122    664   -260      4       C  
ATOM  11931  CG  ARG D 365     107.650 -13.363-210.502  1.00 35.68           C  
ANISOU11931  CG  ARG D 365     4423   4465   4668    675   -252     31       C  
ATOM  11932  CD  ARG D 365     107.621 -14.669-209.690  1.00 32.66           C  
ANISOU11932  CD  ARG D 365     4060   4067   4283    736   -289     75       C  
ATOM  11933  NE  ARG D 365     108.538 -15.677-210.218  1.00 36.59           N  
ANISOU11933  NE  ARG D 365     4525   4579   4800    818   -311     77       N  
ATOM  11934  CZ  ARG D 365     108.296 -16.412-211.303  1.00 38.04           C  
ANISOU11934  CZ  ARG D 365     4733   4702   5019    863   -296     69       C  
ATOM  11935  NH1 ARG D 365     107.146 -16.280-211.964  1.00 34.57           N  
ANISOU11935  NH1 ARG D 365     4345   4191   4599    822   -265     64       N  
ATOM  11936  NH2 ARG D 365     109.201 -17.279-211.722  1.00 35.44           N  
ANISOU11936  NH2 ARG D 365     4378   4389   4700    951   -314     63       N  
ATOM  11937  N   ASN D 366     111.375 -10.957-210.613  1.00 35.10           N  
ANISOU11937  N   ASN D 366     4146   4688   4504    526   -276    -45       N  
ATOM  11938  CA  ASN D 366     112.643 -10.483-211.161  1.00 32.41           C  
ANISOU11938  CA  ASN D 366     3716   4460   4140    478   -275    -68       C  
ATOM  11939  C   ASN D 366     113.685 -10.246-210.074  1.00 36.43           C  
ANISOU11939  C   ASN D 366     4155   5088   4597    440   -323    -62       C  
ATOM  11940  O   ASN D 366     114.868 -10.548-210.268  1.00 38.86           O  
ANISOU11940  O   ASN D 366     4349   5525   4892    459   -339    -64       O  
ATOM  11941  CB  ASN D 366     112.427  -9.206-211.974  1.00 33.80           C  
ANISOU11941  CB  ASN D 366     3936   4603   4304    371   -239    -95       C  
ATOM  11942  CG  ASN D 366     111.539  -9.426-213.189  1.00 32.81           C  
ANISOU11942  CG  ASN D 366     3863   4383   4222    407   -197    -99       C  
ATOM  11943  OD1 ASN D 366     111.224 -10.563-213.552  1.00 35.07           O  
ANISOU11943  OD1 ASN D 366     4141   4637   4545    504   -193    -88       O  
ATOM  11944  ND2 ASN D 366     111.111  -8.335-213.804  1.00 33.37           N  
ANISOU11944  ND2 ASN D 366     3998   4400   4283    327   -172   -114       N  
ATOM  11945  N   LEU D 367     113.282  -9.696-208.930  1.00 31.03           N  
ANISOU11945  N   LEU D 367     3534   4378   3879    386   -346    -56       N  
ATOM  11946  CA  LEU D 367     114.284  -9.386-207.916  1.00 36.39           C  
ANISOU11946  CA  LEU D 367     4153   5177   4499    332   -396    -53       C  
ATOM  11947  C   LEU D 367     114.498 -10.500-206.894  1.00 39.31           C  
ANISOU11947  C   LEU D 367     4488   5586   4862    428   -448    -13       C  
ATOM  11948  O   LEU D 367     115.607 -10.610-206.358  1.00 37.75           O  
ANISOU11948  O   LEU D 367     4195   5523   4626    422   -497     -3       O  
ATOM  11949  CB  LEU D 367     113.923  -8.082-207.191  1.00 32.21           C  
ANISOU11949  CB  LEU D 367     3715   4608   3917    208   -399    -76       C  
ATOM  11950  CG  LEU D 367     114.055  -6.805-208.048  1.00 36.11           C  
ANISOU11950  CG  LEU D 367     4244   5081   4394     87   -366   -112       C  
ATOM  11951  CD1 LEU D 367     113.623  -5.548-207.284  1.00 31.69           C  
ANISOU11951  CD1 LEU D 367     3806   4455   3780    -19   -372   -139       C  
ATOM  11952  CD2 LEU D 367     115.479  -6.654-208.567  1.00 37.92           C  
ANISOU11952  CD2 LEU D 367     4347   5464   4598     22   -381   -117       C  
ATOM  11953  N   CYS D 368     113.491 -11.338-206.613  1.00 33.59           N  
ANISOU11953  N   CYS D 368     3837   4756   4169    513   -443     14       N  
ATOM  11954  CA  CYS D 368     113.619 -12.356-205.565  1.00 36.29           C  
ANISOU11954  CA  CYS D 368     4174   5119   4494    592   -496     60       C  
ATOM  11955  C   CYS D 368     113.691 -13.803-206.042  1.00 35.07           C  
ANISOU11955  C   CYS D 368     4000   4935   4388    733   -506     91       C  
ATOM  11956  O   CYS D 368     113.953 -14.677-205.208  1.00 36.48           O  
ANISOU11956  O   CYS D 368     4177   5133   4549    806   -560    134       O  
ATOM  11957  CB  CYS D 368     112.455 -12.262-204.568  1.00 40.44           C  
ANISOU11957  CB  CYS D 368     4812   5557   4997    567   -492     77       C  
ATOM  11958  SG  CYS D 368     112.326 -10.695-203.697  1.00 39.08           S  
ANISOU11958  SG  CYS D 368     4691   5404   4752    425   -488     39       S  
ATOM  11959  N   ASP D 369     113.426 -14.112-207.318  1.00 31.87           N  
ANISOU11959  N   ASP D 369     3599   4473   4037    775   -461     71       N  
ATOM  11960  CA  ASP D 369     113.629 -15.491-207.747  1.00 31.38           C  
ANISOU11960  CA  ASP D 369     3529   4383   4011    913   -477     93       C  
ATOM  11961  C   ASP D 369     115.074 -15.884-207.455  1.00 35.14           C  
ANISOU11961  C   ASP D 369     3886   5004   4464    987   -528    102       C  
ATOM  11962  O   ASP D 369     115.991 -15.098-207.724  1.00 38.48           O  
ANISOU11962  O   ASP D 369     4202   5557   4863    930   -522     72       O  
ATOM  11963  CB  ASP D 369     113.366 -15.688-209.247  1.00 29.50           C  
ANISOU11963  CB  ASP D 369     3299   4088   3822    942   -422     59       C  
ATOM  11964  CG  ASP D 369     111.900 -15.989-209.591  1.00 38.25           C  
ANISOU11964  CG  ASP D 369     4528   5042   4964    931   -390     68       C  
ATOM  11965  OD1 ASP D 369     111.014 -16.011-208.717  1.00 36.12           O  
ANISOU11965  OD1 ASP D 369     4331   4711   4681    896   -401     98       O  
ATOM  11966  OD2 ASP D 369     111.637 -16.194-210.795  1.00 36.34           O  
ANISOU11966  OD2 ASP D 369     4299   4751   4756    951   -352     43       O  
ATOM  11967  N   PRO D 370     115.314 -17.093-206.928  1.00 39.29           N  
ANISOU11967  N   PRO D 370     4425   5513   4990   1113   -580    145       N  
ATOM  11968  CA  PRO D 370     116.701 -17.523-206.671  1.00 42.07           C  
ANISOU11968  CA  PRO D 370     4653   6013   5320   1209   -634    155       C  
ATOM  11969  C   PRO D 370     117.547 -17.588-207.926  1.00 46.87           C  
ANISOU11969  C   PRO D 370     5150   6708   5951   1272   -597    109       C  
ATOM  11970  O   PRO D 370     118.780 -17.488-207.844  1.00 41.14           O  
ANISOU11970  O   PRO D 370     4279   6156   5197   1308   -625    103       O  
ATOM  11971  CB  PRO D 370     116.539 -18.918-206.041  1.00 47.06           C  
ANISOU11971  CB  PRO D 370     5363   6560   5956   1350   -691    213       C  
ATOM  11972  CG  PRO D 370     115.074 -19.093-205.776  1.00 53.61           C  
ANISOU11972  CG  PRO D 370     6354   7217   6799   1289   -670    236       C  
ATOM  11973  CD  PRO D 370     114.336 -18.165-206.691  1.00 45.29           C  
ANISOU11973  CD  PRO D 370     5317   6120   5773   1177   -590    185       C  
ATOM  11974  N   HIS D 371     116.921 -17.771-209.085  1.00 44.08           N  
ANISOU11974  N   HIS D 371     4856   6250   5642   1285   -534     77       N  
ATOM  11975  CA  HIS D 371     117.624 -17.838-210.357  1.00 45.73           C  
ANISOU11975  CA  HIS D 371     4974   6535   5867   1339   -488     29       C  
ATOM  11976  C   HIS D 371     117.541 -16.529-211.126  1.00 46.11           C  
ANISOU11976  C   HIS D 371     4986   6629   5906   1182   -427    -13       C  
ATOM  11977  O   HIS D 371     117.825 -16.497-212.328  1.00 44.70           O  
ANISOU11977  O   HIS D 371     4763   6482   5739   1198   -373    -54       O  
ATOM  11978  CB  HIS D 371     117.078 -18.995-211.200  1.00 40.76           C  
ANISOU11978  CB  HIS D 371     4444   5762   5282   1465   -465     19       C  
ATOM  11979  CG  HIS D 371     115.593 -18.951-211.418  1.00 44.61           C  
ANISOU11979  CG  HIS D 371     5087   6066   5798   1386   -436     26       C  
ATOM  11980  ND1 HIS D 371     114.682 -19.083-210.391  1.00 43.76           N  
ANISOU11980  ND1 HIS D 371     5084   5857   5686   1341   -470     74       N  
ATOM  11981  CD2 HIS D 371     114.863 -18.815-212.552  1.00 41.82           C  
ANISOU11981  CD2 HIS D 371     4794   5626   5472   1345   -377     -8       C  
ATOM  11982  CE1 HIS D 371     113.455 -19.020-210.880  1.00 38.75           C  
ANISOU11982  CE1 HIS D 371     4555   5090   5076   1276   -432     69       C  
ATOM  11983  NE2 HIS D 371     113.538 -18.856-212.190  1.00 45.16           N  
ANISOU11983  NE2 HIS D 371     5344   5905   5908   1278   -379     20       N  
ATOM  11984  N   ARG D 372     117.116 -15.456-210.473  1.00 39.68           N  
ANISOU11984  N   ARG D 372     4204   5806   5067   1031   -432     -4       N  
ATOM  11985  CA  ARG D 372     117.199 -14.133-211.076  1.00 33.98           C  
ANISOU11985  CA  ARG D 372     3453   5132   4325    878   -386    -39       C  
ATOM  11986  C   ARG D 372     118.127 -13.289-210.207  1.00 39.07           C  
ANISOU11986  C   ARG D 372     4001   5932   4910    777   -427    -34       C  
ATOM  11987  O   ARG D 372     119.222 -13.745-209.861  1.00 37.68           O  
ANISOU11987  O   ARG D 372     3700   5906   4712    847   -468    -23       O  
ATOM  11988  CB  ARG D 372     115.809 -13.519-211.221  1.00 30.19           C  
ANISOU11988  CB  ARG D 372     3117   4490   3865    787   -352    -42       C  
ATOM  11989  CG  ARG D 372     114.880 -14.300-212.141  1.00 31.93           C  
ANISOU11989  CG  ARG D 372     3425   4571   4138    864   -316    -48       C  
ATOM  11990  CD  ARG D 372     115.310 -14.198-213.643  1.00 29.13           C  
ANISOU11990  CD  ARG D 372     3018   4260   3791    868   -261    -89       C  
ATOM  11991  NE  ARG D 372     115.184 -12.841-214.189  1.00 34.83           N  
ANISOU11991  NE  ARG D 372     3747   4995   4491    719   -224   -110       N  
ATOM  11992  CZ  ARG D 372     114.033 -12.226-214.459  1.00 41.92           C  
ANISOU11992  CZ  ARG D 372     4756   5768   5403    648   -201   -110       C  
ATOM  11993  NH1 ARG D 372     112.869 -12.834-214.241  1.00 39.88           N  
ANISOU11993  NH1 ARG D 372     4596   5376   5180    700   -207    -91       N  
ATOM  11994  NH2 ARG D 372     114.044 -10.991-214.959  1.00 40.69           N  
ANISOU11994  NH2 ARG D 372     4613   5624   5222    523   -174   -126       N  
ATOM  11995  N   TYR D 373     117.716 -12.076-209.827  1.00 38.20           N  
ANISOU11995  N   TYR D 373     3951   5791   4770    619   -422    -41       N  
ATOM  11996  CA  TYR D 373     118.636 -11.217-209.084  1.00 36.64           C  
ANISOU11996  CA  TYR D 373     3673   5741   4508    501   -462    -42       C  
ATOM  11997  C   TYR D 373     118.826 -11.693-207.644  1.00 37.81           C  
ANISOU11997  C   TYR D 373     3814   5925   4627    547   -537     -5       C  
ATOM  11998  O   TYR D 373     119.863 -11.406-207.031  1.00 38.04           O  
ANISOU11998  O   TYR D 373     3734   6118   4602    498   -587      2       O  
ATOM  11999  CB  TYR D 373     118.153  -9.768-209.121  1.00 34.45           C  
ANISOU11999  CB  TYR D 373     3488   5402   4201    319   -437    -66       C  
ATOM  12000  CG  TYR D 373     118.544  -9.042-210.396  1.00 37.01           C  
ANISOU12000  CG  TYR D 373     3774   5771   4519    227   -384    -97       C  
ATOM  12001  CD1 TYR D 373     117.730  -9.093-211.522  1.00 32.93           C  
ANISOU12001  CD1 TYR D 373     3333   5130   4048    255   -324   -110       C  
ATOM  12002  CD2 TYR D 373     119.733  -8.324-210.481  1.00 38.15           C  
ANISOU12002  CD2 TYR D 373     3803   6089   4603    103   -395   -108       C  
ATOM  12003  CE1 TYR D 373     118.084  -8.436-212.696  1.00 38.62           C  
ANISOU12003  CE1 TYR D 373     4027   5892   4754    166   -277   -133       C  
ATOM  12004  CE2 TYR D 373     120.089  -7.665-211.646  1.00 40.59           C  
ANISOU12004  CE2 TYR D 373     4083   6444   4898      4   -345   -130       C  
ATOM  12005  CZ  TYR D 373     119.265  -7.729-212.750  1.00 38.28           C  
ANISOU12005  CZ  TYR D 373     3876   6019   4650     40   -285   -142       C  
ATOM  12006  OH  TYR D 373     119.611  -7.068-213.914  1.00 32.74           O  
ANISOU12006  OH  TYR D 373     3154   5362   3925    -63   -236   -159       O  
ATOM  12007  N   ASN D 374     117.848 -12.412-207.087  1.00 36.84           N  
ANISOU12007  N   ASN D 374     3804   5662   4533    631   -549     24       N  
ATOM  12008  CA  ASN D 374     118.062 -13.191-205.861  1.00 37.90           C  
ANISOU12008  CA  ASN D 374     3932   5827   4643    712   -621     69       C  
ATOM  12009  C   ASN D 374     118.524 -12.311-204.690  1.00 37.79           C  
ANISOU12009  C   ASN D 374     3897   5911   4551    585   -673     74       C  
ATOM  12010  O   ASN D 374     119.538 -12.585-204.035  1.00 36.78           O  
ANISOU12010  O   ASN D 374     3662   5933   4381    613   -739     97       O  
ATOM  12011  CB  ASN D 374     119.066 -14.320-206.140  1.00 40.33           C  
ANISOU12011  CB  ASN D 374     4117   6242   4966    873   -654     88       C  
ATOM  12012  CG  ASN D 374     119.237 -15.267-204.958  1.00 43.63           C  
ANISOU12012  CG  ASN D 374     4546   6670   5362    981   -734    145       C  
ATOM  12013  OD1 ASN D 374     118.298 -15.494-204.199  1.00 44.83           O  
ANISOU12013  OD1 ASN D 374     4827   6696   5510    973   -747    175       O  
ATOM  12014  ND2 ASN D 374     120.441 -15.815-204.797  1.00 40.86           N  
ANISOU12014  ND2 ASN D 374     4056   6479   4992   1084   -789    162       N  
ATOM  12015  N   ILE D 375     117.770 -11.242-204.414  1.00 35.16           N  
ANISOU12015  N   ILE D 375     3671   5493   4194    450   -646     49       N  
ATOM  12016  CA  ILE D 375     118.181 -10.274-203.385  1.00 39.55           C  
ANISOU12016  CA  ILE D 375     4230   6128   4669    311   -689     40       C  
ATOM  12017  C   ILE D 375     117.526 -10.518-202.024  1.00 34.81           C  
ANISOU12017  C   ILE D 375     3729   5467   4030    324   -727     69       C  
ATOM  12018  O   ILE D 375     117.796  -9.762-201.073  1.00 37.89           O  
ANISOU12018  O   ILE D 375     4139   5913   4343    212   -766     59       O  
ATOM  12019  CB  ILE D 375     117.904  -8.821-203.826  1.00 39.97           C  
ANISOU12019  CB  ILE D 375     4353   6133   4701    145   -643    -12       C  
ATOM  12020  CG1 ILE D 375     116.398  -8.527-203.799  1.00 42.33           C  
ANISOU12020  CG1 ILE D 375     4820   6237   5026    148   -591    -25       C  
ATOM  12021  CG2 ILE D 375     118.470  -8.553-205.224  1.00 36.88           C  
ANISOU12021  CG2 ILE D 375     3877   5796   4341    118   -599    -35       C  
ATOM  12022  CD1 ILE D 375     116.046  -7.074-204.048  1.00 39.29           C  
ANISOU12022  CD1 ILE D 375     4532   5784   4612      3   -555    -74       C  
ATOM  12023  N   LEU D 376     116.698 -11.559-201.889  1.00 36.48           N  
ANISOU12023  N   LEU D 376     4007   5570   4282    446   -719    105       N  
ATOM  12024  CA  LEU D 376     115.850 -11.696-200.707  1.00 40.30           C  
ANISOU12024  CA  LEU D 376     4604   5982   4727    440   -735    130       C  
ATOM  12025  C   LEU D 376     116.674 -11.761-199.422  1.00 45.99           C  
ANISOU12025  C   LEU D 376     5281   6829   5364    415   -821    160       C  
ATOM  12026  O   LEU D 376     116.396 -11.039-198.451  1.00 41.93           O  
ANISOU12026  O   LEU D 376     4839   6315   4778    315   -834    146       O  
ATOM  12027  CB  LEU D 376     114.976 -12.940-200.850  1.00 41.96           C  
ANISOU12027  CB  LEU D 376     4877   6074   4991    567   -719    173       C  
ATOM  12028  CG  LEU D 376     113.797 -13.050-199.897  1.00 52.32           C  
ANISOU12028  CG  LEU D 376     6317   7292   6272    549   -707    195       C  
ATOM  12029  CD1 LEU D 376     112.877 -11.862-200.114  1.00 46.29           C  
ANISOU12029  CD1 LEU D 376     5630   6453   5504    450   -637    139       C  
ATOM  12030  CD2 LEU D 376     113.072 -14.354-200.131  1.00 46.21           C  
ANISOU12030  CD2 LEU D 376     5594   6415   5547    658   -698    245       C  
ATOM  12031  N   GLU D 377     117.700 -12.617-199.399  1.00 38.62           N  
ANISOU12031  N   GLU D 377     4231   6011   4434    511   -884    200       N  
ATOM  12032  CA  GLU D 377     118.470 -12.807-198.169  1.00 43.53           C  
ANISOU12032  CA  GLU D 377     4805   6759   4974    505   -978    239       C  
ATOM  12033  C   GLU D 377     119.182 -11.520-197.768  1.00 41.48           C  
ANISOU12033  C   GLU D 377     4499   6625   4638    335  -1003    197       C  
ATOM  12034  O   GLU D 377     119.207 -11.156-196.586  1.00 44.58           O  
ANISOU12034  O   GLU D 377     4938   7056   4944    257  -1052    205       O  
ATOM  12035  CB  GLU D 377     119.472 -13.944-198.368  1.00 48.44           C  
ANISOU12035  CB  GLU D 377     5299   7486   5619    661  -1040    287       C  
ATOM  12036  CG  GLU D 377     120.028 -14.561-197.090  1.00 65.54           C  
ANISOU12036  CG  GLU D 377     7443   9745   7713    713  -1144    352       C  
ATOM  12037  CD  GLU D 377     121.104 -15.600-197.378  1.00 81.29           C  
ANISOU12037  CD  GLU D 377     9301  11855   9733    885  -1208    394       C  
ATOM  12038  OE1 GLU D 377     122.153 -15.233-197.949  1.00 89.55           O  
ANISOU12038  OE1 GLU D 377    10183  13062  10779    874  -1216    366       O  
ATOM  12039  OE2 GLU D 377     120.895 -16.787-197.048  1.00 86.50           O  
ANISOU12039  OE2 GLU D 377    10018  12443  10407   1034  -1247    456       O  
ATOM  12040  N   ASP D 378     119.750 -10.803-198.745  1.00 44.08           N  
ANISOU12040  N   ASP D 378     4744   7015   4988    264   -970    151       N  
ATOM  12041  CA  ASP D 378     120.494  -9.584-198.439  1.00 42.33           C  
ANISOU12041  CA  ASP D 378     4482   6913   4689     83   -998    113       C  
ATOM  12042  C   ASP D 378     119.589  -8.516-197.830  1.00 40.87           C  
ANISOU12042  C   ASP D 378     4470   6606   4453    -53   -967     70       C  
ATOM  12043  O   ASP D 378     119.977  -7.833-196.873  1.00 44.18           O  
ANISOU12043  O   ASP D 378     4912   7098   4778   -177  -1020     56       O  
ATOM  12044  CB  ASP D 378     121.181  -9.059-199.699  1.00 59.86           C  
ANISOU12044  CB  ASP D 378     6593   9208   6941     25   -959     77       C  
ATOM  12045  CG  ASP D 378     122.207  -7.977-199.392  1.00 81.14           C  
ANISOU12045  CG  ASP D 378     9213  12066   9548   -167  -1005     50       C  
ATOM  12046  OD1 ASP D 378     122.914  -8.099-198.367  1.00 89.25           O  
ANISOU12046  OD1 ASP D 378    10175  13234  10501   -193  -1093     77       O  
ATOM  12047  OD2 ASP D 378     122.315  -7.009-200.176  1.00 87.43           O  
ANISOU12047  OD2 ASP D 378    10022  12854  10345   -299   -959      6       O  
ATOM  12048  N   VAL D 379     118.379  -8.367-198.368  1.00 38.22           N  
ANISOU12048  N   VAL D 379     4259   6089   4175    -26   -884     45       N  
ATOM  12049  CA  VAL D 379     117.419  -7.408-197.832  1.00 36.20           C  
ANISOU12049  CA  VAL D 379     4169   5710   3875   -121   -846      1       C  
ATOM  12050  C   VAL D 379     117.009  -7.803-196.420  1.00 39.95           C  
ANISOU12050  C   VAL D 379     4715   6181   4282    -97   -886     30       C  
ATOM  12051  O   VAL D 379     116.923  -6.951-195.527  1.00 39.63           O  
ANISOU12051  O   VAL D 379     4763   6143   4153   -210   -903     -5       O  
ATOM  12052  CB  VAL D 379     116.203  -7.303-198.771  1.00 36.64           C  
ANISOU12052  CB  VAL D 379     4317   5591   4012    -69   -752    -22       C  
ATOM  12053  CG1 VAL D 379     115.106  -6.443-198.165  1.00 35.88           C  
ANISOU12053  CG1 VAL D 379     4389   5371   3873   -126   -711    -65       C  
ATOM  12054  CG2 VAL D 379     116.634  -6.755-200.130  1.00 37.03           C  
ANISOU12054  CG2 VAL D 379     4313   5647   4110   -116   -715    -52       C  
ATOM  12055  N   ALA D 380     116.751  -9.098-196.197  1.00 42.79           N  
ANISOU12055  N   ALA D 380     5052   6531   4677     44   -903     93       N  
ATOM  12056  CA  ALA D 380     116.337  -9.571-194.876  1.00 38.76           C  
ANISOU12056  CA  ALA D 380     4613   6017   4097     66   -940    131       C  
ATOM  12057  C   ALA D 380     117.430  -9.358-193.847  1.00 46.55           C  
ANISOU12057  C   ALA D 380     5541   7164   4980     -9  -1038    145       C  
ATOM  12058  O   ALA D 380     117.146  -9.002-192.695  1.00 42.50           O  
ANISOU12058  O   ALA D 380     5119   6655   4373    -78  -1061    138       O  
ATOM  12059  CB  ALA D 380     115.960 -11.051-194.933  1.00 37.37           C  
ANISOU12059  CB  ALA D 380     4426   5796   3976    225   -948    205       C  
ATOM  12060  N   VAL D 381     118.686  -9.592-194.233  1.00 43.43           N  
ANISOU12060  N   VAL D 381     4991   6915   4597      4  -1099    165       N  
ATOM  12061  CA  VAL D 381     119.800  -9.315-193.329  1.00 49.61           C  
ANISOU12061  CA  VAL D 381     5696   7876   5278    -82  -1199    177       C  
ATOM  12062  C   VAL D 381     119.821  -7.837-192.960  1.00 50.30           C  
ANISOU12062  C   VAL D 381     5865   7965   5282   -282  -1190    103       C  
ATOM  12063  O   VAL D 381     119.936  -7.476-191.785  1.00 44.84           O  
ANISOU12063  O   VAL D 381     5233   7323   4482   -369  -1243     98       O  
ATOM  12064  CB  VAL D 381     121.128  -9.765-193.962  1.00 50.77           C  
ANISOU12064  CB  VAL D 381     5639   8196   5456    -29  -1255    206       C  
ATOM  12065  CG1 VAL D 381     122.305  -9.276-193.144  1.00 49.89           C  
ANISOU12065  CG1 VAL D 381     5430   8289   5235   -148  -1356    210       C  
ATOM  12066  CG2 VAL D 381     121.165 -11.286-194.080  1.00 52.57           C  
ANISOU12066  CG2 VAL D 381     5810   8418   5745    183  -1282    281       C  
ATOM  12067  N   CYS D 382     119.678  -6.959-193.961  1.00 44.79           N  
ANISOU12067  N   CYS D 382     5188   7201   4629   -358  -1121     43       N  
ATOM  12068  CA  CYS D 382     119.654  -5.522-193.698  1.00 47.85           C  
ANISOU12068  CA  CYS D 382     5682   7560   4940   -547  -1110    -31       C  
ATOM  12069  C   CYS D 382     118.469  -5.123-192.826  1.00 52.53           C  
ANISOU12069  C   CYS D 382     6471   8009   5479   -560  -1070    -65       C  
ATOM  12070  O   CYS D 382     118.583  -4.194-192.017  1.00 47.74           O  
ANISOU12070  O   CYS D 382     5961   7413   4767   -699  -1096   -113       O  
ATOM  12071  CB  CYS D 382     119.626  -4.746-195.014  1.00 53.58           C  
ANISOU12071  CB  CYS D 382     6412   8218   5729   -608  -1043    -78       C  
ATOM  12072  SG  CYS D 382     121.112  -4.921-195.998  1.00 55.28           S  
ANISOU12072  SG  CYS D 382     6397   8631   5975   -640  -1082    -55       S  
ATOM  12073  N   MET D 383     117.327  -5.797-192.980  1.00 47.02           N  
ANISOU12073  N   MET D 383     5835   7183   4848   -423  -1004    -44       N  
ATOM  12074  CA  MET D 383     116.166  -5.555-192.128  1.00 46.30           C  
ANISOU12074  CA  MET D 383     5907   6982   4705   -417   -959    -71       C  
ATOM  12075  C   MET D 383     116.342  -6.113-190.729  1.00 47.83           C  
ANISOU12075  C   MET D 383     6111   7263   4799   -413  -1029    -27       C  
ATOM  12076  O   MET D 383     115.436  -5.956-189.902  1.00 45.04           O  
ANISOU12076  O   MET D 383     5886   6843   4384   -414   -993    -47       O  
ATOM  12077  CB  MET D 383     114.906  -6.159-192.753  1.00 46.75           C  
ANISOU12077  CB  MET D 383     6005   6899   4859   -281   -870    -55       C  
ATOM  12078  CG  MET D 383     114.436  -5.436-193.983  1.00 44.23           C  
ANISOU12078  CG  MET D 383     5720   6467   4619   -290   -792   -107       C  
ATOM  12079  SD  MET D 383     113.097  -6.356-194.778  1.00 43.60           S  
ANISOU12079  SD  MET D 383     5651   6260   4654   -129   -707    -73       S  
ATOM  12080  CE  MET D 383     111.798  -6.292-193.554  1.00 47.98           C  
ANISOU12080  CE  MET D 383     6344   6752   5133   -110   -662    -87       C  
ATOM  12081  N   ASP D 384     117.477  -6.761-190.466  1.00 42.74           N  
ANISOU12081  N   ASP D 384     5332   6775   4134   -403  -1126     32       N  
ATOM  12082  CA  ASP D 384     117.786  -7.380-189.177  1.00 49.23           C  
ANISOU12082  CA  ASP D 384     6150   7696   4859   -393  -1210     88       C  
ATOM  12083  C   ASP D 384     116.797  -8.488-188.821  1.00 47.29           C  
ANISOU12083  C   ASP D 384     5961   7367   4638   -256  -1178    149       C  
ATOM  12084  O   ASP D 384     116.454  -8.685-187.654  1.00 51.54           O  
ANISOU12084  O   ASP D 384     6581   7921   5080   -271  -1202    171       O  
ATOM  12085  CB  ASP D 384     117.858  -6.334-188.064  1.00 49.03           C  
ANISOU12085  CB  ASP D 384     6237   7703   4689   -551  -1238     29       C  
ATOM  12086  CG  ASP D 384     118.572  -6.849-186.842  1.00 69.50           C  
ANISOU12086  CG  ASP D 384     8790  10446   7171   -571  -1351     87       C  
ATOM  12087  OD1 ASP D 384     119.605  -7.535-187.010  1.00 74.75           O  
ANISOU12087  OD1 ASP D 384     9295  11249   7858   -523  -1437    152       O  
ATOM  12088  OD2 ASP D 384     118.097  -6.572-185.723  1.00 78.14           O  
ANISOU12088  OD2 ASP D 384    10011  11526   8152   -626  -1354     68       O  
ATOM  12089  N   LEU D 385     116.344  -9.237-189.815  1.00 44.01           N  
ANISOU12089  N   LEU D 385     5507   6868   4346   -132  -1125    180       N  
ATOM  12090  CA  LEU D 385     115.486 -10.382-189.561  1.00 50.87           C  
ANISOU12090  CA  LEU D 385     6425   7663   5241    -15  -1104    247       C  
ATOM  12091  C   LEU D 385     116.331 -11.623-189.274  1.00 48.71           C  
ANISOU12091  C   LEU D 385     6058   7483   4967     85  -1205    344       C  
ATOM  12092  O   LEU D 385     117.495 -11.726-189.676  1.00 45.67           O  
ANISOU12092  O   LEU D 385     5540   7209   4605    104  -1271    357       O  
ATOM  12093  CB  LEU D 385     114.558 -10.631-190.755  1.00 42.34           C  
ANISOU12093  CB  LEU D 385     5361   6442   4285     64  -1006    234       C  
ATOM  12094  CG  LEU D 385     113.729  -9.426-191.211  1.00 40.44           C  
ANISOU12094  CG  LEU D 385     5202   6104   4058     -8   -908    143       C  
ATOM  12095  CD1 LEU D 385     112.905  -9.763-192.464  1.00 37.05           C  
ANISOU12095  CD1 LEU D 385     4769   5555   3753     76   -826    140       C  
ATOM  12096  CD2 LEU D 385     112.841  -8.929-190.084  1.00 49.60           C  
ANISOU12096  CD2 LEU D 385     6497   7234   5116    -65   -872    112       C  
ATOM  12097  N   ASP D 386     115.728 -12.576-188.576  1.00 49.31           N  
ANISOU12097  N   ASP D 386     6206   7516   5013    151  -1217    415       N  
ATOM  12098  CA  ASP D 386     116.420 -13.807-188.197  1.00 53.18           C  
ANISOU12098  CA  ASP D 386     6642   8070   5493    257  -1318    516       C  
ATOM  12099  C   ASP D 386     116.327 -14.786-189.359  1.00 51.45           C  
ANISOU12099  C   ASP D 386     6377   7766   5406    401  -1294    551       C  
ATOM  12100  O   ASP D 386     115.322 -15.479-189.516  1.00 49.31           O  
ANISOU12100  O   ASP D 386     6195   7366   5173    455  -1241    583       O  
ATOM  12101  CB  ASP D 386     115.809 -14.390-186.927  1.00 60.12           C  
ANISOU12101  CB  ASP D 386     7640   8931   6272    252  -1344    581       C  
ATOM  12102  CG  ASP D 386     116.405 -15.741-186.550  1.00 68.23           C  
ANISOU12102  CG  ASP D 386     8640   9994   7289    375  -1450    696       C  
ATOM  12103  OD1 ASP D 386     117.460 -16.124-187.101  1.00 71.74           O  
ANISOU12103  OD1 ASP D 386     8960  10512   7787    465  -1517    718       O  
ATOM  12104  OD2 ASP D 386     115.804 -16.425-185.696  1.00 71.31           O  
ANISOU12104  OD2 ASP D 386     9141  10341   7614    384  -1465    765       O  
ATOM  12105  N   THR D 387     117.391 -14.871-190.157  1.00 57.70           N  
ANISOU12105  N   THR D 387     7028   8638   6258    461  -1333    545       N  
ATOM  12106  CA  THR D 387     117.392 -15.682-191.371  1.00 62.72           C  
ANISOU12106  CA  THR D 387     7616   9199   7014    597  -1304    560       C  
ATOM  12107  C   THR D 387     117.820 -17.129-191.129  1.00 63.84           C  
ANISOU12107  C   THR D 387     7750   9342   7164    759  -1389    658       C  
ATOM  12108  O   THR D 387     117.953 -17.891-192.093  1.00 63.11           O  
ANISOU12108  O   THR D 387     7623   9192   7164    888  -1377    671       O  
ATOM  12109  CB  THR D 387     118.289 -15.046-192.445  1.00 62.89           C  
ANISOU12109  CB  THR D 387     7491   9309   7095    586  -1290    499       C  
ATOM  12110  OG1 THR D 387     119.650 -15.018-192.004  1.00 70.63           O  
ANISOU12110  OG1 THR D 387     8336  10480   8019    592  -1394    521       O  
ATOM  12111  CG2 THR D 387     117.831 -13.623-192.765  1.00 55.23           C  
ANISOU12111  CG2 THR D 387     6555   8311   6120    428  -1208    406       C  
ATOM  12112  N   ARG D 388     118.019 -17.529-189.878  1.00 69.95           N  
ANISOU12112  N   ARG D 388     8568  10169   7839    758  -1475    727       N  
ATOM  12113  CA  ARG D 388     118.482 -18.878-189.578  1.00 77.19           C  
ANISOU12113  CA  ARG D 388     9493  11084   8754    918  -1569    827       C  
ATOM  12114  C   ARG D 388     117.351 -19.865-189.323  1.00 74.17           C  
ANISOU12114  C   ARG D 388     9283  10524   8376    959  -1544    893       C  
ATOM  12115  O   ARG D 388     117.607 -21.073-189.281  1.00 83.23           O  
ANISOU12115  O   ARG D 388    10466  11620   9537   1101  -1611    975       O  
ATOM  12116  CB  ARG D 388     119.419 -18.857-188.372  1.00 74.69           C  
ANISOU12116  CB  ARG D 388     9127  10933   8320    904  -1694    879       C  
ATOM  12117  CG  ARG D 388     120.837 -18.436-188.709  1.00 78.79           C  
ANISOU12117  CG  ARG D 388     9445  11649   8844    930  -1759    851       C  
ATOM  12118  CD  ARG D 388     121.443 -17.579-187.612  1.00 88.16           C  
ANISOU12118  CD  ARG D 388    10585  13008   9902    789  -1832    843       C  
ATOM  12119  NE  ARG D 388     121.261 -18.149-186.277  1.00 93.96           N  
ANISOU12119  NE  ARG D 388    11429  13744  10528    794  -1916    930       N  
ATOM  12120  CZ  ARG D 388     120.314 -17.770-185.422  1.00 88.66           C  
ANISOU12120  CZ  ARG D 388    10910  13001   9775    666  -1876    924       C  
ATOM  12121  NH1 ARG D 388     119.453 -16.820-185.763  1.00 86.70           N  
ANISOU12121  NH1 ARG D 388    10723  12673   9548    537  -1757    833       N  
ATOM  12122  NH2 ARG D 388     120.222 -18.343-184.229  1.00 86.98           N  
ANISOU12122  NH2 ARG D 388    10790  12802   9455    672  -1956   1010       N  
ATOM  12123  N   THR D 389     116.120 -19.392-189.145  1.00 60.05           N  
ANISOU12123  N   THR D 389     7604   8642   6571    838  -1451    861       N  
ATOM  12124  CA  THR D 389     114.960 -20.266-189.027  1.00 59.60           C  
ANISOU12124  CA  THR D 389     7698   8426   6521    852  -1412    918       C  
ATOM  12125  C   THR D 389     113.899 -19.833-190.029  1.00 56.10           C  
ANISOU12125  C   THR D 389     7280   7873   6164    801  -1283    846       C  
ATOM  12126  O   THR D 389     113.614 -18.635-190.158  1.00 49.45           O  
ANISOU12126  O   THR D 389     6404   7070   5316    696  -1214    761       O  
ATOM  12127  CB  THR D 389     114.390 -20.263-187.601  1.00 65.66           C  
ANISOU12127  CB  THR D 389     8580   9210   7157    754  -1432    969       C  
ATOM  12128  OG1 THR D 389     113.188 -21.043-187.566  1.00 74.02           O  
ANISOU12128  OG1 THR D 389     9778  10124   8222    743  -1381   1020       O  
ATOM  12129  CG2 THR D 389     114.086 -18.849-187.140  1.00 59.17           C  
ANISOU12129  CG2 THR D 389     7743   8468   6270    600  -1371    882       C  
ATOM  12130  N   THR D 390     113.327 -20.812-190.746  1.00 46.88           N  
ANISOU12130  N   THR D 390     6177   6565   5070    878  -1257    881       N  
ATOM  12131  CA  THR D 390     112.249 -20.513-191.684  1.00 47.34           C  
ANISOU12131  CA  THR D 390     6262   6521   5203    831  -1143    823       C  
ATOM  12132  C   THR D 390     111.020 -19.974-190.968  1.00 39.80           C  
ANISOU12132  C   THR D 390     5391   5551   4182    695  -1070    812       C  
ATOM  12133  O   THR D 390     110.255 -19.195-191.548  1.00 39.14           O  
ANISOU12133  O   THR D 390     5294   5440   4138    633   -974    739       O  
ATOM  12134  CB  THR D 390     111.865 -21.763-192.487  1.00 51.70           C  
ANISOU12134  CB  THR D 390     6885   6927   5833    927  -1141    870       C  
ATOM  12135  OG1 THR D 390     111.521 -22.826-191.586  1.00 54.78           O  
ANISOU12135  OG1 THR D 390     7405   7253   6155    936  -1197    974       O  
ATOM  12136  CG2 THR D 390     113.011 -22.215-193.386  1.00 47.74           C  
ANISOU12136  CG2 THR D 390     6295   6438   5407   1077  -1191    860       C  
ATOM  12137  N   SER D 391     110.818 -20.350-189.703  1.00 42.06           N  
ANISOU12137  N   SER D 391     5760   5861   4359    653  -1113    882       N  
ATOM  12138  CA  SER D 391     109.535 -20.036-189.091  1.00 44.94           C  
ANISOU12138  CA  SER D 391     6208   6208   4660    537  -1033    877       C  
ATOM  12139  C   SER D 391     109.427 -18.583-188.647  1.00 43.83           C  
ANISOU12139  C   SER D 391     6026   6164   4462    440   -980    786       C  
ATOM  12140  O   SER D 391     108.349 -18.167-188.214  1.00 41.81           O  
ANISOU12140  O   SER D 391     5826   5906   4156    357   -900    763       O  
ATOM  12141  CB  SER D 391     109.258 -20.973-187.912  1.00 42.69           C  
ANISOU12141  CB  SER D 391     6039   5913   4269    513  -1088    986       C  
ATOM  12142  OG  SER D 391     110.242 -20.826-186.910  1.00 43.54           O  
ANISOU12142  OG  SER D 391     6130   6129   4283    518  -1182   1015       O  
ATOM  12143  N   SER D 392     110.499 -17.798-188.747  1.00 41.04           N  
ANISOU12143  N   SER D 392     5583   5898   4112    448  -1021    732       N  
ATOM  12144  CA  SER D 392     110.353 -16.364-188.532  1.00 39.05           C  
ANISOU12144  CA  SER D 392     5311   5707   3819    354   -964    633       C  
ATOM  12145  C   SER D 392     109.666 -15.684-189.708  1.00 41.02           C  
ANISOU12145  C   SER D 392     5534   5885   4166    348   -862    552       C  
ATOM  12146  O   SER D 392     109.252 -14.523-189.591  1.00 37.75           O  
ANISOU12146  O   SER D 392     5133   5488   3722    278   -798    470       O  
ATOM  12147  CB  SER D 392     111.718 -15.723-188.287  1.00 45.27           C  
ANISOU12147  CB  SER D 392     6018   6611   4572    340  -1045    603       C  
ATOM  12148  OG  SER D 392     112.500 -15.755-189.467  1.00 47.03           O  
ANISOU12148  OG  SER D 392     6135   6832   4903    410  -1062    581       O  
ATOM  12149  N   LEU D 393     109.510 -16.397-190.819  1.00 34.24           N  
ANISOU12149  N   LEU D 393     4650   4941   3418    424   -847    573       N  
ATOM  12150  CA  LEU D 393     108.923 -15.836-192.041  1.00 34.77           C  
ANISOU12150  CA  LEU D 393     4687   4941   3581    427   -761    503       C  
ATOM  12151  C   LEU D 393     109.707 -14.622-192.532  1.00 35.70           C  
ANISOU12151  C   LEU D 393     4732   5112   3720    399   -758    418       C  
ATOM  12152  O   LEU D 393     109.132 -13.667-193.073  1.00 35.85           O  
ANISOU12152  O   LEU D 393     4755   5098   3767    361   -682    345       O  
ATOM  12153  CB  LEU D 393     107.437 -15.496-191.834  1.00 37.92           C  
ANISOU12153  CB  LEU D 393     5153   5300   3956    369   -663    480       C  
ATOM  12154  CG  LEU D 393     106.616 -16.718-191.388  1.00 43.02           C  
ANISOU12154  CG  LEU D 393     5871   5901   4575    372   -662    570       C  
ATOM  12155  CD1 LEU D 393     105.113 -16.444-191.456  1.00 38.31           C  
ANISOU12155  CD1 LEU D 393     5306   5278   3972    322   -557    546       C  
ATOM  12156  CD2 LEU D 393     106.981 -17.961-192.233  1.00 38.48           C  
ANISOU12156  CD2 LEU D 393     5289   5244   4086    456   -711    633       C  
ATOM  12157  N   TRP D 394     111.035 -14.661-192.362  1.00 35.73           N  
ANISOU12157  N   TRP D 394     4667   5202   3707    417   -844    431       N  
ATOM  12158  CA  TRP D 394     111.876 -13.580-192.867  1.00 37.55           C  
ANISOU12158  CA  TRP D 394     4821   5494   3952    374   -848    358       C  
ATOM  12159  C   TRP D 394     111.766 -13.449-194.384  1.00 37.93           C  
ANISOU12159  C   TRP D 394     4820   5476   4117    414   -793    319       C  
ATOM  12160  O   TRP D 394     111.834 -12.339-194.918  1.00 36.67           O  
ANISOU12160  O   TRP D 394     4644   5317   3972    352   -753    247       O  
ATOM  12161  CB  TRP D 394     113.337 -13.786-192.461  1.00 35.85           C  
ANISOU12161  CB  TRP D 394     4518   5406   3698    389   -954    388       C  
ATOM  12162  CG  TRP D 394     113.999 -15.035-192.985  1.00 41.93           C  
ANISOU12162  CG  TRP D 394     5220   6179   4531    521  -1012    455       C  
ATOM  12163  CD1 TRP D 394     114.059 -16.259-192.367  1.00 45.42           C  
ANISOU12163  CD1 TRP D 394     5699   6610   4948    604  -1076    544       C  
ATOM  12164  CD2 TRP D 394     114.719 -15.180-194.223  1.00 42.27           C  
ANISOU12164  CD2 TRP D 394     5157   6238   4665    591  -1011    435       C  
ATOM  12165  NE1 TRP D 394     114.765 -17.146-193.145  1.00 46.19           N  
ANISOU12165  NE1 TRP D 394     5726   6705   5118    733  -1116    577       N  
ATOM  12166  CE2 TRP D 394     115.180 -16.511-194.286  1.00 41.17           C  
ANISOU12166  CE2 TRP D 394     4995   6094   4553    728  -1074    508       C  
ATOM  12167  CE3 TRP D 394     115.021 -14.313-195.278  1.00 38.75           C  
ANISOU12167  CE3 TRP D 394     4640   5810   4274    550   -963    363       C  
ATOM  12168  CZ2 TRP D 394     115.916 -16.996-195.369  1.00 41.55           C  
ANISOU12168  CZ2 TRP D 394     4947   6160   4681    836  -1084    504       C  
ATOM  12169  CZ3 TRP D 394     115.753 -14.795-196.349  1.00 44.66           C  
ANISOU12169  CZ3 TRP D 394     5287   6585   5098    642   -972    364       C  
ATOM  12170  CH2 TRP D 394     116.196 -16.121-196.384  1.00 45.27           C  
ANISOU12170  CH2 TRP D 394     5337   6664   5200    789  -1029    429       C  
ATOM  12171  N   LYS D 395     111.588 -14.563-195.099  1.00 32.11           N  
ANISOU12171  N   LYS D 395     4071   4672   3455    511   -792    366       N  
ATOM  12172  CA  LYS D 395     111.466 -14.468-196.558  1.00 36.78           C  
ANISOU12172  CA  LYS D 395     4622   5204   4149    547   -740    328       C  
ATOM  12173  C   LYS D 395     110.222 -13.683-196.950  1.00 34.07           C  
ANISOU12173  C   LYS D 395     4341   4780   3826    490   -647    276       C  
ATOM  12174  O   LYS D 395     110.268 -12.809-197.825  1.00 35.36           O  
ANISOU12174  O   LYS D 395     4476   4929   4029    461   -605    216       O  
ATOM  12175  CB  LYS D 395     111.431 -15.860-197.188  1.00 42.63           C  
ANISOU12175  CB  LYS D 395     5362   5878   4956    661   -758    385       C  
ATOM  12176  CG  LYS D 395     112.765 -16.567-197.218  1.00 48.38           C  
ANISOU12176  CG  LYS D 395     6010   6683   5690    753   -841    420       C  
ATOM  12177  CD  LYS D 395     112.661 -17.843-198.041  1.00 52.82           C  
ANISOU12177  CD  LYS D 395     6591   7152   6325    875   -846    458       C  
ATOM  12178  CE  LYS D 395     113.929 -18.664-197.951  1.00 49.14           C  
ANISOU12178  CE  LYS D 395     6056   6758   5857    996   -932    499       C  
ATOM  12179  NZ  LYS D 395     113.801 -19.915-198.753  1.00 54.84           N  
ANISOU12179  NZ  LYS D 395     6822   7371   6645   1125   -935    528       N  
ATOM  12180  N   ASP D 396     109.099 -13.983-196.293  1.00 34.16           N  
ANISOU12180  N   ASP D 396     4433   4743   3802    476   -615    303       N  
ATOM  12181  CA  ASP D 396     107.843 -13.311-196.584  1.00 33.28           C  
ANISOU12181  CA  ASP D 396     4370   4571   3704    439   -527    258       C  
ATOM  12182  C   ASP D 396     107.928 -11.823-196.257  1.00 34.04           C  
ANISOU12182  C   ASP D 396     4483   4702   3750    366   -501    181       C  
ATOM  12183  O   ASP D 396     107.435 -10.979-197.013  1.00 30.03           O  
ANISOU12183  O   ASP D 396     3985   4145   3281    353   -444    125       O  
ATOM  12184  CB  ASP D 396     106.729 -13.987-195.781  1.00 33.41           C  
ANISOU12184  CB  ASP D 396     4455   4565   3675    432   -503    308       C  
ATOM  12185  CG  ASP D 396     106.816 -15.521-195.824  1.00 40.57           C  
ANISOU12185  CG  ASP D 396     5375   5435   4606    488   -551    395       C  
ATOM  12186  OD1 ASP D 396     106.017 -16.144-196.559  1.00 44.87           O  
ANISOU12186  OD1 ASP D 396     5937   5904   5209    509   -516    415       O  
ATOM  12187  OD2 ASP D 396     107.702 -16.102-195.151  1.00 40.30           O  
ANISOU12187  OD2 ASP D 396     5338   5442   4530    512   -628    444       O  
ATOM  12188  N   LYS D 397     108.546 -11.484-195.118  1.00 37.70           N  
ANISOU12188  N   LYS D 397     4962   5242   4121    317   -548    179       N  
ATOM  12189  CA  LYS D 397     108.637 -10.088-194.698  1.00 35.03           C  
ANISOU12189  CA  LYS D 397     4665   4926   3720    238   -529    103       C  
ATOM  12190  C   LYS D 397     109.535  -9.267-195.624  1.00 36.43           C  
ANISOU12190  C   LYS D 397     4793   5110   3940    204   -542     53       C  
ATOM  12191  O   LYS D 397     109.201  -8.123-195.974  1.00 36.24           O  
ANISOU12191  O   LYS D 397     4817   5038   3914    160   -496    -14       O  
ATOM  12192  CB  LYS D 397     109.135 -10.029-193.248  1.00 32.80           C  
ANISOU12192  CB  LYS D 397     4414   4730   3319    184   -585    117       C  
ATOM  12193  CG  LYS D 397     108.135 -10.661-192.294  1.00 35.62           C  
ANISOU12193  CG  LYS D 397     4835   5083   3617    198   -558    159       C  
ATOM  12194  CD  LYS D 397     108.669 -10.803-190.852  1.00 48.63           C  
ANISOU12194  CD  LYS D 397     6514   6821   5141    150   -623    188       C  
ATOM  12195  CE  LYS D 397     108.503  -9.513-190.050  1.00 55.80           C  
ANISOU12195  CE  LYS D 397     7500   7755   5948     69   -595    105       C  
ATOM  12196  NZ  LYS D 397     108.723  -9.734-188.586  1.00 69.77           N  
ANISOU12196  NZ  LYS D 397     9318   9609   7584     21   -643    135       N  
ATOM  12197  N   ALA D 398     110.677  -9.824-196.036  1.00 33.53           N  
ANISOU12197  N   ALA D 398     4331   4803   3605    225   -605     87       N  
ATOM  12198  CA  ALA D 398     111.554  -9.097-196.948  1.00 36.76           C  
ANISOU12198  CA  ALA D 398     4681   5238   4048    182   -613     45       C  
ATOM  12199  C   ALA D 398     110.895  -8.925-198.309  1.00 38.87           C  
ANISOU12199  C   ALA D 398     4952   5409   4408    217   -544     21       C  
ATOM  12200  O   ALA D 398     110.981  -7.851-198.924  1.00 33.71           O  
ANISOU12200  O   ALA D 398     4319   4727   3763    156   -516    -33       O  
ATOM  12201  CB  ALA D 398     112.889  -9.825-197.090  1.00 36.34           C  
ANISOU12201  CB  ALA D 398     4507   5294   4007    213   -689     89       C  
ATOM  12202  N   ALA D 399     110.204  -9.961-198.775  1.00 37.46           N  
ANISOU12202  N   ALA D 399     4767   5174   4294    308   -520     64       N  
ATOM  12203  CA  ALA D 399     109.582  -9.891-200.091  1.00 31.66           C  
ANISOU12203  CA  ALA D 399     4031   4355   3642    341   -462     46       C  
ATOM  12204  C   ALA D 399     108.494  -8.823-200.135  1.00 33.50           C  
ANISOU12204  C   ALA D 399     4351   4513   3863    306   -397     -6       C  
ATOM  12205  O   ALA D 399     108.373  -8.079-201.126  1.00 29.65           O  
ANISOU12205  O   ALA D 399     3874   3977   3416    289   -364    -45       O  
ATOM  12206  CB  ALA D 399     109.030 -11.261-200.473  1.00 29.89           C  
ANISOU12206  CB  ALA D 399     3795   4085   3476    432   -456    102       C  
ATOM  12207  N   VAL D 400     107.703  -8.717-199.071  1.00 30.67           N  
ANISOU12207  N   VAL D 400     4059   4148   3445    299   -379     -7       N  
ATOM  12208  CA  VAL D 400     106.679  -7.676-199.027  1.00 34.01           C  
ANISOU12208  CA  VAL D 400     4563   4510   3848    286   -316    -62       C  
ATOM  12209  C   VAL D 400     107.321  -6.291-199.081  1.00 36.31           C  
ANISOU12209  C   VAL D 400     4901   4794   4102    209   -325   -128       C  
ATOM  12210  O   VAL D 400     106.871  -5.415-199.832  1.00 32.19           O  
ANISOU12210  O   VAL D 400     4426   4197   3606    208   -285   -171       O  
ATOM  12211  CB  VAL D 400     105.780  -7.845-197.786  1.00 40.07           C  
ANISOU12211  CB  VAL D 400     5385   5296   4545    295   -291    -54       C  
ATOM  12212  CG1 VAL D 400     104.858  -6.638-197.650  1.00 40.98           C  
ANISOU12212  CG1 VAL D 400     5582   5360   4626    295   -228   -124       C  
ATOM  12213  CG2 VAL D 400     104.953  -9.105-197.919  1.00 35.44           C  
ANISOU12213  CG2 VAL D 400     4767   4701   3999    354   -273     10       C  
ATOM  12214  N   GLU D 401     108.400  -6.072-198.319  1.00 32.97           N  
ANISOU12214  N   GLU D 401     4469   4445   3612    138   -383   -133       N  
ATOM  12215  CA  GLU D 401     109.018  -4.743-198.347  1.00 32.07           C  
ANISOU12215  CA  GLU D 401     4412   4320   3451     41   -396   -195       C  
ATOM  12216  C   GLU D 401     109.653  -4.430-199.705  1.00 31.36           C  
ANISOU12216  C   GLU D 401     4275   4214   3428     12   -399   -201       C  
ATOM  12217  O   GLU D 401     109.706  -3.257-200.103  1.00 32.68           O  
ANISOU12217  O   GLU D 401     4517   4320   3578    -54   -384   -252       O  
ATOM  12218  CB  GLU D 401     110.056  -4.596-197.241  1.00 35.31           C  
ANISOU12218  CB  GLU D 401     4818   4829   3769    -46   -464   -197       C  
ATOM  12219  CG  GLU D 401     109.451  -4.561-195.834  1.00 43.45           C  
ANISOU12219  CG  GLU D 401     5929   5872   4709    -44   -457   -209       C  
ATOM  12220  CD  GLU D 401     108.230  -3.656-195.722  1.00 47.04           C  
ANISOU12220  CD  GLU D 401     6509   6223   5141    -19   -382   -272       C  
ATOM  12221  OE1 GLU D 401     108.274  -2.503-196.210  1.00 43.28           O  
ANISOU12221  OE1 GLU D 401     6111   5674   4662    -65   -366   -332       O  
ATOM  12222  OE2 GLU D 401     107.214  -4.106-195.147  1.00 49.66           O  
ANISOU12222  OE2 GLU D 401     6862   6550   5455     48   -338   -260       O  
ATOM  12223  N   ILE D 402     110.154  -5.442-200.418  1.00 31.47           N  
ANISOU12223  N   ILE D 402     4174   4277   3508     59   -417   -151       N  
ATOM  12224  CA  ILE D 402     110.709  -5.184-201.745  1.00 31.28           C  
ANISOU12224  CA  ILE D 402     4099   4246   3539     35   -411   -157       C  
ATOM  12225  C   ILE D 402     109.601  -4.768-202.697  1.00 33.70           C  
ANISOU12225  C   ILE D 402     4472   4432   3901     78   -347   -177       C  
ATOM  12226  O   ILE D 402     109.761  -3.836-203.501  1.00 29.97           O  
ANISOU12226  O   ILE D 402     4040   3912   3434     20   -333   -209       O  
ATOM  12227  CB  ILE D 402     111.474  -6.422-202.249  1.00 34.01           C  
ANISOU12227  CB  ILE D 402     4310   4677   3937     95   -441   -106       C  
ATOM  12228  CG1 ILE D 402     112.772  -6.597-201.466  1.00 32.84           C  
ANISOU12228  CG1 ILE D 402     4081   4666   3729     44   -512    -90       C  
ATOM  12229  CG2 ILE D 402     111.732  -6.335-203.769  1.00 30.46           C  
ANISOU12229  CG2 ILE D 402     3812   4209   3552     98   -413   -112       C  
ATOM  12230  CD1 ILE D 402     113.257  -8.023-201.437  1.00 30.50           C  
ANISOU12230  CD1 ILE D 402     3679   4444   3467    147   -549    -32       C  
ATOM  12231  N   ASN D 403     108.446  -5.435-202.596  1.00 33.15           N  
ANISOU12231  N   ASN D 403     4418   4315   3865    172   -312   -156       N  
ATOM  12232  CA  ASN D 403     107.298  -5.050-203.400  1.00 34.69           C  
ANISOU12232  CA  ASN D 403     4666   4410   4104    220   -256   -172       C  
ATOM  12233  C   ASN D 403     106.829  -3.649-203.046  1.00 33.68           C  
ANISOU12233  C   ASN D 403     4662   4212   3924    183   -233   -231       C  
ATOM  12234  O   ASN D 403     106.467  -2.866-203.931  1.00 30.58           O  
ANISOU12234  O   ASN D 403     4324   3739   3556    183   -208   -255       O  
ATOM  12235  CB  ASN D 403     106.191  -6.079-203.226  1.00 22.74           C  
ANISOU12235  CB  ASN D 403     3131   2884   2623    311   -229   -135       C  
ATOM  12236  CG  ASN D 403     106.433  -7.328-204.085  1.00 38.07           C  
ANISOU12236  CG  ASN D 403     4986   4844   4636    359   -241    -85       C  
ATOM  12237  OD1 ASN D 403     105.911  -7.437-205.195  1.00 34.92           O  
ANISOU12237  OD1 ASN D 403     4578   4394   4294    392   -214    -82       O  
ATOM  12238  ND2 ASN D 403     107.257  -8.242-203.588  1.00 34.58           N  
ANISOU12238  ND2 ASN D 403     4484   4472   4183    365   -286    -49       N  
ATOM  12239  N   VAL D 404     106.830  -3.308-201.757  1.00 32.42           N  
ANISOU12239  N   VAL D 404     4558   4074   3685    155   -244   -255       N  
ATOM  12240  CA  VAL D 404     106.513  -1.943-201.369  1.00 28.44           C  
ANISOU12240  CA  VAL D 404     4189   3497   3120    120   -226   -320       C  
ATOM  12241  C   VAL D 404     107.485  -0.960-202.010  1.00 29.46           C  
ANISOU12241  C   VAL D 404     4363   3595   3236     11   -255   -348       C  
ATOM  12242  O   VAL D 404     107.078   0.107-202.476  1.00 32.71           O  
ANISOU12242  O   VAL D 404     4887   3900   3641      4   -233   -388       O  
ATOM  12243  CB  VAL D 404     106.523  -1.810-199.833  1.00 28.87           C  
ANISOU12243  CB  VAL D 404     4295   3594   3079     95   -238   -345       C  
ATOM  12244  CG1 VAL D 404     106.529  -0.331-199.447  1.00 30.87           C  
ANISOU12244  CG1 VAL D 404     4704   3769   3258     36   -233   -422       C  
ATOM  12245  CG2 VAL D 404     105.322  -2.522-199.204  1.00 32.35           C  
ANISOU12245  CG2 VAL D 404     4721   4053   3519    195   -192   -326       C  
ATOM  12246  N   ALA D 405     108.783  -1.280-202.034  1.00 27.46           N  
ANISOU12246  N   ALA D 405     4026   3437   2972    -76   -307   -326       N  
ATOM  12247  CA  ALA D 405     109.734  -0.338-202.624  1.00 28.78           C  
ANISOU12247  CA  ALA D 405     4227   3592   3115   -202   -333   -349       C  
ATOM  12248  C   ALA D 405     109.443  -0.118-204.112  1.00 31.78           C  
ANISOU12248  C   ALA D 405     4611   3899   3566   -179   -302   -338       C  
ATOM  12249  O   ALA D 405     109.508   1.011-204.613  1.00 33.44           O  
ANISOU12249  O   ALA D 405     4930   4022   3752   -251   -299   -369       O  
ATOM  12250  CB  ALA D 405     111.161  -0.846-202.451  1.00 30.78           C  
ANISOU12250  CB  ALA D 405     4354   3993   3348   -289   -391   -320       C  
ATOM  12251  N   VAL D 406     109.141  -1.194-204.830  1.00 32.33           N  
ANISOU12251  N   VAL D 406     4571   3999   3715    -86   -282   -294       N  
ATOM  12252  CA  VAL D 406     108.846  -1.077-206.263  1.00 28.20           C  
ANISOU12252  CA  VAL D 406     4046   3416   3253    -62   -254   -282       C  
ATOM  12253  C   VAL D 406     107.658  -0.152-206.483  1.00 29.24           C  
ANISOU12253  C   VAL D 406     4318   3407   3385    -13   -219   -312       C  
ATOM  12254  O   VAL D 406     107.715   0.777-207.298  1.00 32.31           O  
ANISOU12254  O   VAL D 406     4791   3716   3769    -63   -216   -326       O  
ATOM  12255  CB  VAL D 406     108.600  -2.473-206.868  1.00 29.83           C  
ANISOU12255  CB  VAL D 406     4126   3671   3537     38   -240   -234       C  
ATOM  12256  CG1 VAL D 406     108.118  -2.353-208.336  1.00 29.20           C  
ANISOU12256  CG1 VAL D 406     4056   3524   3514     68   -209   -225       C  
ATOM  12257  CG2 VAL D 406     109.877  -3.304-206.807  1.00 26.87           C  
ANISOU12257  CG2 VAL D 406     3619   3429   3162      4   -277   -207       C  
ATOM  12258  N   LEU D 407     106.554  -0.398-205.761  1.00 28.67           N  
ANISOU12258  N   LEU D 407     4272   3309   3314     89   -192   -320       N  
ATOM  12259  CA  LEU D 407     105.366   0.442-205.908  1.00 31.09           C  
ANISOU12259  CA  LEU D 407     4696   3499   3617    162   -157   -350       C  
ATOM  12260  C   LEU D 407     105.665   1.892-205.549  1.00 38.05           C  
ANISOU12260  C   LEU D 407     5742   4291   4425     85   -171   -406       C  
ATOM  12261  O   LEU D 407     105.323   2.818-206.296  1.00 32.30           O  
ANISOU12261  O   LEU D 407     5122   3450   3700     90   -163   -422       O  
ATOM  12262  CB  LEU D 407     104.220  -0.095-205.050  1.00 32.27           C  
ANISOU12262  CB  LEU D 407     4827   3669   3766    275   -123   -352       C  
ATOM  12263  CG  LEU D 407     103.590  -1.378-205.588  1.00 33.55           C  
ANISOU12263  CG  LEU D 407     4863   3881   4001    356   -104   -298       C  
ATOM  12264  CD1 LEU D 407     102.831  -2.089-204.466  1.00 28.26           C  
ANISOU12264  CD1 LEU D 407     4157   3271   3310    418    -81   -289       C  
ATOM  12265  CD2 LEU D 407     102.672  -1.084-206.787  1.00 29.06           C  
ANISOU12265  CD2 LEU D 407     4314   3242   3487    426    -79   -290       C  
ATOM  12266  N   HIS D 408     106.281   2.110-204.388  1.00 31.22           N  
ANISOU12266  N   HIS D 408     4910   3467   3487     11   -195   -435       N  
ATOM  12267  CA  HIS D 408     106.632   3.467-203.995  1.00 33.67           C  
ANISOU12267  CA  HIS D 408     5391   3687   3717    -81   -215   -493       C  
ATOM  12268  C   HIS D 408     107.512   4.148-205.037  1.00 34.52           C  
ANISOU12268  C   HIS D 408     5541   3752   3824   -209   -244   -483       C  
ATOM  12269  O   HIS D 408     107.309   5.327-205.354  1.00 33.73           O  
ANISOU12269  O   HIS D 408     5610   3515   3691   -239   -245   -517       O  
ATOM  12270  CB  HIS D 408     107.332   3.433-202.638  1.00 34.37           C  
ANISOU12270  CB  HIS D 408     5484   3852   3722   -164   -247   -519       C  
ATOM  12271  CG  HIS D 408     108.043   4.701-202.292  1.00 40.63           C  
ANISOU12271  CG  HIS D 408     6436   4575   4425   -308   -283   -572       C  
ATOM  12272  ND1 HIS D 408     107.380   5.852-201.922  1.00 42.08           N  
ANISOU12272  ND1 HIS D 408     6824   4612   4552   -280   -266   -637       N  
ATOM  12273  CD2 HIS D 408     109.363   4.996-202.250  1.00 42.29           C  
ANISOU12273  CD2 HIS D 408     6637   4845   4587   -486   -338   -569       C  
ATOM  12274  CE1 HIS D 408     108.262   6.803-201.677  1.00 47.95           C  
ANISOU12274  CE1 HIS D 408     7694   5312   5215   -443   -311   -674       C  
ATOM  12275  NE2 HIS D 408     109.472   6.311-201.873  1.00 45.27           N  
ANISOU12275  NE2 HIS D 408     7220   5103   4878   -579   -355   -632       N  
ATOM  12276  N   SER D 409     108.479   3.416-205.595  1.00 30.67           N  
ANISOU12276  N   SER D 409     4904   3379   3368   -281   -266   -437       N  
ATOM  12277  CA  SER D 409     109.456   4.043-206.480  1.00 36.10           C  
ANISOU12277  CA  SER D 409     5616   4061   4039   -428   -291   -428       C  
ATOM  12278  C   SER D 409     108.849   4.393-207.841  1.00 33.76           C  
ANISOU12278  C   SER D 409     5373   3660   3794   -381   -264   -409       C  
ATOM  12279  O   SER D 409     109.165   5.448-208.419  1.00 34.67           O  
ANISOU12279  O   SER D 409     5617   3684   3872   -485   -279   -418       O  
ATOM  12280  CB  SER D 409     110.664   3.119-206.645  1.00 35.46           C  
ANISOU12280  CB  SER D 409     5343   4157   3972   -503   -317   -388       C  
ATOM  12281  OG  SER D 409     111.260   2.815-205.389  1.00 37.41           O  
ANISOU12281  OG  SER D 409     5541   4506   4166   -547   -352   -400       O  
ATOM  12282  N   TYR D 410     107.995   3.519-208.383  1.00 32.12           N  
ANISOU12282  N   TYR D 410     5074   3465   3666   -235   -231   -378       N  
ATOM  12283  CA  TYR D 410     107.332   3.849-209.646  1.00 33.43           C  
ANISOU12283  CA  TYR D 410     5292   3535   3875   -182   -211   -358       C  
ATOM  12284  C   TYR D 410     106.354   5.003-209.456  1.00 38.25           C  
ANISOU12284  C   TYR D 410     6097   3980   4455   -118   -203   -396       C  
ATOM  12285  O   TYR D 410     106.287   5.914-210.292  1.00 35.51           O  
ANISOU12285  O   TYR D 410     5877   3520   4095   -154   -211   -393       O  
ATOM  12286  CB  TYR D 410     106.626   2.617-210.220  1.00 28.67           C  
ANISOU12286  CB  TYR D 410     4547   2990   3357    -50   -182   -318       C  
ATOM  12287  CG  TYR D 410     107.544   1.742-211.024  1.00 30.22           C  
ANISOU12287  CG  TYR D 410     4596   3301   3586   -106   -187   -280       C  
ATOM  12288  CD1 TYR D 410     107.339   1.563-212.392  1.00 29.53           C  
ANISOU12288  CD1 TYR D 410     4484   3194   3542    -86   -172   -250       C  
ATOM  12289  CD2 TYR D 410     108.639   1.123-210.430  1.00 33.15           C  
ANISOU12289  CD2 TYR D 410     4854   3803   3939   -174   -208   -276       C  
ATOM  12290  CE1 TYR D 410     108.182   0.787-213.137  1.00 31.95           C  
ANISOU12290  CE1 TYR D 410     4662   3607   3871   -128   -170   -223       C  
ATOM  12291  CE2 TYR D 410     109.495   0.345-211.162  1.00 31.02           C  
ANISOU12291  CE2 TYR D 410     4448   3643   3696   -206   -209   -247       C  
ATOM  12292  CZ  TYR D 410     109.256   0.176-212.527  1.00 31.22           C  
ANISOU12292  CZ  TYR D 410     4456   3644   3762   -182   -186   -224       C  
ATOM  12293  OH  TYR D 410     110.120  -0.594-213.242  1.00 31.07           O  
ANISOU12293  OH  TYR D 410     4304   3738   3761   -206   -181   -203       O  
ATOM  12294  N   GLN D 411     105.606   4.998-208.348  1.00 35.84           N  
ANISOU12294  N   GLN D 411     5826   3658   4131    -21   -186   -432       N  
ATOM  12295  CA  GLN D 411     104.698   6.114-208.070  1.00 37.11           C  
ANISOU12295  CA  GLN D 411     6176   3669   4257     59   -176   -478       C  
ATOM  12296  C   GLN D 411     105.462   7.422-207.911  1.00 35.79           C  
ANISOU12296  C   GLN D 411     6203   3391   4006    -85   -211   -516       C  
ATOM  12297  O   GLN D 411     105.066   8.447-208.475  1.00 39.43           O  
ANISOU12297  O   GLN D 411     6835   3698   4450    -66   -218   -528       O  
ATOM  12298  CB  GLN D 411     103.848   5.816-206.828  1.00 40.34           C  
ANISOU12298  CB  GLN D 411     6570   4107   4648    182   -145   -515       C  
ATOM  12299  CG  GLN D 411     102.803   4.714-207.096  1.00 45.68           C  
ANISOU12299  CG  GLN D 411     7091   4863   5401    332   -107   -477       C  
ATOM  12300  CD  GLN D 411     102.244   4.080-205.827  1.00 57.43           C  
ANISOU12300  CD  GLN D 411     8515   6437   6870    408    -77   -496       C  
ATOM  12301  OE1 GLN D 411     102.676   4.392-204.721  1.00 55.90           O  
ANISOU12301  OE1 GLN D 411     8382   6253   6605    354    -85   -538       O  
ATOM  12302  NE2 GLN D 411     101.286   3.177-205.989  1.00 55.00           N  
ANISOU12302  NE2 GLN D 411     8084   6196   6616    522    -44   -463       N  
ATOM  12303  N   LEU D 412     106.570   7.400-207.164  1.00 39.61           N  
ANISOU12303  N   LEU D 412     6667   3950   4433   -235   -241   -533       N  
ATOM  12304  CA  LEU D 412     107.409   8.586-207.007  1.00 43.83           C  
ANISOU12304  CA  LEU D 412     7379   4395   4881   -409   -282   -566       C  
ATOM  12305  C   LEU D 412     107.898   9.113-208.355  1.00 48.72           C  
ANISOU12305  C   LEU D 412     8050   4954   5508   -517   -300   -526       C  
ATOM  12306  O   LEU D 412     107.902  10.329-208.597  1.00 41.28           O  
ANISOU12306  O   LEU D 412     7326   3849   4510   -583   -321   -548       O  
ATOM  12307  CB  LEU D 412     108.598   8.241-206.117  1.00 49.27           C  
ANISOU12307  CB  LEU D 412     7981   5224   5516   -563   -315   -574       C  
ATOM  12308  CG  LEU D 412     109.566   9.322-205.654  1.00 56.22           C  
ANISOU12308  CG  LEU D 412     9020   6051   6290   -771   -365   -613       C  
ATOM  12309  CD1 LEU D 412     108.840  10.255-204.713  1.00 57.82           C  
ANISOU12309  CD1 LEU D 412     9448   6098   6423   -710   -360   -690       C  
ATOM  12310  CD2 LEU D 412     110.763   8.669-204.960  1.00 48.88           C  
ANISOU12310  CD2 LEU D 412     7929   5317   5326   -908   -400   -602       C  
ATOM  12311  N   ALA D 413     108.342   8.219-209.232  1.00 39.83           N  
ANISOU12311  N   ALA D 413     6738   3955   4443   -541   -293   -467       N  
ATOM  12312  CA  ALA D 413     108.840   8.606-210.547  1.00 37.97           C  
ANISOU12312  CA  ALA D 413     6529   3689   4209   -649   -303   -425       C  
ATOM  12313  C   ALA D 413     107.729   8.926-211.539  1.00 39.69           C  
ANISOU12313  C   ALA D 413     6836   3772   4472   -512   -284   -404       C  
ATOM  12314  O   ALA D 413     108.035   9.329-212.671  1.00 41.72           O  
ANISOU12314  O   ALA D 413     7142   3987   4724   -595   -294   -366       O  
ATOM  12315  CB  ALA D 413     109.722   7.494-211.124  1.00 40.92           C  
ANISOU12315  CB  ALA D 413     6665   4259   4625   -710   -296   -377       C  
ATOM  12316  N   LYS D 414     106.463   8.749-211.149  1.00 37.63           N  
ANISOU12316  N   LYS D 414     6591   3457   4250   -309   -259   -424       N  
ATOM  12317  CA  LYS D 414     105.315   8.977-212.031  1.00 41.43           C  
ANISOU12317  CA  LYS D 414     7133   3834   4776   -157   -245   -402       C  
ATOM  12318  C   LYS D 414     105.364   8.062-213.252  1.00 40.69           C  
ANISOU12318  C   LYS D 414     6872   3838   4750   -147   -232   -339       C  
ATOM  12319  O   LYS D 414     105.170   8.496-214.389  1.00 41.74           O  
ANISOU12319  O   LYS D 414     7076   3894   4889   -153   -242   -303       O  
ATOM  12320  CB  LYS D 414     105.216  10.443-212.464  1.00 38.96           C  
ANISOU12320  CB  LYS D 414     7083   3317   4404   -201   -275   -412       C  
ATOM  12321  CG  LYS D 414     104.987  11.445-211.329  1.00 48.54           C  
ANISOU12321  CG  LYS D 414     8502   4397   5545   -182   -287   -484       C  
ATOM  12322  CD  LYS D 414     104.577  12.790-211.944  1.00 64.91           C  
ANISOU12322  CD  LYS D 414    10844   6243   7576   -164   -315   -486       C  
ATOM  12323  CE  LYS D 414     104.703  13.921-210.947  1.00 80.37           C  
ANISOU12323  CE  LYS D 414    13048   8047   9442   -206   -337   -559       C  
ATOM  12324  NZ  LYS D 414     104.202  13.519-209.605  1.00 85.87           N  
ANISOU12324  NZ  LYS D 414    13683   8809  10136    -83   -304   -623       N  
ATOM  12325  N   VAL D 415     105.625   6.782-213.004  1.00 37.57           N  
ANISOU12325  N   VAL D 415     6265   3609   4401   -131   -213   -325       N  
ATOM  12326  CA  VAL D 415     105.593   5.740-214.026  1.00 35.78           C  
ANISOU12326  CA  VAL D 415     5875   3481   4240    -99   -196   -276       C  
ATOM  12327  C   VAL D 415     104.465   4.789-213.662  1.00 36.05           C  
ANISOU12327  C   VAL D 415     5799   3563   4336     79   -169   -274       C  
ATOM  12328  O   VAL D 415     104.420   4.268-212.536  1.00 33.88           O  
ANISOU12328  O   VAL D 415     5459   3353   4060    113   -159   -298       O  
ATOM  12329  CB  VAL D 415     106.933   4.989-214.125  1.00 28.14           C  
ANISOU12329  CB  VAL D 415     4756   2668   3269   -233   -198   -260       C  
ATOM  12330  CG1 VAL D 415     106.836   3.812-215.134  1.00 29.95           C  
ANISOU12330  CG1 VAL D 415     4822   2994   3564   -176   -177   -219       C  
ATOM  12331  CG2 VAL D 415     108.059   5.935-214.482  1.00 32.54           C  
ANISOU12331  CG2 VAL D 415     5405   3202   3755   -429   -223   -258       C  
ATOM  12332  N   THR D 416     103.557   4.567-214.610  1.00 31.21           N  
ANISOU12332  N   THR D 416     5168   2922   3770    181   -160   -243       N  
ATOM  12333  CA  THR D 416     102.426   3.664-214.416  1.00 31.61           C  
ANISOU12333  CA  THR D 416     5109   3025   3875    333   -137   -235       C  
ATOM  12334  C   THR D 416     102.877   2.323-213.857  1.00 33.05           C  
ANISOU12334  C   THR D 416     5122   3348   4086    317   -123   -228       C  
ATOM  12335  O   THR D 416     103.825   1.713-214.359  1.00 31.80           O  
ANISOU12335  O   THR D 416     4879   3266   3940    231   -128   -208       O  
ATOM  12336  CB  THR D 416     101.698   3.444-215.753  1.00 34.55           C  
ANISOU12336  CB  THR D 416     5456   3380   4289    397   -139   -192       C  
ATOM  12337  OG1 THR D 416     101.363   4.718-216.298  1.00 33.42           O  
ANISOU12337  OG1 THR D 416     5484   3101   4115    411   -160   -191       O  
ATOM  12338  CG2 THR D 416     100.408   2.631-215.540  1.00 31.27           C  
ANISOU12338  CG2 THR D 416     4939   3019   3922    545   -119   -183       C  
ATOM  12339  N   ILE D 417     102.190   1.879-212.805  1.00 29.60           N  
ANISOU12339  N   ILE D 417     4642   2948   3657    404   -106   -245       N  
ATOM  12340  CA  ILE D 417     102.379   0.541-212.252  1.00 31.59           C  
ANISOU12340  CA  ILE D 417     4747   3319   3937    411    -96   -231       C  
ATOM  12341  C   ILE D 417     101.065   0.158-211.590  1.00 29.48           C  
ANISOU12341  C   ILE D 417     4447   3069   3684    536    -71   -234       C  
ATOM  12342  O   ILE D 417     100.307   1.027-211.152  1.00 32.64           O  
ANISOU12342  O   ILE D 417     4939   3407   4057    605    -59   -264       O  
ATOM  12343  CB  ILE D 417     103.569   0.487-211.259  1.00 38.00           C  
ANISOU12343  CB  ILE D 417     5547   4187   4706    313   -111   -252       C  
ATOM  12344  CG1 ILE D 417     103.916  -0.965-210.908  1.00 40.57           C  
ANISOU12344  CG1 ILE D 417     5724   4629   5063    321   -111   -225       C  
ATOM  12345  CG2 ILE D 417     103.248   1.292-209.994  1.00 30.96           C  
ANISOU12345  CG2 ILE D 417     4757   3250   3758    332   -107   -298       C  
ATOM  12346  CD1 ILE D 417     105.405  -1.242-210.794  1.00 40.13           C  
ANISOU12346  CD1 ILE D 417     5609   4651   4986    214   -136   -222       C  
ATOM  12347  N   VAL D 418     100.789  -1.148-211.512  1.00 28.30           N  
ANISOU12347  N   VAL D 418     4172   3007   3573    565    -61   -204       N  
ATOM  12348  CA  VAL D 418      99.596  -1.633-210.819  1.00 34.42           C  
ANISOU12348  CA  VAL D 418     4900   3824   4355    658    -35   -200       C  
ATOM  12349  C   VAL D 418     100.007  -2.697-209.806  1.00 31.71           C  
ANISOU12349  C   VAL D 418     4479   3567   4004    627    -34   -189       C  
ATOM  12350  O   VAL D 418     100.848  -3.545-210.111  1.00 29.25           O  
ANISOU12350  O   VAL D 418     4106   3295   3715    573    -53   -164       O  
ATOM  12351  CB  VAL D 418      98.530  -2.174-211.794  1.00 31.21           C  
ANISOU12351  CB  VAL D 418     4430   3432   3997    724    -28   -164       C  
ATOM  12352  CG1 VAL D 418      99.012  -3.445-212.546  1.00 31.45           C  
ANISOU12352  CG1 VAL D 418     4369   3510   4072    675    -43   -125       C  
ATOM  12353  CG2 VAL D 418      97.222  -2.421-211.061  1.00 35.89           C  
ANISOU12353  CG2 VAL D 418     4978   4076   4583    814      2   -164       C  
ATOM  12354  N   ASP D 419      99.452  -2.616-208.579  1.00 31.20           N  
ANISOU12354  N   ASP D 419     4424   3531   3898    666    -11   -208       N  
ATOM  12355  CA  ASP D 419      99.744  -3.665-207.610  1.00 31.20           C  
ANISOU12355  CA  ASP D 419     4358   3612   3885    639    -13   -188       C  
ATOM  12356  C   ASP D 419      98.878  -4.902-207.895  1.00 26.85           C  
ANISOU12356  C   ASP D 419     3711   3114   3375    675     -1   -140       C  
ATOM  12357  O   ASP D 419      97.910  -4.857-208.670  1.00 31.46           O  
ANISOU12357  O   ASP D 419     4275   3689   3990    726     13   -128       O  
ATOM  12358  CB  ASP D 419      99.564  -3.148-206.166  1.00 26.10           C  
ANISOU12358  CB  ASP D 419     3764   2985   3168    650      6   -226       C  
ATOM  12359  CG  ASP D 419      98.117  -2.832-205.822  1.00 27.25           C  
ANISOU12359  CG  ASP D 419     3914   3143   3296    748     53   -242       C  
ATOM  12360  OD1 ASP D 419      97.296  -3.777-205.734  1.00 36.56           O  
ANISOU12360  OD1 ASP D 419     5005   4393   4494    777     73   -204       O  
ATOM  12361  OD2 ASP D 419      97.799  -1.632-205.650  1.00 36.66           O  
ANISOU12361  OD2 ASP D 419     5200   4277   4453    796     69   -293       O  
ATOM  12362  N   HIS D 420      99.250  -6.031-207.272  1.00 26.72           N  
ANISOU12362  N   HIS D 420     3642   3155   3355    641    -14   -108       N  
ATOM  12363  CA  HIS D 420      98.579  -7.295-207.558  1.00 27.80           C  
ANISOU12363  CA  HIS D 420     3708   3329   3525    652    -11    -58       C  
ATOM  12364  C   HIS D 420      97.153  -7.328-207.027  1.00 33.29           C  
ANISOU12364  C   HIS D 420     4378   4073   4199    696     29    -51       C  
ATOM  12365  O   HIS D 420      96.327  -8.081-207.560  1.00 30.51           O  
ANISOU12365  O   HIS D 420     3970   3747   3876    702     35    -15       O  
ATOM  12366  CB  HIS D 420      99.387  -8.490-207.022  1.00 28.06           C  
ANISOU12366  CB  HIS D 420     3712   3394   3555    609    -41    -22       C  
ATOM  12367  CG  HIS D 420      99.767  -8.382-205.573  1.00 30.69           C  
ANISOU12367  CG  HIS D 420     4068   3768   3824    590    -43    -30       C  
ATOM  12368  ND1 HIS D 420     100.708  -7.484-205.117  1.00 31.09           N  
ANISOU12368  ND1 HIS D 420     4164   3810   3838    563    -58    -70       N  
ATOM  12369  CD2 HIS D 420      99.344  -9.071-204.484  1.00 36.15           C  
ANISOU12369  CD2 HIS D 420     4748   4512   4474    582    -35     -1       C  
ATOM  12370  CE1 HIS D 420     100.852  -7.625-203.807  1.00 35.83           C  
ANISOU12370  CE1 HIS D 420     4779   4458   4377    545    -61    -68       C  
ATOM  12371  NE2 HIS D 420     100.026  -8.571-203.395  1.00 32.28           N  
ANISOU12371  NE2 HIS D 420     4297   4046   3923    559    -45    -25       N  
ATOM  12372  N   HIS D 421      96.832  -6.519-206.008  1.00 27.50           N  
ANISOU12372  N   HIS D 421     3681   3360   3407    725     59    -88       N  
ATOM  12373  CA  HIS D 421      95.456  -6.479-205.532  1.00 27.95           C  
ANISOU12373  CA  HIS D 421     3699   3483   3436    778    106    -88       C  
ATOM  12374  C   HIS D 421      94.548  -5.777-206.527  1.00 29.69           C  
ANISOU12374  C   HIS D 421     3909   3683   3689    852    121   -102       C  
ATOM  12375  O   HIS D 421      93.441  -6.245-206.807  1.00 33.22           O  
ANISOU12375  O   HIS D 421     4278   4195   4148    877    140    -73       O  
ATOM  12376  CB  HIS D 421      95.385  -5.802-204.159  1.00 29.81           C  
ANISOU12376  CB  HIS D 421     3983   3751   3593    799    139   -131       C  
ATOM  12377  CG  HIS D 421      96.191  -6.516-203.125  1.00 30.02           C  
ANISOU12377  CG  HIS D 421     4019   3810   3579    727    119   -110       C  
ATOM  12378  ND1 HIS D 421      95.830  -7.749-202.626  1.00 32.31           N  
ANISOU12378  ND1 HIS D 421     4250   4169   3856    688    122    -53       N  
ATOM  12379  CD2 HIS D 421      97.350  -6.183-202.511  1.00 36.69           C  
ANISOU12379  CD2 HIS D 421     4925   4629   4389    684     89   -134       C  
ATOM  12380  CE1 HIS D 421      96.739  -8.149-201.756  1.00 35.01           C  
ANISOU12380  CE1 HIS D 421     4622   4521   4158    636     93    -40       C  
ATOM  12381  NE2 HIS D 421      97.666  -7.212-201.661  1.00 35.28           N  
ANISOU12381  NE2 HIS D 421     4721   4506   4179    633     73    -90       N  
ATOM  12382  N   ALA D 422      94.971  -4.624-207.023  1.00 31.34           N  
ANISOU12382  N   ALA D 422     4196   3807   3904    883    110   -144       N  
ATOM  12383  CA  ALA D 422      94.143  -3.901-207.977  1.00 28.05           C  
ANISOU12383  CA  ALA D 422     3782   3362   3513    963    116   -153       C  
ATOM  12384  C   ALA D 422      94.045  -4.670-209.289  1.00 28.29           C  
ANISOU12384  C   ALA D 422     3752   3390   3606    932     86   -104       C  
ATOM  12385  O   ALA D 422      92.977  -4.707-209.912  1.00 34.73           O  
ANISOU12385  O   ALA D 422     4512   4244   4441    985     92    -85       O  
ATOM  12386  CB  ALA D 422      94.718  -2.501-208.206  1.00 33.62           C  
ANISOU12386  CB  ALA D 422     4613   3957   4203    990    104   -203       C  
ATOM  12387  N   ALA D 423      95.151  -5.297-209.718  1.00 28.16           N  
ANISOU12387  N   ALA D 423     3745   3338   3618    849     52    -85       N  
ATOM  12388  CA  ALA D 423      95.157  -6.027-210.991  1.00 30.64           C  
ANISOU12388  CA  ALA D 423     4018   3641   3983    819     24    -48       C  
ATOM  12389  C   ALA D 423      94.222  -7.235-210.956  1.00 31.05           C  
ANISOU12389  C   ALA D 423     3979   3772   4046    804     31     -3       C  
ATOM  12390  O   ALA D 423      93.445  -7.458-211.897  1.00 30.43           O  
ANISOU12390  O   ALA D 423     3858   3711   3994    817     22     20       O  
ATOM  12391  CB  ALA D 423      96.581  -6.457-211.328  1.00 26.40           C  
ANISOU12391  CB  ALA D 423     3506   3063   3464    746     -6    -44       C  
ATOM  12392  N   THR D 424      94.260  -8.015-209.868  1.00 28.58           N  
ANISOU12392  N   THR D 424     3642   3511   3707    769     43     13       N  
ATOM  12393  CA  THR D 424      93.365  -9.162-209.777  1.00 30.03           C  
ANISOU12393  CA  THR D 424     3753   3767   3891    734     48     60       C  
ATOM  12394  C   THR D 424      91.913  -8.741-209.592  1.00 27.33           C  
ANISOU12394  C   THR D 424     3346   3513   3526    789     84     60       C  
ATOM  12395  O   THR D 424      91.007  -9.432-210.079  1.00 31.87           O  
ANISOU12395  O   THR D 424     3850   4148   4112    762     80     98       O  
ATOM  12396  CB  THR D 424      93.797 -10.087-208.642  1.00 29.22           C  
ANISOU12396  CB  THR D 424     3655   3690   3756    677     48     84       C  
ATOM  12397  OG1 THR D 424      93.941  -9.316-207.439  1.00 29.62           O  
ANISOU12397  OG1 THR D 424     3734   3766   3755    707     78     50       O  
ATOM  12398  CG2 THR D 424      95.130 -10.725-208.988  1.00 26.78           C  
ANISOU12398  CG2 THR D 424     3390   3310   3476    636      6     93       C  
ATOM  12399  N   ALA D 425      91.664  -7.619-208.905  1.00 28.80           N  
ANISOU12399  N   ALA D 425     3553   3714   3675    866    119     17       N  
ATOM  12400  CA  ALA D 425      90.300  -7.109-208.817  1.00 32.93           C  
ANISOU12400  CA  ALA D 425     4008   4329   4177    946    155     10       C  
ATOM  12401  C   ALA D 425      89.779  -6.732-210.201  1.00 37.24           C  
ANISOU12401  C   ALA D 425     4529   4854   4765    993    128     18       C  
ATOM  12402  O   ALA D 425      88.623  -7.000-210.535  1.00 31.36           O  
ANISOU12402  O   ALA D 425     3688   4208   4021   1012    135     45       O  
ATOM  12403  CB  ALA D 425      90.235  -5.894-207.893  1.00 33.10           C  
ANISOU12403  CB  ALA D 425     4081   4348   4149   1039    196    -50       C  
ATOM  12404  N   SER D 426      90.611  -6.093-211.011  1.00 30.10           N  
ANISOU12404  N   SER D 426     3711   3834   3892   1006     95     -2       N  
ATOM  12405  CA  SER D 426      90.159  -5.707-212.347  1.00 30.31           C  
ANISOU12405  CA  SER D 426     3728   3836   3951   1047     65     11       C  
ATOM  12406  C   SER D 426      89.967  -6.938-213.226  1.00 33.77           C  
ANISOU12406  C   SER D 426     4104   4307   4422    959     33     61       C  
ATOM  12407  O   SER D 426      89.042  -6.989-214.040  1.00 30.83           O  
ANISOU12407  O   SER D 426     3668   3987   4060    982     16     85       O  
ATOM  12408  CB  SER D 426      91.158  -4.737-212.979  1.00 34.92           C  
ANISOU12408  CB  SER D 426     4432   4288   4550   1062     39    -18       C  
ATOM  12409  OG  SER D 426      92.278  -5.443-213.491  1.00 41.39           O  
ANISOU12409  OG  SER D 426     5280   5051   5395    961     11     -4       O  
ATOM  12410  N   PHE D 427      90.809  -7.955-213.053  1.00 31.20           N  
ANISOU12410  N   PHE D 427     3798   3952   4107    861     21     76       N  
ATOM  12411  CA  PHE D 427      90.606  -9.184-213.804  1.00 32.03           C  
ANISOU12411  CA  PHE D 427     3862   4074   4233    778     -8    118       C  
ATOM  12412  C   PHE D 427      89.285  -9.858-213.447  1.00 34.85           C  
ANISOU12412  C   PHE D 427     4116   4557   4568    752      6    154       C  
ATOM  12413  O   PHE D 427      88.668 -10.494-214.302  1.00 29.54           O  
ANISOU12413  O   PHE D 427     3397   3920   3908    704    -22    186       O  
ATOM  12414  CB  PHE D 427      91.763 -10.154-213.591  1.00 27.17           C  
ANISOU12414  CB  PHE D 427     3297   3397   3628    699    -23    125       C  
ATOM  12415  CG  PHE D 427      91.678 -11.375-214.492  1.00 30.86           C  
ANISOU12415  CG  PHE D 427     3756   3852   4117    622    -57    158       C  
ATOM  12416  CD1 PHE D 427      91.947 -11.260-215.843  1.00 27.06           C  
ANISOU12416  CD1 PHE D 427     3301   3318   3662    621    -86    151       C  
ATOM  12417  CD2 PHE D 427      91.283 -12.599-213.992  1.00 27.77           C  
ANISOU12417  CD2 PHE D 427     3341   3500   3711    547    -60    195       C  
ATOM  12418  CE1 PHE D 427      91.843 -12.371-216.692  1.00 28.39           C  
ANISOU12418  CE1 PHE D 427     3474   3471   3842    552   -117    173       C  
ATOM  12419  CE2 PHE D 427      91.178 -13.732-214.824  1.00 28.26           C  
ANISOU12419  CE2 PHE D 427     3416   3535   3786    472    -95    221       C  
ATOM  12420  CZ  PHE D 427      91.460 -13.612-216.172  1.00 28.59           C  
ANISOU12420  CZ  PHE D 427     3485   3523   3854    478   -123    206       C  
ATOM  12421  N   MET D 428      88.847  -9.771-212.181  1.00 31.69           N  
ANISOU12421  N   MET D 428     3678   4236   4128    770     49    151       N  
ATOM  12422  CA  MET D 428      87.538 -10.326-211.837  1.00 33.23           C  
ANISOU12422  CA  MET D 428     3760   4575   4292    739     69    186       C  
ATOM  12423  C   MET D 428      86.425  -9.605-212.590  1.00 34.97           C  
ANISOU12423  C   MET D 428     3897   4875   4516    821     66    186       C  
ATOM  12424  O   MET D 428      85.464 -10.233-213.047  1.00 34.55           O  
ANISOU12424  O   MET D 428     3748   4923   4456    767     51    226       O  
ATOM  12425  CB  MET D 428      87.300 -10.251-210.324  1.00 35.91           C  
ANISOU12425  CB  MET D 428     4074   4994   4577    750    124    178       C  
ATOM  12426  CG  MET D 428      88.217 -11.158-209.516  1.00 35.51           C  
ANISOU12426  CG  MET D 428     4090   4888   4512    657    120    195       C  
ATOM  12427  SD  MET D 428      88.075 -12.919-209.881  1.00 39.88           S  
ANISOU12427  SD  MET D 428     4638   5443   5072    500     81    264       S  
ATOM  12428  CE  MET D 428      86.353 -13.248-209.478  1.00 37.78           C  
ANISOU12428  CE  MET D 428     4227   5375   4752    452    117    305       C  
ATOM  12429  N   LYS D 429      86.524  -8.280-212.707  1.00 30.90           N  
ANISOU12429  N   LYS D 429     3418   4317   4004    950     75    143       N  
ATOM  12430  CA  LYS D 429      85.573  -7.540-213.529  1.00 30.62           C  
ANISOU12430  CA  LYS D 429     3321   4339   3976   1047     60    145       C  
ATOM  12431  C   LYS D 429      85.648  -7.984-214.997  1.00 29.96           C  
ANISOU12431  C   LYS D 429     3245   4210   3929    987     -3    177       C  
ATOM  12432  O   LYS D 429      84.621  -8.093-215.672  1.00 31.95           O  
ANISOU12432  O   LYS D 429     3400   4561   4177    997    -27    207       O  
ATOM  12433  CB  LYS D 429      85.833  -6.041-213.387  1.00 39.15           C  
ANISOU12433  CB  LYS D 429     4481   5342   5051   1196     74     93       C  
ATOM  12434  CG  LYS D 429      84.913  -5.163-214.228  1.00 48.97           C  
ANISOU12434  CG  LYS D 429     5681   6625   6299   1323     52     96       C  
ATOM  12435  CD  LYS D 429      83.455  -5.381-213.856  1.00 51.27           C  
ANISOU12435  CD  LYS D 429     5802   7118   6558   1370     80    117       C  
ATOM  12436  CE  LYS D 429      82.537  -4.578-214.756  1.00 61.19           C  
ANISOU12436  CE  LYS D 429     7004   8426   7819   1505     47    126       C  
ATOM  12437  NZ  LYS D 429      81.106  -4.901-214.517  1.00 71.13           N  
ANISOU12437  NZ  LYS D 429     8068   9912   9046   1537     68    153       N  
ATOM  12438  N   HIS D 430      86.853  -8.268-215.496  1.00 31.70           N  
ANISOU12438  N   HIS D 430     3573   4293   4178    923    -30    170       N  
ATOM  12439  CA  HIS D 430      87.007  -8.792-216.857  1.00 32.59           C  
ANISOU12439  CA  HIS D 430     3704   4363   4317    857    -84    194       C  
ATOM  12440  C   HIS D 430      86.285 -10.129-217.037  1.00 35.94           C  
ANISOU12440  C   HIS D 430     4046   4878   4731    740   -102    238       C  
ATOM  12441  O   HIS D 430      85.600 -10.343-218.045  1.00 31.11           O  
ANISOU12441  O   HIS D 430     3386   4315   4121    715   -142    264       O  
ATOM  12442  CB  HIS D 430      88.494  -8.950-217.200  1.00 26.44           C  
ANISOU12442  CB  HIS D 430     3046   3439   3562    810    -97    173       C  
ATOM  12443  CG  HIS D 430      88.732  -9.533-218.553  1.00 32.10           C  
ANISOU12443  CG  HIS D 430     3789   4110   4296    743   -143    189       C  
ATOM  12444  ND1 HIS D 430      88.449  -8.839-219.715  1.00 31.52           N  
ANISOU12444  ND1 HIS D 430     3727   4023   4227    787   -177    194       N  
ATOM  12445  CD2 HIS D 430      89.200 -10.747-218.938  1.00 31.46           C  
ANISOU12445  CD2 HIS D 430     3734   3995   4223    640   -162    201       C  
ATOM  12446  CE1 HIS D 430      88.746  -9.600-220.754  1.00 29.75           C  
ANISOU12446  CE1 HIS D 430     3531   3765   4009    707   -211    205       C  
ATOM  12447  NE2 HIS D 430      89.205 -10.758-220.314  1.00 34.19           N  
ANISOU12447  NE2 HIS D 430     4105   4311   4575    621   -202    206       N  
ATOM  12448  N   LEU D 431      86.455 -11.064-216.083  1.00 30.23           N  
ANISOU12448  N   LEU D 431     3320   4174   3993    656    -78    250       N  
ATOM  12449  CA  LEU D 431      85.747 -12.339-216.181  1.00 30.14           C  
ANISOU12449  CA  LEU D 431     3249   4240   3964    529    -96    295       C  
ATOM  12450  C   LEU D 431      84.244 -12.124-216.255  1.00 31.42           C  
ANISOU12450  C   LEU D 431     3265   4577   4098    545    -94    322       C  
ATOM  12451  O   LEU D 431      83.550 -12.762-217.060  1.00 32.92           O  
ANISOU12451  O   LEU D 431     3400   4827   4279    461   -135    356       O  
ATOM  12452  CB  LEU D 431      86.088 -13.234-214.984  1.00 35.26           C  
ANISOU12452  CB  LEU D 431     3922   4883   4590    448    -68    309       C  
ATOM  12453  CG  LEU D 431      87.516 -13.775-214.932  1.00 37.36           C  
ANISOU12453  CG  LEU D 431     4318   4996   4880    415    -82    294       C  
ATOM  12454  CD1 LEU D 431      87.700 -14.630-213.686  1.00 31.92           C  
ANISOU12454  CD1 LEU D 431     3650   4316   4161    344    -60    318       C  
ATOM  12455  CD2 LEU D 431      87.799 -14.586-216.165  1.00 35.42           C  
ANISOU12455  CD2 LEU D 431     4128   4673   4656    342   -133    303       C  
ATOM  12456  N   GLU D 432      83.730 -11.207-215.439  1.00 29.38           N  
ANISOU12456  N   GLU D 432     2939   4407   3819    657    -47    304       N  
ATOM  12457  CA  GLU D 432      82.300 -10.907-215.469  1.00 34.40           C  
ANISOU12457  CA  GLU D 432     3416   5231   4424    701    -39    326       C  
ATOM  12458  C   GLU D 432      81.881 -10.302-216.811  1.00 34.18           C  
ANISOU12458  C   GLU D 432     3362   5208   4416    769    -93    331       C  
ATOM  12459  O   GLU D 432      80.829 -10.655-217.360  1.00 38.77           O  
ANISOU12459  O   GLU D 432     3824   5928   4979    725   -124    369       O  
ATOM  12460  CB  GLU D 432      81.961  -9.967-214.313  1.00 42.09           C  
ANISOU12460  CB  GLU D 432     4341   6283   5370    834     29    293       C  
ATOM  12461  CG  GLU D 432      80.548  -9.414-214.305  1.00 67.80           C  
ANISOU12461  CG  GLU D 432     7429   9738   8594    930     46    303       C  
ATOM  12462  CD  GLU D 432      80.311  -8.510-213.103  1.00 82.40           C  
ANISOU12462  CD  GLU D 432     9250  11651  10409   1073    121    259       C  
ATOM  12463  OE1 GLU D 432      81.295  -8.229-212.383  1.00 82.44           O  
ANISOU12463  OE1 GLU D 432     9380  11528  10417   1092    150    221       O  
ATOM  12464  OE2 GLU D 432      79.155  -8.090-212.874  1.00 88.33           O  
ANISOU12464  OE2 GLU D 432     9852  12586  11124   1165    150    261       O  
ATOM  12465  N   ASN D 433      82.667  -9.365-217.340  1.00 31.23           N  
ANISOU12465  N   ASN D 433     3098   4694   4074    872   -108    297       N  
ATOM  12466  CA  ASN D 433      82.350  -8.812-218.662  1.00 30.42           C  
ANISOU12466  CA  ASN D 433     2992   4582   3986    929   -166    309       C  
ATOM  12467  C   ASN D 433      82.321  -9.913-219.714  1.00 33.88           C  
ANISOU12467  C   ASN D 433     3432   5014   4427    777   -224    344       C  
ATOM  12468  O   ASN D 433      81.420  -9.963-220.562  1.00 39.89           O  
ANISOU12468  O   ASN D 433     4106   5876   5174    768   -272    375       O  
ATOM  12469  CB  ASN D 433      83.378  -7.757-219.074  1.00 38.18           C  
ANISOU12469  CB  ASN D 433     4121   5392   4995   1025   -174    272       C  
ATOM  12470  CG  ASN D 433      83.352  -6.528-218.194  1.00 40.76           C  
ANISOU12470  CG  ASN D 433     4469   5706   5313   1184   -128    234       C  
ATOM  12471  OD1 ASN D 433      82.371  -6.261-217.510  1.00 40.56           O  
ANISOU12471  OD1 ASN D 433     4331   5819   5260   1264    -96    233       O  
ATOM  12472  ND2 ASN D 433      84.431  -5.760-218.229  1.00 38.51           N  
ANISOU12472  ND2 ASN D 433     4330   5259   5044   1228   -125    198       N  
ATOM  12473  N   GLU D 434      83.327 -10.788-219.689  1.00 32.39           N  
ANISOU12473  N   GLU D 434     3349   4705   4253    662   -224    335       N  
ATOM  12474  CA  GLU D 434      83.478 -11.789-220.737  1.00 32.45           C  
ANISOU12474  CA  GLU D 434     3397   4671   4261    530   -277    355       C  
ATOM  12475  C   GLU D 434      82.429 -12.881-220.625  1.00 36.55           C  
ANISOU12475  C   GLU D 434     3812   5329   4747    396   -294    398       C  
ATOM  12476  O   GLU D 434      82.012 -13.442-221.645  1.00 32.99           O  
ANISOU12476  O   GLU D 434     3348   4904   4282    307   -351    420       O  
ATOM  12477  CB  GLU D 434      84.879 -12.390-220.683  1.00 31.65           C  
ANISOU12477  CB  GLU D 434     3439   4403   4182    470   -268    328       C  
ATOM  12478  CG  GLU D 434      85.976 -11.446-221.092  1.00 29.28           C  
ANISOU12478  CG  GLU D 434     3244   3973   3909    562   -263    291       C  
ATOM  12479  CD  GLU D 434      85.918 -11.097-222.592  1.00 35.49           C  
ANISOU12479  CD  GLU D 434     4060   4732   4695    571   -316    296       C  
ATOM  12480  OE1 GLU D 434      85.199 -10.157-222.962  1.00 40.23           O  
ANISOU12480  OE1 GLU D 434     4607   5392   5286    661   -334    309       O  
ATOM  12481  OE2 GLU D 434      86.591 -11.778-223.388  1.00 40.13           O  
ANISOU12481  OE2 GLU D 434     4727   5238   5284    493   -339    287       O  
ATOM  12482  N   GLN D 435      82.010 -13.217-219.405  1.00 36.60           N  
ANISOU12482  N   GLN D 435     3749   5427   4732    366   -248    410       N  
ATOM  12483  CA  GLN D 435      80.927 -14.180-219.267  1.00 38.52           C  
ANISOU12483  CA  GLN D 435     3883   5821   4933    226   -262    457       C  
ATOM  12484  C   GLN D 435      79.673 -13.679-219.971  1.00 41.18           C  
ANISOU12484  C   GLN D 435     4067   6333   5248    266   -298    483       C  
ATOM  12485  O   GLN D 435      79.018 -14.434-220.701  1.00 43.24           O  
ANISOU12485  O   GLN D 435     4280   6668   5483    134   -352    518       O  
ATOM  12486  CB  GLN D 435      80.655 -14.473-217.789  1.00 40.99           C  
ANISOU12486  CB  GLN D 435     4139   6219   5216    196   -199    469       C  
ATOM  12487  CG  GLN D 435      79.813 -15.721-217.587  1.00 46.91           C  
ANISOU12487  CG  GLN D 435     4820   7087   5917      1   -214    522       C  
ATOM  12488  CD  GLN D 435      80.469 -16.979-218.153  1.00 41.21           C  
ANISOU12488  CD  GLN D 435     4247   6211   5200   -159   -263    532       C  
ATOM  12489  OE1 GLN D 435      81.676 -17.174-218.023  1.00 47.94           O  
ANISOU12489  OE1 GLN D 435     5250   6881   6084   -137   -256    504       O  
ATOM  12490  NE2 GLN D 435      79.673 -17.827-218.793  1.00 42.80           N  
ANISOU12490  NE2 GLN D 435     4407   6489   5366   -318   -314    571       N  
ATOM  12491  N   LYS D 436      79.350 -12.392-219.809  1.00 37.73           N  
ANISOU12491  N   LYS D 436     3561   5956   4819    450   -275    465       N  
ATOM  12492  CA  LYS D 436      78.201 -11.838-220.522  1.00 39.24           C  
ANISOU12492  CA  LYS D 436     3608   6311   4991    518   -317    491       C  
ATOM  12493  C   LYS D 436      78.465 -11.749-222.019  1.00 44.64           C  
ANISOU12493  C   LYS D 436     4367   6906   5690    507   -395    496       C  
ATOM  12494  O   LYS D 436      77.582 -12.054-222.824  1.00 43.62           O  
ANISOU12494  O   LYS D 436     4140   6901   5531    443   -455    534       O  
ATOM  12495  CB  LYS D 436      77.833 -10.456-219.975  1.00 45.34           C  
ANISOU12495  CB  LYS D 436     4311   7150   5766    742   -274    467       C  
ATOM  12496  CG  LYS D 436      77.750 -10.384-218.452  1.00 64.01           C  
ANISOU12496  CG  LYS D 436     6630   9580   8112    777   -187    448       C  
ATOM  12497  CD  LYS D 436      76.952  -9.166-217.992  1.00 76.55           C  
ANISOU12497  CD  LYS D 436     8101  11302   9684    991   -150    429       C  
ATOM  12498  CE  LYS D 436      77.534  -7.863-218.531  1.00 84.17           C  
ANISOU12498  CE  LYS D 436     9186  12109  10684   1181   -170    392       C  
ATOM  12499  NZ  LYS D 436      78.811  -7.483-217.856  1.00 89.65           N  
ANISOU12499  NZ  LYS D 436    10060  12600  11404   1213   -125    342       N  
ATOM  12500  N   ALA D 437      79.668 -11.330-222.421  1.00 40.51           N  
ANISOU12500  N   ALA D 437     4011   6177   5203    561   -397    461       N  
ATOM  12501  CA  ALA D 437      79.868 -11.025-223.836  1.00 42.43           C  
ANISOU12501  CA  ALA D 437     4320   6351   5452    575   -465    466       C  
ATOM  12502  C   ALA D 437      80.064 -12.283-224.680  1.00 43.33           C  
ANISOU12502  C   ALA D 437     4493   6421   5549    384   -514    478       C  
ATOM  12503  O   ALA D 437      79.620 -12.329-225.832  1.00 38.01           O  
ANISOU12503  O   ALA D 437     3801   5787   4852    349   -582    500       O  
ATOM  12504  CB  ALA D 437      81.058 -10.082-224.019  1.00 44.89           C  
ANISOU12504  CB  ALA D 437     4785   6474   5798    690   -448    426       C  
ATOM  12505  N   ARG D 438      80.732 -13.306-224.138  1.00 34.95           N  
ANISOU12505  N   ARG D 438     3513   5271   4494    264   -484    464       N  
ATOM  12506  CA  ARG D 438      81.117 -14.480-224.906  1.00 42.29           C  
ANISOU12506  CA  ARG D 438     4541   6116   5409    102   -526    462       C  
ATOM  12507  C   ARG D 438      80.789 -15.804-224.221  1.00 43.29           C  
ANISOU12507  C   ARG D 438     4655   6282   5512    -67   -517    483       C  
ATOM  12508  O   ARG D 438      80.975 -16.857-224.839  1.00 37.27           O  
ANISOU12508  O   ARG D 438     3981   5451   4729   -209   -557    483       O  
ATOM  12509  CB  ARG D 438      82.629 -14.444-225.227  1.00 40.41           C  
ANISOU12509  CB  ARG D 438     4482   5668   5204    133   -508    416       C  
ATOM  12510  CG  ARG D 438      83.071 -13.282-226.091  1.00 45.30           C  
ANISOU12510  CG  ARG D 438     5147   6227   5836    257   -523    399       C  
ATOM  12511  CD  ARG D 438      84.308 -13.643-226.924  1.00 47.22           C  
ANISOU12511  CD  ARG D 438     5549   6307   6086    217   -530    363       C  
ATOM  12512  NE  ARG D 438      85.499 -13.851-226.110  1.00 39.72           N  
ANISOU12512  NE  ARG D 438     4687   5237   5168    234   -472    327       N  
ATOM  12513  CZ  ARG D 438      86.698 -14.147-226.600  1.00 40.35           C  
ANISOU12513  CZ  ARG D 438     4889   5186   5255    219   -463    290       C  
ATOM  12514  NH1 ARG D 438      86.882 -14.275-227.905  1.00 44.50           N  
ANISOU12514  NH1 ARG D 438     5476   5676   5757    183   -501    280       N  
ATOM  12515  NH2 ARG D 438      87.721 -14.304-225.783  1.00 37.45           N  
ANISOU12515  NH2 ARG D 438     4579   4734   4915    243   -414    262       N  
ATOM  12516  N   GLY D 439      80.321 -15.793-222.974  1.00 35.69           N  
ANISOU12516  N   GLY D 439     3598   5420   4543    -59   -467    500       N  
ATOM  12517  CA  GLY D 439      80.012 -17.037-222.297  1.00 41.09           C  
ANISOU12517  CA  GLY D 439     4281   6137   5195   -231   -460    527       C  
ATOM  12518  C   GLY D 439      81.209 -17.731-221.692  1.00 40.89           C  
ANISOU12518  C   GLY D 439     4419   5927   5191   -266   -429    503       C  
ATOM  12519  O   GLY D 439      81.152 -18.938-221.427  1.00 40.34           O  
ANISOU12519  O   GLY D 439     4408   5827   5094   -424   -442    525       O  
ATOM  12520  N   GLY D 440      82.297 -17.013-221.463  1.00 37.69           N  
ANISOU12520  N   GLY D 440     4093   5397   4829   -126   -392    461       N  
ATOM  12521  CA  GLY D 440      83.438 -17.599-220.793  1.00 36.76           C  
ANISOU12521  CA  GLY D 440     4109   5128   4731   -141   -363    441       C  
ATOM  12522  C   GLY D 440      84.687 -16.813-221.113  1.00 35.48           C  
ANISOU12522  C   GLY D 440     4038   4828   4613     -6   -347    391       C  
ATOM  12523  O   GLY D 440      84.668 -15.856-221.882  1.00 33.97           O  
ANISOU12523  O   GLY D 440     3825   4648   4436     85   -359    375       O  
ATOM  12524  N   CYS D 441      85.781 -17.256-220.510  1.00 32.08           N  
ANISOU12524  N   CYS D 441     3714   4275   4200     -2   -322    371       N  
ATOM  12525  CA  CYS D 441      87.061 -16.572-220.649  1.00 32.85           C  
ANISOU12525  CA  CYS D 441     3890   4257   4334    110   -302    326       C  
ATOM  12526  C   CYS D 441      88.189 -17.565-220.413  1.00 35.92           C  
ANISOU12526  C   CYS D 441     4405   4511   4733     73   -301    310       C  
ATOM  12527  O   CYS D 441      88.279 -18.139-219.314  1.00 34.23           O  
ANISOU12527  O   CYS D 441     4205   4292   4510     39   -283    329       O  
ATOM  12528  CB  CYS D 441      87.166 -15.413-219.646  1.00 36.21           C  
ANISOU12528  CB  CYS D 441     4260   4727   4773    228   -252    315       C  
ATOM  12529  SG  CYS D 441      88.796 -14.627-219.590  1.00 37.98           S  
ANISOU12529  SG  CYS D 441     4581   4817   5031    334   -227    264       S  
ATOM  12530  N   PRO D 442      89.076 -17.776-221.385  1.00 32.47           N  
ANISOU12530  N   PRO D 442     4060   3967   4308     86   -319    275       N  
ATOM  12531  CA  PRO D 442      90.207 -18.686-221.153  1.00 32.21           C  
ANISOU12531  CA  PRO D 442     4142   3812   4285     79   -316    255       C  
ATOM  12532  C   PRO D 442      91.175 -18.076-220.146  1.00 31.97           C  
ANISOU12532  C   PRO D 442     4109   3759   4277    174   -275    239       C  
ATOM  12533  O   PRO D 442      91.605 -16.931-220.292  1.00 30.35           O  
ANISOU12533  O   PRO D 442     3876   3567   4091    258   -254    215       O  
ATOM  12534  CB  PRO D 442      90.843 -18.830-222.540  1.00 36.30           C  
ANISOU12534  CB  PRO D 442     4735   4253   4805     89   -337    215       C  
ATOM  12535  CG  PRO D 442      90.523 -17.518-223.221  1.00 33.81           C  
ANISOU12535  CG  PRO D 442     4347   4004   4494    146   -334    208       C  
ATOM  12536  CD  PRO D 442      89.143 -17.123-222.710  1.00 34.80           C  
ANISOU12536  CD  PRO D 442     4359   4256   4607    122   -339    252       C  
ATOM  12537  N   ALA D 443      91.529 -18.851-219.126  1.00 28.92           N  
ANISOU12537  N   ALA D 443     3766   3337   3887    153   -269    256       N  
ATOM  12538  CA  ALA D 443      92.348 -18.293-218.060  1.00 28.42           C  
ANISOU12538  CA  ALA D 443     3693   3270   3836    230   -237    246       C  
ATOM  12539  C   ALA D 443      93.150 -19.407-217.410  1.00 30.07           C  
ANISOU12539  C   ALA D 443     3990   3394   4042    218   -248    255       C  
ATOM  12540  O   ALA D 443      92.611 -20.486-217.143  1.00 29.23           O  
ANISOU12540  O   ALA D 443     3928   3266   3911    133   -271    292       O  
ATOM  12541  CB  ALA D 443      91.479 -17.569-217.021  1.00 28.34           C  
ANISOU12541  CB  ALA D 443     3589   3369   3810    236   -207    271       C  
ATOM  12542  N   ASP D 444      94.441 -19.141-217.198  1.00 29.21           N  
ANISOU12542  N   ASP D 444     3909   3239   3952    301   -237    225       N  
ATOM  12543  CA  ASP D 444      95.398 -20.088-216.623  1.00 26.12           C  
ANISOU12543  CA  ASP D 444     3596   2769   3558    323   -252    229       C  
ATOM  12544  C   ASP D 444      95.558 -19.706-215.143  1.00 25.22           C  
ANISOU12544  C   ASP D 444     3446   2704   3432    344   -234    253       C  
ATOM  12545  O   ASP D 444      96.267 -18.756-214.824  1.00 28.54           O  
ANISOU12545  O   ASP D 444     3826   3155   3863    410   -212    227       O  
ATOM  12546  CB  ASP D 444      96.716 -19.988-217.381  1.00 30.06           C  
ANISOU12546  CB  ASP D 444     4126   3216   4081    405   -251    179       C  
ATOM  12547  CG  ASP D 444      97.720 -21.040-216.995  1.00 34.62           C  
ANISOU12547  CG  ASP D 444     4783   3713   4656    451   -272    179       C  
ATOM  12548  OD1 ASP D 444      97.684 -21.528-215.849  1.00 39.93           O  
ANISOU12548  OD1 ASP D 444     5479   4378   5315    439   -284    219       O  
ATOM  12549  OD2 ASP D 444      98.577 -21.346-217.854  1.00 34.20           O  
ANISOU12549  OD2 ASP D 444     4768   3612   4614    506   -275    138       O  
ATOM  12550  N   TRP D 445      94.908 -20.468-214.253  1.00 29.74           N  
ANISOU12550  N   TRP D 445     4042   3282   3973    276   -244    304       N  
ATOM  12551  CA  TRP D 445      94.872 -20.111-212.831  1.00 27.22           C  
ANISOU12551  CA  TRP D 445     3689   3024   3629    281   -224    330       C  
ATOM  12552  C   TRP D 445      96.281 -19.914-212.274  1.00 27.00           C  
ANISOU12552  C   TRP D 445     3684   2965   3611    368   -229    310       C  
ATOM  12553  O   TRP D 445      96.569 -18.923-211.584  1.00 30.92           O  
ANISOU12553  O   TRP D 445     4126   3522   4100    407   -204    294       O  
ATOM  12554  CB  TRP D 445      94.126 -21.209-212.070  1.00 27.90           C  
ANISOU12554  CB  TRP D 445     3823   3105   3674    183   -241    393       C  
ATOM  12555  CG  TRP D 445      93.815 -20.933-210.618  1.00 34.76           C  
ANISOU12555  CG  TRP D 445     4654   4053   4499    163   -216    428       C  
ATOM  12556  CD1 TRP D 445      92.643 -20.442-210.108  1.00 32.67           C  
ANISOU12556  CD1 TRP D 445     4304   3907   4200    109   -179    447       C  
ATOM  12557  CD2 TRP D 445      94.686 -21.142-209.496  1.00 26.66           C  
ANISOU12557  CD2 TRP D 445     3674   3004   3452    200   -226    445       C  
ATOM  12558  NE1 TRP D 445      92.733 -20.334-208.728  1.00 32.28           N  
ANISOU12558  NE1 TRP D 445     4251   3906   4106    106   -160    472       N  
ATOM  12559  CE2 TRP D 445      93.976 -20.754-208.334  1.00 31.67           C  
ANISOU12559  CE2 TRP D 445     4256   3742   4036    157   -192    474       C  
ATOM  12560  CE3 TRP D 445      96.002 -21.608-209.360  1.00 27.45           C  
ANISOU12560  CE3 TRP D 445     3845   3017   3566    271   -262    440       C  
ATOM  12561  CZ2 TRP D 445      94.536 -20.824-207.051  1.00 30.03           C  
ANISOU12561  CZ2 TRP D 445     4078   3546   3788    172   -195    498       C  
ATOM  12562  CZ3 TRP D 445      96.552 -21.700-208.063  1.00 30.81           C  
ANISOU12562  CZ3 TRP D 445     4294   3459   3955    290   -271    469       C  
ATOM  12563  CH2 TRP D 445      95.825 -21.282-206.941  1.00 31.48           C  
ANISOU12563  CH2 TRP D 445     4334   3640   3987    237   -238    497       C  
ATOM  12564  N   ALA D 446      97.174 -20.851-212.567  1.00 27.26           N  
ANISOU12564  N   ALA D 446     3795   2906   3654    402   -263    308       N  
ATOM  12565  CA  ALA D 446      98.525 -20.805-212.008  1.00 32.91           C  
ANISOU12565  CA  ALA D 446     4523   3608   4375    487   -275    295       C  
ATOM  12566  C   ALA D 446      99.272 -19.533-212.385  1.00 35.07           C  
ANISOU12566  C   ALA D 446     4720   3935   4671    547   -248    241       C  
ATOM  12567  O   ALA D 446     100.152 -19.084-211.642  1.00 30.58           O  
ANISOU12567  O   ALA D 446     4125   3400   4093    591   -250    234       O  
ATOM  12568  CB  ALA D 446      99.315 -22.030-212.458  1.00 30.80           C  
ANISOU12568  CB  ALA D 446     4349   3237   4118    533   -315    296       C  
ATOM  12569  N   TRP D 447      98.949 -18.940-213.537  1.00 32.93           N  
ANISOU12569  N   TRP D 447     4419   3671   4422    540   -229    206       N  
ATOM  12570  CA  TRP D 447      99.580 -17.696-213.964  1.00 24.95           C  
ANISOU12570  CA  TRP D 447     3352   2703   3426    579   -205    161       C  
ATOM  12571  C   TRP D 447      98.804 -16.453-213.538  1.00 27.16           C  
ANISOU12571  C   TRP D 447     3578   3047   3694    557   -175    158       C  
ATOM  12572  O   TRP D 447      99.400 -15.375-213.373  1.00 28.38           O  
ANISOU12572  O   TRP D 447     3704   3232   3846    582   -160    129       O  
ATOM  12573  CB  TRP D 447      99.751 -17.731-215.508  1.00 24.50           C  
ANISOU12573  CB  TRP D 447     3305   2613   3391    589   -202    126       C  
ATOM  12574  CG  TRP D 447     100.979 -18.561-215.924  1.00 25.71           C  
ANISOU12574  CG  TRP D 447     3494   2723   3554    650   -219    104       C  
ATOM  12575  CD1 TRP D 447     101.165 -19.898-215.769  1.00 30.74           C  
ANISOU12575  CD1 TRP D 447     4202   3292   4187    671   -249    123       C  
ATOM  12576  CD2 TRP D 447     102.185 -18.053-216.507  1.00 30.24           C  
ANISOU12576  CD2 TRP D 447     4031   3325   4134    701   -205     61       C  
ATOM  12577  NE1 TRP D 447     102.408 -20.262-216.243  1.00 34.15           N  
ANISOU12577  NE1 TRP D 447     4640   3710   4626    752   -253     88       N  
ATOM  12578  CE2 TRP D 447     103.052 -19.141-216.694  1.00 32.34           C  
ANISOU12578  CE2 TRP D 447     4335   3552   4403    767   -223     51       C  
ATOM  12579  CE3 TRP D 447     102.603 -16.780-216.899  1.00 41.35           C  
ANISOU12579  CE3 TRP D 447     5382   4789   5541    694   -178     32       C  
ATOM  12580  CZ2 TRP D 447     104.312 -19.000-217.264  1.00 41.86           C  
ANISOU12580  CZ2 TRP D 447     5501   4793   5609    830   -211      9       C  
ATOM  12581  CZ3 TRP D 447     103.855 -16.640-217.459  1.00 49.82           C  
ANISOU12581  CZ3 TRP D 447     6424   5893   6612    735   -168     -4       C  
ATOM  12582  CH2 TRP D 447     104.693 -17.749-217.639  1.00 43.55           C  
ANISOU12582  CH2 TRP D 447     5647   5079   5820    805   -181    -16       C  
ATOM  12583  N   ILE D 448      97.481 -16.562-213.385  1.00 24.94           N  
ANISOU12583  N   ILE D 448     3286   2790   3401    509   -167    186       N  
ATOM  12584  CA  ILE D 448      96.679 -15.412-212.993  1.00 22.94           C  
ANISOU12584  CA  ILE D 448     2981   2602   3134    510   -136    179       C  
ATOM  12585  C   ILE D 448      96.871 -15.083-211.503  1.00 26.83           C  
ANISOU12585  C   ILE D 448     3466   3136   3591    518   -122    187       C  
ATOM  12586  O   ILE D 448      96.923 -13.908-211.113  1.00 28.63           O  
ANISOU12586  O   ILE D 448     3673   3397   3807    547    -98    158       O  
ATOM  12587  CB  ILE D 448      95.199 -15.687-213.328  1.00 27.78           C  
ANISOU12587  CB  ILE D 448     3565   3251   3740    462   -131    207       C  
ATOM  12588  CG1 ILE D 448      95.004 -15.831-214.863  1.00 24.87           C  
ANISOU12588  CG1 ILE D 448     3205   2848   3398    451   -148    194       C  
ATOM  12589  CG2 ILE D 448      94.296 -14.558-212.784  1.00 29.58           C  
ANISOU12589  CG2 ILE D 448     3731   3560   3947    483    -96    200       C  
ATOM  12590  CD1 ILE D 448      95.304 -14.553-215.646  1.00 26.01           C  
ANISOU12590  CD1 ILE D 448     3331   2992   3558    502   -136    154       C  
ATOM  12591  N   VAL D 449      96.967 -16.107-210.664  1.00 27.66           N  
ANISOU12591  N   VAL D 449     3601   3234   3675    491   -139    226       N  
ATOM  12592  CA  VAL D 449      97.207 -15.895-209.221  1.00 24.06           C  
ANISOU12592  CA  VAL D 449     3146   2820   3176    493   -131    237       C  
ATOM  12593  C   VAL D 449      98.615 -15.346-209.028  1.00 28.33           C  
ANISOU12593  C   VAL D 449     3694   3349   3721    540   -145    204       C  
ATOM  12594  O   VAL D 449      99.587 -15.986-209.454  1.00 29.29           O  
ANISOU12594  O   VAL D 449     3838   3427   3865    563   -176    204       O  
ATOM  12595  CB  VAL D 449      97.022 -17.205-208.455  1.00 27.87           C  
ANISOU12595  CB  VAL D 449     3671   3289   3628    447   -155    296       C  
ATOM  12596  CG1 VAL D 449      97.432 -17.040-206.962  1.00 29.78           C  
ANISOU12596  CG1 VAL D 449     3923   3574   3819    449   -154    311       C  
ATOM  12597  CG2 VAL D 449      95.577 -17.669-208.560  1.00 29.61           C  
ANISOU12597  CG2 VAL D 449     3874   3542   3833    375   -138    332       C  
ATOM  12598  N   PRO D 450      98.779 -14.220-208.336  1.00 32.85           N  
ANISOU12598  N   PRO D 450     4250   3964   4266    553   -124    174       N  
ATOM  12599  CA  PRO D 450     100.103 -13.594-208.199  1.00 30.39           C  
ANISOU12599  CA  PRO D 450     3941   3653   3952    577   -139    141       C  
ATOM  12600  C   PRO D 450     101.056 -14.450-207.380  1.00 32.91           C  
ANISOU12600  C   PRO D 450     4276   3978   4251    583   -179    170       C  
ATOM  12601  O   PRO D 450     100.626 -15.335-206.623  1.00 31.41           O  
ANISOU12601  O   PRO D 450     4110   3791   4035    565   -190    217       O  
ATOM  12602  CB  PRO D 450      99.794 -12.268-207.472  1.00 33.78           C  
ANISOU12602  CB  PRO D 450     4370   4121   4343    576   -108    107       C  
ATOM  12603  CG  PRO D 450      98.305 -12.119-207.492  1.00 46.00           C  
ANISOU12603  CG  PRO D 450     5903   5691   5884    575    -71    115       C  
ATOM  12604  CD  PRO D 450      97.733 -13.489-207.606  1.00 36.47           C  
ANISOU12604  CD  PRO D 450     4690   4481   4687    545    -84    169       C  
ATOM  12605  N   PRO D 451     102.366 -14.187-207.482  1.00 38.47           N  
ANISOU12605  N   PRO D 451     4965   4692   4959    604   -203    148       N  
ATOM  12606  CA  PRO D 451     103.363 -15.044-206.820  1.00 33.23           C  
ANISOU12606  CA  PRO D 451     4306   4042   4280    629   -250    177       C  
ATOM  12607  C   PRO D 451     103.558 -14.775-205.336  1.00 32.18           C  
ANISOU12607  C   PRO D 451     4181   3962   4083    608   -264    192       C  
ATOM  12608  O   PRO D 451     104.290 -15.535-204.691  1.00 38.20           O  
ANISOU12608  O   PRO D 451     4951   4739   4825    631   -310    226       O  
ATOM  12609  CB  PRO D 451     104.656 -14.728-207.593  1.00 30.07           C  
ANISOU12609  CB  PRO D 451     3862   3660   3904    658   -265    142       C  
ATOM  12610  CG  PRO D 451     104.454 -13.321-208.066  1.00 32.21           C  
ANISOU12610  CG  PRO D 451     4120   3941   4176    621   -228     94       C  
ATOM  12611  CD  PRO D 451     102.992 -13.221-208.404  1.00 35.78           C  
ANISOU12611  CD  PRO D 451     4600   4353   4643    607   -192     99       C  
ATOM  12612  N   ILE D 452     102.996 -13.704-204.791  1.00 29.14           N  
ANISOU12612  N   ILE D 452     3802   3609   3664    574   -230    164       N  
ATOM  12613  CA  ILE D 452     102.892 -13.542-203.338  1.00 32.22           C  
ANISOU12613  CA  ILE D 452     4213   4047   3981    548   -234    178       C  
ATOM  12614  C   ILE D 452     101.420 -13.328-203.034  1.00 38.27           C  
ANISOU12614  C   ILE D 452     4996   4819   4726    527   -181    180       C  
ATOM  12615  O   ILE D 452     100.649 -12.910-203.905  1.00 34.50           O  
ANISOU12615  O   ILE D 452     4505   4318   4286    535   -144    157       O  
ATOM  12616  CB  ILE D 452     103.728 -12.373-202.774  1.00 33.60           C  
ANISOU12616  CB  ILE D 452     4385   4268   4114    526   -242    131       C  
ATOM  12617  CG1 ILE D 452     103.430 -11.075-203.541  1.00 38.09           C  
ANISOU12617  CG1 ILE D 452     4957   4812   4703    516   -201     70       C  
ATOM  12618  CG2 ILE D 452     105.212 -12.716-202.754  1.00 41.91           C  
ANISOU12618  CG2 ILE D 452     5402   5353   5168    539   -302    140       C  
ATOM  12619  CD1 ILE D 452     103.886  -9.811-202.780  1.00 41.73           C  
ANISOU12619  CD1 ILE D 452     5450   5303   5104    478   -201     21       C  
ATOM  12620  N   SER D 453     101.020 -13.689-201.819  1.00 36.73           N  
ANISOU12620  N   SER D 453     4824   4664   4466    501   -179    214       N  
ATOM  12621  CA  SER D 453      99.708 -13.335-201.270  1.00 39.36           C  
ANISOU12621  CA  SER D 453     5161   5039   4757    480   -122    209       C  
ATOM  12622  C   SER D 453      98.547 -13.903-202.091  1.00 32.93           C  
ANISOU12622  C   SER D 453     4322   4206   3984    473    -93    235       C  
ATOM  12623  O   SER D 453      97.467 -13.311-202.141  1.00 30.37           O  
ANISOU12623  O   SER D 453     3972   3919   3648    476    -40    213       O  
ATOM  12624  CB  SER D 453      99.576 -11.813-201.135  1.00 39.52           C  
ANISOU12624  CB  SER D 453     5184   5078   4754    497    -82    135       C  
ATOM  12625  OG  SER D 453     100.505 -11.304-200.178  1.00 43.49           O  
ANISOU12625  OG  SER D 453     5718   5608   5198    481   -107    113       O  
ATOM  12626  N   GLY D 454      98.738 -15.079-202.693  1.00 33.49           N  
ANISOU12626  N   GLY D 454     4403   4224   4095    465   -131    282       N  
ATOM  12627  CA  GLY D 454      97.760 -15.592-203.647  1.00 30.28           C  
ANISOU12627  CA  GLY D 454     3980   3794   3731    447   -114    301       C  
ATOM  12628  C   GLY D 454      96.330 -15.596-203.135  1.00 35.06           C  
ANISOU12628  C   GLY D 454     4558   4471   4292    402    -64    321       C  
ATOM  12629  O   GLY D 454      95.428 -15.066-203.787  1.00 31.83           O  
ANISOU12629  O   GLY D 454     4100   4089   3904    411    -26    297       O  
ATOM  12630  N   SER D 455      96.092 -16.199-201.961  1.00 30.14           N  
ANISOU12630  N   SER D 455     3961   3892   3600    352    -63    370       N  
ATOM  12631  CA  SER D 455      94.718 -16.295-201.480  1.00 29.44           C  
ANISOU12631  CA  SER D 455     3834   3892   3460    297    -11    394       C  
ATOM  12632  C   SER D 455      94.186 -14.980-200.916  1.00 28.65           C  
ANISOU12632  C   SER D 455     3686   3882   3317    339     53    335       C  
ATOM  12633  O   SER D 455      93.005 -14.906-200.558  1.00 32.96           O  
ANISOU12633  O   SER D 455     4181   4525   3819    312    107    344       O  
ATOM  12634  CB  SER D 455      94.581 -17.400-200.423  1.00 35.77           C  
ANISOU12634  CB  SER D 455     4686   4714   4191    216    -28    471       C  
ATOM  12635  OG  SER D 455      95.266 -17.065-199.226  1.00 37.59           O  
ANISOU12635  OG  SER D 455     4951   4974   4357    230    -34    466       O  
ATOM  12636  N   LEU D 456      95.002 -13.942-200.835  1.00 26.47           N  
ANISOU12636  N   LEU D 456     3428   3580   3047    402     50    273       N  
ATOM  12637  CA  LEU D 456      94.478 -12.642-200.443  1.00 29.45           C  
ANISOU12637  CA  LEU D 456     3782   4019   3388    454    109    208       C  
ATOM  12638  C   LEU D 456      93.856 -11.914-201.625  1.00 32.04           C  
ANISOU12638  C   LEU D 456     4063   4332   3778    512    132    168       C  
ATOM  12639  O   LEU D 456      93.251 -10.855-201.429  1.00 35.25           O  
ANISOU12639  O   LEU D 456     4451   4783   4158    572    182    115       O  
ATOM  12640  CB  LEU D 456      95.592 -11.789-199.831  1.00 31.91           C  
ANISOU12640  CB  LEU D 456     4152   4302   3671    483     91    157       C  
ATOM  12641  CG  LEU D 456      96.351 -12.486-198.692  1.00 35.38           C  
ANISOU12641  CG  LEU D 456     4638   4757   4048    432     53    199       C  
ATOM  12642  CD1 LEU D 456      97.370 -11.531-198.132  1.00 43.94           C  
ANISOU12642  CD1 LEU D 456     5770   5829   5098    452     34    143       C  
ATOM  12643  CD2 LEU D 456      95.405 -12.962-197.624  1.00 32.29           C  
ANISOU12643  CD2 LEU D 456     4237   4462   3571    384     96    238       C  
ATOM  12644  N   THR D 457      93.963 -12.486-202.826  1.00 32.52           N  
ANISOU12644  N   THR D 457     4112   4332   3913    500     96    193       N  
ATOM  12645  CA  THR D 457      93.390 -11.889-204.016  1.00 31.43           C  
ANISOU12645  CA  THR D 457     3933   4180   3831    547    109    164       C  
ATOM  12646  C   THR D 457      92.154 -12.679-204.439  1.00 29.35           C  
ANISOU12646  C   THR D 457     3601   3980   3572    503    123    212       C  
ATOM  12647  O   THR D 457      92.049 -13.884-204.161  1.00 32.29           O  
ANISOU12647  O   THR D 457     3980   4360   3928    420    104    272       O  
ATOM  12648  CB  THR D 457      94.405 -11.840-205.170  1.00 32.35           C  
ANISOU12648  CB  THR D 457     4083   4189   4018    562     60    150       C  
ATOM  12649  OG1 THR D 457      94.730 -13.163-205.631  1.00 30.21           O  
ANISOU12649  OG1 THR D 457     3823   3876   3778    507     17    203       O  
ATOM  12650  CG2 THR D 457      95.676 -11.131-204.725  1.00 31.88           C  
ANISOU12650  CG2 THR D 457     4082   4085   3947    583     42    110       C  
ATOM  12651  N   PRO D 458      91.187 -12.027-205.090  1.00 30.60           N  
ANISOU12651  N   PRO D 458     3694   4185   3747    552    152    190       N  
ATOM  12652  CA  PRO D 458      89.938 -12.727-205.416  1.00 30.01           C  
ANISOU12652  CA  PRO D 458     3536   4200   3666    499    165    236       C  
ATOM  12653  C   PRO D 458      90.110 -13.817-206.468  1.00 30.06           C  
ANISOU12653  C   PRO D 458     3560   4137   3724    425    111    280       C  
ATOM  12654  O   PRO D 458      89.300 -14.751-206.489  1.00 32.28           O  
ANISOU12654  O   PRO D 458     3802   4478   3985    336    109    333       O  
ATOM  12655  CB  PRO D 458      89.022 -11.600-205.918  1.00 34.95           C  
ANISOU12655  CB  PRO D 458     4090   4890   4300    596    201    194       C  
ATOM  12656  CG  PRO D 458      89.996 -10.555-206.455  1.00 37.70           C  
ANISOU12656  CG  PRO D 458     4513   5119   4690    680    179    137       C  
ATOM  12657  CD  PRO D 458      91.167 -10.614-205.517  1.00 29.90           C  
ANISOU12657  CD  PRO D 458     3609   4074   3676    656    170    125       C  
ATOM  12658  N   VAL D 459      91.142 -13.746-207.316  1.00 33.08           N  
ANISOU12658  N   VAL D 459     4004   4400   4164    451     68    260       N  
ATOM  12659  CA  VAL D 459      91.280 -14.741-208.378  1.00 31.69           C  
ANISOU12659  CA  VAL D 459     3851   4157   4031    393     20    291       C  
ATOM  12660  C   VAL D 459      91.626 -16.115-207.806  1.00 31.07           C  
ANISOU12660  C   VAL D 459     3832   4042   3930    305     -8    345       C  
ATOM  12661  O   VAL D 459      91.282 -17.139-208.406  1.00 30.90           O  
ANISOU12661  O   VAL D 459     3828   3993   3919    231    -38    383       O  
ATOM  12662  CB  VAL D 459      92.323 -14.297-209.429  1.00 29.75           C  
ANISOU12662  CB  VAL D 459     3654   3806   3844    448    -11    251       C  
ATOM  12663  CG1 VAL D 459      91.851 -13.050-210.170  1.00 24.66           C  
ANISOU12663  CG1 VAL D 459     2967   3183   3219    522      7    211       C  
ATOM  12664  CG2 VAL D 459      93.662 -14.024-208.785  1.00 27.85           C  
ANISOU12664  CG2 VAL D 459     3474   3509   3599    481    -20    227       C  
ATOM  12665  N   PHE D 460      92.258 -16.164-206.624  1.00 31.10           N  
ANISOU12665  N   PHE D 460     3877   4045   3895    309     -3    351       N  
ATOM  12666  CA  PHE D 460      92.605 -17.447-206.020  1.00 24.07           C  
ANISOU12666  CA  PHE D 460     3055   3113   2977    236    -36    409       C  
ATOM  12667  C   PHE D 460      91.367 -18.319-205.836  1.00 27.09           C  
ANISOU12667  C   PHE D 460     3413   3563   3319    124    -25    469       C  
ATOM  12668  O   PHE D 460      91.413 -19.545-206.012  1.00 32.42           O  
ANISOU12668  O   PHE D 460     4158   4171   3990     44    -67    520       O  
ATOM  12669  CB  PHE D 460      93.283 -17.193-204.666  1.00 30.38           C  
ANISOU12669  CB  PHE D 460     3887   3932   3726    257    -28    409       C  
ATOM  12670  CG  PHE D 460      93.766 -18.432-203.976  1.00 29.86           C  
ANISOU12670  CG  PHE D 460     3904   3815   3626    198    -70    472       C  
ATOM  12671  CD1 PHE D 460      92.901 -19.227-203.227  1.00 29.66           C  
ANISOU12671  CD1 PHE D 460     3889   3845   3537     97    -59    536       C  
ATOM  12672  CD2 PHE D 460      95.103 -18.805-204.070  1.00 28.34           C  
ANISOU12672  CD2 PHE D 460     3782   3525   3463    246   -124    470       C  
ATOM  12673  CE1 PHE D 460      93.358 -20.362-202.584  1.00 33.82           C  
ANISOU12673  CE1 PHE D 460     4512   4310   4027     44   -104    601       C  
ATOM  12674  CE2 PHE D 460      95.566 -19.940-203.436  1.00 34.00           C  
ANISOU12674  CE2 PHE D 460     4583   4187   4147    211   -170    531       C  
ATOM  12675  CZ  PHE D 460      94.701 -20.721-202.684  1.00 33.82           C  
ANISOU12675  CZ  PHE D 460     4591   4200   4061    109   -163    598       C  
ATOM  12676  N   HIS D 461      90.258 -17.698-205.448  1.00 26.54           N  
ANISOU12676  N   HIS D 461     3246   3627   3209    116     30    464       N  
ATOM  12677  CA  HIS D 461      89.028 -18.387-205.093  1.00 30.19           C  
ANISOU12677  CA  HIS D 461     3659   4196   3616      0     51    520       C  
ATOM  12678  C   HIS D 461      88.111 -18.613-206.288  1.00 33.11           C  
ANISOU12678  C   HIS D 461     3967   4597   4017    -47     39    529       C  
ATOM  12679  O   HIS D 461      86.997 -19.121-206.112  1.00 32.70           O  
ANISOU12679  O   HIS D 461     3852   4654   3918   -154     57    575       O  
ATOM  12680  CB  HIS D 461      88.319 -17.581-204.010  1.00 35.15           C  
ANISOU12680  CB  HIS D 461     4201   4978   4177     26    123    506       C  
ATOM  12681  CG  HIS D 461      89.207 -17.273-202.846  1.00 35.01           C  
ANISOU12681  CG  HIS D 461     4247   4936   4120     69    133    491       C  
ATOM  12682  ND1 HIS D 461      89.535 -18.216-201.897  1.00 35.45           N  
ANISOU12682  ND1 HIS D 461     4379   4971   4118    -17    113    551       N  
ATOM  12683  CD2 HIS D 461      89.882 -16.147-202.507  1.00 38.42           C  
ANISOU12683  CD2 HIS D 461     4689   5352   4558    181    151    426       C  
ATOM  12684  CE1 HIS D 461      90.355 -17.680-201.007  1.00 35.67           C  
ANISOU12684  CE1 HIS D 461     4449   4985   4117     45    119    523       C  
ATOM  12685  NE2 HIS D 461      90.573 -16.422-201.346  1.00 36.82           N  
ANISOU12685  NE2 HIS D 461     4557   5135   4299    159    143    445       N  
ATOM  12686  N   GLN D 462      88.569 -18.271-207.490  1.00 31.20           N  
ANISOU12686  N   GLN D 462     3740   4269   3846     20      9    489       N  
ATOM  12687  CA  GLN D 462      87.779 -18.371-208.715  1.00 27.93           C  
ANISOU12687  CA  GLN D 462     3270   3881   3461    -14     -9    490       C  
ATOM  12688  C   GLN D 462      88.276 -19.546-209.549  1.00 29.82           C  
ANISOU12688  C   GLN D 462     3619   3984   3730    -88    -73    514       C  
ATOM  12689  O   GLN D 462      89.429 -19.552-209.985  1.00 33.00           O  
ANISOU12689  O   GLN D 462     4105   4257   4177    -21   -102    483       O  
ATOM  12690  CB  GLN D 462      87.888 -17.078-209.517  1.00 33.54           C  
ANISOU12690  CB  GLN D 462     3928   4594   4220    116      2    428       C  
ATOM  12691  CG  GLN D 462      87.223 -17.169-210.890  1.00 29.01           C  
ANISOU12691  CG  GLN D 462     3310   4034   3677     90    -29    430       C  
ATOM  12692  CD  GLN D 462      85.719 -17.274-210.761  1.00 35.53           C  
ANISOU12692  CD  GLN D 462     4008   5033   4457     21     -6    465       C  
ATOM  12693  OE1 GLN D 462      85.076 -16.402-210.163  1.00 33.96           O  
ANISOU12693  OE1 GLN D 462     3708   4964   4231     90     45    450       O  
ATOM  12694  NE2 GLN D 462      85.147 -18.352-211.299  1.00 31.07           N  
ANISOU12694  NE2 GLN D 462     3447   4479   3878   -118    -44    511       N  
ATOM  12695  N   GLU D 463      87.424 -20.540-209.759  1.00 32.56           N  
ANISOU12695  N   GLU D 463     3966   4360   4044   -228    -94    566       N  
ATOM  12696  CA  GLU D 463      87.797 -21.612-210.672  1.00 29.31           C  
ANISOU12696  CA  GLU D 463     3669   3811   3656   -294   -156    579       C  
ATOM  12697  C   GLU D 463      87.888 -21.050-212.091  1.00 31.55           C  
ANISOU12697  C   GLU D 463     3925   4065   3995   -227   -174    528       C  
ATOM  12698  O   GLU D 463      87.185 -20.108-212.443  1.00 30.39           O  
ANISOU12698  O   GLU D 463     3660   4032   3856   -183   -149    508       O  
ATOM  12699  CB  GLU D 463      86.787 -22.755-210.611  1.00 31.99           C  
ANISOU12699  CB  GLU D 463     4024   4190   3940   -479   -178    646       C  
ATOM  12700  CG  GLU D 463      86.759 -23.444-209.233  1.00 37.47           C  
ANISOU12700  CG  GLU D 463     4772   4895   4569   -565   -166    707       C  
ATOM  12701  CD  GLU D 463      85.703 -24.527-209.138  1.00 43.62           C  
ANISOU12701  CD  GLU D 463     5566   5724   5282   -771   -185    779       C  
ATOM  12702  OE1 GLU D 463      84.874 -24.614-210.062  1.00 42.37           O  
ANISOU12702  OE1 GLU D 463     5346   5625   5126   -845   -201    779       O  
ATOM  12703  OE2 GLU D 463      85.696 -25.292-208.142  1.00 42.71           O  
ANISOU12703  OE2 GLU D 463     5528   5592   5108   -867   -188    839       O  
ATOM  12704  N   MET D 464      88.792 -21.618-212.891  1.00 33.43           N  
ANISOU12704  N   MET D 464     4281   4152   4270   -209   -217    507       N  
ATOM  12705  CA  MET D 464      89.074 -21.111-214.231  1.00 32.95           C  
ANISOU12705  CA  MET D 464     4213   4051   4255   -143   -233    457       C  
ATOM  12706  C   MET D 464      89.200 -22.269-215.203  1.00 37.09           C  
ANISOU12706  C   MET D 464     4852   4461   4781   -223   -286    461       C  
ATOM  12707  O   MET D 464      89.579 -23.377-214.825  1.00 37.42           O  
ANISOU12707  O   MET D 464     5013   4402   4804   -278   -313    487       O  
ATOM  12708  CB  MET D 464      90.357 -20.266-214.264  1.00 26.37           C  
ANISOU12708  CB  MET D 464     3400   3153   3465      3   -217    403       C  
ATOM  12709  CG  MET D 464      90.232 -19.004-213.435  1.00 29.41           C  
ANISOU12709  CG  MET D 464     3690   3639   3847     83   -168    389       C  
ATOM  12710  SD  MET D 464      91.770 -18.116-213.398  1.00 35.24           S  
ANISOU12710  SD  MET D 464     4466   4300   4624    217   -157    332       S  
ATOM  12711  CE  MET D 464      91.455 -17.029-211.984  1.00 37.84           C  
ANISOU12711  CE  MET D 464     4719   4736   4921    268   -104    329       C  
ATOM  12712  N   VAL D 465      88.862 -22.002-216.464  1.00 28.54           N  
ANISOU12712  N   VAL D 465     3742   3389   3714   -226   -305    434       N  
ATOM  12713  CA  VAL D 465      88.948 -22.985-217.544  1.00 30.16           C  
ANISOU12713  CA  VAL D 465     4057   3489   3915   -296   -354    424       C  
ATOM  12714  C   VAL D 465      89.993 -22.485-218.531  1.00 29.52           C  
ANISOU12714  C   VAL D 465     4013   3328   3875   -177   -354    361       C  
ATOM  12715  O   VAL D 465      89.901 -21.348-219.013  1.00 29.82           O  
ANISOU12715  O   VAL D 465     3959   3436   3934   -106   -335    335       O  
ATOM  12716  CB  VAL D 465      87.599 -23.184-218.247  1.00 35.30           C  
ANISOU12716  CB  VAL D 465     4645   4235   4532   -425   -381    450       C  
ATOM  12717  CG1 VAL D 465      87.671 -24.359-219.242  1.00 32.06           C  
ANISOU12717  CG1 VAL D 465     4377   3702   4103   -523   -437    440       C  
ATOM  12718  CG2 VAL D 465      86.502 -23.398-217.214  1.00 41.98           C  
ANISOU12718  CG2 VAL D 465     5408   5211   5332   -536   -367    513       C  
ATOM  12719  N   ASN D 466      90.990 -23.315-218.821  1.00 31.22           N  
ANISOU12719  N   ASN D 466     4363   3399   4098   -151   -374    336       N  
ATOM  12720  CA  ASN D 466      92.066 -22.918-219.722  1.00 33.60           C  
ANISOU12720  CA  ASN D 466     4696   3637   4431    -41   -367    275       C  
ATOM  12721  C   ASN D 466      91.890 -23.596-221.081  1.00 30.83           C  
ANISOU12721  C   ASN D 466     4430   3221   4063    -98   -404    247       C  
ATOM  12722  O   ASN D 466      91.717 -24.816-221.152  1.00 32.01           O  
ANISOU12722  O   ASN D 466     4697   3280   4184   -181   -439    260       O  
ATOM  12723  CB  ASN D 466      93.428 -23.268-219.123  1.00 34.81           C  
ANISOU12723  CB  ASN D 466     4925   3698   4603     57   -358    256       C  
ATOM  12724  CG  ASN D 466      94.569 -22.594-219.861  1.00 43.26           C  
ANISOU12724  CG  ASN D 466     5984   4749   5703    175   -337    196       C  
ATOM  12725  OD1 ASN D 466      94.352 -21.703-220.692  1.00 37.17           O  
ANISOU12725  OD1 ASN D 466     5149   4036   4940    187   -324    172       O  
ATOM  12726  ND2 ASN D 466      95.791 -23.021-219.571  1.00 41.38           N  
ANISOU12726  ND2 ASN D 466     5808   4438   5477    262   -335    174       N  
ATOM  12727  N   TYR D 467      91.925 -22.800-222.152  1.00 30.27           N  
ANISOU12727  N   TYR D 467     4310   3188   4001    -59   -397    211       N  
ATOM  12728  CA  TYR D 467      91.811 -23.332-223.508  1.00 28.87           C  
ANISOU12728  CA  TYR D 467     4212   2957   3800   -108   -429    178       C  
ATOM  12729  C   TYR D 467      92.366 -22.298-224.481  1.00 30.34           C  
ANISOU12729  C   TYR D 467     4353   3172   4001    -20   -407    133       C  
ATOM  12730  O   TYR D 467      92.607 -21.141-224.126  1.00 31.57           O  
ANISOU12730  O   TYR D 467     4414   3397   4184     57   -374    135       O  
ATOM  12731  CB  TYR D 467      90.367 -23.704-223.861  1.00 32.52           C  
ANISOU12731  CB  TYR D 467     4651   3483   4224   -258   -471    216       C  
ATOM  12732  CG  TYR D 467      89.353 -22.641-223.525  1.00 37.18           C  
ANISOU12732  CG  TYR D 467     5073   4235   4818   -270   -459    256       C  
ATOM  12733  CD1 TYR D 467      88.852 -22.523-222.228  1.00 32.94           C  
ANISOU12733  CD1 TYR D 467     4460   3773   4283   -290   -439    304       C  
ATOM  12734  CD2 TYR D 467      88.882 -21.761-224.492  1.00 30.02           C  
ANISOU12734  CD2 TYR D 467     4088   3411   3908   -254   -469    246       C  
ATOM  12735  CE1 TYR D 467      87.923 -21.566-221.906  1.00 29.63           C  
ANISOU12735  CE1 TYR D 467     3888   3506   3863   -282   -423    333       C  
ATOM  12736  CE2 TYR D 467      87.953 -20.779-224.169  1.00 28.07           C  
ANISOU12736  CE2 TYR D 467     3691   3311   3664   -240   -460    281       C  
ATOM  12737  CZ  TYR D 467      87.478 -20.693-222.881  1.00 30.46           C  
ANISOU12737  CZ  TYR D 467     3917   3686   3969   -250   -435    321       C  
ATOM  12738  OH  TYR D 467      86.539 -19.743-222.555  1.00 33.77           O  
ANISOU12738  OH  TYR D 467     4187   4256   4387   -222   -422    349       O  
ATOM  12739  N   PHE D 468      92.573 -22.734-225.717  1.00 34.03           N  
ANISOU12739  N   PHE D 468     4903   3584   4445    -38   -426     91       N  
ATOM  12740  CA  PHE D 468      93.265 -21.937-226.719  1.00 34.73           C  
ANISOU12740  CA  PHE D 468     4976   3684   4534     37   -403     46       C  
ATOM  12741  C   PHE D 468      92.263 -21.441-227.758  1.00 35.33           C  
ANISOU12741  C   PHE D 468     5007   3835   4580    -32   -434     57       C  
ATOM  12742  O   PHE D 468      91.666 -22.244-228.485  1.00 36.56           O  
ANISOU12742  O   PHE D 468     5231   3965   4695   -129   -476     52       O  
ATOM  12743  CB  PHE D 468      94.366 -22.750-227.408  1.00 42.77           C  
ANISOU12743  CB  PHE D 468     6119   4595   5538     85   -394    -17       C  
ATOM  12744  CG  PHE D 468      94.943 -22.064-228.637  1.00 55.64           C  
ANISOU12744  CG  PHE D 468     7742   6248   7150    132   -372    -64       C  
ATOM  12745  CD1 PHE D 468      96.091 -21.293-228.536  1.00 59.25           C  
ANISOU12745  CD1 PHE D 468     8154   6728   7630    236   -323    -90       C  
ATOM  12746  CD2 PHE D 468      94.327 -22.178-229.883  1.00 63.70           C  
ANISOU12746  CD2 PHE D 468     8801   7277   8124     58   -403    -79       C  
ATOM  12747  CE1 PHE D 468      96.622 -20.659-229.654  1.00 59.88           C  
ANISOU12747  CE1 PHE D 468     8229   6837   7684    263   -300   -127       C  
ATOM  12748  CE2 PHE D 468      94.849 -21.540-231.007  1.00 63.11           C  
ANISOU12748  CE2 PHE D 468     8726   7229   8024     93   -382   -118       C  
ATOM  12749  CZ  PHE D 468      95.999 -20.783-230.889  1.00 58.58           C  
ANISOU12749  CZ  PHE D 468     8110   6677   7472    194   -328   -140       C  
ATOM  12750  N   LEU D 469      92.086 -20.131-227.825  1.00 30.15           N  
ANISOU12750  N   LEU D 469     4247   3267   3940     16   -418     73       N  
ATOM  12751  CA  LEU D 469      91.330 -19.503-228.903  1.00 30.90           C  
ANISOU12751  CA  LEU D 469     4304   3432   4006    -20   -449     83       C  
ATOM  12752  C   LEU D 469      92.272 -18.765-229.846  1.00 32.71           C  
ANISOU12752  C   LEU D 469     4560   3642   4227     50   -424     43       C  
ATOM  12753  O   LEU D 469      93.405 -18.431-229.496  1.00 32.37           O  
ANISOU12753  O   LEU D 469     4526   3565   4209    130   -378     16       O  
ATOM  12754  CB  LEU D 469      90.292 -18.522-228.340  1.00 28.93           C  
ANISOU12754  CB  LEU D 469     3922   3299   3772    -11   -457    137       C  
ATOM  12755  CG  LEU D 469      89.253 -19.102-227.381  1.00 34.13           C  
ANISOU12755  CG  LEU D 469     4524   4013   4430    -86   -475    183       C  
ATOM  12756  CD1 LEU D 469      88.387 -17.960-226.860  1.00 35.08           C  
ANISOU12756  CD1 LEU D 469     4506   4260   4565    -39   -469    224       C  
ATOM  12757  CD2 LEU D 469      88.399 -20.190-228.056  1.00 34.97           C  
ANISOU12757  CD2 LEU D 469     4674   4124   4488   -227   -532    193       C  
ATOM  12758  N   SER D 470      91.774 -18.501-231.067  1.00 30.22           N  
ANISOU12758  N   SER D 470     4253   3360   3868      7   -458     42       N  
ATOM  12759  CA  SER D 470      92.462 -17.720-232.074  1.00 31.03           C  
ANISOU12759  CA  SER D 470     4379   3463   3948     51   -440     16       C  
ATOM  12760  C   SER D 470      91.591 -16.538-232.481  1.00 29.97           C  
ANISOU12760  C   SER D 470     4169   3414   3803     56   -472     64       C  
ATOM  12761  O   SER D 470      90.365 -16.678-232.537  1.00 32.68           O  
ANISOU12761  O   SER D 470     4462   3822   4133     -1   -523    103       O  
ATOM  12762  CB  SER D 470      92.781 -18.576-233.326  1.00 37.45           C  
ANISOU12762  CB  SER D 470     5302   4225   4703      0   -453    -34       C  
ATOM  12763  OG  SER D 470      93.543 -17.837-234.267  1.00 31.87           O  
ANISOU12763  OG  SER D 470     4618   3527   3966     38   -427    -60       O  
ATOM  12764  N   PRO D 471      92.175 -15.363-232.768  1.00 28.92           N  
ANISOU12764  N   PRO D 471     4027   3288   3671    121   -448     65       N  
ATOM  12765  CA  PRO D 471      93.578 -14.925-232.782  1.00 27.70           C  
ANISOU12765  CA  PRO D 471     3910   3089   3524    177   -390     28       C  
ATOM  12766  C   PRO D 471      94.327 -15.168-231.470  1.00 31.38           C  
ANISOU12766  C   PRO D 471     4356   3523   4043    226   -344     13       C  
ATOM  12767  O   PRO D 471      93.698 -15.178-230.400  1.00 29.43           O  
ANISOU12767  O   PRO D 471     4053   3297   3833    236   -352     43       O  
ATOM  12768  CB  PRO D 471      93.470 -13.414-233.034  1.00 26.32           C  
ANISOU12768  CB  PRO D 471     3707   2949   3345    217   -394     63       C  
ATOM  12769  CG  PRO D 471      92.189 -13.284-233.849  1.00 33.24           C  
ANISOU12769  CG  PRO D 471     4566   3878   4184    177   -462    103       C  
ATOM  12770  CD  PRO D 471      91.265 -14.300-233.252  1.00 32.48           C  
ANISOU12770  CD  PRO D 471     4427   3809   4106    132   -490    114       C  
ATOM  12771  N   ALA D 472      95.643 -15.354-231.562  1.00 30.16           N  
ANISOU12771  N   ALA D 472     4242   3333   3886    257   -297    -33       N  
ATOM  12772  CA  ALA D 472      96.403 -15.771-230.390  1.00 32.08           C  
ANISOU12772  CA  ALA D 472     4470   3548   4171    303   -262    -49       C  
ATOM  12773  C   ALA D 472      97.826 -15.243-230.472  1.00 34.22           C  
ANISOU12773  C   ALA D 472     4740   3822   4438    349   -211    -83       C  
ATOM  12774  O   ALA D 472      98.377 -15.045-231.559  1.00 31.54           O  
ANISOU12774  O   ALA D 472     4434   3493   4056    338   -194   -109       O  
ATOM  12775  CB  ALA D 472      96.440 -17.308-230.253  1.00 26.02           C  
ANISOU12775  CB  ALA D 472     3760   2725   3402    286   -271    -76       C  
ATOM  12776  N   PHE D 473      98.404 -15.001-229.302  1.00 28.45           N  
ANISOU12776  N   PHE D 473     3968   3095   3746    393   -186    -79       N  
ATOM  12777  CA  PHE D 473      99.846 -14.903-229.148  1.00 27.00           C  
ANISOU12777  CA  PHE D 473     3774   2923   3562    434   -141   -115       C  
ATOM  12778  C   PHE D 473     100.382 -16.277-228.779  1.00 32.21           C  
ANISOU12778  C   PHE D 473     4459   3546   4232    474   -133   -148       C  
ATOM  12779  O   PHE D 473      99.849 -16.941-227.882  1.00 30.76           O  
ANISOU12779  O   PHE D 473     4281   3329   4078    479   -157   -127       O  
ATOM  12780  CB  PHE D 473     100.218 -13.881-228.064  1.00 27.47           C  
ANISOU12780  CB  PHE D 473     3779   3009   3650    454   -126    -93       C  
ATOM  12781  CG  PHE D 473      99.893 -12.459-228.434  1.00 30.12           C  
ANISOU12781  CG  PHE D 473     4111   3362   3969    427   -131    -66       C  
ATOM  12782  CD1 PHE D 473     100.660 -11.782-229.371  1.00 27.77           C  
ANISOU12782  CD1 PHE D 473     3833   3088   3631    400   -107    -80       C  
ATOM  12783  CD2 PHE D 473      98.819 -11.804-227.848  1.00 25.76           C  
ANISOU12783  CD2 PHE D 473     3544   2806   3437    431   -158    -25       C  
ATOM  12784  CE1 PHE D 473     100.364 -10.475-229.715  1.00 26.99           C  
ANISOU12784  CE1 PHE D 473     3754   2988   3511    373   -118    -50       C  
ATOM  12785  CE2 PHE D 473      98.519 -10.497-228.177  1.00 29.44           C  
ANISOU12785  CE2 PHE D 473     4025   3274   3887    423   -168     -1       C  
ATOM  12786  CZ  PHE D 473      99.293  -9.825-229.119  1.00 29.86           C  
ANISOU12786  CZ  PHE D 473     4115   3331   3900    391   -151    -10       C  
ATOM  12787  N   ARG D 474     101.431 -16.701-229.466  1.00 28.68           N  
ANISOU12787  N   ARG D 474     4033   3107   3757    506   -100   -198       N  
ATOM  12788  CA  ARG D 474     101.949 -18.054-229.335  1.00 33.87           C  
ANISOU12788  CA  ARG D 474     4735   3718   4416    563    -95   -237       C  
ATOM  12789  C   ARG D 474     103.441 -17.985-229.085  1.00 34.69           C  
ANISOU12789  C   ARG D 474     4787   3874   4519    638    -50   -272       C  
ATOM  12790  O   ARG D 474     104.128 -17.088-229.580  1.00 29.81           O  
ANISOU12790  O   ARG D 474     4121   3330   3876    624    -14   -283       O  
ATOM  12791  CB  ARG D 474     101.690 -18.901-230.618  1.00 34.37           C  
ANISOU12791  CB  ARG D 474     4888   3739   4431    544   -101   -279       C  
ATOM  12792  CG  ARG D 474     100.242 -19.288-230.825  1.00 50.15           C  
ANISOU12792  CG  ARG D 474     6942   5688   6426    466   -156   -248       C  
ATOM  12793  CD  ARG D 474     100.030 -19.825-232.242  1.00 64.59           C  
ANISOU12793  CD  ARG D 474     8856   7492   8194    429   -162   -290       C  
ATOM  12794  NE  ARG D 474     101.201 -20.552-232.733  1.00 73.72           N  
ANISOU12794  NE  ARG D 474    10060   8630   9320    506   -119   -362       N  
ATOM  12795  CZ  ARG D 474     101.453 -20.795-234.019  1.00 75.16           C  
ANISOU12795  CZ  ARG D 474    10303   8816   9438    499    -99   -416       C  
ATOM  12796  NH1 ARG D 474     100.617 -20.368-234.961  1.00 63.49           N  
ANISOU12796  NH1 ARG D 474     8849   7358   7918    408   -125   -400       N  
ATOM  12797  NH2 ARG D 474     102.548 -21.460-234.366  1.00 71.55           N  
ANISOU12797  NH2 ARG D 474     9880   8352   8954    588    -52   -486       N  
ATOM  12798  N   TYR D 475     103.941 -18.945-228.319  1.00 31.80           N  
ANISOU12798  N   TYR D 475     4433   3475   4176    713    -54   -285       N  
ATOM  12799  CA  TYR D 475     105.380 -19.126-228.227  1.00 30.30           C  
ANISOU12799  CA  TYR D 475     4193   3343   3977    802    -15   -326       C  
ATOM  12800  C   TYR D 475     105.932 -19.697-229.531  1.00 30.41           C  
ANISOU12800  C   TYR D 475     4250   3365   3940    842     21   -392       C  
ATOM  12801  O   TYR D 475     105.248 -20.412-230.263  1.00 34.28           O  
ANISOU12801  O   TYR D 475     4839   3778   4407    822      4   -412       O  
ATOM  12802  CB  TYR D 475     105.721 -20.059-227.073  1.00 33.57           C  
ANISOU12802  CB  TYR D 475     4618   3713   4425    887    -38   -318       C  
ATOM  12803  CG  TYR D 475     105.226 -19.528-225.753  1.00 32.67           C  
ANISOU12803  CG  TYR D 475     4462   3600   4350    848    -68   -256       C  
ATOM  12804  CD1 TYR D 475     105.481 -18.218-225.366  1.00 36.64           C  
ANISOU12804  CD1 TYR D 475     4877   4187   4859    806    -52   -234       C  
ATOM  12805  CD2 TYR D 475     104.515 -20.347-224.888  1.00 51.09           C  
ANISOU12805  CD2 TYR D 475     6856   5850   6708    850   -111   -222       C  
ATOM  12806  CE1 TYR D 475     105.028 -17.739-224.129  1.00 47.83           C  
ANISOU12806  CE1 TYR D 475     6265   5603   6304    777    -77   -186       C  
ATOM  12807  CE2 TYR D 475     104.057 -19.879-223.665  1.00 54.79           C  
ANISOU12807  CE2 TYR D 475     7287   6329   7203    816   -132   -168       C  
ATOM  12808  CZ  TYR D 475     104.311 -18.582-223.294  1.00 58.28           C  
ANISOU12808  CZ  TYR D 475     7640   6855   7650    786   -114   -154       C  
ATOM  12809  OH  TYR D 475     103.850 -18.139-222.074  1.00 69.23           O  
ANISOU12809  OH  TYR D 475     8999   8249   9055    758   -132   -110       O  
ATOM  12810  N   GLN D 476     107.194 -19.387-229.808  1.00 29.95           N  
ANISOU12810  N   GLN D 476     4114   3409   3857    894     72   -429       N  
ATOM  12811  CA  GLN D 476     107.860 -19.852-231.013  1.00 36.50           C  
ANISOU12811  CA  GLN D 476     4966   4273   4629    942    120   -498       C  
ATOM  12812  C   GLN D 476     109.324 -20.084-230.685  1.00 40.57           C  
ANISOU12812  C   GLN D 476     5388   4889   5139   1057    162   -536       C  
ATOM  12813  O   GLN D 476     109.865 -19.436-229.784  1.00 36.21           O  
ANISOU12813  O   GLN D 476     4732   4412   4613   1054    161   -503       O  
ATOM  12814  CB  GLN D 476     107.734 -18.837-232.172  1.00 36.20           C  
ANISOU12814  CB  GLN D 476     4914   4303   4538    840    151   -500       C  
ATOM  12815  CG  GLN D 476     108.342 -17.476-231.882  1.00 34.29           C  
ANISOU12815  CG  GLN D 476     4560   4176   4294    780    176   -467       C  
ATOM  12816  CD  GLN D 476     108.194 -16.479-233.052  1.00 35.60           C  
ANISOU12816  CD  GLN D 476     4735   4394   4399    673    202   -461       C  
ATOM  12817  OE1 GLN D 476     108.096 -16.860-234.221  1.00 33.79           O  
ANISOU12817  OE1 GLN D 476     4564   4161   4113    667    224   -501       O  
ATOM  12818  NE2 GLN D 476     108.190 -15.207-232.720  1.00 31.19           N  
ANISOU12818  NE2 GLN D 476     4129   3877   3847    588    197   -411       N  
ATOM  12819  N   PRO D 477     109.996 -20.972-231.416  1.00 44.77           N  
ANISOU12819  N   PRO D 477     5949   5431   5630   1161    200   -608       N  
ATOM  12820  CA  PRO D 477     111.402 -21.256-231.109  1.00 51.54           C  
ANISOU12820  CA  PRO D 477     6703   6402   6480   1293    240   -646       C  
ATOM  12821  C   PRO D 477     112.289 -20.041-231.326  1.00 52.32           C  
ANISOU12821  C   PRO D 477     6649   6684   6545   1229    292   -641       C  
ATOM  12822  O   PRO D 477     111.984 -19.146-232.119  1.00 42.95           O  
ANISOU12822  O   PRO D 477     5462   5536   5321   1105    315   -630       O  
ATOM  12823  CB  PRO D 477     111.759 -22.390-232.078  1.00 44.30           C  
ANISOU12823  CB  PRO D 477     5869   5451   5512   1412    275   -733       C  
ATOM  12824  CG  PRO D 477     110.787 -22.290-233.181  1.00 51.83           C  
ANISOU12824  CG  PRO D 477     6933   6333   6426   1302    275   -744       C  
ATOM  12825  CD  PRO D 477     109.520 -21.727-232.589  1.00 46.51           C  
ANISOU12825  CD  PRO D 477     6297   5572   5801   1167    209   -662       C  
ATOM  12826  N   ASP D 478     113.394 -20.015-230.594  1.00 52.72           N  
ANISOU12826  N   ASP D 478     6573   6851   6607   1310    306   -643       N  
ATOM  12827  CA  ASP D 478     114.369 -18.955-230.769  1.00 53.72           C  
ANISOU12827  CA  ASP D 478     6548   7169   6695   1245    356   -641       C  
ATOM  12828  C   ASP D 478     114.988 -19.061-232.159  1.00 56.94           C  
ANISOU12828  C   ASP D 478     6933   7681   7022   1265    436   -710       C  
ATOM  12829  O   ASP D 478     115.240 -20.167-232.647  1.00 60.85           O  
ANISOU12829  O   ASP D 478     7476   8149   7495   1406    460   -776       O  
ATOM  12830  CB  ASP D 478     115.454 -19.034-229.693  1.00 60.01           C  
ANISOU12830  CB  ASP D 478     7205   8083   7514   1334    349   -632       C  
ATOM  12831  CG  ASP D 478     114.935 -18.671-228.316  1.00 62.05           C  
ANISOU12831  CG  ASP D 478     7471   8270   7836   1284    277   -560       C  
ATOM  12832  OD1 ASP D 478     114.125 -17.729-228.216  1.00 65.66           O  
ANISOU12832  OD1 ASP D 478     7969   8674   8306   1137    257   -513       O  
ATOM  12833  OD2 ASP D 478     115.332 -19.325-227.330  1.00 68.58           O  
ANISOU12833  OD2 ASP D 478     8266   9093   8697   1398    241   -551       O  
ATOM  12834  N   PRO D 479     115.219 -17.931-232.832  1.00 54.96           N  
ANISOU12834  N   PRO D 479     6623   7542   6716   1124    479   -697       N  
ATOM  12835  CA  PRO D 479     115.640 -17.982-234.246  1.00 56.01           C  
ANISOU12835  CA  PRO D 479     6753   7767   6760   1118    556   -757       C  
ATOM  12836  C   PRO D 479     117.061 -18.470-234.452  1.00 63.21           C  
ANISOU12836  C   PRO D 479     7526   8867   7625   1251    628   -824       C  
ATOM  12837  O   PRO D 479     117.456 -18.685-235.604  1.00 69.36           O  
ANISOU12837  O   PRO D 479     8302   9728   8324   1273    700   -886       O  
ATOM  12838  CB  PRO D 479     115.483 -16.531-234.712  1.00 47.84           C  
ANISOU12838  CB  PRO D 479     5697   6795   5683    915    571   -706       C  
ATOM  12839  CG  PRO D 479     115.635 -15.723-233.437  1.00 48.08           C  
ANISOU12839  CG  PRO D 479     5650   6849   5770    850    525   -639       C  
ATOM  12840  CD  PRO D 479     115.070 -16.558-232.326  1.00 47.82           C  
ANISOU12840  CD  PRO D 479     5670   6675   5825    960    456   -625       C  
ATOM  12841  N   TRP D 480     117.840 -18.645-233.392  1.00 64.49           N  
ANISOU12841  N   TRP D 480     7566   9111   7827   1341    611   -813       N  
ATOM  12842  CA  TRP D 480     119.198 -19.149-233.531  1.00 70.52           C  
ANISOU12842  CA  TRP D 480     8178  10069   8546   1488    674   -875       C  
ATOM  12843  C   TRP D 480     119.236 -20.645-233.244  1.00 79.34           C  
ANISOU12843  C   TRP D 480     9367  11081   9698   1726    652   -928       C  
ATOM  12844  O   TRP D 480     118.189 -21.283-233.114  1.00 81.68           O  
ANISOU12844  O   TRP D 480     9841  11153  10039   1750    596   -921       O  
ATOM  12845  CB  TRP D 480     120.151 -18.394-232.599  1.00 65.64           C  
ANISOU12845  CB  TRP D 480     7366   9636   7937   1442    667   -831       C  
ATOM  12846  CG  TRP D 480     119.791 -18.491-231.145  1.00 60.19           C  
ANISOU12846  CG  TRP D 480     6694   8838   7337   1467    575   -771       C  
ATOM  12847  CD1 TRP D 480     120.143 -19.484-230.279  1.00 63.24           C  
ANISOU12847  CD1 TRP D 480     7058   9200   7769   1657    534   -782       C  
ATOM  12848  CD2 TRP D 480     119.019 -17.554-230.386  1.00 56.26           C  
ANISOU12848  CD2 TRP D 480     6247   8245   6886   1300    512   -691       C  
ATOM  12849  NE1 TRP D 480     119.630 -19.230-229.030  1.00 60.24           N  
ANISOU12849  NE1 TRP D 480     6710   8720   7457   1607    451   -711       N  
ATOM  12850  CE2 TRP D 480     118.940 -18.047-229.069  1.00 59.24           C  
ANISOU12850  CE2 TRP D 480     6625   8552   7332   1392    440   -659       C  
ATOM  12851  CE3 TRP D 480     118.388 -16.346-230.691  1.00 56.78           C  
ANISOU12851  CE3 TRP D 480     6363   8274   6936   1091    509   -645       C  
ATOM  12852  CZ2 TRP D 480     118.254 -17.373-228.059  1.00 58.14           C  
ANISOU12852  CZ2 TRP D 480     6528   8317   7243   1279    373   -588       C  
ATOM  12853  CZ3 TRP D 480     117.707 -15.680-229.689  1.00 52.34           C  
ANISOU12853  CZ3 TRP D 480     5848   7610   6429    992    440   -576       C  
ATOM  12854  CH2 TRP D 480     117.644 -16.195-228.389  1.00 57.04           C  
ANISOU12854  CH2 TRP D 480     6436   8146   7089   1084    376   -552       C  
ATOM  12855  OXT TRP D 480     120.306 -21.248-233.142  1.00 83.40           O  
ANISOU12855  OXT TRP D 480     9765  11731  10192   1898    688   -978       O  
TER   12856      TRP D 480                                                      
HETATM12857  CHA HEM A 501      66.623  29.933-182.562  1.00 40.55           C  
HETATM12858  CHB HEM A 501      70.131  28.509-185.604  1.00 44.92           C  
HETATM12859  CHC HEM A 501      70.042  32.960-187.550  1.00 47.83           C  
HETATM12860  CHD HEM A 501      66.827  34.490-184.247  1.00 52.89           C  
HETATM12861  C1A HEM A 501      67.506  29.129-183.245  1.00 42.64           C  
HETATM12862  C2A HEM A 501      67.653  27.687-183.128  1.00 45.12           C  
HETATM12863  C3A HEM A 501      68.625  27.308-183.970  1.00 44.97           C  
HETATM12864  C4A HEM A 501      69.126  28.478-184.657  1.00 45.60           C  
HETATM12865  CMA HEM A 501      69.152  25.881-184.203  1.00 41.43           C  
HETATM12866  CAA HEM A 501      66.858  26.740-182.196  1.00 53.99           C  
HETATM12867  CBA HEM A 501      65.379  26.705-182.561  1.00 66.14           C  
HETATM12868  CGA HEM A 501      64.876  25.283-182.618  1.00 74.01           C  
HETATM12869  O1A HEM A 501      65.677  24.334-182.440  1.00 74.38           O  
HETATM12870  O2A HEM A 501      63.661  25.085-182.859  1.00 80.70           O  
HETATM12871  C1B HEM A 501      70.429  29.596-186.402  1.00 51.17           C  
HETATM12872  C2B HEM A 501      71.425  29.644-187.451  1.00 48.62           C  
HETATM12873  C3B HEM A 501      71.422  30.870-187.993  1.00 54.42           C  
HETATM12874  C4B HEM A 501      70.397  31.649-187.305  1.00 55.35           C  
HETATM12875  CMB HEM A 501      72.339  28.471-187.854  1.00 40.68           C  
HETATM12876  CAB HEM A 501      72.347  31.318-189.162  1.00 45.08           C  
HETATM12877  CBB HEM A 501      72.515  32.598-189.517  1.00 45.45           C  
HETATM12878  C1C HEM A 501      69.144  33.749-186.864  1.00 55.15           C  
HETATM12879  C2C HEM A 501      68.740  35.098-187.228  1.00 53.89           C  
HETATM12880  C3C HEM A 501      67.841  35.521-186.316  1.00 56.57           C  
HETATM12881  C4C HEM A 501      67.663  34.457-185.344  1.00 54.43           C  
HETATM12882  CMC HEM A 501      69.279  35.854-188.466  1.00 40.37           C  
HETATM12883  CAC HEM A 501      67.105  36.877-186.197  1.00 51.60           C  
HETATM12884  CBC HEM A 501      67.477  37.990-186.836  1.00 59.06           C  
HETATM12885  C1D HEM A 501      66.458  33.379-183.521  1.00 54.70           C  
HETATM12886  C2D HEM A 501      65.439  33.324-182.495  1.00 55.92           C  
HETATM12887  C3D HEM A 501      65.372  32.063-182.044  1.00 52.86           C  
HETATM12888  C4D HEM A 501      66.368  31.275-182.743  1.00 51.78           C  
HETATM12889  CMD HEM A 501      64.586  34.530-182.041  1.00 53.40           C  
HETATM12890  CAD HEM A 501      64.452  31.563-180.912  1.00 49.64           C  
HETATM12891  CBD HEM A 501      65.319  31.997-179.738  1.00 60.08           C  
HETATM12892  CGD HEM A 501      64.625  32.483-178.494  1.00 72.19           C  
HETATM12893  O1D HEM A 501      63.376  32.356-178.363  1.00 83.24           O  
HETATM12894  O2D HEM A 501      65.372  32.996-177.622  1.00 62.05           O  
HETATM12895  NA  HEM A 501      68.429  29.565-184.181  1.00 45.71           N  
HETATM12896  NB  HEM A 501      69.827  30.836-186.342  1.00 47.18           N  
HETATM12897  NC  HEM A 501      68.462  33.398-185.716  1.00 43.49           N  
HETATM12898  ND  HEM A 501      67.000  32.115-183.646  1.00 47.81           N  
HETATM12899 FE   HEM A 501      68.644  31.551-184.761  1.00 48.93          FE  
HETATM12900  N1  H4B A 502      65.913  22.894-178.094  1.00 63.97           N  
HETATM12901  C2  H4B A 502      65.747  23.394-179.342  1.00 62.13           C  
HETATM12902  N2  H4B A 502      66.813  23.901-180.007  1.00 54.47           N  
HETATM12903  N3  H4B A 502      64.528  23.389-179.927  1.00 64.57           N  
HETATM12904  C4  H4B A 502      63.456  22.885-179.277  1.00 66.29           C  
HETATM12905  O4  H4B A 502      62.330  22.886-179.821  1.00 66.41           O  
HETATM12906  C4A H4B A 502      63.610  22.376-177.998  1.00 59.69           C  
HETATM12907  C8A H4B A 502      64.863  22.385-177.414  1.00 59.79           C  
HETATM12908  N5  H4B A 502      62.557  21.869-177.325  1.00 53.43           N  
HETATM12909  N8  H4B A 502      65.048  21.901-176.160  1.00 55.78           N  
HETATM12910  C6  H4B A 502      62.624  21.864-175.871  1.00 54.30           C  
HETATM12911  C7  H4B A 502      63.964  21.318-175.381  1.00 46.71           C  
HETATM12912  C9  H4B A 502      61.453  21.103-175.237  1.00 53.25           C  
HETATM12913  O9  H4B A 502      61.298  19.798-175.795  1.00 48.48           O  
HETATM12914  C10 H4B A 502      61.679  20.938-173.741  1.00 62.00           C  
HETATM12915  C11 H4B A 502      60.490  20.247-173.079  1.00 56.71           C  
HETATM12916  O10 H4B A 502      61.913  22.218-173.142  1.00 72.03           O  
HETATM12917  C02 OU1 A 503      67.360  28.593-187.846  1.00 52.25           C  
HETATM12918  C03 OU1 A 503      67.369  29.949-188.157  1.00 57.64           C  
HETATM12919  C04 OU1 A 503      66.435  30.779-187.551  1.00 66.74           C  
HETATM12920  C05 OU1 A 503      65.514  30.249-186.652  1.00 71.49           C  
HETATM12921  C06 OU1 A 503      64.574  31.067-186.034  1.00 74.27           C  
HETATM12922  C07 OU1 A 503      63.661  30.531-185.132  1.00 75.77           C  
HETATM12923  C08 OU1 A 503      63.661  29.171-184.853  1.00 75.14           C  
HETATM12924  C09 OU1 A 503      64.606  28.353-185.473  1.00 69.18           C  
HETATM12925  C10 OU1 A 503      65.532  28.891-186.373  1.00 65.01           C  
HETATM12926  C11 OU1 A 503      66.415  32.248-187.866  1.00 65.36           C  
HETATM12927  C21 OU1 A 503      62.662  28.614-183.888  1.00 75.87           C  
HETATM12928  C22 OU1 A 503      62.253  29.343-182.770  1.00 80.48           C  
HETATM12929  C23 OU1 A 503      61.319  28.806-181.884  1.00 85.12           C  
HETATM12930  C24 OU1 A 503      60.792  27.536-182.121  1.00 87.89           C  
HETATM12931  C25 OU1 A 503      61.197  26.815-183.227  1.00 78.64           C  
HETATM12932  C26 OU1 A 503      62.126  27.350-184.113  1.00 69.42           C  
HETATM12933  C27 OU1 A 503      60.621  25.437-183.461  1.00 79.97           C  
HETATM12934  C30 OU1 A 503      58.641  27.612-180.957  1.00 98.49           C  
HETATM12935  C31 OU1 A 503      57.697  26.583-180.346  1.00 96.55           C  
HETATM12936  C32 OU1 A 503      57.147  25.713-181.471  1.00 97.13           C  
HETATM12937  C33 OU1 A 503      56.281  26.809-180.864  1.00 97.27           C  
HETATM12938  N01 OU1 A 503      66.446  28.103-186.981  1.00 51.69           N  
HETATM12939  N02 OU1 A 503      68.260  27.750-188.426  1.00 43.55           N  
HETATM12940  O29 OU1 A 503      59.875  26.968-181.271  1.00 97.00           O  
HETATM12941  N28 OU1 A 503      61.198  24.512-182.464  1.00 76.56           N  
HETATM12942  C1  BTB A 504      64.026  -1.695-197.528  1.00 81.43           C  
HETATM12943  O1  BTB A 504      62.887  -1.395-198.340  1.00 84.27           O  
HETATM12944  C2  BTB A 504      64.766  -2.952-197.982  1.00 72.79           C  
HETATM12945  C3  BTB A 504      65.458  -3.513-196.743  1.00 54.61           C  
HETATM12946  O3  BTB A 504      66.218  -4.731-196.881  1.00 33.44           O  
HETATM12947  C4  BTB A 504      63.726  -3.937-198.519  1.00 73.86           C  
HETATM12948  O4  BTB A 504      64.243  -5.243-198.792  1.00 75.21           O  
HETATM12949  N   BTB A 504      65.763  -2.595-199.024  1.00 76.82           N  
HETATM12950  C5  BTB A 504      66.542  -1.400-198.647  1.00 76.68           C  
HETATM12951  C6  BTB A 504      68.002  -1.771-198.386  1.00 81.11           C  
HETATM12952  O6  BTB A 504      68.398  -2.890-199.181  1.00 84.87           O  
HETATM12953  C7  BTB A 504      65.134  -2.382-200.345  1.00 72.82           C  
HETATM12954  C8  BTB A 504      66.186  -2.272-201.451  1.00 70.68           C  
HETATM12955  O8  BTB A 504      66.759  -3.561-201.714  1.00 76.78           O  
HETATM12956  C1  BTB A 505      56.574  -1.106-184.390  1.00 63.76           C  
HETATM12957  O1  BTB A 505      55.895  -0.547-183.263  1.00 67.64           O  
HETATM12958  C2  BTB A 505      56.967  -2.541-184.071  1.00 66.05           C  
HETATM12959  C3  BTB A 505      56.035  -3.038-182.989  1.00 77.15           C  
HETATM12960  O3  BTB A 505      54.731  -2.558-183.327  1.00 82.42           O  
HETATM12961  C4  BTB A 505      56.754  -3.388-185.325  1.00 79.35           C  
HETATM12962  O4  BTB A 505      56.503  -4.755-184.970  1.00 79.76           O  
HETATM12963  N   BTB A 505      58.368  -2.644-183.577  1.00 78.80           N  
HETATM12964  C5  BTB A 505      58.996  -1.323-183.371  1.00 78.06           C  
HETATM12965  C6  BTB A 505      59.277  -1.110-181.888  1.00 74.15           C  
HETATM12966  O6  BTB A 505      58.148  -1.561-181.130  1.00 74.19           O  
HETATM12967  C7  BTB A 505      59.229  -3.430-184.480  1.00 80.00           C  
HETATM12968  C8  BTB A 505      59.806  -4.604-183.703  1.00 78.69           C  
HETATM12969  O8  BTB A 505      59.029  -4.818-182.518  1.00 80.81           O  
HETATM12970  C1  BTB A 506      35.978  45.598-198.332  1.00108.61           C  
HETATM12971  O1  BTB A 506      35.350  44.388-198.773  1.00105.88           O  
HETATM12972  C2  BTB A 506      36.683  45.386-196.991  1.00107.17           C  
HETATM12973  C3  BTB A 506      36.154  44.127-196.303  1.00105.73           C  
HETATM12974  O3  BTB A 506      36.704  44.004-194.985  1.00 99.97           O  
HETATM12975  C4  BTB A 506      38.189  45.253-197.213  1.00107.99           C  
HETATM12976  O4  BTB A 506      38.468  44.169-198.109  1.00106.58           O  
HETATM12977  N   BTB A 506      36.457  46.572-196.136  1.00 99.12           N  
HETATM12978  C5  BTB A 506      35.059  46.634-195.675  1.00 97.05           C  
HETATM12979  C6  BTB A 506      35.019  46.656-194.149  1.00 93.97           C  
HETATM12980  O6  BTB A 506      35.948  47.629-193.659  1.00 93.39           O  
HETATM12981  C7  BTB A 506      36.776  47.790-196.906  1.00 90.03           C  
HETATM12982  C8  BTB A 506      37.633  48.731-196.066  1.00 83.50           C  
HETATM12983  O8  BTB A 506      38.512  47.954-195.243  1.00 73.63           O  
HETATM12984  C1  GOL A 507      58.690  23.003-179.953  1.00 88.88           C  
HETATM12985  O1  GOL A 507      59.497  23.756-179.077  1.00 92.92           O  
HETATM12986  C2  GOL A 507      58.645  21.570-179.456  1.00 84.83           C  
HETATM12987  O2  GOL A 507      59.905  21.256-178.910  1.00 84.37           O  
HETATM12988  C3  GOL A 507      58.359  20.660-180.645  1.00 87.60           C  
HETATM12989  O3  GOL A 507      58.225  19.334-180.194  1.00 92.67           O  
HETATM12990 CL    CL A 508      62.347  24.348-189.018  1.00 60.06          CL  
HETATM12991 GD    GD A 509      66.889  -5.160-199.393  1.00105.36          GD  
HETATM12992 ZN    ZN B 501      65.750  28.109-163.665  1.00 39.22          ZN  
HETATM12993  CHA HEM B 502      71.957  10.301-160.733  1.00 25.86           C  
HETATM12994  CHB HEM B 502      70.658   6.316-163.195  1.00 25.69           C  
HETATM12995  CHC HEM B 502      69.932   4.045-158.965  1.00 28.95           C  
HETATM12996  CHD HEM B 502      70.514   8.251-156.564  1.00 29.08           C  
HETATM12997  C1A HEM B 502      71.781   9.386-161.737  1.00 22.59           C  
HETATM12998  C2A HEM B 502      72.192   9.568-163.131  1.00 26.80           C  
HETATM12999  C3A HEM B 502      71.848   8.478-163.810  1.00 28.60           C  
HETATM13000  C4A HEM B 502      71.185   7.562-162.892  1.00 29.80           C  
HETATM13001  CMA HEM B 502      72.106   8.216-165.317  1.00 25.04           C  
HETATM13002  CAA HEM B 502      72.945  10.810-163.667  1.00 29.18           C  
HETATM13003  CBA HEM B 502      74.406  10.660-163.287  1.00 40.82           C  
HETATM13004  CGA HEM B 502      75.366  11.195-164.318  1.00 56.74           C  
HETATM13005  O1A HEM B 502      74.930  11.630-165.385  1.00 53.05           O  
HETATM13006  O2A HEM B 502      76.595  11.161-164.091  1.00 70.32           O  
HETATM13007  C1B HEM B 502      70.361   5.316-162.277  1.00 27.50           C  
HETATM13008  C2B HEM B 502      70.021   3.942-162.576  1.00 27.43           C  
HETATM13009  C3B HEM B 502      69.806   3.299-161.416  1.00 28.23           C  
HETATM13010  C4B HEM B 502      70.001   4.266-160.333  1.00 26.37           C  
HETATM13011  CMB HEM B 502      69.902   3.306-163.988  1.00 29.22           C  
HETATM13012  CAB HEM B 502      69.414   1.803-161.321  1.00 30.19           C  
HETATM13013  CBB HEM B 502      68.787   1.278-160.261  1.00 35.89           C  
HETATM13014  C1C HEM B 502      70.044   4.988-157.956  1.00 26.12           C  
HETATM13015  C2C HEM B 502      69.968   4.702-156.512  1.00 25.25           C  
HETATM13016  C3C HEM B 502      70.135   5.852-155.839  1.00 24.35           C  
HETATM13017  C4C HEM B 502      70.313   6.908-156.819  1.00 30.50           C  
HETATM13018  CMC HEM B 502      69.742   3.282-155.963  1.00 32.25           C  
HETATM13019  CAC HEM B 502      70.110   6.126-154.305  1.00 24.81           C  
HETATM13020  CBC HEM B 502      69.527   5.307-153.417  1.00 33.51           C  
HETATM13021  C1D HEM B 502      70.983   9.164-157.491  1.00 28.31           C  
HETATM13022  C2D HEM B 502      71.381  10.522-157.208  1.00 30.75           C  
HETATM13023  C3D HEM B 502      71.784  11.111-158.348  1.00 31.14           C  
HETATM13024  C4D HEM B 502      71.642  10.121-159.394  1.00 30.80           C  
HETATM13025  CMD HEM B 502      71.318  11.101-155.787  1.00 24.75           C  
HETATM13026  CAD HEM B 502      72.309  12.558-158.621  1.00 32.64           C  
HETATM13027  CBD HEM B 502      72.212  13.610-157.508  1.00 62.33           C  
HETATM13028  CGD HEM B 502      71.296  14.800-157.748  1.00 65.56           C  
HETATM13029  O1D HEM B 502      71.833  15.936-157.648  1.00 59.40           O  
HETATM13030  O2D HEM B 502      70.055  14.641-157.994  1.00 49.71           O  
HETATM13031  NA  HEM B 502      71.158   8.172-161.665  1.00 27.98           N  
HETATM13032  NB  HEM B 502      70.348   5.478-160.905  1.00 33.19           N  
HETATM13033  NC  HEM B 502      70.264   6.333-158.067  1.00 25.94           N  
HETATM13034  ND  HEM B 502      71.148   8.948-158.857  1.00 31.13           N  
HETATM13035 FE   HEM B 502      70.382   7.352-159.896  1.00 28.17          FE  
HETATM13036  N1  H4B B 503      73.591  15.332-167.273  1.00 38.38           N  
HETATM13037  C2  H4B B 503      74.018  14.203-166.652  1.00 35.94           C  
HETATM13038  N2  H4B B 503      73.205  13.120-166.569  1.00 34.07           N  
HETATM13039  N3  H4B B 503      75.261  14.152-166.119  1.00 35.58           N  
HETATM13040  C4  H4B B 503      76.091  15.210-166.180  1.00 37.55           C  
HETATM13041  O4  H4B B 503      77.232  15.109-165.691  1.00 40.84           O  
HETATM13042  C4A H4B B 503      75.662  16.382-166.787  1.00 42.54           C  
HETATM13043  C8A H4B B 503      74.391  16.429-167.343  1.00 34.57           C  
HETATM13044  N5  H4B B 503      76.471  17.455-166.863  1.00 37.82           N  
HETATM13045  N8  H4B B 503      73.938  17.553-167.936  1.00 36.20           N  
HETATM13046  C6  H4B B 503      75.863  18.758-167.082  1.00 45.06           C  
HETATM13047  C7  H4B B 503      74.780  18.725-168.156  1.00 38.27           C  
HETATM13048  C9  H4B B 503      76.923  19.829-167.354  1.00 45.99           C  
HETATM13049  O9  H4B B 503      77.828  19.415-168.372  1.00 46.49           O  
HETATM13050  C10 H4B B 503      76.272  21.147-167.745  1.00 43.50           C  
HETATM13051  C11 H4B B 503      77.289  22.281-167.714  1.00 41.02           C  
HETATM13052  O10 H4B B 503      75.247  21.434-166.788  1.00 52.39           O  
HETATM13053  C02 OU1 B 504      73.956   5.197-161.811  1.00 32.11           C  
HETATM13054  C03 OU1 B 504      73.540   4.776-160.533  1.00 33.14           C  
HETATM13055  C04 OU1 B 504      73.752   5.619-159.450  1.00 36.66           C  
HETATM13056  C05 OU1 B 504      74.359   6.846-159.658  1.00 44.42           C  
HETATM13057  C06 OU1 B 504      74.571   7.714-158.596  1.00 45.36           C  
HETATM13058  C07 OU1 B 504      75.167   8.945-158.835  1.00 51.96           C  
HETATM13059  C08 OU1 B 504      75.592   9.317-160.099  1.00 55.00           C  
HETATM13060  C09 OU1 B 504      75.379   8.441-161.155  1.00 52.14           C  
HETATM13061  C10 OU1 B 504      74.759   7.220-160.936  1.00 46.93           C  
HETATM13062  C11 OU1 B 504      73.332   5.210-158.042  1.00 35.54           C  
HETATM13063  C21 OU1 B 504      76.258  10.639-160.291  1.00 65.14           C  
HETATM13064  C22 OU1 B 504      75.947  11.708-159.456  1.00 74.20           C  
HETATM13065  C23 OU1 B 504      76.580  12.933-159.631  1.00 76.11           C  
HETATM13066  C24 OU1 B 504      77.534  13.080-160.635  1.00 79.39           C  
HETATM13067  C25 OU1 B 504      77.854  12.026-161.466  1.00 74.72           C  
HETATM13068  C26 OU1 B 504      77.224  10.797-161.280  1.00 69.78           C  
HETATM13069  C27 OU1 B 504      78.900  12.237-162.550  1.00 70.14           C  
HETATM13070  C30 OU1 B 504      78.292  15.210-159.765  1.00 89.12           C  
HETATM13071  C31 OU1 B 504      79.239  16.319-160.204  1.00 95.60           C  
HETATM13072  C32 OU1 B 504      80.660  15.778-160.344  1.00 96.88           C  
HETATM13073  C33 OU1 B 504      80.249  16.531-159.087  1.00 98.06           C  
HETATM13074  N01 OU1 B 504      74.562   6.395-161.976  1.00 36.38           N  
HETATM13075  N02 OU1 B 504      73.806   4.437-162.925  1.00 33.53           N  
HETATM13076  O29 OU1 B 504      78.167  14.275-160.830  1.00 86.21           O  
HETATM13077  N28 OU1 B 504      78.333  12.974-163.713  1.00 52.00           N  
HETATM13078  C1  BTB B 505      81.781 -11.111-190.765  1.00 79.44           C  
HETATM13079  O1  BTB B 505      80.424 -11.547-190.647  1.00 85.06           O  
HETATM13080  C2  BTB B 505      82.069  -9.941-189.825  1.00 69.72           C  
HETATM13081  C3  BTB B 505      80.947  -8.894-189.863  1.00 65.86           C  
HETATM13082  O3  BTB B 505      81.296  -7.695-189.137  1.00 51.57           O  
HETATM13083  C4  BTB B 505      82.173 -10.425-188.383  1.00 66.30           C  
HETATM13084  O4  BTB B 505      82.580  -9.326-187.559  1.00 61.63           O  
HETATM13085  N   BTB B 505      83.352  -9.336-190.262  1.00 53.38           N  
HETATM13086  C5  BTB B 505      83.181  -8.704-191.580  1.00 56.46           C  
HETATM13087  C6  BTB B 505      83.439  -7.214-191.426  1.00 50.84           C  
HETATM13088  O6  BTB B 505      84.820  -7.015-191.129  1.00 52.31           O  
HETATM13089  C7  BTB B 505      84.499 -10.268-190.252  1.00 54.54           C  
HETATM13090  C8  BTB B 505      85.463 -10.015-189.082  1.00 54.35           C  
HETATM13091  O8  BTB B 505      85.973  -8.672-189.088  1.00 59.70           O  
HETATM13092  C1  BTB B 506      95.049   7.847-131.535  1.00 66.73           C  
HETATM13093  O1  BTB B 506      95.124   9.225-131.144  1.00 66.18           O  
HETATM13094  C2  BTB B 506      94.473   7.720-132.953  1.00 64.16           C  
HETATM13095  C3  BTB B 506      93.632   8.956-133.281  1.00 45.29           C  
HETATM13096  O3  BTB B 506      92.519   9.169-132.405  1.00 63.54           O  
HETATM13097  C4  BTB B 506      95.582   7.712-134.000  1.00 77.06           C  
HETATM13098  O4  BTB B 506      96.816   8.117-133.398  1.00 86.26           O  
HETATM13099  N   BTB B 506      93.785   6.400-133.055  1.00 58.71           N  
HETATM13100  C5  BTB B 506      92.714   6.273-132.050  1.00 52.23           C  
HETATM13101  C6  BTB B 506      91.653   5.271-132.485  1.00 64.65           C  
HETATM13102  O6  BTB B 506      92.038   3.953-132.061  1.00 72.90           O  
HETATM13103  C7  BTB B 506      94.829   5.407-132.721  1.00 67.80           C  
HETATM13104  C8  BTB B 506      94.773   4.075-133.472  1.00 63.28           C  
HETATM13105  O8  BTB B 506      95.303   3.051-132.603  1.00 32.04           O  
HETATM13106  C1  BTB B 507      96.185  15.369-185.422  1.00 98.43           C  
HETATM13107  O1  BTB B 507      96.033  14.031-185.922  1.00100.73           O  
HETATM13108  C2  BTB B 507      94.944  15.809-184.642  1.00 92.82           C  
HETATM13109  C3  BTB B 507      94.411  14.640-183.817  1.00 87.32           C  
HETATM13110  O3  BTB B 507      95.471  13.930-183.161  1.00 82.48           O  
HETATM13111  C4  BTB B 507      95.368  16.936-183.698  1.00 89.33           C  
HETATM13112  O4  BTB B 507      94.575  16.907-182.503  1.00 90.12           O  
HETATM13113  N   BTB B 507      93.839  16.250-185.548  1.00 91.44           N  
HETATM13114  C5  BTB B 507      94.215  16.281-186.975  1.00 88.28           C  
HETATM13115  C6  BTB B 507      93.505  15.141-187.702  1.00 86.82           C  
HETATM13116  O6  BTB B 507      92.088  15.266-187.528  1.00 87.18           O  
HETATM13117  C7  BTB B 507      93.281  17.569-185.198  1.00 86.13           C  
HETATM13118  C8  BTB B 507      91.952  17.386-184.474  1.00 86.64           C  
HETATM13119  O8  BTB B 507      91.245  18.632-184.495  1.00 86.89           O  
HETATM13120  C1  GOL B 508      79.895  17.449-164.063  1.00 72.46           C  
HETATM13121  O1  GOL B 508      78.788  16.627-163.765  1.00 75.88           O  
HETATM13122  C2  GOL B 508      80.284  17.256-165.520  1.00 72.02           C  
HETATM13123  O2  GOL B 508      79.342  16.421-166.161  1.00 70.15           O  
HETATM13124  C3  GOL B 508      81.663  16.617-165.622  1.00 69.59           C  
HETATM13125  O3  GOL B 508      82.111  16.714-166.955  1.00 64.60           O  
HETATM13126 CL    CL B 509      80.400   6.631-163.494  1.00 46.93          CL  
HETATM13127 GD    GD B 510      83.798  -7.192-188.589  1.00 44.17          GD  
HETATM13128 GD    GD B 511      96.740   2.537-180.757  1.00 78.87          GD  
HETATM13129  CHA HEM C 501      95.454 -32.155-198.080  1.00 33.44           C  
HETATM13130  CHB HEM C 501      99.226 -30.970-195.261  1.00 36.55           C  
HETATM13131  CHC HEM C 501      98.916 -35.414-193.275  1.00 40.04           C  
HETATM13132  CHD HEM C 501      95.794 -36.840-196.690  1.00 46.36           C  
HETATM13133  C1A HEM C 501      96.438 -31.402-197.452  1.00 41.74           C  
HETATM13134  C2A HEM C 501      96.700 -29.966-197.575  1.00 45.73           C  
HETATM13135  C3A HEM C 501      97.742 -29.660-196.801  1.00 39.58           C  
HETATM13136  C4A HEM C 501      98.185 -30.870-196.151  1.00 36.30           C  
HETATM13137  CMA HEM C 501      98.392 -28.274-196.586  1.00 36.55           C  
HETATM13138  CAA HEM C 501      95.929 -28.949-198.439  1.00 43.52           C  
HETATM13139  CBA HEM C 501      94.520 -28.834-197.870  1.00 52.64           C  
HETATM13140  CGA HEM C 501      94.019 -27.422-197.980  1.00 64.14           C  
HETATM13141  O1A HEM C 501      94.845 -26.513-198.215  1.00 65.99           O  
HETATM13142  O2A HEM C 501      92.796 -27.205-197.812  1.00 73.07           O  
HETATM13143  C1B HEM C 501      99.460 -32.071-194.463  1.00 38.60           C  
HETATM13144  C2B HEM C 501     100.470 -32.164-193.436  1.00 38.73           C  
HETATM13145  C3B HEM C 501     100.407 -33.387-192.896  1.00 42.71           C  
HETATM13146  C4B HEM C 501      99.331 -34.120-193.550  1.00 43.61           C  
HETATM13147  CMB HEM C 501     101.465 -31.049-193.042  1.00 34.27           C  
HETATM13148  CAB HEM C 501     101.331 -33.857-191.740  1.00 45.50           C  
HETATM13149  CBB HEM C 501     101.540 -35.152-191.481  1.00 45.48           C  
HETATM13150  C1C HEM C 501      98.006 -36.186-193.962  1.00 43.55           C  
HETATM13151  C2C HEM C 501      97.534 -37.522-193.602  1.00 44.59           C  
HETATM13152  C3C HEM C 501      96.656 -37.918-194.550  1.00 41.79           C  
HETATM13153  C4C HEM C 501      96.569 -36.855-195.547  1.00 42.06           C  
HETATM13154  CMC HEM C 501      97.981 -38.274-192.320  1.00 36.62           C  
HETATM13155  CAC HEM C 501      95.866 -39.243-194.683  1.00 41.41           C  
HETATM13156  CBC HEM C 501      96.260 -40.392-194.119  1.00 40.96           C  
HETATM13157  C1D HEM C 501      95.376 -35.685-197.335  1.00 45.61           C  
HETATM13158  C2D HEM C 501      94.306 -35.576-198.310  1.00 42.67           C  
HETATM13159  C3D HEM C 501      94.206 -34.294-198.678  1.00 43.85           C  
HETATM13160  C4D HEM C 501      95.224 -33.523-197.978  1.00 42.49           C  
HETATM13161  CMD HEM C 501      93.425 -36.742-198.811  1.00 41.49           C  
HETATM13162  CAD HEM C 501      93.195 -33.766-199.714  1.00 45.34           C  
HETATM13163  CBD HEM C 501      93.941 -33.996-201.018  1.00 65.40           C  
HETATM13164  CGD HEM C 501      93.093 -34.387-202.205  1.00 77.07           C  
HETATM13165  O1D HEM C 501      91.868 -34.088-202.223  1.00 83.99           O  
HETATM13166  O2D HEM C 501      93.679 -34.994-203.146  1.00 65.95           O  
HETATM13167  NA  HEM C 501      97.374 -31.898-196.559  1.00 38.72           N  
HETATM13168  NB  HEM C 501      98.784 -33.277-194.515  1.00 42.43           N  
HETATM13169  NC  HEM C 501      97.399 -35.832-195.143  1.00 40.28           N  
HETATM13170  ND  HEM C 501      95.915 -34.421-197.160  1.00 43.87           N  
HETATM13171 FE   HEM C 501      97.608 -33.963-196.077  1.00 37.84          FE  
HETATM13172  N1  H4B C 502      95.124 -24.994-202.414  1.00 46.78           N  
HETATM13173  C2  H4B C 502      94.986 -25.571-201.192  1.00 48.74           C  
HETATM13174  N2  H4B C 502      96.073 -26.108-200.577  1.00 36.34           N  
HETATM13175  N3  H4B C 502      93.777 -25.622-200.588  1.00 43.83           N  
HETATM13176  C4  H4B C 502      92.689 -25.098-201.194  1.00 41.79           C  
HETATM13177  O4  H4B C 502      91.570 -25.146-200.634  1.00 47.20           O  
HETATM13178  C4A H4B C 502      92.812 -24.522-202.448  1.00 44.19           C  
HETATM13179  C8A H4B C 502      94.055 -24.468-203.054  1.00 41.21           C  
HETATM13180  N5  H4B C 502      91.741 -23.997-203.070  1.00 42.84           N  
HETATM13181  N8  H4B C 502      94.214 -23.915-204.277  1.00 44.47           N  
HETATM13182  C6  H4B C 502      91.791 -23.875-204.514  1.00 47.12           C  
HETATM13183  C7  H4B C 502      93.111 -23.276-204.992  1.00 39.71           C  
HETATM13184  C9  H4B C 502      90.610 -23.081-205.054  1.00 48.49           C  
HETATM13185  O9  H4B C 502      90.544 -21.774-204.492  1.00 57.57           O  
HETATM13186  C10 H4B C 502      90.785 -22.945-206.555  1.00 50.39           C  
HETATM13187  C11 H4B C 502      89.609 -22.200-207.169  1.00 48.99           C  
HETATM13188  O10 H4B C 502      90.879 -24.271-207.072  1.00 49.50           O  
HETATM13189  C02 OU1 C 503      96.293 -31.068-192.903  1.00 49.54           C  
HETATM13190  C03 OU1 C 503      96.229 -32.425-192.620  1.00 50.24           C  
HETATM13191  C04 OU1 C 503      95.229 -33.182-193.213  1.00 56.41           C  
HETATM13192  C05 OU1 C 503      94.317 -32.580-194.077  1.00 63.32           C  
HETATM13193  C06 OU1 C 503      93.308 -33.315-194.691  1.00 66.07           C  
HETATM13194  C07 OU1 C 503      92.414 -32.685-195.562  1.00 64.71           C  
HETATM13195  C08 OU1 C 503      92.487 -31.320-195.816  1.00 58.82           C  
HETATM13196  C09 OU1 C 503      93.505 -30.595-195.198  1.00 58.32           C  
HETATM13197  C10 OU1 C 503      94.413 -31.220-194.336  1.00 57.32           C  
HETATM13198  C11 OU1 C 503      95.149 -34.653-192.910  1.00 64.62           C  
HETATM13199  C21 OU1 C 503      91.496 -30.683-196.751  1.00 65.44           C  
HETATM13200  C22 OU1 C 503      90.926 -31.436-197.776  1.00 70.02           C  
HETATM13201  C23 OU1 C 503      90.003 -30.865-198.649  1.00 74.41           C  
HETATM13202  C24 OU1 C 503      89.633 -29.529-198.507  1.00 78.03           C  
HETATM13203  C25 OU1 C 503      90.194 -28.770-197.492  1.00 68.22           C  
HETATM13204  C26 OU1 C 503      91.118 -29.348-196.617  1.00 62.97           C  
HETATM13205  C27 OU1 C 503      89.785 -27.317-197.345  1.00 61.21           C  
HETATM13206  C30 OU1 C 503      87.731 -29.719-200.041  1.00 86.39           C  
HETATM13207  C31 OU1 C 503      86.485 -28.870-200.298  1.00 88.19           C  
HETATM13208  C32 OU1 C 503      86.460 -27.674-199.352  1.00 89.89           C  
HETATM13209  C33 OU1 C 503      85.590 -28.888-199.061  1.00 91.31           C  
HETATM13210  N01 OU1 C 503      95.392 -30.507-193.741  1.00 49.60           N  
HETATM13211  N02 OU1 C 503      97.260 -30.300-192.347  1.00 40.57           N  
HETATM13212  O29 OU1 C 503      88.721 -28.946-199.356  1.00 86.94           O  
HETATM13213  N28 OU1 C 503      90.605 -26.450-198.226  1.00 45.88           N  
HETATM13214  C1  BTB C 504      93.976  -0.893-182.552  1.00 69.20           C  
HETATM13215  O1  BTB C 504      92.905  -1.349-181.720  1.00 71.08           O  
HETATM13216  C2  BTB C 504      94.666   0.338-181.983  1.00 67.18           C  
HETATM13217  C3  BTB C 504      95.280   1.030-183.194  1.00 43.31           C  
HETATM13218  O3  BTB C 504      96.355   2.019-182.985  1.00 21.78           O  
HETATM13219  C4  BTB C 504      93.575   1.202-181.363  1.00 70.26           C  
HETATM13220  O4  BTB C 504      94.026   2.526-181.058  1.00 66.34           O  
HETATM13221  N   BTB C 504      95.675  -0.094-180.977  1.00 64.10           N  
HETATM13222  C5  BTB C 504      96.644  -1.040-181.557  1.00 58.51           C  
HETATM13223  C6  BTB C 504      98.014  -0.367-181.631  1.00 58.09           C  
HETATM13224  O6  BTB C 504      98.294   0.231-180.360  1.00 62.36           O  
HETATM13225  C7  BTB C 504      95.105  -0.638-179.726  1.00 67.85           C  
HETATM13226  C8  BTB C 504      95.386   0.302-178.550  1.00 66.58           C  
HETATM13227  O8  BTB C 504      96.738   0.777-178.599  1.00 66.68           O  
HETATM13228  C1  BTB C 505      84.701  -1.008-196.493  1.00 59.84           C  
HETATM13229  O1  BTB C 505      84.020  -1.539-195.348  1.00 71.46           O  
HETATM13230  C2  BTB C 505      86.161  -0.790-196.153  1.00 44.11           C  
HETATM13231  C3  BTB C 505      86.340  -0.991-194.656  1.00 71.47           C  
HETATM13232  O3  BTB C 505      85.946   0.182-193.942  1.00 81.56           O  
HETATM13233  C4  BTB C 505      87.026  -1.882-196.790  1.00 65.54           C  
HETATM13234  O4  BTB C 505      88.215  -2.082-196.012  1.00 56.90           O  
HETATM13235  N   BTB C 505      86.540   0.583-196.496  1.00 63.63           N  
HETATM13236  C5  BTB C 505      86.072   1.035-197.848  1.00 81.90           C  
HETATM13237  C6  BTB C 505      86.464   0.297-199.139  1.00 80.15           C  
HETATM13238  O6  BTB C 505      87.880   0.107-199.261  1.00 82.48           O  
HETATM13239  C7  BTB C 505      87.981   0.803-196.241  1.00 68.93           C  
HETATM13240  C8  BTB C 505      88.534   2.039-196.931  1.00 72.96           C  
HETATM13241  O8  BTB C 505      87.802   3.213-196.549  1.00 75.89           O  
HETATM13242  C1  BTB C 506      67.549 -51.161-182.969  1.00 86.49           C  
HETATM13243  O1  BTB C 506      68.527 -52.170-182.681  1.00 78.42           O  
HETATM13244  C2  BTB C 506      66.572 -51.687-184.012  1.00 95.86           C  
HETATM13245  C3  BTB C 506      67.370 -52.473-185.054  1.00 96.24           C  
HETATM13246  O3  BTB C 506      66.650 -53.645-185.460  1.00 99.64           O  
HETATM13247  C4  BTB C 506      65.594 -52.634-183.310  1.00 98.69           C  
HETATM13248  O4  BTB C 506      66.272 -53.381-182.293  1.00 98.47           O  
HETATM13249  N   BTB C 506      65.856 -50.525-184.618  1.00 98.47           N  
HETATM13250  C5  BTB C 506      64.405 -50.543-184.346  1.00 98.64           C  
HETATM13251  C6  BTB C 506      64.019 -49.319-183.521  1.00 97.05           C  
HETATM13252  O6  BTB C 506      64.224 -48.132-184.296  1.00 96.70           O  
HETATM13253  C7  BTB C 506      66.046 -50.420-186.078  1.00 93.73           C  
HETATM13254  C8  BTB C 506      66.776 -49.124-186.417  1.00 86.74           C  
HETATM13255  O8  BTB C 506      66.107 -48.005-185.820  1.00 85.03           O  
HETATM13256  C1  GOL C 507      87.796 -25.173-201.427  1.00 88.65           C  
HETATM13257  O1  GOL C 507      88.897 -26.052-201.403  1.00 97.35           O  
HETATM13258  C2  GOL C 507      88.295 -23.745-201.282  1.00 85.78           C  
HETATM13259  O2  GOL C 507      89.575 -23.743-200.689  1.00 93.87           O  
HETATM13260  C3  GOL C 507      87.326 -22.981-200.389  1.00 75.95           C  
HETATM13261  O3  GOL C 507      87.691 -21.624-200.385  1.00 64.81           O  
HETATM13262 CL    CL C 508      91.516 -26.711-191.541  1.00 54.29          CL  
HETATM13263 ZN    ZN D 501      94.538 -29.950-217.036  1.00 33.30          ZN  
HETATM13264  CHA HEM D 502     101.196 -12.204-219.570  1.00 23.96           C  
HETATM13265  CHB HEM D 502      99.944  -8.223-217.022  1.00 27.59           C  
HETATM13266  CHC HEM D 502      99.154  -5.853-221.137  1.00 27.00           C  
HETATM13267  CHD HEM D 502      99.662  -9.968-223.611  1.00 27.11           C  
HETATM13268  C1A HEM D 502     101.011 -11.293-218.553  1.00 26.40           C  
HETATM13269  C2A HEM D 502     101.436 -11.490-217.175  1.00 26.48           C  
HETATM13270  C3A HEM D 502     101.095 -10.396-216.467  1.00 28.24           C  
HETATM13271  C4A HEM D 502     100.457  -9.458-217.372  1.00 28.33           C  
HETATM13272  CMA HEM D 502     101.339 -10.133-214.950  1.00 25.30           C  
HETATM13273  CAA HEM D 502     102.155 -12.765-216.676  1.00 28.19           C  
HETATM13274  CBA HEM D 502     103.622 -12.590-217.048  1.00 40.34           C  
HETATM13275  CGA HEM D 502     104.549 -13.300-216.107  1.00 57.00           C  
HETATM13276  O1A HEM D 502     104.092 -13.748-215.048  1.00 48.38           O  
HETATM13277  O2A HEM D 502     105.757 -13.406-216.403  1.00 69.42           O  
HETATM13278  C1B HEM D 502      99.640  -7.209-217.886  1.00 29.77           C  
HETATM13279  C2B HEM D 502      99.323  -5.832-217.553  1.00 27.66           C  
HETATM13280  C3B HEM D 502      99.087  -5.167-218.709  1.00 29.28           C  
HETATM13281  C4B HEM D 502      99.262  -6.116-219.795  1.00 25.01           C  
HETATM13282  CMB HEM D 502      99.252  -5.212-216.144  1.00 27.89           C  
HETATM13283  CAB HEM D 502      98.727  -3.663-218.785  1.00 26.25           C  
HETATM13284  CBB HEM D 502      98.107  -3.104-219.824  1.00 34.66           C  
HETATM13285  C1C HEM D 502      99.249  -6.754-222.166  1.00 26.54           C  
HETATM13286  C2C HEM D 502      99.148  -6.425-223.578  1.00 28.74           C  
HETATM13287  C3C HEM D 502      99.304  -7.567-224.278  1.00 25.94           C  
HETATM13288  C4C HEM D 502      99.488  -8.649-223.325  1.00 26.29           C  
HETATM13289  CMC HEM D 502      98.952  -4.990-224.126  1.00 27.44           C  
HETATM13290  CAC HEM D 502      99.255  -7.806-225.806  1.00 25.85           C  
HETATM13291  CBC HEM D 502      98.721  -6.910-226.659  1.00 29.19           C  
HETATM13292  C1D HEM D 502     100.137 -10.924-222.731  1.00 26.80           C  
HETATM13293  C2D HEM D 502     100.507 -12.259-223.107  1.00 28.74           C  
HETATM13294  C3D HEM D 502     100.946 -12.898-222.002  1.00 30.54           C  
HETATM13295  C4D HEM D 502     100.842 -11.989-220.879  1.00 22.98           C  
HETATM13296  CMD HEM D 502     100.412 -12.824-224.554  1.00 24.98           C  
HETATM13297  CAD HEM D 502     101.406 -14.369-221.994  1.00 32.23           C  
HETATM13298  CBD HEM D 502     100.059 -15.080-222.012  1.00 47.74           C  
HETATM13299  CGD HEM D 502     100.051 -16.532-222.426  1.00 58.18           C  
HETATM13300  O1D HEM D 502     101.127 -17.155-222.710  1.00 48.89           O  
HETATM13301  O2D HEM D 502      98.900 -17.050-222.458  1.00 51.07           O  
HETATM13302  NA  HEM D 502     100.421 -10.034-218.631  1.00 26.08           N  
HETATM13303  NB  HEM D 502      99.588  -7.351-219.269  1.00 28.84           N  
HETATM13304  NC  HEM D 502      99.441  -8.115-222.055  1.00 23.94           N  
HETATM13305  ND  HEM D 502     100.351 -10.770-221.357  1.00 29.72           N  
HETATM13306 FE   HEM D 502      99.604  -9.190-220.296  1.00 27.56          FE  
HETATM13307  N1  H4B D 503     102.734 -17.473-213.116  1.00 42.58           N  
HETATM13308  C2  H4B D 503     103.169 -16.335-213.689  1.00 42.56           C  
HETATM13309  N2  H4B D 503     102.345 -15.262-213.683  1.00 39.64           N  
HETATM13310  N3  H4B D 503     104.395 -16.273-214.250  1.00 39.34           N  
HETATM13311  C4  H4B D 503     105.211 -17.345-214.267  1.00 42.42           C  
HETATM13312  O4  H4B D 503     106.337 -17.258-214.811  1.00 42.66           O  
HETATM13313  C4A H4B D 503     104.768 -18.529-213.691  1.00 41.06           C  
HETATM13314  C8A H4B D 503     103.512 -18.565-213.105  1.00 32.41           C  
HETATM13315  N5  H4B D 503     105.534 -19.637-213.678  1.00 35.37           N  
HETATM13316  N8  H4B D 503     103.018 -19.678-212.537  1.00 32.83           N  
HETATM13317  C6  H4B D 503     104.875 -20.918-213.522  1.00 37.26           C  
HETATM13318  C7  H4B D 503     103.790 -20.912-212.444  1.00 35.73           C  
HETATM13319  C9  H4B D 503     105.914 -22.011-213.294  1.00 44.92           C  
HETATM13320  O9  H4B D 503     106.822 -21.609-212.260  1.00 48.09           O  
HETATM13321  C10 H4B D 503     105.225 -23.315-212.942  1.00 53.04           C  
HETATM13322  C11 H4B D 503     106.219 -24.478-212.844  1.00 39.99           C  
HETATM13323  O10 H4B D 503     104.259 -23.561-213.968  1.00 52.14           O  
HETATM13324  C02 OU1 D 504     103.261  -7.097-218.400  1.00 33.98           C  
HETATM13325  C03 OU1 D 504     102.855  -6.587-219.641  1.00 35.72           C  
HETATM13326  C04 OU1 D 504     102.981  -7.368-220.771  1.00 37.52           C  
HETATM13327  C05 OU1 D 504     103.513  -8.641-220.663  1.00 35.57           C  
HETATM13328  C06 OU1 D 504     103.639  -9.451-221.794  1.00 39.51           C  
HETATM13329  C07 OU1 D 504     104.153 -10.736-221.650  1.00 44.22           C  
HETATM13330  C08 OU1 D 504     104.580 -11.210-220.414  1.00 50.06           C  
HETATM13331  C09 OU1 D 504     104.450 -10.390-219.296  1.00 51.25           C  
HETATM13332  C10 OU1 D 504     103.909  -9.115-219.419  1.00 38.53           C  
HETATM13333  C11 OU1 D 504     102.549  -6.824-222.117  1.00 38.76           C  
HETATM13334  C21 OU1 D 504     105.162 -12.581-220.268  1.00 53.45           C  
HETATM13335  C22 OU1 D 504     104.687 -13.663-221.014  1.00 68.17           C  
HETATM13336  C23 OU1 D 504     105.257 -14.926-220.857  1.00 73.80           C  
HETATM13337  C24 OU1 D 504     106.309 -15.092-219.956  1.00 78.62           C  
HETATM13338  C25 OU1 D 504     106.779 -14.024-219.218  1.00 62.30           C  
HETATM13339  C26 OU1 D 504     106.216 -12.768-219.385  1.00 48.63           C  
HETATM13340  C27 OU1 D 504     107.923 -14.251-218.249  1.00 56.96           C  
HETATM13341  C30 OU1 D 504     107.545 -17.065-220.752  1.00 89.74           C  
HETATM13342  C31 OU1 D 504     108.396 -18.072-219.994  1.00 93.75           C  
HETATM13343  C32 OU1 D 504     109.832 -18.015-220.507  1.00 96.19           C  
HETATM13344  C33 OU1 D 504     108.891 -19.118-220.970  1.00 94.66           C  
HETATM13345  N01 OU1 D 504     103.782  -8.339-218.317  1.00 36.62           N  
HETATM13346  N02 OU1 D 504     103.148  -6.356-217.279  1.00 32.44           N  
HETATM13347  O29 OU1 D 504     106.893 -16.310-219.745  1.00 86.23           O  
HETATM13348  N28 OU1 D 504     107.439 -15.002-217.067  1.00 54.68           N  
HETATM13349  C1  BTB D 505     111.253   8.581-190.148  1.00 82.47           C  
HETATM13350  O1  BTB D 505     110.250   8.466-189.133  1.00 81.74           O  
HETATM13351  C2  BTB D 505     111.703   7.185-190.563  1.00 83.56           C  
HETATM13352  C3  BTB D 505     110.613   6.159-190.256  1.00 67.61           C  
HETATM13353  O3  BTB D 505     110.997   4.928-190.888  1.00 53.73           O  
HETATM13354  C4  BTB D 505     111.864   7.088-192.083  1.00 88.86           C  
HETATM13355  O4  BTB D 505     113.224   7.157-192.520  1.00 97.97           O  
HETATM13356  N   BTB D 505     112.978   6.843-189.860  1.00 76.07           N  
HETATM13357  C5  BTB D 505     112.771   6.153-188.575  1.00 63.18           C  
HETATM13358  C6  BTB D 505     113.285   4.732-188.775  1.00 45.75           C  
HETATM13359  O6  BTB D 505     114.692   4.773-189.025  1.00 50.31           O  
HETATM13360  C7  BTB D 505     113.956   7.944-189.726  1.00 72.00           C  
HETATM13361  C8  BTB D 505     115.100   7.690-190.713  1.00 68.34           C  
HETATM13362  O8  BTB D 505     115.612   6.356-190.578  1.00 72.24           O  
HETATM13363  C1  BTB D 506     124.102 -10.450-246.392  1.00 70.30           C  
HETATM13364  O1  BTB D 506     124.372 -11.852-246.269  1.00 72.29           O  
HETATM13365  C2  BTB D 506     123.336 -10.238-247.692  1.00 70.31           C  
HETATM13366  C3  BTB D 506     124.152 -10.818-248.848  1.00 68.72           C  
HETATM13367  O3  BTB D 506     123.821 -12.210-248.953  1.00 74.75           O  
HETATM13368  C4  BTB D 506     122.050 -11.033-247.646  1.00 56.66           C  
HETATM13369  O4  BTB D 506     122.207 -12.067-246.667  1.00 69.85           O  
HETATM13370  N   BTB D 506     123.003  -8.803-247.915  1.00 80.84           N  
HETATM13371  C5  BTB D 506     123.342  -8.384-249.293  1.00 85.59           C  
HETATM13372  C6  BTB D 506     122.183  -7.607-249.906  1.00 90.30           C  
HETATM13373  O6  BTB D 506     121.836  -6.511-249.049  1.00 88.98           O  
HETATM13374  C7  BTB D 506     123.635  -7.913-246.909  1.00 74.32           C  
HETATM13375  C8  BTB D 506     124.763  -7.060-247.486  1.00 67.25           C  
HETATM13376  O8  BTB D 506     125.089  -6.015-246.560  1.00 73.81           O  
HETATM13377  C1  GOL D 507     109.101 -19.044-216.670  1.00 77.22           C  
HETATM13378  O1  GOL D 507     107.695 -18.976-216.786  1.00 76.50           O  
HETATM13379  C2  GOL D 507     109.458 -19.525-215.271  1.00 77.14           C  
HETATM13380  O2  GOL D 507     108.385 -19.228-214.403  1.00 76.23           O  
HETATM13381  C3  GOL D 507     110.724 -18.825-214.786  1.00 76.86           C  
HETATM13382  O3  GOL D 507     111.172 -19.420-213.586  1.00 67.71           O  
HETATM13383 CL    CL D 508     109.643  -8.816-216.910  1.00 48.32          CL  
HETATM13384 GD    GD D 509     113.597   4.692-191.463  1.00 48.61          GD  
HETATM13385  O   HOH A 601      56.107   3.070-191.853  1.00 47.10           O  
HETATM13386  O   HOH A 602      48.376  47.795-184.543  1.00 55.56           O  
HETATM13387  O   HOH A 603      58.945  53.047-186.347  1.00 50.87           O  
HETATM13388  O   HOH A 604      62.730  25.021-173.733  1.00 66.37           O  
HETATM13389  O   HOH A 605      54.390  49.765-181.287  1.00 55.45           O  
HETATM13390  O   HOH A 606      70.525  31.181-214.238  1.00 68.38           O  
HETATM13391  O   HOH A 607      64.484  48.969-173.937  1.00 97.49           O  
HETATM13392  O   HOH A 608      68.306  54.240-196.198  1.00 56.29           O  
HETATM13393  O   HOH A 609      60.551   8.871-186.020  1.00 41.40           O  
HETATM13394  O   HOH A 610      59.638  23.123-188.276  1.00 67.51           O  
HETATM13395  O   HOH A 611      64.198  41.125-164.214  1.00 65.46           O  
HETATM13396  O   HOH A 612      64.247  26.092-172.262  1.00 60.84           O  
HETATM13397  O   HOH A 613      74.560  36.203-191.051  1.00 39.47           O  
HETATM13398  O   HOH A 614      51.395  46.306-187.404  1.00 58.41           O  
HETATM13399  O   HOH A 615      75.999  39.199-174.767  1.00 47.94           O  
HETATM13400  O   HOH A 616      67.506  -6.834-197.292  1.00 77.61           O  
HETATM13401  O   HOH A 617      65.656  22.126-183.639  1.00 47.96           O  
HETATM13402  O   HOH A 618      69.177  -5.268-197.825  1.00 78.10           O  
HETATM13403  O   HOH A 619      83.645  29.231-172.011  1.00 49.16           O  
HETATM13404  O   HOH A 620      74.802  37.442-177.519  1.00 43.34           O  
HETATM13405  O   HOH A 621      56.731  51.169-188.096  1.00 60.06           O  
HETATM13406  O   HOH A 622      80.609  37.623-184.094  1.00 49.79           O  
HETATM13407  O   HOH A 623      53.536  12.707-191.630  1.00 52.01           O  
HETATM13408  O   HOH A 624      53.180  37.729-187.940  1.00 54.59           O  
HETATM13409  O   HOH A 625      75.508  32.235-170.309  1.00 37.14           O  
HETATM13410  O   HOH A 626      54.587  28.131-197.155  1.00 60.45           O  
HETATM13411  O   HOH A 627      63.468  27.566-199.435  1.00 43.20           O  
HETATM13412  O   HOH A 628      56.580  38.049-187.198  1.00 48.36           O  
HETATM13413  O   HOH A 629      77.224   7.840-193.360  1.00 44.05           O  
HETATM13414  O   HOH A 630      76.284  -1.717-184.362  1.00 41.95           O  
HETATM13415  O   HOH A 631      59.866  18.824-177.949  1.00 48.63           O  
HETATM13416  O   HOH A 632      85.033  29.512-169.500  1.00 50.64           O  
HETATM13417  O   HOH A 633      64.583  10.786-199.869  1.00 45.77           O  
HETATM13418  O   HOH A 634      77.141  30.947-183.191  1.00 43.25           O  
HETATM13419  O   HOH A 635      78.732  24.594-160.709  1.00 35.63           O  
HETATM13420  O   HOH A 636      59.842  38.565-185.650  1.00 43.08           O  
HETATM13421  O   HOH A 637      77.549  33.610-169.163  1.00 58.20           O  
HETATM13422  O   HOH A 638      59.478   6.059-186.925  1.00 48.46           O  
HETATM13423  O   HOH A 639      61.513  42.582-197.907  1.00 56.88           O  
HETATM13424  O   HOH A 640      63.809  13.799-182.823  1.00 38.19           O  
HETATM13425  O   HOH A 641      82.741  26.329-186.289  1.00 42.57           O  
HETATM13426  O   HOH A 642      74.525   5.375-188.462  1.00 45.88           O  
HETATM13427  O   HOH A 643      69.835  26.901-180.881  1.00 52.21           O  
HETATM13428  O   HOH A 644      57.771  30.168-156.421  1.00 59.15           O  
HETATM13429  O   HOH A 645      80.378  36.976-181.475  1.00 41.64           O  
HETATM13430  O   HOH A 646      73.426  16.886-188.161  1.00 48.66           O  
HETATM13431  O   HOH A 647      63.562  24.154-154.446  1.00 41.41           O  
HETATM13432  O   HOH A 648      62.372  11.015-182.210  1.00 46.23           O  
HETATM13433  O   HOH A 649      73.875  -2.432-182.975  1.00 51.23           O  
HETATM13434  O   HOH A 650      63.560  29.743-201.279  1.00 45.87           O  
HETATM13435  O   HOH A 651      75.903  31.401-197.068  1.00 53.29           O  
HETATM13436  O   HOH A 652      79.354  31.191-188.737  1.00 68.98           O  
HETATM13437  O   HOH A 653      65.857  38.177-178.468  1.00 40.64           O  
HETATM13438  O   HOH A 654      56.792  22.222-192.672  1.00 45.05           O  
HETATM13439  O   HOH A 655      55.107  33.692-181.609  1.00 54.07           O  
HETATM13440  O   HOH A 656      68.212  33.848-194.675  1.00 45.76           O  
HETATM13441  O   HOH A 657      80.346  39.557-180.217  1.00 46.53           O  
HETATM13442  O   HOH A 658      68.289  21.256-178.978  1.00 40.25           O  
HETATM13443  O   HOH A 659      76.284  23.686-198.279  1.00 43.94           O  
HETATM13444  O   HOH A 660      74.272  36.291-193.843  1.00 51.60           O  
HETATM13445  O   HOH A 661      59.711  34.196-161.701  1.00 49.63           O  
HETATM13446  O   HOH A 662      67.961  37.934-173.548  1.00 39.80           O  
HETATM13447  O   HOH A 663      53.714  12.384-186.345  1.00 60.98           O  
HETATM13448  O   HOH A 664      70.469  63.202-183.175  1.00 53.90           O  
HETATM13449  O   HOH A 665      65.241  37.732-167.225  1.00 53.38           O  
HETATM13450  O   HOH A 666      80.010  34.717-167.936  1.00 47.51           O  
HETATM13451  O   HOH A 667      67.747  25.539-170.080  1.00 51.84           O  
HETATM13452  O   HOH A 668      71.389  24.288-180.981  1.00 45.02           O  
HETATM13453  O   HOH A 669      80.100  34.790-172.282  1.00 43.92           O  
HETATM13454  O   HOH A 670      79.733  27.796-161.426  1.00 50.78           O  
HETATM13455  O   HOH A 671      70.213  16.490-176.656  1.00 48.02           O  
HETATM13456  O   HOH A 672      64.978  47.825-176.483  1.00 47.15           O  
HETATM13457  O   HOH A 673      58.678  36.246-186.905  1.00 50.97           O  
HETATM13458  O   HOH A 674      69.649  26.169-194.938  1.00 41.78           O  
HETATM13459  O   HOH A 675      78.939  22.313-191.430  1.00 41.77           O  
HETATM13460  O   HOH A 676      66.313  20.656-181.003  1.00 33.81           O  
HETATM13461  O   HOH A 677      71.081  27.844-166.622  1.00 42.96           O  
HETATM13462  O   HOH A 678      59.285  19.552-183.739  1.00 47.87           O  
HETATM13463  O   HOH A 679      82.465  21.098-182.038  1.00 39.49           O  
HETATM13464  O   HOH A 680      83.483  22.851-173.653  1.00 40.33           O  
HETATM13465  O   HOH A 681      83.023  40.529-180.533  1.00 65.10           O  
HETATM13466  O   HOH A 682      63.914  -3.516-176.176  1.00 50.96           O  
HETATM13467  O   HOH A 683      65.683  27.866-158.254  1.00 41.41           O  
HETATM13468  O   HOH A 684      81.844  18.597-181.468  1.00 33.93           O  
HETATM13469  O   HOH A 685      69.262  19.953-175.588  1.00 37.31           O  
HETATM13470  O   HOH A 686      52.213  18.273-197.703  1.00 56.98           O  
HETATM13471  O   HOH A 687      70.770  28.123-169.479  1.00 36.72           O  
HETATM13472  O   HOH A 688      78.993  39.317-185.696  1.00 71.74           O  
HETATM13473  O   HOH A 689      54.229  16.666-201.947  1.00 64.13           O  
HETATM13474  O   HOH A 690      65.615  54.660-169.259  1.00 55.29           O  
HETATM13475  O   HOH A 691      75.863  34.662-195.635  1.00 58.12           O  
HETATM13476  O   HOH A 692      63.633  33.094-164.395  1.00 50.25           O  
HETATM13477  O   HOH A 693      82.730  29.686-168.112  1.00 46.27           O  
HETATM13478  O   HOH A 694      58.032  30.223-183.977  1.00 62.24           O  
HETATM13479  O   HOH A 695      68.397  21.447-183.741  1.00 40.35           O  
HETATM13480  O   HOH A 696      70.500  -0.955-196.104  1.00 64.74           O  
HETATM13481  O   HOH A 697      70.216  58.097-183.855  1.00 53.52           O  
HETATM13482  O   HOH A 698      70.049   8.198-201.764  1.00 43.90           O  
HETATM13483  O   HOH A 699      82.697  17.079-176.147  1.00 46.98           O  
HETATM13484  O   HOH A 700      83.535  19.154-176.532  1.00 47.09           O  
HETATM13485  O   HOH A 701      78.952  13.897-198.755  1.00 66.95           O  
HETATM13486  O   HOH A 702      85.605  27.084-180.523  1.00 55.70           O  
HETATM13487  O   HOH A 703      57.507  46.324-173.822  1.00 70.23           O  
HETATM13488  O   HOH A 704      53.910  28.875-194.594  1.00 70.49           O  
HETATM13489  O   HOH A 705      78.947  15.510-196.031  1.00 64.51           O  
HETATM13490  O   HOH A 706      67.216   2.138-180.348  1.00 40.41           O  
HETATM13491  O   HOH A 707      55.431  26.675-157.411  1.00 63.88           O  
HETATM13492  O   HOH A 708      77.220  25.254-196.327  1.00 54.85           O  
HETATM13493  O   HOH A 709      65.843  38.619-175.611  1.00 52.45           O  
HETATM13494  O   HOH A 710      65.351  48.838-196.669  1.00 62.30           O  
HETATM13495  O   HOH A 711      75.329  36.259-205.226  1.00 66.95           O  
HETATM13496  O   HOH A 712      53.463   9.837-186.901  1.00 57.31           O  
HETATM13497  O   HOH A 713      62.654  -0.937-180.184  1.00 51.01           O  
HETATM13498  O   HOH A 714      78.498  26.611-193.671  1.00 68.32           O  
HETATM13499  O   HOH A 715      57.948   7.814-201.168  1.00 69.19           O  
HETATM13500  O   HOH A 716      78.300  22.145-193.875  1.00 54.61           O  
HETATM13501  O   HOH A 717      63.252  32.785-175.277  1.00 68.04           O  
HETATM13502  O   HOH A 718      89.738  30.376-165.552  1.00 62.70           O  
HETATM13503  O   HOH A 719      70.750  -3.313-185.625  1.00 66.03           O  
HETATM13504  O   HOH A 720      76.833  28.892-189.056  1.00 56.09           O  
HETATM13505  O   HOH A 721      76.822  31.594-158.863  1.00 68.48           O  
HETATM13506  O   HOH A 722      42.091  36.006-200.025  1.00 67.51           O  
HETATM13507  O   HOH A 723      81.526  24.693-159.622  1.00 55.07           O  
HETATM13508  O   HOH A 724      77.772  31.080-170.687  1.00 61.43           O  
HETATM13509  O   HOH A 725      62.403  44.372-199.611  1.00 60.47           O  
HETATM13510  O   HOH A 726      52.779  48.834-179.439  1.00 70.74           O  
HETATM13511  O   HOH A 727      69.662  22.669-181.223  1.00 41.80           O  
HETATM13512  O   HOH A 728      61.814  -2.766-178.055  1.00 57.41           O  
HETATM13513  O   HOH A 729      65.034  33.203-166.728  1.00 53.68           O  
HETATM13514  O   HOH A 730      63.619  37.129-175.091  1.00 64.88           O  
HETATM13515  O   HOH A 731      49.055  27.028-180.498  1.00 67.70           O  
HETATM13516  O   HOH A 732      68.996  -6.288-200.819  1.00 88.68           O  
HETATM13517  O   HOH A 733      53.885  30.975-180.450  1.00 65.52           O  
HETATM13518  O   HOH A 734      74.166  -5.063-178.878  1.00 82.29           O  
HETATM13519  O   HOH A 735      48.367  43.788-176.778  1.00 71.13           O  
HETATM13520  O   HOH A 736      59.597   7.311-177.715  1.00 58.58           O  
HETATM13521  O   HOH A 737      83.526  32.481-171.987  1.00 58.09           O  
HETATM13522  O   HOH A 738      51.435  30.324-179.660  1.00 60.65           O  
HETATM13523  O   HOH A 739      85.786  24.313-175.013  1.00 55.70           O  
HETATM13524  O   HOH A 740      75.007   2.552-188.852  1.00 60.38           O  
HETATM13525  O   HOH A 741      70.534  17.720-174.125  1.00 38.24           O  
HETATM13526  O   HOH A 742      59.763   5.534-175.583  1.00 45.26           O  
HETATM13527  O   HOH A 743      77.890  31.729-194.854  1.00 66.41           O  
HETATM13528  O   HOH A 744      49.209  45.297-174.038  1.00 70.90           O  
HETATM13529  O   HOH B 601      58.136   2.820-159.273  1.00 47.91           O  
HETATM13530  O   HOH B 602      93.458  -1.684-140.958  1.00 58.38           O  
HETATM13531  O   HOH B 603      55.164  25.375-172.615  1.00 47.80           O  
HETATM13532  O   HOH B 604      87.245  11.200-158.451  1.00 57.99           O  
HETATM13533  O   HOH B 605      57.499  12.831-156.858  1.00 46.30           O  
HETATM13534  O   HOH B 606      74.172  20.597-164.367  1.00 51.09           O  
HETATM13535  O   HOH B 607      85.361  14.964-142.371  1.00 54.61           O  
HETATM13536  O   HOH B 608      90.246   8.246-190.502  1.00 65.86           O  
HETATM13537  O   HOH B 609      75.296  -8.262-178.549  1.00 51.30           O  
HETATM13538  O   HOH B 610      82.702  15.645-142.934  1.00 58.40           O  
HETATM13539  O   HOH B 611      72.618   1.986-131.943  1.00 64.12           O  
HETATM13540  O   HOH B 612      80.788  -3.658-188.093  1.00 47.36           O  
HETATM13541  O   HOH B 613      53.276  17.816-163.332  1.00 52.23           O  
HETATM13542  O   HOH B 614      62.599  23.222-165.636  1.00 40.07           O  
HETATM13543  O   HOH B 615      72.901  13.282-134.175  1.00 60.19           O  
HETATM13544  O   HOH B 616      77.788   8.444-164.281  1.00 41.59           O  
HETATM13545  O   HOH B 617      83.096  -9.957-166.390  1.00 44.53           O  
HETATM13546  O   HOH B 618      82.645  13.100-167.244  1.00 36.45           O  
HETATM13547  O   HOH B 619      84.852  10.834-159.516  1.00 57.01           O  
HETATM13548  O   HOH B 620      80.633  18.299-168.381  1.00 42.09           O  
HETATM13549  O   HOH B 621      59.637   9.798-177.829  1.00 45.37           O  
HETATM13550  O   HOH B 622      73.926   3.871-174.781  1.00 53.12           O  
HETATM13551  O   HOH B 623      57.711   5.717-135.735  1.00 45.28           O  
HETATM13552  O   HOH B 624      64.091  17.208-154.766  1.00 37.11           O  
HETATM13553  O   HOH B 625      59.944  11.005-157.630  1.00 38.02           O  
HETATM13554  O   HOH B 626      89.523  -5.231-172.293  1.00 40.21           O  
HETATM13555  O   HOH B 627      69.690  -6.718-161.847  1.00 36.54           O  
HETATM13556  O   HOH B 628      68.419  -1.934-172.103  1.00 35.75           O  
HETATM13557  O   HOH B 629      93.075   8.257-170.264  1.00 44.24           O  
HETATM13558  O   HOH B 630      69.535   7.635-136.077  1.00 36.80           O  
HETATM13559  O   HOH B 631      74.338  -8.913-146.469  1.00 63.76           O  
HETATM13560  O   HOH B 632      53.790  24.500-169.951  1.00 55.42           O  
HETATM13561  O   HOH B 633      67.489  -3.903-154.071  1.00 37.70           O  
HETATM13562  O   HOH B 634      72.985 -12.561-152.058  1.00 52.63           O  
HETATM13563  O   HOH B 635      76.097  10.528-167.493  1.00 38.44           O  
HETATM13564  O   HOH B 636      61.373   5.277-127.487  1.00 62.45           O  
HETATM13565  O   HOH B 637      82.898  13.936-176.214  1.00 45.18           O  
HETATM13566  O   HOH B 638      75.763  -4.809-144.118  1.00 47.20           O  
HETATM13567  O   HOH B 639      59.606  13.575-149.608  1.00 44.32           O  
HETATM13568  O   HOH B 640      79.811  14.131-136.438  1.00 42.09           O  
HETATM13569  O   HOH B 641      86.890   5.683-162.928  1.00 32.84           O  
HETATM13570  O   HOH B 642      58.786  17.865-163.286  1.00 36.64           O  
HETATM13571  O   HOH B 643      86.719  11.585-176.967  1.00 39.34           O  
HETATM13572  O   HOH B 644      87.932   2.050-155.859  1.00 32.97           O  
HETATM13573  O   HOH B 645      91.261  13.456-171.265  1.00 43.47           O  
HETATM13574  O   HOH B 646      67.340  -6.396-153.412  1.00 65.24           O  
HETATM13575  O   HOH B 647      59.546   6.142-149.069  1.00 62.36           O  
HETATM13576  O   HOH B 648      97.901  11.283-160.132  1.00 57.83           O  
HETATM13577  O   HOH B 649      87.384   4.740-155.491  1.00 34.19           O  
HETATM13578  O   HOH B 650      57.365  12.201-174.877  1.00 44.16           O  
HETATM13579  O   HOH B 651      89.956   6.623-140.255  1.00 41.29           O  
HETATM13580  O   HOH B 652      63.134   5.346-163.940  1.00 39.17           O  
HETATM13581  O   HOH B 653      66.196  -1.313-157.447  1.00 33.43           O  
HETATM13582  O   HOH B 654      54.478  10.394-147.054  1.00 62.47           O  
HETATM13583  O   HOH B 655      67.865  31.599-155.935  1.00 52.89           O  
HETATM13584  O   HOH B 656      86.809   7.399-134.115  1.00 52.15           O  
HETATM13585  O   HOH B 657      78.236   9.025-148.529  1.00 32.65           O  
HETATM13586  O   HOH B 658      73.795  -1.719-156.739  1.00 31.77           O  
HETATM13587  O   HOH B 659      61.617   0.875-170.444  1.00 42.07           O  
HETATM13588  O   HOH B 660      69.133  19.794-159.979  1.00 45.07           O  
HETATM13589  O   HOH B 661      79.566  11.292-136.129  1.00 45.12           O  
HETATM13590  O   HOH B 662      76.686  -2.914-145.832  1.00 34.43           O  
HETATM13591  O   HOH B 663      63.442  14.976-144.394  1.00 33.31           O  
HETATM13592  O   HOH B 664      79.439  10.723-139.196  1.00 40.38           O  
HETATM13593  O   HOH B 665      80.899  12.825-174.226  1.00 30.88           O  
HETATM13594  O   HOH B 666      94.264  -3.611-136.496  1.00 38.80           O  
HETATM13595  O   HOH B 667      88.055  -9.389-181.320  1.00 53.28           O  
HETATM13596  O   HOH B 668      91.099  -3.649-163.813  1.00 66.50           O  
HETATM13597  O   HOH B 669      81.693  -5.466-157.817  1.00 30.55           O  
HETATM13598  O   HOH B 670      81.482   2.569-158.112  1.00 30.28           O  
HETATM13599  O   HOH B 671      57.413   5.281-159.925  1.00 36.72           O  
HETATM13600  O   HOH B 672      79.670  17.568-145.033  1.00 35.88           O  
HETATM13601  O   HOH B 673      69.817  11.229-165.284  1.00 39.66           O  
HETATM13602  O   HOH B 674     100.063   0.112-151.105  1.00 59.80           O  
HETATM13603  O   HOH B 675      63.624   6.352-177.322  1.00 41.85           O  
HETATM13604  O   HOH B 676      89.051   3.686-136.995  1.00 50.31           O  
HETATM13605  O   HOH B 677      67.534  -1.896-142.679  1.00 53.68           O  
HETATM13606  O   HOH B 678      54.385   4.006-134.464  1.00 47.58           O  
HETATM13607  O   HOH B 679      82.514   8.586-163.693  1.00 36.72           O  
HETATM13608  O   HOH B 680      72.705  13.667-169.535  1.00 34.10           O  
HETATM13609  O   HOH B 681      71.081  16.531-171.532  1.00 34.64           O  
HETATM13610  O   HOH B 682      67.488  13.615-153.224  1.00 31.52           O  
HETATM13611  O   HOH B 683      67.681  -6.179-158.857  1.00 42.13           O  
HETATM13612  O   HOH B 684      88.336  -2.770-175.670  1.00 34.87           O  
HETATM13613  O   HOH B 685      62.266   5.231-175.229  1.00 38.27           O  
HETATM13614  O   HOH B 686      67.833 -10.912-154.759  1.00 73.39           O  
HETATM13615  O   HOH B 687      71.551  20.995-164.130  1.00 48.41           O  
HETATM13616  O   HOH B 688      75.880  -1.887-164.346  1.00 28.63           O  
HETATM13617  O   HOH B 689      64.288   1.081-134.509  1.00 51.86           O  
HETATM13618  O   HOH B 690      80.594 -11.580-165.572  1.00 52.49           O  
HETATM13619  O   HOH B 691      94.438   3.508-163.812  1.00 39.04           O  
HETATM13620  O   HOH B 692      71.813  14.042-176.966  1.00 50.99           O  
HETATM13621  O   HOH B 693      91.223  -1.413-154.238  1.00 39.24           O  
HETATM13622  O   HOH B 694      85.768  -6.279-180.517  1.00 33.95           O  
HETATM13623  O   HOH B 695      56.029   6.221-157.752  1.00 46.63           O  
HETATM13624  O   HOH B 696      86.488  16.916-188.024  1.00 50.21           O  
HETATM13625  O   HOH B 697      91.048   9.389-179.119  1.00 49.44           O  
HETATM13626  O   HOH B 698      95.041  -1.199-165.569  1.00 40.95           O  
HETATM13627  O   HOH B 699      60.007   1.549-143.653  1.00 38.33           O  
HETATM13628  O   HOH B 700      74.249  -0.890-137.158  1.00 44.65           O  
HETATM13629  O   HOH B 701      83.618 -10.173-158.883  1.00 47.04           O  
HETATM13630  O   HOH B 702      61.554   0.439-136.796  1.00 41.55           O  
HETATM13631  O   HOH B 703      67.384  -3.801-156.937  1.00 30.98           O  
HETATM13632  O   HOH B 704      74.842   9.386-149.700  1.00 34.26           O  
HETATM13633  O   HOH B 705      88.129  14.822-165.685  1.00 41.71           O  
HETATM13634  O   HOH B 706      95.826   4.278-178.794  1.00 57.07           O  
HETATM13635  O   HOH B 707      92.476   6.890-172.734  1.00 46.21           O  
HETATM13636  O   HOH B 708      77.002   8.774-142.117  1.00 32.10           O  
HETATM13637  O   HOH B 709      72.795  14.729-137.855  1.00 39.25           O  
HETATM13638  O   HOH B 710      75.379  -4.619-137.163  1.00 61.56           O  
HETATM13639  O   HOH B 711      61.777  16.926-143.470  1.00 43.44           O  
HETATM13640  O   HOH B 712      74.292   9.452-169.307  1.00 33.67           O  
HETATM13641  O   HOH B 713      64.184  20.720-165.177  1.00 37.93           O  
HETATM13642  O   HOH B 714      85.031  12.970-150.833  1.00 47.26           O  
HETATM13643  O   HOH B 715      88.923  20.666-150.453  1.00 61.66           O  
HETATM13644  O   HOH B 716      81.343  10.127-147.460  1.00 32.98           O  
HETATM13645  O   HOH B 717      47.971   5.307-132.888  1.00 65.04           O  
HETATM13646  O   HOH B 718      70.616  -3.592-141.913  1.00 43.23           O  
HETATM13647  O   HOH B 719      89.200  11.788-179.166  1.00 39.22           O  
HETATM13648  O   HOH B 720      86.234  -1.950-134.603  1.00 38.52           O  
HETATM13649  O   HOH B 721      89.854  12.836-157.575  1.00 49.02           O  
HETATM13650  O   HOH B 722      71.817  24.462-160.920  1.00 44.58           O  
HETATM13651  O   HOH B 723      98.743  -1.854-163.664  1.00 61.79           O  
HETATM13652  O   HOH B 724      82.093  -3.510-159.881  1.00 31.74           O  
HETATM13653  O   HOH B 725      69.558  10.276-167.882  1.00 38.56           O  
HETATM13654  O   HOH B 726      73.264  11.081-180.882  1.00 42.19           O  
HETATM13655  O   HOH B 727      70.260  18.323-157.829  1.00 41.98           O  
HETATM13656  O   HOH B 728      94.834   6.596-170.288  1.00 46.22           O  
HETATM13657  O   HOH B 729      89.061  -6.161-174.506  1.00 53.19           O  
HETATM13658  O   HOH B 730      82.620  15.309-151.106  1.00 51.82           O  
HETATM13659  O   HOH B 731      69.559  14.568-154.941  1.00 31.56           O  
HETATM13660  O   HOH B 732      79.207  15.372-152.676  1.00 37.09           O  
HETATM13661  O   HOH B 733      70.369  -3.982-171.697  1.00 54.30           O  
HETATM13662  O   HOH B 734      72.764  -7.337-169.154  1.00 42.75           O  
HETATM13663  O   HOH B 735      70.035  11.559-129.039  1.00 47.96           O  
HETATM13664  O   HOH B 736      92.965   2.411-176.189  1.00 50.98           O  
HETATM13665  O   HOH B 737      67.198  23.139-163.118  1.00 50.39           O  
HETATM13666  O   HOH B 738      77.205   8.899-151.238  1.00 31.13           O  
HETATM13667  O   HOH B 739      73.088   7.368-136.754  1.00 34.08           O  
HETATM13668  O   HOH B 740      79.420 -10.834-156.814  1.00 52.08           O  
HETATM13669  O   HOH B 741      58.216   3.414-136.648  1.00 60.35           O  
HETATM13670  O   HOH B 742      94.139  -2.980-147.187  1.00 52.23           O  
HETATM13671  O   HOH B 743      51.037   6.104-158.459  1.00 53.00           O  
HETATM13672  O   HOH B 744      96.351  -0.502-168.924  1.00 50.00           O  
HETATM13673  O   HOH B 745      63.549  -0.565-164.403  1.00 49.25           O  
HETATM13674  O   HOH B 746      85.918  -9.101-163.016  1.00 40.22           O  
HETATM13675  O   HOH B 747      86.374  -9.866-160.278  1.00 65.62           O  
HETATM13676  O   HOH B 748      81.085  -8.860-155.842  1.00 59.19           O  
HETATM13677  O   HOH B 749      66.255  16.130-153.115  1.00 36.24           O  
HETATM13678  O   HOH B 750      53.124  16.922-168.744  1.00 49.77           O  
HETATM13679  O   HOH B 751      77.543  14.121-194.816  1.00 56.14           O  
HETATM13680  O   HOH B 752      55.164   1.393-162.710  1.00 51.48           O  
HETATM13681  O   HOH B 753      82.257  -8.760-171.956  1.00 47.97           O  
HETATM13682  O   HOH B 754      90.618  14.802-159.548  1.00 45.22           O  
HETATM13683  O   HOH B 755      75.312  12.787-169.317  1.00 32.66           O  
HETATM13684  O   HOH B 756      78.665  12.681-156.474  1.00 53.52           O  
HETATM13685  O   HOH B 757      72.139  15.941-174.534  1.00 47.87           O  
HETATM13686  O   HOH B 758      92.848  -3.177-160.718  1.00 41.73           O  
HETATM13687  O   HOH B 759      88.326  19.061-155.123  1.00 65.78           O  
HETATM13688  O   HOH B 760      63.494  -2.473-148.309  1.00 60.63           O  
HETATM13689  O   HOH B 761      61.434  10.691-179.871  1.00 55.99           O  
HETATM13690  O   HOH B 762      67.621  21.636-166.586  1.00 54.64           O  
HETATM13691  O   HOH B 763      56.718   3.491-145.055  1.00 59.34           O  
HETATM13692  O   HOH B 764      63.076  -2.706-150.919  1.00 54.67           O  
HETATM13693  O   HOH B 765      71.843  -9.270-165.087  1.00 58.05           O  
HETATM13694  O   HOH B 766      82.257  18.257-144.816  1.00 52.73           O  
HETATM13695  O   HOH B 767      81.173  10.116-159.423  1.00 52.69           O  
HETATM13696  O   HOH B 768      90.961   4.869-138.392  1.00 50.51           O  
HETATM13697  O   HOH B 769      70.557  -6.047-168.105  1.00 44.09           O  
HETATM13698  O   HOH B 770      65.405  24.907-158.720  1.00 54.33           O  
HETATM13699  O   HOH B 771      53.221   8.694-151.792  1.00 55.93           O  
HETATM13700  O   HOH B 772      83.074   9.258-192.969  1.00 56.31           O  
HETATM13701  O   HOH B 773      81.802  14.867-186.458  1.00 38.70           O  
HETATM13702  O   HOH B 774      68.891  17.510-153.407  1.00 61.49           O  
HETATM13703  O   HOH B 775      73.255  19.613-153.100  1.00 46.28           O  
HETATM13704  O   HOH B 776      80.153  12.036-166.201  1.00 46.27           O  
HETATM13705  O   HOH B 777      73.768  26.570-134.489  1.00 67.54           O  
HETATM13706  O   HOH B 778      46.771   8.418-142.703  1.00 59.21           O  
HETATM13707  O   HOH B 779      65.353  -2.523-146.912  1.00 52.53           O  
HETATM13708  O   HOH B 780      83.959  22.810-189.082  1.00 59.99           O  
HETATM13709  O   HOH B 781      70.449  20.048-143.002  1.00 54.24           O  
HETATM13710  O   HOH B 782      56.312  17.458-163.330  1.00 67.07           O  
HETATM13711  O   HOH B 783      78.844   9.535-166.481  1.00 42.40           O  
HETATM13712  O   HOH B 784      65.900   4.544-132.280  1.00 59.80           O  
HETATM13713  O   HOH B 785      72.077  10.963-168.888  1.00 31.55           O  
HETATM13714  O   HOH B 786      58.614  16.390-149.329  1.00 66.41           O  
HETATM13715  O   HOH B 787      60.021   1.706-146.314  1.00 47.94           O  
HETATM13716  O   HOH B 788      66.248   0.686-165.101  1.00 44.95           O  
HETATM13717  O   HOH B 789      66.171  -3.516-143.963  1.00 61.77           O  
HETATM13718  O   HOH B 790      59.290   1.399-135.289  1.00 57.90           O  
HETATM13719  O   HOH B 791      80.288  10.992-157.439  1.00 53.29           O  
HETATM13720  O   HOH B 792      72.521  -9.725-167.645  1.00 66.75           O  
HETATM13721  O   HOH B 793      60.980  -1.127-143.026  1.00 54.78           O  
HETATM13722  O   HOH B 794      57.521   1.575-143.123  1.00 51.25           O  
HETATM13723  O   HOH B 795      90.423  -5.001-140.118  1.00 63.74           O  
HETATM13724  O   HOH B 796      88.416   5.130-134.446  1.00 73.55           O  
HETATM13725  O   HOH B 797      56.305  -0.054-165.179  1.00 61.44           O  
HETATM13726  O   HOH B 798      59.060   1.140-169.790  1.00 69.23           O  
HETATM13727  O   HOH B 799      55.753  10.174-174.134  1.00 59.55           O  
HETATM13728  O   HOH B 800      67.473  25.159-160.558  1.00 54.74           O  
HETATM13729  O   HOH B 801      66.430  -2.366-166.551  1.00 60.44           O  
HETATM13730  O   HOH B 802      55.792  15.326-164.525  1.00 60.12           O  
HETATM13731  O   HOH B 803      90.590  -5.038-158.859  1.00 54.22           O  
HETATM13732  O   HOH B 804      54.046   4.937-156.796  1.00 61.44           O  
HETATM13733  O   HOH B 805      66.243  -2.688-170.831  1.00 58.48           O  
HETATM13734  O   HOH B 806      58.020   4.039-149.243  1.00 48.11           O  
HETATM13735  O   HOH B 807      84.614  21.816-180.645  1.00 49.73           O  
HETATM13736  O   HOH B 808      66.753  -8.267-157.646  1.00 72.64           O  
HETATM13737  O   HOH B 809      67.054  -5.760-162.991  1.00 56.71           O  
HETATM13738  O   HOH B 810      69.811   0.594-131.468  1.00 69.27           O  
HETATM13739  O   HOH C 601      88.642 -47.540-209.047  1.00 65.40           O  
HETATM13740  O   HOH C 602      95.118 -24.515-197.019  1.00 41.75           O  
HETATM13741  O   HOH C 603     104.501 -34.408-183.656  1.00 74.42           O  
HETATM13742  O   HOH C 604      98.191   3.655-182.783  1.00 75.07           O  
HETATM13743  O   HOH C 605      96.550 -57.072-184.917  1.00 44.56           O  
HETATM13744  O   HOH C 606      93.112 -16.123-197.590  1.00 35.56           O  
HETATM13745  O   HOH C 607     110.450 -29.153-220.688  1.00 57.50           O  
HETATM13746  O   HOH C 608      84.771 -53.095-193.032  1.00 49.65           O  
HETATM13747  O   HOH C 609      93.511 -55.994-184.397  1.00 60.58           O  
HETATM13748  O   HOH C 610      87.036 -56.533-181.798  1.00 70.64           O  
HETATM13749  O   HOH C 611      92.742 -16.194-177.663  1.00 48.11           O  
HETATM13750  O   HOH C 612      87.435 -55.315-194.660  1.00 50.28           O  
HETATM13751  O   HOH C 613     103.315 -39.204-189.911  1.00 42.48           O  
HETATM13752  O   HOH C 614     108.283 -42.077-200.764  1.00 51.89           O  
HETATM13753  O   HOH C 615      90.172 -11.246-194.250  1.00 43.10           O  
HETATM13754  O   HOH C 616     102.756 -19.583-192.271  1.00 42.43           O  
HETATM13755  O   HOH C 617      88.981 -20.755-202.428  1.00 40.44           O  
HETATM13756  O   HOH C 618     108.344 -29.775-219.290  1.00 49.65           O  
HETATM13757  O   HOH C 619      81.753 -20.449-182.789  1.00 49.03           O  
HETATM13758  O   HOH C 620     104.366  -7.964-191.733  1.00 45.10           O  
HETATM13759  O   HOH C 621      90.392 -45.038-182.978  1.00 42.43           O  
HETATM13760  O   HOH C 622      83.318 -14.403-193.979  1.00 48.02           O  
HETATM13761  O   HOH C 623      88.264 -35.722-218.863  1.00 47.08           O  
HETATM13762  O   HOH C 624     106.023  -0.638-195.726  1.00 43.20           O  
HETATM13763  O   HOH C 625      82.981 -20.415-195.924  1.00 54.92           O  
HETATM13764  O   HOH C 626      84.108 -64.815-207.537  1.00 43.38           O  
HETATM13765  O   HOH C 627     108.707 -36.854-212.908  1.00 57.72           O  
HETATM13766  O   HOH C 628      96.739 -40.010-207.451  1.00 34.16           O  
HETATM13767  O   HOH C 629     105.618 -26.688-182.313  1.00 47.40           O  
HETATM13768  O   HOH C 630     113.771 -31.993-211.557  1.00 55.88           O  
HETATM13769  O   HOH C 631     106.136 -36.361-211.786  1.00 48.96           O  
HETATM13770  O   HOH C 632     106.089 -33.484-197.639  1.00 44.32           O  
HETATM13771  O   HOH C 633     107.721  -9.654-184.594  1.00 53.70           O  
HETATM13772  O   HOH C 634     112.353 -25.350-207.084  1.00 42.68           O  
HETATM13773  O   HOH C 635      97.293 -36.612-186.319  1.00 45.63           O  
HETATM13774  O   HOH C 636      86.387 -31.350-224.106  1.00 44.91           O  
HETATM13775  O   HOH C 637     114.243 -29.896-200.266  1.00 51.82           O  
HETATM13776  O   HOH C 638     103.641 -39.797-203.534  1.00 43.40           O  
HETATM13777  O   HOH C 639      92.988 -28.005-208.249  1.00 52.84           O  
HETATM13778  O   HOH C 640      85.331 -40.283-193.521  1.00 48.90           O  
HETATM13779  O   HOH C 641      90.035 -30.341-210.952  1.00 49.02           O  
HETATM13780  O   HOH C 642      86.164 -24.366-187.795  1.00 44.61           O  
HETATM13781  O   HOH C 643     111.093 -21.115-199.182  1.00 40.04           O  
HETATM13782  O   HOH C 644      83.205 -11.627-193.523  1.00 57.33           O  
HETATM13783  O   HOH C 645      97.430 -23.502-201.647  1.00 34.63           O  
HETATM13784  O   HOH C 646      94.477 -40.440-202.603  1.00 37.14           O  
HETATM13785  O   HOH C 647     103.619   0.312-197.331  1.00 53.01           O  
HETATM13786  O   HOH C 648     103.086 -39.294-187.201  1.00 43.42           O  
HETATM13787  O   HOH C 649      91.964 -13.356-198.066  1.00 41.93           O  
HETATM13788  O   HOH C 650      92.832  -0.581-199.754  1.00 40.23           O  
HETATM13789  O   HOH C 651     108.561 -37.437-208.979  1.00 47.79           O  
HETATM13790  O   HOH C 652      82.181 -39.906-193.033  1.00 60.56           O  
HETATM13791  O   HOH C 653      92.846 -49.955-204.626  1.00 50.71           O  
HETATM13792  O   HOH C 654     109.260 -40.477-197.185  1.00 47.66           O  
HETATM13793  O   HOH C 655     112.743 -31.671-209.021  1.00 52.61           O  
HETATM13794  O   HOH C 656      92.526 -51.573-207.348  1.00 50.37           O  
HETATM13795  O   HOH C 657      99.936 -29.942-214.034  1.00 40.92           O  
HETATM13796  O   HOH C 658     111.530 -23.976-198.739  1.00 38.08           O  
HETATM13797  O   HOH C 659     110.982 -41.959-215.594  1.00 64.13           O  
HETATM13798  O   HOH C 660      79.648 -47.989-193.785  1.00 57.69           O  
HETATM13799  O   HOH C 661     108.308 -34.110-192.293  1.00 56.44           O  
HETATM13800  O   HOH C 662      94.616 -50.606-206.112  1.00 80.37           O  
HETATM13801  O   HOH C 663      83.161 -31.036-185.903  1.00 55.36           O  
HETATM13802  O   HOH C 664      98.866 -28.944-185.752  1.00 37.19           O  
HETATM13803  O   HOH C 665     107.629 -26.741-220.154  1.00 37.31           O  
HETATM13804  O   HOH C 666     101.159 -17.210-202.768  1.00 50.34           O  
HETATM13805  O   HOH C 667      88.735 -21.714-196.581  1.00 38.18           O  
HETATM13806  O   HOH C 668     111.948 -19.480-204.620  1.00 55.66           O  
HETATM13807  O   HOH C 669      89.748 -31.290-187.010  1.00 45.59           O  
HETATM13808  O   HOH C 670     101.908 -41.882-186.573  1.00 42.81           O  
HETATM13809  O   HOH C 671      94.286 -13.497-180.560  1.00 34.18           O  
HETATM13810  O   HOH C 672      88.513 -40.901-195.267  1.00 49.09           O  
HETATM13811  O   HOH C 673      94.363 -29.503-222.650  1.00 35.26           O  
HETATM13812  O   HOH C 674      84.070 -16.008-178.690  1.00 56.21           O  
HETATM13813  O   HOH C 675     109.143 -39.742-199.807  1.00 49.14           O  
HETATM13814  O   HOH C 676     108.297 -25.258-189.523  1.00 42.33           O  
HETATM13815  O   HOH C 677     104.353 -34.462-210.598  1.00 39.27           O  
HETATM13816  O   HOH C 678      92.728 -30.318-181.298  1.00 47.64           O  
HETATM13817  O   HOH C 679      96.902 -27.452-210.385  1.00 44.27           O  
HETATM13818  O   HOH C 680     100.579 -26.769-199.696  1.00 37.60           O  
HETATM13819  O   HOH C 681      98.844 -29.058-199.903  1.00 47.86           O  
HETATM13820  O   HOH C 682      83.842 -46.797-193.390  1.00 53.07           O  
HETATM13821  O   HOH C 683      89.141  -8.341-193.422  1.00 45.91           O  
HETATM13822  O   HOH C 684      98.486 -22.091-204.893  1.00 37.88           O  
HETATM13823  O   HOH C 685      93.099 -38.018-202.554  1.00 40.41           O  
HETATM13824  O   HOH C 686     100.470   1.422-194.321  1.00 55.83           O  
HETATM13825  O   HOH C 687     113.060 -21.805-204.094  1.00 51.92           O  
HETATM13826  O   HOH C 688      83.861 -30.314-183.592  1.00 58.06           O  
HETATM13827  O   HOH C 689      92.736 -32.463-179.736  1.00 44.80           O  
HETATM13828  O   HOH C 690      98.007 -59.413-192.129  1.00 66.96           O  
HETATM13829  O   HOH C 691      79.200 -41.552-200.229  1.00 59.60           O  
HETATM13830  O   HOH C 692      83.793 -19.392-178.403  1.00 55.94           O  
HETATM13831  O   HOH C 693      95.324 -55.254-184.735  1.00 54.03           O  
HETATM13832  O   HOH C 694      99.637 -30.175-211.202  1.00 32.19           O  
HETATM13833  O   HOH C 695     111.414 -32.202-212.764  1.00 44.28           O  
HETATM13834  O   HOH C 696     107.625 -42.721-195.893  1.00 58.56           O  
HETATM13835  O   HOH C 697      85.310 -47.774-206.853  1.00 64.95           O  
HETATM13836  O   HOH C 698     107.459 -24.959-186.646  1.00 53.62           O  
HETATM13837  O   HOH C 699      93.108 -51.102-184.238  1.00 55.04           O  
HETATM13838  O   HOH C 700      93.809 -33.267-207.803  1.00 60.61           O  
HETATM13839  O   HOH C 701      94.797 -14.739-177.255  1.00 51.44           O  
HETATM13840  O   HOH C 702      92.646 -34.490-205.771  1.00 43.37           O  
HETATM13841  O   HOH C 703      99.940 -10.814-178.505  1.00 38.01           O  
HETATM13842  O   HOH C 704      90.564 -23.889-196.917  1.00 57.27           O  
HETATM13843  O   HOH C 705     113.666 -38.488-197.487  1.00 51.26           O  
HETATM13844  O   HOH C 706      94.317 -40.789-205.472  1.00 46.27           O  
HETATM13845  O   HOH C 707      95.583 -22.902-199.461  1.00 32.52           O  
HETATM13846  O   HOH C 708      88.788 -25.613-192.807  1.00 64.91           O  
HETATM13847  O   HOH C 709      87.671 -38.440-194.009  1.00 48.35           O  
HETATM13848  O   HOH C 710      83.909 -50.592-206.313  1.00 63.52           O  
HETATM13849  O   HOH C 711      99.336 -18.638-203.819  1.00 47.62           O  
HETATM13850  O   HOH C 712     112.122 -28.966-194.512  1.00 53.72           O  
HETATM13851  O   HOH C 713      84.134 -35.569-199.258  1.00 49.53           O  
HETATM13852  O   HOH C 714      92.529 -64.046-195.070  1.00 58.93           O  
HETATM13853  O   HOH C 715      83.220 -14.529-188.373  1.00 52.24           O  
HETATM13854  O   HOH C 716      87.186 -32.591-197.081  1.00 59.51           O  
HETATM13855  O   HOH C 717      78.696 -26.703-192.742  1.00 56.49           O  
HETATM13856  O   HOH C 718      92.707 -24.300-194.778  1.00 46.41           O  
HETATM13857  O   HOH C 719     118.219 -32.905-215.542  1.00 58.90           O  
HETATM13858  O   HOH C 720      93.223 -26.572-174.817  1.00 42.90           O  
HETATM13859  O   HOH C 721     101.266 -53.611-194.315  1.00 53.18           O  
HETATM13860  O   HOH C 722      97.548 -23.809-196.914  1.00 35.99           O  
HETATM13861  O   HOH C 723     106.384 -28.309-184.408  1.00 59.64           O  
HETATM13862  O   HOH C 724      78.009 -24.539-194.425  1.00 63.45           O  
HETATM13863  O   HOH C 725     103.283  -3.950-179.066  1.00 60.56           O  
HETATM13864  O   HOH C 726     113.510 -39.301-215.627  1.00 49.11           O  
HETATM13865  O   HOH C 727      91.328 -55.322-184.806  1.00 73.98           O  
HETATM13866  O   HOH C 728      95.643 -30.437-212.147  1.00 52.93           O  
HETATM13867  O   HOH C 729      96.883  -4.274-199.724  1.00 32.62           O  
HETATM13868  O   HOH C 730     107.644 -48.137-203.675  1.00 63.02           O  
HETATM13869  O   HOH C 731      87.170 -37.284-205.428  1.00 48.59           O  
HETATM13870  O   HOH C 732      80.224 -31.532-200.057  1.00 67.32           O  
HETATM13871  O   HOH C 733      96.136   4.949-181.966  1.00 59.90           O  
HETATM13872  O   HOH C 734      82.919 -14.074-185.750  1.00 60.37           O  
HETATM13873  O   HOH C 735      70.858 -37.533-201.054  1.00 71.15           O  
HETATM13874  O   HOH C 736     104.243   1.326-201.466  1.00 50.10           O  
HETATM13875  O   HOH C 737     108.884 -16.498-181.835  1.00 64.89           O  
HETATM13876  O   HOH C 738      85.318  -7.645-195.824  1.00 59.33           O  
HETATM13877  O   HOH C 739      85.995 -12.859-185.717  1.00 59.52           O  
HETATM13878  O   HOH C 740      95.467   7.546-196.646  1.00 60.14           O  
HETATM13879  O   HOH C 741      99.026 -47.200-207.911  1.00 60.08           O  
HETATM13880  O   HOH C 742     101.001 -11.231-176.077  1.00 46.12           O  
HETATM13881  O   HOH C 743      98.848 -24.912-199.309  1.00 33.68           O  
HETATM13882  O   HOH C 744     106.400 -33.571-210.386  1.00 48.51           O  
HETATM13883  O   HOH C 745     100.923  -1.585-183.643  1.00 62.53           O  
HETATM13884  O   HOH C 746     104.134 -52.925-197.871  1.00 57.51           O  
HETATM13885  O   HOH C 747      82.403 -30.267-221.105  1.00 54.59           O  
HETATM13886  O   HOH C 748     105.759 -31.785-192.216  1.00 54.50           O  
HETATM13887  O   HOH C 749     104.512 -51.912-205.395  1.00 67.35           O  
HETATM13888  O   HOH C 750     105.194 -34.224-222.694  1.00 65.80           O  
HETATM13889  O   HOH C 751      91.921 -13.461-174.676  1.00 64.69           O  
HETATM13890  O   HOH C 752      85.515  -8.987-180.511  1.00 51.83           O  
HETATM13891  O   HOH C 753      83.208 -32.730-199.434  1.00 57.63           O  
HETATM13892  O   HOH C 754      89.128  -9.131-202.373  1.00 49.84           O  
HETATM13893  O   HOH C 755      63.077  -5.552-189.838  1.00 65.44           O  
HETATM13894  O   HOH C 756      99.008   3.942-179.921  1.00 76.04           O  
HETATM13895  O   HOH C 757      86.836 -30.807-195.500  1.00 60.84           O  
HETATM13896  O   HOH C 758     104.618  -5.115-191.298  1.00 59.10           O  
HETATM13897  O   HOH C 759     106.744 -34.241-185.721  1.00 67.35           O  
HETATM13898  O   HOH C 760      99.593 -19.864-206.318  1.00 37.85           O  
HETATM13899  O   HOH C 761      89.279  -7.351-204.445  1.00 44.70           O  
HETATM13900  O   HOH C 762     109.983 -27.294-189.428  1.00 54.45           O  
HETATM13901  O   HOH D 601     125.151  -7.643-198.055  1.00 73.46           O  
HETATM13902  O   HOH D 602     107.123 -10.575-187.046  1.00 66.92           O  
HETATM13903  O   HOH D 603     109.498 -20.509-212.187  1.00 41.30           O  
HETATM13904  O   HOH D 604     119.029   2.782-207.963  1.00 52.62           O  
HETATM13905  O   HOH D 605     103.045 -22.646-216.295  1.00 46.30           O  
HETATM13906  O   HOH D 606     134.223 -13.904-214.498  1.00 80.90           O  
HETATM13907  O   HOH D 607      86.750  -6.771-242.889  1.00 50.79           O  
HETATM13908  O   HOH D 608      97.997 -12.897-251.404  1.00 48.28           O  
HETATM13909  O   HOH D 609      86.590  -9.617-202.323  1.00 74.82           O  
HETATM13910  O   HOH D 610     107.598  -5.812-246.351  1.00 48.62           O  
HETATM13911  O   HOH D 611     106.510   0.455-243.681  1.00 56.81           O  
HETATM13912  O   HOH D 612      92.882  -1.265-215.794  1.00 58.49           O  
HETATM13913  O   HOH D 613      85.179  -7.669-222.273  1.00 37.02           O  
HETATM13914  O   HOH D 614     115.973   6.794-205.052  1.00 73.25           O  
HETATM13915  O   HOH D 615      97.964 -21.711-220.348  1.00 43.47           O  
HETATM13916  O   HOH D 616      90.736 -28.503-229.690  1.00 63.84           O  
HETATM13917  O   HOH D 617      86.348 -14.374-223.433  1.00 48.69           O  
HETATM13918  O   HOH D 618     110.284 -15.288-206.320  1.00 35.13           O  
HETATM13919  O   HOH D 619     114.286 -11.835-248.611  1.00 50.49           O  
HETATM13920  O   HOH D 620     115.725 -16.823-219.970  1.00 56.52           O  
HETATM13921  O   HOH D 621      83.896 -10.236-252.899  1.00 39.52           O  
HETATM13922  O   HOH D 622     105.064 -10.631-245.730  1.00 42.01           O  
HETATM13923  O   HOH D 623      79.804 -13.364-238.157  1.00 49.31           O  
HETATM13924  O   HOH D 624     111.830 -15.260-213.232  1.00 40.53           O  
HETATM13925  O   HOH D 625      92.389 -25.632-226.169  1.00 34.29           O  
HETATM13926  O   HOH D 626     120.412 -16.040-209.435  1.00 45.66           O  
HETATM13927  O   HOH D 627      82.615 -19.276-216.765  1.00 46.14           O  
HETATM13928  O   HOH D 628     117.337 -17.236-214.802  1.00 44.90           O  
HETATM13929  O   HOH D 629     119.040  -8.497-240.283  1.00 42.38           O  
HETATM13930  O   HOH D 630      84.197 -27.449-208.011  1.00 44.88           O  
HETATM13931  O   HOH D 631      98.101  -8.890-244.089  1.00 33.57           O  
HETATM13932  O   HOH D 632      99.230   5.001-217.965  1.00 35.62           O  
HETATM13933  O   HOH D 633     104.591 -20.911-232.797  1.00 50.47           O  
HETATM13934  O   HOH D 634     107.238 -10.768-231.885  1.00 30.88           O  
HETATM13935  O   HOH D 635     111.045   3.490-222.226  1.00 31.53           O  
HETATM13936  O   HOH D 636      87.871 -19.446-217.036  1.00 35.21           O  
HETATM13937  O   HOH D 637     115.781  -8.740-246.179  1.00 50.29           O  
HETATM13938  O   HOH D 638     128.843  -1.447-217.579  1.00 63.91           O  
HETATM13939  O   HOH D 639     110.705   1.285-191.745  1.00 52.25           O  
HETATM13940  O   HOH D 640      92.468  -7.128-216.018  1.00 30.07           O  
HETATM13941  O   HOH D 641     108.191 -19.166-235.571  1.00 36.59           O  
HETATM13942  O   HOH D 642     103.370  -6.045-205.419  1.00 37.10           O  
HETATM13943  O   HOH D 643     103.121  -0.052-223.211  1.00 31.64           O  
HETATM13944  O   HOH D 644      83.029 -14.926-211.056  1.00 52.07           O  
HETATM13945  O   HOH D 645     112.314 -14.186-230.937  1.00 50.71           O  
HETATM13946  O   HOH D 646      97.019   2.487-225.856  1.00 38.44           O  
HETATM13947  O   HOH D 647      89.311 -12.154-202.290  1.00 48.23           O  
HETATM13948  O   HOH D 648     105.310 -12.648-212.919  1.00 37.71           O  
HETATM13949  O   HOH D 649      88.434 -15.105-230.447  1.00 43.15           O  
HETATM13950  O   HOH D 650      98.008  -0.185-207.908  1.00 37.40           O  
HETATM13951  O   HOH D 651      86.500  -6.962-208.883  1.00 50.62           O  
HETATM13952  O   HOH D 652      96.464 -15.148-227.117  1.00 26.85           O  
HETATM13953  O   HOH D 653     102.533   5.029-210.771  1.00 39.66           O  
HETATM13954  O   HOH D 654     100.578 -26.176-219.597  1.00 43.22           O  
HETATM13955  O   HOH D 655      99.821 -17.790-245.493  1.00 53.53           O  
HETATM13956  O   HOH D 656     100.456 -23.037-216.391  1.00 50.05           O  
HETATM13957  O   HOH D 657     111.502 -17.603-237.532  1.00 50.34           O  
HETATM13958  O   HOH D 658      88.655  -1.374-229.103  1.00 48.67           O  
HETATM13959  O   HOH D 659      89.310  -5.384-249.204  1.00 42.59           O  
HETATM13960  O   HOH D 660      86.784 -14.178-205.438  1.00 43.38           O  
HETATM13961  O   HOH D 661      92.951 -18.810-225.523  1.00 29.68           O  
HETATM13962  O   HOH D 662     115.393   3.579-199.571  1.00 36.20           O  
HETATM13963  O   HOH D 663     120.370  -0.799-226.224  1.00 48.90           O  
HETATM13964  O   HOH D 664     112.159 -16.547-204.415  1.00 60.27           O  
HETATM13965  O   HOH D 665     123.593  -5.936-216.668  1.00 40.62           O  
HETATM13966  O   HOH D 666      93.199  -8.414-202.762  1.00 31.28           O  
HETATM13967  O   HOH D 667     107.013   1.595-194.720  1.00 55.62           O  
HETATM13968  O   HOH D 668     110.196   9.304-214.330  1.00 47.04           O  
HETATM13969  O   HOH D 669      87.222  -4.344-220.785  1.00 42.71           O  
HETATM13970  O   HOH D 670      82.733 -26.201-210.653  1.00 51.16           O  
HETATM13971  O   HOH D 671     105.787   1.345-234.294  1.00 30.47           O  
HETATM13972  O   HOH D 672     100.303 -18.577-208.947  1.00 31.56           O  
HETATM13973  O   HOH D 673      95.505  -0.313-222.391  1.00 34.40           O  
HETATM13974  O   HOH D 674     115.039 -14.384-242.109  1.00 46.28           O  
HETATM13975  O   HOH D 675      92.019 -16.158-235.815  1.00 31.84           O  
HETATM13976  O   HOH D 676      88.996 -12.713-222.340  1.00 37.25           O  
HETATM13977  O   HOH D 677      97.053 -39.630-221.837  1.00 44.64           O  
HETATM13978  O   HOH D 678     107.157 -10.591-216.185  1.00 39.91           O  
HETATM13979  O   HOH D 679     105.876 -10.397-238.204  1.00 29.89           O  
HETATM13980  O   HOH D 680     110.815  -4.559-222.102  1.00 34.09           O  
HETATM13981  O   HOH D 681     116.014 -14.109-203.468  1.00 37.80           O  
HETATM13982  O   HOH D 682      82.418  -9.776-227.745  1.00 47.76           O  
HETATM13983  O   HOH D 683      98.985 -13.073-215.084  1.00 36.00           O  
HETATM13984  O   HOH D 684     118.025  -5.333-243.318  1.00 44.06           O  
HETATM13985  O   HOH D 685     101.999 -15.794-210.780  1.00 33.95           O  
HETATM13986  O   HOH D 686      89.262  -2.620-236.069  1.00 36.73           O  
HETATM13987  O   HOH D 687      80.393  -7.564-221.464  1.00 49.94           O  
HETATM13988  O   HOH D 688     112.991 -25.151-191.341  1.00 63.65           O  
HETATM13989  O   HOH D 689     116.210  -7.752-217.456  1.00 35.70           O  
HETATM13990  O   HOH D 690      80.998 -16.627-210.565  1.00 57.23           O  
HETATM13991  O   HOH D 691     101.659 -14.855-246.366  1.00 39.94           O  
HETATM13992  O   HOH D 692     122.672 -11.083-210.340  1.00 49.51           O  
HETATM13993  O   HOH D 693     111.539   1.550-220.165  1.00 30.74           O  
HETATM13994  O   HOH D 694      91.853  -7.408-204.854  1.00 32.75           O  
HETATM13995  O   HOH D 695      90.318 -18.065-236.852  1.00 38.16           O  
HETATM13996  O   HOH D 696      82.014  -4.943-249.480  1.00 37.37           O  
HETATM13997  O   HOH D 697     124.545  -1.372-214.789  1.00 46.64           O  
HETATM13998  O   HOH D 698      96.020 -24.721-217.377  1.00 55.84           O  
HETATM13999  O   HOH D 699      93.196 -22.487-215.296  1.00 31.37           O  
HETATM14000  O   HOH D 700     123.427  -3.349-207.513  1.00 60.05           O  
HETATM14001  O   HOH D 701     117.184  -4.112-224.355  1.00 37.66           O  
HETATM14002  O   HOH D 702     110.160 -11.830-233.081  1.00 36.69           O  
HETATM14003  O   HOH D 703      96.243 -33.452-224.989  1.00 42.52           O  
HETATM14004  O   HOH D 704     115.303   3.740-240.740  1.00 58.18           O  
HETATM14005  O   HOH D 705     105.324  -0.226-215.697  1.00 30.31           O  
HETATM14006  O   HOH D 706      86.588  -6.772-220.042  1.00 33.97           O  
HETATM14007  O   HOH D 707      92.400 -34.969-216.531  1.00 37.07           O  
HETATM14008  O   HOH D 708     101.998  -8.636-243.537  1.00 32.56           O  
HETATM14009  O   HOH D 709      95.066 -17.760-227.331  1.00 32.29           O  
HETATM14010  O   HOH D 710      85.080 -19.391-217.212  1.00 54.40           O  
HETATM14011  O   HOH D 711     116.553  -6.807-224.889  1.00 33.52           O  
HETATM14012  O   HOH D 712      93.891 -39.579-213.754  1.00 42.29           O  
HETATM14013  O   HOH D 713     122.404   0.669-219.798  1.00 61.30           O  
HETATM14014  O   HOH D 714     108.461 -15.355-244.044  1.00 40.19           O  
HETATM14015  O   HOH D 715     125.945  -2.544-211.295  1.00 65.98           O  
HETATM14016  O   HOH D 716      83.991 -15.598-217.640  1.00 47.08           O  
HETATM14017  O   HOH D 717      83.450  -6.199-247.515  1.00 34.01           O  
HETATM14018  O   HOH D 718     102.962  11.943-220.383  1.00 54.01           O  
HETATM14019  O   HOH D 719     128.983  -1.449-228.217  1.00 68.97           O  
HETATM14020  O   HOH D 720     103.861 -11.004-230.595  1.00 33.38           O  
HETATM14021  O   HOH D 721      99.972   2.335-238.046  1.00 35.35           O  
HETATM14022  O   HOH D 722     102.137 -18.742-242.268  1.00 47.94           O  
HETATM14023  O   HOH D 723      91.794 -25.163-214.933  1.00 38.92           O  
HETATM14024  O   HOH D 724     108.032 -17.202-227.960  1.00 35.20           O  
HETATM14025  O   HOH D 725     118.586 -14.520-201.329  1.00 43.56           O  
HETATM14026  O   HOH D 726     113.943 -18.352-246.686  1.00 47.71           O  
HETATM14027  O   HOH D 727     117.987   0.230-204.459  1.00 38.18           O  
HETATM14028  O   HOH D 728      98.836 -12.322-212.538  1.00 31.03           O  
HETATM14029  O   HOH D 729     107.997 -12.092-241.367  1.00 41.26           O  
HETATM14030  O   HOH D 730     119.689 -17.045-221.107  1.00 44.97           O  
HETATM14031  O   HOH D 731     103.563 -11.506-211.188  1.00 34.18           O  
HETATM14032  O   HOH D 732     107.904 -14.361-223.909  1.00 51.36           O  
HETATM14033  O   HOH D 733      83.626 -10.951-232.226  1.00 54.64           O  
HETATM14034  O   HOH D 734     108.450 -12.528-244.246  1.00 42.32           O  
HETATM14035  O   HOH D 735      90.490  -1.406-243.089  1.00 35.51           O  
HETATM14036  O   HOH D 736     102.785 -13.410-199.537  1.00 36.68           O  
HETATM14037  O   HOH D 737      93.100   0.948-231.731  1.00 59.58           O  
HETATM14038  O   HOH D 738     107.140 -29.214-221.825  1.00 58.15           O  
HETATM14039  O   HOH D 739     106.214 -10.617-229.038  1.00 29.49           O  
HETATM14040  O   HOH D 740     120.483 -11.899-201.369  1.00 49.87           O  
HETATM14041  O   HOH D 741     118.282   3.899-205.581  1.00 54.16           O  
HETATM14042  O   HOH D 742     101.413 -16.022-242.625  1.00 31.10           O  
HETATM14043  O   HOH D 743      82.249 -18.577-211.638  1.00 43.04           O  
HETATM14044  O   HOH D 744      96.601 -23.550-214.026  1.00 56.97           O  
HETATM14045  O   HOH D 745     124.093  -0.420-222.039  1.00 68.78           O  
HETATM14046  O   HOH D 746     121.503   0.711-241.536  1.00 52.26           O  
HETATM14047  O   HOH D 747     115.644   6.784-217.131  1.00 44.63           O  
HETATM14048  O   HOH D 748     123.173   1.564-233.029  1.00 59.33           O  
HETATM14049  O   HOH D 749      96.669   2.037-222.827  1.00 31.85           O  
HETATM14050  O   HOH D 750     103.178  -0.448-243.018  1.00 35.17           O  
HETATM14051  O   HOH D 751     119.017  -2.612-242.525  1.00 42.86           O  
HETATM14052  O   HOH D 752     117.810   7.048-198.814  1.00 53.80           O  
HETATM14053  O   HOH D 753      96.482   0.629-237.399  1.00 59.39           O  
HETATM14054  O   HOH D 754     118.677 -14.811-223.026  1.00 48.94           O  
HETATM14055  O   HOH D 755     110.266  -8.299-247.196  1.00 60.45           O  
HETATM14056  O   HOH D 756      99.997   1.595-208.251  1.00 47.91           O  
HETATM14057  O   HOH D 757      84.615  -2.917-217.358  1.00 44.86           O  
HETATM14058  O   HOH D 758     109.007   8.843-223.194  1.00 47.96           O  
HETATM14059  O   HOH D 759     110.574   7.035-224.131  1.00 51.06           O  
HETATM14060  O   HOH D 760      83.980 -27.702-223.031  1.00 47.66           O  
HETATM14061  O   HOH D 761      82.069 -29.175-214.755  1.00 60.74           O  
HETATM14062  O   HOH D 762      98.511 -16.170-225.311  1.00 29.79           O  
HETATM14063  O   HOH D 763      91.326 -10.124-199.246  1.00 65.14           O  
HETATM14064  O   HOH D 764     122.374  -4.834-204.203  1.00 48.33           O  
HETATM14065  O   HOH D 765     104.562 -14.975-211.148  1.00 33.42           O  
HETATM14066  O   HOH D 766     112.500 -12.918-217.726  1.00 62.11           O  
HETATM14067  O   HOH D 767      85.863  -4.386-233.827  1.00 59.69           O  
HETATM14068  O   HOH D 768     102.331 -21.347-227.454  1.00 46.91           O  
HETATM14069  O   HOH D 769      89.384 -20.060-232.051  1.00 43.66           O  
HETATM14070  O   HOH D 770      99.061 -20.070-222.531  1.00 46.56           O  
HETATM14071  O   HOH D 771     116.050  -1.197-190.894  1.00 56.32           O  
HETATM14072  O   HOH D 772      94.908   1.304-232.982  1.00 42.63           O  
HETATM14073  O   HOH D 773      84.082  -8.635-230.040  1.00 43.70           O  
HETATM14074  O   HOH D 774      82.952 -18.887-237.438  1.00 50.50           O  
HETATM14075  O   HOH D 775     108.099 -19.096-244.993  1.00 50.45           O  
HETATM14076  O   HOH D 776     111.436 -11.204-216.559  1.00 50.35           O  
HETATM14077  O   HOH D 777     124.225  -9.317-210.218  1.00 45.90           O  
HETATM14078  O   HOH D 778     117.672  -7.376-247.744  1.00 63.28           O  
HETATM14079  O   HOH D 779     113.771 -17.091-238.433  1.00 49.27           O  
HETATM14080  O   HOH D 780     112.477   8.404-221.120  1.00 57.34           O  
HETATM14081  O   HOH D 781      75.438  -9.168-236.290  1.00 50.55           O  
HETATM14082  O   HOH D 782     112.716   2.292-190.660  1.00 56.53           O  
HETATM14083  O   HOH D 783     111.329 -17.565-194.026  1.00 40.26           O  
HETATM14084  O   HOH D 784      95.616 -22.767-223.386  1.00 59.16           O  
HETATM14085  O   HOH D 785     100.166   4.139-211.701  1.00 44.24           O  
HETATM14086  O   HOH D 786     109.794 -18.669-242.972  1.00 62.93           O  
HETATM14087  O   HOH D 787      87.724  -3.600-223.486  1.00 41.95           O  
HETATM14088  O   HOH D 788      98.918 -21.425-237.456  1.00 61.08           O  
HETATM14089  O   HOH D 789     125.413  -0.019-224.789  1.00 61.16           O  
HETATM14090  O   HOH D 790      77.055  -9.637-252.267  1.00 70.50           O  
HETATM14091  O   HOH D 791     116.974  11.240-230.461  1.00 69.07           O  
HETATM14092  O   HOH D 792     101.350 -12.940-211.627  1.00 34.55           O  
HETATM14093  O   HOH D 793      93.678  -2.560-212.267  1.00 60.75           O  
HETATM14094  O   HOH D 794     110.043 -12.330-221.188  1.00 67.92           O  
HETATM14095  O   HOH D 795     109.096 -14.449-214.266  1.00 46.56           O  
HETATM14096  O   HOH D 796      94.399 -26.575-221.954  1.00 53.91           O  
HETATM14097  O   HOH D 797      91.661   0.258-239.128  1.00 47.64           O  
HETATM14098  O   HOH D 798      96.621   4.047-220.873  1.00 53.19           O  
HETATM14099  O   HOH D 799     112.859  -7.666-247.056  1.00 62.27           O  
HETATM14100  O   HOH D 800      97.391 -18.952-226.642  1.00 48.46           O  
HETATM14101  O   HOH D 801     109.668  10.791-216.548  1.00 59.49           O  
HETATM14102  O   HOH D 802      95.773  -2.491-214.817  1.00 46.39           O  
HETATM14103  O   HOH D 803     107.954 -11.769-213.850  1.00 40.69           O  
HETATM14104  O   HOH D 804     125.705  -7.614-200.970  1.00 58.97           O  
HETATM14105  O   HOH D 805     110.974 -20.238-236.124  1.00 55.09           O  
HETATM14106  O   HOH D 806      88.888  -3.217-233.261  1.00 52.79           O  
HETATM14107  O   HOH D 807     126.618  -1.523-221.178  1.00 57.85           O  
HETATM14108  O   HOH D 808     109.597 -18.087-184.672  1.00 65.79           O  
HETATM14109  O   HOH D 809      94.720 -25.290-224.275  1.00 57.95           O  
HETATM14110  O   HOH D 810      85.764  -2.476-219.299  1.00 60.92           O  
HETATM14111  O   HOH D 811     109.756 -18.305-225.720  1.00 63.72           O  
HETATM14112  O   HOH D 812      90.102  -0.092-237.015  1.00 50.63           O  
HETATM14113  O   HOH D 813     119.017  -0.868-244.684  1.00 61.51           O  
HETATM14114  O   HOH D 814     105.865 -20.338-245.052  1.00 54.23           O  
HETATM14115  O   HOH D 815      96.350 -26.816-220.225  1.00 48.45           O  
HETATM14116  O   HOH D 816     115.447   6.455-199.582  1.00 47.08           O  
HETATM14117  O   HOH D 817      86.197 -11.333-254.846  1.00 54.23           O  
HETATM14118  O   HOH D 818     105.167   3.407-235.717  1.00 41.61           O  
HETATM14119  O   HOH D 819     114.326 -22.057-202.084  1.00 65.72           O  
HETATM14120  O   HOH D 820      97.818 -25.777-212.591  1.00 59.20           O  
HETATM14121  O   HOH D 821      95.727   0.316-213.719  1.00 60.32           O  
HETATM14122  O   HOH D 822     103.731 -19.361-244.769  1.00 51.55           O  
HETATM14123  O   HOH D 823      84.781 -17.169-215.337  1.00 57.13           O  
HETATM14124  O   HOH D 824      80.393 -14.028-214.327  1.00 48.28           O  
HETATM14125  O   HOH D 825      95.325  -7.103-252.094  1.00 26.70           O  
HETATM14126  O   HOH D 826      95.372   3.908-218.785  1.00 65.87           O  
HETATM14127  O   HOH D 827     113.858 -24.306-200.143  1.00 56.91           O  
HETATM14128  O   HOH D 828      95.802   0.788-209.300  1.00 49.44           O  
HETATM14129  O   HOH D 829      96.603   3.818-216.715  1.00 56.84           O  
HETATM14130  O   HOH D 830     105.184   3.750-195.948  1.00 59.06           O  
HETATM14131  O   HOH D 831      94.461  -0.029-211.255  1.00 50.01           O  
CONECT  21112992                                                                
CONECT  25312992                                                                
CONECT  83912899                                                                
CONECT 342712992                                                                
CONECT 346912992                                                                
CONECT 405513035                                                                
CONECT 514213127                                                                
CONECT 516113127                                                                
CONECT 663913263                                                                
CONECT 668113263                                                                
CONECT 726113171                                                                
CONECT 984913263                                                                
CONECT 989113263                                                                
CONECT1048813306                                                                
CONECT1157013384                                                                
CONECT1158913384                                                                
CONECT128571286112888                                                           
CONECT128581286412871                                                           
CONECT128591287412878                                                           
CONECT128601288112885                                                           
CONECT12861128571286212895                                                      
CONECT12862128611286312866                                                      
CONECT12863128621286412865                                                      
CONECT12864128581286312895                                                      
CONECT1286512863                                                                
CONECT128661286212867                                                           
CONECT128671286612868                                                           
CONECT12868128671286912870                                                      
CONECT1286912868                                                                
CONECT1287012868                                                                
CONECT12871128581287212896                                                      
CONECT12872128711287312875                                                      
CONECT12873128721287412876                                                      
CONECT12874128591287312896                                                      
CONECT1287512872                                                                
CONECT128761287312877                                                           
CONECT1287712876                                                                
CONECT12878128591287912897                                                      
CONECT12879128781288012882                                                      
CONECT12880128791288112883                                                      
CONECT12881128601288012897                                                      
CONECT1288212879                                                                
CONECT128831288012884                                                           
CONECT1288412883                                                                
CONECT12885128601288612898                                                      
CONECT12886128851288712889                                                      
CONECT12887128861288812890                                                      
CONECT12888128571288712898                                                      
CONECT1288912886                                                                
CONECT128901288712891                                                           
CONECT128911289012892                                                           
CONECT12892128911289312894                                                      
CONECT1289312892                                                                
CONECT1289412892                                                                
CONECT12895128611286412899                                                      
CONECT12896128711287412899                                                      
CONECT12897128781288112899                                                      
CONECT12898128851288812899                                                      
CONECT12899  839128951289612897                                                 
CONECT1289912898                                                                
CONECT129001290112907                                                           
CONECT12901129001290212903                                                      
CONECT1290212901                                                                
CONECT129031290112904                                                           
CONECT12904129031290512906                                                      
CONECT1290512904                                                                
CONECT12906129041290712908                                                      
CONECT12907129001290612909                                                      
CONECT129081290612910                                                           
CONECT129091290712911                                                           
CONECT12910129081291112912                                                      
CONECT129111290912910                                                           
CONECT12912129101291312914                                                      
CONECT1291312912                                                                
CONECT12914129121291512916                                                      
CONECT1291512914                                                                
CONECT1291612914                                                                
CONECT12917129181293812939                                                      
CONECT129181291712919                                                           
CONECT12919129181292012926                                                      
CONECT12920129191292112925                                                      
CONECT129211292012922                                                           
CONECT129221292112923                                                           
CONECT12923129221292412927                                                      
CONECT129241292312925                                                           
CONECT12925129201292412938                                                      
CONECT1292612919                                                                
CONECT12927129231292812932                                                      
CONECT129281292712929                                                           
CONECT129291292812930                                                           
CONECT12930129291293112940                                                      
CONECT12931129301293212933                                                      
CONECT129321292712931                                                           
CONECT129331293112941                                                           
CONECT129341293512940                                                           
CONECT12935129341293612937                                                      
CONECT129361293512937                                                           
CONECT129371293512936                                                           
CONECT129381291712925                                                           
CONECT1293912917                                                                
CONECT129401293012934                                                           
CONECT1294112933                                                                
CONECT129421294312944                                                           
CONECT1294312942                                                                
CONECT1294412942129451294712949                                                 
CONECT129451294412946                                                           
CONECT129461294512991                                                           
CONECT129471294412948                                                           
CONECT129481294712991                                                           
CONECT1294912944129501295312991                                                 
CONECT129501294912951                                                           
CONECT129511295012952                                                           
CONECT129521295112991                                                           
CONECT129531294912954                                                           
CONECT129541295312955                                                           
CONECT129551295412991                                                           
CONECT129561295712958                                                           
CONECT1295712956                                                                
CONECT1295812956129591296112963                                                 
CONECT129591295812960                                                           
CONECT1296012959                                                                
CONECT129611295812962                                                           
CONECT1296212961                                                                
CONECT12963129581296412967                                                      
CONECT129641296312965                                                           
CONECT129651296412966                                                           
CONECT1296612965                                                                
CONECT129671296312968                                                           
CONECT129681296712969                                                           
CONECT1296912968                                                                
CONECT129701297112972                                                           
CONECT1297112970                                                                
CONECT1297212970129731297512977                                                 
CONECT129731297212974                                                           
CONECT1297412973                                                                
CONECT129751297212976                                                           
CONECT1297612975                                                                
CONECT12977129721297812981                                                      
CONECT129781297712979                                                           
CONECT129791297812980                                                           
CONECT1298012979                                                                
CONECT129811297712982                                                           
CONECT129821298112983                                                           
CONECT1298312982                                                                
CONECT129841298512986                                                           
CONECT1298512984                                                                
CONECT12986129841298712988                                                      
CONECT1298712986                                                                
CONECT129881298612989                                                           
CONECT1298912988                                                                
CONECT1299112946129481294912952                                                 
CONECT1299112955134001340213516                                                 
CONECT12992  211  253 3427 3469                                                 
CONECT129931299713024                                                           
CONECT129941300013007                                                           
CONECT129951301013014                                                           
CONECT129961301713021                                                           
CONECT12997129931299813031                                                      
CONECT12998129971299913002                                                      
CONECT12999129981300013001                                                      
CONECT13000129941299913031                                                      
CONECT1300112999                                                                
CONECT130021299813003                                                           
CONECT130031300213004                                                           
CONECT13004130031300513006                                                      
CONECT1300513004                                                                
CONECT1300613004                                                                
CONECT13007129941300813032                                                      
CONECT13008130071300913011                                                      
CONECT13009130081301013012                                                      
CONECT13010129951300913032                                                      
CONECT1301113008                                                                
CONECT130121300913013                                                           
CONECT1301313012                                                                
CONECT13014129951301513033                                                      
CONECT13015130141301613018                                                      
CONECT13016130151301713019                                                      
CONECT13017129961301613033                                                      
CONECT1301813015                                                                
CONECT130191301613020                                                           
CONECT1302013019                                                                
CONECT13021129961302213034                                                      
CONECT13022130211302313025                                                      
CONECT13023130221302413026                                                      
CONECT13024129931302313034                                                      
CONECT1302513022                                                                
CONECT130261302313027                                                           
CONECT130271302613028                                                           
CONECT13028130271302913030                                                      
CONECT1302913028                                                                
CONECT1303013028                                                                
CONECT13031129971300013035                                                      
CONECT13032130071301013035                                                      
CONECT13033130141301713035                                                      
CONECT13034130211302413035                                                      
CONECT13035 4055130311303213033                                                 
CONECT1303513034                                                                
CONECT130361303713043                                                           
CONECT13037130361303813039                                                      
CONECT1303813037                                                                
CONECT130391303713040                                                           
CONECT13040130391304113042                                                      
CONECT1304113040                                                                
CONECT13042130401304313044                                                      
CONECT13043130361304213045                                                      
CONECT130441304213046                                                           
CONECT130451304313047                                                           
CONECT13046130441304713048                                                      
CONECT130471304513046                                                           
CONECT13048130461304913050                                                      
CONECT1304913048                                                                
CONECT13050130481305113052                                                      
CONECT1305113050                                                                
CONECT1305213050                                                                
CONECT13053130541307413075                                                      
CONECT130541305313055                                                           
CONECT13055130541305613062                                                      
CONECT13056130551305713061                                                      
CONECT130571305613058                                                           
CONECT130581305713059                                                           
CONECT13059130581306013063                                                      
CONECT130601305913061                                                           
CONECT13061130561306013074                                                      
CONECT1306213055                                                                
CONECT13063130591306413068                                                      
CONECT130641306313065                                                           
CONECT130651306413066                                                           
CONECT13066130651306713076                                                      
CONECT13067130661306813069                                                      
CONECT130681306313067                                                           
CONECT130691306713077                                                           
CONECT130701307113076                                                           
CONECT13071130701307213073                                                      
CONECT130721307113073                                                           
CONECT130731307113072                                                           
CONECT130741305313061                                                           
CONECT1307513053                                                                
CONECT130761306613070                                                           
CONECT1307713069                                                                
CONECT130781307913080                                                           
CONECT1307913078                                                                
CONECT1308013078130811308313085                                                 
CONECT130811308013082                                                           
CONECT130821308113127                                                           
CONECT130831308013084                                                           
CONECT130841308313127                                                           
CONECT1308513080130861308913127                                                 
CONECT130861308513087                                                           
CONECT130871308613088                                                           
CONECT130881308713127                                                           
CONECT130891308513090                                                           
CONECT130901308913091                                                           
CONECT130911309013127                                                           
CONECT130921309313094                                                           
CONECT1309313092                                                                
CONECT1309413092130951309713099                                                 
CONECT130951309413096                                                           
CONECT1309613095                                                                
CONECT130971309413098                                                           
CONECT1309813097                                                                
CONECT13099130941310013103                                                      
CONECT131001309913101                                                           
CONECT131011310013102                                                           
CONECT1310213101                                                                
CONECT131031309913104                                                           
CONECT131041310313105                                                           
CONECT1310513104                                                                
CONECT131061310713108                                                           
CONECT1310713106                                                                
CONECT1310813106131091311113113                                                 
CONECT131091310813110                                                           
CONECT1311013109                                                                
CONECT131111310813112                                                           
CONECT1311213111                                                                
CONECT13113131081311413117                                                      
CONECT131141311313115                                                           
CONECT131151311413116                                                           
CONECT1311613115                                                                
CONECT131171311313118                                                           
CONECT131181311713119                                                           
CONECT1311913118                                                                
CONECT131201312113122                                                           
CONECT1312113120                                                                
CONECT13122131201312313124                                                      
CONECT1312313122                                                                
CONECT131241312213125                                                           
CONECT1312513124                                                                
CONECT13127 5142 51611308213084                                                 
CONECT13127130851308813091                                                      
CONECT1312813218132201322113224                                                 
CONECT1312813227136341374213871                                                 
CONECT1312813894                                                                
CONECT131291313313160                                                           
CONECT131301313613143                                                           
CONECT131311314613150                                                           
CONECT131321315313157                                                           
CONECT13133131291313413167                                                      
CONECT13134131331313513138                                                      
CONECT13135131341313613137                                                      
CONECT13136131301313513167                                                      
CONECT1313713135                                                                
CONECT131381313413139                                                           
CONECT131391313813140                                                           
CONECT13140131391314113142                                                      
CONECT1314113140                                                                
CONECT1314213140                                                                
CONECT13143131301314413168                                                      
CONECT13144131431314513147                                                      
CONECT13145131441314613148                                                      
CONECT13146131311314513168                                                      
CONECT1314713144                                                                
CONECT131481314513149                                                           
CONECT1314913148                                                                
CONECT13150131311315113169                                                      
CONECT13151131501315213154                                                      
CONECT13152131511315313155                                                      
CONECT13153131321315213169                                                      
CONECT1315413151                                                                
CONECT131551315213156                                                           
CONECT1315613155                                                                
CONECT13157131321315813170                                                      
CONECT13158131571315913161                                                      
CONECT13159131581316013162                                                      
CONECT13160131291315913170                                                      
CONECT1316113158                                                                
CONECT131621315913163                                                           
CONECT131631316213164                                                           
CONECT13164131631316513166                                                      
CONECT1316513164                                                                
CONECT1316613164                                                                
CONECT13167131331313613171                                                      
CONECT13168131431314613171                                                      
CONECT13169131501315313171                                                      
CONECT13170131571316013171                                                      
CONECT13171 7261131671316813169                                                 
CONECT1317113170                                                                
CONECT131721317313179                                                           
CONECT13173131721317413175                                                      
CONECT1317413173                                                                
CONECT131751317313176                                                           
CONECT13176131751317713178                                                      
CONECT1317713176                                                                
CONECT13178131761317913180                                                      
CONECT13179131721317813181                                                      
CONECT131801317813182                                                           
CONECT131811317913183                                                           
CONECT13182131801318313184                                                      
CONECT131831318113182                                                           
CONECT13184131821318513186                                                      
CONECT1318513184                                                                
CONECT13186131841318713188                                                      
CONECT1318713186                                                                
CONECT1318813186                                                                
CONECT13189131901321013211                                                      
CONECT131901318913191                                                           
CONECT13191131901319213198                                                      
CONECT13192131911319313197                                                      
CONECT131931319213194                                                           
CONECT131941319313195                                                           
CONECT13195131941319613199                                                      
CONECT131961319513197                                                           
CONECT13197131921319613210                                                      
CONECT1319813191                                                                
CONECT13199131951320013204                                                      
CONECT132001319913201                                                           
CONECT132011320013202                                                           
CONECT13202132011320313212                                                      
CONECT13203132021320413205                                                      
CONECT132041319913203                                                           
CONECT132051320313213                                                           
CONECT132061320713212                                                           
CONECT13207132061320813209                                                      
CONECT132081320713209                                                           
CONECT132091320713208                                                           
CONECT132101318913197                                                           
CONECT1321113189                                                                
CONECT132121320213206                                                           
CONECT1321313205                                                                
CONECT132141321513216                                                           
CONECT1321513214                                                                
CONECT1321613214132171321913221                                                 
CONECT132171321613218                                                           
CONECT132181312813217                                                           
CONECT132191321613220                                                           
CONECT132201312813219                                                           
CONECT1322113128132161322213225                                                 
CONECT132221322113223                                                           
CONECT132231322213224                                                           
CONECT132241312813223                                                           
CONECT132251322113226                                                           
CONECT132261322513227                                                           
CONECT132271312813226                                                           
CONECT132281322913230                                                           
CONECT1322913228                                                                
CONECT1323013228132311323313235                                                 
CONECT132311323013232                                                           
CONECT1323213231                                                                
CONECT132331323013234                                                           
CONECT1323413233                                                                
CONECT13235132301323613239                                                      
CONECT132361323513237                                                           
CONECT132371323613238                                                           
CONECT1323813237                                                                
CONECT132391323513240                                                           
CONECT132401323913241                                                           
CONECT1324113240                                                                
CONECT132421324313244                                                           
CONECT1324313242                                                                
CONECT1324413242132451324713249                                                 
CONECT132451324413246                                                           
CONECT1324613245                                                                
CONECT132471324413248                                                           
CONECT1324813247                                                                
CONECT13249132441325013253                                                      
CONECT132501324913251                                                           
CONECT132511325013252                                                           
CONECT1325213251                                                                
CONECT132531324913254                                                           
CONECT132541325313255                                                           
CONECT1325513254                                                                
CONECT132561325713258                                                           
CONECT1325713256                                                                
CONECT13258132561325913260                                                      
CONECT1325913258                                                                
CONECT132601325813261                                                           
CONECT1326113260                                                                
CONECT13263 6639 6681 9849 9891                                                 
CONECT132641326813295                                                           
CONECT132651327113278                                                           
CONECT132661328113285                                                           
CONECT132671328813292                                                           
CONECT13268132641326913302                                                      
CONECT13269132681327013273                                                      
CONECT13270132691327113272                                                      
CONECT13271132651327013302                                                      
CONECT1327213270                                                                
CONECT132731326913274                                                           
CONECT132741327313275                                                           
CONECT13275132741327613277                                                      
CONECT1327613275                                                                
CONECT1327713275                                                                
CONECT13278132651327913303                                                      
CONECT13279132781328013282                                                      
CONECT13280132791328113283                                                      
CONECT13281132661328013303                                                      
CONECT1328213279                                                                
CONECT132831328013284                                                           
CONECT1328413283                                                                
CONECT13285132661328613304                                                      
CONECT13286132851328713289                                                      
CONECT13287132861328813290                                                      
CONECT13288132671328713304                                                      
CONECT1328913286                                                                
CONECT132901328713291                                                           
CONECT1329113290                                                                
CONECT13292132671329313305                                                      
CONECT13293132921329413296                                                      
CONECT13294132931329513297                                                      
CONECT13295132641329413305                                                      
CONECT1329613293                                                                
CONECT132971329413298                                                           
CONECT132981329713299                                                           
CONECT13299132981330013301                                                      
CONECT1330013299                                                                
CONECT1330113299                                                                
CONECT13302132681327113306                                                      
CONECT13303132781328113306                                                      
CONECT13304132851328813306                                                      
CONECT13305132921329513306                                                      
CONECT1330610488133021330313304                                                 
CONECT1330613305                                                                
CONECT133071330813314                                                           
CONECT13308133071330913310                                                      
CONECT1330913308                                                                
CONECT133101330813311                                                           
CONECT13311133101331213313                                                      
CONECT1331213311                                                                
CONECT13313133111331413315                                                      
CONECT13314133071331313316                                                      
CONECT133151331313317                                                           
CONECT133161331413318                                                           
CONECT13317133151331813319                                                      
CONECT133181331613317                                                           
CONECT13319133171332013321                                                      
CONECT1332013319                                                                
CONECT13321133191332213323                                                      
CONECT1332213321                                                                
CONECT1332313321                                                                
CONECT13324133251334513346                                                      
CONECT133251332413326                                                           
CONECT13326133251332713333                                                      
CONECT13327133261332813332                                                      
CONECT133281332713329                                                           
CONECT133291332813330                                                           
CONECT13330133291333113334                                                      
CONECT133311333013332                                                           
CONECT13332133271333113345                                                      
CONECT1333313326                                                                
CONECT13334133301333513339                                                      
CONECT133351333413336                                                           
CONECT133361333513337                                                           
CONECT13337133361333813347                                                      
CONECT13338133371333913340                                                      
CONECT133391333413338                                                           
CONECT133401333813348                                                           
CONECT133411334213347                                                           
CONECT13342133411334313344                                                      
CONECT133431334213344                                                           
CONECT133441334213343                                                           
CONECT133451332413332                                                           
CONECT1334613324                                                                
CONECT133471333713341                                                           
CONECT1334813340                                                                
CONECT133491335013351                                                           
CONECT1335013349                                                                
CONECT1335113349133521335413356                                                 
CONECT133521335113353                                                           
CONECT133531335213384                                                           
CONECT133541335113355                                                           
CONECT133551335413384                                                           
CONECT1335613351133571336013384                                                 
CONECT133571335613358                                                           
CONECT133581335713359                                                           
CONECT133591335813384                                                           
CONECT133601335613361                                                           
CONECT133611336013362                                                           
CONECT133621336113384                                                           
CONECT133631336413365                                                           
CONECT1336413363                                                                
CONECT1336513363133661336813370                                                 
CONECT133661336513367                                                           
CONECT1336713366                                                                
CONECT133681336513369                                                           
CONECT1336913368                                                                
CONECT13370133651337113374                                                      
CONECT133711337013372                                                           
CONECT133721337113373                                                           
CONECT1337313372                                                                
CONECT133741337013375                                                           
CONECT133751337413376                                                           
CONECT1337613375                                                                
CONECT133771337813379                                                           
CONECT1337813377                                                                
CONECT13379133771338013381                                                      
CONECT1338013379                                                                
CONECT133811337913382                                                           
CONECT1338213381                                                                
CONECT1338411570115891335313355                                                 
CONECT1338413356133591336214082                                                 
CONECT1340012991                                                                
CONECT1340212991                                                                
CONECT1351612991                                                                
CONECT1363413128                                                                
CONECT1374213128                                                                
CONECT1387113128                                                                
CONECT1389413128                                                                
CONECT1408213384                                                                
MASTER      771    0   37   72   72    0   84    614092    4  557  136          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.