CNRS Nantes University US2B US2B
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***  OXIDOREDUCTASE/INHIBITOR 05-JUL-19 6PP1  ***

elNémo ID: 2412161500103475194

Job options:

ID        	=	 2412161500103475194
JOBID     	=	 OXIDOREDUCTASE/INHIBITOR 05-JUL-19 6PP1
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    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