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***  soumi_FcFrag_Bound_BDomain_Rev00  ***

elNémo ID: 20102822413718024

Job options:

ID        	=	 20102822413718024
JOBID     	=	 soumi_FcFrag_Bound_BDomain_Rev00
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -800
DQMAX     	=	 800
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER soumi_FcFrag_Bound_BDomain_Rev00

HEADER    TRANSCRIPTION                           06-DEC-16   5U4Y              
TITLE     IGG FC BOUND TO 3 HELIX OF THE B-DOMAIN FROM PROTEIN A                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IGG1 FC;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 261-472;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN A;                        
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 101-155;                                      
COMPND  10 SYNONYM: IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A;             
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DKFZP686C11235;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  10 ORGANISM_TAXID: 1280;                                                
SOURCE  11 GENE: SPA;                                                           
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IGG1, FC, HELIX, B-DOMAIN, PROTEIN A, TRANSCRIPTION                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.H.ULTSCH,C.EIGENBROT                                                
REVDAT   3   29-JUL-20 5U4Y    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   08-NOV-17 5U4Y    1       JRNL                                     
REVDAT   1   17-MAY-17 5U4Y    0                                                
JRNL        AUTH   M.ULTSCH,A.BRAISTED,H.R.MAUN,C.EIGENBROT                     
JRNL        TITL   3-2-1: STRUCTURAL INSIGHTS FROM STEPWISE SHRINKAGE OF A      
JRNL        TITL 2 THREE-HELIX FC-BINDING DOMAIN TO A SINGLE HELIX.             
JRNL        REF    PROTEIN ENG. DES. SEL.        V.  30   619 2017              
JRNL        REFN                   ESSN 1741-0134                               
JRNL        PMID   28475752                                                     
JRNL        DOI    10.1093/PROTEIN/GZX029                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.DEISENHOFER                                                
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF A HUMAN FC  
REMARK   1  TITL 2 FRAGMENT AND ITS COMPLEX WITH FRAGMENT B OF PROTEIN A FROM   
REMARK   1  TITL 3 STAPHYLOCOCCUS AUREUS AT 2.9- AND 2.8-A RESOLUTION.          
REMARK   1  REF    BIOCHEMISTRY                  V.  20  2361 1981              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   7236608                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25214                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1202                            
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 41.0750 -  5.1957    0.92     2791   143  0.1690 0.1825        
REMARK   3     2  5.1957 -  4.1253    0.95     2766   128  0.1438 0.1846        
REMARK   3     3  4.1253 -  3.6041    0.97     2766   130  0.1851 0.1967        
REMARK   3     4  3.6041 -  3.2748    0.97     2735   164  0.2097 0.2582        
REMARK   3     5  3.2748 -  3.0401    0.96     2701   119  0.2273 0.2823        
REMARK   3     6  3.0401 -  2.8609    0.94     2653   135  0.2371 0.2845        
REMARK   3     7  2.8609 -  2.7177    0.93     2611   119  0.2397 0.3001        
REMARK   3     8  2.7177 -  2.5994    0.90     2529   131  0.2407 0.3023        
REMARK   3     9  2.5994 -  2.5000    0.88     2460   133  0.2590 0.3238        
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.90                          
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      :  0.005           4534                                  
REMARK   3   ANGLE     :  0.962           6183                                  
REMARK   3   CHIRALITY :  0.032            716                                  
REMARK   3   PLANARITY :  0.005            780                                  
REMARK   3   DIHEDRAL  : 16.025           1751                                  
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 8:237 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4000  40.1624  25.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2398 T22:   0.2866                                     
REMARK   3      T33:   0.3594 T12:  -0.0409                                     
REMARK   3      T13:   0.0371 T23:  -0.1138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5964 L22:   2.0844                                     
REMARK   3      L33:   0.6643 L12:   0.2231                                     
REMARK   3      L13:   0.0653 L23:   0.5050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0630 S12:   0.0746 S13:  -0.4103                       
REMARK   3      S21:  -0.0699 S22:   0.2080 S23:  -0.4705                       
REMARK   3      S31:   0.0702 S32:   0.1515 S33:   0.0407                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND ( RESID 235:446 OR RESID 501:507 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4968  55.5914  44.1080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2152 T22:   0.1856                                     
REMARK   3      T33:   0.2691 T12:   0.0491                                     
REMARK   3      T13:  -0.0387 T23:  -0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7397 L22:   0.5538                                     
REMARK   3      L33:   0.6142 L12:  -0.4873                                     
REMARK   3      L13:   0.4171 L23:   0.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0202 S12:  -0.0889 S13:  -0.3865                       
REMARK   3      S21:   0.1185 S22:   0.1680 S23:  -0.1110                       
REMARK   3      S31:   0.1095 S32:  -0.0269 S33:   0.0365                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 103:155 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6122  29.6218  19.0723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3711 T22:   0.3681                                     
REMARK   3      T33:   0.3766 T12:  -0.1434                                     
REMARK   3      T13:   0.0159 T23:  -0.0924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4255 L22:   0.2799                                     
REMARK   3      L33:   0.4384 L12:   0.3139                                     
REMARK   3      L13:   0.2398 L23:   0.0539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0124 S12:   0.1405 S13:  -0.4268                       
REMARK   3      S21:  -0.0775 S22:   0.1072 S23:  -0.1896                       
REMARK   3      S31:   0.0244 S32:  -0.0357 S33:   0.0009                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 101:155 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8872  76.9236  48.0659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3374 T22:   0.3441                                     
REMARK   3      T33:   0.4525 T12:   0.0548                                     
REMARK   3      T13:  -0.1635 T23:  -0.1360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2100 L22:   0.6776                                     
REMARK   3      L33:   0.3860 L12:  -0.1061                                     
REMARK   3      L13:   0.5750 L23:   0.2197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2115 S12:  -0.4831 S13:   0.1732                       
REMARK   3      S21:   0.4062 S22:   0.2484 S23:  -0.4933                       
REMARK   3      S31:  -0.0125 S32:   0.1017 S33:  -0.0458                       
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 5U4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225279.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 1.3.0                     
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.499                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200   FOR THE DATA SET  : 30.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1FC1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD.                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3400, 0.1M MAGNESIUM ACETATE,    
REMARK 280  0.1 M HEPES PH 7.0. PROTEIN CONCENTRATION 5MG/ML., VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       52.97500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.13000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.97500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.13000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 38.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 605  LIES ON A SPECIAL POSITION.                          
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     LEU A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     SER A   444                                                      
REMARK 465     PRO A   445                                                      
REMARK 465     GLY A   446                                                      
REMARK 465     MET C   101                                                      
REMARK 465     LYS C   102                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   296     OE2  GLU C   113     4556     2.17            
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    ASN A 297     -174.45    -66.53                                   
REMARK 500    SER A 298       58.19    -92.65                                   
REMARK 500    ASN A 325      136.34   -171.33                                   
REMARK 500    ALA A 327       35.20    -82.37                                   
REMARK 500    ASN B 297       37.10    -84.69                                   
REMARK 500    ASN B 434       14.17     59.85                                   
REMARK 500    LYS D 102       -1.67     55.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L6X   RELATED DB: PDB                                   
REMARK 900 CONTAINS THE SAME COMPLEX BUT IN A DIFFERENT SPACE GROUP.            
REMARK 900 RELATED ID: 5U52   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5U66   RELATED DB: PDB                                   
DBREF  5U4Y A  235   446  UNP    Q6MZV7   Q6MZV7_HUMAN   261    472             
DBREF  5U4Y B  235   446  UNP    Q6MZV7   Q6MZV7_HUMAN   261    472             
DBREF  5U4Y C  101   155  PDB    5U4Y     5U4Y           101    155             
DBREF  5U4Y D  101   155  PDB    5U4Y     5U4Y           101    155             
SEQRES   1 A  212  LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO          
SEQRES   2 A  212  LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR          
SEQRES   3 A  212  CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL          
SEQRES   4 A  212  LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN          
SEQRES   5 A  212  ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR          
SEQRES   6 A  212  TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP          
SEQRES   7 A  212  TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN          
SEQRES   8 A  212  LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER LYS          
SEQRES   9 A  212  ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU          
SEQRES  10 A  212  PRO PRO SER ARG GLU GLU MET THR LYS ASN GLN VAL SER          
SEQRES  11 A  212  LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE          
SEQRES  12 A  212  ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN          
SEQRES  13 A  212  TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER          
SEQRES  14 A  212  PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG          
SEQRES  15 A  212  TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS          
SEQRES  16 A  212  GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER          
SEQRES  17 A  212  LEU SER PRO GLY                                              
SEQRES   1 B  212  LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO          
SEQRES   2 B  212  LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR          
SEQRES   3 B  212  CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL          
SEQRES   4 B  212  LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN          
SEQRES   5 B  212  ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR          
SEQRES   6 B  212  TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP          
SEQRES   7 B  212  TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN          
SEQRES   8 B  212  LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER LYS          
SEQRES   9 B  212  ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU          
SEQRES  10 B  212  PRO PRO SER ARG GLU GLU MET THR LYS ASN GLN VAL SER          
SEQRES  11 B  212  LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE          
SEQRES  12 B  212  ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN          
SEQRES  13 B  212  TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER          
SEQRES  14 B  212  PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG          
SEQRES  15 B  212  TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS          
SEQRES  16 B  212  GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER          
SEQRES  17 B  212  LEU SER PRO GLY                                              
SEQRES   1 C   55  MET LYS PHE ASN LYS GLU GLN GLN ASN ALA PHE TYR GLU          
SEQRES   2 C   55  ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU GLN ARG ASN          
SEQRES   3 C   55  ALA PHE ILE GLN SER LEU LYS ASP ASP PRO SER GLN SER          
SEQRES   4 C   55  ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA          
SEQRES   5 C   55  GLN ALA PRO                                                  
SEQRES   1 D   55  MET LYS PHE ASN LYS GLU GLN GLN ASN ALA PHE TYR GLU          
SEQRES   2 D   55  ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU GLN ARG ASN          
SEQRES   3 D   55  ALA PHE ILE GLN SER LEU LYS ASP ASP PRO SER GLN SER          
SEQRES   4 D   55  ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA          
SEQRES   5 D   55  GLN ALA PRO                                                  
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    MAN  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    NAG  E   5      14                                                       
HET    GAL  E   6      11                                                       
HET    MAN  E   7      11                                                       
HET    FUC  E   8      10                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    MAN  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    NAG  F   5      14                                                       
HET    MAN  F   6      11                                                       
HET    FUC  F   7      10                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   5  MAN    6(C6 H12 O6)                                                 
FORMUL   5  GAL    C6 H12 O6                                                    
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   7  HOH   *130(H2 O)                                                    
HELIX    1 AA1 LYS A  246  MET A  252  1                                   7    
HELIX    2 AA2 LEU A  309  ASN A  315  1                                   7    
HELIX    3 AA3 SER A  354  LYS A  360  5                                   7    
HELIX    4 AA4 LYS A  414  GLN A  419  1                                   6    
HELIX    5 AA5 LEU A  432  TYR A  436  5                                   5    
HELIX    6 AA6 LYS B  246  MET B  252  1                                   7    
HELIX    7 AA7 LEU B  309  ASN B  315  1                                   7    
HELIX    8 AA8 SER B  354  LYS B  360  5                                   7    
HELIX    9 AA9 LYS B  414  GLN B  419  1                                   6    
HELIX   10 AB1 LEU B  432  ASN B  434  5                                   3    
HELIX   11 AB2 ASN C  104  LEU C  117  1                                  14    
HELIX   12 AB3 ASN C  121  ASP C  135  1                                  15    
HELIX   13 AB4 GLN C  138  GLN C  153  1                                  16    
HELIX   14 AB5 ASN D  104  LEU D  117  1                                  14    
HELIX   15 AB6 ASN D  121  ASP D  135  1                                  15    
HELIX   16 AB7 GLN D  138  GLN D  153  1                                  16    
SHEET    1 AA1 4 SER A 239  PHE A 243  0                                        
SHEET    2 AA1 4 GLU A 258  VAL A 266 -1  O  VAL A 262   N  PHE A 241           
SHEET    3 AA1 4 TYR A 300  THR A 307 -1  O  LEU A 306   N  VAL A 259           
SHEET    4 AA1 4 LYS A 288  THR A 289 -1  N  LYS A 288   O  VAL A 305           
SHEET    1 AA2 4 SER A 239  PHE A 243  0                                        
SHEET    2 AA2 4 GLU A 258  VAL A 266 -1  O  VAL A 262   N  PHE A 241           
SHEET    3 AA2 4 TYR A 300  THR A 307 -1  O  LEU A 306   N  VAL A 259           
SHEET    4 AA2 4 GLU A 293  GLU A 294 -1  N  GLU A 293   O  ARG A 301           
SHEET    1 AA3 4 VAL A 282  VAL A 284  0                                        
SHEET    2 AA3 4 LYS A 274  VAL A 279 -1  N  VAL A 279   O  VAL A 282           
SHEET    3 AA3 4 TYR A 319  SER A 324 -1  O  LYS A 320   N  TYR A 278           
SHEET    4 AA3 4 ILE A 332  ILE A 336 -1  O  ILE A 336   N  TYR A 319           
SHEET    1 AA4 4 GLN A 347  LEU A 351  0                                        
SHEET    2 AA4 4 GLN A 362  PHE A 372 -1  O  THR A 366   N  LEU A 351           
SHEET    3 AA4 4 PHE A 404  ASP A 413 -1  O  LEU A 410   N  LEU A 365           
SHEET    4 AA4 4 TYR A 391  THR A 393 -1  N  LYS A 392   O  LYS A 409           
SHEET    1 AA5 4 GLN A 347  LEU A 351  0                                        
SHEET    2 AA5 4 GLN A 362  PHE A 372 -1  O  THR A 366   N  LEU A 351           
SHEET    3 AA5 4 PHE A 404  ASP A 413 -1  O  LEU A 410   N  LEU A 365           
SHEET    4 AA5 4 VAL A 397  LEU A 398 -1  N  VAL A 397   O  PHE A 405           
SHEET    1 AA6 4 GLN A 386  GLU A 388  0                                        
SHEET    2 AA6 4 ALA A 378  SER A 383 -1  N  SER A 383   O  GLN A 386           
SHEET    3 AA6 4 PHE A 423  MET A 428 -1  O  SER A 426   N  GLU A 380           
SHEET    4 AA6 4 THR A 437  LEU A 441 -1  O  LYS A 439   N  CYS A 425           
SHEET    1 AA7 4 SER B 239  PHE B 243  0                                        
SHEET    2 AA7 4 GLU B 258  VAL B 266 -1  O  VAL B 262   N  PHE B 241           
SHEET    3 AA7 4 TYR B 300  THR B 307 -1  O  SER B 304   N  CYS B 261           
SHEET    4 AA7 4 LYS B 288  THR B 289 -1  N  LYS B 288   O  VAL B 305           
SHEET    1 AA8 4 SER B 239  PHE B 243  0                                        
SHEET    2 AA8 4 GLU B 258  VAL B 266 -1  O  VAL B 262   N  PHE B 241           
SHEET    3 AA8 4 TYR B 300  THR B 307 -1  O  SER B 304   N  CYS B 261           
SHEET    4 AA8 4 GLU B 293  GLU B 294 -1  N  GLU B 293   O  ARG B 301           
SHEET    1 AA9 4 VAL B 282  VAL B 284  0                                        
SHEET    2 AA9 4 LYS B 274  VAL B 279 -1  N  VAL B 279   O  VAL B 282           
SHEET    3 AA9 4 TYR B 319  SER B 324 -1  O  LYS B 320   N  TYR B 278           
SHEET    4 AA9 4 ILE B 332  ILE B 336 -1  O  ILE B 332   N  VAL B 323           
SHEET    1 AB1 4 GLN B 347  LEU B 351  0                                        
SHEET    2 AB1 4 GLN B 362  PHE B 372 -1  O  LEU B 368   N  TYR B 349           
SHEET    3 AB1 4 PHE B 404  ASP B 413 -1  O  LEU B 410   N  LEU B 365           
SHEET    4 AB1 4 TYR B 391  THR B 393 -1  N  LYS B 392   O  LYS B 409           
SHEET    1 AB2 4 GLN B 347  LEU B 351  0                                        
SHEET    2 AB2 4 GLN B 362  PHE B 372 -1  O  LEU B 368   N  TYR B 349           
SHEET    3 AB2 4 PHE B 404  ASP B 413 -1  O  LEU B 410   N  LEU B 365           
SHEET    4 AB2 4 VAL B 397  LEU B 398 -1  N  VAL B 397   O  PHE B 405           
SHEET    1 AB3 4 GLN B 386  GLU B 388  0                                        
SHEET    2 AB3 4 ALA B 378  SER B 383 -1  N  SER B 383   O  GLN B 386           
SHEET    3 AB3 4 PHE B 423  MET B 428 -1  O  SER B 426   N  GLU B 380           
SHEET    4 AB3 4 TYR B 436  LEU B 441 -1  O  LYS B 439   N  CYS B 425           
SSBOND   1 CYS A  261    CYS A  321                          1555   1555  2.04  
SSBOND   2 CYS A  367    CYS A  425                          1555   1555  2.03  
SSBOND   3 CYS B  261    CYS B  321                          1555   1555  2.03  
SSBOND   4 CYS B  367    CYS B  425                          1555   1555  2.03  
LINK         ND2 ASN A 297                 C1  NAG E   1     1555   1555  1.46  
LINK         ND2 ASN B 297                 C1  NAG F   1     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.48  
LINK         O6  NAG E   1                 C1  FUC E   8     1555   1555  1.45  
LINK         O4  NAG E   2                 C1  MAN E   3     1555   1555  1.47  
LINK         O6  MAN E   3                 C1  MAN E   4     1555   1555  1.44  
LINK         O3  MAN E   3                 C1  MAN E   7     1555   1555  1.45  
LINK         O2  MAN E   4                 C1  NAG E   5     1555   1555  1.44  
LINK         O4  NAG E   5                 C1  GAL E   6     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.46  
LINK         O6  NAG F   1                 C1  FUC F   7     1555   1555  1.46  
LINK         O4  NAG F   2                 C1  MAN F   3     1555   1555  1.47  
LINK         O6  MAN F   3                 C1  MAN F   4     1555   1555  1.45  
LINK         O3  MAN F   3                 C1  MAN F   6     1555   1555  1.44  
LINK         O2  MAN F   4                 C1  NAG F   5     1555   1555  1.43  
CISPEP   1 TYR A  373    PRO A  374          0        -3.60                     
CISPEP   2 TYR B  373    PRO B  374          0        -3.04                     
CRYST1  105.950  152.260   46.600  90.00  90.00  90.00 P 21 21 2     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      0.009438  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006568  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021459        0.00000                         
ATOM      1  N   GLY A 237      25.242  23.386  35.215  1.00 94.47           N  
ANISOU    1  N   GLY A 237     9071   9470  17353   1290  -2227  -2220       N  
ATOM      2  CA  GLY A 237      25.136  23.158  33.784  1.00100.31           C  
ANISOU    2  CA  GLY A 237     9702  10256  18155   1212  -1945  -2352       C  
ATOM      3  C   GLY A 237      24.187  24.122  33.097  1.00105.68           C  
ANISOU    3  C   GLY A 237    10439  11087  18627   1128  -1719  -2335       C  
ATOM      4  O   GLY A 237      24.296  25.338  33.256  1.00105.72           O  
ANISOU    4  O   GLY A 237    10437  11181  18549   1090  -1696  -2337       O  
ATOM      5  N   PRO A 238      23.246  23.573  32.321  1.00111.54           N  
ANISOU    5  N   PRO A 238    11242  11854  19283   1096  -1555  -2320       N  
ATOM      6  CA  PRO A 238      22.294  24.346  31.520  1.00111.89           C  
ANISOU    6  CA  PRO A 238    11343  12032  19137   1011  -1324  -2317       C  
ATOM      7  C   PRO A 238      21.126  24.883  32.333  1.00108.32           C  
ANISOU    7  C   PRO A 238    11077  11632  18446   1041  -1414  -2135       C  
ATOM      8  O   PRO A 238      20.820  24.372  33.415  1.00108.98           O  
ANISOU    8  O   PRO A 238    11283  11635  18489   1125  -1632  -1993       O  
ATOM      9  CB  PRO A 238      21.797  23.328  30.481  1.00116.00           C  
ANISOU    9  CB  PRO A 238    11867  12528  19681    978  -1152  -2371       C  
ATOM     10  CG  PRO A 238      22.668  22.100  30.653  1.00118.04           C  
ANISOU   10  CG  PRO A 238    12035  12645  20170   1040  -1275  -2425       C  
ATOM     11  CD  PRO A 238      23.118  22.131  32.070  1.00116.12           C  
ANISOU   11  CD  PRO A 238    11829  12328  19962   1135  -1569  -2323       C  
ATOM     12  N   SER A 239      20.477  25.912  31.800  1.00100.22           N  
ANISOU   12  N   SER A 239    10083  10738  17259    967  -1240  -2140       N  
ATOM     13  CA  SER A 239      19.300  26.497  32.426  1.00 96.60           C  
ANISOU   13  CA  SER A 239     9792  10338  16574    984  -1291  -1982       C  
ATOM     14  C   SER A 239      18.107  26.479  31.473  1.00 91.98           C  
ANISOU   14  C   SER A 239     9298   9826  15825    907  -1065  -1976       C  
ATOM     15  O   SER A 239      18.270  26.387  30.255  1.00 91.25           O  
ANISOU   15  O   SER A 239     9110   9764  15796    841   -850  -2121       O  
ATOM     16  CB  SER A 239      19.598  27.929  32.868  1.00 92.85           C  
ANISOU   16  CB  SER A 239     9292   9966  16020    960  -1326  -1972       C  
ATOM     17  OG  SER A 239      20.995  28.158  32.911  1.00 99.04           O  
ANISOU   17  OG  SER A 239     9923  10723  16984    953  -1374  -2088       O  
ATOM     18  N   VAL A 240      16.903  26.560  32.024  1.00 90.27           N  
ANISOU   18  N   VAL A 240     9307   9656  15336    876  -1104  -1793       N  
ATOM     19  CA  VAL A 240      15.719  26.586  31.181  1.00 92.22           C  
ANISOU   19  CA  VAL A 240     9677   9993  15371    769   -902  -1763       C  
ATOM     20  C   VAL A 240      14.796  27.746  31.572  1.00 90.84           C  
ANISOU   20  C   VAL A 240     9665   9962  14888    690   -878  -1628       C  
ATOM     21  O   VAL A 240      14.576  28.024  32.755  1.00 87.38           O  
ANISOU   21  O   VAL A 240     9337   9517  14345    729  -1048  -1486       O  
ATOM     22  CB  VAL A 240      14.960  25.237  31.229  1.00 89.75           C  
ANISOU   22  CB  VAL A 240     9471   9573  15058    801   -933  -1691       C  
ATOM     23  CG1 VAL A 240      14.272  25.031  32.567  1.00 89.43           C  
ANISOU   23  CG1 VAL A 240     9620   9490  14869    846  -1125  -1484       C  
ATOM     24  CG2 VAL A 240      13.960  25.158  30.100  1.00 89.39           C  
ANISOU   24  CG2 VAL A 240     9496   9605  14863    693   -710  -1717       C  
ATOM     25  N   PHE A 241      14.290  28.447  30.563  1.00 92.54           N  
ANISOU   25  N   PHE A 241     9898  10302  14961    578   -667  -1678       N  
ATOM     26  CA  PHE A 241      13.395  29.571  30.798  1.00 89.35           C  
ANISOU   26  CA  PHE A 241     9637  10034  14277    500   -628  -1565       C  
ATOM     27  C   PHE A 241      12.119  29.414  29.985  1.00 82.97           C  
ANISOU   27  C   PHE A 241     8951   9287  13285    412   -469  -1531       C  
ATOM     28  O   PHE A 241      12.157  29.127  28.785  1.00 79.89           O  
ANISOU   28  O   PHE A 241     8502   8905  12947    362   -306  -1654       O  
ATOM     29  CB  PHE A 241      14.091  30.893  30.466  1.00 90.89           C  
ANISOU   29  CB  PHE A 241     9737  10331  14465    449   -551  -1653       C  
ATOM     30  CG  PHE A 241      15.290  31.173  31.330  1.00 99.32           C  
ANISOU   30  CG  PHE A 241    10685  11346  15705    530   -720  -1682       C  
ATOM     31  CD1 PHE A 241      15.154  31.309  32.703  1.00 98.47           C  
ANISOU   31  CD1 PHE A 241    10679  11212  15524    593   -933  -1537       C  
ATOM     32  CD2 PHE A 241      16.552  31.301  30.770  1.00105.75           C  
ANISOU   32  CD2 PHE A 241    11290  12135  16758    540   -666  -1859       C  
ATOM     33  CE1 PHE A 241      16.253  31.563  33.502  1.00 99.76           C  
ANISOU   33  CE1 PHE A 241    10739  11322  15844    670  -1108  -1566       C  
ATOM     34  CE2 PHE A 241      17.655  31.558  31.565  1.00106.14           C  
ANISOU   34  CE2 PHE A 241    11216  12131  16982    616   -834  -1893       C  
ATOM     35  CZ  PHE A 241      17.504  31.689  32.932  1.00103.26           C  
ANISOU   35  CZ  PHE A 241    10957  11739  16538    683  -1065  -1745       C  
ATOM     36  N   LEU A 242      10.988  29.598  30.654  1.00 75.33           N  
ANISOU   36  N   LEU A 242     8157   8360  12106    392   -519  -1369       N  
ATOM     37  CA  LEU A 242       9.687  29.380  30.040  1.00 66.88           C  
ANISOU   37  CA  LEU A 242     7205   7336  10872    317   -400  -1322       C  
ATOM     38  C   LEU A 242       8.930  30.695  29.876  1.00 64.52           C  
ANISOU   38  C   LEU A 242     6994   7184  10336    230   -316  -1269       C  
ATOM     39  O   LEU A 242       8.714  31.424  30.845  1.00 65.53           O  
ANISOU   39  O   LEU A 242     7197   7354  10346    241   -406  -1160       O  
ATOM     40  CB  LEU A 242       8.873  28.396  30.879  1.00 59.80           C  
ANISOU   40  CB  LEU A 242     6432   6350   9939    359   -508  -1183       C  
ATOM     41  CG  LEU A 242       7.596  27.859  30.242  1.00 55.90           C  
ANISOU   41  CG  LEU A 242     6035   5869   9336    293   -399  -1151       C  
ATOM     42  CD1 LEU A 242       7.907  27.248  28.885  1.00 55.21           C  
ANISOU   42  CD1 LEU A 242     5847   5755   9375    265   -266  -1310       C  
ATOM     43  CD2 LEU A 242       6.951  26.837  31.160  1.00 48.90           C  
ANISOU   43  CD2 LEU A 242     5259   4875   8445    337   -509  -1019       C  
ATOM     44  N   PHE A 243       8.525  30.992  28.648  1.00 59.61           N  
ANISOU   44  N   PHE A 243     6373   6634   9644    144   -147  -1349       N  
ATOM     45  CA  PHE A 243       7.882  32.267  28.357  1.00 59.69           C  
ANISOU   45  CA  PHE A 243     6458   6777   9445     63    -66  -1315       C  
ATOM     46  C   PHE A 243       6.436  32.080  27.916  1.00 61.87           C  
ANISOU   46  C   PHE A 243     6859   7090   9558      1      1  -1250       C  
ATOM     47  O   PHE A 243       6.136  31.194  27.116  1.00 69.30           O  
ANISOU   47  O   PHE A 243     7795   7986  10551    -18     69  -1309       O  
ATOM     48  CB  PHE A 243       8.662  33.018  27.279  1.00 60.10           C  
ANISOU   48  CB  PHE A 243     6418   6889   9530      6     71  -1463       C  
ATOM     49  CG  PHE A 243      10.106  33.235  27.623  1.00 63.76           C  
ANISOU   49  CG  PHE A 243     6736   7315  10176     58     20  -1546       C  
ATOM     50  CD1 PHE A 243      10.497  34.332  28.370  1.00 64.62           C  
ANISOU   50  CD1 PHE A 243     6840   7480  10233     65    -51  -1501       C  
ATOM     51  CD2 PHE A 243      11.073  32.336  27.202  1.00 67.73           C  
ANISOU   51  CD2 PHE A 243     7100   7722  10913    100     39  -1675       C  
ATOM     52  CE1 PHE A 243      11.825  34.532  28.690  1.00 66.81           C  
ANISOU   52  CE1 PHE A 243     6972   7718  10692    112   -107  -1584       C  
ATOM     53  CE2 PHE A 243      12.402  32.530  27.519  1.00 66.62           C  
ANISOU   53  CE2 PHE A 243     6808   7542  10964    150    -13  -1760       C  
ATOM     54  CZ  PHE A 243      12.779  33.630  28.263  1.00 67.37           C  
ANISOU   54  CZ  PHE A 243     6895   7694  11008    155    -90  -1715       C  
ATOM     55  N   PRO A 244       5.538  32.921  28.446  1.00 55.53           N  
ANISOU   55  N   PRO A 244     6165   6367   8567    -29    -20  -1134       N  
ATOM     56  CA  PRO A 244       4.122  32.902  28.078  1.00 53.52           C  
ANISOU   56  CA  PRO A 244     6018   6155   8161    -88     37  -1073       C  
ATOM     57  C   PRO A 244       3.920  33.444  26.668  1.00 48.33           C  
ANISOU   57  C   PRO A 244     5359   5572   7432   -172    177  -1174       C  
ATOM     58  O   PRO A 244       4.857  33.990  26.090  1.00 48.68           O  
ANISOU   58  O   PRO A 244     5333   5644   7520   -190    239  -1277       O  
ATOM     59  CB  PRO A 244       3.482  33.820  29.123  1.00 53.93           C  
ANISOU   59  CB  PRO A 244     6163   6271   8058    -88    -28   -938       C  
ATOM     60  CG  PRO A 244       4.556  34.787  29.456  1.00 47.59           C  
ANISOU   60  CG  PRO A 244     5302   5507   7275    -68    -60   -971       C  
ATOM     61  CD  PRO A 244       5.838  33.992  29.412  1.00 56.12           C  
ANISOU   61  CD  PRO A 244     6259   6495   8569     -9    -99  -1064       C  
ATOM     62  N   PRO A 245       2.716  33.279  26.111  1.00 45.89           N  
ANISOU   62  N   PRO A 245     5131   5288   7018   -225    226  -1148       N  
ATOM     63  CA  PRO A 245       2.417  33.901  24.818  1.00 45.63           C  
ANISOU   63  CA  PRO A 245     5126   5326   6885   -306    339  -1229       C  
ATOM     64  C   PRO A 245       2.271  35.416  24.937  1.00 42.12           C  
ANISOU   64  C   PRO A 245     4729   4987   6289   -341    350  -1189       C  
ATOM     65  O   PRO A 245       2.155  35.926  26.049  1.00 38.91           O  
ANISOU   65  O   PRO A 245     4343   4601   5839   -306    270  -1087       O  
ATOM     66  CB  PRO A 245       1.090  33.247  24.411  1.00 43.26           C  
ANISOU   66  CB  PRO A 245     4900   5010   6525   -341    350  -1194       C  
ATOM     67  CG  PRO A 245       0.511  32.719  25.686  1.00 44.72           C  
ANISOU   67  CG  PRO A 245     5112   5149   6729   -290    250  -1063       C  
ATOM     68  CD  PRO A 245       1.666  32.343  26.544  1.00 47.42           C  
ANISOU   68  CD  PRO A 245     5384   5426   7207   -214    180  -1060       C  
ATOM     69  N   LYS A 246       2.296  36.120  23.807  1.00 45.25           N  
ANISOU   69  N   LYS A 246     5152   5442   6600   -410    448  -1269       N  
ATOM     70  CA  LYS A 246       1.996  37.546  23.797  1.00 42.61           C  
ANISOU   70  CA  LYS A 246     4881   5201   6110   -450    461  -1228       C  
ATOM     71  C   LYS A 246       0.516  37.732  24.071  1.00 50.62           C  
ANISOU   71  C   LYS A 246     5988   6250   6997   -464    415  -1121       C  
ATOM     72  O   LYS A 246      -0.314  37.044  23.473  1.00 56.30           O  
ANISOU   72  O   LYS A 246     6742   6945   7705   -489    430  -1132       O  
ATOM     73  CB  LYS A 246       2.368  38.185  22.461  1.00 41.12           C  
ANISOU   73  CB  LYS A 246     4715   5051   5855   -526    579  -1340       C  
ATOM     74  CG  LYS A 246       3.731  37.775  21.952  1.00 46.43           C  
ANISOU   74  CG  LYS A 246     5291   5677   6674   -526    658  -1472       C  
ATOM     75  CD  LYS A 246       4.189  38.651  20.799  1.00 63.76           C  
ANISOU   75  CD  LYS A 246     7523   7917   8786   -608    786  -1572       C  
ATOM     76  CE  LYS A 246       5.271  39.612  21.260  1.00 76.39           C  
ANISOU   76  CE  LYS A 246     9056   9545  10424   -603    801  -1591       C  
ATOM     77  NZ  LYS A 246       6.427  38.886  21.863  1.00 80.05           N  
ANISOU   77  NZ  LYS A 246     9369   9941  11106   -537    772  -1645       N  
ATOM     78  N   PRO A 247       0.187  38.653  24.991  1.00 44.45           N  
ANISOU   78  N   PRO A 247     5241   5519   6130   -447    360  -1023       N  
ATOM     79  CA  PRO A 247      -1.189  38.945  25.392  1.00 40.56           C  
ANISOU   79  CA  PRO A 247     4823   5058   5529   -456    321   -921       C  
ATOM     80  C   PRO A 247      -2.126  39.064  24.198  1.00 43.58           C  
ANISOU   80  C   PRO A 247     5265   5468   5825   -518    367   -960       C  
ATOM     81  O   PRO A 247      -3.248  38.576  24.257  1.00 46.56           O  
ANISOU   81  O   PRO A 247     5672   5830   6190   -523    341   -913       O  
ATOM     82  CB  PRO A 247      -1.054  40.277  26.131  1.00 29.37           C  
ANISOU   82  CB  PRO A 247     3432   3706   4019   -447    293   -860       C  
ATOM     83  CG  PRO A 247       0.300  40.198  26.749  1.00 28.45           C  
ANISOU   83  CG  PRO A 247     3243   3562   4006   -403    266   -886       C  
ATOM     84  CD  PRO A 247       1.162  39.445  25.762  1.00 34.26           C  
ANISOU   84  CD  PRO A 247     3910   4251   4855   -417    330  -1010       C  
ATOM     85  N   LYS A 248      -1.652  39.670  23.114  1.00 39.07           N  
ANISOU   85  N   LYS A 248     4717   4930   5200   -568    435  -1048       N  
ATOM     86  CA  LYS A 248      -2.483  39.872  21.935  1.00 40.43           C  
ANISOU   86  CA  LYS A 248     4966   5123   5271   -629    466  -1086       C  
ATOM     87  C   LYS A 248      -2.810  38.553  21.232  1.00 42.65           C  
ANISOU   87  C   LYS A 248     5239   5341   5625   -642    482  -1145       C  
ATOM     88  O   LYS A 248      -3.906  38.379  20.699  1.00 33.48           O  
ANISOU   88  O   LYS A 248     4132   4180   4409   -672    460  -1137       O  
ATOM     89  CB  LYS A 248      -1.795  40.832  20.960  1.00 35.28           C  
ANISOU   89  CB  LYS A 248     4360   4511   4533   -684    541  -1166       C  
ATOM     90  CG  LYS A 248      -2.662  41.248  19.783  1.00 41.82           C  
ANISOU   90  CG  LYS A 248     5298   5363   5228   -747    555  -1193       C  
ATOM     91  CD  LYS A 248      -1.906  42.159  18.831  1.00 47.26           C  
ANISOU   91  CD  LYS A 248     6051   6079   5825   -808    640  -1270       C  
ATOM     92  CE  LYS A 248      -2.788  42.586  17.668  1.00 55.54           C  
ANISOU   92  CE  LYS A 248     7233   7142   6726   -868    636  -1291       C  
ATOM     93  NZ  LYS A 248      -2.047  43.405  16.670  1.00 63.09           N  
ANISOU   93  NZ  LYS A 248     8277   8114   7580   -937    730  -1367       N  
ATOM     94  N   ASP A 249      -1.859  37.624  21.239  1.00 45.33           N  
ANISOU   94  N   ASP A 249     5506   5620   6098   -618    513  -1208       N  
ATOM     95  CA  ASP A 249      -2.026  36.361  20.526  1.00 49.27           C  
ANISOU   95  CA  ASP A 249     5995   6051   6674   -631    538  -1279       C  
ATOM     96  C   ASP A 249      -3.093  35.473  21.164  1.00 46.54           C  
ANISOU   96  C   ASP A 249     5643   5662   6377   -604    466  -1198       C  
ATOM     97  O   ASP A 249      -3.788  34.730  20.469  1.00 42.96           O  
ANISOU   97  O   ASP A 249     5216   5173   5933   -634    469  -1235       O  
ATOM     98  CB  ASP A 249      -0.692  35.611  20.451  1.00 49.33           C  
ANISOU   98  CB  ASP A 249     5916   5998   6830   -604    590  -1369       C  
ATOM     99  CG  ASP A 249       0.331  36.326  19.587  1.00 48.72           C  
ANISOU   99  CG  ASP A 249     5843   5950   6719   -648    691  -1476       C  
ATOM    100  OD1 ASP A 249      -0.077  37.132  18.722  1.00 51.00           O  
ANISOU  100  OD1 ASP A 249     6226   6290   6860   -713    731  -1498       O  
ATOM    101  OD2 ASP A 249       1.542  36.079  19.770  1.00 44.69           O  
ANISOU  101  OD2 ASP A 249     5242   5406   6334   -620    730  -1539       O  
ATOM    102  N   THR A 250      -3.225  35.559  22.483  1.00 43.45           N  
ANISOU  102  N   THR A 250     5225   5271   6015   -552    405  -1091       N  
ATOM    103  CA  THR A 250      -4.223  34.773  23.199  1.00 39.43           C  
ANISOU  103  CA  THR A 250     4716   4717   5548   -532    351  -1007       C  
ATOM    104  C   THR A 250      -5.604  35.389  23.087  1.00 35.95           C  
ANISOU  104  C   THR A 250     4332   4327   5000   -569    327   -952       C  
ATOM    105  O   THR A 250      -6.607  34.716  23.292  1.00 39.73           O  
ANISOU  105  O   THR A 250     4813   4769   5513   -575    302   -913       O  
ATOM    106  CB  THR A 250      -3.883  34.635  24.695  1.00 41.61           C  
ANISOU  106  CB  THR A 250     4962   4966   5881   -468    298   -909       C  
ATOM    107  OG1 THR A 250      -4.027  35.907  25.340  1.00 42.27           O  
ANISOU  107  OG1 THR A 250     5077   5126   5857   -463    277   -838       O  
ATOM    108  CG2 THR A 250      -2.471  34.145  24.874  1.00 46.55           C  
ANISOU  108  CG2 THR A 250     5523   5540   6623   -423    299   -963       C  
ATOM    109  N   LEU A 251      -5.651  36.675  22.769  1.00 39.22           N  
ANISOU  109  N   LEU A 251     4788   4820   5293   -592    335   -953       N  
ATOM    110  CA  LEU A 251      -6.905  37.408  22.767  1.00 39.83           C  
ANISOU  110  CA  LEU A 251     4912   4946   5276   -615    302   -898       C  
ATOM    111  C   LEU A 251      -7.539  37.459  21.382  1.00 43.49           C  
ANISOU  111  C   LEU A 251     5427   5418   5680   -672    305   -973       C  
ATOM    112  O   LEU A 251      -8.764  37.408  21.253  1.00 36.41           O  
ANISOU  112  O   LEU A 251     4545   4521   4769   -690    263   -947       O  
ATOM    113  CB  LEU A 251      -6.684  38.825  23.293  1.00 39.15           C  
ANISOU  113  CB  LEU A 251     4851   4933   5092   -603    295   -847       C  
ATOM    114  CG  LEU A 251      -6.266  38.929  24.757  1.00 41.00           C  
ANISOU  114  CG  LEU A 251     5054   5164   5361   -549    273   -761       C  
ATOM    115  CD1 LEU A 251      -5.851  40.354  25.090  1.00 38.39           C  
ANISOU  115  CD1 LEU A 251     4751   4904   4933   -543    272   -735       C  
ATOM    116  CD2 LEU A 251      -7.391  38.471  25.663  1.00 34.73           C  
ANISOU  116  CD2 LEU A 251     4258   4343   4596   -534    243   -670       C  
ATOM    117  N   MET A 252      -6.708  37.563  20.350  1.00 40.14           N  
ANISOU  117  N   MET A 252     5032   4996   5221   -703    355  -1070       N  
ATOM    118  CA  MET A 252      -7.201  37.638  18.978  1.00 35.35           C  
ANISOU  118  CA  MET A 252     4502   4393   4537   -761    356  -1146       C  
ATOM    119  C   MET A 252      -7.200  36.258  18.322  1.00 37.80           C  
ANISOU  119  C   MET A 252     4797   4630   4935   -778    375  -1225       C  
ATOM    120  O   MET A 252      -6.165  35.594  18.258  1.00 42.28           O  
ANISOU  120  O   MET A 252     5324   5156   5583   -766    434  -1284       O  
ATOM    121  CB  MET A 252      -6.355  38.617  18.161  1.00 30.67           C  
ANISOU  121  CB  MET A 252     3978   3843   3832   -797    412  -1209       C  
ATOM    122  CG  MET A 252      -6.294  40.024  18.737  1.00 28.32           C  
ANISOU  122  CG  MET A 252     3702   3614   3446   -784    396  -1139       C  
ATOM    123  SD  MET A 252      -7.904  40.831  18.843  1.00 49.10           S  
ANISOU  123  SD  MET A 252     6384   6284   5989   -787    299  -1058       S  
ATOM    124  CE  MET A 252      -8.162  40.837  20.614  1.00 47.07           C  
ANISOU  124  CE  MET A 252     6034   6036   5814   -720    269   -940       C  
ATOM    125  N   ILE A 253      -8.365  35.837  17.838  1.00 36.58           N  
ANISOU  125  N   ILE A 253     4669   4453   4776   -805    321  -1231       N  
ATOM    126  CA  ILE A 253      -8.515  34.509  17.245  1.00 40.55           C  
ANISOU  126  CA  ILE A 253     5161   4882   5365   -825    329  -1304       C  
ATOM    127  C   ILE A 253      -7.763  34.402  15.916  1.00 35.08           C  
ANISOU  127  C   ILE A 253     4539   4175   4613   -871    393  -1430       C  
ATOM    128  O   ILE A 253      -7.388  33.312  15.489  1.00 42.18           O  
ANISOU  128  O   ILE A 253     5422   5010   5596   -879    432  -1507       O  
ATOM    129  CB  ILE A 253     -10.012  34.145  17.034  1.00 39.49           C  
ANISOU  129  CB  ILE A 253     5034   4726   5243   -848    247  -1284       C  
ATOM    130  CG1 ILE A 253     -10.170  32.651  16.729  1.00 44.27           C  
ANISOU  130  CG1 ILE A 253     5608   5244   5967   -860    253  -1342       C  
ATOM    131  CG2 ILE A 253     -10.642  35.009  15.945  1.00 29.05           C  
ANISOU  131  CG2 ILE A 253     3814   3445   3780   -895    198  -1323       C  
ATOM    132  CD1 ILE A 253      -9.596  31.744  17.797  1.00 38.36           C  
ANISOU  132  CD1 ILE A 253     4773   4441   5362   -811    288  -1299       C  
ATOM    133  N   SER A 254      -7.520  35.543  15.278  1.00 36.39           N  
ANISOU  133  N   SER A 254     4792   4398   4636   -903    411  -1452       N  
ATOM    134  CA  SER A 254      -6.798  35.576  14.012  1.00 39.75           C  
ANISOU  134  CA  SER A 254     5309   4813   4984   -958    488  -1571       C  
ATOM    135  C   SER A 254      -5.321  35.262  14.219  1.00 46.51           C  
ANISOU  135  C   SER A 254     6099   5648   5925   -939    600  -1626       C  
ATOM    136  O   SER A 254      -4.574  35.075  13.260  1.00 53.59           O  
ANISOU  136  O   SER A 254     7046   6521   6793   -981    692  -1738       O  
ATOM    137  CB  SER A 254      -6.951  36.941  13.339  1.00 40.00           C  
ANISOU  137  CB  SER A 254     5464   4904   4831  -1000    477  -1568       C  
ATOM    138  OG  SER A 254      -6.446  37.976  14.167  1.00 43.86           O  
ANISOU  138  OG  SER A 254     5917   5449   5298   -970    495  -1497       O  
ATOM    139  N   ARG A 255      -4.904  35.205  15.478  1.00 42.87           N  
ANISOU  139  N   ARG A 255     5526   5191   5571   -875    591  -1552       N  
ATOM    140  CA  ARG A 255      -3.501  35.004  15.804  1.00 42.81           C  
ANISOU  140  CA  ARG A 255     5440   5164   5661   -847    675  -1598       C  
ATOM    141  C   ARG A 255      -3.250  33.664  16.490  1.00 43.94           C  
ANISOU  141  C   ARG A 255     5477   5230   5990   -792    662  -1596       C  
ATOM    142  O   ARG A 255      -4.174  33.022  16.992  1.00 47.83           O  
ANISOU  142  O   ARG A 255     5950   5692   6530   -771    587  -1531       O  
ATOM    143  CB  ARG A 255      -3.005  36.148  16.686  1.00 43.60           C  
ANISOU  143  CB  ARG A 255     5508   5327   5730   -817    669  -1523       C  
ATOM    144  CG  ARG A 255      -3.147  37.518  16.040  1.00 50.09           C  
ANISOU  144  CG  ARG A 255     6439   6217   6375   -871    686  -1524       C  
ATOM    145  CD  ARG A 255      -2.498  38.588  16.899  1.00 58.59           C  
ANISOU  145  CD  ARG A 255     7476   7347   7438   -843    692  -1464       C  
ATOM    146  NE  ARG A 255      -1.830  39.588  16.077  1.00 65.34           N  
ANISOU  146  NE  ARG A 255     8409   8237   8182   -902    777  -1527       N  
ATOM    147  CZ  ARG A 255      -0.625  39.420  15.547  1.00 70.00           C  
ANISOU  147  CZ  ARG A 255     8974   8801   8821   -929    894  -1634       C  
ATOM    148  NH1 ARG A 255      -0.083  40.377  14.808  1.00 77.75           N  
ANISOU  148  NH1 ARG A 255    10037   9812   9693   -992    981  -1687       N  
ATOM    149  NH2 ARG A 255       0.035  38.290  15.756  1.00 63.50           N  
ANISOU  149  NH2 ARG A 255     8045   7919   8164   -894    927  -1692       N  
ATOM    150  N   THR A 256      -1.989  33.250  16.508  1.00 47.85           N  
ANISOU  150  N   THR A 256     5901   5686   6595   -769    736  -1670       N  
ATOM    151  CA  THR A 256      -1.614  31.948  17.037  1.00 51.68           C  
ANISOU  151  CA  THR A 256     6290   6083   7262   -715    724  -1683       C  
ATOM    152  C   THR A 256      -0.691  32.086  18.244  1.00 50.56           C  
ANISOU  152  C   THR A 256     6046   5936   7230   -642    701  -1630       C  
ATOM    153  O   THR A 256       0.493  32.371  18.085  1.00 49.08           O  
ANISOU  153  O   THR A 256     5807   5749   7092   -637    770  -1704       O  
ATOM    154  CB  THR A 256      -0.914  31.087  15.964  1.00 56.89           C  
ANISOU  154  CB  THR A 256     6945   6676   7993   -742    823  -1837       C  
ATOM    155  OG1 THR A 256      -1.737  31.007  14.796  1.00 55.44           O  
ANISOU  155  OG1 THR A 256     6876   6498   7692   -814    839  -1893       O  
ATOM    156  CG2 THR A 256      -0.640  29.685  16.494  1.00 62.66           C  
ANISOU  156  CG2 THR A 256     7583   7305   8919   -682    798  -1848       C  
ATOM    157  N   PRO A 257      -1.234  31.887  19.455  1.00 48.01           N  
ANISOU  157  N   PRO A 257     5696   5602   6944   -590    604  -1504       N  
ATOM    158  CA  PRO A 257      -0.436  31.968  20.683  1.00 40.77           C  
ANISOU  158  CA  PRO A 257     4699   4671   6121   -518    558  -1442       C  
ATOM    159  C   PRO A 257       0.527  30.798  20.857  1.00 42.35           C  
ANISOU  159  C   PRO A 257     4808   4769   6515   -464    564  -1507       C  
ATOM    160  O   PRO A 257       0.222  29.671  20.471  1.00 43.83           O  
ANISOU  160  O   PRO A 257     4994   4881   6778   -466    570  -1547       O  
ATOM    161  CB  PRO A 257      -1.499  31.975  21.792  1.00 44.00           C  
ANISOU  161  CB  PRO A 257     5138   5088   6493   -492    462  -1294       C  
ATOM    162  CG  PRO A 257      -2.667  31.278  21.192  1.00 45.50           C  
ANISOU  162  CG  PRO A 257     5377   5249   6661   -533    459  -1300       C  
ATOM    163  CD  PRO A 257      -2.661  31.652  19.735  1.00 41.72           C  
ANISOU  163  CD  PRO A 257     4949   4807   6095   -602    534  -1413       C  
ATOM    164  N   GLU A 258       1.687  31.080  21.438  1.00 44.73           N  
ANISOU  164  N   GLU A 258     5028   5063   6902   -415    555  -1519       N  
ATOM    165  CA  GLU A 258       2.705  30.067  21.667  1.00 50.87           C  
ANISOU  165  CA  GLU A 258     5704   5740   7882   -353    547  -1584       C  
ATOM    166  C   GLU A 258       3.283  30.159  23.068  1.00 53.97           C  
ANISOU  166  C   GLU A 258     6041   6108   8356   -270    438  -1494       C  
ATOM    167  O   GLU A 258       3.469  31.250  23.601  1.00 55.34           O  
ANISOU  167  O   GLU A 258     6221   6354   8450   -269    411  -1440       O  
ATOM    168  CB  GLU A 258       3.853  30.209  20.657  1.00 46.92           C  
ANISOU  168  CB  GLU A 258     5141   5237   7451   -379    667  -1747       C  
ATOM    169  CG  GLU A 258       3.462  30.228  19.189  1.00 52.06           C  
ANISOU  169  CG  GLU A 258     5865   5912   8004   -467    787  -1852       C  
ATOM    170  CD  GLU A 258       4.632  30.620  18.300  1.00 57.88           C  
ANISOU  170  CD  GLU A 258     6552   6656   8782   -503    924  -2004       C  
ATOM    171  OE1 GLU A 258       4.632  30.249  17.108  1.00 62.57           O  
ANISOU  171  OE1 GLU A 258     7188   7229   9355   -561   1034  -2122       O  
ATOM    172  OE2 GLU A 258       5.554  31.300  18.800  1.00 60.51           O  
ANISOU  172  OE2 GLU A 258     6808   7014   9169   -477    925  -2009       O  
ATOM    173  N   VAL A 259       3.591  29.014  23.659  1.00 52.29           N  
ANISOU  173  N   VAL A 259     5779   5786   8301   -202    368  -1480       N  
ATOM    174  CA  VAL A 259       4.436  28.996  24.843  1.00 55.35           C  
ANISOU  174  CA  VAL A 259     6105   6130   8797   -117    261  -1427       C  
ATOM    175  C   VAL A 259       5.831  28.560  24.411  1.00 55.20           C  
ANISOU  175  C   VAL A 259     5952   6044   8976    -78    297  -1572       C  
ATOM    176  O   VAL A 259       5.975  27.599  23.656  1.00 57.78           O  
ANISOU  176  O   VAL A 259     6245   6299   9411    -81    357  -1670       O  
ATOM    177  CB  VAL A 259       3.887  28.067  25.926  1.00 56.02           C  
ANISOU  177  CB  VAL A 259     6235   6126   8922    -60    142  -1302       C  
ATOM    178  CG1 VAL A 259       4.904  27.896  27.032  1.00 56.80           C  
ANISOU  178  CG1 VAL A 259     6274   6158   9151     34     19  -1268       C  
ATOM    179  CG2 VAL A 259       2.582  28.624  26.477  1.00 59.35           C  
ANISOU  179  CG2 VAL A 259     6776   6617   9157    -98    115  -1162       C  
ATOM    180  N   THR A 260       6.858  29.270  24.872  1.00 50.37           N  
ANISOU  180  N   THR A 260     5261   5455   8423    -43    265  -1593       N  
ATOM    181  CA  THR A 260       8.211  29.044  24.373  1.00 47.57           C  
ANISOU  181  CA  THR A 260     4762   5050   8264    -17    319  -1748       C  
ATOM    182  C   THR A 260       9.178  28.613  25.472  1.00 50.27           C  
ANISOU  182  C   THR A 260     5004   5299   8796     92    172  -1727       C  
ATOM    183  O   THR A 260       9.426  29.347  26.428  1.00 55.27           O  
ANISOU  183  O   THR A 260     5640   5967   9393    124     69  -1646       O  
ATOM    184  CB  THR A 260       8.760  30.310  23.682  1.00 51.38           C  
ANISOU  184  CB  THR A 260     5211   5632   8678    -85    439  -1836       C  
ATOM    185  OG1 THR A 260       7.801  30.794  22.731  1.00 57.96           O  
ANISOU  185  OG1 THR A 260     6161   6549   9311   -183    552  -1838       O  
ATOM    186  CG2 THR A 260      10.061  30.010  22.962  1.00 59.67           C  
ANISOU  186  CG2 THR A 260     6112   6627   9931    -77    538  -2018       C  
ATOM    187  N   CYS A 261       9.726  27.412  25.322  1.00 55.45           N  
ANISOU  187  N   CYS A 261     5576   5832   9659    150    155  -1805       N  
ATOM    188  CA  CYS A 261      10.688  26.877  26.276  1.00 60.20           C  
ANISOU  188  CA  CYS A 261     6078   6327  10468    261      2  -1799       C  
ATOM    189  C   CYS A 261      12.100  27.032  25.730  1.00 64.54           C  
ANISOU  189  C   CYS A 261     6444   6851  11227    280     70  -1977       C  
ATOM    190  O   CYS A 261      12.430  26.483  24.678  1.00 60.57           O  
ANISOU  190  O   CYS A 261     5871   6310  10832    255    205  -2124       O  
ATOM    191  CB  CYS A 261      10.381  25.409  26.574  1.00 61.18           C  
ANISOU  191  CB  CYS A 261     6229   6314  10703    324    -80  -1762       C  
ATOM    192  SG  CYS A 261      11.358  24.690  27.896  1.00 66.23           S  
ANISOU  192  SG  CYS A 261     6792   6806  11568    469   -309  -1717       S  
ATOM    193  N   VAL A 262      12.929  27.787  26.443  1.00 68.41           N  
ANISOU  193  N   VAL A 262     6856   7362  11777    319    -19  -1971       N  
ATOM    194  CA  VAL A 262      14.276  28.100  25.973  1.00 71.30           C  
ANISOU  194  CA  VAL A 262     7035   7713  12343    327     52  -2142       C  
ATOM    195  C   VAL A 262      15.336  27.512  26.895  1.00 69.42           C  
ANISOU  195  C   VAL A 262     6660   7351  12367    454   -133  -2161       C  
ATOM    196  O   VAL A 262      15.345  27.785  28.096  1.00 65.65           O  
ANISOU  196  O   VAL A 262     6225   6865  11856    513   -322  -2035       O  
ATOM    197  CB  VAL A 262      14.493  29.626  25.859  1.00 74.65           C  
ANISOU  197  CB  VAL A 262     7456   8269  12639    254    123  -2152       C  
ATOM    198  CG1 VAL A 262      15.883  29.934  25.315  1.00 79.07           C  
ANISOU  198  CG1 VAL A 262     7815   8809  13419    250    219  -2340       C  
ATOM    199  CG2 VAL A 262      13.424  30.249  24.975  1.00 70.23           C  
ANISOU  199  CG2 VAL A 262     7043   7825  11816    135    285  -2125       C  
ATOM    200  N   VAL A 263      16.228  26.705  26.327  1.00 71.10           N  
ANISOU  200  N   VAL A 263     6713   7462  12841    495    -81  -2322       N  
ATOM    201  CA  VAL A 263      17.309  26.099  27.097  1.00 74.67           C  
ANISOU  201  CA  VAL A 263     7021   7788  13564    614   -259  -2355       C  
ATOM    202  C   VAL A 263      18.652  26.752  26.768  1.00 80.94           C  
ANISOU  202  C   VAL A 263     7652   8618  14482    565   -203  -2483       C  
ATOM    203  O   VAL A 263      19.059  26.809  25.606  1.00 79.86           O  
ANISOU  203  O   VAL A 263     7457   8518  14369    468     -1  -2615       O  
ATOM    204  CB  VAL A 263      17.408  24.585  26.840  1.00 71.33           C  
ANISOU  204  CB  VAL A 263     6583   7244  13274    649   -285  -2380       C  
ATOM    205  CG1 VAL A 263      18.340  23.941  27.854  1.00 70.09           C  
ANISOU  205  CG1 VAL A 263     6345   6970  13315    754   -520  -2350       C  
ATOM    206  CG2 VAL A 263      16.033  23.944  26.905  1.00 65.85           C  
ANISOU  206  CG2 VAL A 263     6060   6513  12447    664   -289  -2276       C  
ATOM    207  N   VAL A 264      19.334  27.243  27.798  1.00 85.76           N  
ANISOU  207  N   VAL A 264     8205   9212  15168    627   -386  -2441       N  
ATOM    208  CA  VAL A 264      20.621  27.904  27.617  1.00 90.39           C  
ANISOU  208  CA  VAL A 264     8646   9816  15881    582   -353  -2559       C  
ATOM    209  C   VAL A 264      21.729  27.176  28.375  1.00 97.20           C  
ANISOU  209  C   VAL A 264     9402  10549  16981    670   -559  -2580       C  
ATOM    210  O   VAL A 264      21.455  26.270  29.166  1.00 97.75           O  
ANISOU  210  O   VAL A 264     9526  10526  17088    768   -748  -2482       O  
ATOM    211  CB  VAL A 264      20.564  29.375  28.074  1.00 87.97           C  
ANISOU  211  CB  VAL A 264     8360   9617  15447    555   -368  -2514       C  
ATOM    212  CG1 VAL A 264      19.566  30.159  27.225  1.00 85.72           C  
ANISOU  212  CG1 VAL A 264     8172   9464  14933    456   -149  -2510       C  
ATOM    213  CG2 VAL A 264      20.203  29.462  29.546  1.00 89.90           C  
ANISOU  213  CG2 VAL A 264     8678   9834  15646    665   -635  -2352       C  
ATOM    214  N   ASP A 265      22.975  27.579  28.119  1.00101.14           N  
ANISOU  214  N   ASP A 265     9758  11034  17635    630   -521  -2710       N  
ATOM    215  CA  ASP A 265      24.167  26.943  28.692  1.00101.89           C  
ANISOU  215  CA  ASP A 265     9732  11003  17979    700   -695  -2765       C  
ATOM    216  C   ASP A 265      24.242  25.470  28.311  1.00 99.83           C  
ANISOU  216  C   ASP A 265     9437  10637  17856    734   -697  -2804       C  
ATOM    217  O   ASP A 265      24.521  24.613  29.150  1.00 99.49           O  
ANISOU  217  O   ASP A 265     9388  10483  17932    834   -915  -2751       O  
ATOM    218  CB  ASP A 265      24.200  27.101  30.220  1.00105.09           C  
ANISOU  218  CB  ASP A 265    10192  11366  18373    809   -993  -2628       C  
ATOM    219  CG  ASP A 265      24.433  28.534  30.644  1.00104.06           C  
ANISOU  219  CG  ASP A 265    10061  11322  18156    778  -1012  -2613       C  
ATOM    220  OD1 ASP A 265      24.782  29.346  29.766  1.00104.06           O  
ANISOU  220  OD1 ASP A 265     9995  11396  18147    677   -802  -2726       O  
ATOM    221  OD2 ASP A 265      24.279  28.846  31.846  1.00101.20           O  
ANISOU  221  OD2 ASP A 265     9774  10950  17727    851  -1234  -2488       O  
ATOM    222  N   VAL A 266      23.996  25.186  27.038  1.00100.18           N  
ANISOU  222  N   VAL A 266     9471  10716  17875    646   -454  -2896       N  
ATOM    223  CA  VAL A 266      23.982  23.817  26.537  1.00100.24           C  
ANISOU  223  CA  VAL A 266     9454  10637  17995    666   -425  -2940       C  
ATOM    224  C   VAL A 266      25.360  23.386  26.055  1.00 97.80           C  
ANISOU  224  C   VAL A 266     8962  10246  17951    645   -383  -3110       C  
ATOM    225  O   VAL A 266      25.915  23.967  25.120  1.00 98.92           O  
ANISOU  225  O   VAL A 266     9028  10435  18122    541   -178  -3243       O  
ATOM    226  CB  VAL A 266      22.968  23.656  25.391  1.00100.08           C  
ANISOU  226  CB  VAL A 266     9529  10691  17805    581   -190  -2951       C  
ATOM    227  CG1 VAL A 266      23.119  22.295  24.730  1.00100.58           C  
ANISOU  227  CG1 VAL A 266     9547  10668  18000    587   -134  -3024       C  
ATOM    228  CG2 VAL A 266      21.548  23.861  25.904  1.00 98.41           C  
ANISOU  228  CG2 VAL A 266     9499  10535  17359    614   -247  -2785       C  
ATOM    229  N   SER A 267      25.893  22.349  26.690  1.00 98.38           N  
ANISOU  229  N   SER A 267     8973  10191  18216    742   -575  -3104       N  
ATOM    230  CA  SER A 267      27.249  21.864  26.422  1.00104.81           C  
ANISOU  230  CA  SER A 267     9604  10907  19313    743   -579  -3261       C  
ATOM    231  C   SER A 267      27.503  21.408  24.981  1.00109.09           C  
ANISOU  231  C   SER A 267    10070  11452  19927    646   -314  -3415       C  
ATOM    232  O   SER A 267      26.623  20.841  24.325  1.00105.89           O  
ANISOU  232  O   SER A 267     9754  11076  19403    619   -194  -3387       O  
ATOM    233  CB  SER A 267      27.567  20.709  27.375  1.00104.02           C  
ANISOU  233  CB  SER A 267     9480  10665  19376    871   -845  -3206       C  
ATOM    234  OG  SER A 267      28.557  19.850  26.834  1.00105.12           O  
ANISOU  234  OG  SER A 267     9461  10705  19776    869   -805  -3357       O  
ATOM    235  N   HIS A 268      28.720  21.661  24.505  1.00116.12           N  
ANISOU  235  N   HIS A 268    10800  12307  21013    592   -226  -3580       N  
ATOM    236  CA  HIS A 268      29.193  21.141  23.224  1.00116.25           C  
ANISOU  236  CA  HIS A 268    10726  12300  21144    506      3  -3740       C  
ATOM    237  C   HIS A 268      29.380  19.632  23.311  1.00113.85           C  
ANISOU  237  C   HIS A 268    10363  11874  21022    588    -99  -3759       C  
ATOM    238  O   HIS A 268      29.115  18.909  22.348  1.00110.49           O  
ANISOU  238  O   HIS A 268     9944  11445  20593    542     67  -3818       O  
ATOM    239  CB  HIS A 268      30.515  21.803  22.821  1.00122.00           C  
ANISOU  239  CB  HIS A 268    11295  13003  22057    435    105  -3911       C  
ATOM    240  CG  HIS A 268      30.366  22.919  21.833  1.00122.43           C  
ANISOU  240  CG  HIS A 268    11399  13172  21946    291    373  -3968       C  
ATOM    241  ND1 HIS A 268      29.357  23.855  21.911  1.00118.66           N  
ANISOU  241  ND1 HIS A 268    11082  12821  21183    256    415  -3849       N  
ATOM    242  CD2 HIS A 268      31.099  23.249  20.743  1.00123.78           C  
ANISOU  242  CD2 HIS A 268    11491  13345  22196    171    612  -4131       C  
ATOM    243  CE1 HIS A 268      29.476  24.713  20.914  1.00116.64           C  
ANISOU  243  CE1 HIS A 268    10847  12641  20830    121    661  -3932       C  
ATOM    244  NE2 HIS A 268      30.525  24.369  20.190  1.00119.72           N  
ANISOU  244  NE2 HIS A 268    11100  12957  21433     65    787  -4101       N  
ATOM    245  N   GLU A 269      29.833  19.164  24.473  1.00116.24           N  
ANISOU  245  N   GLU A 269    10618  12074  21476    710   -376  -3707       N  
ATOM    246  CA  GLU A 269      30.069  17.739  24.706  1.00120.38           C  
ANISOU  246  CA  GLU A 269    11089  12468  22182    800   -509  -3715       C  
ATOM    247  C   GLU A 269      28.826  16.893  24.461  1.00124.07           C  
ANISOU  247  C   GLU A 269    11705  12952  22482    821   -475  -3608       C  
ATOM    248  O   GLU A 269      28.811  16.032  23.574  1.00122.79           O  
ANISOU  248  O   GLU A 269    11509  12758  22387    791   -335  -3691       O  
ATOM    249  CB  GLU A 269      30.563  17.502  26.137  1.00119.49           C  
ANISOU  249  CB  GLU A 269    10951  12253  22196    929   -841  -3637       C  
ATOM    250  CG  GLU A 269      32.070  17.649  26.328  1.00119.75           C  
ANISOU  250  CG  GLU A 269    10785  12194  22521    939   -914  -3786       C  
ATOM    251  CD  GLU A 269      32.487  19.064  26.680  1.00114.46           C  
ANISOU  251  CD  GLU A 269    10096  11588  21805    899   -921  -3799       C  
ATOM    252  OE1 GLU A 269      31.600  19.902  26.953  1.00110.63           O  
ANISOU  252  OE1 GLU A 269     9758  11214  21062    879   -909  -3673       O  
ATOM    253  OE2 GLU A 269      33.707  19.337  26.685  1.00111.43           O  
ANISOU  253  OE2 GLU A 269     9548  11139  21651    887   -937  -3938       O  
ATOM    254  N   ASP A 270      27.789  17.140  25.256  1.00133.20           N  
ANISOU  254  N   ASP A 270    13030  14155  23426    871   -602  -3427       N  
ATOM    255  CA  ASP A 270      26.527  16.414  25.174  1.00129.72           C  
ANISOU  255  CA  ASP A 270    12750  13723  22817    896   -591  -3309       C  
ATOM    256  C   ASP A 270      25.400  17.382  24.809  1.00122.27           C  
ANISOU  256  C   ASP A 270    11953  12924  21579    818   -441  -3232       C  
ATOM    257  O   ASP A 270      24.737  17.941  25.693  1.00115.05           O  
ANISOU  257  O   ASP A 270    11159  12049  20507    860   -571  -3086       O  
ATOM    258  CB  ASP A 270      26.236  15.706  26.508  1.00132.95           C  
ANISOU  258  CB  ASP A 270    13245  14032  23238   1030   -890  -3151       C  
ATOM    259  CG  ASP A 270      27.301  16.008  27.570  1.00130.99           C  
ANISOU  259  CG  ASP A 270    12904  13713  23154   1101  -1126  -3155       C  
ATOM    260  OD1 ASP A 270      27.733  17.194  27.647  1.00129.36           O  
ANISOU  260  OD1 ASP A 270    12649  13579  22924   1054  -1093  -3193       O  
ATOM    261  OD2 ASP A 270      27.694  15.070  28.317  1.00132.35           O  
ANISOU  261  OD2 ASP A 270    13059  13756  23472   1201  -1344  -3119       O  
ATOM    262  N   PRO A 271      25.181  17.587  23.501  1.00123.32           N  
ANISOU  262  N   PRO A 271    12085  13135  21635    704   -168  -3331       N  
ATOM    263  CA  PRO A 271      24.274  18.646  23.056  1.00124.46           C  
ANISOU  263  CA  PRO A 271    12355  13422  21514    616    -13  -3284       C  
ATOM    264  C   PRO A 271      22.896  18.161  22.599  1.00124.86           C  
ANISOU  264  C   PRO A 271    12572  13509  21361    598     73  -3202       C  
ATOM    265  O   PRO A 271      22.162  18.945  21.997  1.00125.02           O  
ANISOU  265  O   PRO A 271    12691  13644  21168    512    232  -3188       O  
ATOM    266  CB  PRO A 271      25.044  19.242  21.882  1.00124.85           C  
ANISOU  266  CB  PRO A 271    12303  13526  21611    491    231  -3454       C  
ATOM    267  CG  PRO A 271      25.713  18.041  21.263  1.00124.22           C  
ANISOU  267  CG  PRO A 271    12109  13343  21745    496    284  -3577       C  
ATOM    268  CD  PRO A 271      25.992  17.064  22.382  1.00124.44           C  
ANISOU  268  CD  PRO A 271    12094  13241  21948    638     12  -3512       C  
ATOM    269  N   GLU A 272      22.542  16.911  22.881  1.00120.88           N  
ANISOU  269  N   GLU A 272    12105  12905  20918    676    -32  -3150       N  
ATOM    270  CA  GLU A 272      21.259  16.379  22.416  1.00110.73           C  
ANISOU  270  CA  GLU A 272    10976  11640  19457    655     51  -3084       C  
ATOM    271  C   GLU A 272      20.168  16.545  23.478  1.00 98.77           C  
ANISOU  271  C   GLU A 272     9623  10126  17778    721   -113  -2894       C  
ATOM    272  O   GLU A 272      20.112  15.792  24.454  1.00 98.44           O  
ANISOU  272  O   GLU A 272     9613   9978  17811    824   -322  -2797       O  
ATOM    273  CB  GLU A 272      21.406  14.910  22.019  1.00109.48           C  
ANISOU  273  CB  GLU A 272    10781  11370  19445    689     53  -3138       C  
ATOM    274  CG  GLU A 272      22.597  14.634  21.098  1.00111.70           C  
ANISOU  274  CG  GLU A 272    10889  11626  19926    637    192  -3327       C  
ATOM    275  CD  GLU A 272      22.215  14.558  19.628  1.00111.66           C  
ANISOU  275  CD  GLU A 272    10926  11688  19812    520    462  -3425       C  
ATOM    276  OE1 GLU A 272      23.113  14.705  18.770  1.00110.53           O  
ANISOU  276  OE1 GLU A 272    10665  11556  19776    447    620  -3578       O  
ATOM    277  OE2 GLU A 272      21.020  14.343  19.332  1.00112.03           O  
ANISOU  277  OE2 GLU A 272    11130  11770  19665    498    514  -3351       O  
ATOM    278  N   VAL A 273      19.293  17.525  23.263  1.00 85.30           N  
ANISOU  278  N   VAL A 273     8031   8536  15843    656    -15  -2843       N  
ATOM    279  CA  VAL A 273      18.312  17.938  24.265  1.00 85.67           C  
ANISOU  279  CA  VAL A 273     8224   8596  15729    704   -152  -2673       C  
ATOM    280  C   VAL A 273      16.902  17.392  23.997  1.00 86.64           C  
ANISOU  280  C   VAL A 273     8520   8712  15686    684   -101  -2592       C  
ATOM    281  O   VAL A 273      16.411  17.442  22.868  1.00 89.10           O  
ANISOU  281  O   VAL A 273     8873   9090  15891    590     97  -2662       O  
ATOM    282  CB  VAL A 273      18.247  19.480  24.345  1.00 86.72           C  
ANISOU  282  CB  VAL A 273     8371   8858  15722    651    -96  -2661       C  
ATOM    283  CG1 VAL A 273      17.375  19.922  25.509  1.00 86.17           C  
ANISOU  283  CG1 VAL A 273     8438   8789  15512    713   -259  -2487       C  
ATOM    284  CG2 VAL A 273      19.649  20.063  24.482  1.00 86.97           C  
ANISOU  284  CG2 VAL A 273     8231   8896  15917    651   -123  -2758       C  
ATOM    285  N   LYS A 274      16.254  16.884  25.046  1.00 87.56           N  
ANISOU  285  N   LYS A 274     8749   8745  15776    766   -283  -2441       N  
ATOM    286  CA  LYS A 274      14.909  16.319  24.926  1.00 89.29           C  
ANISOU  286  CA  LYS A 274     9136   8937  15854    745   -254  -2355       C  
ATOM    287  C   LYS A 274      13.849  17.078  25.734  1.00 92.56           C  
ANISOU  287  C   LYS A 274     9706   9383  16078    748   -326  -2204       C  
ATOM    288  O   LYS A 274      14.028  17.354  26.925  1.00 98.46           O  
ANISOU  288  O   LYS A 274    10479  10092  16840    825   -509  -2094       O  
ATOM    289  CB  LYS A 274      14.918  14.855  25.358  1.00 90.31           C  
ANISOU  289  CB  LYS A 274     9287   8914  16111    821   -382  -2306       C  
ATOM    290  CG  LYS A 274      13.608  14.129  25.114  1.00 93.15           C  
ANISOU  290  CG  LYS A 274     9807   9234  16353    788   -337  -2238       C  
ATOM    291  CD  LYS A 274      13.493  12.894  25.993  1.00 94.80           C  
ANISOU  291  CD  LYS A 274    10079   9285  16655    876   -516  -2130       C  
ATOM    292  CE  LYS A 274      12.213  12.128  25.696  1.00 94.10           C  
ANISOU  292  CE  LYS A 274    10141   9150  16462    830   -459  -2072       C  
ATOM    293  NZ  LYS A 274      12.013  10.970  26.611  1.00 96.53           N  
ANISOU  293  NZ  LYS A 274    10536   9302  16838    907   -629  -1950       N  
ATOM    294  N   PHE A 275      12.734  17.397  25.081  1.00 81.20           N  
ANISOU  294  N   PHE A 275     8381   8013  14458    661   -185  -2198       N  
ATOM    295  CA  PHE A 275      11.638  18.107  25.732  1.00 72.97           C  
ANISOU  295  CA  PHE A 275     7491   7002  13232    646   -230  -2065       C  
ATOM    296  C   PHE A 275      10.437  17.205  25.997  1.00 73.14           C  
ANISOU  296  C   PHE A 275     7673   6959  13159    629   -272  -1939       C  
ATOM    297  O   PHE A 275      10.127  16.309  25.208  1.00 70.84           O  
ANISOU  297  O   PHE A 275     7388   6607  12922    602   -184  -2015       O  
ATOM    298  CB  PHE A 275      11.178  19.296  24.884  1.00 67.56           C  
ANISOU  298  CB  PHE A 275     6839   6499  12331    523    -55  -2104       C  
ATOM    299  CG  PHE A 275      12.241  20.319  24.622  1.00 70.41           C  
ANISOU  299  CG  PHE A 275     7064   6939  12752    519      5  -2215       C  
ATOM    300  CD1 PHE A 275      13.080  20.200  23.524  1.00 68.72           C  
ANISOU  300  CD1 PHE A 275     6725   6751  12637    475    155  -2382       C  
ATOM    301  CD2 PHE A 275      12.382  21.420  25.454  1.00 69.58           C  
ANISOU  301  CD2 PHE A 275     6973   6922  12544    525    -84  -2116       C  
ATOM    302  CE1 PHE A 275      14.054  21.150  23.271  1.00 71.71           C  
ANISOU  302  CE1 PHE A 275     6984   7212  13049    447    220  -2468       C  
ATOM    303  CE2 PHE A 275      13.352  22.373  25.207  1.00 69.51           C  
ANISOU  303  CE2 PHE A 275     6836   6980  12594    514    -25  -2221       C  
ATOM    304  CZ  PHE A 275      14.191  22.237  24.113  1.00 71.52           C  
ANISOU  304  CZ  PHE A 275     6956   7236  12981    478    132  -2405       C  
ATOM    305  N   ASN A 276       9.765  17.453  27.116  1.00 73.94           N  
ANISOU  305  N   ASN A 276     7907   7076  13111    637   -401  -1747       N  
ATOM    306  CA  ASN A 276       8.443  16.890  27.367  1.00 73.19           C  
ANISOU  306  CA  ASN A 276     7978   6957  12875    589   -410  -1614       C  
ATOM    307  C   ASN A 276       7.460  17.984  27.775  1.00 75.40           C  
ANISOU  307  C   ASN A 276     8381   7387  12881    510   -392  -1478       C  
ATOM    308  O   ASN A 276       7.688  18.703  28.748  1.00 77.94           O  
ANISOU  308  O   ASN A 276     8730   7747  13135    544   -499  -1378       O  
ATOM    309  CB  ASN A 276       8.509  15.802  28.437  1.00 69.21           C  
ANISOU  309  CB  ASN A 276     7535   6275  12485    684   -588  -1504       C  
ATOM    310  CG  ASN A 276       8.801  14.443  27.850  1.00 74.56           C  
ANISOU  310  CG  ASN A 276     8155   6796  13378    725   -569  -1611       C  
ATOM    311  OD1 ASN A 276       7.893  13.636  27.649  1.00 79.11           O  
ANISOU  311  OD1 ASN A 276     8828   7314  13917    683   -532  -1571       O  
ATOM    312  ND2 ASN A 276      10.067  14.187  27.551  1.00 77.84           N  
ANISOU  312  ND2 ASN A 276     8410   7175  13992    791   -585  -1739       N  
ATOM    313  N   TRP A 277       6.376  18.113  27.015  1.00 68.90           N  
ANISOU  313  N   TRP A 277     7629   6644  11905    406   -262  -1482       N  
ATOM    314  CA  TRP A 277       5.380  19.143  27.282  1.00 66.08           C  
ANISOU  314  CA  TRP A 277     7377   6428  11302    328   -234  -1368       C  
ATOM    315  C   TRP A 277       4.154  18.567  27.969  1.00 74.63           C  
ANISOU  315  C   TRP A 277     8607   7461  12289    302   -281  -1213       C  
ATOM    316  O   TRP A 277       3.721  17.457  27.661  1.00 81.38           O  
ANISOU  316  O   TRP A 277     9489   8213  13221    294   -262  -1229       O  
ATOM    317  CB  TRP A 277       4.963  19.842  25.987  1.00 63.11           C  
ANISOU  317  CB  TRP A 277     6985   6186  10810    226    -66  -1473       C  
ATOM    318  CG  TRP A 277       6.022  20.722  25.414  1.00 68.18           C  
ANISOU  318  CG  TRP A 277     7511   6905  11488    228      0  -1601       C  
ATOM    319  CD1 TRP A 277       7.005  20.354  24.544  1.00 71.71           C  
ANISOU  319  CD1 TRP A 277     7835   7306  12105    248     77  -1775       C  
ATOM    320  CD2 TRP A 277       6.218  22.119  25.673  1.00 72.24           C  
ANISOU  320  CD2 TRP A 277     8022   7553  11874    206      4  -1568       C  
ATOM    321  NE1 TRP A 277       7.799  21.436  24.239  1.00 76.22           N  
ANISOU  321  NE1 TRP A 277     8324   7973  12662    233    136  -1854       N  
ATOM    322  CE2 TRP A 277       7.336  22.530  24.921  1.00 73.37           C  
ANISOU  322  CE2 TRP A 277     8036   7722  12118    208     87  -1727       C  
ATOM    323  CE3 TRP A 277       5.557  23.063  26.467  1.00 73.11           C  
ANISOU  323  CE3 TRP A 277     8224   7758  11797    181    -48  -1424       C  
ATOM    324  CZ2 TRP A 277       7.806  23.841  24.937  1.00 69.25           C  
ANISOU  324  CZ2 TRP A 277     7479   7317  11517    184    116  -1742       C  
ATOM    325  CZ3 TRP A 277       6.027  24.366  26.481  1.00 70.20           C  
ANISOU  325  CZ3 TRP A 277     7820   7504  11347    164    -26  -1441       C  
ATOM    326  CH2 TRP A 277       7.138  24.741  25.721  1.00 66.17           C  
ANISOU  326  CH2 TRP A 277     7184   7016  10941    164     54  -1596       C  
ATOM    327  N   TYR A 278       3.596  19.328  28.905  1.00 76.68           N  
ANISOU  327  N   TYR A 278     8961   7789  12383    286   -333  -1067       N  
ATOM    328  CA  TYR A 278       2.402  18.897  29.622  1.00 77.80           C  
ANISOU  328  CA  TYR A 278     9245   7891  12423    252   -360   -917       C  
ATOM    329  C   TYR A 278       1.382  20.022  29.763  1.00 72.99           C  
ANISOU  329  C   TYR A 278     8710   7432  11592    170   -300   -836       C  
ATOM    330  O   TYR A 278       1.722  21.153  30.117  1.00 70.82           O  
ANISOU  330  O   TYR A 278     8426   7259  11225    177   -320   -812       O  
ATOM    331  CB  TYR A 278       2.772  18.359  31.006  1.00 81.36           C  
ANISOU  331  CB  TYR A 278     9771   8215  12928    337   -518   -789       C  
ATOM    332  CG  TYR A 278       3.836  17.285  30.983  1.00 79.50           C  
ANISOU  332  CG  TYR A 278     9460   7820  12926    433   -604   -861       C  
ATOM    333  CD1 TYR A 278       5.185  17.616  31.048  1.00 78.82           C  
ANISOU  333  CD1 TYR A 278     9256   7726  12965    516   -678   -942       C  
ATOM    334  CD2 TYR A 278       3.494  15.940  30.900  1.00 76.75           C  
ANISOU  334  CD2 TYR A 278     9153   7322  12685    442   -614   -854       C  
ATOM    335  CE1 TYR A 278       6.162  16.639  31.026  1.00 83.28           C  
ANISOU  335  CE1 TYR A 278     9740   8140  13764    610   -762  -1016       C  
ATOM    336  CE2 TYR A 278       4.466  14.957  30.879  1.00 79.24           C  
ANISOU  336  CE2 TYR A 278     9399   7484  13225    535   -697   -923       C  
ATOM    337  CZ  TYR A 278       5.797  15.310  30.942  1.00 81.99           C  
ANISOU  337  CZ  TYR A 278     9623   7827  13701    622   -773  -1005       C  
ATOM    338  OH  TYR A 278       6.765  14.330  30.920  1.00 85.30           O  
ANISOU  338  OH  TYR A 278     9961   8088  14363    721   -860  -1081       O  
ATOM    339  N   VAL A 279       0.125  19.701  29.479  1.00 76.83           N  
ANISOU  339  N   VAL A 279     9265   7925  12003     92   -229   -799       N  
ATOM    340  CA  VAL A 279      -0.972  20.632  29.697  1.00 68.63           C  
ANISOU  340  CA  VAL A 279     8297   7006  10773     18   -179   -715       C  
ATOM    341  C   VAL A 279      -1.852  20.091  30.817  1.00 72.55           C  
ANISOU  341  C   VAL A 279     8920   7423  11223      7   -220   -559       C  
ATOM    342  O   VAL A 279      -2.532  19.076  30.649  1.00 74.69           O  
ANISOU  342  O   VAL A 279     9225   7602  11552    -25   -192   -548       O  
ATOM    343  CB  VAL A 279      -1.805  20.848  28.420  1.00 58.51           C  
ANISOU  343  CB  VAL A 279     6988   5810   9435    -73    -60   -806       C  
ATOM    344  CG1 VAL A 279      -2.906  21.865  28.675  1.00 56.16           C  
ANISOU  344  CG1 VAL A 279     6750   5631   8955   -140    -21   -723       C  
ATOM    345  CG2 VAL A 279      -0.910  21.300  27.272  1.00 52.13           C  
ANISOU  345  CG2 VAL A 279     6076   5066   8666    -70     -6   -965       C  
ATOM    346  N   ASP A 280      -1.819  20.771  31.961  1.00 77.81           N  
ANISOU  346  N   ASP A 280     9660   8118  11785     31   -280   -440       N  
ATOM    347  CA  ASP A 280      -2.500  20.314  33.170  1.00 78.74           C  
ANISOU  347  CA  ASP A 280     9917   8151  11848     25   -320   -285       C  
ATOM    348  C   ASP A 280      -2.127  18.872  33.510  1.00 80.49           C  
ANISOU  348  C   ASP A 280    10176   8186  12219     77   -393   -262       C  
ATOM    349  O   ASP A 280      -2.987  18.066  33.862  1.00 89.11           O  
ANISOU  349  O   ASP A 280    11359   9188  13311     37   -367   -186       O  
ATOM    350  CB  ASP A 280      -4.022  20.449  33.027  1.00 79.36           C  
ANISOU  350  CB  ASP A 280    10047   8282  11824    -77   -210   -239       C  
ATOM    351  CG  ASP A 280      -4.520  21.849  33.353  1.00 80.36           C  
ANISOU  351  CG  ASP A 280    10198   8557  11778   -114   -172   -191       C  
ATOM    352  OD1 ASP A 280      -3.809  22.586  34.071  1.00 82.94           O  
ANISOU  352  OD1 ASP A 280    10549   8921  12043    -62   -241   -148       O  
ATOM    353  OD2 ASP A 280      -5.627  22.209  32.899  1.00 76.98           O  
ANISOU  353  OD2 ASP A 280     9763   8204  11283   -193    -78   -199       O  
ATOM    354  N   GLY A 281      -0.842  18.550  33.396  1.00 79.92           N  
ANISOU  354  N   GLY A 281    10030   8051  12283    166   -482   -332       N  
ATOM    355  CA  GLY A 281      -0.344  17.248  33.804  1.00 82.75           C  
ANISOU  355  CA  GLY A 281    10424   8223  12794    233   -577   -309       C  
ATOM    356  C   GLY A 281      -0.365  16.196  32.711  1.00 83.14           C  
ANISOU  356  C   GLY A 281    10393   8196  13002    221   -518   -428       C  
ATOM    357  O   GLY A 281       0.334  15.187  32.805  1.00 86.76           O  
ANISOU  357  O   GLY A 281    10837   8505  13623    293   -599   -453       O  
ATOM    358  N   VAL A 282      -1.166  16.425  31.676  1.00 77.82           N  
ANISOU  358  N   VAL A 282     9671   7616  12282    132   -386   -505       N  
ATOM    359  CA  VAL A 282      -1.272  15.476  30.570  1.00 75.37           C  
ANISOU  359  CA  VAL A 282     9293   7240  12103    109   -323   -626       C  
ATOM    360  C   VAL A 282      -0.291  15.824  29.447  1.00 75.07           C  
ANISOU  360  C   VAL A 282     9109   7265  12148    137   -286   -802       C  
ATOM    361  O   VAL A 282      -0.272  16.949  28.952  1.00 82.17           O  
ANISOU  361  O   VAL A 282     9959   8317  12943    101   -227   -852       O  
ATOM    362  CB  VAL A 282      -2.707  15.427  30.002  1.00 72.18           C  
ANISOU  362  CB  VAL A 282     8923   6887  11613     -5   -208   -623       C  
ATOM    363  CG1 VAL A 282      -2.792  14.417  28.874  1.00 71.51           C  
ANISOU  363  CG1 VAL A 282     8780   6727  11663    -29   -153   -752       C  
ATOM    364  CG2 VAL A 282      -3.707  15.076  31.099  1.00 69.23           C  
ANISOU  364  CG2 VAL A 282     8688   6447  11169    -43   -219   -458       C  
ATOM    365  N   GLU A 283       0.524  14.852  29.047  1.00 68.96           N  
ANISOU  365  N   GLU A 283     8269   6368  11565    198   -316   -897       N  
ATOM    366  CA  GLU A 283       1.545  15.097  28.034  1.00 72.17           C  
ANISOU  366  CA  GLU A 283     8535   6816  12070    226   -271  -1071       C  
ATOM    367  C   GLU A 283       0.934  15.332  26.656  1.00 71.01           C  
ANISOU  367  C   GLU A 283     8353   6766  11861    131   -125  -1192       C  
ATOM    368  O   GLU A 283       0.004  14.637  26.248  1.00 70.29           O  
ANISOU  368  O   GLU A 283     8310   6631  11766     70    -77  -1194       O  
ATOM    369  CB  GLU A 283       2.541  13.935  27.973  1.00 77.34           C  
ANISOU  369  CB  GLU A 283     9125   7301  12961    319   -335  -1149       C  
ATOM    370  CG  GLU A 283       3.712  14.183  27.030  1.00 80.65           C  
ANISOU  370  CG  GLU A 283     9388   7750  13504    355   -283  -1335       C  
ATOM    371  CD  GLU A 283       4.766  13.095  27.095  1.00 92.20           C  
ANISOU  371  CD  GLU A 283    10773   9040  15220    460   -358  -1411       C  
ATOM    372  OE1 GLU A 283       5.530  12.946  26.116  1.00 93.37           O  
ANISOU  372  OE1 GLU A 283    10797   9181  15500    474   -280  -1587       O  
ATOM    373  OE2 GLU A 283       4.834  12.390  28.125  1.00 98.20           O  
ANISOU  373  OE2 GLU A 283    11600   9663  16047    527   -494  -1296       O  
ATOM    374  N   VAL A 284       1.461  16.332  25.953  1.00 73.27           N  
ANISOU  374  N   VAL A 284     8562   7180  12098    115    -60  -1293       N  
ATOM    375  CA  VAL A 284       1.064  16.615  24.577  1.00 70.62           C  
ANISOU  375  CA  VAL A 284     8202   6932  11699     30     71  -1421       C  
ATOM    376  C   VAL A 284       2.271  16.463  23.653  1.00 65.53           C  
ANISOU  376  C   VAL A 284     7441   6265  11192     65    131  -1603       C  
ATOM    377  O   VAL A 284       3.416  16.459  24.111  1.00 65.72           O  
ANISOU  377  O   VAL A 284     7386   6242  11343    151     73  -1626       O  
ATOM    378  CB  VAL A 284       0.463  18.026  24.437  1.00 68.28           C  
ANISOU  378  CB  VAL A 284     7939   6813  11190    -40    118  -1380       C  
ATOM    379  CG1 VAL A 284      -0.792  18.149  25.289  1.00 63.73           C  
ANISOU  379  CG1 VAL A 284     7469   6255  10490    -79     77  -1216       C  
ATOM    380  CG2 VAL A 284       1.479  19.080  24.835  1.00 62.51           C  
ANISOU  380  CG2 VAL A 284     7151   6160  10439      9     90  -1382       C  
ATOM    381  N   HIS A 285       2.023  16.340  22.353  1.00 65.74           N  
ANISOU  381  N   HIS A 285     7458   6322  11198     -4    248  -1737       N  
ATOM    382  CA  HIS A 285       3.087  15.952  21.428  1.00 70.01           C  
ANISOU  382  CA  HIS A 285     7900   6813  11886     22    325  -1921       C  
ATOM    383  C   HIS A 285       3.205  16.826  20.177  1.00 67.83           C  
ANISOU  383  C   HIS A 285     7613   6663  11497    -57    464  -2054       C  
ATOM    384  O   HIS A 285       3.895  16.455  19.228  1.00 64.26           O  
ANISOU  384  O   HIS A 285     7102   6171  11144    -60    561  -2220       O  
ATOM    385  CB  HIS A 285       2.885  14.495  21.004  1.00 76.52           C  
ANISOU  385  CB  HIS A 285     8733   7488  12855     29    336  -1988       C  
ATOM    386  CG  HIS A 285       2.795  13.541  22.154  1.00 81.97           C  
ANISOU  386  CG  HIS A 285     9448   8034  13662    102    205  -1864       C  
ATOM    387  ND1 HIS A 285       3.896  12.891  22.669  1.00 84.02           N  
ANISOU  387  ND1 HIS A 285     9628   8165  14130    212    129  -1891       N  
ATOM    388  CD2 HIS A 285       1.736  13.131  22.892  1.00 80.14           C  
ANISOU  388  CD2 HIS A 285     9319   7762  13370     80    137  -1714       C  
ATOM    389  CE1 HIS A 285       3.518  12.122  23.674  1.00 83.57           C  
ANISOU  389  CE1 HIS A 285     9639   7992  14123    254     13  -1755       C  
ATOM    390  NE2 HIS A 285       2.213  12.248  23.830  1.00 80.41           N  
ANISOU  390  NE2 HIS A 285     9351   7643  13560    172     25  -1647       N  
ATOM    391  N   ASN A 286       2.549  17.983  20.178  1.00 68.41           N  
ANISOU  391  N   ASN A 286     7750   6880  11365   -120    478  -1982       N  
ATOM    392  CA  ASN A 286       2.529  18.829  18.985  1.00 68.96           C  
ANISOU  392  CA  ASN A 286     7838   7062  11301   -202    602  -2093       C  
ATOM    393  C   ASN A 286       3.593  19.925  18.981  1.00 69.12           C  
ANISOU  393  C   ASN A 286     7789   7167  11308   -185    645  -2139       C  
ATOM    394  O   ASN A 286       3.596  20.788  18.101  1.00 70.59           O  
ANISOU  394  O   ASN A 286     8005   7454  11364   -257    746  -2212       O  
ATOM    395  CB  ASN A 286       1.148  19.466  18.817  1.00 68.68           C  
ANISOU  395  CB  ASN A 286     7916   7130  11050   -288    595  -2004       C  
ATOM    396  CG  ASN A 286       0.690  20.208  20.060  1.00 69.70           C  
ANISOU  396  CG  ASN A 286     8072   7321  11090   -265    496  -1825       C  
ATOM    397  OD1 ASN A 286       0.788  19.694  21.175  1.00 71.00           O  
ANISOU  397  OD1 ASN A 286     8221   7409  11347   -198    402  -1724       O  
ATOM    398  ND2 ASN A 286       0.187  21.423  19.872  1.00 67.96           N  
ANISOU  398  ND2 ASN A 286     7902   7235  10685   -321    518  -1787       N  
ATOM    399  N   ALA A 287       4.500  19.890  19.952  1.00 64.90           N  
ANISOU  399  N   ALA A 287     7165   6585  10910    -94    566  -2100       N  
ATOM    400  CA  ALA A 287       5.526  20.918  20.035  1.00 63.44           C  
ANISOU  400  CA  ALA A 287     6900   6472  10732    -76    597  -2143       C  
ATOM    401  C   ALA A 287       6.575  20.750  18.950  1.00 72.57           C  
ANISOU  401  C   ALA A 287     7965   7599  12007    -87    738  -2346       C  
ATOM    402  O   ALA A 287       6.972  19.633  18.613  1.00 78.41           O  
ANISOU  402  O   ALA A 287     8652   8230  12911    -53    759  -2433       O  
ATOM    403  CB  ALA A 287       6.180  20.905  21.391  1.00 59.27           C  
ANISOU  403  CB  ALA A 287     6305   5895  10321     26    456  -2046       C  
ATOM    404  N   LYS A 288       7.025  21.874  18.410  1.00 76.98           N  
ANISOU  404  N   LYS A 288     8510   8263  12474   -140    838  -2411       N  
ATOM    405  CA  LYS A 288       8.056  21.859  17.390  1.00 81.81           C  
ANISOU  405  CA  LYS A 288     9041   8894  13149   -169    980  -2560       C  
ATOM    406  C   LYS A 288       9.354  22.451  17.925  1.00 80.34           C  
ANISOU  406  C   LYS A 288     8711   8716  13097   -116    969  -2592       C  
ATOM    407  O   LYS A 288       9.399  23.597  18.378  1.00 74.17           O  
ANISOU  407  O   LYS A 288     7939   8004  12238   -123    953  -2556       O  
ATOM    408  CB  LYS A 288       7.575  22.601  16.143  1.00 83.96           C  
ANISOU  408  CB  LYS A 288     9424   9285  13190   -292   1118  -2600       C  
ATOM    409  CG  LYS A 288       6.299  21.993  15.578  1.00 89.34           C  
ANISOU  409  CG  LYS A 288    10241   9957  13746   -344   1113  -2573       C  
ATOM    410  CD  LYS A 288       5.916  22.562  14.226  1.00 93.07           C  
ANISOU  410  CD  LYS A 288    10828  10533  14002   -456   1235  -2617       C  
ATOM    411  CE  LYS A 288       4.751  21.772  13.641  1.00 94.66           C  
ANISOU  411  CE  LYS A 288    11143  10707  14116   -496   1214  -2603       C  
ATOM    412  NZ  LYS A 288       4.304  22.269  12.310  1.00 96.85           N  
ANISOU  412  NZ  LYS A 288    11550  11073  14175   -599   1307  -2638       N  
ATOM    413  N   THR A 289      10.404  21.637  17.889  1.00 82.22           N  
ANISOU  413  N   THR A 289     8814   8879  13545    -62    969  -2663       N  
ATOM    414  CA  THR A 289      11.713  22.030  18.383  1.00 81.47           C  
ANISOU  414  CA  THR A 289     8562   8778  13616    -10    943  -2703       C  
ATOM    415  C   THR A 289      12.562  22.580  17.245  1.00 83.76           C  
ANISOU  415  C   THR A 289     8797   9146  13882   -104   1124  -2824       C  
ATOM    416  O   THR A 289      12.674  21.963  16.185  1.00 86.37           O  
ANISOU  416  O   THR A 289     9138   9468  14211   -160   1241  -2907       O  
ATOM    417  CB  THR A 289      12.442  20.844  19.049  1.00 80.29           C  
ANISOU  417  CB  THR A 289     8289   8494  13725    100    821  -2709       C  
ATOM    418  OG1 THR A 289      11.788  20.507  20.278  1.00 78.63           O  
ANISOU  418  OG1 THR A 289     8135   8206  13537    190    637  -2577       O  
ATOM    419  CG2 THR A 289      13.890  21.196  19.341  1.00 79.99           C  
ANISOU  419  CG2 THR A 289     8075   8449  13867    136    804  -2776       C  
ATOM    420  N   LYS A 290      13.147  23.751  17.460  1.00 79.53           N  
ANISOU  420  N   LYS A 290     8213   8682  13325   -125   1148  -2833       N  
ATOM    421  CA  LYS A 290      14.002  24.352  16.451  1.00 82.68           C  
ANISOU  421  CA  LYS A 290     8564   9144  13705   -223   1319  -2940       C  
ATOM    422  C   LYS A 290      15.359  23.658  16.409  1.00 93.75           C  
ANISOU  422  C   LYS A 290     9783  10463  15374   -188   1328  -3043       C  
ATOM    423  O   LYS A 290      15.844  23.181  17.437  1.00 93.61           O  
ANISOU  423  O   LYS A 290     9653  10363  15552    -79   1173  -3019       O  
ATOM    424  CB  LYS A 290      14.173  25.847  16.717  1.00 75.37           C  
ANISOU  424  CB  LYS A 290     7651   8316  12672   -264   1340  -2913       C  
ATOM    425  CG  LYS A 290      13.309  26.705  15.815  1.00 74.88           C  
ANISOU  425  CG  LYS A 290     7764   8362  12323   -379   1461  -2889       C  
ATOM    426  CD  LYS A 290      13.356  28.167  16.196  1.00 77.69           C  
ANISOU  426  CD  LYS A 290     8146   8808  12563   -411   1463  -2846       C  
ATOM    427  CE  LYS A 290      12.491  28.980  15.251  1.00 77.41           C  
ANISOU  427  CE  LYS A 290     8297   8875  12240   -527   1570  -2815       C  
ATOM    428  NZ  LYS A 290      12.507  30.427  15.585  1.00 81.21           N  
ANISOU  428  NZ  LYS A 290     8815   9444  12599   -562   1574  -2769       N  
ATOM    429  N   PRO A 291      15.966  23.579  15.211  1.00 98.30           N  
ANISOU  429  N   PRO A 291    10337  11055  15958   -282   1505  -3158       N  
ATOM    430  CA  PRO A 291      17.340  23.078  15.130  1.00 93.94           C  
ANISOU  430  CA  PRO A 291     9603  10427  15664   -265   1529  -3270       C  
ATOM    431  C   PRO A 291      18.265  23.964  15.948  1.00 90.85           C  
ANISOU  431  C   PRO A 291     9086  10042  15389   -238   1459  -3275       C  
ATOM    432  O   PRO A 291      18.328  25.177  15.743  1.00 88.69           O  
ANISOU  432  O   PRO A 291     8856   9856  14987   -313   1536  -3271       O  
ATOM    433  CB  PRO A 291      17.664  23.148  13.632  1.00 93.44           C  
ANISOU  433  CB  PRO A 291     9579  10398  15527   -396   1756  -3381       C  
ATOM    434  CG  PRO A 291      16.696  24.127  13.074  1.00 97.27           C  
ANISOU  434  CG  PRO A 291    10252  10995  15709   -487   1838  -3317       C  
ATOM    435  CD  PRO A 291      15.449  23.982  13.893  1.00 99.18           C  
ANISOU  435  CD  PRO A 291    10595  11247  15842   -410   1683  -3187       C  
ATOM    436  N   ARG A 292      18.936  23.333  16.901  1.00 92.84           N  
ANISOU  436  N   ARG A 292     9196  10197  15880   -127   1298  -3276       N  
ATOM    437  CA  ARG A 292      19.863  23.970  17.825  1.00 98.10           C  
ANISOU  437  CA  ARG A 292     9734  10846  16694    -78   1185  -3279       C  
ATOM    438  C   ARG A 292      20.814  24.968  17.146  1.00 95.63           C  
ANISOU  438  C   ARG A 292     9360  10582  16392   -190   1345  -3386       C  
ATOM    439  O   ARG A 292      21.388  24.671  16.097  1.00 94.84           O  
ANISOU  439  O   ARG A 292     9223  10463  16348   -273   1511  -3503       O  
ATOM    440  CB  ARG A 292      20.634  22.861  18.538  1.00105.68           C  
ANISOU  440  CB  ARG A 292    10546  11673  17933     36   1025  -3305       C  
ATOM    441  CG  ARG A 292      21.916  23.263  19.177  1.00112.23           C  
ANISOU  441  CG  ARG A 292    11212  12458  18971     69    936  -3361       C  
ATOM    442  CD  ARG A 292      22.662  22.036  19.676  1.00118.78           C  
ANISOU  442  CD  ARG A 292    11908  13150  20073    170    792  -3399       C  
ATOM    443  NE  ARG A 292      23.257  21.273  18.583  1.00120.47           N  
ANISOU  443  NE  ARG A 292    12048  13317  20408    109    952  -3540       N  
ATOM    444  CZ  ARG A 292      23.042  19.978  18.379  1.00119.80           C  
ANISOU  444  CZ  ARG A 292    11961  13155  20404    156    931  -3551       C  
ATOM    445  NH1 ARG A 292      22.246  19.302  19.197  1.00123.17           N  
ANISOU  445  NH1 ARG A 292    12461  13537  20800    260    755  -3425       N  
ATOM    446  NH2 ARG A 292      23.624  19.356  17.362  1.00115.85           N  
ANISOU  446  NH2 ARG A 292    11389  12614  20013     96   1087  -3686       N  
ATOM    447  N   GLU A 293      20.960  26.155  17.735  1.00 97.02           N  
ANISOU  447  N   GLU A 293     9536  10816  16512   -196   1299  -3344       N  
ATOM    448  CA  GLU A 293      21.747  27.228  17.119  1.00103.53           C  
ANISOU  448  CA  GLU A 293    10330  11687  17318   -310   1452  -3432       C  
ATOM    449  C   GLU A 293      22.953  27.644  17.960  1.00105.19           C  
ANISOU  449  C   GLU A 293    10378  11843  17748   -261   1340  -3479       C  
ATOM    450  O   GLU A 293      22.868  27.728  19.187  1.00103.09           O  
ANISOU  450  O   GLU A 293    10080  11558  17533   -151   1133  -3393       O  
ATOM    451  CB  GLU A 293      20.864  28.452  16.849  1.00 99.00           C  
ANISOU  451  CB  GLU A 293     9923  11240  16453   -389   1533  -3354       C  
ATOM    452  CG  GLU A 293      20.272  29.102  18.093  1.00 97.42           C  
ANISOU  452  CG  GLU A 293     9758  11083  16176   -303   1356  -3225       C  
ATOM    453  CD  GLU A 293      19.358  30.265  17.763  1.00101.03           C  
ANISOU  453  CD  GLU A 293    10382  11663  16344   -384   1442  -3153       C  
ATOM    454  OE1 GLU A 293      19.560  31.367  18.321  1.00 98.79           O  
ANISOU  454  OE1 GLU A 293    10090  11428  16020   -388   1403  -3122       O  
ATOM    455  OE2 GLU A 293      18.443  30.085  16.932  1.00105.68           O  
ANISOU  455  OE2 GLU A 293    11116  12297  16743   -445   1545  -3129       O  
ATOM    456  N   GLU A 294      24.073  27.909  17.293  1.00107.47           N  
ANISOU  456  N   GLU A 294    10571  12100  18162   -345   1476  -3616       N  
ATOM    457  CA  GLU A 294      25.300  28.316  17.979  1.00107.43           C  
ANISOU  457  CA  GLU A 294    10409  12032  18377   -310   1385  -3682       C  
ATOM    458  C   GLU A 294      25.179  29.687  18.626  1.00103.63           C  
ANISOU  458  C   GLU A 294     9975  11626  17772   -315   1331  -3612       C  
ATOM    459  O   GLU A 294      24.524  30.588  18.097  1.00103.22           O  
ANISOU  459  O   GLU A 294    10061  11676  17480   -405   1457  -3570       O  
ATOM    460  CB  GLU A 294      26.484  28.326  17.011  1.00110.77           C  
ANISOU  460  CB  GLU A 294    10730  12401  18957   -412   1571  -3855       C  
ATOM    461  CG  GLU A 294      27.134  26.978  16.803  1.00116.37           C  
ANISOU  461  CG  GLU A 294    11305  12994  19914   -369   1556  -3953       C  
ATOM    462  CD  GLU A 294      28.570  27.097  16.338  1.00122.43           C  
ANISOU  462  CD  GLU A 294    11918  13682  20917   -432   1666  -4127       C  
ATOM    463  OE1 GLU A 294      29.071  28.239  16.263  1.00126.53           O  
ANISOU  463  OE1 GLU A 294    12435  14230  21410   -503   1740  -4166       O  
ATOM    464  OE2 GLU A 294      29.196  26.055  16.053  1.00123.22           O  
ANISOU  464  OE2 GLU A 294    11900  13685  21232   -412   1681  -4227       O  
ATOM    465  N   GLN A 295      25.830  29.849  19.770  1.00105.51           N  
ANISOU  465  N   GLN A 295    10102  11811  18174   -217   1136  -3599       N  
ATOM    466  CA  GLN A 295      25.744  31.107  20.492  1.00110.37           C  
ANISOU  466  CA  GLN A 295    10756  12494  18686   -209   1064  -3529       C  
ATOM    467  C   GLN A 295      27.045  31.885  20.530  1.00125.93           C  
ANISOU  467  C   GLN A 295    12609  14426  20814   -248   1098  -3643       C  
ATOM    468  O   GLN A 295      28.081  31.446  20.019  1.00128.33           O  
ANISOU  468  O   GLN A 295    12791  14643  21328   -282   1177  -3784       O  
ATOM    469  CB  GLN A 295      25.264  30.861  21.923  1.00105.48           C  
ANISOU  469  CB  GLN A 295    10139  11862  18077    -60    790  -3391       C  
ATOM    470  CG  GLN A 295      23.960  31.558  22.235  1.00102.47           C  
ANISOU  470  CG  GLN A 295     9918  11596  17419    -59    771  -3245       C  
ATOM    471  CD  GLN A 295      22.899  31.275  21.190  1.00 98.55           C  
ANISOU  471  CD  GLN A 295     9560  11164  16722   -137    946  -3226       C  
ATOM    472  OE1 GLN A 295      22.798  30.161  20.674  1.00102.43           O  
ANISOU  472  OE1 GLN A 295    10040  11600  17279   -131    985  -3263       O  
ATOM    473  NE2 GLN A 295      22.106  32.287  20.866  1.00 92.50           N  
ANISOU  473  NE2 GLN A 295     8928  10511  15706   -211   1047  -3168       N  
ATOM    474  N   TYR A 296      26.943  33.068  21.123  1.00135.17           N  
ANISOU  474  N   TYR A 296    13822  15662  21876   -246   1046  -3580       N  
ATOM    475  CA  TYR A 296      28.061  33.939  21.455  1.00144.62           C  
ANISOU  475  CA  TYR A 296    14917  16827  23204   -258   1031  -3658       C  
ATOM    476  C   TYR A 296      29.200  33.166  22.125  1.00142.24           C  
ANISOU  476  C   TYR A 296    14431  16390  23222   -162    865  -3737       C  
ATOM    477  O   TYR A 296      30.367  33.271  21.732  1.00136.66           O  
ANISOU  477  O   TYR A 296    13602  15611  22712   -208    950  -3884       O  
ATOM    478  CB  TYR A 296      27.538  35.061  22.366  1.00152.06           C  
ANISOU  478  CB  TYR A 296    15936  17860  23980   -221    915  -3532       C  
ATOM    479  CG  TYR A 296      28.452  35.425  23.501  1.00158.98           C  
ANISOU  479  CG  TYR A 296    16691  18679  25034   -133    717  -3540       C  
ATOM    480  CD1 TYR A 296      29.433  36.392  23.336  1.00159.28           C  
ANISOU  480  CD1 TYR A 296    16661  18705  25151   -193    800  -3640       C  
ATOM    481  CD2 TYR A 296      28.325  34.814  24.747  1.00162.96           C  
ANISOU  481  CD2 TYR A 296    17160  19136  25621     10    442  -3445       C  
ATOM    482  CE1 TYR A 296      30.269  36.725  24.369  1.00161.18           C  
ANISOU  482  CE1 TYR A 296    16792  18892  25555   -112    614  -3650       C  
ATOM    483  CE2 TYR A 296      29.158  35.137  25.781  1.00164.71           C  
ANISOU  483  CE2 TYR A 296    17286  19302  25995     87    248  -3448       C  
ATOM    484  CZ  TYR A 296      30.124  36.095  25.595  1.00163.83           C  
ANISOU  484  CZ  TYR A 296    17099  19183  25965     28    333  -3552       C  
ATOM    485  OH  TYR A 296      30.940  36.403  26.658  1.00165.44           O  
ANISOU  485  OH  TYR A 296    17209  19329  26322    109    127  -3554       O  
ATOM    486  N   ASN A 297      28.828  32.372  23.124  1.00142.45           N  
ANISOU  486  N   ASN A 297    14446  16379  23298    -30    628  -3636       N  
ATOM    487  CA  ASN A 297      29.731  31.482  23.836  1.00143.06           C  
ANISOU  487  CA  ASN A 297    14375  16325  23659     74    434  -3684       C  
ATOM    488  C   ASN A 297      30.208  30.383  22.869  1.00133.52           C  
ANISOU  488  C   ASN A 297    13080  15033  22617     33    567  -3815       C  
ATOM    489  O   ASN A 297      29.922  30.440  21.676  1.00137.21           O  
ANISOU  489  O   ASN A 297    13606  15549  22978    -82    809  -3871       O  
ATOM    490  CB  ASN A 297      29.003  30.916  25.083  1.00152.29           C  
ANISOU  490  CB  ASN A 297    15600  17482  24783    214    157  -3519       C  
ATOM    491  CG  ASN A 297      29.168  31.811  26.328  1.00148.47           C  
ANISOU  491  CG  ASN A 297    15123  17016  24272    284    -49  -3432       C  
ATOM    492  OD1 ASN A 297      30.312  32.140  26.669  1.00154.03           O  
ANISOU  492  OD1 ASN A 297    15706  17653  25165    299   -115  -3521       O  
ATOM    493  ND2 ASN A 297      28.060  32.222  27.012  1.00139.52           N  
ANISOU  493  ND2 ASN A 297    14128  15970  22912    325   -152  -3264       N  
ATOM    494  N   SER A 298      30.955  29.395  23.339  1.00124.51           N  
ANISOU  494  N   SER A 298    11806  13767  21734    120    413  -3867       N  
ATOM    495  CA  SER A 298      31.120  28.212  22.504  1.00114.24           C  
ANISOU  495  CA  SER A 298    10449  12401  20556     95    518  -3958       C  
ATOM    496  C   SER A 298      30.021  27.270  22.947  1.00115.58           C  
ANISOU  496  C   SER A 298    10718  12580  20619    184    382  -3814       C  
ATOM    497  O   SER A 298      30.273  26.152  23.392  1.00116.40           O  
ANISOU  497  O   SER A 298    10751  12582  20893    277    227  -3813       O  
ATOM    498  CB  SER A 298      32.511  27.593  22.634  1.00103.37           C  
ANISOU  498  CB  SER A 298     8872  10881  19525    132    450  -4105       C  
ATOM    499  OG  SER A 298      33.353  28.051  21.587  1.00100.09           O  
ANISOU  499  OG  SER A 298     8376  10451  19202      8    694  -4275       O  
ATOM    500  N   THR A 299      28.790  27.762  22.835  1.00113.95           N  
ANISOU  500  N   THR A 299    10678  12490  20126    155    440  -3692       N  
ATOM    501  CA  THR A 299      27.620  27.132  23.432  1.00110.13           C  
ANISOU  501  CA  THR A 299    10312  12027  19507    243    298  -3533       C  
ATOM    502  C   THR A 299      26.469  27.180  22.434  1.00103.40           C  
ANISOU  502  C   THR A 299     9605  11276  18408    155    505  -3497       C  
ATOM    503  O   THR A 299      26.462  27.997  21.511  1.00 97.10           O  
ANISOU  503  O   THR A 299     8848  10554  17491     32    723  -3558       O  
ATOM    504  CB  THR A 299      27.217  27.841  24.765  1.00105.21           C  
ANISOU  504  CB  THR A 299     9755  11440  18780    330     75  -3384       C  
ATOM    505  OG1 THR A 299      28.355  27.919  25.636  1.00110.92           O  
ANISOU  505  OG1 THR A 299    10351  12072  19721    399   -113  -3426       O  
ATOM    506  CG2 THR A 299      26.100  27.104  25.492  1.00 98.62           C  
ANISOU  506  CG2 THR A 299     9036  10600  17835    429    -92  -3220       C  
ATOM    507  N   TYR A 300      25.510  26.283  22.609  1.00113.36           N  
ANISOU  507  N   TYR A 300    10951  12528  19593    217    434  -3399       N  
ATOM    508  CA  TYR A 300      24.324  26.243  21.773  1.00116.93           C  
ANISOU  508  CA  TYR A 300    11552  13067  19811    149    599  -3354       C  
ATOM    509  C   TYR A 300      23.100  26.744  22.531  1.00110.25           C  
ANISOU  509  C   TYR A 300    10852  12297  18742    198    493  -3186       C  
ATOM    510  O   TYR A 300      23.054  26.688  23.763  1.00108.75           O  
ANISOU  510  O   TYR A 300    10657  12068  18596    309    263  -3087       O  
ATOM    511  CB  TYR A 300      24.071  24.821  21.289  1.00127.69           C  
ANISOU  511  CB  TYR A 300    12912  14359  21247    174    622  -3378       C  
ATOM    512  CG  TYR A 300      25.073  24.277  20.291  1.00140.64           C  
ANISOU  512  CG  TYR A 300    14429  15938  23070    107    777  -3549       C  
ATOM    513  CD1 TYR A 300      25.013  24.638  18.948  1.00145.52           C  
ANISOU  513  CD1 TYR A 300    15095  16620  23576    -33   1042  -3636       C  
ATOM    514  CD2 TYR A 300      26.054  23.370  20.681  1.00148.31           C  
ANISOU  514  CD2 TYR A 300    15247  16781  24323    182    655  -3619       C  
ATOM    515  CE1 TYR A 300      25.907  24.129  18.029  1.00150.67           C  
ANISOU  515  CE1 TYR A 300    15643  17212  24392    -98   1190  -3791       C  
ATOM    516  CE2 TYR A 300      26.958  22.859  19.765  1.00154.51           C  
ANISOU  516  CE2 TYR A 300    15915  17506  25285    120    803  -3781       C  
ATOM    517  CZ  TYR A 300      26.881  23.246  18.440  1.00154.84           C  
ANISOU  517  CZ  TYR A 300    16006  17616  25212    -21   1075  -3867       C  
ATOM    518  OH  TYR A 300      27.776  22.744  17.520  1.00157.48           O  
ANISOU  518  OH  TYR A 300    16229  17886  25719    -87   1231  -4028       O  
ATOM    519  N   ARG A 301      22.108  27.231  21.793  1.00102.98           N  
ANISOU  519  N   ARG A 301    10070  11480  17579    114    656  -3154       N  
ATOM    520  CA  ARG A 301      20.796  27.516  22.366  1.00 93.57           C  
ANISOU  520  CA  ARG A 301     9025  10351  16177    156    578  -3003       C  
ATOM    521  C   ARG A 301      19.752  26.701  21.618  1.00 84.72           C  
ANISOU  521  C   ARG A 301     8021   9235  14934    130    677  -2982       C  
ATOM    522  O   ARG A 301      19.801  26.590  20.391  1.00 85.14           O  
ANISOU  522  O   ARG A 301     8094   9316  14939     27    877  -3073       O  
ATOM    523  CB  ARG A 301      20.465  29.008  22.291  1.00 92.73           C  
ANISOU  523  CB  ARG A 301     8992  10368  15872     82    662  -2972       C  
ATOM    524  CG  ARG A 301      19.326  29.441  23.203  1.00 95.24           C  
ANISOU  524  CG  ARG A 301     9426  10740  16020    148    536  -2817       C  
ATOM    525  CD  ARG A 301      18.186  30.078  22.419  1.00 97.56           C  
ANISOU  525  CD  ARG A 301     9880  11146  16041     53    705  -2787       C  
ATOM    526  NE  ARG A 301      18.592  31.299  21.728  1.00 94.04           N  
ANISOU  526  NE  ARG A 301     9442  10792  15499    -67    867  -2851       N  
ATOM    527  CZ  ARG A 301      17.751  32.099  21.078  1.00 88.87           C  
ANISOU  527  CZ  ARG A 301     8929  10241  14596   -160   1004  -2824       C  
ATOM    528  NH1 ARG A 301      16.454  31.810  21.030  1.00 78.44           N  
ANISOU  528  NH1 ARG A 301     7750   8946  13107   -147    999  -2743       N  
ATOM    529  NH2 ARG A 301      18.205  33.190  20.475  1.00 91.34           N  
ANISOU  529  NH2 ARG A 301     9255  10623  14829   -270   1141  -2877       N  
ATOM    530  N   VAL A 302      18.814  26.118  22.354  1.00 77.45           N  
ANISOU  530  N   VAL A 302     7187   8281  13962    222    533  -2860       N  
ATOM    531  CA  VAL A 302      17.798  25.285  21.727  1.00 76.28           C  
ANISOU  531  CA  VAL A 302     7155   8121  13708    203    608  -2838       C  
ATOM    532  C   VAL A 302      16.397  25.627  22.245  1.00 73.03           C  
ANISOU  532  C   VAL A 302     6909   7752  13086    228    549  -2702       C  
ATOM    533  O   VAL A 302      16.163  25.777  23.451  1.00 71.74           O  
ANISOU  533  O   VAL A 302     6764   7558  12935    322    365  -2592       O  
ATOM    534  CB  VAL A 302      18.115  23.779  21.924  1.00 70.22           C  
ANISOU  534  CB  VAL A 302     6322   7220  13138    284    507  -2853       C  
ATOM    535  CG1 VAL A 302      18.118  23.397  23.402  1.00 65.31           C  
ANISOU  535  CG1 VAL A 302     5689   6510  12615    423    242  -2734       C  
ATOM    536  CG2 VAL A 302      17.155  22.911  21.118  1.00 75.23           C  
ANISOU  536  CG2 VAL A 302     7069   7843  13670    248    607  -2851       C  
ATOM    537  N   VAL A 303      15.468  25.768  21.307  1.00 72.99           N  
ANISOU  537  N   VAL A 303     7037   7815  12882    136    704  -2709       N  
ATOM    538  CA  VAL A 303      14.136  26.280  21.603  1.00 68.87           C  
ANISOU  538  CA  VAL A 303     6681   7344  12142    128    682  -2603       C  
ATOM    539  C   VAL A 303      13.044  25.340  21.097  1.00 73.08           C  
ANISOU  539  C   VAL A 303     7342   7839  12585    106    714  -2577       C  
ATOM    540  O   VAL A 303      13.109  24.850  19.967  1.00 71.14           O  
ANISOU  540  O   VAL A 303     7104   7603  12323     33    852  -2660       O  
ATOM    541  CB  VAL A 303      13.932  27.671  20.964  1.00 60.06           C  
ANISOU  541  CB  VAL A 303     5634   6369  10819     14    828  -2623       C  
ATOM    542  CG1 VAL A 303      12.541  28.193  21.252  1.00 53.82           C  
ANISOU  542  CG1 VAL A 303     5039   5674   9738    -33    769  -2447       C  
ATOM    543  CG2 VAL A 303      14.995  28.651  21.454  1.00 60.52           C  
ANISOU  543  CG2 VAL A 303     5565   6463  10966     28    803  -2654       C  
ATOM    544  N   SER A 304      12.048  25.076  21.936  1.00 76.28           N  
ANISOU  544  N   SER A 304     7867   8243  12873    135    564  -2399       N  
ATOM    545  CA  SER A 304      10.862  24.361  21.476  1.00 78.34           C  
ANISOU  545  CA  SER A 304     8264   8490  13013     94    593  -2354       C  
ATOM    546  C   SER A 304       9.614  25.206  21.710  1.00 71.77           C  
ANISOU  546  C   SER A 304     7595   7777  11898     27    567  -2201       C  
ATOM    547  O   SER A 304       9.461  25.849  22.751  1.00 65.49           O  
ANISOU  547  O   SER A 304     6827   7026  11029     57    446  -2068       O  
ATOM    548  CB  SER A 304      10.724  23.006  22.166  1.00 85.04           C  
ANISOU  548  CB  SER A 304     9103   9196  14011    187    454  -2297       C  
ATOM    549  OG  SER A 304      10.620  23.151  23.578  1.00 90.90           O  
ANISOU  549  OG  SER A 304     9873   9924  14742    260    261  -2133       O  
ATOM    550  N   VAL A 305       8.726  25.199  20.723  1.00 68.19           N  
ANISOU  550  N   VAL A 305     7248   7371  11289    -63    678  -2226       N  
ATOM    551  CA  VAL A 305       7.548  26.052  20.741  1.00 62.82           C  
ANISOU  551  CA  VAL A 305     6712   6806  10352   -134    672  -2108       C  
ATOM    552  C   VAL A 305       6.252  25.243  20.754  1.00 66.44           C  
ANISOU  552  C   VAL A 305     7281   7230  10732   -149    625  -2023       C  
ATOM    553  O   VAL A 305       5.977  24.477  19.829  1.00 62.27           O  
ANISOU  553  O   VAL A 305     6777   6655  10227   -185    704  -2114       O  
ATOM    554  CB  VAL A 305       7.544  26.988  19.526  1.00 61.42           C  
ANISOU  554  CB  VAL A 305     6582   6728  10029   -239    835  -2206       C  
ATOM    555  CG1 VAL A 305       6.357  27.921  19.584  1.00 56.55           C  
ANISOU  555  CG1 VAL A 305     6106   6223   9160   -302    811  -2083       C  
ATOM    556  CG2 VAL A 305       8.843  27.772  19.467  1.00 59.16           C  
ANISOU  556  CG2 VAL A 305     6181   6468   9830   -234    902  -2300       C  
ATOM    557  N   LEU A 306       5.460  25.409  21.807  1.00 62.88           N  
ANISOU  557  N   LEU A 306     6898   6799  10193   -126    501  -1854       N  
ATOM    558  CA  LEU A 306       4.179  24.725  21.897  1.00 56.47           C  
ANISOU  558  CA  LEU A 306     6187   5958   9311   -148    461  -1768       C  
ATOM    559  C   LEU A 306       3.036  25.654  21.515  1.00 59.54           C  
ANISOU  559  C   LEU A 306     6686   6466   9469   -234    498  -1709       C  
ATOM    560  O   LEU A 306       2.746  26.625  22.215  1.00 64.31           O  
ANISOU  560  O   LEU A 306     7326   7151   9957   -236    447  -1603       O  
ATOM    561  CB  LEU A 306       3.954  24.170  23.308  1.00 50.94           C  
ANISOU  561  CB  LEU A 306     5501   5184   8670    -71    312  -1621       C  
ATOM    562  CG  LEU A 306       2.654  23.386  23.518  1.00 51.74           C  
ANISOU  562  CG  LEU A 306     5698   5240   8721    -95    276  -1527       C  
ATOM    563  CD1 LEU A 306       2.701  22.046  22.793  1.00 56.12           C  
ANISOU  563  CD1 LEU A 306     6228   5678   9415    -92    316  -1628       C  
ATOM    564  CD2 LEU A 306       2.359  23.190  24.997  1.00 44.07           C  
ANISOU  564  CD2 LEU A 306     4772   4222   7751    -38    144  -1361       C  
ATOM    565  N   THR A 307       2.396  25.358  20.389  1.00 56.51           N  
ANISOU  565  N   THR A 307     6359   6090   9023   -305    579  -1783       N  
ATOM    566  CA  THR A 307       1.196  26.079  19.992  1.00 49.98           C  
ANISOU  566  CA  THR A 307     5639   5358   7995   -382    592  -1730       C  
ATOM    567  C   THR A 307       0.084  25.763  20.989  1.00 47.50           C  
ANISOU  567  C   THR A 307     5374   5025   7650   -364    488  -1575       C  
ATOM    568  O   THR A 307      -0.156  24.598  21.309  1.00 53.70           O  
ANISOU  568  O   THR A 307     6150   5707   8546   -335    447  -1554       O  
ATOM    569  CB  THR A 307       0.751  25.710  18.561  1.00 49.28           C  
ANISOU  569  CB  THR A 307     5607   5263   7855   -458    683  -1848       C  
ATOM    570  OG1 THR A 307       1.649  26.297  17.611  1.00 48.94           O  
ANISOU  570  OG1 THR A 307     5550   5260   7786   -494    798  -1980       O  
ATOM    571  CG2 THR A 307      -0.649  26.218  18.292  1.00 51.69           C  
ANISOU  571  CG2 THR A 307     6018   5640   7982   -524    656  -1778       C  
ATOM    572  N   VAL A 308      -0.580  26.799  21.495  1.00 42.15           N  
ANISOU  572  N   VAL A 308     4747   4441   6826   -385    453  -1469       N  
ATOM    573  CA  VAL A 308      -1.636  26.609  22.485  1.00 37.99           C  
ANISOU  573  CA  VAL A 308     4267   3901   6265   -375    373  -1325       C  
ATOM    574  C   VAL A 308      -2.982  27.145  22.003  1.00 43.94           C  
ANISOU  574  C   VAL A 308     5095   4728   6870   -448    386  -1293       C  
ATOM    575  O   VAL A 308      -3.048  27.995  21.113  1.00 46.94           O  
ANISOU  575  O   VAL A 308     5504   5190   7140   -498    435  -1354       O  
ATOM    576  CB  VAL A 308      -1.275  27.281  23.818  1.00 41.23           C  
ANISOU  576  CB  VAL A 308     4669   4340   6655   -319    302  -1209       C  
ATOM    577  CG1 VAL A 308       0.106  26.842  24.267  1.00 44.03           C  
ANISOU  577  CG1 VAL A 308     4944   4623   7163   -243    271  -1247       C  
ATOM    578  CG2 VAL A 308      -1.321  28.786  23.680  1.00 40.79           C  
ANISOU  578  CG2 VAL A 308     4639   4413   6448   -353    327  -1195       C  
ATOM    579  N   LEU A 309      -4.055  26.622  22.587  1.00 48.68           N  
ANISOU  579  N   LEU A 309     5727   5292   7477   -455    341  -1201       N  
ATOM    580  CA  LEU A 309      -5.397  27.103  22.293  1.00 45.58           C  
ANISOU  580  CA  LEU A 309     5388   4959   6970   -517    338  -1163       C  
ATOM    581  C   LEU A 309      -5.662  28.354  23.115  1.00 39.46           C  
ANISOU  581  C   LEU A 309     4636   4277   6081   -508    312  -1060       C  
ATOM    582  O   LEU A 309      -5.366  28.380  24.312  1.00 38.07           O  
ANISOU  582  O   LEU A 309     4453   4082   5931   -458    274   -967       O  
ATOM    583  CB  LEU A 309      -6.439  26.024  22.594  1.00 41.34           C  
ANISOU  583  CB  LEU A 309     4863   4339   6504   -534    313  -1115       C  
ATOM    584  CG  LEU A 309      -6.274  24.716  21.817  1.00 47.26           C  
ANISOU  584  CG  LEU A 309     5596   4988   7373   -545    334  -1215       C  
ATOM    585  CD1 LEU A 309      -7.265  23.674  22.307  1.00 48.29           C  
ANISOU  585  CD1 LEU A 309     5738   5028   7583   -560    307  -1152       C  
ATOM    586  CD2 LEU A 309      -6.434  24.960  20.322  1.00 41.14           C  
ANISOU  586  CD2 LEU A 309     4844   4256   6531   -605    378  -1343       C  
ATOM    587  N   HIS A 310      -6.193  29.387  22.462  1.00 37.44           N  
ANISOU  587  N   HIS A 310     4414   4114   5696   -555    327  -1079       N  
ATOM    588  CA  HIS A 310      -6.561  30.636  23.127  1.00 40.24           C  
ANISOU  588  CA  HIS A 310     4793   4557   5938   -552    306   -990       C  
ATOM    589  C   HIS A 310      -7.347  30.362  24.398  1.00 42.56           C  
ANISOU  589  C   HIS A 310     5095   4821   6256   -533    269   -864       C  
ATOM    590  O   HIS A 310      -7.020  30.862  25.473  1.00 41.54           O  
ANISOU  590  O   HIS A 310     4972   4710   6100   -493    247   -780       O  
ATOM    591  CB  HIS A 310      -7.404  31.527  22.208  1.00 43.00           C  
ANISOU  591  CB  HIS A 310     5187   4986   6164   -610    312  -1022       C  
ATOM    592  CG  HIS A 310      -6.762  31.845  20.893  1.00 43.67           C  
ANISOU  592  CG  HIS A 310     5296   5099   6198   -644    355  -1143       C  
ATOM    593  ND1 HIS A 310      -6.463  30.882  19.952  1.00 43.57           N  
ANISOU  593  ND1 HIS A 310     5281   5024   6250   -665    389  -1249       N  
ATOM    594  CD2 HIS A 310      -6.396  33.030  20.347  1.00 38.53           C  
ANISOU  594  CD2 HIS A 310     4685   4527   5429   -665    379  -1175       C  
ATOM    595  CE1 HIS A 310      -5.926  31.458  18.891  1.00 40.51           C  
ANISOU  595  CE1 HIS A 310     4933   4676   5781   -700    438  -1343       C  
ATOM    596  NE2 HIS A 310      -5.872  32.761  19.106  1.00 42.65           N  
ANISOU  596  NE2 HIS A 310     5233   5033   5941   -702    432  -1298       N  
ATOM    597  N   GLN A 311      -8.386  29.546  24.253  1.00 43.91           N  
ANISOU  597  N   GLN A 311     5269   4939   6477   -566    266   -856       N  
ATOM    598  CA  GLN A 311      -9.298  29.244  25.349  1.00 45.98           C  
ANISOU  598  CA  GLN A 311     5542   5165   6762   -565    252   -744       C  
ATOM    599  C   GLN A 311      -8.594  28.541  26.500  1.00 47.59           C  
ANISOU  599  C   GLN A 311     5753   5289   7041   -509    234   -673       C  
ATOM    600  O   GLN A 311      -8.947  28.741  27.659  1.00 43.74           O  
ANISOU  600  O   GLN A 311     5298   4796   6525   -495    225   -565       O  
ATOM    601  CB  GLN A 311     -10.469  28.389  24.857  1.00 46.25           C  
ANISOU  601  CB  GLN A 311     5568   5145   6859   -618    259   -767       C  
ATOM    602  CG  GLN A 311     -10.074  27.084  24.188  1.00 50.18           C  
ANISOU  602  CG  GLN A 311     6048   5548   7471   -622    265   -849       C  
ATOM    603  CD  GLN A 311     -10.033  27.189  22.675  1.00 51.62           C  
ANISOU  603  CD  GLN A 311     6230   5762   7623   -661    273   -979       C  
ATOM    604  OE1 GLN A 311      -9.596  28.199  22.122  1.00 53.11           O  
ANISOU  604  OE1 GLN A 311     6435   6035   7712   -664    279  -1021       O  
ATOM    605  NE2 GLN A 311     -10.498  26.145  21.997  1.00 46.94           N  
ANISOU  605  NE2 GLN A 311     5630   5095   7111   -697    274  -1044       N  
ATOM    606  N   ASP A 312      -7.595  27.726  26.186  1.00 46.48           N  
ANISOU  606  N   ASP A 312     5586   5080   6993   -477    228   -736       N  
ATOM    607  CA  ASP A 312      -6.888  26.987  27.222  1.00 43.21           C  
ANISOU  607  CA  ASP A 312     5180   4574   6662   -418    191   -673       C  
ATOM    608  C   ASP A 312      -6.056  27.905  28.110  1.00 43.38           C  
ANISOU  608  C   ASP A 312     5215   4645   6622   -366    154   -615       C  
ATOM    609  O   ASP A 312      -6.080  27.771  29.335  1.00 44.07           O  
ANISOU  609  O   ASP A 312     5350   4691   6704   -334    117   -508       O  
ATOM    610  CB  ASP A 312      -6.001  25.914  26.604  1.00 45.27           C  
ANISOU  610  CB  ASP A 312     5399   4745   7055   -391    188   -768       C  
ATOM    611  CG  ASP A 312      -6.786  24.701  26.157  1.00 50.34           C  
ANISOU  611  CG  ASP A 312     6044   5297   7785   -430    207   -794       C  
ATOM    612  OD1 ASP A 312      -7.947  24.541  26.599  1.00 52.85           O  
ANISOU  612  OD1 ASP A 312     6396   5602   8081   -469    214   -719       O  
ATOM    613  OD2 ASP A 312      -6.236  23.904  25.366  1.00 50.12           O  
ANISOU  613  OD2 ASP A 312     5981   5208   7853   -423    219   -896       O  
ATOM    614  N   TRP A 313      -5.321  28.831  27.495  1.00 42.87           N  
ANISOU  614  N   TRP A 313     5117   4664   6507   -361    166   -687       N  
ATOM    615  CA  TRP A 313      -4.543  29.800  28.254  1.00 35.19           C  
ANISOU  615  CA  TRP A 313     4150   3745   5476   -318    131   -644       C  
ATOM    616  C   TRP A 313      -5.460  30.644  29.120  1.00 36.05           C  
ANISOU  616  C   TRP A 313     4320   3913   5463   -335    127   -533       C  
ATOM    617  O   TRP A 313      -5.229  30.812  30.317  1.00 39.02           O  
ANISOU  617  O   TRP A 313     4739   4272   5815   -296     82   -441       O  
ATOM    618  CB  TRP A 313      -3.729  30.711  27.329  1.00 39.88           C  
ANISOU  618  CB  TRP A 313     4699   4421   6033   -328    163   -747       C  
ATOM    619  CG  TRP A 313      -2.948  31.738  28.097  1.00 39.93           C  
ANISOU  619  CG  TRP A 313     4706   4481   5986   -289    126   -707       C  
ATOM    620  CD1 TRP A 313      -3.295  33.038  28.320  1.00 32.80           C  
ANISOU  620  CD1 TRP A 313     3837   3677   4950   -310    133   -665       C  
ATOM    621  CD2 TRP A 313      -1.705  31.532  28.778  1.00 39.64           C  
ANISOU  621  CD2 TRP A 313     4631   4394   6035   -222     65   -706       C  
ATOM    622  NE1 TRP A 313      -2.340  33.658  29.094  1.00 38.48           N  
ANISOU  622  NE1 TRP A 313     4547   4413   5662   -264     85   -639       N  
ATOM    623  CE2 TRP A 313      -1.353  32.754  29.386  1.00 43.37           C  
ANISOU  623  CE2 TRP A 313     5119   4942   6416   -209     39   -665       C  
ATOM    624  CE3 TRP A 313      -0.853  30.435  28.927  1.00 41.76           C  
ANISOU  624  CE3 TRP A 313     4852   4556   6457   -168     24   -740       C  
ATOM    625  CZ2 TRP A 313      -0.186  32.908  30.128  1.00 40.99           C  
ANISOU  625  CZ2 TRP A 313     4786   4615   6172   -148    -34   -658       C  
ATOM    626  CZ3 TRP A 313       0.304  30.589  29.665  1.00 48.44           C  
ANISOU  626  CZ3 TRP A 313     5663   5374   7367   -102    -52   -733       C  
ATOM    627  CH2 TRP A 313       0.627  31.816  30.256  1.00 45.04           C  
ANISOU  627  CH2 TRP A 313     5248   5024   6843    -94    -82   -693       C  
ATOM    628  N   LEU A 314      -6.506  31.175  28.499  1.00 42.24           N  
ANISOU  628  N   LEU A 314     5113   4763   6173   -393    171   -548       N  
ATOM    629  CA  LEU A 314      -7.439  32.061  29.182  1.00 44.03           C  
ANISOU  629  CA  LEU A 314     5384   5050   6294   -412    179   -461       C  
ATOM    630  C   LEU A 314      -8.220  31.347  30.286  1.00 53.23           C  
ANISOU  630  C   LEU A 314     6597   6142   7485   -412    179   -355       C  
ATOM    631  O   LEU A 314      -8.641  31.979  31.255  1.00 54.50           O  
ANISOU  631  O   LEU A 314     6808   6332   7568   -409    183   -268       O  
ATOM    632  CB  LEU A 314      -8.403  32.686  28.171  1.00 34.59           C  
ANISOU  632  CB  LEU A 314     4177   3928   5038   -470    214   -511       C  
ATOM    633  CG  LEU A 314      -7.741  33.628  27.163  1.00 32.08           C  
ANISOU  633  CG  LEU A 314     3842   3689   4656   -479    222   -599       C  
ATOM    634  CD1 LEU A 314      -8.705  34.009  26.054  1.00 32.08           C  
ANISOU  634  CD1 LEU A 314     3846   3736   4606   -535    239   -654       C  
ATOM    635  CD2 LEU A 314      -7.220  34.869  27.866  1.00 23.57           C  
ANISOU  635  CD2 LEU A 314     2787   2683   3488   -451    207   -552       C  
ATOM    636  N   ASN A 315      -8.407  30.037  30.147  1.00 57.17           N  
ANISOU  636  N   ASN A 315     7089   6541   8091   -420    183   -365       N  
ATOM    637  CA  ASN A 315      -9.150  29.275  31.152  1.00 58.07           C  
ANISOU  637  CA  ASN A 315     7257   6572   8233   -430    195   -267       C  
ATOM    638  C   ASN A 315      -8.260  28.756  32.278  1.00 59.10           C  
ANISOU  638  C   ASN A 315     7447   6620   8389   -370    140   -192       C  
ATOM    639  O   ASN A 315      -8.720  28.013  33.145  1.00 65.06           O  
ANISOU  639  O   ASN A 315     8268   7286   9165   -376    146   -107       O  
ATOM    640  CB  ASN A 315      -9.897  28.105  30.505  1.00 49.98           C  
ANISOU  640  CB  ASN A 315     6206   5470   7313   -475    226   -307       C  
ATOM    641  CG  ASN A 315     -11.142  28.549  29.758  1.00 43.14           C  
ANISOU  641  CG  ASN A 315     5302   4666   6421   -541    270   -346       C  
ATOM    642  OD1 ASN A 315     -11.825  29.490  30.163  1.00 43.91           O  
ANISOU  642  OD1 ASN A 315     5414   4834   6437   -558    293   -300       O  
ATOM    643  ND2 ASN A 315     -11.447  27.865  28.660  1.00 38.31           N  
ANISOU  643  ND2 ASN A 315     4646   4026   5886   -576    276   -435       N  
ATOM    644  N   GLY A 316      -6.989  29.146  32.255  1.00 54.40           N  
ANISOU  644  N   GLY A 316     6830   6048   7794   -314     83   -227       N  
ATOM    645  CA  GLY A 316      -6.096  28.916  33.378  1.00 53.88           C  
ANISOU  645  CA  GLY A 316     6820   5917   7737   -250      6   -156       C  
ATOM    646  C   GLY A 316      -5.315  27.615  33.381  1.00 54.27           C  
ANISOU  646  C   GLY A 316     6857   5838   7925   -204    -50   -177       C  
ATOM    647  O   GLY A 316      -4.805  27.198  34.421  1.00 57.39           O  
ANISOU  647  O   GLY A 316     7320   6150   8333   -153   -124    -99       O  
ATOM    648  N   LYS A 317      -5.207  26.972  32.224  1.00 49.76           N  
ANISOU  648  N   LYS A 317     6206   5244   7455   -219    -22   -282       N  
ATOM    649  CA  LYS A 317      -4.500  25.701  32.146  1.00 54.28           C  
ANISOU  649  CA  LYS A 317     6759   5689   8175   -174    -69   -313       C  
ATOM    650  C   LYS A 317      -2.997  25.885  32.327  1.00 63.38           C  
ANISOU  650  C   LYS A 317     7866   6828   9388    -94   -152   -353       C  
ATOM    651  O   LYS A 317      -2.416  26.855  31.836  1.00 65.43           O  
ANISOU  651  O   LYS A 317     8062   7185   9612    -91   -141   -423       O  
ATOM    652  CB  LYS A 317      -4.791  25.008  30.817  1.00 56.39           C  
ANISOU  652  CB  LYS A 317     6956   5938   8532   -215     -9   -427       C  
ATOM    653  CG  LYS A 317      -6.259  24.680  30.620  1.00 54.30           C  
ANISOU  653  CG  LYS A 317     6723   5668   8239   -292     59   -396       C  
ATOM    654  CD  LYS A 317      -6.441  23.400  29.823  1.00 54.77           C  
ANISOU  654  CD  LYS A 317     6750   5631   8429   -312     80   -469       C  
ATOM    655  CE  LYS A 317      -7.912  23.019  29.736  1.00 57.00           C  
ANISOU  655  CE  LYS A 317     7060   5896   8701   -390    138   -435       C  
ATOM    656  NZ  LYS A 317      -8.131  21.740  29.002  1.00 58.47           N  
ANISOU  656  NZ  LYS A 317     7220   5979   9016   -414    155   -505       N  
ATOM    657  N   GLU A 318      -2.376  24.950  33.039  1.00 71.81           N  
ANISOU  657  N   GLU A 318     8965   7767  10553    -32   -239   -311       N  
ATOM    658  CA  GLU A 318      -0.937  24.990  33.284  1.00 73.89           C  
ANISOU  658  CA  GLU A 318     9175   7996  10904     53   -338   -351       C  
ATOM    659  C   GLU A 318      -0.139  24.335  32.162  1.00 69.08           C  
ANISOU  659  C   GLU A 318     8443   7345  10462     75   -320   -498       C  
ATOM    660  O   GLU A 318      -0.490  23.257  31.678  1.00 69.28           O  
ANISOU  660  O   GLU A 318     8461   7284  10577     61   -288   -529       O  
ATOM    661  CB  GLU A 318      -0.602  24.302  34.610  1.00 79.47           C  
ANISOU  661  CB  GLU A 318     9981   8573  11640    118   -461   -236       C  
ATOM    662  CG  GLU A 318      -1.310  24.880  35.821  1.00 85.53           C  
ANISOU  662  CG  GLU A 318    10892   9366  12239     97   -476    -90       C  
ATOM    663  CD  GLU A 318      -0.943  24.149  37.096  1.00 91.17           C  
ANISOU  663  CD  GLU A 318    11730   9940  12972    159   -603     24       C  
ATOM    664  OE1 GLU A 318      -0.187  23.159  37.010  1.00 90.89           O  
ANISOU  664  OE1 GLU A 318    11660   9783  13091    221   -684    -11       O  
ATOM    665  OE2 GLU A 318      -1.406  24.561  38.181  1.00 92.66           O  
ANISOU  665  OE2 GLU A 318    12055  10133  13018    147   -622    145       O  
ATOM    666  N   TYR A 319       0.945  24.986  31.759  1.00 67.15           N  
ANISOU  666  N   TYR A 319     8098   7154  10261    108   -333   -592       N  
ATOM    667  CA  TYR A 319       1.820  24.437  30.736  1.00 65.17           C  
ANISOU  667  CA  TYR A 319     7725   6862  10174    131   -304   -742       C  
ATOM    668  C   TYR A 319       3.193  24.149  31.321  1.00 68.79           C  
ANISOU  668  C   TYR A 319     8121   7234  10783    231   -425   -764       C  
ATOM    669  O   TYR A 319       3.854  25.039  31.859  1.00 70.03           O  
ANISOU  669  O   TYR A 319     8259   7444  10907    263   -486   -749       O  
ATOM    670  CB  TYR A 319       1.928  25.396  29.552  1.00 60.23           C  
ANISOU  670  CB  TYR A 319     7024   6367   9493     73   -190   -860       C  
ATOM    671  CG  TYR A 319       0.621  25.579  28.826  1.00 52.31           C  
ANISOU  671  CG  TYR A 319     6074   5434   8367    -20    -86   -856       C  
ATOM    672  CD1 TYR A 319      -0.328  26.482  29.283  1.00 48.94           C  
ANISOU  672  CD1 TYR A 319     5728   5101   7768    -65    -74   -758       C  
ATOM    673  CD2 TYR A 319       0.327  24.837  27.693  1.00 51.65           C  
ANISOU  673  CD2 TYR A 319     5960   5319   8346    -60     -8   -956       C  
ATOM    674  CE1 TYR A 319      -1.530  26.643  28.626  1.00 51.49           C  
ANISOU  674  CE1 TYR A 319     6086   5479   7997   -143      6   -759       C  
ATOM    675  CE2 TYR A 319      -0.870  24.992  27.031  1.00 48.47           C  
ANISOU  675  CE2 TYR A 319     5605   4974   7838   -141     67   -956       C  
ATOM    676  CZ  TYR A 319      -1.794  25.896  27.500  1.00 51.05           C  
ANISOU  676  CZ  TYR A 319     5999   5391   8007   -181     69   -858       C  
ATOM    677  OH  TYR A 319      -2.988  26.048  26.833  1.00 48.44           O  
ANISOU  677  OH  TYR A 319     5704   5111   7590   -257    131   -864       O  
ATOM    678  N   LYS A 320       3.617  22.894  31.226  1.00 72.25           N  
ANISOU  678  N   LYS A 320     8525   7532  11394    282   -468   -803       N  
ATOM    679  CA  LYS A 320       4.902  22.504  31.781  1.00 77.36           C  
ANISOU  679  CA  LYS A 320     9105   8078  12210    386   -600   -829       C  
ATOM    680  C   LYS A 320       5.898  22.077  30.711  1.00 74.44           C  
ANISOU  680  C   LYS A 320     8573   7671  12040    414   -548  -1010       C  
ATOM    681  O   LYS A 320       5.594  21.263  29.837  1.00 68.22           O  
ANISOU  681  O   LYS A 320     7761   6837  11323    385   -462  -1087       O  
ATOM    682  CB  LYS A 320       4.730  21.377  32.798  1.00 79.46           C  
ANISOU  682  CB  LYS A 320     9476   8184  12531    445   -727   -711       C  
ATOM    683  CG  LYS A 320       6.040  20.916  33.415  1.00 83.12           C  
ANISOU  683  CG  LYS A 320     9878   8526  13177    562   -892   -732       C  
ATOM    684  CD  LYS A 320       5.838  19.765  34.386  1.00 89.22           C  
ANISOU  684  CD  LYS A 320    10776   9129  13996    619  -1022   -610       C  
ATOM    685  CE  LYS A 320       5.112  20.212  35.644  1.00 89.35           C  
ANISOU  685  CE  LYS A 320    10980   9163  13807    599  -1088   -426       C  
ATOM    686  NZ  LYS A 320       5.059  19.125  36.659  1.00 90.15           N  
ANISOU  686  NZ  LYS A 320    11220   9085  13948    658  -1227   -305       N  
ATOM    687  N   CYS A 321       7.094  22.647  30.790  1.00 71.98           N  
ANISOU  687  N   CYS A 321     8148   7378  11823    466   -597  -1084       N  
ATOM    688  CA  CYS A 321       8.206  22.209  29.968  1.00 68.32           C  
ANISOU  688  CA  CYS A 321     7518   6858  11582    506   -561  -1258       C  
ATOM    689  C   CYS A 321       9.149  21.360  30.812  1.00 73.66           C  
ANISOU  689  C   CYS A 321     8149   7373  12464    629   -741  -1245       C  
ATOM    690  O   CYS A 321       9.497  21.726  31.936  1.00 71.26           O  
ANISOU  690  O   CYS A 321     7886   7053  12138    686   -895  -1148       O  
ATOM    691  CB  CYS A 321       8.945  23.405  29.368  1.00 63.70           C  
ANISOU  691  CB  CYS A 321     6818   6395  10990    475   -476  -1372       C  
ATOM    692  SG  CYS A 321      10.353  22.969  28.326  1.00 65.80           S  
ANISOU  692  SG  CYS A 321     6869   6598  11535    513   -400  -1602       S  
ATOM    693  N   LYS A 322       9.545  20.212  30.272  1.00 78.54           N  
ANISOU  693  N   LYS A 322     8691   7868  13283    670   -728  -1343       N  
ATOM    694  CA  LYS A 322      10.473  19.323  30.956  1.00 77.23           C  
ANISOU  694  CA  LYS A 322     8469   7533  13341    794   -901  -1347       C  
ATOM    695  C   LYS A 322      11.666  19.021  30.060  1.00 78.49           C  
ANISOU  695  C   LYS A 322     8419   7645  13760    837   -843  -1554       C  
ATOM    696  O   LYS A 322      11.527  18.420  28.993  1.00 76.78           O  
ANISOU  696  O   LYS A 322     8153   7406  13615    800   -701  -1670       O  
ATOM    697  CB  LYS A 322       9.763  18.034  31.379  1.00 78.27           C  
ANISOU  697  CB  LYS A 322     8730   7522  13488    818   -968  -1245       C  
ATOM    698  CG  LYS A 322      10.663  17.001  32.031  1.00 80.70           C  
ANISOU  698  CG  LYS A 322     8995   7635  14031    948  -1154  -1246       C  
ATOM    699  CD  LYS A 322       9.909  16.230  33.103  1.00 82.69           C  
ANISOU  699  CD  LYS A 322     9449   7771  14200    972  -1285  -1058       C  
ATOM    700  CE  LYS A 322      10.318  14.767  33.142  1.00 83.63           C  
ANISOU  700  CE  LYS A 322     9547   7680  14547   1060  -1378  -1088       C  
ATOM    701  NZ  LYS A 322       9.738  13.997  32.006  1.00 80.57           N  
ANISOU  701  NZ  LYS A 322     9134   7273  14205    997  -1206  -1181       N  
ATOM    702  N   VAL A 323      12.843  19.452  30.500  1.00 83.44           N  
ANISOU  702  N   VAL A 323     8921   8253  14531    913   -951  -1606       N  
ATOM    703  CA  VAL A 323      14.048  19.334  29.690  1.00 90.02           C  
ANISOU  703  CA  VAL A 323     9534   9052  15618    949   -884  -1813       C  
ATOM    704  C   VAL A 323      14.989  18.267  30.239  1.00 96.43           C  
ANISOU  704  C   VAL A 323    10279   9740  16620   1035  -1055  -1810       C  
ATOM    705  O   VAL A 323      15.340  18.276  31.421  1.00 97.57           O  
ANISOU  705  O   VAL A 323    10465   9825  16782   1112  -1270  -1703       O  
ATOM    706  CB  VAL A 323      14.789  20.682  29.601  1.00 89.53           C  
ANISOU  706  CB  VAL A 323     9358   9115  15545    924   -845  -1885       C  
ATOM    707  CG1 VAL A 323      16.093  20.522  28.844  1.00 87.26           C  
ANISOU  707  CG1 VAL A 323     8864   8837  15452    909   -771  -2061       C  
ATOM    708  CG2 VAL A 323      13.905  21.723  28.928  1.00 91.22           C  
ANISOU  708  CG2 VAL A 323     9658   9513  15489    787   -657  -1867       C  
ATOM    709  N   SER A 324      15.392  17.348  29.366  1.00 99.35           N  
ANISOU  709  N   SER A 324    10552  10070  17124   1018   -960  -1928       N  
ATOM    710  CA  SER A 324      16.271  16.251  29.749  1.00 95.43           C  
ANISOU  710  CA  SER A 324     9985   9451  16823   1094  -1105  -1943       C  
ATOM    711  C   SER A 324      17.563  16.263  28.929  1.00 92.15           C  
ANISOU  711  C   SER A 324     9349   9062  16601   1074  -1016  -2134       C  
ATOM    712  O   SER A 324      17.538  16.375  27.698  1.00 88.88           O  
ANISOU  712  O   SER A 324     8866   8718  16185    990   -795  -2264       O  
ATOM    713  CB  SER A 324      15.541  14.919  29.589  1.00 92.22           C  
ANISOU  713  CB  SER A 324     9681   8939  16419   1103  -1097  -1895       C  
ATOM    714  OG  SER A 324      14.231  14.996  30.126  1.00 93.18           O  
ANISOU  714  OG  SER A 324    10008   9047  16350   1089  -1124  -1736       O  
ATOM    715  N   ASN A 325      18.688  16.138  29.628  1.00 92.33           N  
ANISOU  715  N   ASN A 325     9273   9023  16786   1144  -1191  -2149       N  
ATOM    716  CA  ASN A 325      20.010  16.237  29.025  1.00 93.83           C  
ANISOU  716  CA  ASN A 325     9251   9224  17178   1125  -1132  -2325       C  
ATOM    717  C   ASN A 325      21.070  15.835  30.052  1.00 98.62           C  
ANISOU  717  C   ASN A 325     9789   9720  17960   1221  -1384  -2306       C  
ATOM    718  O   ASN A 325      20.999  16.238  31.215  1.00 93.74           O  
ANISOU  718  O   ASN A 325     9262   9085  17269   1278  -1581  -2177       O  
ATOM    719  CB  ASN A 325      20.250  17.653  28.502  1.00 91.49           C  
ANISOU  719  CB  ASN A 325     8880   9070  16812   1042   -982  -2407       C  
ATOM    720  CG  ASN A 325      21.676  17.885  28.061  1.00 94.67           C  
ANISOU  720  CG  ASN A 325     9074   9474  17423   1018   -939  -2576       C  
ATOM    721  OD1 ASN A 325      22.421  18.619  28.707  1.00 93.95           O  
ANISOU  721  OD1 ASN A 325     8918   9393  17386   1041  -1054  -2580       O  
ATOM    722  ND2 ASN A 325      22.065  17.267  26.950  1.00 96.90           N  
ANISOU  722  ND2 ASN A 325     9255   9741  17822    967   -770  -2720       N  
ATOM    723  N   LYS A 326      22.045  15.039  29.618  1.00108.59           N  
ANISOU  723  N   LYS A 326    10900  10906  19452   1237  -1380  -2435       N  
ATOM    724  CA  LYS A 326      22.943  14.333  30.539  1.00118.53           C  
ANISOU  724  CA  LYS A 326    12111  12032  20892   1336  -1629  -2416       C  
ATOM    725  C   LYS A 326      23.740  15.247  31.489  1.00122.64           C  
ANISOU  725  C   LYS A 326    12588  12564  21446   1370  -1809  -2397       C  
ATOM    726  O   LYS A 326      24.164  14.812  32.565  1.00123.07           O  
ANISOU  726  O   LYS A 326    12681  12515  21566   1458  -2061  -2320       O  
ATOM    727  CB  LYS A 326      23.903  13.436  29.746  1.00121.43           C  
ANISOU  727  CB  LYS A 326    12298  12325  21516   1334  -1561  -2587       C  
ATOM    728  CG  LYS A 326      25.383  13.743  29.960  1.00123.58           C  
ANISOU  728  CG  LYS A 326    12378  12559  22016   1354  -1654  -2711       C  
ATOM    729  CD  LYS A 326      26.263  12.535  29.668  1.00122.47           C  
ANISOU  729  CD  LYS A 326    12100  12289  22142   1397  -1694  -2826       C  
ATOM    730  CE  LYS A 326      26.079  12.033  28.240  1.00115.96           C  
ANISOU  730  CE  LYS A 326    11209  11495  21358   1321  -1421  -2955       C  
ATOM    731  NZ  LYS A 326      27.101  11.002  27.894  1.00113.99           N  
ANISOU  731  NZ  LYS A 326    10795  11125  21392   1355  -1444  -3093       N  
ATOM    732  N   ALA A 327      23.934  16.507  31.108  1.00123.02           N  
ANISOU  732  N   ALA A 327    12569  12734  21440   1298  -1683  -2464       N  
ATOM    733  CA  ALA A 327      24.654  17.455  31.963  1.00126.62           C  
ANISOU  733  CA  ALA A 327    12987  13206  21916   1322  -1839  -2451       C  
ATOM    734  C   ALA A 327      23.743  18.061  33.037  1.00126.06           C  
ANISOU  734  C   ALA A 327    13121  13174  21604   1355  -1980  -2253       C  
ATOM    735  O   ALA A 327      23.880  19.231  33.400  1.00125.99           O  
ANISOU  735  O   ALA A 327    13113  13245  21514   1333  -2002  -2238       O  
ATOM    736  CB  ALA A 327      25.287  18.556  31.121  1.00128.54           C  
ANISOU  736  CB  ALA A 327    13078  13555  22207   1228  -1644  -2606       C  
ATOM    737  N   LEU A 328      22.813  17.249  33.533  1.00125.27           N  
ANISOU  737  N   LEU A 328    13198  13010  21389   1403  -2067  -2104       N  
ATOM    738  CA  LEU A 328      21.911  17.625  34.618  1.00123.62           C  
ANISOU  738  CA  LEU A 328    13207  12812  20952   1436  -2208  -1904       C  
ATOM    739  C   LEU A 328      21.583  16.377  35.429  1.00125.18           C  
ANISOU  739  C   LEU A 328    13555  12867  21140   1515  -2395  -1772       C  
ATOM    740  O   LEU A 328      21.240  15.342  34.857  1.00125.64           O  
ANISOU  740  O   LEU A 328    13618  12866  21251   1515  -2312  -1793       O  
ATOM    741  CB  LEU A 328      20.624  18.261  34.080  1.00120.07           C  
ANISOU  741  CB  LEU A 328    12863  12476  20280   1366  -2010  -1849       C  
ATOM    742  CG  LEU A 328      20.706  19.671  33.490  1.00114.26           C  
ANISOU  742  CG  LEU A 328    12040  11892  19483   1289  -1845  -1934       C  
ATOM    743  CD1 LEU A 328      19.445  20.006  32.708  1.00105.42           C  
ANISOU  743  CD1 LEU A 328    11009  10864  18181   1217  -1624  -1910       C  
ATOM    744  CD2 LEU A 328      20.952  20.701  34.585  1.00113.87           C  
ANISOU  744  CD2 LEU A 328    12043  11877  19345   1317  -2019  -1848       C  
ATOM    745  N   PRO A 329      21.694  16.464  36.764  1.00124.75           N  
ANISOU  745  N   PRO A 329    13634  12756  21010   1578  -2645  -1637       N  
ATOM    746  CA  PRO A 329      21.420  15.295  37.612  1.00127.57           C  
ANISOU  746  CA  PRO A 329    14157  12972  21343   1648  -2830  -1503       C  
ATOM    747  C   PRO A 329      19.973  14.825  37.482  1.00124.83           C  
ANISOU  747  C   PRO A 329    14004  12620  20807   1621  -2723  -1373       C  
ATOM    748  O   PRO A 329      19.716  13.635  37.286  1.00121.10           O  
ANISOU  748  O   PRO A 329    13571  12048  20391   1642  -2715  -1358       O  
ATOM    749  CB  PRO A 329      21.712  15.809  39.027  1.00126.42           C  
ANISOU  749  CB  PRO A 329    14140  12800  21094   1696  -3085  -1382       C  
ATOM    750  CG  PRO A 329      21.589  17.297  38.932  1.00120.45           C  
ANISOU  750  CG  PRO A 329    13353  12189  20223   1641  -2999  -1399       C  
ATOM    751  CD  PRO A 329      22.049  17.656  37.554  1.00119.89           C  
ANISOU  751  CD  PRO A 329    13039  12202  20311   1580  -2765  -1599       C  
ATOM    752  N   ALA A 330      19.043  15.768  37.587  1.00126.60           N  
ANISOU  752  N   ALA A 330    14344  12944  20814   1572  -2640  -1285       N  
ATOM    753  CA  ALA A 330      17.632  15.502  37.340  1.00125.58           C  
ANISOU  753  CA  ALA A 330    14382  12822  20512   1528  -2507  -1182       C  
ATOM    754  C   ALA A 330      17.147  16.390  36.197  1.00121.63           C  
ANISOU  754  C   ALA A 330    13786  12462  19967   1444  -2251  -1281       C  
ATOM    755  O   ALA A 330      17.711  17.462  35.966  1.00125.30           O  
ANISOU  755  O   ALA A 330    14123  13029  20456   1422  -2210  -1369       O  
ATOM    756  CB  ALA A 330      16.812  15.743  38.599  1.00127.55           C  
ANISOU  756  CB  ALA A 330    14897  13045  20521   1540  -2646   -967       C  
ATOM    757  N   PRO A 331      16.113  15.948  35.464  1.00112.05           N  
ANISOU  757  N   PRO A 331    12636  11251  18688   1392  -2075  -1273       N  
ATOM    758  CA  PRO A 331      15.585  16.817  34.409  1.00107.15           C  
ANISOU  758  CA  PRO A 331    11949  10762  18001   1308  -1837  -1362       C  
ATOM    759  C   PRO A 331      14.844  18.012  35.001  1.00103.27           C  
ANISOU  759  C   PRO A 331    11587  10352  17297   1283  -1851  -1246       C  
ATOM    760  O   PRO A 331      14.185  17.877  36.032  1.00104.34           O  
ANISOU  760  O   PRO A 331    11926  10429  17289   1306  -1981  -1070       O  
ATOM    761  CB  PRO A 331      14.636  15.898  33.637  1.00104.19           C  
ANISOU  761  CB  PRO A 331    11639  10344  17604   1262  -1685  -1367       C  
ATOM    762  CG  PRO A 331      14.200  14.893  34.639  1.00106.62           C  
ANISOU  762  CG  PRO A 331    12131  10513  17867   1313  -1852  -1203       C  
ATOM    763  CD  PRO A 331      15.381  14.673  35.548  1.00111.01           C  
ANISOU  763  CD  PRO A 331    12641  11001  18536   1401  -2083  -1188       C  
ATOM    764  N   ILE A 332      14.954  19.167  34.357  1.00 96.12           N  
ANISOU  764  N   ILE A 332    10575   9581  16367   1232  -1713  -1344       N  
ATOM    765  CA  ILE A 332      14.376  20.387  34.904  1.00 89.25           C  
ANISOU  765  CA  ILE A 332     9818   8830  15264   1186  -1716  -1238       C  
ATOM    766  C   ILE A 332      12.937  20.611  34.426  1.00 86.83           C  
ANISOU  766  C   ILE A 332     9658   8639  14693   1059  -1521  -1162       C  
ATOM    767  O   ILE A 332      12.617  20.382  33.259  1.00 91.37           O  
ANISOU  767  O   ILE A 332    10170   9257  15291    993  -1328  -1266       O  
ATOM    768  CB  ILE A 332      15.229  21.617  34.542  1.00 81.45           C  
ANISOU  768  CB  ILE A 332     8659   7965  14324   1165  -1663  -1361       C  
ATOM    769  CG1 ILE A 332      16.702  21.362  34.862  1.00 82.21           C  
ANISOU  769  CG1 ILE A 332     8590   7985  14662   1247  -1820  -1453       C  
ATOM    770  CG2 ILE A 332      14.748  22.836  35.301  1.00 79.59           C  
ANISOU  770  CG2 ILE A 332     8556   7859  13827   1113  -1699  -1232       C  
ATOM    771  CD1 ILE A 332      17.603  22.549  34.569  1.00 80.34           C  
ANISOU  771  CD1 ILE A 332     8184   7859  14482   1217  -1772  -1574       C  
ATOM    772  N   GLU A 333      12.077  21.051  35.343  1.00 80.02           N  
ANISOU  772  N   GLU A 333     8995   7824  13585   1024  -1578   -984       N  
ATOM    773  CA  GLU A 333      10.683  21.354  35.027  1.00 75.84           C  
ANISOU  773  CA  GLU A 333     8603   7406  12808    908  -1412   -904       C  
ATOM    774  C   GLU A 333      10.324  22.818  35.290  1.00 77.53           C  
ANISOU  774  C   GLU A 333     8869   7791  12800    839  -1364   -850       C  
ATOM    775  O   GLU A 333      10.730  23.399  36.295  1.00 80.51           O  
ANISOU  775  O   GLU A 333     9293   8169  13127    883  -1513   -777       O  
ATOM    776  CB  GLU A 333       9.752  20.450  35.833  1.00 67.34           C  
ANISOU  776  CB  GLU A 333     7733   6221  11633    913  -1484   -737       C  
ATOM    777  CG  GLU A 333       9.904  18.971  35.541  1.00 70.41           C  
ANISOU  777  CG  GLU A 333     8097   6438  12217    968  -1515   -776       C  
ATOM    778  CD  GLU A 333       8.921  18.131  36.328  1.00 75.75           C  
ANISOU  778  CD  GLU A 333     8989   7010  12782    958  -1569   -606       C  
ATOM    779  OE1 GLU A 333       8.787  16.924  36.032  1.00 75.16           O  
ANISOU  779  OE1 GLU A 333     8921   6803  12833    980  -1565   -624       O  
ATOM    780  OE2 GLU A 333       8.278  18.686  37.244  1.00 81.90           O  
ANISOU  780  OE2 GLU A 333     9936   7836  13347    924  -1608   -456       O  
ATOM    781  N   LYS A 334       9.560  23.411  34.381  1.00 77.84           N  
ANISOU  781  N   LYS A 334     8904   7967  12704    732  -1164   -888       N  
ATOM    782  CA  LYS A 334       9.056  24.764  34.576  1.00 81.47           C  
ANISOU  782  CA  LYS A 334     9427   8585  12943    661  -1106   -832       C  
ATOM    783  C   LYS A 334       7.576  24.808  34.236  1.00 81.83           C  
ANISOU  783  C   LYS A 334     9599   8703  12790    562   -964   -757       C  
ATOM    784  O   LYS A 334       7.149  24.217  33.247  1.00 86.35           O  
ANISOU  784  O   LYS A 334    10136   9269  13406    519   -839   -828       O  
ATOM    785  CB  LYS A 334       9.829  25.771  33.719  1.00 83.82           C  
ANISOU  785  CB  LYS A 334     9560   8995  13293    631  -1009   -981       C  
ATOM    786  CG  LYS A 334      11.238  26.056  34.210  1.00 84.80           C  
ANISOU  786  CG  LYS A 334     9558   9074  13589    717  -1154  -1044       C  
ATOM    787  CD  LYS A 334      11.228  26.671  35.598  1.00 82.99           C  
ANISOU  787  CD  LYS A 334     9450   8851  13232    753  -1325   -903       C  
ATOM    788  CE  LYS A 334      12.634  26.779  36.167  1.00 82.31           C  
ANISOU  788  CE  LYS A 334     9243   8693  13340    851  -1507   -963       C  
ATOM    789  NZ  LYS A 334      13.487  27.747  35.420  1.00 80.33           N  
ANISOU  789  NZ  LYS A 334     8806   8538  13178    820  -1415  -1117       N  
ATOM    790  N   THR A 335       6.797  25.502  35.060  1.00 75.30           N  
ANISOU  790  N   THR A 335     8917   7941  11752    527   -984   -621       N  
ATOM    791  CA  THR A 335       5.355  25.600  34.850  1.00 70.10           C  
ANISOU  791  CA  THR A 335     8372   7349  10914    435   -858   -546       C  
ATOM    792  C   THR A 335       4.883  27.052  34.837  1.00 65.19           C  
ANISOU  792  C   THR A 335     7780   6890  10100    369   -784   -523       C  
ATOM    793  O   THR A 335       5.247  27.839  35.710  1.00 64.54           O  
ANISOU  793  O   THR A 335     7738   6839   9945    396   -875   -465       O  
ATOM    794  CB  THR A 335       4.576  24.829  35.938  1.00 72.63           C  
ANISOU  794  CB  THR A 335     8870   7567  11160    448   -936   -386       C  
ATOM    795  OG1 THR A 335       4.827  23.425  35.806  1.00 76.79           O  
ANISOU  795  OG1 THR A 335     9379   7939  11856    497   -983   -407       O  
ATOM    796  CG2 THR A 335       3.076  25.084  35.822  1.00 72.53           C  
ANISOU  796  CG2 THR A 335     8964   7631  10965    350   -803   -310       C  
ATOM    797  N   ILE A 336       4.079  27.408  33.838  1.00 59.57           N  
ANISOU  797  N   ILE A 336     7051   6274   9308    283   -626   -570       N  
ATOM    798  CA  ILE A 336       3.451  28.723  33.806  1.00 61.54           C  
ANISOU  798  CA  ILE A 336     7343   6668   9371    217   -553   -538       C  
ATOM    799  C   ILE A 336       1.968  28.624  33.475  1.00 60.45           C  
ANISOU  799  C   ILE A 336     7289   6571   9109    138   -444   -484       C  
ATOM    800  O   ILE A 336       1.498  27.622  32.933  1.00 59.99           O  
ANISOU  800  O   ILE A 336     7226   6449   9117    119   -397   -508       O  
ATOM    801  CB  ILE A 336       4.115  29.662  32.782  1.00 60.64           C  
ANISOU  801  CB  ILE A 336     7104   6658   9277    187   -471   -672       C  
ATOM    802  CG1 ILE A 336       4.050  29.055  31.380  1.00 59.25           C  
ANISOU  802  CG1 ILE A 336     6847   6474   9192    148   -351   -797       C  
ATOM    803  CG2 ILE A 336       5.553  29.967  33.176  1.00 59.08           C  
ANISOU  803  CG2 ILE A 336     6813   6434   9200    258   -574   -727       C  
ATOM    804  CD1 ILE A 336       4.493  30.001  30.293  1.00 60.62           C  
ANISOU  804  CD1 ILE A 336     6933   6752   9348     98   -242   -921       C  
ATOM    805  N   SER A 337       1.239  29.680  33.813  1.00 57.60           N  
ANISOU  805  N   SER A 337     6999   6313   8575     92   -407   -417       N  
ATOM    806  CA  SER A 337      -0.172  29.796  33.490  1.00 57.06           C  
ANISOU  806  CA  SER A 337     6992   6296   8393     15   -305   -376       C  
ATOM    807  C   SER A 337      -0.562  31.250  33.641  1.00 55.74           C  
ANISOU  807  C   SER A 337     6855   6258   8065    -22   -269   -348       C  
ATOM    808  O   SER A 337       0.198  32.041  34.199  1.00 52.08           O  
ANISOU  808  O   SER A 337     6388   5829   7571     12   -332   -338       O  
ATOM    809  CB  SER A 337      -1.026  28.912  34.399  1.00 62.31           C  
ANISOU  809  CB  SER A 337     7773   6867   9034     15   -331   -254       C  
ATOM    810  OG  SER A 337      -0.909  29.326  35.750  1.00 65.47           O  
ANISOU  810  OG  SER A 337     8276   7254   9345     49   -414   -141       O  
ATOM    811  N   LYS A 338      -1.736  31.608  33.139  1.00 57.20           N  
ANISOU  811  N   LYS A 338     7066   6511   8158    -91   -174   -339       N  
ATOM    812  CA  LYS A 338      -2.243  32.962  33.305  1.00 50.48           C  
ANISOU  812  CA  LYS A 338     6250   5773   7157   -126   -139   -307       C  
ATOM    813  C   LYS A 338      -2.430  33.254  34.787  1.00 44.96           C  
ANISOU  813  C   LYS A 338     5658   5056   6368    -99   -201   -181       C  
ATOM    814  O   LYS A 338      -2.742  32.353  35.565  1.00 51.90           O  
ANISOU  814  O   LYS A 338     6611   5841   7268    -82   -233   -101       O  
ATOM    815  CB  LYS A 338      -3.564  33.142  32.551  1.00 51.02           C  
ANISOU  815  CB  LYS A 338     6326   5896   7161   -198    -43   -317       C  
ATOM    816  CG  LYS A 338      -3.975  34.589  32.355  1.00 47.31           C  
ANISOU  816  CG  LYS A 338     5868   5547   6561   -233     -3   -318       C  
ATOM    817  CD  LYS A 338      -5.440  34.682  31.976  1.00 44.75           C  
ANISOU  817  CD  LYS A 338     5567   5255   6180   -292     66   -298       C  
ATOM    818  CE  LYS A 338      -6.325  34.344  33.163  1.00 44.92           C  
ANISOU  818  CE  LYS A 338     5670   5231   6167   -293     67   -182       C  
ATOM    819  NZ  LYS A 338      -7.762  34.246  32.783  1.00 45.48           N  
ANISOU  819  NZ  LYS A 338     5741   5315   6222   -352    136   -173       N  
ATOM    820  N   ALA A 339      -2.227  34.508  35.176  1.00 39.11           N  
ANISOU  820  N   ALA A 339     4938   4399   5524    -98   -213   -165       N  
ATOM    821  CA  ALA A 339      -2.366  34.904  36.572  1.00 41.94           C  
ANISOU  821  CA  ALA A 339     5409   4746   5781    -75   -268    -53       C  
ATOM    822  C   ALA A 339      -3.778  34.637  37.083  1.00 49.75           C  
ANISOU  822  C   ALA A 339     6494   5718   6691   -119   -201     38       C  
ATOM    823  O   ALA A 339      -4.759  34.891  36.383  1.00 45.41           O  
ANISOU  823  O   ALA A 339     5916   5225   6115   -174   -106     13       O  
ATOM    824  CB  ALA A 339      -2.003  36.372  36.744  1.00 37.20           C  
ANISOU  824  CB  ALA A 339     4807   4246   5081    -77   -278    -66       C  
ATOM    825  N   LYS A 340      -3.874  34.114  38.301  1.00 53.98           N  
ANISOU  825  N   LYS A 340     7147   6172   7194    -95   -250    140       N  
ATOM    826  CA  LYS A 340      -5.163  33.846  38.924  1.00 57.37           C  
ANISOU  826  CA  LYS A 340     7676   6573   7549   -140   -173    230       C  
ATOM    827  C   LYS A 340      -5.720  35.123  39.530  1.00 57.60           C  
ANISOU  827  C   LYS A 340     7768   6688   7428   -164   -130    274       C  
ATOM    828  O   LYS A 340      -4.968  36.044  39.845  1.00 59.30           O  
ANISOU  828  O   LYS A 340     7991   6956   7585   -133   -191    264       O  
ATOM    829  CB  LYS A 340      -5.021  32.762  39.994  1.00 61.10           C  
ANISOU  829  CB  LYS A 340     8269   6911   8035   -111   -235    325       C  
ATOM    830  CG  LYS A 340      -4.391  31.476  39.491  1.00 65.72           C  
ANISOU  830  CG  LYS A 340     8798   7395   8778    -78   -292    284       C  
ATOM    831  CD  LYS A 340      -3.813  30.662  40.635  1.00 70.34           C  
ANISOU  831  CD  LYS A 340     9508   7849   9370    -24   -406    374       C  
ATOM    832  CE  LYS A 340      -4.365  29.249  40.633  1.00 72.42           C  
ANISOU  832  CE  LYS A 340     9815   7989   9714    -43   -375    412       C  
ATOM    833  NZ  LYS A 340      -4.170  28.576  39.322  1.00 69.05           N  
ANISOU  833  NZ  LYS A 340     9237   7552   9445    -44   -351    302       N  
ATOM    834  N   GLY A 341      -7.036  35.179  39.699  1.00 49.49           N  
ANISOU  834  N   GLY A 341     6782   5673   6348   -220    -22    316       N  
ATOM    835  CA  GLY A 341      -7.676  36.354  40.263  1.00 41.43           C  
ANISOU  835  CA  GLY A 341     5817   4728   5196   -244     34    351       C  
ATOM    836  C   GLY A 341      -8.787  36.848  39.364  1.00 43.54           C  
ANISOU  836  C   GLY A 341     5997   5071   5474   -298    139    300       C  
ATOM    837  O   GLY A 341      -8.748  36.635  38.154  1.00 47.61           O  
ANISOU  837  O   GLY A 341     6401   5611   6076   -309    144    218       O  
ATOM    838  N   GLN A 342      -9.780  37.511  39.951  1.00 49.78           N  
ANISOU  838  N   GLN A 342     6842   5895   6178   -332    222    344       N  
ATOM    839  CA  GLN A 342     -10.930  37.986  39.184  1.00 49.70           C  
ANISOU  839  CA  GLN A 342     6749   5948   6189   -379    312    297       C  
ATOM    840  C   GLN A 342     -10.520  38.993  38.117  1.00 45.09           C  
ANISOU  840  C   GLN A 342     6069   5463   5600   -368    278    210       C  
ATOM    841  O   GLN A 342      -9.901  40.015  38.418  1.00 44.01           O  
ANISOU  841  O   GLN A 342     5959   5381   5381   -341    238    210       O  
ATOM    842  CB  GLN A 342     -11.977  38.615  40.103  1.00 53.39           C  
ANISOU  842  CB  GLN A 342     7287   6428   6569   -410    407    354       C  
ATOM    843  CG  GLN A 342     -13.278  38.965  39.389  1.00 66.14           C  
ANISOU  843  CG  GLN A 342     8807   8088   8233   -457    496    308       C  
ATOM    844  CD  GLN A 342     -14.352  39.461  40.339  1.00 85.58           C  
ANISOU  844  CD  GLN A 342    11330  10551  10637   -488    606    357       C  
ATOM    845  OE1 GLN A 342     -14.108  40.337  41.168  1.00 96.08           O  
ANISOU  845  OE1 GLN A 342    12742  11910  11853   -469    608    392       O  
ATOM    846  NE2 GLN A 342     -15.548  38.895  40.227  1.00 87.68           N  
ANISOU  846  NE2 GLN A 342    11551  10777  10984   -540    702    355       N  
ATOM    847  N   PRO A 343     -10.850  38.690  36.856  1.00 44.39           N  
ANISOU  847  N   PRO A 343     5880   5391   5597   -392    291    136       N  
ATOM    848  CA  PRO A 343     -10.597  39.624  35.760  1.00 39.90           C  
ANISOU  848  CA  PRO A 343     5238   4909   5015   -392    269     55       C  
ATOM    849  C   PRO A 343     -11.325  40.944  35.980  1.00 42.36           C  
ANISOU  849  C   PRO A 343     5562   5294   5240   -404    308     65       C  
ATOM    850  O   PRO A 343     -12.447  40.961  36.483  1.00 48.67           O  
ANISOU  850  O   PRO A 343     6377   6080   6035   -429    376    103       O  
ATOM    851  CB  PRO A 343     -11.146  38.886  34.533  1.00 45.74           C  
ANISOU  851  CB  PRO A 343     5895   5632   5853   -426    287    -12       C  
ATOM    852  CG  PRO A 343     -11.087  37.441  34.908  1.00 41.25           C  
ANISOU  852  CG  PRO A 343     5344   4963   5367   -426    289     21       C  
ATOM    853  CD  PRO A 343     -11.388  37.407  36.379  1.00 38.33           C  
ANISOU  853  CD  PRO A 343     5072   4552   4940   -421    319    122       C  
ATOM    854  N   ARG A 344     -10.681  42.042  35.616  1.00 44.50           N  
ANISOU  854  N   ARG A 344     5823   5634   5449   -386    270     28       N  
ATOM    855  CA AARG A 344     -11.307  43.345  35.747  0.43 38.95           C  
ANISOU  855  CA AARG A 344     5133   4999   4670   -393    299     31       C  
ATOM    856  CA BARG A 344     -11.276  43.364  35.762  0.57 38.48           C  
ANISOU  856  CA BARG A 344     5074   4939   4607   -392    297     31       C  
ATOM    857  C   ARG A 344     -11.171  44.142  34.455  1.00 39.74           C  
ANISOU  857  C   ARG A 344     5176   5162   4761   -403    273    -47       C  
ATOM    858  O   ARG A 344     -10.114  44.165  33.831  1.00 43.71           O  
ANISOU  858  O   ARG A 344     5661   5678   5268   -394    230    -94       O  
ATOM    859  CB AARG A 344     -10.707  44.111  36.924  0.43 37.21           C  
ANISOU  859  CB AARG A 344     4996   4793   4349   -363    281     83       C  
ATOM    860  CB BARG A 344     -10.596  44.134  36.896  0.57 36.51           C  
ANISOU  860  CB BARG A 344     4907   4706   4259   -361    275     80       C  
ATOM    861  CG AARG A 344     -10.960  43.453  38.271  0.43 38.64           C  
ANISOU  861  CG AARG A 344     5264   4907   4509   -359    311    168       C  
ATOM    862  CG BARG A 344     -10.787  43.522  38.275  0.57 38.62           C  
ANISOU  862  CG BARG A 344     5264   4908   4500   -354    300    166       C  
ATOM    863  CD AARG A 344     -11.150  44.501  39.345  0.43 35.96           C  
ANISOU  863  CD AARG A 344     5011   4597   4056   -349    336    214       C  
ATOM    864  CD BARG A 344     -11.814  44.292  39.082  0.57 36.47           C  
ANISOU  864  CD BARG A 344     5044   4656   4157   -368    377    206       C  
ATOM    865  NE AARG A 344     -10.116  44.431  40.369  0.43 30.81           N  
ANISOU  865  NE AARG A 344     4455   3913   3337   -316    272    262       N  
ATOM    866  NE BARG A 344     -11.927  43.784  40.445  0.57 31.85           N  
ANISOU  866  NE BARG A 344     4571   4006   3522   -368    409    289       N  
ATOM    867  CZ AARG A 344      -9.818  45.431  41.192  0.43 26.99           C  
ANISOU  867  CZ AARG A 344     4049   3460   2747   -299    257    287       C  
ATOM    868  CZ BARG A 344     -13.064  43.376  40.996  0.57 34.67           C  
ANISOU  868  CZ BARG A 344     4958   4323   3893   -402    510    328       C  
ATOM    869  NH1AARG A 344      -8.864  45.279  42.100  0.43 24.55           N  
ANISOU  869  NH1AARG A 344     3831   3114   2384   -267    181    328       N  
ATOM    870  NH1BARG A 344     -13.074  42.929  42.244  0.57 22.52           N  
ANISOU  870  NH1BARG A 344     3545   2720   2291   -406    542    405       N  
ATOM    871  NH2AARG A 344     -10.472  46.582  41.104  0.43 20.02           N  
ANISOU  871  NH2AARG A 344     3156   2638   1814   -310    308    267       N  
ATOM    872  NH2BARG A 344     -14.191  43.422  40.301  0.57 28.48           N  
ANISOU  872  NH2BARG A 344     4080   3556   3184   -435    578    288       N  
ATOM    873  N   GLU A 345     -12.264  44.780  34.051  1.00 41.31           N  
ANISOU  873  N   GLU A 345     5349   5394   4953   -422    303    -63       N  
ATOM    874  CA  GLU A 345     -12.306  45.523  32.796  1.00 38.65           C  
ANISOU  874  CA  GLU A 345     4978   5108   4601   -435    273   -131       C  
ATOM    875  C   GLU A 345     -11.490  46.816  32.835  1.00 37.36           C  
ANISOU  875  C   GLU A 345     4853   4999   4341   -418    245   -140       C  
ATOM    876  O   GLU A 345     -11.676  47.652  33.721  1.00 41.74           O  
ANISOU  876  O   GLU A 345     5449   5576   4835   -401    260    -99       O  
ATOM    877  CB  GLU A 345     -13.757  45.839  32.430  1.00 36.65           C  
ANISOU  877  CB  GLU A 345     4686   4862   4377   -455    295   -143       C  
ATOM    878  CG  GLU A 345     -13.933  46.506  31.080  1.00 41.98           C  
ANISOU  878  CG  GLU A 345     5340   5574   5036   -468    248   -210       C  
ATOM    879  CD  GLU A 345     -15.388  46.766  30.757  1.00 55.35           C  
ANISOU  879  CD  GLU A 345     6987   7265   6777   -480    249   -223       C  
ATOM    880  OE1 GLU A 345     -16.238  46.545  31.644  1.00 58.31           O  
ANISOU  880  OE1 GLU A 345     7340   7616   7199   -480    303   -184       O  
ATOM    881  OE2 GLU A 345     -15.682  47.188  29.619  1.00 63.32           O  
ANISOU  881  OE2 GLU A 345     7986   8292   7780   -492    196   -276       O  
ATOM    882  N   PRO A 346     -10.576  46.977  31.870  1.00 38.97           N  
ANISOU  882  N   PRO A 346     5047   5224   4535   -426    212   -199       N  
ATOM    883  CA  PRO A 346      -9.810  48.219  31.749  1.00 37.61           C  
ANISOU  883  CA  PRO A 346     4908   5102   4281   -420    193   -216       C  
ATOM    884  C   PRO A 346     -10.686  49.383  31.313  1.00 33.02           C  
ANISOU  884  C   PRO A 346     4342   4559   3644   -429    192   -225       C  
ATOM    885  O   PRO A 346     -11.418  49.259  30.333  1.00 28.92           O  
ANISOU  885  O   PRO A 346     3801   4037   3150   -451    182   -261       O  
ATOM    886  CB  PRO A 346      -8.763  47.886  30.679  1.00 30.19           C  
ANISOU  886  CB  PRO A 346     3946   4160   3363   -438    179   -287       C  
ATOM    887  CG  PRO A 346      -9.360  46.767  29.899  1.00 28.83           C  
ANISOU  887  CG  PRO A 346     3736   3952   3267   -459    186   -317       C  
ATOM    888  CD  PRO A 346     -10.152  45.965  30.886  1.00 31.74           C  
ANISOU  888  CD  PRO A 346     4093   4279   3688   -444    203   -255       C  
ATOM    889  N   GLN A 347     -10.619  50.487  32.045  1.00 33.09           N  
ANISOU  889  N   GLN A 347     4393   4597   3583   -412    193   -194       N  
ATOM    890  CA  GLN A 347     -11.242  51.726  31.606  1.00 37.30           C  
ANISOU  890  CA  GLN A 347     4947   5164   4061   -415    182   -207       C  
ATOM    891  C   GLN A 347     -10.245  52.493  30.740  1.00 38.15           C  
ANISOU  891  C   GLN A 347     5087   5299   4109   -434    158   -253       C  
ATOM    892  O   GLN A 347      -9.106  52.726  31.147  1.00 35.51           O  
ANISOU  892  O   GLN A 347     4770   4975   3748   -430    158   -254       O  
ATOM    893  CB  GLN A 347     -11.697  52.565  32.802  1.00 38.41           C  
ANISOU  893  CB  GLN A 347     5120   5316   4157   -388    204   -157       C  
ATOM    894  CG  GLN A 347     -12.605  51.808  33.764  1.00 49.30           C  
ANISOU  894  CG  GLN A 347     6481   6663   5589   -378    251   -110       C  
ATOM    895  CD  GLN A 347     -13.852  51.257  33.086  1.00 59.80           C  
ANISOU  895  CD  GLN A 347     7749   7971   7003   -394    260   -131       C  
ATOM    896  OE1 GLN A 347     -14.609  52.000  32.454  1.00 64.73           O  
ANISOU  896  OE1 GLN A 347     8356   8610   7629   -394    239   -158       O  
ATOM    897  NE2 GLN A 347     -14.066  49.952  33.207  1.00 57.42           N  
ANISOU  897  NE2 GLN A 347     7412   7629   6776   -406    284   -121       N  
ATOM    898  N   VAL A 348     -10.668  52.865  29.537  1.00 35.15           N  
ANISOU  898  N   VAL A 348     4719   4926   3712   -457    136   -294       N  
ATOM    899  CA  VAL A 348      -9.768  53.517  28.599  1.00 27.95           C  
ANISOU  899  CA  VAL A 348     3850   4031   2738   -487    127   -341       C  
ATOM    900  C   VAL A 348     -10.150  54.974  28.363  1.00 33.30           C  
ANISOU  900  C   VAL A 348     4588   4730   3335   -486    104   -336       C  
ATOM    901  O   VAL A 348     -11.222  55.273  27.842  1.00 38.72           O  
ANISOU  901  O   VAL A 348     5285   5409   4020   -484     70   -338       O  
ATOM    902  CB  VAL A 348      -9.742  52.780  27.255  1.00 30.51           C  
ANISOU  902  CB  VAL A 348     4172   4337   3085   -523    121   -399       C  
ATOM    903  CG1 VAL A 348      -8.711  53.404  26.338  1.00 25.44           C  
ANISOU  903  CG1 VAL A 348     3585   3706   2373   -562    134   -450       C  
ATOM    904  CG2 VAL A 348      -9.437  51.310  27.475  1.00 28.66           C  
ANISOU  904  CG2 VAL A 348     3876   4073   2940   -520    142   -406       C  
ATOM    905  N   TYR A 349      -9.257  55.880  28.756  1.00 36.94           N  
ANISOU  905  N   TYR A 349     5087   5211   3738   -488    114   -333       N  
ATOM    906  CA  TYR A 349      -9.486  57.305  28.575  1.00 26.45           C  
ANISOU  906  CA  TYR A 349     3822   3895   2331   -489     94   -327       C  
ATOM    907  C   TYR A 349      -8.391  57.940  27.729  1.00 32.52           C  
ANISOU  907  C   TYR A 349     4649   4670   3036   -535    107   -371       C  
ATOM    908  O   TYR A 349      -7.206  57.708  27.956  1.00 33.89           O  
ANISOU  908  O   TYR A 349     4804   4851   3224   -551    139   -391       O  
ATOM    909  CB  TYR A 349      -9.570  58.016  29.926  1.00 23.15           C  
ANISOU  909  CB  TYR A 349     3409   3491   1895   -452    102   -281       C  
ATOM    910  CG  TYR A 349     -10.559  57.404  30.891  1.00 30.52           C  
ANISOU  910  CG  TYR A 349     4295   4414   2885   -415    114   -240       C  
ATOM    911  CD1 TYR A 349     -11.929  57.505  30.673  1.00 25.63           C  
ANISOU  911  CD1 TYR A 349     3658   3782   2298   -399     99   -233       C  
ATOM    912  CD2 TYR A 349     -10.124  56.738  32.031  1.00 26.54           C  
ANISOU  912  CD2 TYR A 349     3769   3907   2408   -398    140   -209       C  
ATOM    913  CE1 TYR A 349     -12.837  56.949  31.554  1.00 24.30           C  
ANISOU  913  CE1 TYR A 349     3441   3600   2191   -373    129   -201       C  
ATOM    914  CE2 TYR A 349     -11.028  56.180  32.922  1.00 29.47           C  
ANISOU  914  CE2 TYR A 349     4114   4262   2821   -372    166   -169       C  
ATOM    915  CZ  TYR A 349     -12.382  56.290  32.675  1.00 29.06           C  
ANISOU  915  CZ  TYR A 349     4036   4200   2806   -364    170   -167       C  
ATOM    916  OH  TYR A 349     -13.289  55.739  33.550  1.00 35.66           O  
ANISOU  916  OH  TYR A 349     4840   5015   3692   -347    214   -135       O  
ATOM    917  N   THR A 350      -8.799  58.744  26.753  1.00 31.82           N  
ANISOU  917  N   THR A 350     4611   4553   2927   -534     76   -371       N  
ATOM    918  CA  THR A 350      -7.847  59.498  25.955  1.00 32.55           C  
ANISOU  918  CA  THR A 350     4738   4615   3014   -547     92   -383       C  
ATOM    919  C   THR A 350      -7.733  60.919  26.488  1.00 36.44           C  
ANISOU  919  C   THR A 350     5254   5097   3496   -513     80   -346       C  
ATOM    920  O   THR A 350      -8.734  61.538  26.847  1.00 32.31           O  
ANISOU  920  O   THR A 350     4746   4572   2958   -476     42   -316       O  
ATOM    921  CB  THR A 350      -8.244  59.547  24.472  1.00 31.27           C  
ANISOU  921  CB  THR A 350     4631   4419   2830   -568     69   -403       C  
ATOM    922  OG1 THR A 350      -9.517  60.186  24.342  1.00 30.03           O  
ANISOU  922  OG1 THR A 350     4508   4252   2648   -536      2   -377       O  
ATOM    923  CG2 THR A 350      -8.317  58.144  23.891  1.00 36.10           C  
ANISOU  923  CG2 THR A 350     5225   5037   3455   -605     82   -448       C  
ATOM    924  N   LEU A 351      -6.506  61.425  26.555  1.00 39.22           N  
ANISOU  924  N   LEU A 351     5605   5441   3855   -531    114   -356       N  
ATOM    925  CA  LEU A 351      -6.265  62.786  27.010  1.00 36.74           C  
ANISOU  925  CA  LEU A 351     5314   5114   3531   -507    106   -330       C  
ATOM    926  C   LEU A 351      -5.488  63.570  25.956  1.00 32.97           C  
ANISOU  926  C   LEU A 351     4883   4605   3040   -548    129   -347       C  
ATOM    927  O   LEU A 351      -4.466  63.100  25.460  1.00 25.84           O  
ANISOU  927  O   LEU A 351     3971   3701   2147   -601    179   -387       O  
ATOM    928  CB  LEU A 351      -5.493  62.791  28.340  1.00 38.29           C  
ANISOU  928  CB  LEU A 351     5471   5335   3744   -498    121   -326       C  
ATOM    929  CG  LEU A 351      -5.748  61.681  29.364  1.00 33.93           C  
ANISOU  929  CG  LEU A 351     4875   4817   3202   -482    119   -319       C  
ATOM    930  CD1 LEU A 351      -4.828  61.856  30.562  1.00 21.74           C  
ANISOU  930  CD1 LEU A 351     3313   3290   1659   -477    122   -317       C  
ATOM    931  CD2 LEU A 351      -7.203  61.645  29.808  1.00 34.06           C  
ANISOU  931  CD2 LEU A 351     4898   4839   3206   -441     93   -282       C  
ATOM    932  N   PRO A 352      -5.968  64.776  25.614  1.00 32.34           N  
ANISOU  932  N   PRO A 352     4856   4499   2934   -529    100   -322       N  
ATOM    933  CA  PRO A 352      -5.313  65.628  24.616  1.00 30.87           C  
ANISOU  933  CA  PRO A 352     4730   4277   2724   -574    124   -332       C  
ATOM    934  C   PRO A 352      -4.012  66.216  25.167  1.00 31.62           C  
ANISOU  934  C   PRO A 352     4809   4373   2831   -607    171   -347       C  
ATOM    935  O   PRO A 352      -3.744  66.042  26.352  1.00 37.18           O  
ANISOU  935  O   PRO A 352     5462   5106   3559   -585    168   -345       O  
ATOM    936  CB  PRO A 352      -6.358  66.719  24.360  1.00 31.09           C  
ANISOU  936  CB  PRO A 352     4813   4280   2719   -537     68   -298       C  
ATOM    937  CG  PRO A 352      -7.069  66.846  25.654  1.00 23.74           C  
ANISOU  937  CG  PRO A 352     3838   3377   1805   -477     36   -276       C  
ATOM    938  CD  PRO A 352      -7.132  65.443  26.226  1.00 22.49           C  
ANISOU  938  CD  PRO A 352     3616   3253   1675   -471     49   -287       C  
ATOM    939  N   PRO A 353      -3.211  66.882  24.319  1.00 41.73           N  
ANISOU  939  N   PRO A 353     6142   5622   4093   -668    213   -364       N  
ATOM    940  CA  PRO A 353      -1.986  67.503  24.833  1.00 32.28           C  
ANISOU  940  CA  PRO A 353     4932   4425   2907   -712    258   -387       C  
ATOM    941  C   PRO A 353      -2.273  68.531  25.916  1.00 32.07           C  
ANISOU  941  C   PRO A 353     4904   4402   2878   -663    216   -354       C  
ATOM    942  O   PRO A 353      -3.326  69.170  25.875  1.00 34.12           O  
ANISOU  942  O   PRO A 353     5198   4647   3118   -613    166   -316       O  
ATOM    943  CB  PRO A 353      -1.388  68.180  23.594  1.00 31.80           C  
ANISOU  943  CB  PRO A 353     4949   4318   2814   -787    309   -404       C  
ATOM    944  CG  PRO A 353      -1.920  67.406  22.451  1.00 32.80           C  
ANISOU  944  CG  PRO A 353     5109   4430   2922   -796    310   -408       C  
ATOM    945  CD  PRO A 353      -3.310  67.000  22.853  1.00 37.58           C  
ANISOU  945  CD  PRO A 353     5693   5056   3530   -711    228   -371       C  
ATOM    946  N   SER A 354      -1.360  68.669  26.870  1.00 24.02           N  
ANISOU  946  N   SER A 354     3846   3404   1878   -680    234   -376       N  
ATOM    947  CA  SER A 354      -1.407  69.776  27.814  1.00 18.52           C  
ANISOU  947  CA  SER A 354     3160   2704   1173   -649    204   -354       C  
ATOM    948  C   SER A 354      -1.348  71.074  27.036  1.00 29.13           C  
ANISOU  948  C   SER A 354     4581   4000   2486   -684    217   -344       C  
ATOM    949  O   SER A 354      -0.622  71.165  26.044  1.00 31.09           O  
ANISOU  949  O   SER A 354     4866   4222   2722   -761    272   -371       O  
ATOM    950  CB  SER A 354      -0.251  69.709  28.809  1.00 29.47           C  
ANISOU  950  CB  SER A 354     4504   4118   2576   -680    222   -391       C  
ATOM    951  OG  SER A 354      -0.353  70.739  29.781  1.00 36.13           O  
ANISOU  951  OG  SER A 354     5363   4957   3408   -647    187   -370       O  
ATOM    952  N   ARG A 355      -2.111  72.068  27.484  1.00 35.21           N  
ANISOU  952  N   ARG A 355     5381   4756   3241   -633    172   -308       N  
ATOM    953  CA  ARG A 355      -2.133  73.378  26.836  1.00 38.47           C  
ANISOU  953  CA  ARG A 355     5877   5119   3620   -664    175   -296       C  
ATOM    954  C   ARG A 355      -0.722  73.920  26.628  1.00 39.29           C  
ANISOU  954  C   ARG A 355     6009   5202   3718   -759    239   -332       C  
ATOM    955  O   ARG A 355      -0.417  74.500  25.586  1.00 36.13           O  
ANISOU  955  O   ARG A 355     5685   4755   3288   -824    276   -336       O  
ATOM    956  CB  ARG A 355      -2.960  74.372  27.660  1.00 38.23           C  
ANISOU  956  CB  ARG A 355     5862   5084   3581   -600    124   -265       C  
ATOM    957  CG  ARG A 355      -4.446  74.051  27.709  1.00 30.79           C  
ANISOU  957  CG  ARG A 355     4906   4155   2637   -524     70   -237       C  
ATOM    958  CD  ARG A 355      -5.282  75.189  27.162  1.00 36.99           C  
ANISOU  958  CD  ARG A 355     5772   4896   3387   -512     34   -214       C  
ATOM    959  NE  ARG A 355      -5.766  76.080  28.211  1.00 38.97           N  
ANISOU  959  NE  ARG A 355     6022   5149   3636   -467      7   -203       N  
ATOM    960  CZ  ARG A 355      -6.036  77.366  28.020  1.00 40.03           C  
ANISOU  960  CZ  ARG A 355     6233   5236   3741   -473    -13   -190       C  
ATOM    961  NH1 ARG A 355      -6.481  78.110  29.022  1.00 50.72           N  
ANISOU  961  NH1 ARG A 355     7586   6592   5093   -432    -33   -186       N  
ATOM    962  NH2 ARG A 355      -5.854  77.912  26.825  1.00 25.00           N  
ANISOU  962  NH2 ARG A 355     4419   3276   1804   -524    -11   -183       N  
ATOM    963  N   GLU A 356       0.135  73.707  27.621  1.00 37.07           N  
ANISOU  963  N   GLU A 356     5670   4954   3461   -774    255   -363       N  
ATOM    964  CA  GLU A 356       1.506  74.195  27.581  1.00 33.44           C  
ANISOU  964  CA  GLU A 356     5223   4483   2999   -872    318   -413       C  
ATOM    965  C   GLU A 356       2.368  73.503  26.527  1.00 27.72           C  
ANISOU  965  C   GLU A 356     4495   3753   2283   -964    402   -463       C  
ATOM    966  O   GLU A 356       3.320  74.095  26.019  1.00 39.97           O  
ANISOU  966  O   GLU A 356     6084   5275   3826  -1062    476   -504       O  
ATOM    967  CB  GLU A 356       2.164  74.035  28.953  1.00 31.23           C  
ANISOU  967  CB  GLU A 356     4877   4246   2741   -863    300   -444       C  
ATOM    968  CG  GLU A 356       1.747  75.074  29.972  1.00 28.26           C  
ANISOU  968  CG  GLU A 356     4525   3862   2350   -809    245   -414       C  
ATOM    969  CD  GLU A 356       2.605  75.030  31.220  1.00 46.47           C  
ANISOU  969  CD  GLU A 356     6786   6202   4667   -821    227   -455       C  
ATOM    970  OE1 GLU A 356       2.872  73.913  31.714  1.00 56.20           O  
ANISOU  970  OE1 GLU A 356     7954   7478   5920   -807    213   -479       O  
ATOM    971  OE2 GLU A 356       3.018  76.107  31.701  1.00 46.26           O  
ANISOU  971  OE2 GLU A 356     6795   6157   4625   -846    221   -467       O  
ATOM    972  N   GLU A 357       2.040  72.257  26.194  1.00 29.17           N  
ANISOU  972  N   GLU A 357     4635   3962   2485   -938    400   -467       N  
ATOM    973  CA  GLU A 357       2.845  71.504  25.233  1.00 29.58           C  
ANISOU  973  CA  GLU A 357     4677   4011   2551  -1021    486   -523       C  
ATOM    974  C   GLU A 357       2.649  72.029  23.818  1.00 33.75           C  
ANISOU  974  C   GLU A 357     5307   4478   3039  -1070    524   -506       C  
ATOM    975  O   GLU A 357       3.420  71.704  22.916  1.00 38.60           O  
ANISOU  975  O   GLU A 357     5937   5072   3656  -1158    613   -556       O  
ATOM    976  CB  GLU A 357       2.515  70.011  25.283  1.00 31.17           C  
ANISOU  976  CB  GLU A 357     4808   4253   2781   -979    471   -534       C  
ATOM    977  CG  GLU A 357       3.585  69.132  24.635  1.00 35.83           C  
ANISOU  977  CG  GLU A 357     5356   4853   3405  -1066    570   -617       C  
ATOM    978  CD  GLU A 357       3.222  67.659  24.617  1.00 38.56           C  
ANISOU  978  CD  GLU A 357     5641   5232   3778  -1026    556   -629       C  
ATOM    979  OE1 GLU A 357       4.129  66.818  24.436  1.00 30.15           O  
ANISOU  979  OE1 GLU A 357     4511   4186   2757  -1082    630   -711       O  
ATOM    980  OE2 GLU A 357       2.023  67.344  24.776  1.00 41.08           O  
ANISOU  980  OE2 GLU A 357     5971   5556   4079   -942    477   -565       O  
ATOM    981  N   MET A 358       1.633  72.866  23.633  1.00 37.01           N  
ANISOU  981  N   MET A 358     5793   4857   3412  -1017    458   -443       N  
ATOM    982  CA  MET A 358       1.302  73.385  22.309  1.00 42.33           C  
ANISOU  982  CA  MET A 358     6580   5468   4036  -1055    473   -421       C  
ATOM    983  C   MET A 358       2.299  74.414  21.784  1.00 45.52           C  
ANISOU  983  C   MET A 358     7066   5817   4414  -1166    556   -449       C  
ATOM    984  O   MET A 358       2.120  74.949  20.689  1.00 50.65           O  
ANISOU  984  O   MET A 358     7830   6404   5012  -1209    573   -432       O  
ATOM    985  CB  MET A 358      -0.100  73.993  22.320  1.00 44.65           C  
ANISOU  985  CB  MET A 358     6923   5743   4299   -967    375   -356       C  
ATOM    986  CG  MET A 358      -1.202  72.967  22.522  1.00 49.31           C  
ANISOU  986  CG  MET A 358     7453   6376   4908   -875    307   -334       C  
ATOM    987  SD  MET A 358      -1.213  71.715  21.226  1.00 46.02           S  
ANISOU  987  SD  MET A 358     7053   5954   4478   -911    342   -357       S  
ATOM    988  CE  MET A 358      -1.791  72.670  19.825  1.00 68.88           C  
ANISOU  988  CE  MET A 358    10105   8769   7295   -943    321   -325       C  
ATOM    989  N   THR A 359       3.346  74.691  22.554  1.00 46.97           N  
ANISOU  989  N   THR A 359     7199   6021   4629  -1218    607   -496       N  
ATOM    990  CA  THR A 359       4.410  75.582  22.098  1.00 42.45           C  
ANISOU  990  CA  THR A 359     6692   5397   4040  -1341    705   -538       C  
ATOM    991  C   THR A 359       5.539  74.793  21.449  1.00 45.15           C  
ANISOU  991  C   THR A 359     6998   5742   4416  -1446    830   -622       C  
ATOM    992  O   THR A 359       6.499  75.375  20.948  1.00 50.46           O  
ANISOU  992  O   THR A 359     7717   6369   5085  -1563    937   -674       O  
ATOM    993  CB  THR A 359       4.988  76.425  23.253  1.00 39.96           C  
ANISOU  993  CB  THR A 359     6344   5098   3742  -1357    703   -558       C  
ATOM    994  OG1 THR A 359       5.476  75.559  24.285  1.00 47.85           O  
ANISOU  994  OG1 THR A 359     7211   6173   4798  -1333    698   -605       O  
ATOM    995  CG2 THR A 359       3.928  77.344  23.826  1.00 41.68           C  
ANISOU  995  CG2 THR A 359     6609   5301   3929  -1263    595   -483       C  
ATOM    996  N   LYS A 360       5.421  73.468  21.466  1.00 39.95           N  
ANISOU  996  N   LYS A 360     6253   5132   3793  -1406    824   -642       N  
ATOM    997  CA  LYS A 360       6.443  72.597  20.891  1.00 35.79           C  
ANISOU  997  CA  LYS A 360     5676   4611   3313  -1495    944   -732       C  
ATOM    998  C   LYS A 360       6.083  72.149  19.472  1.00 43.97           C  
ANISOU  998  C   LYS A 360     6797   5599   4310  -1519    975   -719       C  
ATOM    999  O   LYS A 360       4.934  72.275  19.044  1.00 43.12           O  
ANISOU  999  O   LYS A 360     6768   5471   4145  -1450    886   -641       O  
ATOM   1000  CB  LYS A 360       6.658  71.373  21.785  1.00 34.74           C  
ANISOU 1000  CB  LYS A 360     5394   4557   3248  -1446    927   -777       C  
ATOM   1001  CG  LYS A 360       6.933  71.683  23.247  1.00 22.41           C  
ANISOU 1001  CG  LYS A 360     3752   3047   1716  -1411    878   -792       C  
ATOM   1002  CD  LYS A 360       8.293  72.319  23.456  1.00 24.91           C  
ANISOU 1002  CD  LYS A 360     4033   3356   2074  -1525    984   -889       C  
ATOM   1003  CE  LYS A 360       8.532  72.586  24.935  1.00 35.71           C  
ANISOU 1003  CE  LYS A 360     5326   4777   3464  -1485    917   -911       C  
ATOM   1004  NZ  LYS A 360       9.769  73.385  25.155  1.00 48.03           N  
ANISOU 1004  NZ  LYS A 360     6858   6326   5065  -1594   1009  -1010       N  
ATOM   1005  N   ASN A 361       7.069  71.619  18.752  1.00 50.19           N  
ANISOU 1005  N   ASN A 361     7568   6369   5134  -1618   1104   -804       N  
ATOM   1006  CA  ASN A 361       6.853  71.133  17.390  1.00 49.38           C  
ANISOU 1006  CA  ASN A 361     7552   6218   4991  -1652   1146   -803       C  
ATOM   1007  C   ASN A 361       6.119  69.802  17.377  1.00 48.34           C  
ANISOU 1007  C   ASN A 361     7360   6134   4872  -1565   1083   -786       C  
ATOM   1008  O   ASN A 361       5.347  69.512  16.462  1.00 45.34           O  
ANISOU 1008  O   ASN A 361     7067   5725   4434  -1543   1048   -744       O  
ATOM   1009  CB  ASN A 361       8.182  70.998  16.650  1.00 54.86           C  
ANISOU 1009  CB  ASN A 361     8245   6870   5729  -1789   1317   -911       C  
ATOM   1010  CG  ASN A 361       8.889  72.326  16.476  1.00 63.95           C  
ANISOU 1010  CG  ASN A 361     9478   7958   6861  -1890   1393   -934       C  
ATOM   1011  OD1 ASN A 361       8.247  73.364  16.318  1.00 68.03           O  
ANISOU 1011  OD1 ASN A 361    10117   8432   7297  -1874   1327   -856       O  
ATOM   1012  ND2 ASN A 361      10.216  72.302  16.512  1.00 69.14           N  
ANISOU 1012  ND2 ASN A 361    10063   8605   7602  -1996   1535  -1051       N  
ATOM   1013  N   GLN A 362       6.369  68.993  18.398  1.00 47.90           N  
ANISOU 1013  N   GLN A 362     7160   6148   4891  -1521   1068   -823       N  
ATOM   1014  CA  GLN A 362       5.661  67.735  18.561  1.00 46.78           C  
ANISOU 1014  CA  GLN A 362     6956   6052   4766  -1437   1004   -808       C  
ATOM   1015  C   GLN A 362       4.854  67.748  19.853  1.00 39.24           C  
ANISOU 1015  C   GLN A 362     5942   5152   3816  -1325    877   -748       C  
ATOM   1016  O   GLN A 362       5.264  68.351  20.845  1.00 42.40           O  
ANISOU 1016  O   GLN A 362     6296   5575   4239  -1322    866   -757       O  
ATOM   1017  CB  GLN A 362       6.641  66.561  18.552  1.00 52.98           C  
ANISOU 1017  CB  GLN A 362     7626   6863   5640  -1483   1106   -915       C  
ATOM   1018  CG  GLN A 362       7.500  66.489  17.301  1.00 57.35           C  
ANISOU 1018  CG  GLN A 362     8228   7357   6203  -1598   1247   -986       C  
ATOM   1019  CD  GLN A 362       7.746  65.062  16.850  1.00 70.21           C  
ANISOU 1019  CD  GLN A 362     9788   8998   7890  -1603   1304  -1054       C  
ATOM   1020  OE1 GLN A 362       8.523  64.329  17.462  1.00 73.05           O  
ANISOU 1020  OE1 GLN A 362    10005   9395   8357  -1608   1357  -1143       O  
ATOM   1021  NE2 GLN A 362       7.075  64.657  15.775  1.00 73.69           N  
ANISOU 1021  NE2 GLN A 362    10329   9406   8264  -1599   1292  -1017       N  
ATOM   1022  N   VAL A 363       3.698  67.095  19.834  1.00 30.65           N  
ANISOU 1022  N   VAL A 363     4858   4081   2706  -1236    786   -693       N  
ATOM   1023  CA  VAL A 363       2.854  67.030  21.019  1.00 32.75           C  
ANISOU 1023  CA  VAL A 363     5073   4392   2980  -1132    674   -639       C  
ATOM   1024  C   VAL A 363       2.534  65.591  21.389  1.00 35.99           C  
ANISOU 1024  C   VAL A 363     5398   4847   3429  -1083    650   -657       C  
ATOM   1025  O   VAL A 363       2.714  64.676  20.585  1.00 32.99           O  
ANISOU 1025  O   VAL A 363     5014   4460   3061  -1115    702   -699       O  
ATOM   1026  CB  VAL A 363       1.544  67.804  20.827  1.00 35.53           C  
ANISOU 1026  CB  VAL A 363     5510   4718   3274  -1063    576   -551       C  
ATOM   1027  CG1 VAL A 363       1.828  69.292  20.713  1.00 35.51           C  
ANISOU 1027  CG1 VAL A 363     5584   4671   3236  -1102    588   -531       C  
ATOM   1028  CG2 VAL A 363       0.803  67.288  19.602  1.00 35.31           C  
ANISOU 1028  CG2 VAL A 363     5550   4660   3205  -1060    563   -535       C  
ATOM   1029  N   SER A 364       2.056  65.399  22.613  1.00 32.17           N  
ANISOU 1029  N   SER A 364     4853   4406   2963  -1007    574   -628       N  
ATOM   1030  CA  SER A 364       1.798  64.062  23.122  1.00 30.53           C  
ANISOU 1030  CA  SER A 364     4568   4240   2792   -965    551   -647       C  
ATOM   1031  C   SER A 364       0.304  63.788  23.225  1.00 33.67           C  
ANISOU 1031  C   SER A 364     4992   4641   3162   -880    457   -574       C  
ATOM   1032  O   SER A 364      -0.438  64.562  23.826  1.00 33.03           O  
ANISOU 1032  O   SER A 364     4932   4558   3060   -822    389   -515       O  
ATOM   1033  CB  SER A 364       2.456  63.874  24.491  1.00 28.15           C  
ANISOU 1033  CB  SER A 364     4179   3987   2532   -953    542   -683       C  
ATOM   1034  OG  SER A 364       3.753  64.443  24.525  1.00 32.07           O  
ANISOU 1034  OG  SER A 364     4650   4480   3054  -1030    618   -753       O  
ATOM   1035  N   LEU A 365      -0.134  62.687  22.623  1.00 32.57           N  
ANISOU 1035  N   LEU A 365     4846   4502   3027   -875    460   -589       N  
ATOM   1036  CA  LEU A 365      -1.490  62.197  22.819  1.00 29.01           C  
ANISOU 1036  CA  LEU A 365     4399   4061   2563   -805    381   -540       C  
ATOM   1037  C   LEU A 365      -1.444  61.048  23.818  1.00 29.33           C  
ANISOU 1037  C   LEU A 365     4353   4146   2645   -780    373   -563       C  
ATOM   1038  O   LEU A 365      -0.686  60.096  23.647  1.00 32.52           O  
ANISOU 1038  O   LEU A 365     4710   4563   3085   -820    430   -630       O  
ATOM   1039  CB  LEU A 365      -2.114  61.751  21.496  1.00 27.10           C  
ANISOU 1039  CB  LEU A 365     4218   3790   2290   -819    378   -543       C  
ATOM   1040  CG  LEU A 365      -2.071  62.765  20.347  1.00 30.46           C  
ANISOU 1040  CG  LEU A 365     4744   4166   2663   -856    392   -528       C  
ATOM   1041  CD1 LEU A 365      -2.929  62.292  19.179  1.00 35.58           C  
ANISOU 1041  CD1 LEU A 365     5460   4790   3270   -855    362   -523       C  
ATOM   1042  CD2 LEU A 365      -2.495  64.153  20.805  1.00 33.30           C  
ANISOU 1042  CD2 LEU A 365     5139   4514   2998   -819    339   -473       C  
ATOM   1043  N   THR A 366      -2.253  61.142  24.867  1.00 27.17           N  
ANISOU 1043  N   THR A 366     4062   3895   2369   -717    307   -513       N  
ATOM   1044  CA  THR A 366      -2.154  60.204  25.977  1.00 20.43           C  
ANISOU 1044  CA  THR A 366     3139   3082   1542   -697    296   -527       C  
ATOM   1045  C   THR A 366      -3.354  59.268  26.073  1.00 32.62           C  
ANISOU 1045  C   THR A 366     4675   4637   3084   -661    257   -503       C  
ATOM   1046  O   THR A 366      -4.504  59.708  26.035  1.00 34.20           O  
ANISOU 1046  O   THR A 366     4910   4825   3261   -622    209   -452       O  
ATOM   1047  CB  THR A 366      -2.004  60.951  27.312  1.00 23.97           C  
ANISOU 1047  CB  THR A 366     3574   3549   1985   -661    261   -492       C  
ATOM   1048  OG1 THR A 366      -0.760  61.662  27.323  1.00 19.63           O  
ANISOU 1048  OG1 THR A 366     3020   2997   1443   -707    300   -533       O  
ATOM   1049  CG2 THR A 366      -2.049  59.985  28.481  1.00 15.82           C  
ANISOU 1049  CG2 THR A 366     2491   2557    964   -637    237   -495       C  
ATOM   1050  N   CYS A 367      -3.078  57.973  26.202  1.00 34.35           N  
ANISOU 1050  N   CYS A 367     4845   4878   3330   -680    280   -551       N  
ATOM   1051  CA  CYS A 367      -4.118  56.989  26.465  1.00 32.96           C  
ANISOU 1051  CA  CYS A 367     4654   4717   3153   -657    250   -536       C  
ATOM   1052  C   CYS A 367      -3.932  56.381  27.847  1.00 35.92           C  
ANISOU 1052  C   CYS A 367     4952   5096   3599   -605    225   -500       C  
ATOM   1053  O   CYS A 367      -2.999  55.613  28.080  1.00 26.88           O  
ANISOU 1053  O   CYS A 367     3742   3940   2533   -602    240   -530       O  
ATOM   1054  CB  CYS A 367      -4.110  55.890  25.397  1.00 26.10           C  
ANISOU 1054  CB  CYS A 367     3773   3829   2315   -689    281   -591       C  
ATOM   1055  SG  CYS A 367      -5.464  54.694  25.520  1.00 33.89           S  
ANISOU 1055  SG  CYS A 367     4720   4800   3355   -647    234   -554       S  
ATOM   1056  N   LEU A 368      -4.822  56.740  28.767  1.00 38.68           N  
ANISOU 1056  N   LEU A 368     5317   5456   3924   -561    186   -435       N  
ATOM   1057  CA  LEU A 368      -4.819  56.151  30.098  1.00 30.04           C  
ANISOU 1057  CA  LEU A 368     4177   4358   2881   -512    163   -389       C  
ATOM   1058  C   LEU A 368      -5.688  54.901  30.132  1.00 36.62           C  
ANISOU 1058  C   LEU A 368     4973   5169   3772   -491    158   -367       C  
ATOM   1059  O   LEU A 368      -6.858  54.931  29.744  1.00 39.44           O  
ANISOU 1059  O   LEU A 368     5348   5526   4113   -490    153   -351       O  
ATOM   1060  CB  LEU A 368      -5.299  57.166  31.136  1.00 21.75           C  
ANISOU 1060  CB  LEU A 368     3170   3323   1770   -482    140   -336       C  
ATOM   1061  CG  LEU A 368      -5.693  56.623  32.512  1.00 26.43           C  
ANISOU 1061  CG  LEU A 368     3750   3906   2386   -434    122   -277       C  
ATOM   1062  CD1 LEU A 368      -4.522  55.930  33.180  1.00 28.08           C  
ANISOU 1062  CD1 LEU A 368     3921   4100   2649   -421    100   -283       C  
ATOM   1063  CD2 LEU A 368      -6.226  57.741  33.395  1.00 28.79           C  
ANISOU 1063  CD2 LEU A 368     4104   4220   2613   -412    114   -236       C  
ATOM   1064  N   VAL A 369      -5.097  53.801  30.586  1.00 33.26           N  
ANISOU 1064  N   VAL A 369     4493   4720   3424   -474    155   -369       N  
ATOM   1065  CA  VAL A 369      -5.813  52.543  30.732  1.00 29.42           C  
ANISOU 1065  CA  VAL A 369     3972   4204   3000   -456    153   -345       C  
ATOM   1066  C   VAL A 369      -5.678  52.059  32.172  1.00 34.20           C  
ANISOU 1066  C   VAL A 369     4572   4791   3633   -413    130   -286       C  
ATOM   1067  O   VAL A 369      -4.586  51.697  32.607  1.00 35.52           O  
ANISOU 1067  O   VAL A 369     4715   4941   3842   -399    107   -298       O  
ATOM   1068  CB  VAL A 369      -5.280  51.466  29.774  1.00 28.86           C  
ANISOU 1068  CB  VAL A 369     3854   4107   3003   -479    172   -405       C  
ATOM   1069  CG1 VAL A 369      -6.134  50.220  29.857  1.00 27.09           C  
ANISOU 1069  CG1 VAL A 369     3600   3849   2843   -465    170   -382       C  
ATOM   1070  CG2 VAL A 369      -5.248  51.989  28.348  1.00 29.28           C  
ANISOU 1070  CG2 VAL A 369     3938   4177   3012   -528    199   -467       C  
ATOM   1071  N   LYS A 370      -6.781  52.057  32.915  1.00 26.93           N  
ANISOU 1071  N   LYS A 370     3677   3865   2690   -393    135   -227       N  
ATOM   1072  CA  LYS A 370      -6.713  51.716  34.333  1.00 31.04           C  
ANISOU 1072  CA  LYS A 370     4222   4363   3208   -358    120   -165       C  
ATOM   1073  C   LYS A 370      -7.731  50.665  34.757  1.00 29.46           C  
ANISOU 1073  C   LYS A 370     4017   4126   3052   -350    145   -120       C  
ATOM   1074  O   LYS A 370      -8.700  50.397  34.051  1.00 27.67           O  
ANISOU 1074  O   LYS A 370     3762   3897   2854   -368    173   -133       O  
ATOM   1075  CB  LYS A 370      -6.893  52.971  35.191  1.00 30.75           C  
ANISOU 1075  CB  LYS A 370     4247   4354   3081   -345    117   -132       C  
ATOM   1076  CG  LYS A 370      -8.186  53.718  34.930  1.00 32.96           C  
ANISOU 1076  CG  LYS A 370     4545   4656   3323   -352    152   -123       C  
ATOM   1077  CD  LYS A 370      -8.516  54.690  36.056  1.00 32.90           C  
ANISOU 1077  CD  LYS A 370     4600   4661   3240   -331    161    -81       C  
ATOM   1078  CE  LYS A 370      -8.968  53.956  37.309  1.00 31.86           C  
ANISOU 1078  CE  LYS A 370     4501   4494   3108   -311    185    -21       C  
ATOM   1079  NZ  LYS A 370      -9.545  54.885  38.320  1.00 29.96           N  
ANISOU 1079  NZ  LYS A 370     4327   4263   2792   -297    216     13       N  
ATOM   1080  N   GLY A 371      -7.486  50.070  35.919  1.00 26.18           N  
ANISOU 1080  N   GLY A 371     3634   3673   2639   -324    131    -68       N  
ATOM   1081  CA  GLY A 371      -8.428  49.158  36.533  1.00 25.66           C  
ANISOU 1081  CA  GLY A 371     3584   3565   2602   -321    166    -15       C  
ATOM   1082  C   GLY A 371      -8.532  47.793  35.882  1.00 35.54           C  
ANISOU 1082  C   GLY A 371     4780   4772   3952   -333    171    -33       C  
ATOM   1083  O   GLY A 371      -9.529  47.093  36.069  1.00 33.24           O  
ANISOU 1083  O   GLY A 371     4486   4448   3697   -344    214     -3       O  
ATOM   1084  N   PHE A 372      -7.516  47.397  35.122  1.00 35.84           N  
ANISOU 1084  N   PHE A 372     4771   4804   4041   -333    135    -87       N  
ATOM   1085  CA  PHE A 372      -7.562  46.080  34.499  1.00 29.61           C  
ANISOU 1085  CA  PHE A 372     3932   3968   3349   -343    141   -111       C  
ATOM   1086  C   PHE A 372      -6.788  45.033  35.289  1.00 30.41           C  
ANISOU 1086  C   PHE A 372     4047   4005   3504   -312    100    -79       C  
ATOM   1087  O   PHE A 372      -5.791  45.331  35.948  1.00 38.24           O  
ANISOU 1087  O   PHE A 372     5063   4993   4474   -283     47    -68       O  
ATOM   1088  CB  PHE A 372      -7.053  46.128  33.055  1.00 27.34           C  
ANISOU 1088  CB  PHE A 372     3587   3704   3098   -367    140   -200       C  
ATOM   1089  CG  PHE A 372      -5.635  46.609  32.902  1.00 33.37           C  
ANISOU 1089  CG  PHE A 372     4335   4485   3858   -357    108   -245       C  
ATOM   1090  CD1 PHE A 372      -4.581  45.710  32.898  1.00 32.55           C  
ANISOU 1090  CD1 PHE A 372     4190   4335   3842   -338     79   -275       C  
ATOM   1091  CD2 PHE A 372      -5.359  47.954  32.714  1.00 35.79           C  
ANISOU 1091  CD2 PHE A 372     4663   4847   4088   -369    110   -265       C  
ATOM   1092  CE1 PHE A 372      -3.278  46.142  32.736  1.00 33.09           C  
ANISOU 1092  CE1 PHE A 372     4226   4416   3931   -332     55   -327       C  
ATOM   1093  CE2 PHE A 372      -4.056  48.395  32.552  1.00 31.75           C  
ANISOU 1093  CE2 PHE A 372     4129   4348   3587   -368     89   -313       C  
ATOM   1094  CZ  PHE A 372      -3.013  47.487  32.565  1.00 28.94           C  
ANISOU 1094  CZ  PHE A 372     3719   3948   3328   -350     64   -347       C  
ATOM   1095  N   TYR A 373      -7.290  43.808  35.228  1.00 31.00           N  
ANISOU 1095  N   TYR A 373     4108   4021   3651   -318    118    -63       N  
ATOM   1096  CA  TYR A 373      -6.619  42.647  35.790  1.00 38.22           C  
ANISOU 1096  CA  TYR A 373     5032   4858   4631   -289     75    -37       C  
ATOM   1097  C   TYR A 373      -6.982  41.431  34.946  1.00 42.11           C  
ANISOU 1097  C   TYR A 373     5470   5303   5228   -309    100    -72       C  
ATOM   1098  O   TYR A 373      -8.133  41.280  34.549  1.00 43.49           O  
ANISOU 1098  O   TYR A 373     5632   5483   5409   -343    154    -71       O  
ATOM   1099  CB  TYR A 373      -7.016  42.430  37.250  1.00 37.49           C  
ANISOU 1099  CB  TYR A 373     5038   4721   4485   -273     72     62       C  
ATOM   1100  CG  TYR A 373      -6.193  41.370  37.946  1.00 39.59           C  
ANISOU 1100  CG  TYR A 373     5339   4901   4803   -235      3     98       C  
ATOM   1101  CD1 TYR A 373      -6.522  40.026  37.841  1.00 45.56           C  
ANISOU 1101  CD1 TYR A 373     6088   5578   5644   -241     16    114       C  
ATOM   1102  CD2 TYR A 373      -5.082  41.714  38.704  1.00 36.73           C  
ANISOU 1102  CD2 TYR A 373     5017   4529   4410   -193    -85    114       C  
ATOM   1103  CE1 TYR A 373      -5.767  39.057  38.468  1.00 40.99           C  
ANISOU 1103  CE1 TYR A 373     5547   4910   5116   -202    -57    148       C  
ATOM   1104  CE2 TYR A 373      -4.325  40.748  39.337  1.00 39.03           C  
ANISOU 1104  CE2 TYR A 373     5342   4732   4755   -152   -168    146       C  
ATOM   1105  CZ  TYR A 373      -4.672  39.422  39.214  1.00 39.25           C  
ANISOU 1105  CZ  TYR A 373     5368   4679   4865   -155   -154    165       C  
ATOM   1106  OH  TYR A 373      -3.924  38.453  39.840  1.00 41.76           O  
ANISOU 1106  OH  TYR A 373     5726   4900   5241   -110   -245    200       O  
ATOM   1107  N   PRO A 374      -6.005  40.560  34.658  1.00 45.97           N  
ANISOU 1107  N   PRO A 374     5919   5741   5806   -286     57   -110       N  
ATOM   1108  CA  PRO A 374      -4.579  40.658  34.996  1.00 39.29           C  
ANISOU 1108  CA  PRO A 374     5061   4881   4986   -244    -15   -129       C  
ATOM   1109  C   PRO A 374      -3.829  41.699  34.167  1.00 39.20           C  
ANISOU 1109  C   PRO A 374     4995   4942   4956   -255    -11   -212       C  
ATOM   1110  O   PRO A 374      -4.439  42.402  33.363  1.00 35.85           O  
ANISOU 1110  O   PRO A 374     4561   4579   4481   -295     43   -245       O  
ATOM   1111  CB  PRO A 374      -4.052  39.246  34.705  1.00 38.66           C  
ANISOU 1111  CB  PRO A 374     4937   4715   5036   -223    -43   -158       C  
ATOM   1112  CG  PRO A 374      -5.011  38.676  33.719  1.00 38.73           C  
ANISOU 1112  CG  PRO A 374     4913   4721   5083   -268     27   -193       C  
ATOM   1113  CD  PRO A 374      -6.345  39.243  34.092  1.00 45.12           C  
ANISOU 1113  CD  PRO A 374     5774   5568   5800   -300     77   -132       C  
ATOM   1114  N   SER A 375      -2.519  41.785  34.376  1.00 37.04           N  
ANISOU 1114  N   SER A 375     4689   4654   4729   -221    -71   -245       N  
ATOM   1115  CA  SER A 375      -1.691  42.807  33.744  1.00 32.00           C  
ANISOU 1115  CA  SER A 375     4003   4078   4079   -236    -63   -320       C  
ATOM   1116  C   SER A 375      -1.465  42.545  32.259  1.00 34.11           C  
ANISOU 1116  C   SER A 375     4197   4356   4409   -272      0   -424       C  
ATOM   1117  O   SER A 375      -1.018  43.430  31.529  1.00 40.61           O  
ANISOU 1117  O   SER A 375     4996   5231   5203   -303     36   -488       O  
ATOM   1118  CB  SER A 375      -0.347  42.918  34.463  1.00 32.92           C  
ANISOU 1118  CB  SER A 375     4095   4167   4247   -190   -149   -331       C  
ATOM   1119  OG  SER A 375       0.344  41.684  34.449  1.00 32.45           O  
ANISOU 1119  OG  SER A 375     3980   4026   4324   -153   -193   -358       O  
ATOM   1120  N   ASP A 376      -1.770  41.329  31.816  1.00 36.51           N  
ANISOU 1120  N   ASP A 376     4475   4603   4793   -274     17   -440       N  
ATOM   1121  CA  ASP A 376      -1.628  40.966  30.408  1.00 33.33           C  
ANISOU 1121  CA  ASP A 376     4018   4201   4443   -311     80   -541       C  
ATOM   1122  C   ASP A 376      -2.530  41.840  29.546  1.00 35.37           C  
ANISOU 1122  C   ASP A 376     4316   4531   4594   -367    139   -556       C  
ATOM   1123  O   ASP A 376      -3.755  41.802  29.672  1.00 41.82           O  
ANISOU 1123  O   ASP A 376     5176   5356   5358   -381    146   -501       O  
ATOM   1124  CB  ASP A 376      -1.955  39.486  30.196  1.00 35.98           C  
ANISOU 1124  CB  ASP A 376     4334   4459   4878   -302     82   -546       C  
ATOM   1125  CG  ASP A 376      -1.014  38.565  30.954  1.00 43.62           C  
ANISOU 1125  CG  ASP A 376     5266   5343   5965   -242     13   -537       C  
ATOM   1126  OD1 ASP A 376       0.186  38.902  31.074  1.00 48.91           O  
ANISOU 1126  OD1 ASP A 376     5885   6014   6687   -216    -18   -583       O  
ATOM   1127  OD2 ASP A 376      -1.474  37.503  31.429  1.00 44.17           O  
ANISOU 1127  OD2 ASP A 376     5358   5340   6083   -221    -13   -484       O  
ATOM   1128  N   ILE A 377      -1.921  42.628  28.666  1.00 34.14           N  
ANISOU 1128  N   ILE A 377     4144   4419   4408   -400    180   -633       N  
ATOM   1129  CA  ILE A 377      -2.665  43.615  27.896  1.00 33.48           C  
ANISOU 1129  CA  ILE A 377     4114   4399   4209   -450    220   -643       C  
ATOM   1130  C   ILE A 377      -1.851  44.092  26.693  1.00 32.24           C  
ANISOU 1130  C   ILE A 377     3945   4264   4042   -495    281   -747       C  
ATOM   1131  O   ILE A 377      -0.623  44.005  26.692  1.00 28.95           O  
ANISOU 1131  O   ILE A 377     3470   3830   3700   -487    295   -804       O  
ATOM   1132  CB  ILE A 377      -3.055  44.823  28.784  1.00 29.61           C  
ANISOU 1132  CB  ILE A 377     3675   3960   3617   -438    190   -566       C  
ATOM   1133  CG1 ILE A 377      -4.228  45.593  28.185  1.00 30.80           C  
ANISOU 1133  CG1 ILE A 377     3883   4156   3664   -474    211   -552       C  
ATOM   1134  CG2 ILE A 377      -1.865  45.742  29.022  1.00 31.28           C  
ANISOU 1134  CG2 ILE A 377     3871   4198   3817   -434    185   -595       C  
ATOM   1135  CD1 ILE A 377      -4.710  46.704  29.071  1.00 27.02           C  
ANISOU 1135  CD1 ILE A 377     3451   3718   3097   -459    187   -480       C  
ATOM   1136  N   ALA A 378      -2.543  44.575  25.664  1.00 26.33           N  
ANISOU 1136  N   ALA A 378     3253   3547   3204   -546    318   -774       N  
ATOM   1137  CA  ALA A 378      -1.889  45.135  24.485  1.00 26.40           C  
ANISOU 1137  CA  ALA A 378     3284   3576   3173   -601    386   -865       C  
ATOM   1138  C   ALA A 378      -2.535  46.462  24.107  1.00 33.81           C  
ANISOU 1138  C   ALA A 378     4312   4568   3967   -636    386   -839       C  
ATOM   1139  O   ALA A 378      -3.751  46.613  24.207  1.00 32.33           O  
ANISOU 1139  O   ALA A 378     4167   4393   3723   -630    344   -781       O  
ATOM   1140  CB  ALA A 378      -1.948  44.161  23.319  1.00 20.43           C  
ANISOU 1140  CB  ALA A 378     2527   2780   2455   -634    434   -947       C  
ATOM   1141  N   VAL A 379      -1.716  47.423  23.689  1.00 30.33           N  
ANISOU 1141  N   VAL A 379     3894   4153   3476   -672    434   -884       N  
ATOM   1142  CA  VAL A 379      -2.203  48.749  23.320  1.00 28.51           C  
ANISOU 1142  CA  VAL A 379     3758   3966   3109   -706    433   -861       C  
ATOM   1143  C   VAL A 379      -1.590  49.209  21.999  1.00 35.26           C  
ANISOU 1143  C   VAL A 379     4675   4821   3902   -779    517   -950       C  
ATOM   1144  O   VAL A 379      -0.386  49.077  21.785  1.00 39.21           O  
ANISOU 1144  O   VAL A 379     5126   5306   4465   -801    587  -1022       O  
ATOM   1145  CB  VAL A 379      -1.894  49.793  24.418  1.00 30.62           C  
ANISOU 1145  CB  VAL A 379     4018   4266   3352   -678    400   -802       C  
ATOM   1146  CG1 VAL A 379      -2.449  51.157  24.040  1.00 26.96           C  
ANISOU 1146  CG1 VAL A 379     3654   3838   2751   -709    396   -777       C  
ATOM   1147  CG2 VAL A 379      -2.469  49.349  25.748  1.00 29.70           C  
ANISOU 1147  CG2 VAL A 379     3861   4145   3281   -612    328   -716       C  
ATOM   1148  N   GLU A 380      -2.424  49.739  21.109  1.00 36.27           N  
ANISOU 1148  N   GLU A 380     4913   4959   3910   -818    509   -946       N  
ATOM   1149  CA  GLU A 380      -1.962  50.234  19.818  1.00 38.85           C  
ANISOU 1149  CA  GLU A 380     5334   5279   4147   -895    588  -1022       C  
ATOM   1150  C   GLU A 380      -2.636  51.554  19.468  1.00 40.31           C  
ANISOU 1150  C   GLU A 380     5626   5477   4214   -901    540   -946       C  
ATOM   1151  O   GLU A 380      -3.653  51.918  20.065  1.00 42.25           O  
ANISOU 1151  O   GLU A 380     5887   5744   4423   -864    456   -879       O  
ATOM   1152  CB  GLU A 380      -2.232  49.199  18.719  1.00 33.90           C  
ANISOU 1152  CB  GLU A 380     4741   4615   3523   -928    617  -1089       C  
ATOM   1153  CG  GLU A 380      -1.481  47.891  18.900  1.00 40.83           C  
ANISOU 1153  CG  GLU A 380     5502   5458   4552   -908    663  -1147       C  
ATOM   1154  CD  GLU A 380      -2.043  46.770  18.049  1.00 41.93           C  
ANISOU 1154  CD  GLU A 380     5668   5560   4704   -924    664  -1195       C  
ATOM   1155  OE1 GLU A 380      -1.543  45.632  18.167  1.00 47.04           O  
ANISOU 1155  OE1 GLU A 380     6224   6170   5478   -904    694  -1242       O  
ATOM   1156  OE2 GLU A 380      -2.985  47.022  17.269  1.00 33.88           O  
ANISOU 1156  OE2 GLU A 380     4760   4541   3571   -954    625  -1187       O  
ATOM   1157  N   TRP A 381      -2.068  52.272  18.503  1.00 37.49           N  
ANISOU 1157  N   TRP A 381     5330   5094   3819   -938    589   -946       N  
ATOM   1158  CA  TRP A 381      -2.658  53.513  18.011  1.00 35.89           C  
ANISOU 1158  CA  TRP A 381     5226   4881   3530   -932    536   -867       C  
ATOM   1159  C   TRP A 381      -2.905  53.442  16.510  1.00 42.47           C  
ANISOU 1159  C   TRP A 381     6160   5671   4306   -967    546   -878       C  
ATOM   1160  O   TRP A 381      -2.214  52.714  15.791  1.00 41.45           O  
ANISOU 1160  O   TRP A 381     6028   5519   4201  -1011    628   -948       O  
ATOM   1161  CB  TRP A 381      -1.753  54.708  18.312  1.00 33.95           C  
ANISOU 1161  CB  TRP A 381     4981   4640   3280   -949    576   -849       C  
ATOM   1162  CG  TRP A 381      -1.651  55.076  19.760  1.00 39.91           C  
ANISOU 1162  CG  TRP A 381     5664   5435   4066   -909    544   -821       C  
ATOM   1163  CD1 TRP A 381      -0.843  54.498  20.693  1.00 39.10           C  
ANISOU 1163  CD1 TRP A 381     5462   5360   4035   -908    583   -876       C  
ATOM   1164  CD2 TRP A 381      -2.359  56.124  20.436  1.00 35.14           C  
ANISOU 1164  CD2 TRP A 381     5086   4845   3420   -864    465   -738       C  
ATOM   1165  NE1 TRP A 381      -1.009  55.112  21.914  1.00 35.58           N  
ANISOU 1165  NE1 TRP A 381     4989   4948   3582   -868    529   -826       N  
ATOM   1166  CE2 TRP A 381      -1.933  56.115  21.780  1.00 38.93           C  
ANISOU 1166  CE2 TRP A 381     5487   5363   3940   -841    462   -739       C  
ATOM   1167  CE3 TRP A 381      -3.315  57.064  20.038  1.00 29.11           C  
ANISOU 1167  CE3 TRP A 381     4403   4062   2595   -837    396   -669       C  
ATOM   1168  CZ2 TRP A 381      -2.427  57.010  22.724  1.00 36.34           C  
ANISOU 1168  CZ2 TRP A 381     5165   5053   3588   -795    399   -669       C  
ATOM   1169  CZ3 TRP A 381      -3.805  57.952  20.981  1.00 33.50           C  
ANISOU 1169  CZ3 TRP A 381     4952   4636   3142   -789    337   -607       C  
ATOM   1170  CH2 TRP A 381      -3.363  57.915  22.308  1.00 31.25           C  
ANISOU 1170  CH2 TRP A 381     4593   4388   2894   -769    342   -605       C  
ATOM   1171  N   GLU A 382      -3.885  54.202  16.035  1.00 46.67           N  
ANISOU 1171  N   GLU A 382     6781   6189   4763   -946    462   -816       N  
ATOM   1172  CA  GLU A 382      -4.129  54.307  14.604  1.00 49.95           C  
ANISOU 1172  CA  GLU A 382     7309   6561   5107   -977    460   -821       C  
ATOM   1173  C   GLU A 382      -4.857  55.594  14.255  1.00 47.70           C  
ANISOU 1173  C   GLU A 382     7117   6259   4746   -955    379   -750       C  
ATOM   1174  O   GLU A 382      -5.420  56.263  15.123  1.00 37.53           O  
ANISOU 1174  O   GLU A 382     5800   4994   3467   -905    313   -698       O  
ATOM   1175  CB  GLU A 382      -4.926  53.105  14.097  1.00 52.07           C  
ANISOU 1175  CB  GLU A 382     7588   6820   5377   -971    416   -856       C  
ATOM   1176  CG  GLU A 382      -6.406  53.127  14.441  1.00 56.70           C  
ANISOU 1176  CG  GLU A 382     8180   7417   5948   -918    284   -813       C  
ATOM   1177  CD  GLU A 382      -7.133  51.899  13.922  1.00 72.17           C  
ANISOU 1177  CD  GLU A 382    10145   9360   7918   -922    242   -860       C  
ATOM   1178  OE1 GLU A 382      -8.342  52.001  13.618  1.00 74.55           O  
ANISOU 1178  OE1 GLU A 382    10489   9651   8187   -896    130   -838       O  
ATOM   1179  OE2 GLU A 382      -6.489  50.832  13.818  1.00 77.25           O  
ANISOU 1179  OE2 GLU A 382    10744   9997   8609   -952    318   -925       O  
ATOM   1180  N   SER A 383      -4.836  55.933  12.972  1.00 50.54           N  
ANISOU 1180  N   SER A 383     7592   6576   5033   -992    389   -753       N  
ATOM   1181  CA  SER A 383      -5.495  57.133  12.476  1.00 47.90           C  
ANISOU 1181  CA  SER A 383     7359   6215   4624   -977    314   -694       C  
ATOM   1182  C   SER A 383      -5.952  56.913  11.039  1.00 54.91           C  
ANISOU 1182  C   SER A 383     8372   7059   5431  -1006    284   -709       C  
ATOM   1183  O   SER A 383      -5.172  56.467  10.197  1.00 57.76           O  
ANISOU 1183  O   SER A 383     8782   7394   5770  -1068    376   -754       O  
ATOM   1184  CB  SER A 383      -4.556  58.334  12.567  1.00 38.64           C  
ANISOU 1184  CB  SER A 383     6213   5030   3439  -1011    382   -672       C  
ATOM   1185  OG  SER A 383      -5.200  59.520  12.145  1.00 49.84           O  
ANISOU 1185  OG  SER A 383     7729   6417   4790   -996    308   -616       O  
ATOM   1186  N   ASN A 384      -7.217  57.231  10.771  1.00 58.33           N  
ANISOU 1186  N   ASN A 384     8859   7481   5823   -961    156   -674       N  
ATOM   1187  CA  ASN A 384      -7.838  56.975   9.473  1.00 59.81           C  
ANISOU 1187  CA  ASN A 384     9165   7626   5933   -979     98   -687       C  
ATOM   1188  C   ASN A 384      -7.586  55.555   8.967  1.00 57.15           C  
ANISOU 1188  C   ASN A 384     8817   7289   5611  -1011    147   -756       C  
ATOM   1189  O   ASN A 384      -7.113  55.360   7.845  1.00 55.30           O  
ANISOU 1189  O   ASN A 384     8682   7015   5314  -1068    204   -785       O  
ATOM   1190  CB  ASN A 384      -7.354  57.989   8.434  1.00 63.55           C  
ANISOU 1190  CB  ASN A 384     9785   8046   6315  -1033    136   -664       C  
ATOM   1191  CG  ASN A 384      -8.052  59.330   8.561  1.00 74.94           C  
ANISOU 1191  CG  ASN A 384    11281   9470   7722   -997     41   -599       C  
ATOM   1192  OD1 ASN A 384      -9.239  59.451   8.258  1.00 81.01           O  
ANISOU 1192  OD1 ASN A 384    12093  10224   8462   -956    -90   -580       O  
ATOM   1193  ND2 ASN A 384      -7.318  60.348   9.004  1.00 76.03           N  
ANISOU 1193  ND2 ASN A 384    11416   9605   7868  -1013    103   -569       N  
ATOM   1194  N   GLY A 385      -7.885  54.576   9.815  1.00 53.59           N  
ANISOU 1194  N   GLY A 385     8246   6874   5241   -978    129   -783       N  
ATOM   1195  CA  GLY A 385      -7.769  53.170   9.465  1.00 55.37           C  
ANISOU 1195  CA  GLY A 385     8447   7095   5494  -1001    164   -851       C  
ATOM   1196  C   GLY A 385      -6.353  52.624   9.461  1.00 61.11           C  
ANISOU 1196  C   GLY A 385     9135   7825   6261  -1055    322   -903       C  
ATOM   1197  O   GLY A 385      -6.148  51.412   9.394  1.00 68.31           O  
ANISOU 1197  O   GLY A 385     9999   8735   7219  -1070    364   -965       O  
ATOM   1198  N   GLN A 386      -5.375  53.517   9.542  1.00 60.55           N  
ANISOU 1198  N   GLN A 386     9076   7751   6180  -1087    410   -884       N  
ATOM   1199  CA  GLN A 386      -3.973  53.133   9.419  1.00 60.77           C  
ANISOU 1199  CA  GLN A 386     9070   7774   6248  -1148    565   -941       C  
ATOM   1200  C   GLN A 386      -3.208  53.271  10.735  1.00 57.91           C  
ANISOU 1200  C   GLN A 386     8571   7451   5981  -1135    621   -943       C  
ATOM   1201  O   GLN A 386      -3.423  54.222  11.486  1.00 58.83           O  
ANISOU 1201  O   GLN A 386     8667   7587   6097  -1101    571   -885       O  
ATOM   1202  CB  GLN A 386      -3.303  53.967   8.325  1.00 69.35           C  
ANISOU 1202  CB  GLN A 386    10285   8814   7252  -1218    639   -937       C  
ATOM   1203  CG  GLN A 386      -3.673  53.535   6.912  1.00 80.45           C  
ANISOU 1203  CG  GLN A 386    11826  10175   8568  -1254    628   -962       C  
ATOM   1204  CD  GLN A 386      -3.042  52.203   6.528  1.00 89.49           C  
ANISOU 1204  CD  GLN A 386    12933  11311   9757  -1293    730  -1051       C  
ATOM   1205  OE1 GLN A 386      -3.742  51.231   6.239  1.00 92.07           O  
ANISOU 1205  OE1 GLN A 386    13263  11636  10082  -1269    670  -1080       O  
ATOM   1206  NE2 GLN A 386      -1.712  52.154   6.528  1.00 91.57           N  
ANISOU 1206  NE2 GLN A 386    13154  11568  10070  -1354    884  -1100       N  
ATOM   1207  N   PRO A 387      -2.301  52.319  11.010  1.00 51.96           N  
ANISOU 1207  N   PRO A 387     7724   6705   5312  -1161    723  -1017       N  
ATOM   1208  CA  PRO A 387      -1.551  52.296  12.272  1.00 41.11           C  
ANISOU 1208  CA  PRO A 387     6214   5368   4037  -1147    770  -1033       C  
ATOM   1209  C   PRO A 387      -0.598  53.475  12.456  1.00 42.94           C  
ANISOU 1209  C   PRO A 387     6450   5599   4268  -1182    836  -1017       C  
ATOM   1210  O   PRO A 387       0.145  53.832  11.540  1.00 39.36           O  
ANISOU 1210  O   PRO A 387     6064   5109   3783  -1250    927  -1044       O  
ATOM   1211  CB  PRO A 387      -0.766  50.983  12.185  1.00 37.42           C  
ANISOU 1211  CB  PRO A 387     5665   4893   3660  -1174    869  -1132       C  
ATOM   1212  CG  PRO A 387      -0.650  50.702  10.728  1.00 45.20           C  
ANISOU 1212  CG  PRO A 387     6759   5832   4582  -1229    923  -1166       C  
ATOM   1213  CD  PRO A 387      -1.934  51.198  10.129  1.00 47.17           C  
ANISOU 1213  CD  PRO A 387     7134   6070   4717  -1203    798  -1095       C  
ATOM   1214  N   GLU A 388      -0.636  54.070  13.643  1.00 47.18           N  
ANISOU 1214  N   GLU A 388     6918   6172   4838  -1140    792   -976       N  
ATOM   1215  CA  GLU A 388       0.355  55.049  14.073  1.00 42.20           C  
ANISOU 1215  CA  GLU A 388     6259   5544   4230  -1171    854   -975       C  
ATOM   1216  C   GLU A 388       1.389  54.341  14.937  1.00 39.89           C  
ANISOU 1216  C   GLU A 388     5822   5277   4057  -1177    931  -1053       C  
ATOM   1217  O   GLU A 388       1.032  53.680  15.910  1.00 48.56           O  
ANISOU 1217  O   GLU A 388     6835   6410   5208  -1122    880  -1056       O  
ATOM   1218  CB  GLU A 388      -0.315  56.189  14.843  1.00 40.33           C  
ANISOU 1218  CB  GLU A 388     6039   5327   3955  -1119    754   -886       C  
ATOM   1219  CG  GLU A 388      -1.335  56.970  14.035  1.00 43.98           C  
ANISOU 1219  CG  GLU A 388     6633   5761   4317  -1104    670   -818       C  
ATOM   1220  CD  GLU A 388      -0.704  58.059  13.191  1.00 56.55           C  
ANISOU 1220  CD  GLU A 388     8327   7309   5853  -1170    731   -810       C  
ATOM   1221  OE1 GLU A 388      -1.372  58.559  12.261  1.00 56.53           O  
ANISOU 1221  OE1 GLU A 388     8448   7269   5763  -1174    682   -772       O  
ATOM   1222  OE2 GLU A 388       0.461  58.423  13.463  1.00 63.34           O  
ANISOU 1222  OE2 GLU A 388     9144   8167   6756  -1220    826   -846       O  
ATOM   1223  N   ASN A 389       2.663  54.468  14.589  1.00 38.45           N  
ANISOU 1223  N   ASN A 389     5611   5074   3923  -1245   1056  -1123       N  
ATOM   1224  CA  ASN A 389       3.681  53.656  15.244  1.00 45.42           C  
ANISOU 1224  CA  ASN A 389     6347   5971   4940  -1249   1135  -1220       C  
ATOM   1225  C   ASN A 389       4.699  54.436  16.066  1.00 45.48           C  
ANISOU 1225  C   ASN A 389     6272   5994   5012  -1268   1179  -1249       C  
ATOM   1226  O   ASN A 389       5.575  53.842  16.692  1.00 48.62           O  
ANISOU 1226  O   ASN A 389     6534   6402   5535  -1263   1235  -1338       O  
ATOM   1227  CB  ASN A 389       4.417  52.811  14.203  1.00 58.41           C  
ANISOU 1227  CB  ASN A 389     7984   7574   6636  -1310   1256  -1315       C  
ATOM   1228  CG  ASN A 389       3.634  51.577  13.799  1.00 64.29           C  
ANISOU 1228  CG  ASN A 389     8742   8311   7373  -1277   1219  -1326       C  
ATOM   1229  OD1 ASN A 389       3.066  50.880  14.638  1.00 60.69           O  
ANISOU 1229  OD1 ASN A 389     8219   7883   6958  -1212   1144  -1321       O  
ATOM   1230  ND2 ASN A 389       3.593  51.304  12.497  1.00 66.90           N  
ANISOU 1230  ND2 ASN A 389     9170   8601   7649  -1328   1272  -1345       N  
ATOM   1231  N   ASN A 390       4.588  55.762  16.069  1.00 38.41           N  
ANISOU 1231  N   ASN A 390     5456   5098   4041  -1285   1151  -1180       N  
ATOM   1232  CA  ASN A 390       5.492  56.584  16.868  1.00 33.84           C  
ANISOU 1232  CA  ASN A 390     4808   4534   3515  -1304   1185  -1206       C  
ATOM   1233  C   ASN A 390       4.960  56.743  18.291  1.00 39.36           C  
ANISOU 1233  C   ASN A 390     5451   5287   4218  -1224   1074  -1156       C  
ATOM   1234  O   ASN A 390       4.764  57.858  18.770  1.00 36.03           O  
ANISOU 1234  O   ASN A 390     5069   4876   3744  -1213   1022  -1092       O  
ATOM   1235  CB  ASN A 390       5.700  57.959  16.220  1.00 35.06           C  
ANISOU 1235  CB  ASN A 390     5075   4653   3592  -1368   1216  -1164       C  
ATOM   1236  CG  ASN A 390       6.841  58.742  16.860  1.00 41.60           C  
ANISOU 1236  CG  ASN A 390     5829   5488   4490  -1412   1281  -1217       C  
ATOM   1237  OD1 ASN A 390       7.642  58.188  17.614  1.00 46.90           O  
ANISOU 1237  OD1 ASN A 390     6356   6184   5282  -1404   1323  -1305       O  
ATOM   1238  ND2 ASN A 390       6.917  60.034  16.558  1.00 44.56           N  
ANISOU 1238  ND2 ASN A 390     6299   5835   4797  -1456   1288  -1171       N  
ATOM   1239  N   TYR A 391       4.722  55.618  18.961  1.00 37.90           N  
ANISOU 1239  N   TYR A 391     5178   5129   4093  -1168   1038  -1188       N  
ATOM   1240  CA  TYR A 391       4.207  55.647  20.323  1.00 33.99           C  
ANISOU 1240  CA  TYR A 391     4638   4681   3596  -1096    936  -1147       C  
ATOM   1241  C   TYR A 391       5.018  54.768  21.269  1.00 39.02           C  
ANISOU 1241  C   TYR A 391     5125   5334   4365  -1068    957  -1249       C  
ATOM   1242  O   TYR A 391       5.698  53.833  20.845  1.00 45.14           O  
ANISOU 1242  O   TYR A 391     5819   6080   5253  -1080   1028  -1336       O  
ATOM   1243  CB  TYR A 391       2.736  55.215  20.356  1.00 33.65           C  
ANISOU 1243  CB  TYR A 391     4657   4647   3481  -1038    831  -1061       C  
ATOM   1244  CG  TYR A 391       2.494  53.753  20.021  1.00 33.30           C  
ANISOU 1244  CG  TYR A 391     4575   4592   3487  -1025    847  -1117       C  
ATOM   1245  CD1 TYR A 391       2.571  52.769  21.003  1.00 35.29           C  
ANISOU 1245  CD1 TYR A 391     4718   4857   3833   -973    813  -1150       C  
ATOM   1246  CD2 TYR A 391       2.170  53.358  18.728  1.00 36.80           C  
ANISOU 1246  CD2 TYR A 391     5089   4997   3894  -1057    879  -1121       C  
ATOM   1247  CE1 TYR A 391       2.347  51.436  20.706  1.00 32.98           C  
ANISOU 1247  CE1 TYR A 391     4381   4537   3612   -951    813  -1180       C  
ATOM   1248  CE2 TYR A 391       1.939  52.021  18.420  1.00 39.06           C  
ANISOU 1248  CE2 TYR A 391     5343   5269   4228  -1047    892  -1175       C  
ATOM   1249  CZ  TYR A 391       2.031  51.065  19.417  1.00 35.49           C  
ANISOU 1249  CZ  TYR A 391     4784   4832   3867  -1003    872  -1227       C  
ATOM   1250  OH  TYR A 391       1.809  49.736  19.141  1.00 42.86           O  
ANISOU 1250  OH  TYR A 391     5678   5737   4871   -985    875  -1269       O  
ATOM   1251  N   LYS A 392       4.931  55.076  22.558  1.00 31.55           N  
ANISOU 1251  N   LYS A 392     4121   4411   3456  -1001    848  -1178       N  
ATOM   1252  CA  LYS A 392       5.546  54.253  23.587  1.00 27.75           C  
ANISOU 1252  CA  LYS A 392     3487   3917   3141   -931    786  -1186       C  
ATOM   1253  C   LYS A 392       4.546  54.014  24.709  1.00 33.68           C  
ANISOU 1253  C   LYS A 392     4247   4686   3863   -844    647  -1072       C  
ATOM   1254  O   LYS A 392       3.764  54.900  25.053  1.00 34.89           O  
ANISOU 1254  O   LYS A 392     4489   4870   3898   -837    598   -995       O  
ATOM   1255  CB  LYS A 392       6.818  54.908  24.127  1.00 34.25           C  
ANISOU 1255  CB  LYS A 392     4217   4735   4061   -946    803  -1237       C  
ATOM   1256  CG  LYS A 392       7.839  55.273  23.061  1.00 41.86           C  
ANISOU 1256  CG  LYS A 392     5170   5677   5059  -1044    960  -1354       C  
ATOM   1257  CD  LYS A 392       9.109  54.447  23.185  1.00 50.31           C  
ANISOU 1257  CD  LYS A 392     6062   6708   6344  -1032   1000  -1460       C  
ATOM   1258  CE  LYS A 392       9.115  53.272  22.225  1.00 50.42           C  
ANISOU 1258  CE  LYS A 392     6059   6690   6409  -1047   1087  -1532       C  
ATOM   1259  NZ  LYS A 392      10.443  52.599  22.196  1.00 55.36           N  
ANISOU 1259  NZ  LYS A 392     6509   7269   7254  -1047   1150  -1655       N  
ATOM   1260  N   THR A 393       4.570  52.811  25.269  1.00 34.23           N  
ANISOU 1260  N   THR A 393     4230   4733   4045   -780    590  -1064       N  
ATOM   1261  CA  THR A 393       3.636  52.439  26.320  1.00 29.31           C  
ANISOU 1261  CA  THR A 393     3620   4118   3400   -704    475   -959       C  
ATOM   1262  C   THR A 393       4.395  52.024  27.571  1.00 38.45           C  
ANISOU 1262  C   THR A 393     4676   5253   4680   -640    391   -947       C  
ATOM   1263  O   THR A 393       5.324  51.220  27.499  1.00 43.82           O  
ANISOU 1263  O   THR A 393     5251   5894   5504   -627    402  -1017       O  
ATOM   1264  CB  THR A 393       2.714  51.289  25.868  1.00 26.30           C  
ANISOU 1264  CB  THR A 393     3257   3718   3018   -687    472   -942       C  
ATOM   1265  OG1 THR A 393       2.071  51.645  24.636  1.00 29.47           O  
ANISOU 1265  OG1 THR A 393     3757   4133   3308   -748    538   -963       O  
ATOM   1266  CG2 THR A 393       1.656  50.991  26.924  1.00 18.62           C  
ANISOU 1266  CG2 THR A 393     2308   2751   2014   -621    373   -834       C  
ATOM   1267  N   THR A 394       4.010  52.585  28.713  1.00 36.09           N  
ANISOU 1267  N   THR A 394     4413   4974   4325   -597    301   -862       N  
ATOM   1268  CA  THR A 394       4.618  52.212  29.985  1.00 32.15           C  
ANISOU 1268  CA  THR A 394     3847   4450   3918   -533    200   -837       C  
ATOM   1269  C   THR A 394       4.282  50.765  30.311  1.00 29.76           C  
ANISOU 1269  C   THR A 394     3512   4105   3691   -477    152   -807       C  
ATOM   1270  O   THR A 394       3.291  50.230  29.809  1.00 28.43           O  
ANISOU 1270  O   THR A 394     3391   3938   3474   -483    183   -779       O  
ATOM   1271  CB  THR A 394       4.136  53.126  31.145  1.00 30.71           C  
ANISOU 1271  CB  THR A 394     3738   4296   3633   -503    120   -747       C  
ATOM   1272  OG1 THR A 394       2.823  52.730  31.560  1.00 26.14           O  
ANISOU 1272  OG1 THR A 394     3234   3723   2973   -469     90   -655       O  
ATOM   1273  CG2 THR A 394       4.126  54.590  30.721  1.00 25.96           C  
ANISOU 1273  CG2 THR A 394     3197   3736   2931   -561    173   -761       C  
ATOM   1274  N   PRO A 395       5.108  50.115  31.145  1.00 32.19           N  
ANISOU 1274  N   PRO A 395     3741   4367   4121   -422     69   -815       N  
ATOM   1275  CA  PRO A 395       4.716  48.791  31.635  1.00 35.62           C  
ANISOU 1275  CA  PRO A 395     4168   4754   4614   -364      9   -768       C  
ATOM   1276  C   PRO A 395       3.487  48.911  32.528  1.00 36.88           C  
ANISOU 1276  C   PRO A 395     4438   4929   4645   -336    -43   -646       C  
ATOM   1277  O   PRO A 395       3.175  50.012  32.973  1.00 38.16           O  
ANISOU 1277  O   PRO A 395     4666   5135   4699   -347    -54   -605       O  
ATOM   1278  CB  PRO A 395       5.939  48.326  32.436  1.00 31.03           C  
ANISOU 1278  CB  PRO A 395     3493   4118   4180   -309    -90   -797       C  
ATOM   1279  CG  PRO A 395       7.068  49.180  31.962  1.00 34.27           C  
ANISOU 1279  CG  PRO A 395     3824   4545   4652   -352    -45   -897       C  
ATOM   1280  CD  PRO A 395       6.453  50.497  31.606  1.00 31.56           C  
ANISOU 1280  CD  PRO A 395     3573   4271   4147   -412     23   -873       C  
ATOM   1281  N   PRO A 396       2.788  47.799  32.778  1.00 39.10           N  
ANISOU 1281  N   PRO A 396     4740   5173   4944   -303    -65   -594       N  
ATOM   1282  CA  PRO A 396       1.670  47.873  33.723  1.00 31.93           C  
ANISOU 1282  CA  PRO A 396     3932   4272   3928   -279   -103   -483       C  
ATOM   1283  C   PRO A 396       2.164  48.216  35.122  1.00 36.14           C  
ANISOU 1283  C   PRO A 396     4499   4789   4443   -234   -207   -430       C  
ATOM   1284  O   PRO A 396       3.226  47.740  35.527  1.00 36.85           O  
ANISOU 1284  O   PRO A 396     4529   4831   4640   -197   -284   -459       O  
ATOM   1285  CB  PRO A 396       1.068  46.460  33.678  1.00 33.70           C  
ANISOU 1285  CB  PRO A 396     4154   4442   4208   -258   -102   -454       C  
ATOM   1286  CG  PRO A 396       1.552  45.870  32.389  1.00 36.46           C  
ANISOU 1286  CG  PRO A 396     4419   4777   4658   -286    -39   -553       C  
ATOM   1287  CD  PRO A 396       2.907  46.469  32.155  1.00 36.92           C  
ANISOU 1287  CD  PRO A 396     4402   4844   4782   -294    -42   -638       C  
ATOM   1288  N   VAL A 397       1.418  49.045  35.844  1.00 34.96           N  
ANISOU 1288  N   VAL A 397     4446   4675   4163   -235   -215   -358       N  
ATOM   1289  CA  VAL A 397       1.795  49.412  37.205  1.00 32.71           C  
ANISOU 1289  CA  VAL A 397     4219   4374   3836   -195   -313   -305       C  
ATOM   1290  C   VAL A 397       0.693  49.030  38.184  1.00 32.44           C  
ANISOU 1290  C   VAL A 397     4297   4319   3710   -173   -325   -200       C  
ATOM   1291  O   VAL A 397      -0.478  49.347  37.974  1.00 35.08           O  
ANISOU 1291  O   VAL A 397     4680   4687   3961   -199   -247   -166       O  
ATOM   1292  CB  VAL A 397       2.095  50.922  37.324  1.00 31.33           C  
ANISOU 1292  CB  VAL A 397     4067   4255   3584   -221   -311   -326       C  
ATOM   1293  CG1 VAL A 397       2.493  51.276  38.752  1.00 26.59           C  
ANISOU 1293  CG1 VAL A 397     3535   3633   2935   -181   -421   -275       C  
ATOM   1294  CG2 VAL A 397       3.193  51.321  36.355  1.00 28.19           C  
ANISOU 1294  CG2 VAL A 397     3561   3872   3278   -254   -282   -433       C  
ATOM   1295  N   LEU A 398       1.078  48.338  39.251  1.00 32.67           N  
ANISOU 1295  N   LEU A 398     4369   4285   3760   -125   -422   -150       N  
ATOM   1296  CA  LEU A 398       0.135  47.910  40.278  1.00 32.44           C  
ANISOU 1296  CA  LEU A 398     4463   4223   3641   -108   -428    -49       C  
ATOM   1297  C   LEU A 398      -0.451  49.110  41.017  1.00 35.41           C  
ANISOU 1297  C   LEU A 398     4941   4645   3867   -121   -408     -4       C  
ATOM   1298  O   LEU A 398       0.287  49.941  41.544  1.00 33.83           O  
ANISOU 1298  O   LEU A 398     4761   4459   3632   -110   -477    -18       O  
ATOM   1299  CB  LEU A 398       0.826  46.957  41.258  1.00 29.77           C  
ANISOU 1299  CB  LEU A 398     4164   3796   3349    -54   -552     -7       C  
ATOM   1300  CG  LEU A 398      -0.058  46.208  42.258  1.00 37.07           C  
ANISOU 1300  CG  LEU A 398     5224   4663   4196    -40   -554     99       C  
ATOM   1301  CD1 LEU A 398      -1.071  45.333  41.537  1.00 33.81           C  
ANISOU 1301  CD1 LEU A 398     4783   4240   3823    -67   -447    109       C  
ATOM   1302  CD2 LEU A 398       0.797  45.375  43.199  1.00 36.13           C  
ANISOU 1302  CD2 LEU A 398     5157   4450   4119     17   -700    136       C  
ATOM   1303  N   ASP A 399      -1.778  49.195  41.048  1.00 31.92           N  
ANISOU 1303  N   ASP A 399     4558   4224   3348   -145   -314     44       N  
ATOM   1304  CA  ASP A 399      -2.458  50.319  41.683  1.00 36.11           C  
ANISOU 1304  CA  ASP A 399     5179   4795   3746   -158   -276     79       C  
ATOM   1305  C   ASP A 399      -2.812  49.987  43.134  1.00 41.69           C  
ANISOU 1305  C   ASP A 399     6028   5450   4362   -136   -306    167       C  
ATOM   1306  O   ASP A 399      -2.570  48.871  43.601  1.00 41.31           O  
ANISOU 1306  O   ASP A 399     6012   5332   4350   -112   -359    206       O  
ATOM   1307  CB  ASP A 399      -3.725  50.697  40.905  1.00 35.77           C  
ANISOU 1307  CB  ASP A 399     5113   4799   3680   -195   -155     71       C  
ATOM   1308  CG  ASP A 399      -3.909  52.201  40.773  1.00 37.36           C  
ANISOU 1308  CG  ASP A 399     5329   5064   3803   -213   -125     46       C  
ATOM   1309  OD1 ASP A 399      -3.368  52.946  41.619  1.00 40.20           O  
ANISOU 1309  OD1 ASP A 399     5752   5428   4094   -199   -180     57       O  
ATOM   1310  OD2 ASP A 399      -4.590  52.641  39.820  1.00 36.33           O  
ANISOU 1310  OD2 ASP A 399     5151   4973   3678   -241    -56     15       O  
ATOM   1311  N   SER A 400      -3.386  50.960  43.836  1.00 42.82           N  
ANISOU 1311  N   SER A 400     6265   5622   4383   -145   -268    197       N  
ATOM   1312  CA  SER A 400      -3.735  50.810  45.244  1.00 38.23           C  
ANISOU 1312  CA  SER A 400     5842   4994   3690   -132   -282    276       C  
ATOM   1313  C   SER A 400      -4.701  49.651  45.470  1.00 38.84           C  
ANISOU 1313  C   SER A 400     5964   5018   3776   -143   -208    337       C  
ATOM   1314  O   SER A 400      -4.601  48.931  46.463  1.00 42.90           O  
ANISOU 1314  O   SER A 400     6596   5462   4244   -127   -251    402       O  
ATOM   1315  CB  SER A 400      -4.354  52.104  45.779  1.00 34.56           C  
ANISOU 1315  CB  SER A 400     5456   4574   3100   -148   -221    283       C  
ATOM   1316  OG  SER A 400      -3.642  53.243  45.329  1.00 46.69           O  
ANISOU 1316  OG  SER A 400     6934   6165   4641   -150   -264    219       O  
ATOM   1317  N   ASP A 401      -5.627  49.470  44.537  1.00 35.37           N  
ANISOU 1317  N   ASP A 401     5435   4606   3397   -173   -101    314       N  
ATOM   1318  CA  ASP A 401      -6.726  48.531  44.735  1.00 34.12           C  
ANISOU 1318  CA  ASP A 401     5311   4402   3249   -194     -8    365       C  
ATOM   1319  C   ASP A 401      -6.437  47.130  44.195  1.00 34.07           C  
ANISOU 1319  C   ASP A 401     5242   4341   3362   -187    -40    365       C  
ATOM   1320  O   ASP A 401      -7.332  46.291  44.121  1.00 43.68           O  
ANISOU 1320  O   ASP A 401     6461   5521   4615   -211     38    395       O  
ATOM   1321  CB  ASP A 401      -7.994  49.086  44.088  1.00 32.14           C  
ANISOU 1321  CB  ASP A 401     4998   4204   3010   -229    120    339       C  
ATOM   1322  CG  ASP A 401      -7.893  49.176  42.578  1.00 45.93           C  
ANISOU 1322  CG  ASP A 401     6592   5998   4860   -238    117    264       C  
ATOM   1323  OD1 ASP A 401      -6.775  49.014  42.039  1.00 45.11           O  
ANISOU 1323  OD1 ASP A 401     6430   5898   4811   -221     32    223       O  
ATOM   1324  OD2 ASP A 401      -8.934  49.415  41.931  1.00 47.21           O  
ANISOU 1324  OD2 ASP A 401     6696   6190   5051   -263    201    241       O  
ATOM   1325  N   GLY A 402      -5.190  46.880  43.809  1.00 27.97           N  
ANISOU 1325  N   GLY A 402     4408   3559   2661   -157   -152    326       N  
ATOM   1326  CA  GLY A 402      -4.802  45.566  43.333  1.00 30.38           C  
ANISOU 1326  CA  GLY A 402     4654   3805   3085   -143   -191    319       C  
ATOM   1327  C   GLY A 402      -4.923  45.426  41.828  1.00 32.35           C  
ANISOU 1327  C   GLY A 402     4750   4096   3445   -165   -143    240       C  
ATOM   1328  O   GLY A 402      -4.417  44.473  41.247  1.00 39.51           O  
ANISOU 1328  O   GLY A 402     5587   4962   4462   -153   -178    210       O  
ATOM   1329  N   SER A 403      -5.601  46.376  41.194  1.00 33.87           N  
ANISOU 1329  N   SER A 403     4899   4363   3606   -196    -65    204       N  
ATOM   1330  CA  SER A 403      -5.696  46.392  39.739  1.00 36.90           C  
ANISOU 1330  CA  SER A 403     5160   4788   4072   -219    -29    127       C  
ATOM   1331  C   SER A 403      -4.450  47.040  39.133  1.00 35.87           C  
ANISOU 1331  C   SER A 403     4963   4696   3969   -209    -90     54       C  
ATOM   1332  O   SER A 403      -3.607  47.576  39.853  1.00 31.50           O  
ANISOU 1332  O   SER A 403     4448   4143   3376   -184   -161     62       O  
ATOM   1333  CB  SER A 403      -6.957  47.129  39.279  1.00 33.04           C  
ANISOU 1333  CB  SER A 403     4658   4353   3542   -254     66    119       C  
ATOM   1334  OG  SER A 403      -6.836  48.527  39.446  1.00 34.48           O  
ANISOU 1334  OG  SER A 403     4866   4595   3639   -254     63    105       O  
ATOM   1335  N   PHE A 404      -4.337  46.989  37.810  1.00 31.51           N  
ANISOU 1335  N   PHE A 404     4315   4172   3486   -232    -60    -19       N  
ATOM   1336  CA  PHE A 404      -3.198  47.588  37.129  1.00 29.52           C  
ANISOU 1336  CA  PHE A 404     3998   3953   3267   -234    -92    -96       C  
ATOM   1337  C   PHE A 404      -3.617  48.792  36.298  1.00 30.72           C  
ANISOU 1337  C   PHE A 404     4137   4176   3359   -271    -36   -137       C  
ATOM   1338  O   PHE A 404      -4.787  48.940  35.940  1.00 34.86           O  
ANISOU 1338  O   PHE A 404     4676   4721   3850   -294     23   -121       O  
ATOM   1339  CB  PHE A 404      -2.503  46.564  36.231  1.00 26.56           C  
ANISOU 1339  CB  PHE A 404     3532   3541   3019   -233   -101   -160       C  
ATOM   1340  CG  PHE A 404      -1.760  45.500  36.984  1.00 28.72           C  
ANISOU 1340  CG  PHE A 404     3805   3737   3369   -187   -181   -136       C  
ATOM   1341  CD1 PHE A 404      -2.395  44.327  37.355  1.00 36.66           C  
ANISOU 1341  CD1 PHE A 404     4845   4679   4404   -176   -177    -80       C  
ATOM   1342  CD2 PHE A 404      -0.424  45.668  37.313  1.00 30.45           C  
ANISOU 1342  CD2 PHE A 404     3990   3940   3640   -156   -265   -170       C  
ATOM   1343  CE1 PHE A 404      -1.713  43.344  38.046  1.00 31.57           C  
ANISOU 1343  CE1 PHE A 404     4215   3954   3829   -131   -260    -53       C  
ATOM   1344  CE2 PHE A 404       0.263  44.689  38.004  1.00 30.94           C  
ANISOU 1344  CE2 PHE A 404     4053   3921   3780   -107   -357   -148       C  
ATOM   1345  CZ  PHE A 404      -0.385  43.524  38.372  1.00 28.92           C  
ANISOU 1345  CZ  PHE A 404     3845   3599   3543    -93   -358    -86       C  
ATOM   1346  N   PHE A 405      -2.654  49.655  35.997  1.00 23.78           N  
ANISOU 1346  N   PHE A 405     3232   3330   2475   -279    -57   -190       N  
ATOM   1347  CA  PHE A 405      -2.880  50.744  35.060  1.00 25.23           C  
ANISOU 1347  CA  PHE A 405     3408   3570   2608   -318     -7   -235       C  
ATOM   1348  C   PHE A 405      -1.632  50.971  34.224  1.00 27.92           C  
ANISOU 1348  C   PHE A 405     3683   3920   3007   -340     -9   -321       C  
ATOM   1349  O   PHE A 405      -0.545  50.525  34.586  1.00 25.66           O  
ANISOU 1349  O   PHE A 405     3351   3602   2798   -317    -59   -345       O  
ATOM   1350  CB  PHE A 405      -3.278  52.038  35.785  1.00 28.08           C  
ANISOU 1350  CB  PHE A 405     3842   3969   2859   -316    -10   -195       C  
ATOM   1351  CG  PHE A 405      -2.118  52.784  36.394  1.00 25.08           C  
ANISOU 1351  CG  PHE A 405     3470   3595   2463   -305    -67   -212       C  
ATOM   1352  CD1 PHE A 405      -1.691  52.492  37.679  1.00 26.55           C  
ANISOU 1352  CD1 PHE A 405     3697   3748   2643   -265   -138   -166       C  
ATOM   1353  CD2 PHE A 405      -1.468  53.791  35.688  1.00 23.62           C  
ANISOU 1353  CD2 PHE A 405     3261   3445   2268   -337    -52   -273       C  
ATOM   1354  CE1 PHE A 405      -0.631  53.175  38.244  1.00 24.31           C  
ANISOU 1354  CE1 PHE A 405     3418   3467   2352   -255   -206   -186       C  
ATOM   1355  CE2 PHE A 405      -0.404  54.474  36.246  1.00 28.22           C  
ANISOU 1355  CE2 PHE A 405     3841   4030   2849   -332   -105   -295       C  
ATOM   1356  CZ  PHE A 405       0.013  54.167  37.528  1.00 27.57           C  
ANISOU 1356  CZ  PHE A 405     3789   3917   2770   -288   -187   -253       C  
ATOM   1357  N   LEU A 406      -1.799  51.665  33.104  1.00 29.42           N  
ANISOU 1357  N   LEU A 406     3869   4146   3164   -384     47   -370       N  
ATOM   1358  CA  LEU A 406      -0.670  52.109  32.302  1.00 25.91           C  
ANISOU 1358  CA  LEU A 406     3378   3712   2754   -418     70   -454       C  
ATOM   1359  C   LEU A 406      -1.023  53.370  31.542  1.00 31.83           C  
ANISOU 1359  C   LEU A 406     4179   4506   3411   -465    117   -473       C  
ATOM   1360  O   LEU A 406      -2.181  53.782  31.499  1.00 33.78           O  
ANISOU 1360  O   LEU A 406     4485   4772   3580   -465    126   -428       O  
ATOM   1361  CB  LEU A 406      -0.210  51.018  31.323  1.00 27.31           C  
ANISOU 1361  CB  LEU A 406     3484   3857   3033   -435    106   -522       C  
ATOM   1362  CG  LEU A 406      -1.137  50.381  30.276  1.00 28.11           C  
ANISOU 1362  CG  LEU A 406     3597   3955   3129   -460    157   -536       C  
ATOM   1363  CD1 LEU A 406      -1.511  51.308  29.127  1.00 23.87           C  
ANISOU 1363  CD1 LEU A 406     3110   3454   2505   -516    212   -572       C  
ATOM   1364  CD2 LEU A 406      -0.499  49.114  29.716  1.00 34.18           C  
ANISOU 1364  CD2 LEU A 406     4292   4678   4017   -460    175   -598       C  
ATOM   1365  N   TYR A 407      -0.011  53.976  30.942  1.00 33.32           N  
ANISOU 1365  N   TYR A 407     4343   4703   3613   -504    148   -542       N  
ATOM   1366  CA  TYR A 407      -0.224  55.053  29.997  1.00 28.15           C  
ANISOU 1366  CA  TYR A 407     3746   4077   2874   -557    201   -569       C  
ATOM   1367  C   TYR A 407       0.438  54.713  28.666  1.00 33.49           C  
ANISOU 1367  C   TYR A 407     4392   4741   3594   -612    275   -658       C  
ATOM   1368  O   TYR A 407       1.509  54.108  28.636  1.00 33.13           O  
ANISOU 1368  O   TYR A 407     4263   4671   3654   -614    289   -717       O  
ATOM   1369  CB  TYR A 407       0.339  56.364  30.533  1.00 23.70           C  
ANISOU 1369  CB  TYR A 407     3209   3533   2262   -568    186   -567       C  
ATOM   1370  CG  TYR A 407      -0.457  57.016  31.639  1.00 28.86           C  
ANISOU 1370  CG  TYR A 407     3924   4203   2838   -528    133   -487       C  
ATOM   1371  CD1 TYR A 407      -0.292  56.634  32.962  1.00 17.54           C  
ANISOU 1371  CD1 TYR A 407     2476   2758   1432   -476     68   -443       C  
ATOM   1372  CD2 TYR A 407      -1.348  58.041  31.360  1.00 29.77           C  
ANISOU 1372  CD2 TYR A 407     4120   4341   2851   -542    149   -459       C  
ATOM   1373  CE1 TYR A 407      -1.003  57.248  33.973  1.00 25.39           C  
ANISOU 1373  CE1 TYR A 407     3536   3763   2346   -445     35   -376       C  
ATOM   1374  CE2 TYR A 407      -2.066  58.662  32.360  1.00 23.52           C  
ANISOU 1374  CE2 TYR A 407     3379   3560   1996   -506    113   -396       C  
ATOM   1375  CZ  TYR A 407      -1.891  58.262  33.667  1.00 25.81           C  
ANISOU 1375  CZ  TYR A 407     3657   3841   2309   -460     64   -357       C  
ATOM   1376  OH  TYR A 407      -2.598  58.869  34.673  1.00 24.73           O  
ANISOU 1376  OH  TYR A 407     3582   3713   2103   -429     42   -300       O  
ATOM   1377  N   SER A 408      -0.199  55.101  27.569  1.00 25.76           N  
ANISOU 1377  N   SER A 408     3482   3771   2533   -657    321   -672       N  
ATOM   1378  CA  SER A 408       0.439  54.999  26.267  1.00 32.73           C  
ANISOU 1378  CA  SER A 408     4368   4641   3425   -722    404   -759       C  
ATOM   1379  C   SER A 408       0.569  56.399  25.685  1.00 37.75           C  
ANISOU 1379  C   SER A 408     5094   5294   3957   -779    445   -772       C  
ATOM   1380  O   SER A 408      -0.382  57.178  25.710  1.00 41.64           O  
ANISOU 1380  O   SER A 408     5672   5802   4347   -773    410   -716       O  
ATOM   1381  CB  SER A 408      -0.342  54.089  25.318  1.00 31.17           C  
ANISOU 1381  CB  SER A 408     4197   4428   3220   -733    423   -773       C  
ATOM   1382  OG  SER A 408       0.317  53.964  24.070  1.00 28.53           O  
ANISOU 1382  OG  SER A 408     3878   4076   2884   -800    513   -862       O  
ATOM   1383  N   LYS A 409       1.756  56.721  25.180  1.00 34.65           N  
ANISOU 1383  N   LYS A 409     4678   4890   3597   -836    521   -850       N  
ATOM   1384  CA  LYS A 409       2.018  58.056  24.669  1.00 29.25           C  
ANISOU 1384  CA  LYS A 409     4078   4209   2826   -895    567   -860       C  
ATOM   1385  C   LYS A 409       2.293  58.044  23.172  1.00 37.33           C  
ANISOU 1385  C   LYS A 409     5144   5189   3851   -952    649   -890       C  
ATOM   1386  O   LYS A 409       3.299  57.501  22.723  1.00 39.75           O  
ANISOU 1386  O   LYS A 409     5393   5484   4225  -1001    740   -989       O  
ATOM   1387  CB  LYS A 409       3.199  58.690  25.408  1.00 18.58           C  
ANISOU 1387  CB  LYS A 409     2660   2862   1536   -907    578   -894       C  
ATOM   1388  CG  LYS A 409       3.485  60.128  25.009  1.00 21.88           C  
ANISOU 1388  CG  LYS A 409     3154   3269   1889   -959    615   -883       C  
ATOM   1389  CD  LYS A 409       4.494  60.769  25.949  1.00 30.48           C  
ANISOU 1389  CD  LYS A 409     4183   4373   3025   -971    609   -924       C  
ATOM   1390  CE  LYS A 409       5.879  60.156  25.794  1.00 28.93           C  
ANISOU 1390  CE  LYS A 409     3854   4154   2983  -1001    674  -1025       C  
ATOM   1391  NZ  LYS A 409       6.505  60.487  24.482  1.00 22.12           N  
ANISOU 1391  NZ  LYS A 409     3032   3269   2103  -1104    820  -1110       N  
ATOM   1392  N   LEU A 410       1.389  58.646  22.406  1.00 31.61           N  
ANISOU 1392  N   LEU A 410     4517   4435   3057   -943    613   -811       N  
ATOM   1393  CA  LEU A 410       1.594  58.817  20.977  1.00 31.73           C  
ANISOU 1393  CA  LEU A 410     4601   4406   3050  -1000    676   -828       C  
ATOM   1394  C   LEU A 410       2.105  60.224  20.677  1.00 44.60           C  
ANISOU 1394  C   LEU A 410     6290   6009   4647  -1043    705   -808       C  
ATOM   1395  O   LEU A 410       1.526  61.219  21.118  1.00 48.38           O  
ANISOU 1395  O   LEU A 410     6811   6487   5083  -1005    635   -735       O  
ATOM   1396  CB  LEU A 410       0.300  58.546  20.204  1.00 30.47           C  
ANISOU 1396  CB  LEU A 410     4519   4225   2833   -968    614   -772       C  
ATOM   1397  CG  LEU A 410       0.327  58.869  18.708  1.00 35.37           C  
ANISOU 1397  CG  LEU A 410     5240   4795   3403  -1021    656   -775       C  
ATOM   1398  CD1 LEU A 410       1.275  57.936  17.974  1.00 30.84           C  
ANISOU 1398  CD1 LEU A 410     4636   4206   2875  -1085    767   -868       C  
ATOM   1399  CD2 LEU A 410      -1.064  58.817  18.092  1.00 30.80           C  
ANISOU 1399  CD2 LEU A 410     4742   4201   2762   -979    568   -717       C  
ATOM   1400  N   THR A 411       3.202  60.299  19.931  1.00 38.54           N  
ANISOU 1400  N   THR A 411     5521   5215   3907  -1125    816   -879       N  
ATOM   1401  CA  THR A 411       3.793  61.579  19.582  1.00 34.61           C  
ANISOU 1401  CA  THR A 411     5082   4686   3382  -1183    861   -873       C  
ATOM   1402  C   THR A 411       3.509  61.917  18.124  1.00 39.19           C  
ANISOU 1402  C   THR A 411     5788   5209   3895  -1229    891   -851       C  
ATOM   1403  O   THR A 411       3.829  61.140  17.226  1.00 43.92           O  
ANISOU 1403  O   THR A 411     6396   5787   4507  -1274    964   -904       O  
ATOM   1404  CB  THR A 411       5.310  61.580  19.819  1.00 36.38           C  
ANISOU 1404  CB  THR A 411     5217   4916   3691  -1257    977   -981       C  
ATOM   1405  OG1 THR A 411       5.583  61.229  21.181  1.00 26.75           O  
ANISOU 1405  OG1 THR A 411     3883   3749   2531  -1211    940  -1013       O  
ATOM   1406  CG2 THR A 411       5.890  62.954  19.527  1.00 26.89           C  
ANISOU 1406  CG2 THR A 411     4078   3678   2459  -1325   1026   -975       C  
ATOM   1407  N   VAL A 412       2.893  63.075  17.898  1.00 35.82           N  
ANISOU 1407  N   VAL A 412     5461   4755   3395  -1215    833   -775       N  
ATOM   1408  CA  VAL A 412       2.583  63.530  16.547  1.00 34.02           C  
ANISOU 1408  CA  VAL A 412     5368   4468   3092  -1257    848   -751       C  
ATOM   1409  C   VAL A 412       3.068  64.963  16.319  1.00 41.15           C  
ANISOU 1409  C   VAL A 412     6350   5327   3957  -1315    883   -735       C  
ATOM   1410  O   VAL A 412       3.286  65.711  17.274  1.00 43.39           O  
ANISOU 1410  O   VAL A 412     6593   5630   4263  -1298    860   -720       O  
ATOM   1411  CB  VAL A 412       1.062  63.461  16.250  1.00 29.34           C  
ANISOU 1411  CB  VAL A 412     4840   3871   2436  -1178    726   -675       C  
ATOM   1412  CG1 VAL A 412       0.506  62.082  16.590  1.00 29.79           C  
ANISOU 1412  CG1 VAL A 412     4819   3970   2530  -1122    687   -690       C  
ATOM   1413  CG2 VAL A 412       0.310  64.541  17.014  1.00 32.51           C  
ANISOU 1413  CG2 VAL A 412     5256   4280   2816  -1111    627   -602       C  
ATOM   1414  N   ASP A 413       3.253  65.338  15.056  1.00 49.52           N  
ANISOU 1414  N   ASP A 413     7531   6326   4959  -1388    941   -741       N  
ATOM   1415  CA  ASP A 413       3.518  66.730  14.717  1.00 45.11           C  
ANISOU 1415  CA  ASP A 413     7077   5714   4350  -1442    964   -717       C  
ATOM   1416  C   ASP A 413       2.340  67.586  15.164  1.00 42.50           C  
ANISOU 1416  C   ASP A 413     6791   5385   3973  -1353    827   -626       C  
ATOM   1417  O   ASP A 413       1.182  67.206  14.968  1.00 47.26           O  
ANISOU 1417  O   ASP A 413     7416   5998   4544  -1279    730   -580       O  
ATOM   1418  CB  ASP A 413       3.767  66.897  13.216  1.00 56.77           C  
ANISOU 1418  CB  ASP A 413     8697   7116   5758  -1533   1042   -734       C  
ATOM   1419  CG  ASP A 413       5.136  66.396  12.789  1.00 71.76           C  
ANISOU 1419  CG  ASP A 413    10558   8996   7711  -1643   1206   -837       C  
ATOM   1420  OD1 ASP A 413       6.080  66.476  13.606  1.00 75.53           O  
ANISOU 1420  OD1 ASP A 413    10923   9500   8273  -1672   1270   -894       O  
ATOM   1421  OD2 ASP A 413       5.270  65.927  11.638  1.00 77.89           O  
ANISOU 1421  OD2 ASP A 413    11416   9729   8450  -1701   1273   -866       O  
ATOM   1422  N   LYS A 414       2.638  68.729  15.780  1.00 43.89           N  
ANISOU 1422  N   LYS A 414     6973   5552   4152  -1363    823   -608       N  
ATOM   1423  CA  LYS A 414       1.603  69.620  16.294  1.00 48.81           C  
ANISOU 1423  CA  LYS A 414     7628   6174   4743  -1280    704   -531       C  
ATOM   1424  C   LYS A 414       0.602  69.989  15.210  1.00 56.04           C  
ANISOU 1424  C   LYS A 414     8682   7036   5576  -1266    641   -481       C  
ATOM   1425  O   LYS A 414      -0.603  70.031  15.449  1.00 60.71           O  
ANISOU 1425  O   LYS A 414     9272   7642   6153  -1175    528   -431       O  
ATOM   1426  CB  LYS A 414       2.218  70.889  16.883  1.00 44.15           C  
ANISOU 1426  CB  LYS A 414     7053   5565   4159  -1317    729   -528       C  
ATOM   1427  CG  LYS A 414       1.191  71.978  17.167  1.00 45.04           C  
ANISOU 1427  CG  LYS A 414     7226   5656   4230  -1247    621   -455       C  
ATOM   1428  CD  LYS A 414       1.748  73.078  18.048  1.00 44.35           C  
ANISOU 1428  CD  LYS A 414     7125   5565   4161  -1266    635   -454       C  
ATOM   1429  CE  LYS A 414       2.812  73.888  17.328  1.00 41.77           C  
ANISOU 1429  CE  LYS A 414     6896   5170   3803  -1394    744   -490       C  
ATOM   1430  NZ  LYS A 414       3.435  74.905  18.222  1.00 47.80           N  
ANISOU 1430  NZ  LYS A 414     7641   5932   4588  -1422    765   -500       N  
ATOM   1431  N   SER A 415       1.116  70.244  14.012  1.00 56.12           N  
ANISOU 1431  N   SER A 415     8814   6980   5530  -1361    719   -502       N  
ATOM   1432  CA  SER A 415       0.286  70.625  12.876  1.00 54.30           C  
ANISOU 1432  CA  SER A 415     8739   6687   5208  -1363    665   -461       C  
ATOM   1433  C   SER A 415      -0.778  69.572  12.547  1.00 48.61           C  
ANISOU 1433  C   SER A 415     7999   5995   4474  -1291    582   -446       C  
ATOM   1434  O   SER A 415      -1.925  69.918  12.248  1.00 55.26           O  
ANISOU 1434  O   SER A 415     8911   6817   5269  -1234    473   -397       O  
ATOM   1435  CB  SER A 415       1.166  70.883  11.655  1.00 53.82           C  
ANISOU 1435  CB  SER A 415     8813   6548   5089  -1490    783   -497       C  
ATOM   1436  OG  SER A 415       2.052  69.801  11.427  1.00 63.14           O  
ANISOU 1436  OG  SER A 415     9926   7751   6313  -1548    894   -569       O  
ATOM   1437  N   ARG A 416      -0.393  68.297  12.599  1.00 44.20           N  
ANISOU 1437  N   ARG A 416     7351   5481   3963  -1297    633   -494       N  
ATOM   1438  CA  ARG A 416      -1.332  67.195  12.389  1.00 47.44           C  
ANISOU 1438  CA  ARG A 416     7731   5923   4371  -1234    561   -490       C  
ATOM   1439  C   ARG A 416      -2.468  67.269  13.402  1.00 54.34           C  
ANISOU 1439  C   ARG A 416     8524   6845   5278  -1119    435   -444       C  
ATOM   1440  O   ARG A 416      -3.638  67.077  13.064  1.00 56.66           O  
ANISOU 1440  O   ARG A 416     8854   7135   5538  -1064    336   -416       O  
ATOM   1441  CB  ARG A 416      -0.619  65.841  12.489  1.00 42.92           C  
ANISOU 1441  CB  ARG A 416     7058   5391   3857  -1260    644   -555       C  
ATOM   1442  CG  ARG A 416      -0.116  65.305  11.159  1.00 53.92           C  
ANISOU 1442  CG  ARG A 416     8547   6738   5202  -1347    734   -600       C  
ATOM   1443  CD  ARG A 416      -0.571  63.876  10.931  1.00 51.87           C  
ANISOU 1443  CD  ARG A 416     8238   6511   4958  -1314    714   -628       C  
ATOM   1444  NE  ARG A 416       0.158  62.933  11.771  1.00 47.59           N  
ANISOU 1444  NE  ARG A 416     7543   6023   4514  -1311    778   -684       N  
ATOM   1445  CZ  ARG A 416      -0.197  61.664  11.938  1.00 45.35           C  
ANISOU 1445  CZ  ARG A 416     7185   5778   4269  -1271    757   -710       C  
ATOM   1446  NH1 ARG A 416       0.522  60.867  12.717  1.00 44.05           N  
ANISOU 1446  NH1 ARG A 416     6887   5656   4196  -1272    817   -764       N  
ATOM   1447  NH2 ARG A 416      -1.277  61.191  11.330  1.00 34.79           N  
ANISOU 1447  NH2 ARG A 416     5907   4433   2878  -1232    672   -687       N  
ATOM   1448  N   TRP A 417      -2.110  67.564  14.647  1.00 46.75           N  
ANISOU 1448  N   TRP A 417     7457   5925   4381  -1089    441   -442       N  
ATOM   1449  CA  TRP A 417      -3.091  67.686  15.713  1.00 44.86           C  
ANISOU 1449  CA  TRP A 417     7140   5729   4176   -989    339   -404       C  
ATOM   1450  C   TRP A 417      -3.993  68.895  15.505  1.00 49.08           C  
ANISOU 1450  C   TRP A 417     7765   6222   4660   -955    254   -351       C  
ATOM   1451  O   TRP A 417      -5.206  68.809  15.690  1.00 47.85           O  
ANISOU 1451  O   TRP A 417     7598   6080   4502   -882    155   -324       O  
ATOM   1452  CB  TRP A 417      -2.396  67.782  17.073  1.00 40.80           C  
ANISOU 1452  CB  TRP A 417     6508   5261   3733   -974    372   -416       C  
ATOM   1453  CG  TRP A 417      -3.343  68.046  18.193  1.00 35.80           C  
ANISOU 1453  CG  TRP A 417     5810   4664   3128   -879    281   -377       C  
ATOM   1454  CD1 TRP A 417      -3.492  69.211  18.883  1.00 37.69           C  
ANISOU 1454  CD1 TRP A 417     6056   4896   3368   -851    249   -345       C  
ATOM   1455  CD2 TRP A 417      -4.292  67.126  18.747  1.00 36.58           C  
ANISOU 1455  CD2 TRP A 417     5835   4808   3257   -805    217   -370       C  
ATOM   1456  NE1 TRP A 417      -4.471  69.074  19.838  1.00 41.29           N  
ANISOU 1456  NE1 TRP A 417     6445   5392   3853   -764    174   -321       N  
ATOM   1457  CE2 TRP A 417      -4.980  67.804  19.774  1.00 37.50           C  
ANISOU 1457  CE2 TRP A 417     5914   4942   3391   -737    154   -335       C  
ATOM   1458  CE3 TRP A 417      -4.628  65.796  18.473  1.00 36.74           C  
ANISOU 1458  CE3 TRP A 417     5819   4850   3290   -797    211   -393       C  
ATOM   1459  CZ2 TRP A 417      -5.980  67.195  20.531  1.00 32.41           C  
ANISOU 1459  CZ2 TRP A 417     5202   4337   2775   -666     94   -323       C  
ATOM   1460  CZ3 TRP A 417      -5.623  65.196  19.223  1.00 38.03           C  
ANISOU 1460  CZ3 TRP A 417     5915   5051   3482   -727    145   -380       C  
ATOM   1461  CH2 TRP A 417      -6.287  65.895  20.242  1.00 34.28           C  
ANISOU 1461  CH2 TRP A 417     5408   4594   3024   -665     90   -345       C  
ATOM   1462  N   GLN A 418      -3.390  70.015  15.121  1.00 51.68           N  
ANISOU 1462  N   GLN A 418     8188   6497   4951  -1015    295   -342       N  
ATOM   1463  CA  GLN A 418      -4.114  71.264  14.909  1.00 54.90           C  
ANISOU 1463  CA  GLN A 418     8697   6854   5309   -994    222   -295       C  
ATOM   1464  C   GLN A 418      -5.203  71.141  13.844  1.00 54.90           C  
ANISOU 1464  C   GLN A 418     8804   6813   5244   -975    137   -272       C  
ATOM   1465  O   GLN A 418      -6.189  71.873  13.872  1.00 61.33           O  
ANISOU 1465  O   GLN A 418     9667   7600   6034   -925     39   -235       O  
ATOM   1466  CB  GLN A 418      -3.140  72.377  14.509  1.00 60.78           C  
ANISOU 1466  CB  GLN A 418     9544   7534   6016  -1083    297   -296       C  
ATOM   1467  CG  GLN A 418      -2.175  72.817  15.597  1.00 68.03           C  
ANISOU 1467  CG  GLN A 418    10375   8482   6992  -1101    361   -315       C  
ATOM   1468  CD  GLN A 418      -2.748  73.917  16.468  1.00 78.64           C  
ANISOU 1468  CD  GLN A 418    11711   9823   8344  -1041    288   -275       C  
ATOM   1469  OE1 GLN A 418      -3.965  74.084  16.555  1.00 82.40           O  
ANISOU 1469  OE1 GLN A 418    12199  10300   8809   -964    187   -240       O  
ATOM   1470  NE2 GLN A 418      -1.872  74.683  17.111  1.00 76.84           N  
ANISOU 1470  NE2 GLN A 418    11468   9590   8137  -1080    343   -286       N  
ATOM   1471  N   GLN A 419      -5.021  70.214  12.910  1.00 50.05           N  
ANISOU 1471  N   GLN A 419     8228   6189   4600  -1018    171   -299       N  
ATOM   1472  CA  GLN A 419      -5.914  70.106  11.762  1.00 55.64           C  
ANISOU 1472  CA  GLN A 419     9060   6848   5234  -1015     94   -283       C  
ATOM   1473  C   GLN A 419      -7.139  69.236  12.011  1.00 61.31           C  
ANISOU 1473  C   GLN A 419     9704   7613   5979   -931    -11   -281       C  
ATOM   1474  O   GLN A 419      -7.975  69.066  11.124  1.00 70.54           O  
ANISOU 1474  O   GLN A 419    10964   8744   7093   -923    -92   -272       O  
ATOM   1475  CB  GLN A 419      -5.148  69.570  10.555  1.00 64.24           C  
ANISOU 1475  CB  GLN A 419    10246   7896   6266  -1108    182   -316       C  
ATOM   1476  CG  GLN A 419      -4.249  70.596   9.909  1.00 81.18           C  
ANISOU 1476  CG  GLN A 419    12529   9963   8352  -1204    264   -312       C  
ATOM   1477  CD  GLN A 419      -3.794  70.165   8.537  1.00 96.37           C  
ANISOU 1477  CD  GLN A 419    14588  11829  10197  -1294    332   -338       C  
ATOM   1478  OE1 GLN A 419      -3.667  68.972   8.261  1.00 97.10           O  
ANISOU 1478  OE1 GLN A 419    14633  11957  10304  -1301    367   -376       O  
ATOM   1479  NE2 GLN A 419      -3.547  71.135   7.662  1.00104.36           N  
ANISOU 1479  NE2 GLN A 419    15782  12747  11123  -1366    355   -320       N  
ATOM   1480  N   GLY A 420      -7.245  68.678  13.210  1.00 55.32           N  
ANISOU 1480  N   GLY A 420     8788   6930   5303   -875    -11   -293       N  
ATOM   1481  CA  GLY A 420      -8.433  67.930  13.582  1.00 49.67           C  
ANISOU 1481  CA  GLY A 420     7999   6255   4619   -801   -107   -294       C  
ATOM   1482  C   GLY A 420      -8.429  66.469  13.178  1.00 46.80           C  
ANISOU 1482  C   GLY A 420     7597   5920   4265   -813    -88   -334       C  
ATOM   1483  O   GLY A 420      -9.484  65.835  13.145  1.00 46.65           O  
ANISOU 1483  O   GLY A 420     7554   5917   4255   -767   -176   -339       O  
ATOM   1484  N   ASN A 421      -7.255  65.931  12.866  1.00 42.52           N  
ANISOU 1484  N   ASN A 421     7052   5379   3724   -878     25   -368       N  
ATOM   1485  CA  ASN A 421      -7.136  64.501  12.597  1.00 51.43           C  
ANISOU 1485  CA  ASN A 421     8135   6536   4871   -891     56   -412       C  
ATOM   1486  C   ASN A 421      -7.576  63.680  13.804  1.00 51.51           C  
ANISOU 1486  C   ASN A 421     7997   6613   4962   -827     28   -422       C  
ATOM   1487  O   ASN A 421      -7.228  63.996  14.943  1.00 51.34           O  
ANISOU 1487  O   ASN A 421     7888   6626   4994   -803     53   -412       O  
ATOM   1488  CB  ASN A 421      -5.700  64.138  12.207  1.00 61.78           C  
ANISOU 1488  CB  ASN A 421     9454   7838   6182   -974    195   -453       C  
ATOM   1489  CG  ASN A 421      -5.350  64.571  10.797  1.00 67.36           C  
ANISOU 1489  CG  ASN A 421    10323   8473   6798  -1051    232   -455       C  
ATOM   1490  OD1 ASN A 421      -5.738  63.922   9.824  1.00 77.85           O  
ANISOU 1490  OD1 ASN A 421    11725   9778   8076  -1068    210   -472       O  
ATOM   1491  ND2 ASN A 421      -4.608  65.665  10.677  1.00 66.26           N  
ANISOU 1491  ND2 ASN A 421    10249   8293   6634  -1102    291   -440       N  
ATOM   1492  N   VAL A 422      -8.354  62.632  13.556  1.00 52.48           N  
ANISOU 1492  N   VAL A 422     8100   6750   5090   -805    -27   -444       N  
ATOM   1493  CA  VAL A 422      -8.826  61.768  14.631  1.00 46.01           C  
ANISOU 1493  CA  VAL A 422     7156   5984   4340   -757    -53   -457       C  
ATOM   1494  C   VAL A 422      -7.840  60.638  14.894  1.00 43.80           C  
ANISOU 1494  C   VAL A 422     6805   5732   4106   -792     47   -502       C  
ATOM   1495  O   VAL A 422      -7.370  59.982  13.962  1.00 49.90           O  
ANISOU 1495  O   VAL A 422     7623   6484   4853   -842     96   -539       O  
ATOM   1496  CB  VAL A 422     -10.209  61.185  14.304  1.00 39.10           C  
ANISOU 1496  CB  VAL A 422     6291   5108   3459   -722   -168   -464       C  
ATOM   1497  CG1 VAL A 422     -10.644  60.192  15.375  1.00 40.33           C  
ANISOU 1497  CG1 VAL A 422     6326   5312   3685   -689   -182   -483       C  
ATOM   1498  CG2 VAL A 422     -11.215  62.307  14.175  1.00 28.38           C  
ANISOU 1498  CG2 VAL A 422     4990   3722   2070   -683   -275   -424       C  
ATOM   1499  N   PHE A 423      -7.518  60.425  16.167  1.00 42.18           N  
ANISOU 1499  N   PHE A 423     6491   5569   3965   -769     77   -501       N  
ATOM   1500  CA  PHE A 423      -6.606  59.362  16.563  1.00 38.27           C  
ANISOU 1500  CA  PHE A 423     5920   5100   3521   -799    162   -545       C  
ATOM   1501  C   PHE A 423      -7.317  58.375  17.478  1.00 32.04           C  
ANISOU 1501  C   PHE A 423     5043   4349   2783   -760    121   -553       C  
ATOM   1502  O   PHE A 423      -8.186  58.759  18.264  1.00 40.41           O  
ANISOU 1502  O   PHE A 423     6074   5427   3853   -711     54   -518       O  
ATOM   1503  CB  PHE A 423      -5.368  59.943  17.249  1.00 35.69           C  
ANISOU 1503  CB  PHE A 423     5551   4785   3226   -821    244   -545       C  
ATOM   1504  CG  PHE A 423      -4.537  60.822  16.356  1.00 32.85           C  
ANISOU 1504  CG  PHE A 423     5275   4384   2823   -879    304   -548       C  
ATOM   1505  CD1 PHE A 423      -4.910  62.137  16.119  1.00 38.50           C  
ANISOU 1505  CD1 PHE A 423     6067   5071   3491   -867    259   -501       C  
ATOM   1506  CD2 PHE A 423      -3.393  60.334  15.743  1.00 31.18           C  
ANISOU 1506  CD2 PHE A 423     5071   4158   2619   -952    410   -603       C  
ATOM   1507  CE1 PHE A 423      -4.158  62.948  15.292  1.00 35.83           C  
ANISOU 1507  CE1 PHE A 423     5818   4688   3107   -931    317   -504       C  
ATOM   1508  CE2 PHE A 423      -2.635  61.142  14.912  1.00 41.72           C  
ANISOU 1508  CE2 PHE A 423     6492   5450   3911  -1017    475   -609       C  
ATOM   1509  CZ  PHE A 423      -3.021  62.452  14.688  1.00 36.46           C  
ANISOU 1509  CZ  PHE A 423     5909   4753   3191  -1009    428   -557       C  
ATOM   1510  N   SER A 424      -6.959  57.100  17.371  1.00 31.54           N  
ANISOU 1510  N   SER A 424     4938   4294   2750   -789    167   -604       N  
ATOM   1511  CA  SER A 424      -7.608  56.066  18.169  1.00 39.19           C  
ANISOU 1511  CA  SER A 424     5831   5295   3767   -767    135   -619       C  
ATOM   1512  C   SER A 424      -6.629  55.245  19.002  1.00 31.86           C  
ANISOU 1512  C   SER A 424     4811   4395   2899   -785    216   -657       C  
ATOM   1513  O   SER A 424      -5.575  54.819  18.527  1.00 37.33           O  
ANISOU 1513  O   SER A 424     5499   5077   3609   -828    298   -706       O  
ATOM   1514  CB  SER A 424      -8.426  55.137  17.265  1.00 40.76           C  
ANISOU 1514  CB  SER A 424     6064   5471   3951   -779     86   -654       C  
ATOM   1515  OG  SER A 424      -9.614  55.776  16.825  1.00 50.87           O  
ANISOU 1515  OG  SER A 424     7405   6733   5189   -749    -20   -622       O  
ATOM   1516  N   CYS A 425      -6.993  55.039  20.263  1.00 33.58           N  
ANISOU 1516  N   CYS A 425     4958   4649   3150   -755    192   -637       N  
ATOM   1517  CA  CYS A 425      -6.253  54.154  21.148  1.00 35.31           C  
ANISOU 1517  CA  CYS A 425     5092   4898   3426   -765    249   -676       C  
ATOM   1518  C   CYS A 425      -6.979  52.814  21.237  1.00 34.15           C  
ANISOU 1518  C   CYS A 425     4904   4754   3317   -768    226   -709       C  
ATOM   1519  O   CYS A 425      -8.113  52.745  21.713  1.00 32.58           O  
ANISOU 1519  O   CYS A 425     4678   4557   3145   -727    159   -659       O  
ATOM   1520  CB  CYS A 425      -6.100  54.785  22.533  1.00 29.04           C  
ANISOU 1520  CB  CYS A 425     4254   4139   2640   -731    240   -630       C  
ATOM   1521  SG  CYS A 425      -5.272  53.735  23.740  1.00 33.34           S  
ANISOU 1521  SG  CYS A 425     4680   4700   3288   -709    277   -645       S  
ATOM   1522  N   SER A 426      -6.334  51.756  20.755  1.00 36.44           N  
ANISOU 1522  N   SER A 426     5162   5023   3661   -793    279   -771       N  
ATOM   1523  CA  SER A 426      -6.936  50.425  20.776  1.00 36.95           C  
ANISOU 1523  CA  SER A 426     5162   5062   3816   -772    255   -777       C  
ATOM   1524  C   SER A 426      -6.356  49.604  21.913  1.00 33.48           C  
ANISOU 1524  C   SER A 426     4604   4619   3498   -730    280   -758       C  
ATOM   1525  O   SER A 426      -5.141  49.528  22.082  1.00 31.56           O  
ANISOU 1525  O   SER A 426     4327   4375   3289   -737    338   -792       O  
ATOM   1526  CB  SER A 426      -6.726  49.702  19.441  1.00 34.74           C  
ANISOU 1526  CB  SER A 426     4933   4749   3516   -826    288   -862       C  
ATOM   1527  OG  SER A 426      -7.397  50.365  18.382  1.00 51.15           O  
ANISOU 1527  OG  SER A 426     7131   6818   5484   -855    242   -865       O  
ATOM   1528  N   VAL A 427      -7.240  48.997  22.697  1.00 28.16           N  
ANISOU 1528  N   VAL A 427     3872   3936   2892   -686    233   -703       N  
ATOM   1529  CA  VAL A 427      -6.825  48.192  23.836  1.00 29.33           C  
ANISOU 1529  CA  VAL A 427     3930   4070   3144   -644    244   -672       C  
ATOM   1530  C   VAL A 427      -7.405  46.786  23.736  1.00 34.45           C  
ANISOU 1530  C   VAL A 427     4530   4675   3884   -636    233   -680       C  
ATOM   1531  O   VAL A 427      -8.595  46.604  23.466  1.00 39.06           O  
ANISOU 1531  O   VAL A 427     5124   5250   4467   -640    194   -665       O  
ATOM   1532  CB  VAL A 427      -7.253  48.824  25.177  1.00 29.80           C  
ANISOU 1532  CB  VAL A 427     3974   4153   3195   -598    213   -585       C  
ATOM   1533  CG1 VAL A 427      -6.714  48.016  26.340  1.00 24.19           C  
ANISOU 1533  CG1 VAL A 427     3198   3421   2574   -558    217   -551       C  
ATOM   1534  CG2 VAL A 427      -6.775  50.269  25.268  1.00 28.72           C  
ANISOU 1534  CG2 VAL A 427     3890   4056   2967   -607    218   -577       C  
ATOM   1535  N   MET A 428      -6.549  45.793  23.948  1.00 30.24           N  
ANISOU 1535  N   MET A 428     3940   4108   3440   -626    264   -709       N  
ATOM   1536  CA  MET A 428      -6.967  44.404  23.922  1.00 26.39           C  
ANISOU 1536  CA  MET A 428     3407   3570   3050   -618    258   -717       C  
ATOM   1537  C   MET A 428      -6.720  43.749  25.278  1.00 30.96           C  
ANISOU 1537  C   MET A 428     3926   4122   3716   -567    247   -655       C  
ATOM   1538  O   MET A 428      -5.596  43.739  25.783  1.00 28.63           O  
ANISOU 1538  O   MET A 428     3603   3822   3455   -545    258   -661       O  
ATOM   1539  CB  MET A 428      -6.239  43.661  22.803  1.00 27.20           C  
ANISOU 1539  CB  MET A 428     3508   3641   3186   -652    303   -816       C  
ATOM   1540  CG  MET A 428      -6.701  44.077  21.414  1.00 25.09           C  
ANISOU 1540  CG  MET A 428     3324   3385   2824   -707    305   -874       C  
ATOM   1541  SD  MET A 428      -5.445  43.861  20.144  1.00 49.36           S  
ANISOU 1541  SD  MET A 428     6431   6441   5882   -760    393   -996       S  
ATOM   1542  CE  MET A 428      -4.439  45.319  20.416  1.00 31.67           C  
ANISOU 1542  CE  MET A 428     4217   4251   3566   -769    434   -989       C  
ATOM   1543  N   HIS A 429      -7.788  43.217  25.866  1.00 29.77           N  
ANISOU 1543  N   HIS A 429     3761   3949   3602   -552    222   -596       N  
ATOM   1544  CA  HIS A 429      -7.741  42.628  27.201  1.00 34.84           C  
ANISOU 1544  CA  HIS A 429     4374   4557   4305   -510    212   -524       C  
ATOM   1545  C   HIS A 429      -8.914  41.657  27.385  1.00 35.34           C  
ANISOU 1545  C   HIS A 429     4419   4575   4433   -515    209   -492       C  
ATOM   1546  O   HIS A 429      -9.984  41.860  26.815  1.00 38.05           O  
ANISOU 1546  O   HIS A 429     4769   4931   4758   -542    201   -503       O  
ATOM   1547  CB  HIS A 429      -7.765  43.729  28.267  1.00 34.51           C  
ANISOU 1547  CB  HIS A 429     4362   4558   4192   -484    200   -453       C  
ATOM   1548  CG  HIS A 429      -7.614  43.224  29.667  1.00 34.35           C  
ANISOU 1548  CG  HIS A 429     4340   4503   4211   -444    187   -378       C  
ATOM   1549  ND1 HIS A 429      -8.690  42.841  30.438  1.00 39.88           N  
ANISOU 1549  ND1 HIS A 429     5051   5178   4925   -439    194   -310       N  
ATOM   1550  CD2 HIS A 429      -6.516  43.047  30.439  1.00 28.51           C  
ANISOU 1550  CD2 HIS A 429     3595   3741   3495   -409    164   -361       C  
ATOM   1551  CE1 HIS A 429      -8.262  42.443  31.622  1.00 45.00           C  
ANISOU 1551  CE1 HIS A 429     5720   5790   5590   -405    181   -249       C  
ATOM   1552  NE2 HIS A 429      -6.946  42.559  31.649  1.00 36.65           N  
ANISOU 1552  NE2 HIS A 429     4652   4733   4539   -383    152   -278       N  
ATOM   1553  N   GLU A 430      -8.711  40.605  28.176  1.00 28.23           N  
ANISOU 1553  N   GLU A 430     3497   3614   3614   -491    209   -455       N  
ATOM   1554  CA  GLU A 430      -9.704  39.536  28.277  1.00 31.65           C  
ANISOU 1554  CA  GLU A 430     3912   3991   4124   -504    217   -434       C  
ATOM   1555  C   GLU A 430     -11.007  39.994  28.927  1.00 37.66           C  
ANISOU 1555  C   GLU A 430     4684   4769   4858   -512    227   -368       C  
ATOM   1556  O   GLU A 430     -12.070  39.433  28.660  1.00 38.69           O  
ANISOU 1556  O   GLU A 430     4788   4869   5043   -538    236   -373       O  
ATOM   1557  CB  GLU A 430      -9.135  38.344  29.043  1.00 31.18           C  
ANISOU 1557  CB  GLU A 430     3842   3854   4152   -475    214   -402       C  
ATOM   1558  CG  GLU A 430      -8.877  38.603  30.512  1.00 34.66           C  
ANISOU 1558  CG  GLU A 430     4321   4287   4562   -437    203   -309       C  
ATOM   1559  CD  GLU A 430      -8.490  37.345  31.263  1.00 43.87           C  
ANISOU 1559  CD  GLU A 430     5495   5362   5812   -410    188   -268       C  
ATOM   1560  OE1 GLU A 430      -9.386  36.526  31.558  1.00 49.98           O  
ANISOU 1560  OE1 GLU A 430     6277   6081   6634   -429    212   -230       O  
ATOM   1561  OE2 GLU A 430      -7.290  37.176  31.560  1.00 46.25           O  
ANISOU 1561  OE2 GLU A 430     5794   5640   6138   -371    150   -276       O  
ATOM   1562  N   ALA A 431     -10.931  41.020  29.767  1.00 36.78           N  
ANISOU 1562  N   ALA A 431     4605   4701   4669   -490    228   -314       N  
ATOM   1563  CA  ALA A 431     -12.107  41.494  30.487  1.00 35.51           C  
ANISOU 1563  CA  ALA A 431     4453   4552   4488   -494    252   -256       C  
ATOM   1564  C   ALA A 431     -12.892  42.517  29.670  1.00 40.63           C  
ANISOU 1564  C   ALA A 431     5090   5255   5091   -513    238   -294       C  
ATOM   1565  O   ALA A 431     -13.854  43.108  30.157  1.00 36.57           O  
ANISOU 1565  O   ALA A 431     4573   4758   4565   -514    255   -259       O  
ATOM   1566  CB  ALA A 431     -11.707  42.081  31.820  1.00 25.83           C  
ANISOU 1566  CB  ALA A 431     3277   3339   3198   -462    262   -183       C  
ATOM   1567  N   LEU A 432     -12.477  42.726  28.426  1.00 34.63           N  
ANISOU 1567  N   LEU A 432     4331   4519   4310   -530    207   -367       N  
ATOM   1568  CA  LEU A 432     -13.224  43.582  27.520  1.00 36.31           C  
ANISOU 1568  CA  LEU A 432     4547   4768   4479   -549    175   -405       C  
ATOM   1569  C   LEU A 432     -14.132  42.732  26.645  1.00 40.27           C  
ANISOU 1569  C   LEU A 432     5010   5231   5058   -581    154   -452       C  
ATOM   1570  O   LEU A 432     -13.804  41.589  26.336  1.00 44.17           O  
ANISOU 1570  O   LEU A 432     5487   5679   5616   -594    162   -481       O  
ATOM   1571  CB  LEU A 432     -12.279  44.415  26.655  1.00 34.67           C  
ANISOU 1571  CB  LEU A 432     4388   4604   4182   -556    155   -455       C  
ATOM   1572  CG  LEU A 432     -11.579  45.602  27.318  1.00 30.78           C  
ANISOU 1572  CG  LEU A 432     3934   4159   3603   -532    163   -420       C  
ATOM   1573  CD1 LEU A 432     -10.455  46.091  26.425  1.00 35.05           C  
ANISOU 1573  CD1 LEU A 432     4513   4724   4081   -549    161   -479       C  
ATOM   1574  CD2 LEU A 432     -12.565  46.725  27.604  1.00 28.77           C  
ANISOU 1574  CD2 LEU A 432     3693   3937   3302   -522    147   -387       C  
ATOM   1575  N   HIS A 433     -15.278  43.282  26.256  1.00 38.30           N  
ANISOU 1575  N   HIS A 433     4744   4994   4812   -592    119   -463       N  
ATOM   1576  CA  HIS A 433     -16.147  42.612  25.295  1.00 36.59           C  
ANISOU 1576  CA  HIS A 433     4493   4743   4665   -623     77   -519       C  
ATOM   1577  C   HIS A 433     -15.413  42.477  23.964  1.00 43.08           C  
ANISOU 1577  C   HIS A 433     5368   5568   5432   -647     41   -594       C  
ATOM   1578  O   HIS A 433     -14.842  43.451  23.470  1.00 43.12           O  
ANISOU 1578  O   HIS A 433     5437   5615   5332   -645     22   -612       O  
ATOM   1579  CB  HIS A 433     -17.460  43.376  25.115  1.00 33.54           C  
ANISOU 1579  CB  HIS A 433     4077   4369   4296   -623     29   -522       C  
ATOM   1580  CG  HIS A 433     -18.534  42.583  24.439  1.00 41.34           C  
ANISOU 1580  CG  HIS A 433     5006   5310   5389   -653    -17   -569       C  
ATOM   1581  ND1 HIS A 433     -19.138  41.496  25.032  1.00 44.76           N  
ANISOU 1581  ND1 HIS A 433     5368   5692   5949   -668     30   -553       N  
ATOM   1582  CD2 HIS A 433     -19.114  42.722  23.223  1.00 46.13           C  
ANISOU 1582  CD2 HIS A 433     5623   5911   5995   -672   -110   -634       C  
ATOM   1583  CE1 HIS A 433     -20.045  41.000  24.209  1.00 51.31           C  
ANISOU 1583  CE1 HIS A 433     6150   6485   6860   -697    -31   -611       C  
ATOM   1584  NE2 HIS A 433     -20.050  41.725  23.105  1.00 49.74           N  
ANISOU 1584  NE2 HIS A 433     6002   6314   6585   -698   -123   -661       N  
ATOM   1585  N   ASN A 434     -15.422  41.265  23.406  1.00 41.15           N  
ANISOU 1585  N   ASN A 434     5104   5274   5259   -672     39   -641       N  
ATOM   1586  CA  ASN A 434     -14.681  40.925  22.189  1.00 40.36           C  
ANISOU 1586  CA  ASN A 434     5056   5164   5116   -699     25   -721       C  
ATOM   1587  C   ASN A 434     -13.163  41.040  22.356  1.00 46.35           C  
ANISOU 1587  C   ASN A 434     5849   5941   5822   -686     81   -725       C  
ATOM   1588  O   ASN A 434     -12.432  41.031  21.365  1.00 53.91           O  
ANISOU 1588  O   ASN A 434     6858   6900   6726   -710     88   -794       O  
ATOM   1589  CB  ASN A 434     -15.121  41.800  21.006  1.00 33.27           C  
ANISOU 1589  CB  ASN A 434     4224   4292   4126   -722    -49   -770       C  
ATOM   1590  CG  ASN A 434     -16.583  41.625  20.659  1.00 40.31           C  
ANISOU 1590  CG  ASN A 434     5074   5157   5085   -735   -126   -785       C  
ATOM   1591  OD1 ASN A 434     -17.144  40.540  20.798  1.00 50.24           O  
ANISOU 1591  OD1 ASN A 434     6266   6365   6458   -748   -122   -795       O  
ATOM   1592  ND2 ASN A 434     -17.213  42.701  20.194  1.00 45.40           N  
ANISOU 1592  ND2 ASN A 434     5756   5828   5666   -731   -202   -788       N  
ATOM   1593  N   HIS A 435     -12.707  41.147  23.605  1.00 33.95           N  
ANISOU 1593  N   HIS A 435     4252   4379   4270   -650    121   -656       N  
ATOM   1594  CA  HIS A 435     -11.293  41.350  23.923  1.00 37.22           C  
ANISOU 1594  CA  HIS A 435     4683   4809   4650   -631    161   -656       C  
ATOM   1595  C   HIS A 435     -10.745  42.616  23.267  1.00 38.92           C  
ANISOU 1595  C   HIS A 435     4961   5080   4745   -643    157   -687       C  
ATOM   1596  O   HIS A 435      -9.540  42.738  23.050  1.00 35.90           O  
ANISOU 1596  O   HIS A 435     4595   4706   4338   -646    193   -723       O  
ATOM   1597  CB  HIS A 435     -10.448  40.146  23.487  1.00 31.58           C  
ANISOU 1597  CB  HIS A 435     3950   4043   4007   -639    190   -715       C  
ATOM   1598  CG  HIS A 435     -10.793  38.865  24.182  1.00 30.86           C  
ANISOU 1598  CG  HIS A 435     3806   3886   4034   -625    197   -682       C  
ATOM   1599  ND1 HIS A 435     -10.464  37.630  23.665  1.00 32.56           N  
ANISOU 1599  ND1 HIS A 435     4001   4039   4333   -637    210   -739       N  
ATOM   1600  CD2 HIS A 435     -11.423  38.625  25.355  1.00 38.08           C  
ANISOU 1600  CD2 HIS A 435     4694   4780   4995   -604    200   -598       C  
ATOM   1601  CE1 HIS A 435     -10.883  36.685  24.487  1.00 34.03           C  
ANISOU 1601  CE1 HIS A 435     4150   4167   4613   -623    214   -687       C  
ATOM   1602  NE2 HIS A 435     -11.467  37.262  25.521  1.00 31.29           N  
ANISOU 1602  NE2 HIS A 435     3802   3844   4241   -605    212   -600       N  
ATOM   1603  N   TYR A 436     -11.626  43.555  22.943  1.00 37.82           N  
ANISOU 1603  N   TYR A 436     4857   4973   4541   -653    113   -676       N  
ATOM   1604  CA  TYR A 436     -11.221  44.722  22.178  1.00 36.62           C  
ANISOU 1604  CA  TYR A 436     4784   4862   4269   -672    103   -706       C  
ATOM   1605  C   TYR A 436     -12.131  45.920  22.413  1.00 35.90           C  
ANISOU 1605  C   TYR A 436     4716   4804   4119   -658     54   -659       C  
ATOM   1606  O   TYR A 436     -13.357  45.801  22.408  1.00 42.34           O  
ANISOU 1606  O   TYR A 436     5503   5605   4978   -653      4   -645       O  
ATOM   1607  CB  TYR A 436     -11.181  44.378  20.683  1.00 47.55           C  
ANISOU 1607  CB  TYR A 436     6228   6224   5614   -720     89   -793       C  
ATOM   1608  CG  TYR A 436     -10.896  45.556  19.775  1.00 66.82           C  
ANISOU 1608  CG  TYR A 436     8775   8695   7917   -750     77   -823       C  
ATOM   1609  CD1 TYR A 436      -9.589  45.919  19.465  1.00 77.58           C  
ANISOU 1609  CD1 TYR A 436    10182  10072   9222   -772    147   -861       C  
ATOM   1610  CD2 TYR A 436     -11.934  46.299  19.222  1.00 76.07           C  
ANISOU 1610  CD2 TYR A 436    10005   9873   9024   -758     -5   -816       C  
ATOM   1611  CE1 TYR A 436      -9.321  46.993  18.637  1.00 80.78           C  
ANISOU 1611  CE1 TYR A 436    10699  10498   9497   -808    148   -886       C  
ATOM   1612  CE2 TYR A 436     -11.678  47.376  18.395  1.00 84.71           C  
ANISOU 1612  CE2 TYR A 436    11216  10985   9984   -786    -22   -837       C  
ATOM   1613  CZ  TYR A 436     -10.368  47.719  18.104  1.00 85.18           C  
ANISOU 1613  CZ  TYR A 436    11330  11059   9977   -815     61   -870       C  
ATOM   1614  OH  TYR A 436     -10.106  48.788  17.279  1.00 86.15           O  
ANISOU 1614  OH  TYR A 436    11581  11192   9962   -852     56   -889       O  
ATOM   1615  N   THR A 437     -11.513  47.076  22.622  1.00 27.86           N  
ANISOU 1615  N   THR A 437     3745   3827   3014   -651     68   -640       N  
ATOM   1616  CA  THR A 437     -12.230  48.337  22.610  1.00 30.86           C  
ANISOU 1616  CA  THR A 437     4167   4234   3325   -641     19   -610       C  
ATOM   1617  C   THR A 437     -11.338  49.415  22.016  1.00 33.06           C  
ANISOU 1617  C   THR A 437     4538   4540   3484   -664     32   -634       C  
ATOM   1618  O   THR A 437     -10.131  49.228  21.871  1.00 31.35           O  
ANISOU 1618  O   THR A 437     4333   4326   3252   -684     93   -666       O  
ATOM   1619  CB  THR A 437     -12.695  48.751  24.012  1.00 35.71           C  
ANISOU 1619  CB  THR A 437     4727   4865   3975   -596     28   -535       C  
ATOM   1620  OG1 THR A 437     -13.631  49.829  23.900  1.00 44.47           O  
ANISOU 1620  OG1 THR A 437     5863   5989   5044   -583    -27   -516       O  
ATOM   1621  CG2 THR A 437     -11.515  49.193  24.862  1.00 35.12           C  
ANISOU 1621  CG2 THR A 437     4661   4818   3867   -580     80   -506       C  
ATOM   1622  N   GLN A 438     -11.935  50.547  21.672  1.00 35.60           N  
ANISOU 1622  N   GLN A 438     4924   4875   3729   -663    -23   -620       N  
ATOM   1623  CA  GLN A 438     -11.200  51.599  20.997  1.00 34.99           C  
ANISOU 1623  CA  GLN A 438     4953   4813   3529   -694    -12   -641       C  
ATOM   1624  C   GLN A 438     -11.759  52.967  21.367  1.00 36.09           C  
ANISOU 1624  C   GLN A 438     5129   4970   3612   -667    -60   -593       C  
ATOM   1625  O   GLN A 438     -12.965  53.186  21.303  1.00 50.87           O  
ANISOU 1625  O   GLN A 438     6992   6830   5507   -644   -137   -575       O  
ATOM   1626  CB  GLN A 438     -11.258  51.374  19.485  1.00 34.79           C  
ANISOU 1626  CB  GLN A 438     5023   4759   3435   -745    -40   -707       C  
ATOM   1627  CG  GLN A 438     -10.273  52.194  18.681  1.00 56.27           C  
ANISOU 1627  CG  GLN A 438     7857   7480   6043   -785      5   -732       C  
ATOM   1628  CD  GLN A 438     -10.459  52.007  17.187  1.00 66.69           C  
ANISOU 1628  CD  GLN A 438     9262   8752   7325   -803    -26   -760       C  
ATOM   1629  OE1 GLN A 438     -11.582  51.860  16.705  1.00 67.75           O  
ANISOU 1629  OE1 GLN A 438     9424   8866   7452   -798   -124   -766       O  
ATOM   1630  NE2 GLN A 438      -9.354  52.001  16.447  1.00 67.95           N  
ANISOU 1630  NE2 GLN A 438     9463   8894   7462   -828     57   -783       N  
ATOM   1631  N   LYS A 439     -10.881  53.881  21.767  1.00 30.33           N  
ANISOU 1631  N   LYS A 439     4435   4266   2822   -670    -15   -576       N  
ATOM   1632  CA  LYS A 439     -11.294  55.231  22.132  1.00 33.56           C  
ANISOU 1632  CA  LYS A 439     4887   4689   3176   -646    -54   -533       C  
ATOM   1633  C   LYS A 439     -10.652  56.261  21.209  1.00 41.05           C  
ANISOU 1633  C   LYS A 439     5931   5613   4053   -656    -48   -531       C  
ATOM   1634  O   LYS A 439      -9.481  56.142  20.847  1.00 36.86           O  
ANISOU 1634  O   LYS A 439     5408   5074   3525   -679     23   -550       O  
ATOM   1635  CB  LYS A 439     -10.941  55.525  23.593  1.00 34.88           C  
ANISOU 1635  CB  LYS A 439     4986   4884   3383   -607    -10   -485       C  
ATOM   1636  CG  LYS A 439     -11.645  54.624  24.590  1.00 39.72           C  
ANISOU 1636  CG  LYS A 439     5491   5495   4107   -566     -6   -452       C  
ATOM   1637  CD  LYS A 439     -13.152  54.765  24.507  1.00 44.55           C  
ANISOU 1637  CD  LYS A 439     6080   6089   4758   -539    -74   -436       C  
ATOM   1638  CE  LYS A 439     -13.827  53.948  25.591  1.00 56.42           C  
ANISOU 1638  CE  LYS A 439     7479   7586   6371   -506    -47   -403       C  
ATOM   1639  NZ  LYS A 439     -15.306  53.994  25.462  1.00 63.96           N  
ANISOU 1639  NZ  LYS A 439     8391   8519   7392   -485   -104   -402       N  
ATOM   1640  N   SER A 440     -11.427  57.268  20.820  1.00 45.19           N  
ANISOU 1640  N   SER A 440     6510   6115   4544   -628   -121   -502       N  
ATOM   1641  CA  SER A 440     -10.944  58.245  19.859  1.00 41.21           C  
ANISOU 1641  CA  SER A 440     6087   5575   3997   -626   -119   -488       C  
ATOM   1642  C   SER A 440     -10.583  59.563  20.525  1.00 42.08           C  
ANISOU 1642  C   SER A 440     6200   5690   4100   -596   -102   -443       C  
ATOM   1643  O   SER A 440     -11.051  59.873  21.618  1.00 33.49           O  
ANISOU 1643  O   SER A 440     5069   4628   3030   -564   -118   -418       O  
ATOM   1644  CB  SER A 440     -11.978  58.483  18.756  1.00 43.86           C  
ANISOU 1644  CB  SER A 440     6495   5874   4296   -619   -218   -493       C  
ATOM   1645  OG  SER A 440     -11.974  57.413  17.826  1.00 62.54           O  
ANISOU 1645  OG  SER A 440     8882   8222   6658   -654   -221   -539       O  
ATOM   1646  N   LEU A 441      -9.751  60.332  19.835  1.00 42.87           N  
ANISOU 1646  N   LEU A 441     6356   5763   4171   -613    -65   -436       N  
ATOM   1647  CA  LEU A 441      -9.207  61.569  20.357  1.00 39.52           C  
ANISOU 1647  CA  LEU A 441     5937   5336   3742   -598    -41   -403       C  
ATOM   1648  C   LEU A 441      -8.932  62.539  19.219  1.00 40.50           C  
ANISOU 1648  C   LEU A 441     6158   5415   3815   -622    -44   -394       C  
ATOM   1649  O   LEU A 441      -8.217  62.210  18.270  1.00 37.66           O  
ANISOU 1649  O   LEU A 441     5843   5034   3434   -672      5   -419       O  
ATOM   1650  CB  LEU A 441      -7.927  61.286  21.146  1.00 33.96           C  
ANISOU 1650  CB  LEU A 441     5170   4656   3077   -619     46   -414       C  
ATOM   1651  CG  LEU A 441      -7.130  62.463  21.703  1.00 30.18           C  
ANISOU 1651  CG  LEU A 441     4692   4174   2601   -615     78   -391       C  
ATOM   1652  CD1 LEU A 441      -7.885  63.158  22.829  1.00 26.89           C  
ANISOU 1652  CD1 LEU A 441     4250   3775   2194   -557     32   -353       C  
ATOM   1653  CD2 LEU A 441      -5.756  61.998  22.169  1.00 31.27           C  
ANISOU 1653  CD2 LEU A 441     4777   4329   2774   -653    158   -422       C  
ATOM   1654  N   SER A 442      -9.510  63.729  19.315  1.00 40.28           N  
ANISOU 1654  N   SER A 442     6170   5371   3765   -590    -97   -360       N  
ATOM   1655  CA  SER A 442      -9.284  64.779  18.332  1.00 43.69           C  
ANISOU 1655  CA  SER A 442     6704   5754   4143   -616   -103   -345       C  
ATOM   1656  C   SER A 442      -9.477  66.136  18.993  1.00 41.06           C  
ANISOU 1656  C   SER A 442     6380   5414   3809   -584   -127   -309       C  
ATOM   1657  O   SER A 442     -10.079  66.222  20.063  1.00 45.96           O  
ANISOU 1657  O   SER A 442     6937   6065   4462   -535   -158   -297       O  
ATOM   1658  CB  SER A 442     -10.229  64.616  17.143  1.00 51.20           C  
ANISOU 1658  CB  SER A 442     7738   6669   5045   -619   -184   -349       C  
ATOM   1659  OG  SER A 442     -11.579  64.663  17.565  1.00 57.14           O  
ANISOU 1659  OG  SER A 442     8467   7431   5812   -565   -286   -339       O  
ATOM   1660  N   LEU A 443      -8.969  67.189  18.358  1.00 38.39           N  
ANISOU 1660  N   LEU A 443     6128   5030   3429   -617   -109   -294       N  
ATOM   1661  CA  LEU A 443      -9.029  68.532  18.934  1.00 47.36           C  
ANISOU 1661  CA  LEU A 443     7282   6151   4562   -596   -125   -263       C  
ATOM   1662  C   LEU A 443     -10.468  68.987  19.142  1.00 44.80           C  
ANISOU 1662  C   LEU A 443     6972   5819   4231   -537   -232   -243       C  
ATOM   1663  O   LEU A 443     -11.145  69.386  18.195  1.00 45.52           O  
ANISOU 1663  O   LEU A 443     7157   5862   4277   -540   -304   -231       O  
ATOM   1664  CB  LEU A 443      -8.278  69.529  18.047  1.00 51.23           C  
ANISOU 1664  CB  LEU A 443     7883   6581   5001   -654    -90   -253       C  
ATOM   1665  CG  LEU A 443      -7.913  70.878  18.679  1.00 55.49           C  
ANISOU 1665  CG  LEU A 443     8439   7102   5541   -652    -77   -230       C  
ATOM   1666  CD1 LEU A 443      -6.596  71.386  18.124  1.00 49.60           C  
ANISOU 1666  CD1 LEU A 443     7758   6318   4770   -734     10   -239       C  
ATOM   1667  CD2 LEU A 443      -9.004  71.917  18.459  1.00 65.26           C  
ANISOU 1667  CD2 LEU A 443     9757   8295   6744   -616   -171   -198       C  
TER    1668      LEU A 443                                                      
ATOM   1669  N   LEU B 235      26.702  27.313  50.062  1.00 82.52           N  
ANISOU 1669  N   LEU B 235     9656   7545  14153    902  -1936     27       N  
ATOM   1670  CA  LEU B 235      26.530  26.271  49.060  1.00 88.61           C  
ANISOU 1670  CA  LEU B 235    10355   8201  15113    864  -2008   -102       C  
ATOM   1671  C   LEU B 235      27.231  26.699  47.781  1.00 95.43           C  
ANISOU 1671  C   LEU B 235    11193   9143  15923    885  -2007   -376       C  
ATOM   1672  O   LEU B 235      28.042  25.961  47.220  1.00 95.31           O  
ANISOU 1672  O   LEU B 235    11128   9081  16006    914  -2077   -521       O  
ATOM   1673  CB  LEU B 235      25.046  25.999  48.789  1.00 80.83           C  
ANISOU 1673  CB  LEU B 235     9343   7152  14216    780  -1997    -18       C  
ATOM   1674  CG  LEU B 235      24.033  25.927  49.939  1.00 70.28           C  
ANISOU 1674  CG  LEU B 235     8033   5786  12884    743  -1964    264       C  
ATOM   1675  CD1 LEU B 235      24.570  25.178  51.167  1.00 63.56           C  
ANISOU 1675  CD1 LEU B 235     7190   4870  12090    782  -2004    445       C  
ATOM   1676  CD2 LEU B 235      23.516  27.323  50.304  1.00 63.00           C  
ANISOU 1676  CD2 LEU B 235     7177   5011  11749    742  -1861    340       C  
ATOM   1677  N   GLY B 236      26.904  27.904  47.325  1.00 97.72           N  
ANISOU 1677  N   GLY B 236    11515   9562  16053    872  -1926   -439       N  
ATOM   1678  CA  GLY B 236      27.581  28.515  46.196  1.00 94.72           C  
ANISOU 1678  CA  GLY B 236    11116   9290  15583    894  -1906   -674       C  
ATOM   1679  C   GLY B 236      28.167  29.836  46.636  1.00 90.06           C  
ANISOU 1679  C   GLY B 236    10585   8844  14790    932  -1831   -668       C  
ATOM   1680  O   GLY B 236      28.476  30.706  45.820  1.00 88.66           O  
ANISOU 1680  O   GLY B 236    10404   8785  14496    938  -1784   -819       O  
ATOM   1681  N   GLY B 237      28.326  29.975  47.951  1.00 84.76           N  
ANISOU 1681  N   GLY B 237     9961   8167  14076    962  -1824   -487       N  
ATOM   1682  CA  GLY B 237      28.713  31.239  48.555  1.00 82.86           C  
ANISOU 1682  CA  GLY B 237     9777   8059  13647   1000  -1758   -450       C  
ATOM   1683  C   GLY B 237      27.523  32.177  48.624  1.00 81.53           C  
ANISOU 1683  C   GLY B 237     9649   7952  13377    958  -1683   -363       C  
ATOM   1684  O   GLY B 237      26.477  31.907  48.034  1.00 80.90           O  
ANISOU 1684  O   GLY B 237     9550   7822  13366    897  -1677   -361       O  
ATOM   1685  N   PRO B 238      27.669  33.284  49.365  1.00 81.95           N  
ANISOU 1685  N   PRO B 238     9754   8116  13267    992  -1630   -291       N  
ATOM   1686  CA  PRO B 238      26.584  34.270  49.375  1.00 78.37           C  
ANISOU 1686  CA  PRO B 238     9337   7732  12707    958  -1560   -224       C  
ATOM   1687  C   PRO B 238      26.569  35.115  48.105  1.00 75.02           C  
ANISOU 1687  C   PRO B 238     8902   7392  12213    932  -1512   -420       C  
ATOM   1688  O   PRO B 238      27.417  34.939  47.227  1.00 76.38           O  
ANISOU 1688  O   PRO B 238     9034   7580  12408    941  -1531   -601       O  
ATOM   1689  CB  PRO B 238      26.904  35.129  50.603  1.00 72.66           C  
ANISOU 1689  CB  PRO B 238     8666   7109  11835   1017  -1532    -99       C  
ATOM   1690  CG  PRO B 238      27.896  34.329  51.407  1.00 76.71           C  
ANISOU 1690  CG  PRO B 238     9170   7575  12402   1074  -1593    -46       C  
ATOM   1691  CD  PRO B 238      28.679  33.558  50.402  1.00 79.30           C  
ANISOU 1691  CD  PRO B 238     9445   7835  12851   1066  -1642   -232       C  
ATOM   1692  N   SER B 239      25.590  36.009  48.002  1.00 67.59           N  
ANISOU 1692  N   SER B 239     7990   6509  11182    900  -1451   -376       N  
ATOM   1693  CA  SER B 239      25.532  36.956  46.899  1.00 68.57           C  
ANISOU 1693  CA  SER B 239     8110   6728  11216    879  -1396   -540       C  
ATOM   1694  C   SER B 239      25.490  38.367  47.459  1.00 67.10           C  
ANISOU 1694  C   SER B 239     7974   6662  10858    905  -1336   -491       C  
ATOM   1695  O   SER B 239      24.987  38.588  48.560  1.00 70.79           O  
ANISOU 1695  O   SER B 239     8480   7135  11282    923  -1330   -314       O  
ATOM   1696  CB  SER B 239      24.311  36.693  46.025  1.00 68.34           C  
ANISOU 1696  CB  SER B 239     8061   6653  11251    812  -1381   -562       C  
ATOM   1697  OG  SER B 239      23.934  35.332  46.101  1.00 74.65           O  
ANISOU 1697  OG  SER B 239     8825   7315  12222    786  -1445   -502       O  
ATOM   1698  N   VAL B 240      26.026  39.322  46.709  1.00 65.88           N  
ANISOU 1698  N   VAL B 240     7815   6613  10603    909  -1293   -644       N  
ATOM   1699  CA  VAL B 240      26.018  40.708  47.159  1.00 60.37           C  
ANISOU 1699  CA  VAL B 240     7158   6029   9750    931  -1241   -617       C  
ATOM   1700  C   VAL B 240      25.350  41.616  46.132  1.00 57.07           C  
ANISOU 1700  C   VAL B 240     6743   5681   9260    888  -1174   -709       C  
ATOM   1701  O   VAL B 240      25.671  41.573  44.942  1.00 52.17           O  
ANISOU 1701  O   VAL B 240     6084   5088   8649    862  -1157   -865       O  
ATOM   1702  CB  VAL B 240      27.437  41.231  47.439  1.00 52.63           C  
ANISOU 1702  CB  VAL B 240     6171   5129   8698    982  -1248   -696       C  
ATOM   1703  CG1 VAL B 240      27.360  42.548  48.177  1.00 49.42           C  
ANISOU 1703  CG1 VAL B 240     5806   4825   8147   1012  -1212   -639       C  
ATOM   1704  CG2 VAL B 240      28.241  40.219  48.253  1.00 52.36           C  
ANISOU 1704  CG2 VAL B 240     6125   5025   8746   1027  -1318   -638       C  
ATOM   1705  N   PHE B 241      24.417  42.436  46.599  1.00 56.13           N  
ANISOU 1705  N   PHE B 241     6666   5599   9060    884  -1136   -608       N  
ATOM   1706  CA  PHE B 241      23.747  43.388  45.727  1.00 51.17           C  
ANISOU 1706  CA  PHE B 241     6047   5040   8355    847  -1071   -683       C  
ATOM   1707  C   PHE B 241      23.927  44.802  46.253  1.00 48.12           C  
ANISOU 1707  C   PHE B 241     5700   4790   7793    861  -1020   -659       C  
ATOM   1708  O   PHE B 241      23.753  45.066  47.445  1.00 43.63           O  
ANISOU 1708  O   PHE B 241     5167   4255   7154    885  -1027   -520       O  
ATOM   1709  CB  PHE B 241      22.266  43.038  45.590  1.00 62.88           C  
ANISOU 1709  CB  PHE B 241     7542   6471   9880    793  -1057   -588       C  
ATOM   1710  CG  PHE B 241      22.028  41.681  44.993  1.00 76.90           C  
ANISOU 1710  CG  PHE B 241     9274   8122  11823    763  -1105   -622       C  
ATOM   1711  CD1 PHE B 241      22.371  41.422  43.675  1.00 81.75           C  
ANISOU 1711  CD1 PHE B 241     9844   8755  12462    737  -1099   -801       C  
ATOM   1712  CD2 PHE B 241      21.473  40.662  45.750  1.00 79.14           C  
ANISOU 1712  CD2 PHE B 241     9555   8295  12220    753  -1153   -466       C  
ATOM   1713  CE1 PHE B 241      22.161  40.175  43.123  1.00 82.70           C  
ANISOU 1713  CE1 PHE B 241     9919   8782  12722    709  -1148   -839       C  
ATOM   1714  CE2 PHE B 241      21.261  39.411  45.203  1.00 80.04           C  
ANISOU 1714  CE2 PHE B 241     9624   8303  12485    716  -1198   -499       C  
ATOM   1715  CZ  PHE B 241      21.605  39.169  43.887  1.00 82.71           C  
ANISOU 1715  CZ  PHE B 241     9918   8657  12850    697  -1201   -694       C  
ATOM   1716  N   LEU B 242      24.294  45.704  45.352  1.00 45.58           N  
ANISOU 1716  N   LEU B 242     5367   4557   7395    842   -969   -794       N  
ATOM   1717  CA  LEU B 242      24.622  47.073  45.721  1.00 44.13           C  
ANISOU 1717  CA  LEU B 242     5211   4499   7058    847   -924   -794       C  
ATOM   1718  C   LEU B 242      23.607  48.045  45.136  1.00 42.90           C  
ANISOU 1718  C   LEU B 242     5082   4428   6789    785   -846   -790       C  
ATOM   1719  O   LEU B 242      23.413  48.097  43.921  1.00 44.97           O  
ANISOU 1719  O   LEU B 242     5320   4703   7065    747   -811   -892       O  
ATOM   1720  CB  LEU B 242      26.031  47.424  45.244  1.00 40.80           C  
ANISOU 1720  CB  LEU B 242     4747   4112   6645    878   -931   -941       C  
ATOM   1721  CG  LEU B 242      26.628  48.742  45.733  1.00 40.55           C  
ANISOU 1721  CG  LEU B 242     4730   4187   6490    891   -905   -949       C  
ATOM   1722  CD1 LEU B 242      26.574  48.814  47.249  1.00 36.94           C  
ANISOU 1722  CD1 LEU B 242     4314   3735   5986    937   -946   -816       C  
ATOM   1723  CD2 LEU B 242      28.057  48.880  45.236  1.00 41.25           C  
ANISOU 1723  CD2 LEU B 242     4762   4302   6607    910   -914  -1082       C  
ATOM   1724  N   PHE B 243      22.965  48.820  46.003  1.00 43.92           N  
ANISOU 1724  N   PHE B 243     5260   4624   6803    781   -821   -676       N  
ATOM   1725  CA  PHE B 243      21.897  49.708  45.564  1.00 47.97           C  
ANISOU 1725  CA  PHE B 243     5801   5212   7212    727   -752   -656       C  
ATOM   1726  C   PHE B 243      22.260  51.185  45.702  1.00 47.88           C  
ANISOU 1726  C   PHE B 243     5811   5310   7072    731   -714   -689       C  
ATOM   1727  O   PHE B 243      22.831  51.604  46.712  1.00 41.11           O  
ANISOU 1727  O   PHE B 243     4969   4483   6169    778   -743   -654       O  
ATOM   1728  CB  PHE B 243      20.622  49.410  46.347  1.00 40.75           C  
ANISOU 1728  CB  PHE B 243     4921   4287   6273    715   -749   -496       C  
ATOM   1729  CG  PHE B 243      20.179  47.979  46.246  1.00 48.90           C  
ANISOU 1729  CG  PHE B 243     5929   5201   7449    702   -789   -447       C  
ATOM   1730  CD1 PHE B 243      20.545  47.058  47.214  1.00 49.76           C  
ANISOU 1730  CD1 PHE B 243     6032   5235   7639    748   -852   -355       C  
ATOM   1731  CD2 PHE B 243      19.417  47.550  45.174  1.00 53.28           C  
ANISOU 1731  CD2 PHE B 243     6462   5715   8067    648   -770   -496       C  
ATOM   1732  CE1 PHE B 243      20.148  45.738  47.120  1.00 55.16           C  
ANISOU 1732  CE1 PHE B 243     6689   5794   8476    733   -894   -304       C  
ATOM   1733  CE2 PHE B 243      19.016  46.231  45.074  1.00 57.23           C  
ANISOU 1733  CE2 PHE B 243     6934   6093   8719    635   -816   -460       C  
ATOM   1734  CZ  PHE B 243      19.381  45.323  46.049  1.00 54.84           C  
ANISOU 1734  CZ  PHE B 243     6625   5703   8508    675   -879   -360       C  
ATOM   1735  N   PRO B 244      21.924  51.976  44.674  1.00 43.62           N  
ANISOU 1735  N   PRO B 244     5268   4827   6478    683   -655   -756       N  
ATOM   1736  CA  PRO B 244      22.154  53.420  44.669  1.00 36.67           C  
ANISOU 1736  CA  PRO B 244     4404   4038   5491    676   -617   -784       C  
ATOM   1737  C   PRO B 244      21.221  54.137  45.647  1.00 35.35           C  
ANISOU 1737  C   PRO B 244     4292   3923   5218    683   -606   -671       C  
ATOM   1738  O   PRO B 244      20.280  53.527  46.155  1.00 37.98           O  
ANISOU 1738  O   PRO B 244     4646   4234   5551    683   -612   -569       O  
ATOM   1739  CB  PRO B 244      21.841  53.812  43.224  1.00 30.59           C  
ANISOU 1739  CB  PRO B 244     3613   3304   4707    621   -558   -864       C  
ATOM   1740  CG  PRO B 244      20.827  52.819  42.791  1.00 31.71           C  
ANISOU 1740  CG  PRO B 244     3753   3394   4900    595   -556   -834       C  
ATOM   1741  CD  PRO B 244      21.225  51.526  43.459  1.00 40.36           C  
ANISOU 1741  CD  PRO B 244     4835   4394   6106    634   -624   -805       C  
ATOM   1742  N   PRO B 245      21.492  55.417  45.919  1.00 33.08           N  
ANISOU 1742  N   PRO B 245     4020   3704   4845    691   -591   -690       N  
ATOM   1743  CA  PRO B 245      20.579  56.220  46.736  1.00 38.19           C  
ANISOU 1743  CA  PRO B 245     4715   4412   5384    703   -579   -605       C  
ATOM   1744  C   PRO B 245      19.302  56.565  45.991  1.00 36.59           C  
ANISOU 1744  C   PRO B 245     4530   4238   5133    649   -519   -579       C  
ATOM   1745  O   PRO B 245      19.289  56.553  44.759  1.00 49.44           O  
ANISOU 1745  O   PRO B 245     6133   5857   6793    602   -484   -646       O  
ATOM   1746  CB  PRO B 245      21.394  57.482  47.039  1.00 27.67           C  
ANISOU 1746  CB  PRO B 245     3383   3127   4003    725   -590   -666       C  
ATOM   1747  CG  PRO B 245      22.436  57.529  45.976  1.00 29.00           C  
ANISOU 1747  CG  PRO B 245     3503   3273   4244    696   -578   -776       C  
ATOM   1748  CD  PRO B 245      22.755  56.117  45.638  1.00 28.31           C  
ANISOU 1748  CD  PRO B 245     3384   3118   4253    699   -598   -791       C  
ATOM   1749  N   LYS B 246      18.234  56.844  46.733  1.00 35.04           N  
ANISOU 1749  N   LYS B 246     4372   4085   4858    661   -510   -482       N  
ATOM   1750  CA  LYS B 246      17.005  57.324  46.123  1.00 31.25           C  
ANISOU 1750  CA  LYS B 246     3909   3644   4322    616   -456   -457       C  
ATOM   1751  C   LYS B 246      17.314  58.642  45.423  1.00 37.12           C  
ANISOU 1751  C   LYS B 246     4654   4429   5021    594   -426   -537       C  
ATOM   1752  O   LYS B 246      17.979  59.504  46.002  1.00 39.31           O  
ANISOU 1752  O   LYS B 246     4939   4732   5265    628   -448   -564       O  
ATOM   1753  CB  LYS B 246      15.906  57.506  47.172  1.00 32.58           C  
ANISOU 1753  CB  LYS B 246     4111   3864   4402    644   -453   -342       C  
ATOM   1754  CG  LYS B 246      15.822  56.377  48.186  1.00 42.41           C  
ANISOU 1754  CG  LYS B 246     5354   5082   5680    681   -490   -241       C  
ATOM   1755  CD  LYS B 246      14.523  56.437  48.974  1.00 57.49           C  
ANISOU 1755  CD  LYS B 246     7285   7055   7505    696   -470   -115       C  
ATOM   1756  CE  LYS B 246      13.501  55.453  48.417  1.00 72.03           C  
ANISOU 1756  CE  LYS B 246     9107   8850   9413    639   -444    -49       C  
ATOM   1757  NZ  LYS B 246      14.007  54.046  48.470  1.00 75.45           N  
ANISOU 1757  NZ  LYS B 246     9509   9182   9975    636   -485    -22       N  
ATOM   1758  N   PRO B 247      16.858  58.787  44.167  1.00 35.48           N  
ANISOU 1758  N   PRO B 247     4434   4228   4820    539   -378   -575       N  
ATOM   1759  CA  PRO B 247      17.112  59.970  43.337  1.00 35.41           C  
ANISOU 1759  CA  PRO B 247     4419   4257   4777    511   -343   -636       C  
ATOM   1760  C   PRO B 247      16.870  61.271  44.096  1.00 35.39           C  
ANISOU 1760  C   PRO B 247     4452   4301   4695    537   -348   -609       C  
ATOM   1761  O   PRO B 247      17.663  62.202  43.980  1.00 33.98           O  
ANISOU 1761  O   PRO B 247     4263   4129   4519    538   -354   -662       O  
ATOM   1762  CB  PRO B 247      16.110  59.809  42.192  1.00 30.85           C  
ANISOU 1762  CB  PRO B 247     3837   3698   4188    461   -294   -634       C  
ATOM   1763  CG  PRO B 247      15.968  58.337  42.047  1.00 31.30           C  
ANISOU 1763  CG  PRO B 247     3872   3700   4321    456   -312   -630       C  
ATOM   1764  CD  PRO B 247      16.063  57.775  43.448  1.00 26.38           C  
ANISOU 1764  CD  PRO B 247     3266   3045   3711    502   -359   -558       C  
ATOM   1765  N   LYS B 248      15.804  61.311  44.886  1.00 34.94           N  
ANISOU 1765  N   LYS B 248     4430   4275   4572    561   -350   -531       N  
ATOM   1766  CA  LYS B 248      15.456  62.501  45.647  1.00 32.75           C  
ANISOU 1766  CA  LYS B 248     4184   4047   4212    597   -361   -513       C  
ATOM   1767  C   LYS B 248      16.510  62.854  46.695  1.00 36.68           C  
ANISOU 1767  C   LYS B 248     4682   4541   4712    656   -419   -545       C  
ATOM   1768  O   LYS B 248      16.814  64.026  46.908  1.00 39.26           O  
ANISOU 1768  O   LYS B 248     5017   4886   5016    673   -435   -587       O  
ATOM   1769  CB  LYS B 248      14.097  62.308  46.320  1.00 26.09           C  
ANISOU 1769  CB  LYS B 248     3369   3249   3293    619   -350   -420       C  
ATOM   1770  CG  LYS B 248      13.622  63.512  47.098  1.00 31.17           C  
ANISOU 1770  CG  LYS B 248     4044   3955   3844    666   -361   -410       C  
ATOM   1771  CD  LYS B 248      12.329  63.202  47.803  1.00 29.50           C  
ANISOU 1771  CD  LYS B 248     3850   3802   3555    693   -347   -314       C  
ATOM   1772  CE  LYS B 248      11.838  64.388  48.593  1.00 28.08           C  
ANISOU 1772  CE  LYS B 248     3697   3695   3278    752   -361   -316       C  
ATOM   1773  NZ  LYS B 248      10.653  63.957  49.365  1.00 35.11           N  
ANISOU 1773  NZ  LYS B 248     4594   4656   4089    785   -346   -215       N  
ATOM   1774  N   ASP B 249      17.067  61.833  47.341  1.00 29.63           N  
ANISOU 1774  N   ASP B 249     3778   3623   3857    688   -455   -527       N  
ATOM   1775  CA  ASP B 249      18.024  62.040  48.424  1.00 31.99           C  
ANISOU 1775  CA  ASP B 249     4075   3927   4153    752   -517   -552       C  
ATOM   1776  C   ASP B 249      19.329  62.681  47.945  1.00 32.66           C  
ANISOU 1776  C   ASP B 249     4128   3978   4303    737   -535   -654       C  
ATOM   1777  O   ASP B 249      19.981  63.405  48.694  1.00 30.10           O  
ANISOU 1777  O   ASP B 249     3803   3667   3967    782   -584   -696       O  
ATOM   1778  CB  ASP B 249      18.319  60.716  49.133  1.00 32.47           C  
ANISOU 1778  CB  ASP B 249     4127   3965   4246    789   -551   -499       C  
ATOM   1779  CG  ASP B 249      17.107  60.154  49.851  1.00 29.86           C  
ANISOU 1779  CG  ASP B 249     3821   3675   3849    812   -540   -381       C  
ATOM   1780  OD1 ASP B 249      16.190  60.941  50.170  1.00 39.03           O  
ANISOU 1780  OD1 ASP B 249     5008   4902   4918    827   -521   -350       O  
ATOM   1781  OD2 ASP B 249      17.071  58.931  50.102  1.00 38.01           O  
ANISOU 1781  OD2 ASP B 249     4842   4673   4928    817   -551   -315       O  
ATOM   1782  N   THR B 250      19.702  62.419  46.698  1.00 33.65           N  
ANISOU 1782  N   THR B 250     4221   4067   4498    675   -497   -696       N  
ATOM   1783  CA  THR B 250      20.913  63.003  46.129  1.00 31.48           C  
ANISOU 1783  CA  THR B 250     3905   3770   4287    652   -503   -781       C  
ATOM   1784  C   THR B 250      20.677  64.415  45.620  1.00 33.50           C  
ANISOU 1784  C   THR B 250     4165   4045   4519    620   -477   -801       C  
ATOM   1785  O   THR B 250      21.621  65.184  45.438  1.00 39.80           O  
ANISOU 1785  O   THR B 250     4929   4827   5365    608   -492   -858       O  
ATOM   1786  CB  THR B 250      21.452  62.162  44.960  1.00 36.57           C  
ANISOU 1786  CB  THR B 250     4504   4384   5007    606   -470   -819       C  
ATOM   1787  OG1 THR B 250      20.574  62.286  43.835  1.00 41.74           O  
ANISOU 1787  OG1 THR B 250     5163   5058   5638    551   -406   -803       O  
ATOM   1788  CG2 THR B 250      21.536  60.719  45.361  1.00 38.01           C  
ANISOU 1788  CG2 THR B 250     4684   4533   5227    635   -497   -795       C  
ATOM   1789  N   LEU B 251      19.416  64.744  45.376  1.00 29.02           N  
ANISOU 1789  N   LEU B 251     3633   3508   3886    603   -439   -750       N  
ATOM   1790  CA  LEU B 251      19.066  66.009  44.746  1.00 33.71           C  
ANISOU 1790  CA  LEU B 251     4231   4115   4462    569   -410   -758       C  
ATOM   1791  C   LEU B 251      18.734  67.090  45.766  1.00 27.47           C  
ANISOU 1791  C   LEU B 251     3473   3341   3623    618   -454   -758       C  
ATOM   1792  O   LEU B 251      19.077  68.254  45.576  1.00 27.11           O  
ANISOU 1792  O   LEU B 251     3416   3279   3604    605   -465   -793       O  
ATOM   1793  CB  LEU B 251      17.892  65.804  43.787  1.00 29.00           C  
ANISOU 1793  CB  LEU B 251     3649   3544   3825    524   -346   -712       C  
ATOM   1794  CG  LEU B 251      18.167  64.911  42.576  1.00 32.81           C  
ANISOU 1794  CG  LEU B 251     4094   4018   4353    476   -302   -731       C  
ATOM   1795  CD1 LEU B 251      16.873  64.576  41.844  1.00 28.97           C  
ANISOU 1795  CD1 LEU B 251     3626   3562   3819    446   -253   -687       C  
ATOM   1796  CD2 LEU B 251      19.165  65.575  41.643  1.00 23.22           C  
ANISOU 1796  CD2 LEU B 251     2832   2800   3191    436   -279   -780       C  
ATOM   1797  N   MET B 252      18.066  66.701  46.847  1.00 29.03           N  
ANISOU 1797  N   MET B 252     3706   3574   3751    678   -481   -718       N  
ATOM   1798  CA  MET B 252      17.676  67.640  47.891  1.00 31.67           C  
ANISOU 1798  CA  MET B 252     4069   3942   4023    741   -526   -725       C  
ATOM   1799  C   MET B 252      18.693  67.664  49.029  1.00 35.75           C  
ANISOU 1799  C   MET B 252     4574   4455   4554    808   -603   -776       C  
ATOM   1800  O   MET B 252      18.969  66.639  49.654  1.00 32.06           O  
ANISOU 1800  O   MET B 252     4104   4000   4077    844   -624   -751       O  
ATOM   1801  CB  MET B 252      16.290  67.282  48.435  1.00 28.52           C  
ANISOU 1801  CB  MET B 252     3709   3605   3522    776   -507   -648       C  
ATOM   1802  CG  MET B 252      15.196  67.218  47.376  1.00 30.19           C  
ANISOU 1802  CG  MET B 252     3931   3826   3715    715   -437   -600       C  
ATOM   1803  SD  MET B 252      14.960  68.775  46.489  1.00 48.71           S  
ANISOU 1803  SD  MET B 252     6278   6156   6072    677   -417   -636       S  
ATOM   1804  CE  MET B 252      15.595  68.356  44.872  1.00 37.52           C  
ANISOU 1804  CE  MET B 252     4822   4695   4741    584   -361   -649       C  
ATOM   1805  N   ILE B 253      19.242  68.845  49.296  1.00 38.18           N  
ANISOU 1805  N   ILE B 253     4871   4744   4892    826   -651   -847       N  
ATOM   1806  CA  ILE B 253      20.254  68.998  50.332  1.00 39.32           C  
ANISOU 1806  CA  ILE B 253     4997   4885   5057    891   -733   -912       C  
ATOM   1807  C   ILE B 253      19.669  68.710  51.718  1.00 44.64           C  
ANISOU 1807  C   ILE B 253     5705   5639   5618    991   -776   -886       C  
ATOM   1808  O   ILE B 253      20.394  68.345  52.642  1.00 43.93           O  
ANISOU 1808  O   ILE B 253     5603   5566   5521   1054   -836   -913       O  
ATOM   1809  CB  ILE B 253      20.877  70.415  50.302  1.00 38.46           C  
ANISOU 1809  CB  ILE B 253     4865   4732   5016    886   -782   -999       C  
ATOM   1810  CG1 ILE B 253      22.107  70.488  51.210  1.00 40.20           C  
ANISOU 1810  CG1 ILE B 253     5054   4940   5283    942   -869  -1080       C  
ATOM   1811  CG2 ILE B 253      19.855  71.472  50.686  1.00 18.26           C  
ANISOU 1811  CG2 ILE B 253     2343   2203   2393    925   -798  -1005       C  
ATOM   1812  CD1 ILE B 253      23.217  69.556  50.800  1.00 40.68           C  
ANISOU 1812  CD1 ILE B 253     5071   4966   5421    906   -859  -1086       C  
ATOM   1813  N   SER B 254      18.352  68.846  51.849  1.00 39.92           N  
ANISOU 1813  N   SER B 254     5144   5097   4927   1008   -742   -827       N  
ATOM   1814  CA  SER B 254      17.682  68.594  53.121  1.00 39.21           C  
ANISOU 1814  CA  SER B 254     5080   5102   4716   1104   -771   -788       C  
ATOM   1815  C   SER B 254      17.572  67.100  53.415  1.00 37.36           C  
ANISOU 1815  C   SER B 254     4846   4895   4455   1111   -746   -693       C  
ATOM   1816  O   SER B 254      17.195  66.706  54.517  1.00 41.41           O  
ANISOU 1816  O   SER B 254     5371   5491   4873   1191   -770   -643       O  
ATOM   1817  CB  SER B 254      16.293  69.230  53.129  1.00 35.81           C  
ANISOU 1817  CB  SER B 254     4679   4728   4197   1118   -739   -754       C  
ATOM   1818  OG  SER B 254      15.503  68.732  52.063  1.00 37.12           O  
ANISOU 1818  OG  SER B 254     4854   4874   4377   1036   -656   -678       O  
ATOM   1819  N   ARG B 255      17.902  66.276  52.425  1.00 34.45           N  
ANISOU 1819  N   ARG B 255     4460   4456   4172   1030   -701   -667       N  
ATOM   1820  CA  ARG B 255      17.869  64.825  52.584  1.00 35.62           C  
ANISOU 1820  CA  ARG B 255     4604   4604   4327   1028   -685   -583       C  
ATOM   1821  C   ARG B 255      19.279  64.241  52.677  1.00 32.81           C  
ANISOU 1821  C   ARG B 255     4215   4194   4056   1034   -729   -629       C  
ATOM   1822  O   ARG B 255      20.256  64.893  52.306  1.00 30.95           O  
ANISOU 1822  O   ARG B 255     3956   3913   3891   1015   -755   -725       O  
ATOM   1823  CB  ARG B 255      17.109  64.176  51.424  1.00 41.41           C  
ANISOU 1823  CB  ARG B 255     5337   5300   5096    941   -608   -524       C  
ATOM   1824  CG  ARG B 255      15.676  64.663  51.246  1.00 45.43           C  
ANISOU 1824  CG  ARG B 255     5872   5861   5526    929   -561   -473       C  
ATOM   1825  CD  ARG B 255      14.737  64.052  52.273  1.00 51.93           C  
ANISOU 1825  CD  ARG B 255     6711   6766   6255    987   -558   -367       C  
ATOM   1826  NE  ARG B 255      14.708  62.595  52.181  1.00 65.06           N  
ANISOU 1826  NE  ARG B 255     8358   8394   7967    959   -540   -283       N  
ATOM   1827  CZ  ARG B 255      13.973  61.809  52.960  1.00 72.19           C  
ANISOU 1827  CZ  ARG B 255     9263   9351   8815    993   -532   -166       C  
ATOM   1828  NH1 ARG B 255      14.014  60.493  52.806  1.00 71.61           N  
ANISOU 1828  NH1 ARG B 255     9171   9224   8813    961   -523    -92       N  
ATOM   1829  NH2 ARG B 255      13.195  62.332  53.897  1.00 74.36           N  
ANISOU 1829  NH2 ARG B 255     9552   9733   8967   1061   -534   -121       N  
ATOM   1830  N   THR B 256      19.371  63.008  53.169  1.00 34.00           N  
ANISOU 1830  N   THR B 256     4363   4349   4208   1060   -738   -557       N  
ATOM   1831  CA  THR B 256      20.653  62.321  53.316  1.00 30.74           C  
ANISOU 1831  CA  THR B 256     3919   3886   3875   1075   -784   -593       C  
ATOM   1832  C   THR B 256      20.706  61.054  52.458  1.00 33.50           C  
ANISOU 1832  C   THR B 256     4250   4163   4315   1012   -745   -549       C  
ATOM   1833  O   THR B 256      20.087  60.044  52.787  1.00 40.18           O  
ANISOU 1833  O   THR B 256     5106   5015   5147   1023   -733   -446       O  
ATOM   1834  CB  THR B 256      20.932  61.946  54.787  1.00 39.18           C  
ANISOU 1834  CB  THR B 256     4993   5020   4875   1180   -849   -553       C  
ATOM   1835  OG1 THR B 256      20.996  63.135  55.580  1.00 42.74           O  
ANISOU 1835  OG1 THR B 256     5453   5540   5245   1248   -897   -619       O  
ATOM   1836  CG2 THR B 256      22.250  61.194  54.909  1.00 43.53           C  
ANISOU 1836  CG2 THR B 256     5509   5516   5512   1197   -898   -587       C  
ATOM   1837  N   PRO B 257      21.452  61.111  51.349  1.00 29.32           N  
ANISOU 1837  N   PRO B 257     3689   3566   3883    949   -727   -629       N  
ATOM   1838  CA  PRO B 257      21.557  59.965  50.442  1.00 33.09           C  
ANISOU 1838  CA  PRO B 257     4145   3978   4451    896   -696   -615       C  
ATOM   1839  C   PRO B 257      22.412  58.821  50.999  1.00 38.43           C  
ANISOU 1839  C   PRO B 257     4798   4614   5187    940   -748   -600       C  
ATOM   1840  O   PRO B 257      23.424  59.065  51.654  1.00 44.82           O  
ANISOU 1840  O   PRO B 257     5591   5432   6005    992   -805   -650       O  
ATOM   1841  CB  PRO B 257      22.196  60.576  49.188  1.00 37.56           C  
ANISOU 1841  CB  PRO B 257     4678   4511   5084    831   -665   -715       C  
ATOM   1842  CG  PRO B 257      22.973  61.741  49.697  1.00 29.55           C  
ANISOU 1842  CG  PRO B 257     3654   3519   4055    862   -707   -785       C  
ATOM   1843  CD  PRO B 257      22.171  62.292  50.840  1.00 26.04           C  
ANISOU 1843  CD  PRO B 257     3254   3139   3502    923   -733   -735       C  
ATOM   1844  N   GLU B 258      21.994  57.587  50.731  1.00 40.13           N  
ANISOU 1844  N   GLU B 258     5011   4784   5454    920   -732   -534       N  
ATOM   1845  CA  GLU B 258      22.711  56.397  51.175  1.00 36.85           C  
ANISOU 1845  CA  GLU B 258     4573   4317   5113    958   -782   -509       C  
ATOM   1846  C   GLU B 258      22.965  55.410  50.040  1.00 40.09           C  
ANISOU 1846  C   GLU B 258     4949   4638   5645    905   -764   -548       C  
ATOM   1847  O   GLU B 258      22.116  55.220  49.175  1.00 33.33           O  
ANISOU 1847  O   GLU B 258     4096   3764   4803    846   -713   -535       O  
ATOM   1848  CB  GLU B 258      21.926  55.677  52.269  1.00 39.45           C  
ANISOU 1848  CB  GLU B 258     4928   4671   5392   1006   -800   -365       C  
ATOM   1849  CG  GLU B 258      21.469  56.517  53.436  1.00 44.98           C  
ANISOU 1849  CG  GLU B 258     5660   5477   5952   1069   -814   -315       C  
ATOM   1850  CD  GLU B 258      20.519  55.739  54.321  1.00 46.49           C  
ANISOU 1850  CD  GLU B 258     5868   5704   6092   1103   -812   -153       C  
ATOM   1851  OE1 GLU B 258      20.439  56.032  55.534  1.00 50.90           O  
ANISOU 1851  OE1 GLU B 258     6441   6354   6544   1183   -843    -98       O  
ATOM   1852  OE2 GLU B 258      19.859  54.818  53.791  1.00 44.21           O  
ANISOU 1852  OE2 GLU B 258     5572   5354   5872   1050   -780    -82       O  
ATOM   1853  N   VAL B 259      24.124  54.763  50.063  1.00 33.27           N  
ANISOU 1853  N   VAL B 259     4049   3723   4869    933   -810   -600       N  
ATOM   1854  CA  VAL B 259      24.351  53.599  49.218  1.00 32.48           C  
ANISOU 1854  CA  VAL B 259     3915   3536   4890    905   -810   -629       C  
ATOM   1855  C   VAL B 259      24.217  52.360  50.096  1.00 34.23           C  
ANISOU 1855  C   VAL B 259     4141   3704   5159    951   -861   -521       C  
ATOM   1856  O   VAL B 259      24.720  52.335  51.219  1.00 38.57           O  
ANISOU 1856  O   VAL B 259     4698   4277   5678   1019   -913   -477       O  
ATOM   1857  CB  VAL B 259      25.725  53.639  48.526  1.00 39.27           C  
ANISOU 1857  CB  VAL B 259     4722   4371   5828    905   -825   -765       C  
ATOM   1858  CG1 VAL B 259      26.023  52.314  47.851  1.00 42.70           C  
ANISOU 1858  CG1 VAL B 259     5118   4717   6388    899   -842   -798       C  
ATOM   1859  CG2 VAL B 259      25.763  54.763  47.507  1.00 34.81           C  
ANISOU 1859  CG2 VAL B 259     4144   3855   5227    849   -766   -851       C  
ATOM   1860  N   THR B 260      23.524  51.340  49.598  1.00 34.24           N  
ANISOU 1860  N   THR B 260     4136   3633   5239    915   -850   -474       N  
ATOM   1861  CA  THR B 260      23.188  50.190  50.431  1.00 36.43           C  
ANISOU 1861  CA  THR B 260     4419   3854   5569    948   -892   -343       C  
ATOM   1862  C   THR B 260      23.756  48.882  49.883  1.00 45.42           C  
ANISOU 1862  C   THR B 260     5515   4869   6873    948   -935   -384       C  
ATOM   1863  O   THR B 260      23.443  48.478  48.760  1.00 44.73           O  
ANISOU 1863  O   THR B 260     5406   4727   6863    894   -911   -450       O  
ATOM   1864  CB  THR B 260      21.662  50.046  50.582  1.00 34.95           C  
ANISOU 1864  CB  THR B 260     4258   3682   5340    910   -851   -213       C  
ATOM   1865  OG1 THR B 260      21.099  51.306  50.972  1.00 35.65           O  
ANISOU 1865  OG1 THR B 260     4382   3886   5275    912   -810   -192       O  
ATOM   1866  CG2 THR B 260      21.331  49.006  51.629  1.00 34.49           C  
ANISOU 1866  CG2 THR B 260     4202   3583   5321    948   -893    -49       C  
ATOM   1867  N   CYS B 261      24.588  48.224  50.689  1.00 46.69           N  
ANISOU 1867  N   CYS B 261     5662   4989   7087   1013  -1003   -350       N  
ATOM   1868  CA  CYS B 261      25.190  46.942  50.322  1.00 35.05           C  
ANISOU 1868  CA  CYS B 261     4147   3391   5779   1027  -1057   -384       C  
ATOM   1869  C   CYS B 261      24.472  45.796  51.028  1.00 36.51           C  
ANISOU 1869  C   CYS B 261     4338   3495   6038   1037  -1092   -214       C  
ATOM   1870  O   CYS B 261      24.458  45.724  52.257  1.00 40.53           O  
ANISOU 1870  O   CYS B 261     4868   4039   6492   1090  -1120    -81       O  
ATOM   1871  CB  CYS B 261      26.678  46.936  50.673  1.00 28.84           C  
ANISOU 1871  CB  CYS B 261     3334   2604   5021   1095  -1114   -466       C  
ATOM   1872  SG  CYS B 261      27.616  45.532  50.042  1.00 47.16           S  
ANISOU 1872  SG  CYS B 261     5598   4794   7527   1105  -1169   -552       S  
ATOM   1873  N   VAL B 262      23.880  44.898  50.245  1.00 34.41           N  
ANISOU 1873  N   VAL B 262     4051   3124   5901    987  -1092   -217       N  
ATOM   1874  CA  VAL B 262      23.051  43.831  50.798  1.00 38.38           C  
ANISOU 1874  CA  VAL B 262     4552   3537   6492    979  -1120    -47       C  
ATOM   1875  C   VAL B 262      23.610  42.454  50.476  1.00 45.65           C  
ANISOU 1875  C   VAL B 262     5429   4295   7620    996  -1195    -78       C  
ATOM   1876  O   VAL B 262      23.773  42.093  49.308  1.00 51.28           O  
ANISOU 1876  O   VAL B 262     6111   4953   8420    954  -1190   -224       O  
ATOM   1877  CB  VAL B 262      21.605  43.916  50.269  1.00 39.60           C  
ANISOU 1877  CB  VAL B 262     4717   3696   6634    899  -1061      4       C  
ATOM   1878  CG1 VAL B 262      20.750  42.813  50.872  1.00 39.78           C  
ANISOU 1878  CG1 VAL B 262     4728   3624   6761    884  -1089    193       C  
ATOM   1879  CG2 VAL B 262      21.006  45.277  50.569  1.00 33.99           C  
ANISOU 1879  CG2 VAL B 262     4048   3142   5724    886   -989     32       C  
ATOM   1880  N   VAL B 263      23.895  41.683  51.519  1.00 46.20           N  
ANISOU 1880  N   VAL B 263     5499   4330   7724   1034  -1241     58       N  
ATOM   1881  CA  VAL B 263      24.438  40.341  51.340  1.00 50.63           C  
ANISOU 1881  CA  VAL B 263     6028   4774   8437   1024  -1289     40       C  
ATOM   1882  C   VAL B 263      23.372  39.282  51.618  1.00 48.96           C  
ANISOU 1882  C   VAL B 263     5806   4459   8337    979  -1302    208       C  
ATOM   1883  O   VAL B 263      22.804  39.230  52.709  1.00 50.09           O  
ANISOU 1883  O   VAL B 263     5969   4632   8431    997  -1298    409       O  
ATOM   1884  CB  VAL B 263      25.653  40.088  52.257  1.00 57.76           C  
ANISOU 1884  CB  VAL B 263     6932   5699   9317   1096  -1335     63       C  
ATOM   1885  CG1 VAL B 263      26.364  38.813  51.832  1.00 54.98           C  
ANISOU 1885  CG1 VAL B 263     6540   5229   9122   1085  -1387     -4       C  
ATOM   1886  CG2 VAL B 263      26.617  41.276  52.220  1.00 50.77           C  
ANISOU 1886  CG2 VAL B 263     6054   4932   8303   1139  -1320    -71       C  
ATOM   1887  N   VAL B 264      23.105  38.444  50.622  1.00 45.93           N  
ANISOU 1887  N   VAL B 264     5386   3966   8100    919  -1318    124       N  
ATOM   1888  CA  VAL B 264      22.129  37.370  50.761  1.00 62.21           C  
ANISOU 1888  CA  VAL B 264     7427   5916  10295    865  -1336    262       C  
ATOM   1889  C   VAL B 264      22.806  36.016  50.603  1.00 67.85           C  
ANISOU 1889  C   VAL B 264     8100   6508  11173    863  -1404    222       C  
ATOM   1890  O   VAL B 264      23.959  35.940  50.183  1.00 63.97           O  
ANISOU 1890  O   VAL B 264     7595   6021  10691    897  -1432     65       O  
ATOM   1891  CB  VAL B 264      20.997  37.495  49.728  1.00 70.38           C  
ANISOU 1891  CB  VAL B 264     8445   6919  11375    790  -1304    206       C  
ATOM   1892  CG1 VAL B 264      20.226  38.790  49.943  1.00 72.76           C  
ANISOU 1892  CG1 VAL B 264     8786   7336  11523    792  -1240    266       C  
ATOM   1893  CG2 VAL B 264      21.562  37.421  48.316  1.00 68.98           C  
ANISOU 1893  CG2 VAL B 264     8236   6723  11249    772  -1314    -44       C  
ATOM   1894  N   ASP B 265      22.070  34.957  50.932  1.00 70.81           N  
ANISOU 1894  N   ASP B 265     8450   6776  11676    820  -1431    367       N  
ATOM   1895  CA  ASP B 265      22.598  33.593  50.962  1.00 70.87           C  
ANISOU 1895  CA  ASP B 265     8418   6658  11852    819  -1504    365       C  
ATOM   1896  C   ASP B 265      23.769  33.478  51.935  1.00 77.38           C  
ANISOU 1896  C   ASP B 265     9262   7512  12627    900  -1533    414       C  
ATOM   1897  O   ASP B 265      24.725  32.734  51.703  1.00 84.11           O  
ANISOU 1897  O   ASP B 265    10086   8298  13573    924  -1591    318       O  
ATOM   1898  CB  ASP B 265      23.012  33.118  49.563  1.00 68.66           C  
ANISOU 1898  CB  ASP B 265     8090   6314  11683    793  -1541    127       C  
ATOM   1899  CG  ASP B 265      21.819  32.870  48.660  1.00 68.33           C  
ANISOU 1899  CG  ASP B 265     8016   6218  11730    714  -1532     92       C  
ATOM   1900  OD1 ASP B 265      20.679  32.817  49.177  1.00 62.87           O  
ANISOU 1900  OD1 ASP B 265     7330   5505  11054    670  -1508    271       O  
ATOM   1901  OD2 ASP B 265      22.021  32.719  47.435  1.00 72.64           O  
ANISOU 1901  OD2 ASP B 265     8525   6751  12325    697  -1550   -112       O  
ATOM   1902  N   VAL B 266      23.681  34.233  53.025  1.00 77.30           N  
ANISOU 1902  N   VAL B 266     9297   7613  12462    946  -1496    562       N  
ATOM   1903  CA  VAL B 266      24.557  34.035  54.168  1.00 69.92           C  
ANISOU 1903  CA  VAL B 266     8378   6712  11475   1024  -1524    660       C  
ATOM   1904  C   VAL B 266      24.049  32.834  54.955  1.00 78.80           C  
ANISOU 1904  C   VAL B 266     9485   7743  12713   1006  -1554    871       C  
ATOM   1905  O   VAL B 266      22.899  32.815  55.394  1.00 80.73           O  
ANISOU 1905  O   VAL B 266     9732   8000  12941    965  -1517   1045       O  
ATOM   1906  CB  VAL B 266      24.602  35.270  55.083  1.00 59.85           C  
ANISOU 1906  CB  VAL B 266     7152   5606   9983   1088  -1479    740       C  
ATOM   1907  CG1 VAL B 266      25.519  35.015  56.260  1.00 51.52           C  
ANISOU 1907  CG1 VAL B 266     6110   4593   8872   1175  -1513    834       C  
ATOM   1908  CG2 VAL B 266      25.067  36.486  54.310  1.00 65.34           C  
ANISOU 1908  CG2 VAL B 266     7859   6390  10576   1099  -1450    537       C  
ATOM   1909  N   SER B 267      24.895  31.824  55.120  1.00 84.08           N  
ANISOU 1909  N   SER B 267    10130   8318  13498   1033  -1619    857       N  
ATOM   1910  CA  SER B 267      24.480  30.629  55.840  1.00 86.85           C  
ANISOU 1910  CA  SER B 267    10457   8570  13971   1014  -1652   1054       C  
ATOM   1911  C   SER B 267      24.638  30.832  57.342  1.00 90.02           C  
ANISOU 1911  C   SER B 267    10896   9078  14230   1088  -1635   1264       C  
ATOM   1912  O   SER B 267      25.429  31.666  57.790  1.00 92.49           O  
ANISOU 1912  O   SER B 267    11243   9513  14384   1169  -1624   1220       O  
ATOM   1913  CB  SER B 267      25.271  29.406  55.371  1.00 90.62           C  
ANISOU 1913  CB  SER B 267    10890   8898  14645   1013  -1736    954       C  
ATOM   1914  OG  SER B 267      25.236  28.366  56.336  1.00 97.18           O  
ANISOU 1914  OG  SER B 267    11706   9654  15562   1025  -1774   1153       O  
ATOM   1915  N   HIS B 268      23.875  30.064  58.111  1.00 91.72           N  
ANISOU 1915  N   HIS B 268    11097   9252  14502   1061  -1633   1491       N  
ATOM   1916  CA  HIS B 268      23.884  30.151  59.562  1.00 91.03           C  
ANISOU 1916  CA  HIS B 268    11039   9276  14275   1129  -1614   1709       C  
ATOM   1917  C   HIS B 268      25.229  29.765  60.167  1.00 86.67           C  
ANISOU 1917  C   HIS B 268    10496   8721  13713   1225  -1672   1692       C  
ATOM   1918  O   HIS B 268      25.488  30.051  61.331  1.00 86.64           O  
ANISOU 1918  O   HIS B 268    10523   8840  13555   1307  -1660   1825       O  
ATOM   1919  CB  HIS B 268      22.798  29.247  60.148  1.00 97.78           C  
ANISOU 1919  CB  HIS B 268    11862  10072  15220   1067  -1602   1949       C  
ATOM   1920  CG  HIS B 268      23.107  27.787  60.026  1.00105.72           C  
ANISOU 1920  CG  HIS B 268    12817  10891  16459   1039  -1677   1975       C  
ATOM   1921  ND1 HIS B 268      22.904  27.076  58.862  1.00106.50           N  
ANISOU 1921  ND1 HIS B 268    12865  10822  16776    957  -1721   1842       N  
ATOM   1922  CD2 HIS B 268      23.617  26.906  60.919  1.00109.85           C  
ANISOU 1922  CD2 HIS B 268    13332  11373  17032   1086  -1721   2114       C  
ATOM   1923  CE1 HIS B 268      23.270  25.820  59.045  1.00108.75           C  
ANISOU 1923  CE1 HIS B 268    13110  10967  17242    953  -1791   1896       C  
ATOM   1924  NE2 HIS B 268      23.704  25.690  60.286  1.00111.50           N  
ANISOU 1924  NE2 HIS B 268    13485  11384  17495   1029  -1791   2066       N  
ATOM   1925  N   GLU B 269      26.073  29.114  59.370  1.00 89.77           N  
ANISOU 1925  N   GLU B 269    10859   8982  14266   1219  -1735   1522       N  
ATOM   1926  CA  GLU B 269      27.314  28.521  59.865  1.00 97.59           C  
ANISOU 1926  CA  GLU B 269    11847   9941  15290   1300  -1799   1509       C  
ATOM   1927  C   GLU B 269      28.546  29.411  59.682  1.00 98.72           C  
ANISOU 1927  C   GLU B 269    12013  10183  15313   1378  -1805   1318       C  
ATOM   1928  O   GLU B 269      29.589  29.175  60.294  1.00 94.54           O  
ANISOU 1928  O   GLU B 269    11488   9674  14759   1462  -1847   1323       O  
ATOM   1929  CB  GLU B 269      27.543  27.171  59.190  1.00100.06           C  
ANISOU 1929  CB  GLU B 269    12107  10052  15859   1251  -1872   1446       C  
ATOM   1930  CG  GLU B 269      26.960  26.007  59.978  1.00103.05           C  
ANISOU 1930  CG  GLU B 269    12461  10336  16357   1226  -1897   1685       C  
ATOM   1931  CD  GLU B 269      26.656  24.798  59.119  1.00106.53           C  
ANISOU 1931  CD  GLU B 269    12838  10573  17065   1142  -1958   1630       C  
ATOM   1932  OE1 GLU B 269      26.757  24.907  57.880  1.00106.39           O  
ANISOU 1932  OE1 GLU B 269    12797  10501  17125   1100  -1975   1406       O  
ATOM   1933  OE2 GLU B 269      26.311  23.738  59.688  1.00107.56           O  
ANISOU 1933  OE2 GLU B 269    12937  10604  17327   1119  -1992   1809       O  
ATOM   1934  N   ASP B 270      28.421  30.440  58.851  1.00107.89           N  
ANISOU 1934  N   ASP B 270    13183  11409  16400   1350  -1764   1154       N  
ATOM   1935  CA  ASP B 270      29.513  31.390  58.647  1.00118.15           C  
ANISOU 1935  CA  ASP B 270    14496  12812  17584   1411  -1764    974       C  
ATOM   1936  C   ASP B 270      29.229  32.834  59.093  1.00133.33           C  
ANISOU 1936  C   ASP B 270    16458  14918  19283   1445  -1702    994       C  
ATOM   1937  O   ASP B 270      30.033  33.730  58.820  1.00136.31           O  
ANISOU 1937  O   ASP B 270    16841  15381  19571   1481  -1698    833       O  
ATOM   1938  CB  ASP B 270      29.890  31.403  57.160  1.00113.62           C  
ANISOU 1938  CB  ASP B 270    13890  12164  17116   1356  -1777    719       C  
ATOM   1939  CG  ASP B 270      28.673  31.309  56.256  1.00107.18           C  
ANISOU 1939  CG  ASP B 270    13060  11280  16382   1256  -1746    701       C  
ATOM   1940  OD1 ASP B 270      27.728  30.574  56.637  1.00109.48           O  
ANISOU 1940  OD1 ASP B 270    13344  11498  16755   1214  -1748    877       O  
ATOM   1941  OD2 ASP B 270      28.656  31.952  55.185  1.00 94.94           O  
ANISOU 1941  OD2 ASP B 270    11503   9755  14816   1219  -1721    517       O  
ATOM   1942  N   PRO B 271      28.112  33.065  59.821  1.00148.13           N  
ANISOU 1942  N   PRO B 271    18357  16860  21065   1436  -1657   1191       N  
ATOM   1943  CA  PRO B 271      27.541  34.417  59.755  1.00140.26           C  
ANISOU 1943  CA  PRO B 271    17388  16004  19901   1432  -1596   1163       C  
ATOM   1944  C   PRO B 271      28.358  35.487  60.475  1.00129.33           C  
ANISOU 1944  C   PRO B 271    16027  14789  18324   1530  -1594   1121       C  
ATOM   1945  O   PRO B 271      27.956  35.937  61.541  1.00131.52           O  
ANISOU 1945  O   PRO B 271    16330  15200  18441   1586  -1572   1272       O  
ATOM   1946  CB  PRO B 271      26.189  34.237  60.444  1.00144.72           C  
ANISOU 1946  CB  PRO B 271    17966  16601  20421   1402  -1553   1396       C  
ATOM   1947  CG  PRO B 271      26.451  33.209  61.491  1.00148.57           C  
ANISOU 1947  CG  PRO B 271    18449  17059  20942   1450  -1591   1574       C  
ATOM   1948  CD  PRO B 271      27.577  32.325  60.986  1.00149.59           C  
ANISOU 1948  CD  PRO B 271    18549  17048  21240   1459  -1660   1447       C  
ATOM   1949  N   GLU B 272      29.484  35.897  59.896  1.00115.30           N  
ANISOU 1949  N   GLU B 272    14237  13015  16558   1549  -1619    914       N  
ATOM   1950  CA  GLU B 272      30.237  37.034  60.424  1.00100.54           C  
ANISOU 1950  CA  GLU B 272    12380  11303  14519   1625  -1618    844       C  
ATOM   1951  C   GLU B 272      30.807  37.856  59.276  1.00 81.59           C  
ANISOU 1951  C   GLU B 272     9967   8904  12130   1585  -1608    594       C  
ATOM   1952  O   GLU B 272      32.002  37.798  58.977  1.00 76.91           O  
ANISOU 1952  O   GLU B 272     9350   8294  11578   1606  -1643    448       O  
ATOM   1953  CB  GLU B 272      31.344  36.573  61.368  1.00106.47           C  
ANISOU 1953  CB  GLU B 272    13122  12083  15250   1718  -1672    888       C  
ATOM   1954  CG  GLU B 272      30.964  36.717  62.835  1.00112.43           C  
ANISOU 1954  CG  GLU B 272    13900  12974  15843   1803  -1664   1102       C  
ATOM   1955  CD  GLU B 272      31.886  35.960  63.772  1.00120.49           C  
ANISOU 1955  CD  GLU B 272    14910  14000  16869   1894  -1719   1184       C  
ATOM   1956  OE1 GLU B 272      32.967  35.517  63.329  1.00122.66           O  
ANISOU 1956  OE1 GLU B 272    15159  14190  17257   1897  -1765   1053       O  
ATOM   1957  OE2 GLU B 272      31.523  35.804  64.957  1.00123.07           O  
ANISOU 1957  OE2 GLU B 272    15257  14424  17080   1966  -1716   1377       O  
ATOM   1958  N   VAL B 273      29.930  38.639  58.660  1.00 69.04           N  
ANISOU 1958  N   VAL B 273     8391   7345  10496   1528  -1557    554       N  
ATOM   1959  CA  VAL B 273      30.226  39.363  57.431  1.00 62.13           C  
ANISOU 1959  CA  VAL B 273     7503   6464   9638   1476  -1535    334       C  
ATOM   1960  C   VAL B 273      30.950  40.688  57.681  1.00 54.75           C  
ANISOU 1960  C   VAL B 273     6576   5670   8556   1520  -1529    222       C  
ATOM   1961  O   VAL B 273      30.572  41.454  58.566  1.00 56.02           O  
ANISOU 1961  O   VAL B 273     6763   5952   8570   1564  -1516    311       O  
ATOM   1962  CB  VAL B 273      28.925  39.637  56.650  1.00 60.67           C  
ANISOU 1962  CB  VAL B 273     7329   6252   9471   1397  -1483    343       C  
ATOM   1963  CG1 VAL B 273      29.239  40.164  55.267  1.00 56.47           C  
ANISOU 1963  CG1 VAL B 273     6778   5702   8976   1343  -1459    119       C  
ATOM   1964  CG2 VAL B 273      28.085  38.364  56.560  1.00 57.35           C  
ANISOU 1964  CG2 VAL B 273     6899   5701   9192   1349  -1490    475       C  
ATOM   1965  N   LYS B 274      31.988  40.955  56.893  1.00 53.71           N  
ANISOU 1965  N   LYS B 274     6416   5527   8463   1506  -1538     23       N  
ATOM   1966  CA  LYS B 274      32.760  42.181  57.047  1.00 55.15           C  
ANISOU 1966  CA  LYS B 274     6599   5830   8528   1535  -1534    -96       C  
ATOM   1967  C   LYS B 274      32.751  43.017  55.772  1.00 54.66           C  
ANISOU 1967  C   LYS B 274     6523   5778   8468   1468  -1488   -273       C  
ATOM   1968  O   LYS B 274      32.968  42.499  54.669  1.00 57.85           O  
ANISOU 1968  O   LYS B 274     6897   6101   8984   1417  -1480   -379       O  
ATOM   1969  CB  LYS B 274      34.198  41.862  57.448  1.00 63.31           C  
ANISOU 1969  CB  LYS B 274     7603   6868   9584   1589  -1589   -162       C  
ATOM   1970  CG  LYS B 274      34.841  42.947  58.290  1.00 71.11           C  
ANISOU 1970  CG  LYS B 274     8597   7993  10430   1645  -1603   -196       C  
ATOM   1971  CD  LYS B 274      36.205  43.341  57.756  1.00 79.89           C  
ANISOU 1971  CD  LYS B 274     9669   9118  11568   1639  -1622   -390       C  
ATOM   1972  CE  LYS B 274      36.778  44.506  58.551  1.00 85.17           C  
ANISOU 1972  CE  LYS B 274    10342   9916  12102   1684  -1638   -435       C  
ATOM   1973  NZ  LYS B 274      38.122  44.919  58.060  1.00 88.36           N  
ANISOU 1973  NZ  LYS B 274    10700  10333  12538   1674  -1657   -616       N  
ATOM   1974  N   PHE B 275      32.507  44.317  55.931  1.00 45.74           N  
ANISOU 1974  N   PHE B 275     5412   4757   7210   1471  -1458   -306       N  
ATOM   1975  CA  PHE B 275      32.405  45.241  54.800  1.00 46.40           C  
ANISOU 1975  CA  PHE B 275     5486   4865   7280   1409  -1407   -452       C  
ATOM   1976  C   PHE B 275      33.583  46.204  54.705  1.00 49.61           C  
ANISOU 1976  C   PHE B 275     5866   5349   7635   1419  -1413   -600       C  
ATOM   1977  O   PHE B 275      34.064  46.728  55.712  1.00 48.08           O  
ANISOU 1977  O   PHE B 275     5681   5233   7353   1475  -1446   -580       O  
ATOM   1978  CB  PHE B 275      31.110  46.056  54.887  1.00 45.27           C  
ANISOU 1978  CB  PHE B 275     5382   4776   7043   1392  -1363   -381       C  
ATOM   1979  CG  PHE B 275      29.860  45.229  54.903  1.00 44.56           C  
ANISOU 1979  CG  PHE B 275     5313   4615   7004   1371  -1352   -234       C  
ATOM   1980  CD1 PHE B 275      29.331  44.776  56.098  1.00 49.24           C  
ANISOU 1980  CD1 PHE B 275     5931   5226   7553   1421  -1376    -46       C  
ATOM   1981  CD2 PHE B 275      29.200  44.918  53.722  1.00 52.52           C  
ANISOU 1981  CD2 PHE B 275     6310   5543   8101   1299  -1314   -281       C  
ATOM   1982  CE1 PHE B 275      28.174  44.017  56.120  1.00 57.35           C  
ANISOU 1982  CE1 PHE B 275     6969   6186   8635   1392  -1363    103       C  
ATOM   1983  CE2 PHE B 275      28.040  44.161  53.737  1.00 56.96           C  
ANISOU 1983  CE2 PHE B 275     6885   6033   8722   1271  -1307   -147       C  
ATOM   1984  CZ  PHE B 275      27.528  43.710  54.940  1.00 58.17           C  
ANISOU 1984  CZ  PHE B 275     7062   6199   8842   1314  -1331     49       C  
ATOM   1985  N   ASN B 276      34.039  46.442  53.482  1.00 50.14           N  
ANISOU 1985  N   ASN B 276     5895   5401   7755   1362  -1381   -748       N  
ATOM   1986  CA  ASN B 276      34.992  47.509  53.219  1.00 51.30           C  
ANISOU 1986  CA  ASN B 276     6010   5623   7857   1352  -1372   -882       C  
ATOM   1987  C   ASN B 276      34.472  48.416  52.114  1.00 46.60           C  
ANISOU 1987  C   ASN B 276     5408   5058   7239   1283  -1302   -960       C  
ATOM   1988  O   ASN B 276      34.138  47.949  51.025  1.00 42.90           O  
ANISOU 1988  O   ASN B 276     4922   4542   6837   1232  -1265  -1000       O  
ATOM   1989  CB  ASN B 276      36.360  46.940  52.840  1.00 60.13           C  
ANISOU 1989  CB  ASN B 276     7073   6716   9058   1355  -1404   -986       C  
ATOM   1990  CG  ASN B 276      37.093  46.362  54.032  1.00 56.21           C  
ANISOU 1990  CG  ASN B 276     6580   6215   8564   1430  -1475   -928       C  
ATOM   1991  OD1 ASN B 276      36.819  45.240  54.460  1.00 60.19           O  
ANISOU 1991  OD1 ASN B 276     7100   6650   9121   1459  -1506   -826       O  
ATOM   1992  ND2 ASN B 276      38.034  47.125  54.575  1.00 42.54           N  
ANISOU 1992  ND2 ASN B 276     4831   4556   6778   1459  -1503   -989       N  
ATOM   1993  N   TRP B 277      34.399  49.711  52.404  1.00 41.66           N  
ANISOU 1993  N   TRP B 277     4795   4515   6520   1284  -1287   -982       N  
ATOM   1994  CA  TRP B 277      33.831  50.681  51.472  1.00 39.07           C  
ANISOU 1994  CA  TRP B 277     4465   4220   6161   1223  -1219  -1038       C  
ATOM   1995  C   TRP B 277      34.890  51.554  50.826  1.00 42.82           C  
ANISOU 1995  C   TRP B 277     4884   4743   6644   1187  -1201  -1170       C  
ATOM   1996  O   TRP B 277      35.843  51.976  51.479  1.00 50.54           O  
ANISOU 1996  O   TRP B 277     5841   5757   7605   1218  -1245  -1207       O  
ATOM   1997  CB  TRP B 277      32.806  51.566  52.185  1.00 40.69           C  
ANISOU 1997  CB  TRP B 277     4725   4478   6259   1245  -1211   -960       C  
ATOM   1998  CG  TRP B 277      31.557  50.845  52.552  1.00 41.80           C  
ANISOU 1998  CG  TRP B 277     4912   4580   6391   1263  -1210   -824       C  
ATOM   1999  CD1 TRP B 277      31.322  50.145  53.698  1.00 37.15           C  
ANISOU 1999  CD1 TRP B 277     4352   3983   5779   1324  -1258   -698       C  
ATOM   2000  CD2 TRP B 277      30.363  50.743  51.765  1.00 44.04           C  
ANISOU 2000  CD2 TRP B 277     5214   4828   6689   1216  -1157   -793       C  
ATOM   2001  NE1 TRP B 277      30.052  49.620  53.679  1.00 41.01           N  
ANISOU 2001  NE1 TRP B 277     4872   4434   6274   1315  -1239   -581       N  
ATOM   2002  CE2 TRP B 277      29.444  49.972  52.503  1.00 40.51           C  
ANISOU 2002  CE2 TRP B 277     4808   4356   6230   1239  -1173   -640       C  
ATOM   2003  CE3 TRP B 277      29.982  51.230  50.509  1.00 40.17           C  
ANISOU 2003  CE3 TRP B 277     4714   4344   6205   1138  -1084   -867       C  
ATOM   2004  CZ2 TRP B 277      28.169  49.679  52.031  1.00 41.34           C  
ANISOU 2004  CZ2 TRP B 277     4940   4434   6333   1180  -1119   -566       C  
ATOM   2005  CZ3 TRP B 277      28.712  50.937  50.043  1.00 35.15           C  
ANISOU 2005  CZ3 TRP B 277     4110   3686   5558   1085  -1034   -799       C  
ATOM   2006  CH2 TRP B 277      27.823  50.168  50.802  1.00 33.04           C  
ANISOU 2006  CH2 TRP B 277     3880   3388   5287   1104  -1053   -653       C  
ATOM   2007  N   TYR B 278      34.711  51.831  49.540  1.00 39.29           N  
ANISOU 2007  N   TYR B 278     4407   4300   6220   1121  -1135  -1235       N  
ATOM   2008  CA  TYR B 278      35.663  52.649  48.806  1.00 36.87           C  
ANISOU 2008  CA  TYR B 278     4037   4044   5928   1081  -1108  -1343       C  
ATOM   2009  C   TYR B 278      34.953  53.678  47.942  1.00 40.06           C  
ANISOU 2009  C   TYR B 278     4444   4487   6292   1022  -1032  -1361       C  
ATOM   2010  O   TYR B 278      33.976  53.363  47.262  1.00 47.31           O  
ANISOU 2010  O   TYR B 278     5385   5385   7205    992   -984  -1334       O  
ATOM   2011  CB  TYR B 278      36.569  51.772  47.938  1.00 39.43           C  
ANISOU 2011  CB  TYR B 278     4296   4350   6335   1064  -1105  -1419       C  
ATOM   2012  CG  TYR B 278      37.252  50.658  48.696  1.00 40.59           C  
ANISOU 2012  CG  TYR B 278     4441   4449   6532   1121  -1178  -1403       C  
ATOM   2013  CD1 TYR B 278      36.636  49.422  48.862  1.00 45.18           C  
ANISOU 2013  CD1 TYR B 278     5056   4955   7153   1143  -1200  -1335       C  
ATOM   2014  CD2 TYR B 278      38.513  50.841  49.248  1.00 50.27           C  
ANISOU 2014  CD2 TYR B 278     5628   5700   7773   1152  -1228  -1453       C  
ATOM   2015  CE1 TYR B 278      37.258  48.403  49.558  1.00 53.58           C  
ANISOU 2015  CE1 TYR B 278     6117   5970   8269   1195  -1267  -1311       C  
ATOM   2016  CE2 TYR B 278      39.140  49.826  49.943  1.00 52.67           C  
ANISOU 2016  CE2 TYR B 278     5931   5961   8120   1206  -1295  -1436       C  
ATOM   2017  CZ  TYR B 278      38.509  48.612  50.096  1.00 53.67           C  
ANISOU 2017  CZ  TYR B 278     6094   6013   8285   1228  -1313  -1361       C  
ATOM   2018  OH  TYR B 278      39.135  47.603  50.789  1.00 57.54           O  
ANISOU 2018  OH  TYR B 278     6582   6457   8824   1283  -1379  -1336       O  
ATOM   2019  N   VAL B 279      35.445  54.911  47.985  1.00 37.05           N  
ANISOU 2019  N   VAL B 279     4035   4155   5886   1005  -1025  -1406       N  
ATOM   2020  CA  VAL B 279      34.950  55.976  47.124  1.00 38.80           C  
ANISOU 2020  CA  VAL B 279     4249   4413   6081    947   -953  -1427       C  
ATOM   2021  C   VAL B 279      36.050  56.360  46.146  1.00 49.55           C  
ANISOU 2021  C   VAL B 279     5518   5810   7498    905   -919  -1519       C  
ATOM   2022  O   VAL B 279      37.065  56.938  46.541  1.00 57.76           O  
ANISOU 2022  O   VAL B 279     6511   6869   8567    914   -954  -1565       O  
ATOM   2023  CB  VAL B 279      34.508  57.213  47.930  1.00 37.56           C  
ANISOU 2023  CB  VAL B 279     4132   4280   5861    959   -970  -1399       C  
ATOM   2024  CG1 VAL B 279      34.000  58.301  46.995  1.00 32.20           C  
ANISOU 2024  CG1 VAL B 279     3444   3626   5164    896   -896  -1418       C  
ATOM   2025  CG2 VAL B 279      33.440  56.835  48.944  1.00 35.33           C  
ANISOU 2025  CG2 VAL B 279     3932   3979   5513   1013  -1003  -1306       C  
ATOM   2026  N   ASP B 280      35.844  56.026  44.873  1.00 46.93           N  
ANISOU 2026  N   ASP B 280     5156   5493   7182    863   -851  -1546       N  
ATOM   2027  CA  ASP B 280      36.870  56.179  43.842  1.00 47.07           C  
ANISOU 2027  CA  ASP B 280     5079   5557   7250    833   -812  -1630       C  
ATOM   2028  C   ASP B 280      38.186  55.520  44.257  1.00 47.24           C  
ANISOU 2028  C   ASP B 280     5047   5570   7332    870   -874  -1680       C  
ATOM   2029  O   ASP B 280      39.258  56.091  44.068  1.00 51.43           O  
ANISOU 2029  O   ASP B 280     5501   6136   7904    860   -872  -1742       O  
ATOM   2030  CB  ASP B 280      37.103  57.657  43.511  1.00 44.49           C  
ANISOU 2030  CB  ASP B 280     4709   5272   6923    795   -770  -1655       C  
ATOM   2031  CG  ASP B 280      36.132  58.179  42.470  1.00 47.10           C  
ANISOU 2031  CG  ASP B 280     5052   5632   7212    748   -681  -1639       C  
ATOM   2032  OD1 ASP B 280      35.536  57.356  41.745  1.00 46.87           O  
ANISOU 2032  OD1 ASP B 280     5039   5608   7160    740   -646  -1634       O  
ATOM   2033  OD2 ASP B 280      35.970  59.413  42.373  1.00 50.21           O  
ANISOU 2033  OD2 ASP B 280     5445   6051   7583    702   -650  -1614       O  
ATOM   2034  N   GLY B 281      38.094  54.323  44.830  1.00 43.41           N  
ANISOU 2034  N   GLY B 281     4600   5034   6858    912   -928  -1652       N  
ATOM   2035  CA  GLY B 281      39.272  53.555  45.192  1.00 38.86           C  
ANISOU 2035  CA  GLY B 281     3982   4445   6340    950   -988  -1698       C  
ATOM   2036  C   GLY B 281      39.830  53.836  46.575  1.00 47.39           C  
ANISOU 2036  C   GLY B 281     5080   5509   7416    996  -1067  -1679       C  
ATOM   2037  O   GLY B 281      40.610  53.045  47.105  1.00 58.11           O  
ANISOU 2037  O   GLY B 281     6425   6842   8811   1039  -1127  -1697       O  
ATOM   2038  N   VAL B 282      39.444  54.962  47.162  1.00 50.89           N  
ANISOU 2038  N   VAL B 282     5553   5969   7813    991  -1071  -1650       N  
ATOM   2039  CA  VAL B 282      39.923  55.326  48.491  1.00 51.87           C  
ANISOU 2039  CA  VAL B 282     5696   6091   7921   1038  -1150  -1641       C  
ATOM   2040  C   VAL B 282      38.972  54.824  49.567  1.00 53.77           C  
ANISOU 2040  C   VAL B 282     6030   6300   8100   1091  -1191  -1545       C  
ATOM   2041  O   VAL B 282      37.771  55.072  49.504  1.00 58.18           O  
ANISOU 2041  O   VAL B 282     6645   6855   8607   1079  -1155  -1484       O  
ATOM   2042  CB  VAL B 282      40.084  56.846  48.632  1.00 50.91           C  
ANISOU 2042  CB  VAL B 282     5550   6004   7788   1011  -1145  -1671       C  
ATOM   2043  CG1 VAL B 282      40.604  57.195  50.016  1.00 49.59           C  
ANISOU 2043  CG1 VAL B 282     5400   5841   7601   1065  -1236  -1677       C  
ATOM   2044  CG2 VAL B 282      41.016  57.371  47.561  1.00 46.59           C  
ANISOU 2044  CG2 VAL B 282     4901   5488   7314    959  -1099  -1754       C  
ATOM   2045  N   GLU B 283      39.509  54.123  50.560  1.00 48.20           N  
ANISOU 2045  N   GLU B 283     5338   5576   7399   1153  -1264  -1528       N  
ATOM   2046  CA  GLU B 283      38.673  53.537  51.603  1.00 47.66           C  
ANISOU 2046  CA  GLU B 283     5349   5484   7275   1211  -1301  -1424       C  
ATOM   2047  C   GLU B 283      38.097  54.595  52.543  1.00 54.48           C  
ANISOU 2047  C   GLU B 283     6260   6392   8047   1237  -1322  -1387       C  
ATOM   2048  O   GLU B 283      38.791  55.523  52.958  1.00 56.22           O  
ANISOU 2048  O   GLU B 283     6454   6651   8256   1242  -1356  -1449       O  
ATOM   2049  CB  GLU B 283      39.459  52.498  52.408  1.00 44.57           C  
ANISOU 2049  CB  GLU B 283     4954   5066   6913   1274  -1371  -1410       C  
ATOM   2050  CG  GLU B 283      38.616  51.736  53.427  1.00 46.64           C  
ANISOU 2050  CG  GLU B 283     5289   5304   7129   1335  -1404  -1282       C  
ATOM   2051  CD  GLU B 283      39.362  50.585  54.079  1.00 52.94           C  
ANISOU 2051  CD  GLU B 283     6079   6066   7970   1393  -1466  -1256       C  
ATOM   2052  OE1 GLU B 283      38.874  50.057  55.100  1.00 55.44           O  
ANISOU 2052  OE1 GLU B 283     6444   6376   8243   1452  -1501  -1145       O  
ATOM   2053  OE2 GLU B 283      40.438  50.207  53.569  1.00 61.20           O  
ANISOU 2053  OE2 GLU B 283     7067   7095   9092   1381  -1478  -1343       O  
ATOM   2054  N   VAL B 284      36.814  54.444  52.865  1.00 52.28           N  
ANISOU 2054  N   VAL B 284     6049   6108   7706   1254  -1305  -1290       N  
ATOM   2055  CA  VAL B 284      36.147  55.295  53.845  1.00 44.39           C  
ANISOU 2055  CA  VAL B 284     5102   5161   6605   1292  -1328  -1244       C  
ATOM   2056  C   VAL B 284      35.612  54.427  54.985  1.00 43.44           C  
ANISOU 2056  C   VAL B 284     5036   5044   6426   1368  -1369  -1126       C  
ATOM   2057  O   VAL B 284      35.490  53.210  54.834  1.00 46.48           O  
ANISOU 2057  O   VAL B 284     5425   5373   6862   1376  -1367  -1066       O  
ATOM   2058  CB  VAL B 284      35.004  56.107  53.207  1.00 43.67           C  
ANISOU 2058  CB  VAL B 284     5036   5080   6475   1246  -1264  -1229       C  
ATOM   2059  CG1 VAL B 284      35.543  56.997  52.093  1.00 35.79           C  
ANISOU 2059  CG1 VAL B 284     3979   4084   5535   1171  -1219  -1330       C  
ATOM   2060  CG2 VAL B 284      33.925  55.176  52.677  1.00 41.65           C  
ANISOU 2060  CG2 VAL B 284     4815   4779   6232   1231  -1217  -1145       C  
ATOM   2061  N   HIS B 285      35.290  55.043  56.120  1.00 39.62           N  
ANISOU 2061  N   HIS B 285     4590   4627   5835   1423  -1405  -1088       N  
ATOM   2062  CA  HIS B 285      35.038  54.267  57.334  1.00 43.11           C  
ANISOU 2062  CA  HIS B 285     5071   5096   6212   1502  -1448   -975       C  
ATOM   2063  C   HIS B 285      33.731  54.581  58.066  1.00 49.42           C  
ANISOU 2063  C   HIS B 285     5931   5960   6888   1539  -1435   -865       C  
ATOM   2064  O   HIS B 285      33.501  54.064  59.162  1.00 52.10           O  
ANISOU 2064  O   HIS B 285     6298   6344   7153   1607  -1466   -761       O  
ATOM   2065  CB  HIS B 285      36.202  54.464  58.311  1.00 42.32           C  
ANISOU 2065  CB  HIS B 285     4952   5041   6087   1559  -1519  -1029       C  
ATOM   2066  CG  HIS B 285      37.533  54.076  57.752  1.00 48.26           C  
ANISOU 2066  CG  HIS B 285     5643   5742   6953   1534  -1539  -1126       C  
ATOM   2067  ND1 HIS B 285      38.064  52.814  57.907  1.00 51.18           N  
ANISOU 2067  ND1 HIS B 285     5999   6064   7381   1563  -1565  -1083       N  
ATOM   2068  CD2 HIS B 285      38.442  54.784  57.041  1.00 49.30           C  
ANISOU 2068  CD2 HIS B 285     5718   5864   7150   1482  -1537  -1258       C  
ATOM   2069  CE1 HIS B 285      39.242  52.761  57.312  1.00 56.36           C  
ANISOU 2069  CE1 HIS B 285     6596   6690   8128   1533  -1577  -1194       C  
ATOM   2070  NE2 HIS B 285      39.495  53.943  56.779  1.00 58.80           N  
ANISOU 2070  NE2 HIS B 285     6875   7024   8442   1483  -1559  -1297       N  
ATOM   2071  N   ASN B 286      32.880  55.415  57.474  1.00 46.55           N  
ANISOU 2071  N   ASN B 286     5584   5608   6496   1497  -1388   -883       N  
ATOM   2072  CA  ASN B 286      31.679  55.882  58.166  1.00 43.82           C  
ANISOU 2072  CA  ASN B 286     5291   5339   6022   1532  -1376   -797       C  
ATOM   2073  C   ASN B 286      30.464  54.982  57.997  1.00 45.27           C  
ANISOU 2073  C   ASN B 286     5505   5495   6200   1528  -1336   -653       C  
ATOM   2074  O   ASN B 286      29.366  55.335  58.422  1.00 50.77           O  
ANISOU 2074  O   ASN B 286     6242   6257   6793   1548  -1315   -574       O  
ATOM   2075  CB  ASN B 286      31.325  57.295  57.704  1.00 47.33           C  
ANISOU 2075  CB  ASN B 286     5737   5811   6433   1495  -1351   -885       C  
ATOM   2076  CG  ASN B 286      31.292  57.424  56.194  1.00 53.96           C  
ANISOU 2076  CG  ASN B 286     6547   6572   7382   1408  -1294   -946       C  
ATOM   2077  OD1 ASN B 286      32.198  56.963  55.504  1.00 54.69           O  
ANISOU 2077  OD1 ASN B 286     6593   6604   7582   1370  -1291  -1006       O  
ATOM   2078  ND2 ASN B 286      30.242  58.051  55.674  1.00 55.22           N  
ANISOU 2078  ND2 ASN B 286     6735   6744   7501   1362  -1235   -927       N  
ATOM   2079  N   ALA B 287      30.654  53.822  57.379  1.00 40.90           N  
ANISOU 2079  N   ALA B 287     4931   4846   5761   1501  -1327   -622       N  
ATOM   2080  CA  ALA B 287      29.538  52.920  57.119  1.00 41.71           C  
ANISOU 2080  CA  ALA B 287     5057   4901   5889   1487  -1296   -493       C  
ATOM   2081  C   ALA B 287      29.017  52.276  58.398  1.00 44.61           C  
ANISOU 2081  C   ALA B 287     5453   5323   6172   1556  -1321   -326       C  
ATOM   2082  O   ALA B 287      29.785  51.968  59.310  1.00 46.22           O  
ANISOU 2082  O   ALA B 287     5649   5561   6351   1611  -1367   -306       O  
ATOM   2083  CB  ALA B 287      29.946  51.854  56.134  1.00 32.78           C  
ANISOU 2083  CB  ALA B 287     3893   3648   4915   1439  -1286   -520       C  
ATOM   2084  N   LYS B 288      27.705  52.074  58.452  1.00 47.22           N  
ANISOU 2084  N   LYS B 288     5816   5669   6456   1544  -1280   -201       N  
ATOM   2085  CA  LYS B 288      27.065  51.427  59.591  1.00 46.22           C  
ANISOU 2085  CA  LYS B 288     5710   5599   6251   1607  -1296    -18       C  
ATOM   2086  C   LYS B 288      26.398  50.121  59.158  1.00 46.35           C  
ANISOU 2086  C   LYS B 288     5722   5507   6380   1557  -1270    112       C  
ATOM   2087  O   LYS B 288      25.821  50.035  58.072  1.00 50.32           O  
ANISOU 2087  O   LYS B 288     6226   5937   6955   1463  -1211     82       O  
ATOM   2088  CB  LYS B 288      26.046  52.370  60.230  1.00 50.39           C  
ANISOU 2088  CB  LYS B 288     6273   6266   6607   1633  -1263     34       C  
ATOM   2089  CG  LYS B 288      26.617  53.721  60.619  1.00 51.36           C  
ANISOU 2089  CG  LYS B 288     6399   6485   6629   1659  -1279   -106       C  
ATOM   2090  CD  LYS B 288      27.689  53.578  61.685  1.00 54.36           C  
ANISOU 2090  CD  LYS B 288     6765   6917   6973   1723  -1335   -119       C  
ATOM   2091  CE  LYS B 288      28.475  54.869  61.852  1.00 53.46           C  
ANISOU 2091  CE  LYS B 288     6646   6858   6810   1735  -1363   -293       C  
ATOM   2092  NZ  LYS B 288      29.540  54.745  62.886  1.00 55.43           N  
ANISOU 2092  NZ  LYS B 288     6879   7157   7024   1800  -1422   -317       N  
ATOM   2093  N   THR B 289      26.486  49.103  60.007  1.00 49.29           N  
ANISOU 2093  N   THR B 289     6088   5868   6771   1615  -1313    258       N  
ATOM   2094  CA  THR B 289      26.010  47.771  59.651  1.00 54.75           C  
ANISOU 2094  CA  THR B 289     6767   6433   7602   1574  -1307    381       C  
ATOM   2095  C   THR B 289      24.791  47.383  60.473  1.00 58.36           C  
ANISOU 2095  C   THR B 289     7241   6953   7979   1587  -1277    602       C  
ATOM   2096  O   THR B 289      24.783  47.533  61.695  1.00 60.96           O  
ANISOU 2096  O   THR B 289     7578   7407   8175   1671  -1298    705       O  
ATOM   2097  CB  THR B 289      27.115  46.708  59.850  1.00 54.10           C  
ANISOU 2097  CB  THR B 289     6654   6264   7639   1599  -1360    386       C  
ATOM   2098  OG1 THR B 289      28.152  46.898  58.878  1.00 53.69           O  
ANISOU 2098  OG1 THR B 289     6577   6142   7682   1563  -1370    186       O  
ATOM   2099  CG2 THR B 289      26.543  45.307  59.691  1.00 55.05           C  
ANISOU 2099  CG2 THR B 289     6761   6258   7898   1565  -1360    537       C  
ATOM   2100  N   LYS B 290      23.759  46.892  59.795  1.00 65.50           N  
ANISOU 2100  N   LYS B 290     8145   7781   8960   1498  -1222    673       N  
ATOM   2101  CA  LYS B 290      22.546  46.433  60.462  1.00 78.96           C  
ANISOU 2101  CA  LYS B 290     9855   9533  10615   1496  -1187    894       C  
ATOM   2102  C   LYS B 290      22.743  45.038  61.049  1.00 90.56           C  
ANISOU 2102  C   LYS B 290    11297  10913  12197   1530  -1240   1069       C  
ATOM   2103  O   LYS B 290      23.448  44.212  60.467  1.00 87.76           O  
ANISOU 2103  O   LYS B 290    10920  10405  12019   1510  -1285   1012       O  
ATOM   2104  CB  LYS B 290      21.364  46.429  59.490  1.00 76.63           C  
ANISOU 2104  CB  LYS B 290     9561   9183  10372   1384  -1112    900       C  
ATOM   2105  CG  LYS B 290      20.473  47.658  59.589  1.00 77.77           C  
ANISOU 2105  CG  LYS B 290     9734   9476  10340   1373  -1045    881       C  
ATOM   2106  CD  LYS B 290      19.437  47.691  58.474  1.00 77.69           C  
ANISOU 2106  CD  LYS B 290     9722   9403  10393   1262   -977    857       C  
ATOM   2107  CE  LYS B 290      18.417  48.795  58.711  1.00 74.61           C  
ANISOU 2107  CE  LYS B 290     9358   9163   9829   1259   -912    873       C  
ATOM   2108  NZ  LYS B 290      17.417  48.875  57.612  1.00 74.10           N  
ANISOU 2108  NZ  LYS B 290     9291   9045   9821   1155   -849    844       N  
ATOM   2109  N   PRO B 291      22.121  44.774  62.209  1.00 97.65           N  
ANISOU 2109  N   PRO B 291    12195  11914  12993   1585  -1234   1285       N  
ATOM   2110  CA  PRO B 291      22.203  43.448  62.834  1.00101.85           C  
ANISOU 2110  CA  PRO B 291    12719  12386  13594   1597  -1248   1443       C  
ATOM   2111  C   PRO B 291      21.620  42.353  61.942  1.00105.50           C  
ANISOU 2111  C   PRO B 291    13158  12662  14266   1484  -1225   1491       C  
ATOM   2112  O   PRO B 291      20.523  42.529  61.404  1.00108.82           O  
ANISOU 2112  O   PRO B 291    13573  13069  14705   1407  -1172   1527       O  
ATOM   2113  CB  PRO B 291      21.378  43.611  64.116  1.00100.11           C  
ANISOU 2113  CB  PRO B 291    12522  12332  13184   1632  -1219   1609       C  
ATOM   2114  CG  PRO B 291      20.497  44.792  63.863  1.00 94.97           C  
ANISOU 2114  CG  PRO B 291    11879  11797  12409   1604  -1158   1568       C  
ATOM   2115  CD  PRO B 291      21.289  45.706  62.990  1.00 94.66           C  
ANISOU 2115  CD  PRO B 291    11837  11736  12393   1624  -1183   1355       C  
ATOM   2116  N   ARG B 292      22.348  41.250  61.793  1.00101.50           N  
ANISOU 2116  N   ARG B 292    12634  12016  13914   1478  -1267   1484       N  
ATOM   2117  CA  ARG B 292      21.936  40.141  60.929  1.00101.73           C  
ANISOU 2117  CA  ARG B 292    12636  11855  14161   1377  -1263   1502       C  
ATOM   2118  C   ARG B 292      20.479  39.731  61.154  1.00102.61           C  
ANISOU 2118  C   ARG B 292    12738  11973  14275   1307  -1206   1692       C  
ATOM   2119  O   ARG B 292      20.020  39.654  62.294  1.00106.27           O  
ANISOU 2119  O   ARG B 292    13213  12554  14612   1344  -1183   1865       O  
ATOM   2120  CB  ARG B 292      22.842  38.925  61.157  1.00105.76           C  
ANISOU 2120  CB  ARG B 292    13130  12249  14803   1399  -1319   1521       C  
ATOM   2121  CG  ARG B 292      24.229  39.232  61.704  1.00108.38           C  
ANISOU 2121  CG  ARG B 292    13472  12649  15059   1504  -1370   1434       C  
ATOM   2122  CD  ARG B 292      24.769  38.007  62.437  1.00110.30           C  
ANISOU 2122  CD  ARG B 292    13706  12830  15374   1544  -1413   1551       C  
ATOM   2123  NE  ARG B 292      26.151  38.160  62.883  1.00109.10           N  
ANISOU 2123  NE  ARG B 292    13554  12725  15176   1640  -1465   1463       N  
ATOM   2124  CZ  ARG B 292      26.760  37.323  63.721  1.00106.24           C  
ANISOU 2124  CZ  ARG B 292    13189  12351  14827   1705  -1507   1562       C  
ATOM   2125  NH1 ARG B 292      26.111  36.272  64.209  1.00106.79           N  
ANISOU 2125  NH1 ARG B 292    13258  12358  14958   1680  -1505   1752       N  
ATOM   2126  NH2 ARG B 292      28.022  37.530  64.067  1.00 99.22           N  
ANISOU 2126  NH2 ARG B 292    12293  11511  13896   1789  -1551   1472       N  
ATOM   2127  N   GLU B 293      19.753  39.472  60.071  1.00 97.64           N  
ANISOU 2127  N   GLU B 293    12086  11223  13788   1205  -1184   1652       N  
ATOM   2128  CA  GLU B 293      18.346  39.100  60.191  1.00 95.08           C  
ANISOU 2128  CA  GLU B 293    11743  10901  13483   1129  -1128   1821       C  
ATOM   2129  C   GLU B 293      18.055  37.763  59.504  1.00 92.32           C  
ANISOU 2129  C   GLU B 293    11350  10345  13382   1036  -1150   1844       C  
ATOM   2130  O   GLU B 293      18.562  37.478  58.416  1.00 90.72           O  
ANISOU 2130  O   GLU B 293    11134  10003  13334   1002  -1190   1672       O  
ATOM   2131  CB  GLU B 293      17.444  40.207  59.630  1.00 91.36           C  
ANISOU 2131  CB  GLU B 293    11279  10512  12920   1092  -1071   1773       C  
ATOM   2132  CG  GLU B 293      17.395  40.296  58.108  1.00 92.04           C  
ANISOU 2132  CG  GLU B 293    11351  10460  13160   1020  -1082   1591       C  
ATOM   2133  CD  GLU B 293      16.760  41.586  57.616  1.00 90.33           C  
ANISOU 2133  CD  GLU B 293    11152  10349  12819   1005  -1030   1514       C  
ATOM   2134  OE1 GLU B 293      15.637  41.530  57.070  1.00 89.32           O  
ANISOU 2134  OE1 GLU B 293    11008  10199  12731    922   -982   1546       O  
ATOM   2135  OE2 GLU B 293      17.391  42.655  57.768  1.00 86.43           O  
ANISOU 2135  OE2 GLU B 293    10696   9981  12163   1060  -1020   1385       O  
ATOM   2136  N   GLU B 294      17.244  36.939  60.161  1.00 87.64           N  
ANISOU 2136  N   GLU B 294    10731   9743  12827    996  -1127   2050       N  
ATOM   2137  CA  GLU B 294      16.919  35.617  59.642  1.00 86.28           C  
ANISOU 2137  CA  GLU B 294    10507   9378  12897    907  -1156   2089       C  
ATOM   2138  C   GLU B 294      15.834  35.698  58.578  1.00 81.10           C  
ANISOU 2138  C   GLU B 294     9821   8652  12342    804  -1125   2043       C  
ATOM   2139  O   GLU B 294      14.877  36.463  58.707  1.00 71.69           O  
ANISOU 2139  O   GLU B 294     8635   7580  11025    785  -1060   2109       O  
ATOM   2140  CB  GLU B 294      16.484  34.685  60.776  1.00 92.60           C  
ANISOU 2140  CB  GLU B 294    11281  10193  13712    901  -1146   2334       C  
ATOM   2141  CG  GLU B 294      16.279  33.239  60.336  1.00 98.35           C  
ANISOU 2141  CG  GLU B 294    11948  10713  14706    817  -1190   2377       C  
ATOM   2142  CD  GLU B 294      15.799  32.341  61.461  1.00106.07           C  
ANISOU 2142  CD  GLU B 294    12891  11707  15705    805  -1177   2631       C  
ATOM   2143  OE1 GLU B 294      15.247  31.260  61.162  1.00108.10           O  
ANISOU 2143  OE1 GLU B 294    13085  11816  16172    719  -1198   2705       O  
ATOM   2144  OE2 GLU B 294      15.979  32.713  62.642  1.00108.12           O  
ANISOU 2144  OE2 GLU B 294    13179  12129  15771    884  -1150   2752       O  
ATOM   2145  N   GLN B 295      15.986  34.898  57.529  1.00 86.03           N  
ANISOU 2145  N   GLN B 295    10411   9090  13188    741  -1175   1922       N  
ATOM   2146  CA  GLN B 295      15.063  34.937  56.404  1.00 89.69           C  
ANISOU 2146  CA  GLN B 295    10844   9476  13758    649  -1159   1843       C  
ATOM   2147  C   GLN B 295      14.074  33.776  56.373  1.00102.31           C  
ANISOU 2147  C   GLN B 295    12374  10959  15540    554  -1165   1980       C  
ATOM   2148  O   GLN B 295      14.167  32.820  57.149  1.00103.49           O  
ANISOU 2148  O   GLN B 295    12496  11065  15762    553  -1188   2131       O  
ATOM   2149  CB  GLN B 295      15.839  34.958  55.083  1.00 83.71           C  
ANISOU 2149  CB  GLN B 295    10089   8607  13112    645  -1211   1573       C  
ATOM   2150  CG  GLN B 295      16.662  36.214  54.857  1.00 78.49           C  
ANISOU 2150  CG  GLN B 295     9481   8054  12288    720  -1199   1412       C  
ATOM   2151  CD  GLN B 295      15.816  37.471  54.834  1.00 76.46           C  
ANISOU 2151  CD  GLN B 295     9249   7935  11866    716  -1130   1438       C  
ATOM   2152  OE1 GLN B 295      15.227  37.820  53.812  1.00 75.46           O  
ANISOU 2152  OE1 GLN B 295     9113   7775  11783    663  -1113   1331       O  
ATOM   2153  NE2 GLN B 295      15.755  38.162  55.965  1.00 79.91           N  
ANISOU 2153  NE2 GLN B 295     9718   8538  12107    778  -1092   1574       N  
ATOM   2154  N   TYR B 296      13.115  33.916  55.464  1.00115.04           N  
ANISOU 2154  N   TYR B 296    13958  12527  17224    475  -1145   1925       N  
ATOM   2155  CA  TYR B 296      12.206  32.866  55.017  1.00121.88           C  
ANISOU 2155  CA  TYR B 296    14749  13256  18303    374  -1167   1978       C  
ATOM   2156  C   TYR B 296      12.866  31.485  54.961  1.00113.89           C  
ANISOU 2156  C   TYR B 296    13694  12075  17503    363  -1253   1960       C  
ATOM   2157  O   TYR B 296      12.518  30.581  55.721  1.00116.36           O  
ANISOU 2157  O   TYR B 296    13961  12349  17901    335  -1262   2150       O  
ATOM   2158  CB  TYR B 296      11.686  33.249  53.628  1.00134.79           C  
ANISOU 2158  CB  TYR B 296    16372  14836  20005    318  -1169   1790       C  
ATOM   2159  CG  TYR B 296      10.399  32.600  53.167  1.00144.66           C  
ANISOU 2159  CG  TYR B 296    17548  16001  21415    213  -1169   1851       C  
ATOM   2160  CD1 TYR B 296       9.164  33.154  53.490  1.00145.98           C  
ANISOU 2160  CD1 TYR B 296    17702  16275  21488    172  -1093   1998       C  
ATOM   2161  CD2 TYR B 296      10.418  31.465  52.361  1.00149.45           C  
ANISOU 2161  CD2 TYR B 296    18092  16430  22263    160  -1248   1747       C  
ATOM   2162  CE1 TYR B 296       7.985  32.581  53.050  1.00147.21           C  
ANISOU 2162  CE1 TYR B 296    17783  16357  21792     76  -1094   2047       C  
ATOM   2163  CE2 TYR B 296       9.242  30.885  51.917  1.00150.92           C  
ANISOU 2163  CE2 TYR B 296    18202  16541  22599     68  -1255   1790       C  
ATOM   2164  CZ  TYR B 296       8.029  31.446  52.264  1.00148.69           C  
ANISOU 2164  CZ  TYR B 296    17907  16361  22226     24  -1178   1942       C  
ATOM   2165  OH  TYR B 296       6.859  30.869  51.822  1.00147.51           O  
ANISOU 2165  OH  TYR B 296    17676  16139  22231    -66  -1188   1983       O  
ATOM   2166  N   ASN B 297      13.841  31.356  54.066  1.00103.08           N  
ANISOU 2166  N   ASN B 297    12338  10618  16212    390  -1314   1728       N  
ATOM   2167  CA  ASN B 297      14.446  30.070  53.722  1.00 94.30           C  
ANISOU 2167  CA  ASN B 297    11177   9337  15315    376  -1404   1657       C  
ATOM   2168  C   ASN B 297      15.578  29.609  54.648  1.00 89.61           C  
ANISOU 2168  C   ASN B 297    10606   8740  14703    452  -1440   1726       C  
ATOM   2169  O   ASN B 297      16.539  28.993  54.181  1.00 88.74           O  
ANISOU 2169  O   ASN B 297    10485   8527  14706    477  -1512   1580       O  
ATOM   2170  CB  ASN B 297      14.965  30.143  52.282  1.00 92.43           C  
ANISOU 2170  CB  ASN B 297    10936   9027  15155    375  -1451   1362       C  
ATOM   2171  CG  ASN B 297      15.590  31.492  51.954  1.00 94.05           C  
ANISOU 2171  CG  ASN B 297    11212   9360  15163    438  -1409   1211       C  
ATOM   2172  OD1 ASN B 297      15.971  32.235  52.859  1.00 97.55           O  
ANISOU 2172  OD1 ASN B 297    11709   9926  15428    502  -1367   1305       O  
ATOM   2173  ND2 ASN B 297      15.701  31.815  50.668  1.00 89.73           N  
ANISOU 2173  ND2 ASN B 297    10660   8793  14641    425  -1421    975       N  
ATOM   2174  N   SER B 298      15.450  29.876  55.949  1.00 91.25           N  
ANISOU 2174  N   SER B 298    10841   9065  14766    490  -1391   1945       N  
ATOM   2175  CA  SER B 298      16.497  29.566  56.933  1.00 93.99           C  
ANISOU 2175  CA  SER B 298    11215   9435  15061    573  -1418   2021       C  
ATOM   2176  C   SER B 298      17.851  30.078  56.463  1.00100.48           C  
ANISOU 2176  C   SER B 298    12085  10271  15821    652  -1452   1797       C  
ATOM   2177  O   SER B 298      18.855  29.364  56.496  1.00101.47           O  
ANISOU 2177  O   SER B 298    12203  10310  16039    691  -1518   1738       O  
ATOM   2178  CB  SER B 298      16.564  28.063  57.218  1.00 92.21           C  
ANISOU 2178  CB  SER B 298    10928   9055  15054    539  -1484   2126       C  
ATOM   2179  OG  SER B 298      15.770  27.724  58.344  1.00 91.69           O  
ANISOU 2179  OG  SER B 298    10836   9044  14957    518  -1442   2402       O  
ATOM   2180  N   THR B 299      17.847  31.325  56.006  1.00103.92           N  
ANISOU 2180  N   THR B 299    12565  10817  16105    674  -1407   1673       N  
ATOM   2181  CA  THR B 299      19.039  32.012  55.537  1.00100.86           C  
ANISOU 2181  CA  THR B 299    12217  10469  15637    744  -1426   1460       C  
ATOM   2182  C   THR B 299      19.208  33.249  56.410  1.00 97.84           C  
ANISOU 2182  C   THR B 299    11893  10279  15002    821  -1370   1528       C  
ATOM   2183  O   THR B 299      18.309  33.600  57.173  1.00100.61           O  
ANISOU 2183  O   THR B 299    12253  10732  15243    812  -1314   1712       O  
ATOM   2184  CB  THR B 299      18.911  32.408  54.037  1.00 96.50           C  
ANISOU 2184  CB  THR B 299    11652   9871  15140    699  -1428   1220       C  
ATOM   2185  OG1 THR B 299      18.486  31.274  53.270  1.00 99.29           O  
ANISOU 2185  OG1 THR B 299    11943  10065  15719    623  -1478   1173       O  
ATOM   2186  CG2 THR B 299      20.226  32.914  53.473  1.00 96.65           C  
ANISOU 2186  CG2 THR B 299    11696   9919  15108    763  -1452    991       C  
ATOM   2187  N   TYR B 300      20.359  33.902  56.327  1.00 94.35           N  
ANISOU 2187  N   TYR B 300    11486   9897  14467    898  -1386   1379       N  
ATOM   2188  CA  TYR B 300      20.501  35.199  56.960  1.00 97.27           C  
ANISOU 2188  CA  TYR B 300    11904  10450  14605    968  -1341   1400       C  
ATOM   2189  C   TYR B 300      20.747  36.289  55.943  1.00 95.45           C  
ANISOU 2189  C   TYR B 300    11690  10261  14316    967  -1324   1181       C  
ATOM   2190  O   TYR B 300      21.225  36.040  54.835  1.00 94.23           O  
ANISOU 2190  O   TYR B 300    11515  10010  14278    939  -1353    987       O  
ATOM   2191  CB  TYR B 300      21.615  35.183  57.994  1.00101.26           C  
ANISOU 2191  CB  TYR B 300    12433  11024  15017   1070  -1373   1442       C  
ATOM   2192  CG  TYR B 300      21.255  34.343  59.174  1.00110.53           C  
ANISOU 2192  CG  TYR B 300    13598  12203  16194   1082  -1375   1685       C  
ATOM   2193  CD1 TYR B 300      20.519  34.870  60.225  1.00112.79           C  
ANISOU 2193  CD1 TYR B 300    13906  12646  16302   1109  -1321   1871       C  
ATOM   2194  CD2 TYR B 300      21.624  33.013  59.224  1.00119.42           C  
ANISOU 2194  CD2 TYR B 300    14692  13182  17501   1066  -1431   1727       C  
ATOM   2195  CE1 TYR B 300      20.178  34.094  61.303  1.00119.75           C  
ANISOU 2195  CE1 TYR B 300    14776  13544  17179   1119  -1317   2093       C  
ATOM   2196  CE2 TYR B 300      21.291  32.233  60.288  1.00126.28           C  
ANISOU 2196  CE2 TYR B 300    15549  14052  18378   1074  -1432   1954       C  
ATOM   2197  CZ  TYR B 300      20.572  32.772  61.324  1.00127.22           C  
ANISOU 2197  CZ  TYR B 300    15689  14334  18314   1099  -1373   2137       C  
ATOM   2198  OH  TYR B 300      20.251  31.969  62.383  1.00131.24           O  
ANISOU 2198  OH  TYR B 300    16181  14853  18829   1106  -1372   2363       O  
ATOM   2199  N   ARG B 301      20.406  37.502  56.349  1.00 89.30           N  
ANISOU 2199  N   ARG B 301    10945   9636  13348   1001  -1275   1215       N  
ATOM   2200  CA  ARG B 301      20.480  38.669  55.499  1.00 79.65           C  
ANISOU 2200  CA  ARG B 301     9740   8472  12053    999  -1251   1035       C  
ATOM   2201  C   ARG B 301      21.154  39.780  56.284  1.00 71.80           C  
ANISOU 2201  C   ARG B 301     8782   7639  10861   1092  -1246   1022       C  
ATOM   2202  O   ARG B 301      20.762  40.064  57.415  1.00 74.56           O  
ANISOU 2202  O   ARG B 301     9150   8108  11074   1135  -1225   1192       O  
ATOM   2203  CB  ARG B 301      19.077  39.078  55.051  1.00 83.14           C  
ANISOU 2203  CB  ARG B 301    10178   8931  12482    929  -1196   1089       C  
ATOM   2204  CG  ARG B 301      19.017  40.325  54.203  1.00 78.36           C  
ANISOU 2204  CG  ARG B 301     9590   8390  11792    926  -1166    921       C  
ATOM   2205  CD  ARG B 301      17.577  40.609  53.807  1.00 69.84           C  
ANISOU 2205  CD  ARG B 301     8510   7347  10680    842  -1096    976       C  
ATOM   2206  NE  ARG B 301      17.505  41.477  52.640  1.00 52.92           N  
ANISOU 2206  NE  ARG B 301     6382   5250   8477    799  -1050    767       N  
ATOM   2207  CZ  ARG B 301      17.523  42.802  52.707  1.00 54.18           C  
ANISOU 2207  CZ  ARG B 301     6581   5571   8435    816   -993    699       C  
ATOM   2208  NH1 ARG B 301      17.613  43.401  53.888  1.00 59.78           N  
ANISOU 2208  NH1 ARG B 301     7318   6412   8982    879   -979    808       N  
ATOM   2209  NH2 ARG B 301      17.452  43.525  51.597  1.00 53.86           N  
ANISOU 2209  NH2 ARG B 301     6548   5560   8356    774   -953    523       N  
ATOM   2210  N   VAL B 302      22.178  40.393  55.704  1.00 67.67           N  
ANISOU 2210  N   VAL B 302     8264   7130  10317   1123  -1265    815       N  
ATOM   2211  CA  VAL B 302      22.926  41.417  56.421  1.00 67.05           C  
ANISOU 2211  CA  VAL B 302     8212   7195  10068   1208  -1272    779       C  
ATOM   2212  C   VAL B 302      23.204  42.611  55.517  1.00 60.51           C  
ANISOU 2212  C   VAL B 302     7395   6420   9178   1197  -1249    571       C  
ATOM   2213  O   VAL B 302      23.552  42.459  54.342  1.00 57.53           O  
ANISOU 2213  O   VAL B 302     6995   5955   8907   1154  -1251    404       O  
ATOM   2214  CB  VAL B 302      24.245  40.847  57.004  1.00 65.85           C  
ANISOU 2214  CB  VAL B 302     8052   7027   9940   1274  -1326    758       C  
ATOM   2215  CG1 VAL B 302      25.184  40.388  55.897  1.00 68.99           C  
ANISOU 2215  CG1 VAL B 302     8422   7311  10479   1245  -1354    555       C  
ATOM   2216  CG2 VAL B 302      24.922  41.864  57.916  1.00 61.40           C  
ANISOU 2216  CG2 VAL B 302     7512   6623   9194   1366  -1337    742       C  
ATOM   2217  N   VAL B 303      23.034  43.805  56.078  1.00 52.92           N  
ANISOU 2217  N   VAL B 303     6468   5626   8015   1223  -1206    574       N  
ATOM   2218  CA  VAL B 303      23.040  45.034  55.293  1.00 46.54           C  
ANISOU 2218  CA  VAL B 303     5677   4897   7110   1185  -1151    403       C  
ATOM   2219  C   VAL B 303      24.025  46.074  55.825  1.00 46.19           C  
ANISOU 2219  C   VAL B 303     5647   4969   6933   1255  -1169    308       C  
ATOM   2220  O   VAL B 303      24.105  46.307  57.034  1.00 48.98           O  
ANISOU 2220  O   VAL B 303     6016   5419   7174   1329  -1191    410       O  
ATOM   2221  CB  VAL B 303      21.628  45.652  55.260  1.00 35.01           C  
ANISOU 2221  CB  VAL B 303     4242   3521   5541   1131  -1073    481       C  
ATOM   2222  CG1 VAL B 303      21.622  46.904  54.421  1.00 28.17           C  
ANISOU 2222  CG1 VAL B 303     3392   2725   4585   1092  -1020    314       C  
ATOM   2223  CG2 VAL B 303      20.619  44.651  54.721  1.00 32.07           C  
ANISOU 2223  CG2 VAL B 303     3847   3032   5306   1056  -1058    572       C  
ATOM   2224  N   SER B 304      24.775  46.696  54.921  1.00 40.61           N  
ANISOU 2224  N   SER B 304     4929   4257   6243   1233  -1160    113       N  
ATOM   2225  CA  SER B 304      25.671  47.790  55.290  1.00 43.67           C  
ANISOU 2225  CA  SER B 304     5324   4748   6522   1284  -1175      7       C  
ATOM   2226  C   SER B 304      25.288  49.068  54.544  1.00 45.98           C  
ANISOU 2226  C   SER B 304     5633   5112   6727   1227  -1107   -103       C  
ATOM   2227  O   SER B 304      25.066  49.047  53.332  1.00 39.13           O  
ANISOU 2227  O   SER B 304     4752   4189   5927   1153  -1065   -188       O  
ATOM   2228  CB  SER B 304      27.126  47.425  54.995  1.00 40.57           C  
ANISOU 2228  CB  SER B 304     4892   4289   6235   1320  -1235   -120       C  
ATOM   2229  OG  SER B 304      27.995  48.509  55.274  1.00 35.74           O  
ANISOU 2229  OG  SER B 304     4278   3769   5534   1360  -1249   -230       O  
ATOM   2230  N   VAL B 305      25.215  50.177  55.274  1.00 40.54           N  
ANISOU 2230  N   VAL B 305     4970   4546   5886   1265  -1100   -102       N  
ATOM   2231  CA  VAL B 305      24.771  51.444  54.703  1.00 33.48           C  
ANISOU 2231  CA  VAL B 305     4095   3720   4908   1216  -1041   -186       C  
ATOM   2232  C   VAL B 305      25.850  52.523  54.768  1.00 36.49           C  
ANISOU 2232  C   VAL B 305     4464   4154   5247   1247  -1067   -328       C  
ATOM   2233  O   VAL B 305      26.353  52.847  55.843  1.00 40.31           O  
ANISOU 2233  O   VAL B 305     4952   4705   5658   1327  -1120   -316       O  
ATOM   2234  CB  VAL B 305      23.508  51.963  55.416  1.00 41.44           C  
ANISOU 2234  CB  VAL B 305     5142   4828   5775   1226  -1003    -67       C  
ATOM   2235  CG1 VAL B 305      23.037  53.273  54.789  1.00 33.33           C  
ANISOU 2235  CG1 VAL B 305     4133   3860   4671   1177   -947   -157       C  
ATOM   2236  CG2 VAL B 305      22.407  50.907  55.374  1.00 36.15           C  
ANISOU 2236  CG2 VAL B 305     4475   4108   5154   1189   -976     85       C  
ATOM   2237  N   LEU B 306      26.199  53.078  53.610  1.00 34.91           N  
ANISOU 2237  N   LEU B 306     4243   3926   5094   1184  -1031   -460       N  
ATOM   2238  CA  LEU B 306      27.181  54.149  53.540  1.00 31.50           C  
ANISOU 2238  CA  LEU B 306     3791   3535   4642   1196  -1050   -591       C  
ATOM   2239  C   LEU B 306      26.525  55.484  53.178  1.00 37.27           C  
ANISOU 2239  C   LEU B 306     4546   4329   5287   1152   -996   -628       C  
ATOM   2240  O   LEU B 306      25.957  55.641  52.096  1.00 38.52           O  
ANISOU 2240  O   LEU B 306     4704   4464   5468   1075   -932   -649       O  
ATOM   2241  CB  LEU B 306      28.272  53.809  52.521  1.00 35.23           C  
ANISOU 2241  CB  LEU B 306     4209   3936   5241   1165  -1054   -712       C  
ATOM   2242  CG  LEU B 306      29.363  54.868  52.342  1.00 35.70           C  
ANISOU 2242  CG  LEU B 306     4231   4028   5303   1167  -1069   -843       C  
ATOM   2243  CD1 LEU B 306      30.299  54.892  53.545  1.00 33.66           C  
ANISOU 2243  CD1 LEU B 306     3961   3801   5029   1258  -1155   -853       C  
ATOM   2244  CD2 LEU B 306      30.139  54.680  51.042  1.00 27.23           C  
ANISOU 2244  CD2 LEU B 306     3102   2906   4340   1113  -1041   -955       C  
ATOM   2245  N   THR B 307      26.595  56.440  54.097  1.00 37.71           N  
ANISOU 2245  N   THR B 307     4618   4465   5244   1205  -1028   -637       N  
ATOM   2246  CA  THR B 307      26.116  57.785  53.828  1.00 32.40           C  
ANISOU 2246  CA  THR B 307     3964   3844   4504   1173   -992   -686       C  
ATOM   2247  C   THR B 307      27.071  58.469  52.861  1.00 40.23           C  
ANISOU 2247  C   THR B 307     4912   4799   5575   1120   -982   -819       C  
ATOM   2248  O   THR B 307      28.287  58.397  53.033  1.00 42.02           O  
ANISOU 2248  O   THR B 307     5096   5006   5862   1150  -1033   -892       O  
ATOM   2249  CB  THR B 307      25.987  58.609  55.119  1.00 39.23           C  
ANISOU 2249  CB  THR B 307     4854   4804   5249   1255  -1041   -676       C  
ATOM   2250  OG1 THR B 307      24.833  58.173  55.849  1.00 42.25           O  
ANISOU 2250  OG1 THR B 307     5276   5243   5535   1291  -1026   -541       O  
ATOM   2251  CG2 THR B 307      25.850  60.094  54.807  1.00 42.75           C  
ANISOU 2251  CG2 THR B 307     5304   5280   5659   1227  -1026   -763       C  
ATOM   2252  N   VAL B 308      26.524  59.119  51.836  1.00 37.66           N  
ANISOU 2252  N   VAL B 308     4590   4468   5251   1044   -916   -845       N  
ATOM   2253  CA  VAL B 308      27.346  59.750  50.809  1.00 39.51           C  
ANISOU 2253  CA  VAL B 308     4777   4675   5561    986   -893   -950       C  
ATOM   2254  C   VAL B 308      27.048  61.235  50.655  1.00 36.94           C  
ANISOU 2254  C   VAL B 308     4462   4384   5190    958   -875   -986       C  
ATOM   2255  O   VAL B 308      26.012  61.718  51.102  1.00 36.85           O  
ANISOU 2255  O   VAL B 308     4498   4413   5088    972   -864   -934       O  
ATOM   2256  CB  VAL B 308      27.137  59.063  49.451  1.00 41.12           C  
ANISOU 2256  CB  VAL B 308     4960   4834   5828    914   -827   -954       C  
ATOM   2257  CG1 VAL B 308      27.342  57.568  49.586  1.00 39.66           C  
ANISOU 2257  CG1 VAL B 308     4766   4601   5703    943   -852   -920       C  
ATOM   2258  CG2 VAL B 308      25.743  59.357  48.929  1.00 36.82           C  
ANISOU 2258  CG2 VAL B 308     4458   4310   5221    865   -761   -894       C  
ATOM   2259  N   LEU B 309      27.966  61.956  50.022  1.00 40.32           N  
ANISOU 2259  N   LEU B 309     4839   4793   5687    919   -872  -1074       N  
ATOM   2260  CA  LEU B 309      27.755  63.367  49.724  1.00 37.78           C  
ANISOU 2260  CA  LEU B 309     4518   4485   5351    882   -854  -1106       C  
ATOM   2261  C   LEU B 309      26.982  63.506  48.419  1.00 32.65           C  
ANISOU 2261  C   LEU B 309     3875   3831   4700    799   -764  -1076       C  
ATOM   2262  O   LEU B 309      27.309  62.837  47.438  1.00 32.33           O  
ANISOU 2262  O   LEU B 309     3799   3770   4714    757   -721  -1089       O  
ATOM   2263  CB  LEU B 309      29.093  64.106  49.634  1.00 33.51           C  
ANISOU 2263  CB  LEU B 309     3912   3924   4898    871   -892  -1201       C  
ATOM   2264  CG  LEU B 309      29.975  64.101  50.886  1.00 38.83           C  
ANISOU 2264  CG  LEU B 309     4569   4605   5581    954   -991  -1250       C  
ATOM   2265  CD1 LEU B 309      31.314  64.760  50.597  1.00 30.45           C  
ANISOU 2265  CD1 LEU B 309     3428   3515   4627    928  -1021  -1345       C  
ATOM   2266  CD2 LEU B 309      29.268  64.808  52.028  1.00 29.29           C  
ANISOU 2266  CD2 LEU B 309     3413   3441   4277   1019  -1041  -1237       C  
ATOM   2267  N   HIS B 310      25.958  64.361  48.422  1.00 30.54           N  
ANISOU 2267  N   HIS B 310     3650   3588   4366    785   -740  -1041       N  
ATOM   2268  CA  HIS B 310      25.152  64.627  47.231  1.00 35.73           C  
ANISOU 2268  CA  HIS B 310     4316   4249   5011    713   -659  -1010       C  
ATOM   2269  C   HIS B 310      26.027  64.886  46.012  1.00 34.04           C  
ANISOU 2269  C   HIS B 310     4037   4015   4880    647   -618  -1060       C  
ATOM   2270  O   HIS B 310      25.849  64.274  44.958  1.00 29.24           O  
ANISOU 2270  O   HIS B 310     3412   3412   4285    604   -558  -1050       O  
ATOM   2271  CB  HIS B 310      24.234  65.837  47.439  1.00 34.31           C  
ANISOU 2271  CB  HIS B 310     4177   4091   4768    711   -654   -988       C  
ATOM   2272  CG  HIS B 310      23.341  65.732  48.637  1.00 35.47           C  
ANISOU 2272  CG  HIS B 310     4381   4277   4819    781   -689   -942       C  
ATOM   2273  ND1 HIS B 310      23.826  65.675  49.926  1.00 43.84           N  
ANISOU 2273  ND1 HIS B 310     5445   5355   5858    862   -767   -965       N  
ATOM   2274  CD2 HIS B 310      21.993  65.698  48.742  1.00 38.46           C  
ANISOU 2274  CD2 HIS B 310     4808   4692   5111    787   -657   -873       C  
ATOM   2275  CE1 HIS B 310      22.817  65.600  50.774  1.00 44.54           C  
ANISOU 2275  CE1 HIS B 310     5583   5496   5845    916   -777   -907       C  
ATOM   2276  NE2 HIS B 310      21.693  65.608  50.081  1.00 46.68           N  
ANISOU 2276  NE2 HIS B 310     5881   5778   6079    870   -710   -850       N  
ATOM   2277  N   GLN B 311      26.980  65.794  46.184  1.00 28.61           N  
ANISOU 2277  N   GLN B 311     3307   3312   4251    643   -653  -1116       N  
ATOM   2278  CA  GLN B 311      27.829  66.247  45.092  1.00 29.87           C  
ANISOU 2278  CA  GLN B 311     3395   3463   4490    578   -613  -1151       C  
ATOM   2279  C   GLN B 311      28.698  65.124  44.548  1.00 32.34           C  
ANISOU 2279  C   GLN B 311     3654   3778   4858    575   -596  -1185       C  
ATOM   2280  O   GLN B 311      28.987  65.080  43.356  1.00 37.14           O  
ANISOU 2280  O   GLN B 311     4213   4404   5495    521   -533  -1194       O  
ATOM   2281  CB  GLN B 311      28.707  67.418  45.539  1.00 32.33           C  
ANISOU 2281  CB  GLN B 311     3665   3748   4871    577   -667  -1201       C  
ATOM   2282  CG  GLN B 311      29.579  67.141  46.755  1.00 36.78           C  
ANISOU 2282  CG  GLN B 311     4214   4296   5463    648   -759  -1259       C  
ATOM   2283  CD  GLN B 311      28.934  67.580  48.055  1.00 36.54           C  
ANISOU 2283  CD  GLN B 311     4247   4274   5364    718   -828  -1256       C  
ATOM   2284  OE1 GLN B 311      27.727  67.436  48.244  1.00 35.70           O  
ANISOU 2284  OE1 GLN B 311     4207   4193   5163    735   -805  -1198       O  
ATOM   2285  NE2 GLN B 311      29.741  68.126  48.959  1.00 37.83           N  
ANISOU 2285  NE2 GLN B 311     4383   4421   5569    762   -914  -1324       N  
ATOM   2286  N   ASP B 312      29.114  64.213  45.419  1.00 35.40           N  
ANISOU 2286  N   ASP B 312     4047   4150   5253    637   -654  -1205       N  
ATOM   2287  CA  ASP B 312      29.950  63.102  44.985  1.00 35.84           C  
ANISOU 2287  CA  ASP B 312     4051   4199   5367    644   -649  -1245       C  
ATOM   2288  C   ASP B 312      29.195  62.166  44.050  1.00 38.89           C  
ANISOU 2288  C   ASP B 312     4453   4596   5727    620   -587  -1216       C  
ATOM   2289  O   ASP B 312      29.712  61.780  43.004  1.00 43.31           O  
ANISOU 2289  O   ASP B 312     4956   5172   6329    590   -544  -1256       O  
ATOM   2290  CB  ASP B 312      30.479  62.322  46.184  1.00 38.61           C  
ANISOU 2290  CB  ASP B 312     4411   4528   5733    722   -732  -1262       C  
ATOM   2291  CG  ASP B 312      31.607  63.033  46.894  1.00 42.70           C  
ANISOU 2291  CG  ASP B 312     4884   5038   6303    749   -798  -1323       C  
ATOM   2292  OD1 ASP B 312      32.258  63.905  46.278  1.00 39.67           O  
ANISOU 2292  OD1 ASP B 312     4440   4655   5976    698   -777  -1362       O  
ATOM   2293  OD2 ASP B 312      31.847  62.703  48.071  1.00 40.41           O  
ANISOU 2293  OD2 ASP B 312     4613   4741   5999    821   -875  -1328       O  
ATOM   2294  N   TRP B 313      27.977  61.796  44.432  1.00 30.87           N  
ANISOU 2294  N   TRP B 313     3509   3578   4644    635   -585  -1151       N  
ATOM   2295  CA  TRP B 313      27.148  60.947  43.585  1.00 36.40           C  
ANISOU 2295  CA  TRP B 313     4224   4282   5325    610   -534  -1126       C  
ATOM   2296  C   TRP B 313      26.869  61.621  42.249  1.00 39.32           C  
ANISOU 2296  C   TRP B 313     4569   4694   5678    544   -456  -1133       C  
ATOM   2297  O   TRP B 313      26.985  61.001  41.193  1.00 41.40           O  
ANISOU 2297  O   TRP B 313     4794   4975   5961    522   -414  -1166       O  
ATOM   2298  CB  TRP B 313      25.819  60.603  44.265  1.00 34.93           C  
ANISOU 2298  CB  TRP B 313     4113   4089   5070    631   -543  -1044       C  
ATOM   2299  CG  TRP B 313      24.950  59.766  43.388  1.00 36.96           C  
ANISOU 2299  CG  TRP B 313     4379   4344   5321    602   -497  -1024       C  
ATOM   2300  CD1 TRP B 313      23.907  60.190  42.617  1.00 30.98           C  
ANISOU 2300  CD1 TRP B 313     3643   3619   4509    556   -439   -993       C  
ATOM   2301  CD2 TRP B 313      25.069  58.359  43.161  1.00 40.05           C  
ANISOU 2301  CD2 TRP B 313     4751   4694   5771    617   -511  -1040       C  
ATOM   2302  NE1 TRP B 313      23.361  59.131  41.932  1.00 34.20           N  
ANISOU 2302  NE1 TRP B 313     4046   4013   4936    543   -418   -995       N  
ATOM   2303  CE2 TRP B 313      24.058  57.994  42.249  1.00 36.57           C  
ANISOU 2303  CE2 TRP B 313     4321   4264   5311    579   -463  -1025       C  
ATOM   2304  CE3 TRP B 313      25.929  57.370  43.646  1.00 40.89           C  
ANISOU 2304  CE3 TRP B 313     4832   4754   5952    664   -566  -1069       C  
ATOM   2305  CZ2 TRP B 313      23.888  56.682  41.813  1.00 38.89           C  
ANISOU 2305  CZ2 TRP B 313     4598   4515   5663    584   -472  -1046       C  
ATOM   2306  CZ3 TRP B 313      25.755  56.071  43.213  1.00 48.02           C  
ANISOU 2306  CZ3 TRP B 313     5720   5610   6914    669   -574  -1082       C  
ATOM   2307  CH2 TRP B 313      24.745  55.738  42.305  1.00 43.84           C  
ANISOU 2307  CH2 TRP B 313     5200   5087   6372    629   -529  -1074       C  
ATOM   2308  N   LEU B 314      26.490  62.892  42.310  1.00 41.16           N  
ANISOU 2308  N   LEU B 314     4822   4945   5872    518   -441  -1102       N  
ATOM   2309  CA  LEU B 314      26.136  63.647  41.117  1.00 38.26           C  
ANISOU 2309  CA  LEU B 314     4436   4618   5481    457   -369  -1089       C  
ATOM   2310  C   LEU B 314      27.341  63.900  40.210  1.00 42.69           C  
ANISOU 2310  C   LEU B 314     4910   5207   6104    425   -337  -1140       C  
ATOM   2311  O   LEU B 314      27.185  64.046  38.999  1.00 35.14           O  
ANISOU 2311  O   LEU B 314     3921   4301   5129    383   -269  -1135       O  
ATOM   2312  CB  LEU B 314      25.484  64.973  41.513  1.00 29.85           C  
ANISOU 2312  CB  LEU B 314     3414   3554   4375    444   -373  -1041       C  
ATOM   2313  CG  LEU B 314      24.146  64.835  42.245  1.00 29.67           C  
ANISOU 2313  CG  LEU B 314     3472   3528   4274    473   -389   -985       C  
ATOM   2314  CD1 LEU B 314      23.682  66.177  42.789  1.00 22.33           C  
ANISOU 2314  CD1 LEU B 314     2577   2596   3312    475   -407   -958       C  
ATOM   2315  CD2 LEU B 314      23.084  64.227  41.334  1.00 31.46           C  
ANISOU 2315  CD2 LEU B 314     3718   3783   4452    445   -330   -951       C  
ATOM   2316  N   ASN B 315      28.535  63.943  40.793  1.00 41.06           N  
ANISOU 2316  N   ASN B 315     4658   4975   5967    447   -385  -1187       N  
ATOM   2317  CA  ASN B 315      29.744  64.186  40.010  1.00 37.34           C  
ANISOU 2317  CA  ASN B 315     4093   4535   5561    418   -355  -1232       C  
ATOM   2318  C   ASN B 315      30.378  62.901  39.485  1.00 42.48           C  
ANISOU 2318  C   ASN B 315     4692   5204   6242    442   -346  -1295       C  
ATOM   2319  O   ASN B 315      31.442  62.935  38.871  1.00 43.63           O  
ANISOU 2319  O   ASN B 315     4752   5386   6439    429   -322  -1340       O  
ATOM   2320  CB  ASN B 315      30.769  64.974  40.829  1.00 37.26           C  
ANISOU 2320  CB  ASN B 315     4047   4490   5622    425   -413  -1258       C  
ATOM   2321  CG  ASN B 315      30.379  66.431  40.998  1.00 43.08           C  
ANISOU 2321  CG  ASN B 315     4803   5210   6354    388   -414  -1212       C  
ATOM   2322  OD1 ASN B 315      29.748  67.025  40.125  1.00 46.33           O  
ANISOU 2322  OD1 ASN B 315     5219   5652   6731    340   -350  -1161       O  
ATOM   2323  ND2 ASN B 315      30.758  67.016  42.130  1.00 46.01           N  
ANISOU 2323  ND2 ASN B 315     5183   5534   6763    417   -491  -1234       N  
ATOM   2324  N   GLY B 316      29.726  61.769  39.736  1.00 42.11           N  
ANISOU 2324  N   GLY B 316     4695   5133   6171    480   -367  -1296       N  
ATOM   2325  CA  GLY B 316      30.092  60.521  39.088  1.00 43.19           C  
ANISOU 2325  CA  GLY B 316     4790   5283   6339    503   -357  -1358       C  
ATOM   2326  C   GLY B 316      31.081  59.627  39.812  1.00 44.99           C  
ANISOU 2326  C   GLY B 316     4988   5464   6641    560   -425  -1415       C  
ATOM   2327  O   GLY B 316      31.663  58.730  39.204  1.00 48.44           O  
ANISOU 2327  O   GLY B 316     5370   5915   7121    581   -419  -1484       O  
ATOM   2328  N   LYS B 317      31.273  59.854  41.108  1.00 41.40           N  
ANISOU 2328  N   LYS B 317     4569   4960   6201    592   -493  -1392       N  
ATOM   2329  CA  LYS B 317      32.222  59.052  41.873  1.00 42.50           C  
ANISOU 2329  CA  LYS B 317     4682   5058   6409    652   -564  -1439       C  
ATOM   2330  C   LYS B 317      31.742  57.617  42.023  1.00 45.92           C  
ANISOU 2330  C   LYS B 317     5147   5443   6856    694   -593  -1436       C  
ATOM   2331  O   LYS B 317      30.546  57.363  42.151  1.00 43.36           O  
ANISOU 2331  O   LYS B 317     4890   5100   6483    687   -584  -1373       O  
ATOM   2332  CB  LYS B 317      32.467  59.671  43.250  1.00 40.78           C  
ANISOU 2332  CB  LYS B 317     4495   4809   6189    684   -634  -1413       C  
ATOM   2333  CG  LYS B 317      33.075  61.056  43.191  1.00 41.58           C  
ANISOU 2333  CG  LYS B 317     4555   4938   6307    645   -624  -1428       C  
ATOM   2334  CD  LYS B 317      33.933  61.345  44.410  1.00 46.38           C  
ANISOU 2334  CD  LYS B 317     5149   5518   6955    693   -710  -1457       C  
ATOM   2335  CE  LYS B 317      34.657  62.674  44.257  1.00 56.34           C  
ANISOU 2335  CE  LYS B 317     6351   6794   8261    649   -706  -1483       C  
ATOM   2336  NZ  LYS B 317      35.559  62.956  45.407  1.00 58.14           N  
ANISOU 2336  NZ  LYS B 317     6556   6997   8538    698   -798  -1529       N  
ATOM   2337  N   GLU B 318      32.684  56.681  42.004  1.00 49.24           N  
ANISOU 2337  N   GLU B 318     5516   5843   7351    735   -629  -1500       N  
ATOM   2338  CA  GLU B 318      32.362  55.265  42.133  1.00 45.61           C  
ANISOU 2338  CA  GLU B 318     5081   5334   6916    762   -664  -1483       C  
ATOM   2339  C   GLU B 318      32.332  54.828  43.588  1.00 48.70           C  
ANISOU 2339  C   GLU B 318     5522   5664   7318    815   -745  -1423       C  
ATOM   2340  O   GLU B 318      33.203  55.190  44.379  1.00 53.11           O  
ANISOU 2340  O   GLU B 318     6063   6226   7889    843   -791  -1433       O  
ATOM   2341  CB  GLU B 318      33.370  54.408  41.364  1.00 43.77           C  
ANISOU 2341  CB  GLU B 318     4771   5120   6741    766   -666  -1562       C  
ATOM   2342  CG  GLU B 318      33.474  54.721  39.883  1.00 47.18           C  
ANISOU 2342  CG  GLU B 318     5141   5629   7154    727   -587  -1626       C  
ATOM   2343  CD  GLU B 318      34.476  53.828  39.168  1.00 53.67           C  
ANISOU 2343  CD  GLU B 318     5886   6480   8027    742   -595  -1709       C  
ATOM   2344  OE1 GLU B 318      35.104  52.975  39.839  1.00 47.70           O  
ANISOU 2344  OE1 GLU B 318     5126   5672   7326    779   -664  -1716       O  
ATOM   2345  OE2 GLU B 318      34.636  53.979  37.938  1.00 55.63           O  
ANISOU 2345  OE2 GLU B 318     6077   6806   8254    721   -533  -1767       O  
ATOM   2346  N   TYR B 319      31.327  54.034  43.933  1.00 46.67           N  
ANISOU 2346  N   TYR B 319     5322   5352   7059    832   -763  -1360       N  
ATOM   2347  CA  TYR B 319      31.218  53.500  45.281  1.00 40.11           C  
ANISOU 2347  CA  TYR B 319     4535   4467   6238    891   -835  -1290       C  
ATOM   2348  C   TYR B 319      31.344  51.991  45.266  1.00 39.30           C  
ANISOU 2348  C   TYR B 319     4422   4297   6212    912   -875  -1282       C  
ATOM   2349  O   TYR B 319      30.581  51.302  44.591  1.00 38.48           O  
ANISOU 2349  O   TYR B 319     4326   4160   6136    889   -853  -1276       O  
ATOM   2350  CB  TYR B 319      29.899  53.920  45.921  1.00 37.78           C  
ANISOU 2350  CB  TYR B 319     4317   4172   5866    889   -826  -1187       C  
ATOM   2351  CG  TYR B 319      29.814  55.405  46.140  1.00 40.47           C  
ANISOU 2351  CG  TYR B 319     4674   4581   6121    864   -799  -1180       C  
ATOM   2352  CD1 TYR B 319      29.406  56.253  45.120  1.00 42.09           C  
ANISOU 2352  CD1 TYR B 319     4873   4833   6288    798   -726  -1204       C  
ATOM   2353  CD2 TYR B 319      30.159  55.963  47.359  1.00 40.38           C  
ANISOU 2353  CD2 TYR B 319     4683   4588   6072    910   -852  -1153       C  
ATOM   2354  CE1 TYR B 319      29.335  57.613  45.312  1.00 46.49           C  
ANISOU 2354  CE1 TYR B 319     5443   5437   6784    775   -708  -1196       C  
ATOM   2355  CE2 TYR B 319      30.091  57.323  47.560  1.00 41.58           C  
ANISOU 2355  CE2 TYR B 319     4847   4792   6161    890   -838  -1159       C  
ATOM   2356  CZ  TYR B 319      29.676  58.141  46.535  1.00 46.91           C  
ANISOU 2356  CZ  TYR B 319     5514   5496   6812    820   -767  -1178       C  
ATOM   2357  OH  TYR B 319      29.604  59.493  46.731  1.00 48.54           O  
ANISOU 2357  OH  TYR B 319     5731   5740   6972    801   -759  -1182       O  
ATOM   2358  N   LYS B 320      32.317  51.480  46.010  1.00 41.89           N  
ANISOU 2358  N   LYS B 320     4731   4603   6581    957   -939  -1285       N  
ATOM   2359  CA  LYS B 320      32.536  50.046  46.047  1.00 41.85           C  
ANISOU 2359  CA  LYS B 320     4715   4527   6660    979   -984  -1278       C  
ATOM   2360  C   LYS B 320      32.238  49.447  47.411  1.00 42.97           C  
ANISOU 2360  C   LYS B 320     4905   4609   6812   1038  -1050  -1168       C  
ATOM   2361  O   LYS B 320      32.686  49.947  48.445  1.00 48.78           O  
ANISOU 2361  O   LYS B 320     5655   5375   7504   1081  -1087  -1136       O  
ATOM   2362  CB  LYS B 320      33.968  49.709  45.638  1.00 40.03           C  
ANISOU 2362  CB  LYS B 320     4413   4316   6480    984  -1003  -1375       C  
ATOM   2363  CG  LYS B 320      34.277  48.222  45.688  1.00 43.70           C  
ANISOU 2363  CG  LYS B 320     4863   4704   7037   1011  -1057  -1376       C  
ATOM   2364  CD  LYS B 320      35.720  47.951  45.332  1.00 46.81           C  
ANISOU 2364  CD  LYS B 320     5185   5125   7475   1023  -1079  -1476       C  
ATOM   2365  CE  LYS B 320      35.985  48.216  43.865  1.00 47.40           C  
ANISOU 2365  CE  LYS B 320     5197   5267   7544    978  -1018  -1579       C  
ATOM   2366  NZ  LYS B 320      37.365  47.804  43.492  1.00 49.54           N  
ANISOU 2366  NZ  LYS B 320     5394   5565   7866    996  -1042  -1675       N  
ATOM   2367  N   CYS B 321      31.462  48.371  47.401  1.00 42.07           N  
ANISOU 2367  N   CYS B 321     4812   4415   6757   1040  -1066  -1104       N  
ATOM   2368  CA  CYS B 321      31.285  47.554  48.586  1.00 40.86           C  
ANISOU 2368  CA  CYS B 321     4690   4199   6635   1094  -1129   -987       C  
ATOM   2369  C   CYS B 321      32.124  46.291  48.429  1.00 46.12           C  
ANISOU 2369  C   CYS B 321     5318   4798   7408   1107  -1177  -1024       C  
ATOM   2370  O   CYS B 321      32.117  45.653  47.372  1.00 46.61           O  
ANISOU 2370  O   CYS B 321     5346   4826   7538   1070  -1162  -1097       O  
ATOM   2371  CB  CYS B 321      29.812  47.208  48.797  1.00 40.03           C  
ANISOU 2371  CB  CYS B 321     4631   4042   6535   1086  -1120   -868       C  
ATOM   2372  SG  CYS B 321      29.487  46.278  50.308  1.00 47.95           S  
ANISOU 2372  SG  CYS B 321     5670   4986   7564   1149  -1190   -686       S  
ATOM   2373  N   LYS B 322      32.870  45.950  49.472  1.00 50.45           N  
ANISOU 2373  N   LYS B 322     5869   5336   7964   1164  -1236   -979       N  
ATOM   2374  CA  LYS B 322      33.674  44.736  49.481  1.00 46.35           C  
ANISOU 2374  CA  LYS B 322     5317   4748   7547   1186  -1290  -1002       C  
ATOM   2375  C   LYS B 322      33.247  43.874  50.660  1.00 46.68           C  
ANISOU 2375  C   LYS B 322     5396   4719   7621   1233  -1343   -844       C  
ATOM   2376  O   LYS B 322      33.285  44.311  51.812  1.00 50.19           O  
ANISOU 2376  O   LYS B 322     5871   5209   7990   1283  -1365   -755       O  
ATOM   2377  CB  LYS B 322      35.165  45.079  49.547  1.00 55.42           C  
ANISOU 2377  CB  LYS B 322     6421   5953   8684   1210  -1312  -1104       C  
ATOM   2378  CG  LYS B 322      36.108  43.884  49.567  1.00 59.48           C  
ANISOU 2378  CG  LYS B 322     6898   6404   9299   1239  -1371  -1139       C  
ATOM   2379  CD  LYS B 322      37.393  44.205  48.817  1.00 59.68           C  
ANISOU 2379  CD  LYS B 322     6856   6490   9331   1228  -1364  -1291       C  
ATOM   2380  CE  LYS B 322      38.612  43.634  49.515  1.00 61.50           C  
ANISOU 2380  CE  LYS B 322     7062   6702   9605   1285  -1432  -1306       C  
ATOM   2381  NZ  LYS B 322      38.978  44.436  50.712  1.00 60.56           N  
ANISOU 2381  NZ  LYS B 322     6969   6638   9405   1328  -1456  -1255       N  
ATOM   2382  N   VAL B 323      32.820  42.651  50.363  1.00 51.21           N  
ANISOU 2382  N   VAL B 323     5963   5189   8307   1218  -1364   -806       N  
ATOM   2383  CA  VAL B 323      32.267  41.762  51.379  1.00 55.20           C  
ANISOU 2383  CA  VAL B 323     6499   5618   8857   1250  -1407   -636       C  
ATOM   2384  C   VAL B 323      33.196  40.581  51.644  1.00 57.67           C  
ANISOU 2384  C   VAL B 323     6782   5856   9274   1285  -1472   -641       C  
ATOM   2385  O   VAL B 323      33.618  39.889  50.715  1.00 53.00           O  
ANISOU 2385  O   VAL B 323     6148   5209   8780   1259  -1486   -752       O  
ATOM   2386  CB  VAL B 323      30.879  41.255  50.959  1.00 48.45           C  
ANISOU 2386  CB  VAL B 323     5660   4688   8062   1200  -1385   -558       C  
ATOM   2387  CG1 VAL B 323      30.387  40.194  51.917  1.00 42.69           C  
ANISOU 2387  CG1 VAL B 323     4948   3872   7401   1224  -1429   -376       C  
ATOM   2388  CG2 VAL B 323      29.898  42.417  50.893  1.00 47.68           C  
ANISOU 2388  CG2 VAL B 323     5597   4666   7854   1176  -1326   -528       C  
ATOM   2389  N   SER B 324      33.511  40.351  52.916  1.00 66.91           N  
ANISOU 2389  N   SER B 324     7973   7032  10418   1349  -1515   -520       N  
ATOM   2390  CA  SER B 324      34.523  39.361  53.276  1.00 69.93           C  
ANISOU 2390  CA  SER B 324     8329   7357  10886   1393  -1578   -526       C  
ATOM   2391  C   SER B 324      34.076  38.386  54.361  1.00 67.57           C  
ANISOU 2391  C   SER B 324     8054   6987  10633   1431  -1619   -327       C  
ATOM   2392  O   SER B 324      33.277  38.720  55.236  1.00 69.91           O  
ANISOU 2392  O   SER B 324     8389   7327  10848   1451  -1603   -171       O  
ATOM   2393  CB  SER B 324      35.801  40.071  53.728  1.00 78.04           C  
ANISOU 2393  CB  SER B 324     9341   8479  11833   1443  -1597   -606       C  
ATOM   2394  OG  SER B 324      36.182  41.081  52.809  1.00 86.45           O  
ANISOU 2394  OG  SER B 324    10381   9618  12846   1404  -1553   -768       O  
ATOM   2395  N   ASN B 325      34.605  37.170  54.281  1.00 72.83           N  
ANISOU 2395  N   ASN B 325     8692   7551  11429   1443  -1673   -334       N  
ATOM   2396  CA  ASN B 325      34.433  36.167  55.325  1.00 79.19           C  
ANISOU 2396  CA  ASN B 325     9511   8288  12290   1486  -1718   -150       C  
ATOM   2397  C   ASN B 325      35.708  35.363  55.490  1.00 77.19           C  
ANISOU 2397  C   ASN B 325     9224   7987  12117   1536  -1783   -208       C  
ATOM   2398  O   ASN B 325      36.507  35.255  54.557  1.00 81.79           O  
ANISOU 2398  O   ASN B 325     9767   8553  12758   1518  -1797   -390       O  
ATOM   2399  CB  ASN B 325      33.259  35.235  55.010  1.00 82.61           C  
ANISOU 2399  CB  ASN B 325     9947   8600  12842   1429  -1716    -50       C  
ATOM   2400  CG  ASN B 325      32.030  35.546  55.844  1.00 90.96           C  
ANISOU 2400  CG  ASN B 325    11047   9696  13818   1426  -1680    156       C  
ATOM   2401  OD1 ASN B 325      31.965  36.580  56.507  1.00 97.44           O  
ANISOU 2401  OD1 ASN B 325    11896  10644  14483   1464  -1650    201       O  
ATOM   2402  ND2 ASN B 325      31.049  34.651  55.815  1.00 94.08           N  
ANISOU 2402  ND2 ASN B 325    11440   9985  14320   1381  -1684    279       N  
ATOM   2403  N   LYS B 326      35.906  34.805  56.680  1.00 72.21           N  
ANISOU 2403  N   LYS B 326     8608   7345  11484   1601  -1823    -50       N  
ATOM   2404  CA  LYS B 326      37.004  33.875  56.908  1.00 69.67           C  
ANISOU 2404  CA  LYS B 326     8256   6960  11256   1651  -1891    -78       C  
ATOM   2405  C   LYS B 326      36.838  32.660  56.003  1.00 76.00           C  
ANISOU 2405  C   LYS B 326     9025   7607  12245   1601  -1925   -133       C  
ATOM   2406  O   LYS B 326      37.810  31.979  55.674  1.00 77.02           O  
ANISOU 2406  O   LYS B 326     9116   7680  12469   1622  -1978   -238       O  
ATOM   2407  CB  LYS B 326      37.047  33.445  58.374  1.00 67.42           C  
ANISOU 2407  CB  LYS B 326     7994   6691  10931   1729  -1923    131       C  
ATOM   2408  CG  LYS B 326      37.567  34.515  59.319  1.00 69.34           C  
ANISOU 2408  CG  LYS B 326     8254   7095  10996   1799  -1914    152       C  
ATOM   2409  CD  LYS B 326      36.827  34.496  60.650  1.00 68.08           C  
ANISOU 2409  CD  LYS B 326     8131   6998  10737   1853  -1904    396       C  
ATOM   2410  CE  LYS B 326      36.648  33.082  61.180  1.00 70.84           C  
ANISOU 2410  CE  LYS B 326     8479   7234  11203   1878  -1946    565       C  
ATOM   2411  NZ  LYS B 326      36.262  33.080  62.620  1.00 73.43           N  
ANISOU 2411  NZ  LYS B 326     8834   7658  11407   1956  -1943    797       N  
ATOM   2412  N   ALA B 327      35.594  32.404  55.598  1.00 77.70           N  
ANISOU 2412  N   ALA B 327     9251   7758  12513   1534  -1896    -67       N  
ATOM   2413  CA  ALA B 327      35.279  31.297  54.703  1.00 80.11           C  
ANISOU 2413  CA  ALA B 327     9521   7919  12997   1479  -1930   -123       C  
ATOM   2414  C   ALA B 327      34.547  31.763  53.440  1.00 81.87           C  
ANISOU 2414  C   ALA B 327     9732   8151  13224   1399  -1882   -251       C  
ATOM   2415  O   ALA B 327      33.492  31.232  53.086  1.00 83.20           O  
ANISOU 2415  O   ALA B 327     9897   8233  13481   1340  -1878   -193       O  
ATOM   2416  CB  ALA B 327      34.457  30.251  55.433  1.00 83.26           C  
ANISOU 2416  CB  ALA B 327     9932   8208  13497   1472  -1958     92       C  
ATOM   2417  N   LEU B 328      35.099  32.778  52.787  1.00 82.09           N  
ANISOU 2417  N   LEU B 328     9751   8288  13152   1396  -1844   -417       N  
ATOM   2418  CA  LEU B 328      34.794  33.079  51.396  1.00 78.51           C  
ANISOU 2418  CA  LEU B 328     9269   7848  12713   1333  -1810   -585       C  
ATOM   2419  C   LEU B 328      36.081  32.785  50.639  1.00 81.68           C  
ANISOU 2419  C   LEU B 328     9615   8260  13160   1355  -1847   -780       C  
ATOM   2420  O   LEU B 328      37.153  33.184  51.093  1.00 77.65           O  
ANISOU 2420  O   LEU B 328     9101   7818  12585   1407  -1857   -817       O  
ATOM   2421  CB  LEU B 328      34.363  34.538  51.214  1.00 74.32           C  
ANISOU 2421  CB  LEU B 328     8768   7447  12022   1310  -1730   -610       C  
ATOM   2422  CG  LEU B 328      32.905  34.885  50.895  1.00 71.42           C  
ANISOU 2422  CG  LEU B 328     8427   7074  11636   1248  -1678   -543       C  
ATOM   2423  CD1 LEU B 328      32.717  36.396  50.885  1.00 67.80           C  
ANISOU 2423  CD1 LEU B 328     7999   6753  11010   1243  -1607   -568       C  
ATOM   2424  CD2 LEU B 328      32.463  34.290  49.567  1.00 75.25           C  
ANISOU 2424  CD2 LEU B 328     8869   7493  12228   1188  -1682   -665       C  
ATOM   2425  N   PRO B 329      35.997  32.072  49.503  1.00 85.22           N  
ANISOU 2425  N   PRO B 329    10014   8647  13718   1319  -1871   -907       N  
ATOM   2426  CA  PRO B 329      37.239  31.779  48.774  1.00 81.81           C  
ANISOU 2426  CA  PRO B 329     9523   8238  13322   1346  -1906  -1092       C  
ATOM   2427  C   PRO B 329      37.961  33.067  48.389  1.00 79.39           C  
ANISOU 2427  C   PRO B 329     9208   8089  12867   1352  -1847  -1210       C  
ATOM   2428  O   PRO B 329      39.171  33.192  48.590  1.00 79.39           O  
ANISOU 2428  O   PRO B 329     9184   8138  12844   1398  -1870  -1278       O  
ATOM   2429  CB  PRO B 329      36.757  31.015  47.536  1.00 84.39           C  
ANISOU 2429  CB  PRO B 329     9800   8503  13762   1302  -1928  -1205       C  
ATOM   2430  CG  PRO B 329      35.315  31.365  47.391  1.00 89.44           C  
ANISOU 2430  CG  PRO B 329    10473   9132  14378   1242  -1877  -1119       C  
ATOM   2431  CD  PRO B 329      34.802  31.593  48.785  1.00 89.18           C  
ANISOU 2431  CD  PRO B 329    10506   9074  14304   1255  -1865   -900       C  
ATOM   2432  N   ALA B 330      37.204  34.017  47.856  1.00 77.80           N  
ANISOU 2432  N   ALA B 330     9024   7966  12573   1303  -1774  -1229       N  
ATOM   2433  CA  ALA B 330      37.687  35.370  47.632  1.00 73.06           C  
ANISOU 2433  CA  ALA B 330     8422   7511  11827   1300  -1710  -1303       C  
ATOM   2434  C   ALA B 330      36.607  36.337  48.091  1.00 73.62           C  
ANISOU 2434  C   ALA B 330     8553   7622  11796   1272  -1648  -1186       C  
ATOM   2435  O   ALA B 330      35.421  36.007  48.054  1.00 75.21           O  
ANISOU 2435  O   ALA B 330     8781   7758  12038   1237  -1639  -1101       O  
ATOM   2436  CB  ALA B 330      38.029  35.593  46.166  1.00 65.62           C  
ANISOU 2436  CB  ALA B 330     7418   6643  10871   1271  -1680  -1488       C  
ATOM   2437  N   PRO B 331      37.006  37.533  48.542  1.00 74.10           N  
ANISOU 2437  N   PRO B 331     8634   7790  11729   1286  -1610  -1182       N  
ATOM   2438  CA  PRO B 331      35.975  38.507  48.909  1.00 75.47           C  
ANISOU 2438  CA  PRO B 331     8861   8011  11803   1262  -1553  -1086       C  
ATOM   2439  C   PRO B 331      35.280  39.067  47.668  1.00 72.16           C  
ANISOU 2439  C   PRO B 331     8428   7639  11349   1199  -1487  -1174       C  
ATOM   2440  O   PRO B 331      35.912  39.190  46.618  1.00 71.43           O  
ANISOU 2440  O   PRO B 331     8282   7601  11256   1183  -1470  -1323       O  
ATOM   2441  CB  PRO B 331      36.766  39.589  49.649  1.00 77.75           C  
ANISOU 2441  CB  PRO B 331     9161   8403  11976   1299  -1542  -1087       C  
ATOM   2442  CG  PRO B 331      38.138  39.502  49.073  1.00 74.02           C  
ANISOU 2442  CG  PRO B 331     8626   7969  11528   1313  -1561  -1239       C  
ATOM   2443  CD  PRO B 331      38.367  38.045  48.777  1.00 75.84           C  
ANISOU 2443  CD  PRO B 331     8826   8092  11898   1326  -1621  -1262       C  
ATOM   2444  N   ILE B 332      33.998  39.388  47.792  1.00 64.98           N  
ANISOU 2444  N   ILE B 332     7563   6716  10408   1167  -1450  -1078       N  
ATOM   2445  CA  ILE B 332      33.207  39.868  46.663  1.00 60.95           C  
ANISOU 2445  CA  ILE B 332     7046   6246   9868   1109  -1390  -1147       C  
ATOM   2446  C   ILE B 332      33.178  41.396  46.612  1.00 56.60           C  
ANISOU 2446  C   ILE B 332     6513   5818   9175   1096  -1321  -1169       C  
ATOM   2447  O   ILE B 332      33.000  42.055  47.633  1.00 56.62           O  
ANISOU 2447  O   ILE B 332     6561   5848   9106   1121  -1317  -1069       O  
ATOM   2448  CB  ILE B 332      31.764  39.328  46.729  1.00 59.01           C  
ANISOU 2448  CB  ILE B 332     6831   5910   9679   1075  -1389  -1037       C  
ATOM   2449  CG1 ILE B 332      31.783  37.799  46.792  1.00 53.98           C  
ANISOU 2449  CG1 ILE B 332     6170   5142   9199   1082  -1462  -1011       C  
ATOM   2450  CG2 ILE B 332      30.943  39.799  45.533  1.00 54.72           C  
ANISOU 2450  CG2 ILE B 332     6278   5411   9103   1018  -1329  -1116       C  
ATOM   2451  CD1 ILE B 332      30.425  37.180  47.011  1.00 49.72           C  
ANISOU 2451  CD1 ILE B 332     5655   4501   8735   1047  -1471   -883       C  
ATOM   2452  N   GLU B 333      33.361  41.951  45.417  1.00 46.79           N  
ANISOU 2452  N   GLU B 333     5232   4656   7891   1060  -1270  -1296       N  
ATOM   2453  CA  GLU B 333      33.353  43.395  45.229  1.00 43.19           C  
ANISOU 2453  CA  GLU B 333     4785   4312   7313   1041  -1203  -1322       C  
ATOM   2454  C   GLU B 333      32.244  43.845  44.265  1.00 46.67           C  
ANISOU 2454  C   GLU B 333     5234   4783   7714    986  -1138  -1342       C  
ATOM   2455  O   GLU B 333      32.015  43.217  43.229  1.00 49.39           O  
ANISOU 2455  O   GLU B 333     5543   5114   8108    962  -1133  -1414       O  
ATOM   2456  CB  GLU B 333      34.716  43.869  44.718  1.00 38.03           C  
ANISOU 2456  CB  GLU B 333     4071   3748   6631   1048  -1192  -1445       C  
ATOM   2457  CG  GLU B 333      35.888  43.454  45.599  1.00 40.88           C  
ANISOU 2457  CG  GLU B 333     4418   4085   7030   1101  -1258  -1442       C  
ATOM   2458  CD  GLU B 333      37.193  44.060  45.130  1.00 48.55           C  
ANISOU 2458  CD  GLU B 333     5326   5149   7970   1104  -1243  -1558       C  
ATOM   2459  OE1 GLU B 333      38.084  43.309  44.690  1.00 55.89           O  
ANISOU 2459  OE1 GLU B 333     6200   6070   8965   1122  -1276  -1642       O  
ATOM   2460  OE2 GLU B 333      37.332  45.296  45.204  1.00 49.89           O  
ANISOU 2460  OE2 GLU B 333     5498   5401   8057   1088  -1200  -1564       O  
ATOM   2461  N   LYS B 334      31.558  44.930  44.620  1.00 43.04           N  
ANISOU 2461  N   LYS B 334     4821   4370   7163    973  -1092  -1280       N  
ATOM   2462  CA  LYS B 334      30.536  45.527  43.764  1.00 41.80           C  
ANISOU 2462  CA  LYS B 334     4676   4253   6954    924  -1026  -1296       C  
ATOM   2463  C   LYS B 334      30.761  47.031  43.637  1.00 42.92           C  
ANISOU 2463  C   LYS B 334     4821   4505   6981    909   -966  -1323       C  
ATOM   2464  O   LYS B 334      31.037  47.709  44.626  1.00 48.24           O  
ANISOU 2464  O   LYS B 334     5523   5199   7609    937   -979  -1270       O  
ATOM   2465  CB  LYS B 334      29.135  45.253  44.317  1.00 45.39           C  
ANISOU 2465  CB  LYS B 334     5188   4631   7428    917  -1033  -1174       C  
ATOM   2466  CG  LYS B 334      28.748  43.783  44.339  1.00 48.46           C  
ANISOU 2466  CG  LYS B 334     5568   4901   7945    917  -1089  -1138       C  
ATOM   2467  CD  LYS B 334      28.630  43.231  42.928  1.00 56.76           C  
ANISOU 2467  CD  LYS B 334     6568   5956   9042    880  -1076  -1257       C  
ATOM   2468  CE  LYS B 334      28.427  41.721  42.928  1.00 64.62           C  
ANISOU 2468  CE  LYS B 334     7543   6829  10182    883  -1145  -1241       C  
ATOM   2469  NZ  LYS B 334      28.473  41.151  41.548  1.00 70.98           N  
ANISOU 2469  NZ  LYS B 334     8288   7652  11030    861  -1145  -1377       N  
ATOM   2470  N   THR B 335      30.643  47.552  42.421  1.00 38.05           N  
ANISOU 2470  N   THR B 335     4173   3962   6320    867   -902  -1404       N  
ATOM   2471  CA  THR B 335      30.860  48.973  42.176  1.00 40.32           C  
ANISOU 2471  CA  THR B 335     4457   4349   6512    845   -842  -1428       C  
ATOM   2472  C   THR B 335      29.680  49.597  41.440  1.00 44.67           C  
ANISOU 2472  C   THR B 335     5035   4938   7002    800   -775  -1419       C  
ATOM   2473  O   THR B 335      29.192  49.035  40.461  1.00 47.22           O  
ANISOU 2473  O   THR B 335     5336   5260   7343    777   -756  -1462       O  
ATOM   2474  CB  THR B 335      32.138  49.209  41.352  1.00 40.37           C  
ANISOU 2474  CB  THR B 335     4385   4435   6517    840   -821  -1536       C  
ATOM   2475  OG1 THR B 335      33.283  48.832  42.125  1.00 45.08           O  
ANISOU 2475  OG1 THR B 335     4959   5007   7161    882   -882  -1546       O  
ATOM   2476  CG2 THR B 335      32.259  50.671  40.946  1.00 44.63           C  
ANISOU 2476  CG2 THR B 335     4913   5070   6973    808   -752  -1555       C  
ATOM   2477  N   ILE B 336      29.218  50.753  41.914  1.00 43.83           N  
ANISOU 2477  N   ILE B 336     4970   4864   6818    792   -744  -1367       N  
ATOM   2478  CA  ILE B 336      28.184  51.509  41.207  1.00 47.86           C  
ANISOU 2478  CA  ILE B 336     5503   5420   7260    749   -677  -1363       C  
ATOM   2479  C   ILE B 336      28.505  52.999  41.127  1.00 43.84           C  
ANISOU 2479  C   ILE B 336     4992   4994   6673    730   -628  -1375       C  
ATOM   2480  O   ILE B 336      29.337  53.512  41.873  1.00 41.31           O  
ANISOU 2480  O   ILE B 336     4664   4683   6351    754   -654  -1370       O  
ATOM   2481  CB  ILE B 336      26.799  51.362  41.866  1.00 45.06           C  
ANISOU 2481  CB  ILE B 336     5220   5009   6892    747   -687  -1260       C  
ATOM   2482  CG1 ILE B 336      26.838  51.848  43.313  1.00 39.26           C  
ANISOU 2482  CG1 ILE B 336     4533   4272   6112    774   -720  -1156       C  
ATOM   2483  CG2 ILE B 336      26.308  49.925  41.798  1.00 22.35           C  
ANISOU 2483  CG2 ILE B 336     2340   2033   4118    761   -732  -1251       C  
ATOM   2484  CD1 ILE B 336      25.476  51.891  43.954  1.00 39.93           C  
ANISOU 2484  CD1 ILE B 336     4682   4348   6140    755   -712  -1028       C  
ATOM   2485  N   SER B 337      27.826  53.682  40.211  1.00 43.12           N  
ANISOU 2485  N   SER B 337     4903   4963   6516    684   -560  -1385       N  
ATOM   2486  CA  SER B 337      27.954  55.123  40.042  1.00 43.78           C  
ANISOU 2486  CA  SER B 337     4988   5127   6521    646   -508  -1369       C  
ATOM   2487  C   SER B 337      26.776  55.618  39.212  1.00 46.31           C  
ANISOU 2487  C   SER B 337     5335   5496   6764    595   -443  -1338       C  
ATOM   2488  O   SER B 337      26.081  54.818  38.589  1.00 44.64           O  
ANISOU 2488  O   SER B 337     5124   5270   6566    589   -436  -1357       O  
ATOM   2489  CB  SER B 337      29.288  55.489  39.381  1.00 45.06           C  
ANISOU 2489  CB  SER B 337     5067   5344   6711    648   -486  -1460       C  
ATOM   2490  OG  SER B 337      29.423  54.894  38.107  1.00 53.60           O  
ANISOU 2490  OG  SER B 337     6092   6468   7805    641   -451  -1538       O  
ATOM   2491  N   LYS B 338      26.546  56.928  39.213  1.00 46.76           N  
ANISOU 2491  N   LYS B 338     5411   5607   6747    559   -403  -1292       N  
ATOM   2492  CA  LYS B 338      25.450  57.508  38.445  1.00 48.18           C  
ANISOU 2492  CA  LYS B 338     5617   5839   6850    512   -343  -1257       C  
ATOM   2493  C   LYS B 338      25.623  57.251  36.952  1.00 45.95           C  
ANISOU 2493  C   LYS B 338     5273   5622   6563    496   -291  -1335       C  
ATOM   2494  O   LYS B 338      26.748  57.200  36.451  1.00 45.88           O  
ANISOU 2494  O   LYS B 338     5195   5648   6589    507   -281  -1407       O  
ATOM   2495  CB  LYS B 338      25.347  59.015  38.704  1.00 49.92           C  
ANISOU 2495  CB  LYS B 338     5860   6098   7008    482   -315  -1201       C  
ATOM   2496  CG  LYS B 338      24.046  59.638  38.225  1.00 50.16           C  
ANISOU 2496  CG  LYS B 338     5934   6167   6957    443   -267  -1142       C  
ATOM   2497  CD  LYS B 338      24.150  61.149  38.162  1.00 44.31           C  
ANISOU 2497  CD  LYS B 338     5195   5466   6173    411   -236  -1106       C  
ATOM   2498  CE  LYS B 338      25.009  61.585  36.988  1.00 39.78           C  
ANISOU 2498  CE  LYS B 338     4546   4959   5611    383   -183  -1152       C  
ATOM   2499  NZ  LYS B 338      25.284  63.049  37.021  1.00 44.69           N  
ANISOU 2499  NZ  LYS B 338     5160   5601   6220    350   -162  -1110       N  
ATOM   2500  N   ALA B 339      24.503  57.081  36.253  1.00 47.15           N  
ANISOU 2500  N   ALA B 339     5448   5799   6670    473   -260  -1323       N  
ATOM   2501  CA  ALA B 339      24.518  56.864  34.813  1.00 43.18           C  
ANISOU 2501  CA  ALA B 339     4889   5375   6142    464   -212  -1398       C  
ATOM   2502  C   ALA B 339      25.252  57.998  34.114  1.00 44.18           C  
ANISOU 2502  C   ALA B 339     4966   5599   6221    439   -150  -1402       C  
ATOM   2503  O   ALA B 339      25.017  59.167  34.412  1.00 48.56           O  
ANISOU 2503  O   ALA B 339     5552   6169   6730    407   -126  -1323       O  
ATOM   2504  CB  ALA B 339      23.097  56.739  34.278  1.00 29.64           C  
ANISOU 2504  CB  ALA B 339     3212   3678   4373    441   -190  -1371       C  
ATOM   2505  N   LYS B 340      26.148  57.652  33.195  1.00 43.07           N  
ANISOU 2505  N   LYS B 340     4744   5525   6096    457   -126  -1491       N  
ATOM   2506  CA  LYS B 340      26.878  58.654  32.432  1.00 43.90           C  
ANISOU 2506  CA  LYS B 340     4787   5735   6159    432    -60  -1486       C  
ATOM   2507  C   LYS B 340      26.037  59.156  31.260  1.00 47.02           C  
ANISOU 2507  C   LYS B 340     5179   6233   6455    403      9  -1462       C  
ATOM   2508  O   LYS B 340      25.147  58.455  30.781  1.00 43.42           O  
ANISOU 2508  O   LYS B 340     4742   5786   5971    416      4  -1496       O  
ATOM   2509  CB  LYS B 340      28.203  58.079  31.930  1.00 44.91           C  
ANISOU 2509  CB  LYS B 340     4819   5909   6335    468    -57  -1588       C  
ATOM   2510  CG  LYS B 340      29.008  57.328  32.985  1.00 49.82           C  
ANISOU 2510  CG  LYS B 340     5439   6430   7060    509   -133  -1629       C  
ATOM   2511  CD  LYS B 340      30.347  56.856  32.431  1.00 45.61           C  
ANISOU 2511  CD  LYS B 340     4802   5954   6572    546   -126  -1732       C  
ATOM   2512  CE  LYS B 340      30.934  55.739  33.278  1.00 42.16           C  
ANISOU 2512  CE  LYS B 340     4371   5416   6233    592   -213  -1778       C  
ATOM   2513  NZ  LYS B 340      31.154  56.159  34.688  1.00 47.38           N  
ANISOU 2513  NZ  LYS B 340     5078   5982   6944    596   -263  -1721       N  
ATOM   2514  N   GLY B 341      26.315  60.371  30.801  1.00 49.07           N  
ANISOU 2514  N   GLY B 341     5409   6569   6665    365     69  -1400       N  
ATOM   2515  CA  GLY B 341      25.582  60.928  29.681  1.00 46.38           C  
ANISOU 2515  CA  GLY B 341     5062   6336   6226    340    136  -1364       C  
ATOM   2516  C   GLY B 341      25.132  62.354  29.924  1.00 43.97           C  
ANISOU 2516  C   GLY B 341     4797   6025   5884    289    164  -1241       C  
ATOM   2517  O   GLY B 341      24.934  62.765  31.065  1.00 44.81           O  
ANISOU 2517  O   GLY B 341     4965   6031   6032    277    120  -1190       O  
ATOM   2518  N   GLN B 342      24.970  63.105  28.841  1.00 42.95           N  
ANISOU 2518  N   GLN B 342     4632   6009   5679    264    235  -1195       N  
ATOM   2519  CA  GLN B 342      24.557  64.495  28.932  1.00 45.08           C  
ANISOU 2519  CA  GLN B 342     4932   6275   5922    216    263  -1076       C  
ATOM   2520  C   GLN B 342      23.167  64.621  29.555  1.00 43.48           C  
ANISOU 2520  C   GLN B 342     4830   5998   5691    211    229  -1030       C  
ATOM   2521  O   GLN B 342      22.200  64.055  29.042  1.00 45.82           O  
ANISOU 2521  O   GLN B 342     5151   6331   5927    226    235  -1053       O  
ATOM   2522  CB  GLN B 342      24.581  65.145  27.549  1.00 48.35           C  
ANISOU 2522  CB  GLN B 342     5283   6834   6253    196    348  -1028       C  
ATOM   2523  CG  GLN B 342      24.120  66.587  27.535  1.00 55.71           C  
ANISOU 2523  CG  GLN B 342     6243   7760   7165    146    376   -897       C  
ATOM   2524  CD  GLN B 342      24.947  67.466  28.451  1.00 64.95           C  
ANISOU 2524  CD  GLN B 342     7405   8835   8437    113    349   -847       C  
ATOM   2525  OE1 GLN B 342      24.417  68.362  29.107  1.00 70.21           O  
ANISOU 2525  OE1 GLN B 342     8131   9420   9126     88    323   -775       O  
ATOM   2526  NE2 GLN B 342      26.253  67.213  28.505  1.00 66.09           N  
ANISOU 2526  NE2 GLN B 342     7473   8991   8647    117    351   -893       N  
ATOM   2527  N   PRO B 343      23.073  65.351  30.682  1.00 39.64           N  
ANISOU 2527  N   PRO B 343     4398   5413   5252    194    189   -971       N  
ATOM   2528  CA  PRO B 343      21.797  65.586  31.362  1.00 35.45           C  
ANISOU 2528  CA  PRO B 343     3957   4820   4692    193    158   -923       C  
ATOM   2529  C   PRO B 343      20.817  66.318  30.468  1.00 33.49           C  
ANISOU 2529  C   PRO B 343     3724   4644   4358    170    209   -856       C  
ATOM   2530  O   PRO B 343      21.215  67.229  29.746  1.00 36.73           O  
ANISOU 2530  O   PRO B 343     4089   5115   4752    141    258   -802       O  
ATOM   2531  CB  PRO B 343      22.190  66.454  32.561  1.00 31.75           C  
ANISOU 2531  CB  PRO B 343     3518   4259   4287    184    114   -881       C  
ATOM   2532  CG  PRO B 343      23.616  66.132  32.800  1.00 36.49           C  
ANISOU 2532  CG  PRO B 343     4055   4843   4965    193     97   -936       C  
ATOM   2533  CD  PRO B 343      24.199  65.929  31.431  1.00 33.88           C  
ANISOU 2533  CD  PRO B 343     3641   4625   4608    182    164   -961       C  
ATOM   2534  N   ARG B 344      19.550  65.919  30.512  1.00 33.17           N  
ANISOU 2534  N   ARG B 344     3740   4597   4265    182    196   -852       N  
ATOM   2535  CA  ARG B 344      18.523  66.595  29.736  1.00 39.43           C  
ANISOU 2535  CA  ARG B 344     4552   5456   4974    165    236   -790       C  
ATOM   2536  C   ARG B 344      17.366  67.027  30.624  1.00 39.54           C  
ANISOU 2536  C   ARG B 344     4648   5400   4975    166    201   -736       C  
ATOM   2537  O   ARG B 344      16.860  66.249  31.430  1.00 37.80           O  
ANISOU 2537  O   ARG B 344     4469   5120   4772    187    157   -766       O  
ATOM   2538  CB  ARG B 344      18.032  65.697  28.602  1.00 41.57           C  
ANISOU 2538  CB  ARG B 344     4794   5823   5177    183    264   -848       C  
ATOM   2539  CG  ARG B 344      19.087  65.440  27.541  1.00 48.48           C  
ANISOU 2539  CG  ARG B 344     5580   6801   6039    190    310   -897       C  
ATOM   2540  CD  ARG B 344      18.487  65.484  26.151  1.00 58.97           C  
ANISOU 2540  CD  ARG B 344     6877   8269   7260    197    363   -895       C  
ATOM   2541  NE  ARG B 344      18.563  64.188  25.485  1.00 66.92           N  
ANISOU 2541  NE  ARG B 344     7842   9338   8248    237    356  -1017       N  
ATOM   2542  CZ  ARG B 344      17.674  63.752  24.602  1.00 63.30           C  
ANISOU 2542  CZ  ARG B 344     7378   8963   7709    258    366  -1057       C  
ATOM   2543  NH1 ARG B 344      17.824  62.558  24.044  1.00 51.14           N  
ANISOU 2543  NH1 ARG B 344     5795   7469   6168    299    349  -1183       N  
ATOM   2544  NH2 ARG B 344      16.634  64.510  24.280  1.00 54.55           N  
ANISOU 2544  NH2 ARG B 344     6307   7892   6528    242    387   -977       N  
ATOM   2545  N   GLU B 345      16.958  68.280  30.473  1.00 40.85           N  
ANISOU 2545  N   GLU B 345     4833   5576   5114    145    221   -653       N  
ATOM   2546  CA  GLU B 345      15.913  68.861  31.302  1.00 37.62           C  
ANISOU 2546  CA  GLU B 345     4495   5108   4691    151    189   -603       C  
ATOM   2547  C   GLU B 345      14.529  68.337  30.937  1.00 38.45           C  
ANISOU 2547  C   GLU B 345     4634   5254   4721    162    195   -604       C  
ATOM   2548  O   GLU B 345      14.123  68.401  29.778  1.00 36.85           O  
ANISOU 2548  O   GLU B 345     4407   5140   4454    155    239   -593       O  
ATOM   2549  CB  GLU B 345      15.946  70.383  31.188  1.00 40.95           C  
ANISOU 2549  CB  GLU B 345     4920   5520   5120    127    203   -520       C  
ATOM   2550  CG  GLU B 345      14.961  71.105  32.083  1.00 53.06           C  
ANISOU 2550  CG  GLU B 345     6522   6992   6645    142    164   -478       C  
ATOM   2551  CD  GLU B 345      14.954  72.599  31.831  1.00 57.04           C  
ANISOU 2551  CD  GLU B 345     7024   7481   7167    120    173   -399       C  
ATOM   2552  OE1 GLU B 345      15.396  73.019  30.742  1.00 41.22           O  
ANISOU 2552  OE1 GLU B 345     4969   5536   5156     90    224   -356       O  
ATOM   2553  OE2 GLU B 345      14.511  73.355  32.723  1.00 70.96           O  
ANISOU 2553  OE2 GLU B 345     8833   9175   8953    136    129   -379       O  
ATOM   2554  N   PRO B 346      13.797  67.818  31.933  1.00 35.22           N  
ANISOU 2554  N   PRO B 346     4276   4788   4320    183    152   -614       N  
ATOM   2555  CA  PRO B 346      12.433  67.332  31.705  1.00 28.78           C  
ANISOU 2555  CA  PRO B 346     3488   4002   3446    190    154   -609       C  
ATOM   2556  C   PRO B 346      11.445  68.457  31.419  1.00 28.64           C  
ANISOU 2556  C   PRO B 346     3500   4017   3366    185    172   -537       C  
ATOM   2557  O   PRO B 346      11.636  69.590  31.863  1.00 28.55           O  
ANISOU 2557  O   PRO B 346     3507   3970   3371    183    164   -487       O  
ATOM   2558  CB  PRO B 346      12.083  66.634  33.023  1.00 26.94           C  
ANISOU 2558  CB  PRO B 346     3294   3693   3249    212    103   -618       C  
ATOM   2559  CG  PRO B 346      12.949  67.289  34.039  1.00 28.53           C  
ANISOU 2559  CG  PRO B 346     3508   3832   3500    222     74   -604       C  
ATOM   2560  CD  PRO B 346      14.233  67.611  33.325  1.00 32.39           C  
ANISOU 2560  CD  PRO B 346     3944   4340   4023    203     99   -627       C  
ATOM   2561  N   GLN B 347      10.404  68.137  30.658  1.00 29.64           N  
ANISOU 2561  N   GLN B 347     3626   4207   3429    185    191   -537       N  
ATOM   2562  CA  GLN B 347       9.247  69.009  30.529  1.00 28.12           C  
ANISOU 2562  CA  GLN B 347     3467   4040   3177    188    199   -474       C  
ATOM   2563  C   GLN B 347       8.127  68.400  31.356  1.00 26.82           C  
ANISOU 2563  C   GLN B 347     3340   3846   3006    205    167   -477       C  
ATOM   2564  O   GLN B 347       7.851  67.208  31.249  1.00 31.96           O  
ANISOU 2564  O   GLN B 347     3975   4502   3667    204    158   -525       O  
ATOM   2565  CB  GLN B 347       8.830  69.168  29.064  1.00 29.26           C  
ANISOU 2565  CB  GLN B 347     3580   4291   3248    181    243   -465       C  
ATOM   2566  CG  GLN B 347       9.800  69.981  28.222  1.00 39.46           C  
ANISOU 2566  CG  GLN B 347     4831   5628   4533    165    283   -430       C  
ATOM   2567  CD  GLN B 347       9.654  71.477  28.442  1.00 45.47           C  
ANISOU 2567  CD  GLN B 347     5619   6358   5299    158    285   -337       C  
ATOM   2568  OE1 GLN B 347       8.578  71.960  28.801  1.00 42.84           O  
ANISOU 2568  OE1 GLN B 347     5330   6009   4939    171    267   -300       O  
ATOM   2569  NE2 GLN B 347      10.736  72.215  28.233  1.00 40.31           N  
ANISOU 2569  NE2 GLN B 347     4933   5692   4688    137    303   -299       N  
ATOM   2570  N   VAL B 348       7.499  69.214  32.196  1.00 30.85           N  
ANISOU 2570  N   VAL B 348     3894   4324   3504    220    148   -425       N  
ATOM   2571  CA  VAL B 348       6.436  68.724  33.060  1.00 20.32           C  
ANISOU 2571  CA  VAL B 348     2590   2973   2158    239    123   -415       C  
ATOM   2572  C   VAL B 348       5.074  69.266  32.647  1.00 25.08           C  
ANISOU 2572  C   VAL B 348     3207   3629   2691    246    136   -374       C  
ATOM   2573  O   VAL B 348       4.861  70.473  32.613  1.00 34.91           O  
ANISOU 2573  O   VAL B 348     4473   4879   3911    256    140   -330       O  
ATOM   2574  CB  VAL B 348       6.701  69.085  34.530  1.00 24.45           C  
ANISOU 2574  CB  VAL B 348     3147   3431   2712    266     86   -398       C  
ATOM   2575  CG1 VAL B 348       5.640  68.463  35.412  1.00 17.62           C  
ANISOU 2575  CG1 VAL B 348     2303   2566   1828    287     67   -378       C  
ATOM   2576  CG2 VAL B 348       8.077  68.604  34.946  1.00 19.51           C  
ANISOU 2576  CG2 VAL B 348     2505   2753   2154    263     69   -438       C  
ATOM   2577  N   TYR B 349       4.155  68.358  32.331  1.00 27.56           N  
ANISOU 2577  N   TYR B 349     3508   3979   2985    240    139   -391       N  
ATOM   2578  CA  TYR B 349       2.806  68.739  31.933  1.00 22.82           C  
ANISOU 2578  CA  TYR B 349     2915   3434   2321    247    148   -358       C  
ATOM   2579  C   TYR B 349       1.754  68.053  32.796  1.00 32.51           C  
ANISOU 2579  C   TYR B 349     4150   4651   3552    256    128   -344       C  
ATOM   2580  O   TYR B 349       1.812  66.843  33.008  1.00 32.49           O  
ANISOU 2580  O   TYR B 349     4126   4623   3596    241    115   -374       O  
ATOM   2581  CB  TYR B 349       2.558  68.396  30.461  1.00 20.44           C  
ANISOU 2581  CB  TYR B 349     2576   3210   1981    230    172   -391       C  
ATOM   2582  CG  TYR B 349       3.560  68.977  29.491  1.00 24.93           C  
ANISOU 2582  CG  TYR B 349     3124   3812   2535    222    201   -395       C  
ATOM   2583  CD1 TYR B 349       3.581  70.336  29.211  1.00 17.02           C  
ANISOU 2583  CD1 TYR B 349     2139   2828   1499    229    217   -331       C  
ATOM   2584  CD2 TYR B 349       4.467  68.162  28.834  1.00 25.40           C  
ANISOU 2584  CD2 TYR B 349     3143   3891   2618    209    211   -458       C  
ATOM   2585  CE1 TYR B 349       4.491  70.867  28.317  1.00 26.85           C  
ANISOU 2585  CE1 TYR B 349     3357   4109   2735    217    248   -317       C  
ATOM   2586  CE2 TYR B 349       5.380  68.683  27.935  1.00 34.07           C  
ANISOU 2586  CE2 TYR B 349     4213   5037   3695    203    244   -454       C  
ATOM   2587  CZ  TYR B 349       5.385  70.035  27.679  1.00 36.43           C  
ANISOU 2587  CZ  TYR B 349     4526   5354   3961    204    265   -376       C  
ATOM   2588  OH  TYR B 349       6.293  70.556  26.788  1.00 42.01           O  
ANISOU 2588  OH  TYR B 349     5198   6113   4652    194    301   -355       O  
ATOM   2589  N   THR B 350       0.787  68.828  33.281  1.00 33.76           N  
ANISOU 2589  N   THR B 350     4333   4828   3664    281    125   -295       N  
ATOM   2590  CA  THR B 350      -0.347  68.265  33.998  1.00 29.44           C  
ANISOU 2590  CA  THR B 350     3784   4292   3108    289    114   -270       C  
ATOM   2591  C   THR B 350      -1.551  68.139  33.069  1.00 33.04           C  
ANISOU 2591  C   THR B 350     4216   4816   3522    278    127   -270       C  
ATOM   2592  O   THR B 350      -1.800  69.017  32.244  1.00 39.54           O  
ANISOU 2592  O   THR B 350     5044   5685   4294    286    141   -262       O  
ATOM   2593  CB  THR B 350      -0.736  69.115  35.224  1.00 26.34           C  
ANISOU 2593  CB  THR B 350     3427   3894   2687    334    101   -223       C  
ATOM   2594  OG1 THR B 350      -1.081  70.439  34.803  1.00 30.93           O  
ANISOU 2594  OG1 THR B 350     4028   4503   3220    356    106   -205       O  
ATOM   2595  CG2 THR B 350       0.415  69.183  36.213  1.00 24.89           C  
ANISOU 2595  CG2 THR B 350     3263   3649   2544    351     80   -231       C  
ATOM   2596  N   LEU B 351      -2.286  67.038  33.196  1.00 29.08           N  
ANISOU 2596  N   LEU B 351     3683   4319   3047    260    119   -275       N  
ATOM   2597  CA  LEU B 351      -3.480  66.814  32.391  1.00 23.23           C  
ANISOU 2597  CA  LEU B 351     2911   3640   2276    249    124   -282       C  
ATOM   2598  C   LEU B 351      -4.667  66.505  33.293  1.00 20.79           C  
ANISOU 2598  C   LEU B 351     2590   3342   1967    255    118   -230       C  
ATOM   2599  O   LEU B 351      -4.565  65.661  34.183  1.00 24.99           O  
ANISOU 2599  O   LEU B 351     3111   3828   2554    244    107   -210       O  
ATOM   2600  CB  LEU B 351      -3.270  65.662  31.399  1.00 24.27           C  
ANISOU 2600  CB  LEU B 351     2997   3772   2453    214    115   -354       C  
ATOM   2601  CG  LEU B 351      -1.890  65.428  30.783  1.00 31.18           C  
ANISOU 2601  CG  LEU B 351     3868   4623   3354    205    118   -414       C  
ATOM   2602  CD1 LEU B 351      -1.917  64.181  29.919  1.00 36.32           C  
ANISOU 2602  CD1 LEU B 351     4467   5280   4054    181    101   -496       C  
ATOM   2603  CD2 LEU B 351      -1.458  66.618  29.966  1.00 33.30           C  
ANISOU 2603  CD2 LEU B 351     4154   4945   3552    222    143   -407       C  
ATOM   2604  N   PRO B 352      -5.802  67.182  33.062  1.00 27.60           N  
ANISOU 2604  N   PRO B 352     3450   4269   2767    274    125   -203       N  
ATOM   2605  CA  PRO B 352      -7.025  66.995  33.851  1.00 23.32           C  
ANISOU 2605  CA  PRO B 352     2889   3758   2215    283    125   -151       C  
ATOM   2606  C   PRO B 352      -7.709  65.670  33.522  1.00 25.09           C  
ANISOU 2606  C   PRO B 352     3052   3980   2501    237    115   -166       C  
ATOM   2607  O   PRO B 352      -7.297  65.012  32.572  1.00 26.22           O  
ANISOU 2607  O   PRO B 352     3172   4105   2685    206    103   -231       O  
ATOM   2608  CB  PRO B 352      -7.889  68.187  33.429  1.00 23.11           C  
ANISOU 2608  CB  PRO B 352     2874   3801   2105    319    133   -134       C  
ATOM   2609  CG  PRO B 352      -7.486  68.440  32.025  1.00 20.97           C  
ANISOU 2609  CG  PRO B 352     2604   3550   1816    306    135   -184       C  
ATOM   2610  CD  PRO B 352      -6.001  68.152  31.969  1.00 25.49           C  
ANISOU 2610  CD  PRO B 352     3192   4058   2433    289    135   -217       C  
ATOM   2611  N   PRO B 353      -8.728  65.278  34.301  1.00 35.03           N  
ANISOU 2611  N   PRO B 353     4279   5258   3771    234    117   -108       N  
ATOM   2612  CA  PRO B 353      -9.436  64.036  33.975  1.00 32.22           C  
ANISOU 2612  CA  PRO B 353     3857   4891   3493    184    102   -117       C  
ATOM   2613  C   PRO B 353     -10.094  64.084  32.602  1.00 31.75           C  
ANISOU 2613  C   PRO B 353     3767   4883   3414    172     91   -181       C  
ATOM   2614  O   PRO B 353     -10.514  65.155  32.159  1.00 34.67           O  
ANISOU 2614  O   PRO B 353     4158   5321   3694    207    103   -181       O  
ATOM   2615  CB  PRO B 353     -10.501  63.937  35.079  1.00 28.41           C  
ANISOU 2615  CB  PRO B 353     3346   4443   3005    192    115    -25       C  
ATOM   2616  CG  PRO B 353      -9.979  64.759  36.196  1.00 32.91           C  
ANISOU 2616  CG  PRO B 353     3969   5020   3514    244    131     24       C  
ATOM   2617  CD  PRO B 353      -9.215  65.879  35.557  1.00 35.14           C  
ANISOU 2617  CD  PRO B 353     4310   5305   3737    277    131    -32       C  
ATOM   2618  N   SER B 354     -10.169  62.938  31.937  1.00 27.56           N  
ANISOU 2618  N   SER B 354     3184   4319   2967    127     64   -239       N  
ATOM   2619  CA  SER B 354     -10.970  62.813  30.730  1.00 31.31           C  
ANISOU 2619  CA  SER B 354     3615   4851   3430    117     46   -304       C  
ATOM   2620  C   SER B 354     -12.416  63.122  31.082  1.00 35.68           C  
ANISOU 2620  C   SER B 354     4135   5468   3953    122     54   -242       C  
ATOM   2621  O   SER B 354     -12.854  62.842  32.196  1.00 35.92           O  
ANISOU 2621  O   SER B 354     4149   5480   4018    113     65   -161       O  
ATOM   2622  CB  SER B 354     -10.848  61.407  30.134  1.00 31.75           C  
ANISOU 2622  CB  SER B 354     3612   4849   3602     69      5   -383       C  
ATOM   2623  OG  SER B 354     -12.049  61.013  29.489  1.00 41.86           O  
ANISOU 2623  OG  SER B 354     4826   6173   4904     50    -21   -417       O  
ATOM   2624  N   ARG B 355     -13.149  63.716  30.145  1.00 46.56           N  
ANISOU 2624  N   ARG B 355     5502   6929   5261    143     49   -277       N  
ATOM   2625  CA  ARG B 355     -14.564  64.005  30.363  1.00 44.65           C  
ANISOU 2625  CA  ARG B 355     5221   6755   4990    151     54   -230       C  
ATOM   2626  C   ARG B 355     -15.328  62.722  30.674  1.00 40.66           C  
ANISOU 2626  C   ARG B 355     4632   6213   4603     94     32   -217       C  
ATOM   2627  O   ARG B 355     -16.241  62.716  31.500  1.00 39.31           O  
ANISOU 2627  O   ARG B 355     4427   6068   4440     90     47   -136       O  
ATOM   2628  CB  ARG B 355     -15.174  64.707  29.150  1.00 59.09           C  
ANISOU 2628  CB  ARG B 355     7043   8676   6734    181     43   -281       C  
ATOM   2629  CG  ARG B 355     -14.734  64.143  27.808  1.00 78.77           C  
ANISOU 2629  CG  ARG B 355     9513  11173   9243    165     12   -391       C  
ATOM   2630  CD  ARG B 355     -15.705  64.517  26.699  1.00 89.04           C  
ANISOU 2630  CD  ARG B 355    10778  12575  10476    188     -8   -437       C  
ATOM   2631  NE  ARG B 355     -16.983  63.821  26.835  1.00 96.16           N  
ANISOU 2631  NE  ARG B 355    11601  13491  11445    157    -34   -437       N  
ATOM   2632  CZ  ARG B 355     -18.141  64.425  27.082  1.00102.22           C  
ANISOU 2632  CZ  ARG B 355    12348  14327  12164    178    -25   -384       C  
ATOM   2633  NH1 ARG B 355     -19.255  63.712  27.191  1.00104.05           N  
ANISOU 2633  NH1 ARG B 355    12497  14569  12469    143    -48   -384       N  
ATOM   2634  NH2 ARG B 355     -18.188  65.743  27.213  1.00101.13           N  
ANISOU 2634  NH2 ARG B 355    12266  14243  11914    236      5   -331       N  
ATOM   2635  N   GLU B 356     -14.931  61.635  30.018  1.00 39.62           N  
ANISOU 2635  N   GLU B 356     4464   6021   4569     51     -6   -297       N  
ATOM   2636  CA  GLU B 356     -15.556  60.331  30.214  1.00 39.03           C  
ANISOU 2636  CA  GLU B 356     4305   5888   4636    -10    -39   -295       C  
ATOM   2637  C   GLU B 356     -15.404  59.811  31.638  1.00 35.87           C  
ANISOU 2637  C   GLU B 356     3900   5419   4311    -36    -18   -181       C  
ATOM   2638  O   GLU B 356     -16.252  59.062  32.121  1.00 41.93           O  
ANISOU 2638  O   GLU B 356     4594   6165   5172    -81    -26   -122       O  
ATOM   2639  CB  GLU B 356     -14.974  59.311  29.236  1.00 50.48           C  
ANISOU 2639  CB  GLU B 356     5724   7275   6181    -40    -91   -419       C  
ATOM   2640  CG  GLU B 356     -15.473  59.444  27.807  1.00 66.06           C  
ANISOU 2640  CG  GLU B 356     7665   9326   8108    -24   -126   -535       C  
ATOM   2641  CD  GLU B 356     -14.990  58.305  26.923  1.00 89.07           C  
ANISOU 2641  CD  GLU B 356    10534  12180  11127    -49   -186   -668       C  
ATOM   2642  OE1 GLU B 356     -13.804  57.922  27.039  1.00 93.72           O  
ANISOU 2642  OE1 GLU B 356    11157  12698  11755    -50   -188   -697       O  
ATOM   2643  OE2 GLU B 356     -15.800  57.789  26.120  1.00 97.44           O  
ANISOU 2643  OE2 GLU B 356    11523  13266  12233    -64   -236   -751       O  
ATOM   2644  N   GLU B 357     -14.328  60.208  32.311  1.00 30.64           N  
ANISOU 2644  N   GLU B 357     3309   4726   3608     -9      9   -146       N  
ATOM   2645  CA  GLU B 357     -14.062  59.705  33.656  1.00 30.99           C  
ANISOU 2645  CA  GLU B 357     3351   4711   3711    -24     26    -40       C  
ATOM   2646  C   GLU B 357     -14.874  60.455  34.714  1.00 34.21           C  
ANISOU 2646  C   GLU B 357     3760   5202   4035      9     70     76       C  
ATOM   2647  O   GLU B 357     -14.988  59.999  35.851  1.00 36.81           O  
ANISOU 2647  O   GLU B 357     4067   5513   4405     -3     88    181       O  
ATOM   2648  CB  GLU B 357     -12.569  59.795  33.988  1.00 28.10           C  
ANISOU 2648  CB  GLU B 357     3056   4283   3337     -3     31    -55       C  
ATOM   2649  CG  GLU B 357     -12.154  58.931  35.178  1.00 29.94           C  
ANISOU 2649  CG  GLU B 357     3277   4437   3662    -27     32     35       C  
ATOM   2650  CD  GLU B 357     -10.727  59.175  35.626  1.00 35.50           C  
ANISOU 2650  CD  GLU B 357     4053   5096   4341      4     39     27       C  
ATOM   2651  OE1 GLU B 357     -10.193  58.343  36.388  1.00 34.54           O  
ANISOU 2651  OE1 GLU B 357     3922   4896   4306    -16     29     79       O  
ATOM   2652  OE2 GLU B 357     -10.139  60.200  35.222  1.00 37.24           O  
ANISOU 2652  OE2 GLU B 357     4334   5355   4459     47     52    -27       O  
ATOM   2653  N   MET B 358     -15.462  61.588  34.333  1.00 35.79           N  
ANISOU 2653  N   MET B 358     3982   5500   4117     55     87     59       N  
ATOM   2654  CA  MET B 358     -16.199  62.426  35.278  1.00 40.51           C  
ANISOU 2654  CA  MET B 358     4584   6186   4622    103    125    149       C  
ATOM   2655  C   MET B 358     -17.504  61.794  35.775  1.00 42.09           C  
ANISOU 2655  C   MET B 358     4690   6426   4878     68    135    232       C  
ATOM   2656  O   MET B 358     -18.214  62.391  36.584  1.00 48.41           O  
ANISOU 2656  O   MET B 358     5478   7312   5602    108    169    310       O  
ATOM   2657  CB  MET B 358     -16.496  63.787  34.649  1.00 47.36           C  
ANISOU 2657  CB  MET B 358     5495   7137   5364    163    132    102       C  
ATOM   2658  CG  MET B 358     -15.260  64.637  34.397  1.00 54.18           C  
ANISOU 2658  CG  MET B 358     6450   7974   6163    204    133     52       C  
ATOM   2659  SD  MET B 358     -14.362  65.048  35.910  1.00 46.79           S  
ANISOU 2659  SD  MET B 358     5574   7013   5193    248    157    122       S  
ATOM   2660  CE  MET B 358     -15.556  66.072  36.771  1.00 44.42           C  
ANISOU 2660  CE  MET B 358     5262   6829   4787    316    184    191       C  
ATOM   2661  N   THR B 359     -17.819  60.593  35.296  1.00 39.02           N  
ANISOU 2661  N   THR B 359     4228   5974   4625     -5    102    214       N  
ATOM   2662  CA  THR B 359     -18.997  59.869  35.768  1.00 44.98           C  
ANISOU 2662  CA  THR B 359     4881   6749   5459    -52    108    301       C  
ATOM   2663  C   THR B 359     -18.667  58.968  36.958  1.00 46.26           C  
ANISOU 2663  C   THR B 359     5017   6849   5711    -86    124    421       C  
ATOM   2664  O   THR B 359     -19.562  58.381  37.565  1.00 52.85           O  
ANISOU 2664  O   THR B 359     5766   7705   6612   -124    139    526       O  
ATOM   2665  CB  THR B 359     -19.624  59.014  34.646  1.00 52.64           C  
ANISOU 2665  CB  THR B 359     5773   7679   6550   -116     56    221       C  
ATOM   2666  OG1 THR B 359     -18.670  58.051  34.178  1.00 52.45           O  
ANISOU 2666  OG1 THR B 359     5755   7529   6645   -160     12    151       O  
ATOM   2667  CG2 THR B 359     -20.059  59.897  33.489  1.00 42.90           C  
ANISOU 2667  CG2 THR B 359     4557   6525   5217    -77     41    115       C  
ATOM   2668  N   LYS B 360     -17.383  58.864  37.287  1.00 38.40           N  
ANISOU 2668  N   LYS B 360     4090   5782   4718    -71    121    411       N  
ATOM   2669  CA  LYS B 360     -16.943  58.029  38.397  1.00 34.10           C  
ANISOU 2669  CA  LYS B 360     3528   5177   4253    -96    132    524       C  
ATOM   2670  C   LYS B 360     -16.870  58.835  39.691  1.00 42.44           C  
ANISOU 2670  C   LYS B 360     4623   6328   5174    -25    185    626       C  
ATOM   2671  O   LYS B 360     -16.909  60.061  39.664  1.00 44.37           O  
ANISOU 2671  O   LYS B 360     4923   6660   5275     45    204    586       O  
ATOM   2672  CB  LYS B 360     -15.581  57.403  38.091  1.00 39.42           C  
ANISOU 2672  CB  LYS B 360     4248   5721   5008   -115     94    455       C  
ATOM   2673  CG  LYS B 360     -15.490  56.699  36.747  1.00 54.65           C  
ANISOU 2673  CG  LYS B 360     6148   7565   7052   -167     36    324       C  
ATOM   2674  CD  LYS B 360     -16.221  55.368  36.745  1.00 61.46           C  
ANISOU 2674  CD  LYS B 360     6904   8350   8100   -249      3    372       C  
ATOM   2675  CE  LYS B 360     -16.098  54.686  35.389  1.00 62.98           C  
ANISOU 2675  CE  LYS B 360     7065   8460   8404   -289    -66    218       C  
ATOM   2676  NZ  LYS B 360     -16.869  53.412  35.326  1.00 58.63           N  
ANISOU 2676  NZ  LYS B 360     6402   7822   8052   -371   -110    251       N  
ATOM   2677  N   ASN B 361     -16.760  58.141  40.820  1.00 48.07           N  
ANISOU 2677  N   ASN B 361     5304   7025   5935    -39    204    757       N  
ATOM   2678  CA  ASN B 361     -16.635  58.803  42.112  1.00 49.85           C  
ANISOU 2678  CA  ASN B 361     5560   7349   6031     36    250    852       C  
ATOM   2679  C   ASN B 361     -15.221  59.306  42.349  1.00 48.82           C  
ANISOU 2679  C   ASN B 361     5533   7180   5837     90    239    792       C  
ATOM   2680  O   ASN B 361     -15.006  60.255  43.103  1.00 50.59           O  
ANISOU 2680  O   ASN B 361     5806   7491   5925    172    264    807       O  
ATOM   2681  CB  ASN B 361     -17.044  57.859  43.238  1.00 51.18           C  
ANISOU 2681  CB  ASN B 361     5651   7531   6266      5    276   1027       C  
ATOM   2682  CG  ASN B 361     -18.482  57.412  43.123  1.00 66.98           C  
ANISOU 2682  CG  ASN B 361     7538   9581   8330    -49    293   1103       C  
ATOM   2683  OD1 ASN B 361     -19.334  58.152  42.636  1.00 68.06           O  
ANISOU 2683  OD1 ASN B 361     7661   9806   8394    -27    304   1051       O  
ATOM   2684  ND2 ASN B 361     -18.761  56.194  43.573  1.00 76.15           N  
ANISOU 2684  ND2 ASN B 361     8615  10684   9636   -120    293   1231       N  
ATOM   2685  N   GLN B 362     -14.257  58.654  41.709  1.00 45.14           N  
ANISOU 2685  N   GLN B 362     5093   6582   5475     47    197    719       N  
ATOM   2686  CA  GLN B 362     -12.862  59.075  41.781  1.00 35.24           C  
ANISOU 2686  CA  GLN B 362     3929   5281   4178     90    182    650       C  
ATOM   2687  C   GLN B 362     -12.327  59.377  40.389  1.00 36.66           C  
ANISOU 2687  C   GLN B 362     4152   5404   4375     76    150    495       C  
ATOM   2688  O   GLN B 362     -12.662  58.691  39.422  1.00 42.65           O  
ANISOU 2688  O   GLN B 362     4866   6107   5234     16    122    440       O  
ATOM   2689  CB  GLN B 362     -12.006  58.005  42.455  1.00 36.17           C  
ANISOU 2689  CB  GLN B 362     4041   5304   4398     64    166    716       C  
ATOM   2690  CG  GLN B 362     -12.471  57.635  43.855  1.00 42.75           C  
ANISOU 2690  CG  GLN B 362     4829   6203   5213     80    200    888       C  
ATOM   2691  CD  GLN B 362     -11.312  57.346  44.792  1.00 60.29           C  
ANISOU 2691  CD  GLN B 362     7091   8385   7431    114    193    937       C  
ATOM   2692  OE1 GLN B 362     -10.694  56.282  44.733  1.00 66.27           O  
ANISOU 2692  OE1 GLN B 362     7833   9022   8324     65    161    955       O  
ATOM   2693  NE2 GLN B 362     -11.007  58.302  45.662  1.00 68.24           N  
ANISOU 2693  NE2 GLN B 362     8148   9493   8286    202    216    952       N  
ATOM   2694  N   VAL B 363     -11.496  60.408  40.285  1.00 28.74           N  
ANISOU 2694  N   VAL B 363     3229   4418   3273    133    151    423       N  
ATOM   2695  CA  VAL B 363     -10.935  60.796  38.995  1.00 25.70           C  
ANISOU 2695  CA  VAL B 363     2882   3995   2886    126    128    291       C  
ATOM   2696  C   VAL B 363      -9.416  60.820  39.017  1.00 28.20           C  
ANISOU 2696  C   VAL B 363     3260   4239   3216    141    111    237       C  
ATOM   2697  O   VAL B 363      -8.791  60.930  40.073  1.00 28.89           O  
ANISOU 2697  O   VAL B 363     3377   4323   3277    176    118    290       O  
ATOM   2698  CB  VAL B 363     -11.445  62.178  38.548  1.00 30.85           C  
ANISOU 2698  CB  VAL B 363     3567   4741   3412    176    145    248       C  
ATOM   2699  CG1 VAL B 363     -12.930  62.109  38.212  1.00 24.52           C  
ANISOU 2699  CG1 VAL B 363     2700   4007   2608    156    154    275       C  
ATOM   2700  CG2 VAL B 363     -11.166  63.232  39.616  1.00 21.12           C  
ANISOU 2700  CG2 VAL B 363     2388   3568   2068    252    166    288       C  
ATOM   2701  N   SER B 364      -8.822  60.722  37.836  1.00 30.58           N  
ANISOU 2701  N   SER B 364     3574   4491   3553    118     88    128       N  
ATOM   2702  CA  SER B 364      -7.375  60.651  37.719  1.00 24.05           C  
ANISOU 2702  CA  SER B 364     2792   3594   2750    126     72     69       C  
ATOM   2703  C   SER B 364      -6.794  61.982  37.275  1.00 28.60           C  
ANISOU 2703  C   SER B 364     3431   4213   3224    171     84      8       C  
ATOM   2704  O   SER B 364      -7.182  62.526  36.241  1.00 31.49           O  
ANISOU 2704  O   SER B 364     3797   4621   3548    170     87    -48       O  
ATOM   2705  CB  SER B 364      -6.972  59.556  36.730  1.00 23.50           C  
ANISOU 2705  CB  SER B 364     2688   3443   2798     74     37    -13       C  
ATOM   2706  OG  SER B 364      -7.702  58.361  36.955  1.00 27.39           O  
ANISOU 2706  OG  SER B 364     3112   3889   3404     25     19     38       O  
ATOM   2707  N   LEU B 365      -5.865  62.506  38.071  1.00 33.82           N  
ANISOU 2707  N   LEU B 365     4140   4860   3848    212     87     23       N  
ATOM   2708  CA  LEU B 365      -5.062  63.650  37.654  1.00 27.82           C  
ANISOU 2708  CA  LEU B 365     3435   4112   3024    245     90    -36       C  
ATOM   2709  C   LEU B 365      -3.713  63.143  37.153  1.00 30.26           C  
ANISOU 2709  C   LEU B 365     3753   4345   3399    224     72   -104       C  
ATOM   2710  O   LEU B 365      -3.047  62.352  37.825  1.00 28.75           O  
ANISOU 2710  O   LEU B 365     3557   4094   3272    218     57    -85       O  
ATOM   2711  CB  LEU B 365      -4.884  64.649  38.794  1.00 25.31           C  
ANISOU 2711  CB  LEU B 365     3160   3828   2630    307     96      8       C  
ATOM   2712  CG  LEU B 365      -6.165  65.150  39.470  1.00 31.35           C  
ANISOU 2712  CG  LEU B 365     3912   4678   3321    342    114     74       C  
ATOM   2713  CD1 LEU B 365      -5.867  66.295  40.420  1.00 33.62           C  
ANISOU 2713  CD1 LEU B 365     4245   5000   3527    416    111     84       C  
ATOM   2714  CD2 LEU B 365      -7.199  65.567  38.446  1.00 27.61           C  
ANISOU 2714  CD2 LEU B 365     3420   4255   2816    329    125     52       C  
ATOM   2715  N   THR B 366      -3.312  63.596  35.971  1.00 28.32           N  
ANISOU 2715  N   THR B 366     3516   4110   3136    216     75   -178       N  
ATOM   2716  CA  THR B 366      -2.141  63.037  35.311  1.00 18.65           C  
ANISOU 2716  CA  THR B 366     2285   2830   1970    196     62   -251       C  
ATOM   2717  C   THR B 366      -0.997  64.043  35.213  1.00 24.45           C  
ANISOU 2717  C   THR B 366     3062   3564   2665    222     71   -278       C  
ATOM   2718  O   THR B 366      -1.208  65.212  34.903  1.00 27.94           O  
ANISOU 2718  O   THR B 366     3528   4054   3035    243     87   -271       O  
ATOM   2719  CB  THR B 366      -2.504  62.535  33.900  1.00 21.76           C  
ANISOU 2719  CB  THR B 366     2639   3247   2384    165     58   -324       C  
ATOM   2720  OG1 THR B 366      -3.474  61.488  34.006  1.00 26.32           O  
ANISOU 2720  OG1 THR B 366     3168   3807   3025    134     40   -307       O  
ATOM   2721  CG2 THR B 366      -1.275  62.009  33.173  1.00 20.13           C  
ANISOU 2721  CG2 THR B 366     2421   3000   2226    154     46   -410       C  
ATOM   2722  N   CYS B 367       0.217  63.579  35.494  1.00 21.02           N  
ANISOU 2722  N   CYS B 367     2631   3068   2287    220     57   -306       N  
ATOM   2723  CA  CYS B 367       1.405  64.398  35.312  1.00 20.36           C  
ANISOU 2723  CA  CYS B 367     2574   2977   2186    236     62   -337       C  
ATOM   2724  C   CYS B 367       2.376  63.736  34.338  1.00 30.69           C  
ANISOU 2724  C   CYS B 367     3853   4263   3546    213     60   -417       C  
ATOM   2725  O   CYS B 367       2.992  62.723  34.654  1.00 31.13           O  
ANISOU 2725  O   CYS B 367     3891   4260   3676    205     38   -441       O  
ATOM   2726  CB  CYS B 367       2.095  64.657  36.650  1.00 21.98           C  
ANISOU 2726  CB  CYS B 367     2809   3141   2400    267     46   -303       C  
ATOM   2727  SG  CYS B 367       3.512  65.764  36.557  1.00 28.68           S  
ANISOU 2727  SG  CYS B 367     3683   3971   3242    285     46   -337       S  
ATOM   2728  N   LEU B 368       2.500  64.316  33.147  1.00 28.65           N  
ANISOU 2728  N   LEU B 368     3585   4058   3242    207     82   -455       N  
ATOM   2729  CA  LEU B 368       3.432  63.816  32.146  1.00 23.94           C  
ANISOU 2729  CA  LEU B 368     2955   3466   2674    195     86   -533       C  
ATOM   2730  C   LEU B 368       4.786  64.503  32.266  1.00 25.47           C  
ANISOU 2730  C   LEU B 368     3162   3644   2872    205     96   -538       C  
ATOM   2731  O   LEU B 368       4.878  65.727  32.214  1.00 28.81           O  
ANISOU 2731  O   LEU B 368     3609   4093   3245    214    115   -499       O  
ATOM   2732  CB  LEU B 368       2.858  64.011  30.738  1.00 23.89           C  
ANISOU 2732  CB  LEU B 368     2922   3546   2608    189    106   -569       C  
ATOM   2733  CG  LEU B 368       3.819  63.863  29.557  1.00 25.39           C  
ANISOU 2733  CG  LEU B 368     3076   3780   2789    189    122   -643       C  
ATOM   2734  CD1 LEU B 368       4.402  62.463  29.503  1.00 21.70           C  
ANISOU 2734  CD1 LEU B 368     2572   3265   2409    183     92   -727       C  
ATOM   2735  CD2 LEU B 368       3.114  64.202  28.253  1.00 29.07           C  
ANISOU 2735  CD2 LEU B 368     3520   4352   3173    193    143   -663       C  
ATOM   2736  N   VAL B 369       5.832  63.701  32.436  1.00 20.35           N  
ANISOU 2736  N   VAL B 369     2494   2945   2292    203     79   -587       N  
ATOM   2737  CA  VAL B 369       7.191  64.215  32.510  1.00 24.86           C  
ANISOU 2737  CA  VAL B 369     3065   3500   2879    209     87   -601       C  
ATOM   2738  C   VAL B 369       8.031  63.565  31.418  1.00 26.60           C  
ANISOU 2738  C   VAL B 369     3234   3749   3122    203     97   -685       C  
ATOM   2739  O   VAL B 369       8.290  62.365  31.467  1.00 35.07           O  
ANISOU 2739  O   VAL B 369     4282   4783   4261    203     70   -742       O  
ATOM   2740  CB  VAL B 369       7.833  63.949  33.886  1.00 25.20           C  
ANISOU 2740  CB  VAL B 369     3130   3463   2982    224     54   -582       C  
ATOM   2741  CG1 VAL B 369       9.190  64.616  33.979  1.00 14.17           C  
ANISOU 2741  CG1 VAL B 369     1730   2051   1604    230     58   -596       C  
ATOM   2742  CG2 VAL B 369       6.929  64.447  34.994  1.00 16.07           C  
ANISOU 2742  CG2 VAL B 369     2016   2294   1794    241     41   -507       C  
ATOM   2743  N   LYS B 370       8.447  64.352  30.430  1.00 24.72           N  
ANISOU 2743  N   LYS B 370     2978   3583   2831    200    135   -690       N  
ATOM   2744  CA  LYS B 370       9.161  63.794  29.290  1.00 28.30           C  
ANISOU 2744  CA  LYS B 370     3375   4093   3283    202    151   -771       C  
ATOM   2745  C   LYS B 370      10.472  64.514  28.980  1.00 30.99           C  
ANISOU 2745  C   LYS B 370     3692   4460   3621    200    182   -766       C  
ATOM   2746  O   LYS B 370      10.653  65.679  29.336  1.00 35.24           O  
ANISOU 2746  O   LYS B 370     4256   4988   4145    192    196   -693       O  
ATOM   2747  CB  LYS B 370       8.276  63.814  28.046  1.00 25.25           C  
ANISOU 2747  CB  LYS B 370     2966   3808   2819    203    173   -792       C  
ATOM   2748  CG  LYS B 370       7.831  65.203  27.639  1.00 26.73           C  
ANISOU 2748  CG  LYS B 370     3174   4060   2921    199    211   -709       C  
ATOM   2749  CD  LYS B 370       7.205  65.214  26.254  1.00 27.99           C  
ANISOU 2749  CD  LYS B 370     3299   4340   2994    209    236   -735       C  
ATOM   2750  CE  LYS B 370       8.262  65.080  25.170  1.00 30.26           C  
ANISOU 2750  CE  LYS B 370     3528   4716   3252    220    268   -789       C  
ATOM   2751  NZ  LYS B 370       7.704  65.268  23.803  1.00 24.61           N  
ANISOU 2751  NZ  LYS B 370     2779   4141   2431    238    297   -803       N  
ATOM   2752  N   GLY B 371      11.381  63.796  28.324  1.00 26.89           N  
ANISOU 2752  N   GLY B 371     3119   3973   3124    209    188   -847       N  
ATOM   2753  CA  GLY B 371      12.612  64.368  27.812  1.00 16.48           C  
ANISOU 2753  CA  GLY B 371     1760   2704   1799    207    225   -847       C  
ATOM   2754  C   GLY B 371      13.758  64.477  28.796  1.00 28.61           C  
ANISOU 2754  C   GLY B 371     3300   4155   3416    204    205   -841       C  
ATOM   2755  O   GLY B 371      14.714  65.210  28.556  1.00 31.21           O  
ANISOU 2755  O   GLY B 371     3599   4512   3748    194    235   -817       O  
ATOM   2756  N   PHE B 372      13.679  63.750  29.903  1.00 25.91           N  
ANISOU 2756  N   PHE B 372     2988   3713   3142    213    155   -858       N  
ATOM   2757  CA  PHE B 372      14.727  63.857  30.908  1.00 30.65           C  
ANISOU 2757  CA  PHE B 372     3594   4238   3815    217    129   -853       C  
ATOM   2758  C   PHE B 372      15.768  62.756  30.780  1.00 33.61           C  
ANISOU 2758  C   PHE B 372     3919   4597   4254    235    111   -944       C  
ATOM   2759  O   PHE B 372      15.468  61.636  30.362  1.00 41.89           O  
ANISOU 2759  O   PHE B 372     4947   5650   5318    249     94  -1014       O  
ATOM   2760  CB  PHE B 372      14.143  63.866  32.325  1.00 28.31           C  
ANISOU 2760  CB  PHE B 372     3360   3851   3547    224     84   -804       C  
ATOM   2761  CG  PHE B 372      13.348  62.640  32.687  1.00 32.73           C  
ANISOU 2761  CG  PHE B 372     3935   4370   4134    235     49   -826       C  
ATOM   2762  CD1 PHE B 372      13.966  61.537  33.259  1.00 32.50           C  
ANISOU 2762  CD1 PHE B 372     3891   4272   4185    252      8   -872       C  
ATOM   2763  CD2 PHE B 372      11.974  62.607  32.499  1.00 32.60           C  
ANISOU 2763  CD2 PHE B 372     3942   4375   4069    227     54   -795       C  
ATOM   2764  CE1 PHE B 372      13.231  60.415  33.613  1.00 32.65           C  
ANISOU 2764  CE1 PHE B 372     3918   4242   4245    257    -27   -879       C  
ATOM   2765  CE2 PHE B 372      11.236  61.486  32.848  1.00 30.63           C  
ANISOU 2765  CE2 PHE B 372     3697   4081   3860    230     21   -806       C  
ATOM   2766  CZ  PHE B 372      11.864  60.392  33.405  1.00 30.37           C  
ANISOU 2766  CZ  PHE B 372     3649   3975   3915    243    -20   -844       C  
ATOM   2767  N   TYR B 373      16.999  63.109  31.124  1.00 29.19           N  
ANISOU 2767  N   TYR B 373     3335   4017   3739    236    110   -948       N  
ATOM   2768  CA  TYR B 373      18.101  62.163  31.210  1.00 38.90           C  
ANISOU 2768  CA  TYR B 373     4519   5220   5039    258     87  -1030       C  
ATOM   2769  C   TYR B 373      19.072  62.644  32.286  1.00 40.40           C  
ANISOU 2769  C   TYR B 373     4717   5343   5291    260     60  -1005       C  
ATOM   2770  O   TYR B 373      19.352  63.840  32.371  1.00 36.50           O  
ANISOU 2770  O   TYR B 373     4225   4861   4781    239     81   -948       O  
ATOM   2771  CB  TYR B 373      18.813  62.022  29.860  1.00 36.68           C  
ANISOU 2771  CB  TYR B 373     4160   5047   4730    263    133  -1095       C  
ATOM   2772  CG  TYR B 373      19.813  60.891  29.831  1.00 39.24           C  
ANISOU 2772  CG  TYR B 373     4432   5352   5125    296    105  -1198       C  
ATOM   2773  CD1 TYR B 373      21.101  61.060  30.319  1.00 41.81           C  
ANISOU 2773  CD1 TYR B 373     4726   5650   5511    301     97  -1209       C  
ATOM   2774  CD2 TYR B 373      19.466  59.647  29.324  1.00 45.36           C  
ANISOU 2774  CD2 TYR B 373     5187   6133   5916    324     81  -1291       C  
ATOM   2775  CE1 TYR B 373      22.011  60.021  30.304  1.00 45.93           C  
ANISOU 2775  CE1 TYR B 373     5198   6153   6099    336     68  -1306       C  
ATOM   2776  CE2 TYR B 373      20.372  58.606  29.301  1.00 44.46           C  
ANISOU 2776  CE2 TYR B 373     5024   5993   5875    359     49  -1391       C  
ATOM   2777  CZ  TYR B 373      21.641  58.797  29.793  1.00 43.10           C  
ANISOU 2777  CZ  TYR B 373     4823   5799   5756    366     44  -1396       C  
ATOM   2778  OH  TYR B 373      22.546  57.761  29.773  1.00 51.26           O  
ANISOU 2778  OH  TYR B 373     5805   6807   6864    407      9  -1499       O  
ATOM   2779  N   PRO B 374      19.588  61.726  33.117  1.00 39.49           N  
ANISOU 2779  N   PRO B 374     4603   5152   5250    287      7  -1046       N  
ATOM   2780  CA  PRO B 374      19.288  60.289  33.167  1.00 37.15           C  
ANISOU 2780  CA  PRO B 374     4305   4814   4997    311    -30  -1105       C  
ATOM   2781  C   PRO B 374      17.908  59.987  33.740  1.00 37.24           C  
ANISOU 2781  C   PRO B 374     4377   4780   4993    307    -54  -1050       C  
ATOM   2782  O   PRO B 374      17.144  60.904  34.040  1.00 40.10           O  
ANISOU 2782  O   PRO B 374     4784   5155   5297    290    -38   -974       O  
ATOM   2783  CB  PRO B 374      20.389  59.731  34.078  1.00 36.88           C  
ANISOU 2783  CB  PRO B 374     4256   4706   5050    339    -80  -1137       C  
ATOM   2784  CG  PRO B 374      20.849  60.896  34.884  1.00 38.08           C  
ANISOU 2784  CG  PRO B 374     4431   4843   5196    330    -82  -1076       C  
ATOM   2785  CD  PRO B 374      20.730  62.079  33.978  1.00 38.73           C  
ANISOU 2785  CD  PRO B 374     4496   5007   5213    296    -20  -1044       C  
ATOM   2786  N   SER B 375      17.600  58.701  33.883  1.00 30.62           N  
ANISOU 2786  N   SER B 375     3536   3888   4213    323    -94  -1089       N  
ATOM   2787  CA  SER B 375      16.273  58.263  34.296  1.00 25.01           C  
ANISOU 2787  CA  SER B 375     2867   3137   3498    315   -114  -1037       C  
ATOM   2788  C   SER B 375      16.018  58.464  35.789  1.00 32.17           C  
ANISOU 2788  C   SER B 375     3828   3980   4416    324   -146   -946       C  
ATOM   2789  O   SER B 375      14.876  58.371  36.244  1.00 31.30           O  
ANISOU 2789  O   SER B 375     3753   3854   4285    315   -152   -880       O  
ATOM   2790  CB  SER B 375      16.075  56.793  33.930  1.00 28.14           C  
ANISOU 2790  CB  SER B 375     3232   3487   3975    326   -152  -1108       C  
ATOM   2791  OG  SER B 375      17.038  55.984  34.575  1.00 33.32           O  
ANISOU 2791  OG  SER B 375     3870   4065   4724    355   -199  -1139       O  
ATOM   2792  N   ASP B 376      17.079  58.727  36.548  1.00 29.59           N  
ANISOU 2792  N   ASP B 376     3501   3624   4117    345   -167   -943       N  
ATOM   2793  CA  ASP B 376      16.945  58.999  37.978  1.00 35.32           C  
ANISOU 2793  CA  ASP B 376     4273   4307   4839    365   -200   -865       C  
ATOM   2794  C   ASP B 376      16.088  60.236  38.213  1.00 35.57           C  
ANISOU 2794  C   ASP B 376     4349   4385   4781    352   -172   -796       C  
ATOM   2795  O   ASP B 376      16.445  61.340  37.795  1.00 35.84           O  
ANISOU 2795  O   ASP B 376     4378   4463   4777    339   -143   -805       O  
ATOM   2796  CB  ASP B 376      18.318  59.171  38.628  1.00 36.39           C  
ANISOU 2796  CB  ASP B 376     4394   4416   5016    393   -230   -891       C  
ATOM   2797  CG  ASP B 376      19.205  57.957  38.444  1.00 40.07           C  
ANISOU 2797  CG  ASP B 376     4815   4835   5574    414   -263   -962       C  
ATOM   2798  OD1 ASP B 376      18.674  56.833  38.338  1.00 40.58           O  
ANISOU 2798  OD1 ASP B 376     4875   4857   5687    416   -284   -967       O  
ATOM   2799  OD2 ASP B 376      20.437  58.125  38.392  1.00 43.28           O  
ANISOU 2799  OD2 ASP B 376     5185   5245   6014    428   -270  -1016       O  
ATOM   2800  N   ILE B 377      14.955  60.043  38.882  1.00 25.19           N  
ANISOU 2800  N   ILE B 377     3072   3059   3438    356   -182   -724       N  
ATOM   2801  CA  ILE B 377      13.976  61.107  39.048  1.00 24.80           C  
ANISOU 2801  CA  ILE B 377     3062   3058   3304    349   -157   -665       C  
ATOM   2802  C   ILE B 377      13.015  60.809  40.200  1.00 23.80           C  
ANISOU 2802  C   ILE B 377     2970   2918   3154    371   -179   -580       C  
ATOM   2803  O   ILE B 377      12.830  59.656  40.592  1.00 27.21           O  
ANISOU 2803  O   ILE B 377     3394   3307   3639    376   -204   -557       O  
ATOM   2804  CB  ILE B 377      13.173  61.329  37.732  1.00 34.25           C  
ANISOU 2804  CB  ILE B 377     4246   4308   4460    312   -110   -681       C  
ATOM   2805  CG1 ILE B 377      12.509  62.706  37.705  1.00 28.65           C  
ANISOU 2805  CG1 ILE B 377     3568   3649   3668    307    -82   -635       C  
ATOM   2806  CG2 ILE B 377      12.142  60.225  37.510  1.00 15.16           C  
ANISOU 2806  CG2 ILE B 377     1821   1875   2065    299   -116   -669       C  
ATOM   2807  CD1 ILE B 377      11.884  63.027  36.374  1.00 28.35           C  
ANISOU 2807  CD1 ILE B 377     3515   3671   3586    276    -38   -650       C  
ATOM   2808  N   ALA B 378      12.421  61.859  40.754  1.00 19.03           N  
ANISOU 2808  N   ALA B 378     2402   2353   2474    386   -171   -532       N  
ATOM   2809  CA  ALA B 378      11.417  61.706  41.792  1.00 24.81           C  
ANISOU 2809  CA  ALA B 378     3163   3100   3164    411   -182   -448       C  
ATOM   2810  C   ALA B 378      10.207  62.583  41.473  1.00 29.75           C  
ANISOU 2810  C   ALA B 378     3810   3785   3710    399   -148   -415       C  
ATOM   2811  O   ALA B 378      10.354  63.730  41.045  1.00 28.83           O  
ANISOU 2811  O   ALA B 378     3703   3694   3556    396   -132   -442       O  
ATOM   2812  CB  ALA B 378      11.993  62.051  43.156  1.00 18.73           C  
ANISOU 2812  CB  ALA B 378     2414   2328   2374    466   -222   -425       C  
ATOM   2813  N   VAL B 379       9.013  62.030  41.659  1.00 27.64           N  
ANISOU 2813  N   VAL B 379     3544   3534   3424    392   -137   -353       N  
ATOM   2814  CA  VAL B 379       7.782  62.768  41.409  1.00 25.88           C  
ANISOU 2814  CA  VAL B 379     3337   3371   3127    386   -107   -320       C  
ATOM   2815  C   VAL B 379       6.852  62.670  42.612  1.00 31.38           C  
ANISOU 2815  C   VAL B 379     4048   4102   3772    421   -114   -231       C  
ATOM   2816  O   VAL B 379       6.623  61.582  43.143  1.00 27.12           O  
ANISOU 2816  O   VAL B 379     3492   3541   3272    420   -126   -177       O  
ATOM   2817  CB  VAL B 379       7.052  62.253  40.150  1.00 29.77           C  
ANISOU 2817  CB  VAL B 379     3803   3870   3640    335    -79   -339       C  
ATOM   2818  CG1 VAL B 379       5.785  63.060  39.900  1.00 29.22           C  
ANISOU 2818  CG1 VAL B 379     3747   3864   3490    333    -51   -304       C  
ATOM   2819  CG2 VAL B 379       7.961  62.321  38.939  1.00 24.31           C  
ANISOU 2819  CG2 VAL B 379     3089   3164   2983    309    -68   -425       C  
ATOM   2820  N   GLU B 380       6.324  63.814  43.041  1.00 26.19           N  
ANISOU 2820  N   GLU B 380     3418   3503   3031    455   -107   -214       N  
ATOM   2821  CA  GLU B 380       5.394  63.863  44.164  1.00 28.34           C  
ANISOU 2821  CA  GLU B 380     3699   3833   3234    499   -109   -134       C  
ATOM   2822  C   GLU B 380       4.168  64.721  43.867  1.00 32.84           C  
ANISOU 2822  C   GLU B 380     4278   4468   3730    503    -80   -117       C  
ATOM   2823  O   GLU B 380       4.182  65.555  42.962  1.00 40.36           O  
ANISOU 2823  O   GLU B 380     5240   5420   4674    484    -68   -167       O  
ATOM   2824  CB  GLU B 380       6.105  64.393  45.413  1.00 22.85           C  
ANISOU 2824  CB  GLU B 380     3026   3155   2499    569   -146   -137       C  
ATOM   2825  CG  GLU B 380       7.229  63.506  45.908  1.00 28.41           C  
ANISOU 2825  CG  GLU B 380     3720   3806   3268    578   -179   -141       C  
ATOM   2826  CD  GLU B 380       8.037  64.152  47.015  1.00 41.20           C  
ANISOU 2826  CD  GLU B 380     5360   5445   4848    649   -222   -165       C  
ATOM   2827  OE1 GLU B 380       9.010  63.521  47.482  1.00 43.93           O  
ANISOU 2827  OE1 GLU B 380     5697   5753   5240    665   -254   -172       O  
ATOM   2828  OE2 GLU B 380       7.703  65.286  47.417  1.00 40.46           O  
ANISOU 2828  OE2 GLU B 380     5287   5404   4680    694   -229   -184       O  
ATOM   2829  N   TRP B 381       3.105  64.506  44.634  1.00 30.05           N  
ANISOU 2829  N   TRP B 381     3919   4177   3323    528    -70    -38       N  
ATOM   2830  CA  TRP B 381       1.904  65.326  44.537  1.00 26.72           C  
ANISOU 2830  CA  TRP B 381     3502   3827   2823    545    -46    -19       C  
ATOM   2831  C   TRP B 381       1.613  66.000  45.863  1.00 34.58           C  
ANISOU 2831  C   TRP B 381     4515   4899   3727    628    -61     12       C  
ATOM   2832  O   TRP B 381       1.959  65.480  46.925  1.00 33.48           O  
ANISOU 2832  O   TRP B 381     4370   4776   3575    666    -79     54       O  
ATOM   2833  CB  TRP B 381       0.692  64.488  44.118  1.00 27.41           C  
ANISOU 2833  CB  TRP B 381     3553   3936   2925    499    -15     43       C  
ATOM   2834  CG  TRP B 381       0.733  63.977  42.710  1.00 34.70           C  
ANISOU 2834  CG  TRP B 381     4458   4805   3923    427     -3     -3       C  
ATOM   2835  CD1 TRP B 381       1.341  62.836  42.271  1.00 30.88           C  
ANISOU 2835  CD1 TRP B 381     3951   4248   3536    382    -14    -20       C  
ATOM   2836  CD2 TRP B 381       0.116  64.571  41.559  1.00 29.87           C  
ANISOU 2836  CD2 TRP B 381     3844   4215   3290    400     18    -41       C  
ATOM   2837  NE1 TRP B 381       1.146  62.684  40.919  1.00 23.56           N  
ANISOU 2837  NE1 TRP B 381     3005   3303   2644    332     -1    -76       N  
ATOM   2838  CE2 TRP B 381       0.396  63.735  40.459  1.00 28.96           C  
ANISOU 2838  CE2 TRP B 381     3702   4047   3252    341     20    -85       C  
ATOM   2839  CE3 TRP B 381      -0.643  65.727  41.352  1.00 24.17           C  
ANISOU 2839  CE3 TRP B 381     3139   3555   2491    425     32    -45       C  
ATOM   2840  CZ2 TRP B 381      -0.054  64.018  39.174  1.00 26.20           C  
ANISOU 2840  CZ2 TRP B 381     3343   3718   2895    310     37   -129       C  
ATOM   2841  CZ3 TRP B 381      -1.087  66.007  40.071  1.00 27.44           C  
ANISOU 2841  CZ3 TRP B 381     3544   3977   2903    390     50    -80       C  
ATOM   2842  CH2 TRP B 381      -0.788  65.157  38.999  1.00 30.61           C  
ANISOU 2842  CH2 TRP B 381     3919   4338   3373    333     53   -121       C  
ATOM   2843  N   GLU B 382       0.969  67.158  45.800  1.00 34.30           N  
ANISOU 2843  N   GLU B 382     4495   4915   3623    662    -57    -11       N  
ATOM   2844  CA  GLU B 382       0.544  67.846  47.007  1.00 34.69           C  
ANISOU 2844  CA  GLU B 382     4554   5051   3576    751    -72      5       C  
ATOM   2845  C   GLU B 382      -0.608  68.790  46.716  1.00 34.82           C  
ANISOU 2845  C   GLU B 382     4574   5129   3528    773    -55     -1       C  
ATOM   2846  O   GLU B 382      -0.887  69.108  45.562  1.00 31.55           O  
ANISOU 2846  O   GLU B 382     4162   4681   3146    723    -38    -27       O  
ATOM   2847  CB  GLU B 382       1.712  68.610  47.635  1.00 30.78           C  
ANISOU 2847  CB  GLU B 382     4089   4530   3077    808   -123    -69       C  
ATOM   2848  CG  GLU B 382       2.111  69.863  46.892  1.00 36.42           C  
ANISOU 2848  CG  GLU B 382     4827   5193   3817    802   -142   -155       C  
ATOM   2849  CD  GLU B 382       3.463  70.378  47.329  1.00 46.92           C  
ANISOU 2849  CD  GLU B 382     6174   6469   5184    833   -195   -228       C  
ATOM   2850  OE1 GLU B 382       3.568  71.578  47.663  1.00 50.78           O  
ANISOU 2850  OE1 GLU B 382     6680   6961   5651    888   -233   -289       O  
ATOM   2851  OE2 GLU B 382       4.424  69.580  47.321  1.00 56.12           O  
ANISOU 2851  OE2 GLU B 382     7332   7583   6410    803   -202   -230       O  
ATOM   2852  N   SER B 383      -1.280  69.226  47.776  1.00 36.57           N  
ANISOU 2852  N   SER B 383     4791   5449   3654    855    -60     24       N  
ATOM   2853  CA  SER B 383      -2.417  70.133  47.659  1.00 31.52           C  
ANISOU 2853  CA  SER B 383     4150   4879   2946    892    -48     17       C  
ATOM   2854  C   SER B 383      -2.564  70.952  48.929  1.00 38.17           C  
ANISOU 2854  C   SER B 383     4997   5803   3704   1000    -78     -9       C  
ATOM   2855  O   SER B 383      -2.559  70.399  50.027  1.00 40.70           O  
ANISOU 2855  O   SER B 383     5292   6179   3992   1038    -76     39       O  
ATOM   2856  CB  SER B 383      -3.700  69.350  47.371  1.00 21.89           C  
ANISOU 2856  CB  SER B 383     2887   3717   1711    851      3    105       C  
ATOM   2857  OG  SER B 383      -4.811  70.220  47.263  1.00 26.24           O  
ANISOU 2857  OG  SER B 383     3431   4336   2202    887     14     96       O  
ATOM   2858  N   ASN B 384      -2.694  72.266  48.766  1.00 39.78           N  
ANISOU 2858  N   ASN B 384     5214   5982   3919   1033   -105    -85       N  
ATOM   2859  CA  ASN B 384      -2.747  73.191  49.895  1.00 45.90           C  
ANISOU 2859  CA  ASN B 384     5979   6791   4670   1123   -140   -136       C  
ATOM   2860  C   ASN B 384      -1.580  72.975  50.855  1.00 55.96           C  
ANISOU 2860  C   ASN B 384     7265   8062   5936   1170   -181   -167       C  
ATOM   2861  O   ASN B 384      -1.769  72.861  52.066  1.00 57.83           O  
ANISOU 2861  O   ASN B 384     7472   8371   6131   1233   -182   -151       O  
ATOM   2862  CB  ASN B 384      -4.080  73.055  50.633  1.00 45.30           C  
ANISOU 2862  CB  ASN B 384     5847   6815   4548   1155   -102    -77       C  
ATOM   2863  CG  ASN B 384      -5.272  73.222  49.712  1.00 53.09           C  
ANISOU 2863  CG  ASN B 384     6817   7810   5545   1110    -67    -47       C  
ATOM   2864  OD1 ASN B 384      -6.279  72.531  49.853  1.00 62.29           O  
ANISOU 2864  OD1 ASN B 384     7938   9042   6688   1090    -21     30       O  
ATOM   2865  ND2 ASN B 384      -5.153  74.130  48.745  1.00 46.21           N  
ANISOU 2865  ND2 ASN B 384     5979   6872   4708   1096    -89   -106       N  
ATOM   2866  N   GLY B 385      -0.376  72.895  50.295  1.00 55.45           N  
ANISOU 2866  N   GLY B 385     7241   7917   5911   1141   -214   -212       N  
ATOM   2867  CA  GLY B 385       0.843  72.792  51.077  1.00 58.29           C  
ANISOU 2867  CA  GLY B 385     7614   8260   6273   1184   -265   -257       C  
ATOM   2868  C   GLY B 385       1.127  71.408  51.625  1.00 62.15           C  
ANISOU 2868  C   GLY B 385     8088   8790   6735   1175   -246   -173       C  
ATOM   2869  O   GLY B 385       2.196  71.167  52.183  1.00 69.08           O  
ANISOU 2869  O   GLY B 385     8975   9646   7628   1200   -286   -202       O  
ATOM   2870  N   GLN B 386       0.184  70.490  51.457  1.00 57.34           N  
ANISOU 2870  N   GLN B 386     7451   8231   6104   1133   -186    -67       N  
ATOM   2871  CA  GLN B 386       0.297  69.178  52.083  1.00 53.17           C  
ANISOU 2871  CA  GLN B 386     6900   7743   5558   1128   -167     34       C  
ATOM   2872  C   GLN B 386       0.312  68.026  51.089  1.00 48.46           C  
ANISOU 2872  C   GLN B 386     6288   7059   5066   1011   -126     98       C  
ATOM   2873  O   GLN B 386      -0.417  68.041  50.100  1.00 50.26           O  
ANISOU 2873  O   GLN B 386     6508   7263   5326    949    -91    108       O  
ATOM   2874  CB  GLN B 386      -0.840  68.987  53.080  1.00 51.75           C  
ANISOU 2874  CB  GLN B 386     6669   7672   5323   1164   -123    110       C  
ATOM   2875  CG  GLN B 386      -0.608  69.731  54.372  1.00 56.90           C  
ANISOU 2875  CG  GLN B 386     7308   8379   5933   1259   -152     51       C  
ATOM   2876  CD  GLN B 386       0.458  69.077  55.220  1.00 69.78           C  
ANISOU 2876  CD  GLN B 386     8943  10017   7551   1293   -182     67       C  
ATOM   2877  OE1 GLN B 386       1.535  69.635  55.422  1.00 80.63           O  
ANISOU 2877  OE1 GLN B 386    10346  11347   8942   1332   -241    -30       O  
ATOM   2878  NE2 GLN B 386       0.167  67.879  55.717  1.00 66.84           N  
ANISOU 2878  NE2 GLN B 386     8539   9699   7158   1277   -145    194       N  
ATOM   2879  N   PRO B 387       1.144  67.010  51.368  1.00 44.53           N  
ANISOU 2879  N   PRO B 387     5783   6515   4621    988   -136    137       N  
ATOM   2880  CA  PRO B 387       1.323  65.873  50.460  1.00 42.63           C  
ANISOU 2880  CA  PRO B 387     5525   6178   4494    885   -111    179       C  
ATOM   2881  C   PRO B 387       0.055  65.059  50.210  1.00 42.69           C  
ANISOU 2881  C   PRO B 387     5493   6223   4505    836    -59    286       C  
ATOM   2882  O   PRO B 387      -0.637  64.676  51.154  1.00 43.68           O  
ANISOU 2882  O   PRO B 387     5590   6447   4562    878    -40    386       O  
ATOM   2883  CB  PRO B 387       2.377  65.017  51.179  1.00 34.56           C  
ANISOU 2883  CB  PRO B 387     4500   5124   3507    901   -141    208       C  
ATOM   2884  CG  PRO B 387       2.298  65.427  52.612  1.00 37.67           C  
ANISOU 2884  CG  PRO B 387     4895   5639   3778   1012   -163    232       C  
ATOM   2885  CD  PRO B 387       1.977  66.885  52.577  1.00 36.89           C  
ANISOU 2885  CD  PRO B 387     4820   5586   3610   1066   -178    136       C  
ATOM   2886  N   GLU B 388      -0.243  64.819  48.941  1.00 39.99           N  
ANISOU 2886  N   GLU B 388     5144   5810   4243    751    -36    266       N  
ATOM   2887  CA  GLU B 388      -1.218  63.814  48.545  1.00 35.67           C  
ANISOU 2887  CA  GLU B 388     4551   5261   3741    686      1    355       C  
ATOM   2888  C   GLU B 388      -0.452  62.516  48.362  1.00 43.52           C  
ANISOU 2888  C   GLU B 388     5529   6155   4852    630    -12    383       C  
ATOM   2889  O   GLU B 388       0.664  62.528  47.843  1.00 47.97           O  
ANISOU 2889  O   GLU B 388     6117   6632   5479    610    -39    300       O  
ATOM   2890  CB  GLU B 388      -1.936  64.220  47.256  1.00 40.37           C  
ANISOU 2890  CB  GLU B 388     5143   5837   4359    631     24    306       C  
ATOM   2891  CG  GLU B 388      -2.660  65.555  47.336  1.00 46.84           C  
ANISOU 2891  CG  GLU B 388     5980   6742   5075    687     32    270       C  
ATOM   2892  CD  GLU B 388      -4.007  65.441  48.011  1.00 47.19           C  
ANISOU 2892  CD  GLU B 388     5984   6903   5043    718     65    365       C  
ATOM   2893  OE1 GLU B 388      -4.506  66.461  48.535  1.00 54.76           O  
ANISOU 2893  OE1 GLU B 388     6953   7953   5898    793     64    346       O  
ATOM   2894  OE2 GLU B 388      -4.567  64.323  48.012  1.00 46.40           O  
ANISOU 2894  OE2 GLU B 388     5837   6801   4993    666     89    457       O  
ATOM   2895  N   ASN B 389      -1.025  61.399  48.789  1.00 39.13           N  
ANISOU 2895  N   ASN B 389     4927   5607   4332    604      4    502       N  
ATOM   2896  CA  ASN B 389      -0.265  60.155  48.775  1.00 51.69           C  
ANISOU 2896  CA  ASN B 389     6501   7097   6040    563    -18    535       C  
ATOM   2897  C   ASN B 389      -0.968  59.009  48.062  1.00 49.85           C  
ANISOU 2897  C   ASN B 389     6218   6797   5926    475     -4    590       C  
ATOM   2898  O   ASN B 389      -0.426  57.908  47.969  1.00 47.04           O  
ANISOU 2898  O   ASN B 389     5842   6343   5687    436    -27    614       O  
ATOM   2899  CB  ASN B 389       0.083  59.736  50.206  1.00 64.72           C  
ANISOU 2899  CB  ASN B 389     8145   8799   7647    626    -31    637       C  
ATOM   2900  CG  ASN B 389       1.156  60.617  50.828  1.00 69.23           C  
ANISOU 2900  CG  ASN B 389     8765   9400   8141    708    -66    557       C  
ATOM   2901  OD1 ASN B 389       2.103  61.039  50.161  1.00 73.70           O  
ANISOU 2901  OD1 ASN B 389     9363   9890   8749    694    -92    437       O  
ATOM   2902  ND2 ASN B 389       1.011  60.901  52.118  1.00 66.55           N  
ANISOU 2902  ND2 ASN B 389     8424   9176   7686    795    -68    622       N  
ATOM   2903  N   ASN B 390      -2.169  59.271  47.556  1.00 38.53           N  
ANISOU 2903  N   ASN B 390     4759   5410   4469    446     29    602       N  
ATOM   2904  CA  ASN B 390      -2.880  58.277  46.759  1.00 32.04           C  
ANISOU 2904  CA  ASN B 390     3885   4523   3767    361     35    632       C  
ATOM   2905  C   ASN B 390      -2.514  58.410  45.288  1.00 36.14           C  
ANISOU 2905  C   ASN B 390     4420   4962   4349    312     20    492       C  
ATOM   2906  O   ASN B 390      -3.381  58.545  44.426  1.00 28.00           O  
ANISOU 2906  O   ASN B 390     3367   3945   3327    273     35    462       O  
ATOM   2907  CB  ASN B 390      -4.396  58.402  46.944  1.00 27.70           C  
ANISOU 2907  CB  ASN B 390     3289   4069   3167    353     75    720       C  
ATOM   2908  CG  ASN B 390      -5.156  57.235  46.329  1.00 32.11           C  
ANISOU 2908  CG  ASN B 390     3781   4556   3865    264     75    770       C  
ATOM   2909  OD1 ASN B 390      -4.568  56.220  45.952  1.00 39.96           O  
ANISOU 2909  OD1 ASN B 390     4759   5428   4995    216     42    757       O  
ATOM   2910  ND2 ASN B 390      -6.472  57.375  46.231  1.00 36.28           N  
ANISOU 2910  ND2 ASN B 390     4263   5157   4364    246    108    823       N  
ATOM   2911  N   TYR B 391      -1.217  58.383  45.008  1.00 33.35           N  
ANISOU 2911  N   TYR B 391     4100   4536   4035    319    -11    406       N  
ATOM   2912  CA  TYR B 391      -0.757  58.431  43.633  1.00 31.58           C  
ANISOU 2912  CA  TYR B 391     3884   4247   3868    278    -23    278       C  
ATOM   2913  C   TYR B 391       0.168  57.261  43.323  1.00 33.64           C  
ANISOU 2913  C   TYR B 391     4126   4389   4265    244    -61    246       C  
ATOM   2914  O   TYR B 391       0.733  56.644  44.228  1.00 31.72           O  
ANISOU 2914  O   TYR B 391     3881   4110   4060    264    -81    310       O  
ATOM   2915  CB  TYR B 391      -0.049  59.762  43.338  1.00 28.98           C  
ANISOU 2915  CB  TYR B 391     3609   3954   3448    319    -20    183       C  
ATOM   2916  CG  TYR B 391       1.262  59.968  44.069  1.00 26.51           C  
ANISOU 2916  CG  TYR B 391     3331   3617   3124    366    -45    163       C  
ATOM   2917  CD1 TYR B 391       2.462  59.499  43.544  1.00 26.57           C  
ANISOU 2917  CD1 TYR B 391     3341   3539   3216    347    -72     87       C  
ATOM   2918  CD2 TYR B 391       1.302  60.660  45.271  1.00 28.23           C  
ANISOU 2918  CD2 TYR B 391     3574   3906   3245    434    -45    211       C  
ATOM   2919  CE1 TYR B 391       3.659  59.698  44.212  1.00 28.96           C  
ANISOU 2919  CE1 TYR B 391     3670   3823   3512    390    -97     66       C  
ATOM   2920  CE2 TYR B 391       2.492  60.866  45.942  1.00 24.19           C  
ANISOU 2920  CE2 TYR B 391     3090   3376   2724    480    -75    185       C  
ATOM   2921  CZ  TYR B 391       3.665  60.387  45.412  1.00 27.67           C  
ANISOU 2921  CZ  TYR B 391     3532   3727   3255    456   -100    115       C  
ATOM   2922  OH  TYR B 391       4.840  60.602  46.097  1.00 34.38           O  
ANISOU 2922  OH  TYR B 391     4404   4562   4097    503   -133     88       O  
ATOM   2923  N   LYS B 392       0.307  56.955  42.036  1.00 34.59           N  
ANISOU 2923  N   LYS B 392     4232   4456   4455    200    -72    143       N  
ATOM   2924  CA  LYS B 392       1.273  55.969  41.570  1.00 33.23           C  
ANISOU 2924  CA  LYS B 392     4042   4176   4407    177   -111     78       C  
ATOM   2925  C   LYS B 392       2.017  56.525  40.365  1.00 34.07           C  
ANISOU 2925  C   LYS B 392     4168   4284   4494    176   -111    -65       C  
ATOM   2926  O   LYS B 392       1.452  57.268  39.561  1.00 32.26           O  
ANISOU 2926  O   LYS B 392     3943   4117   4198    168    -86   -111       O  
ATOM   2927  CB  LYS B 392       0.579  54.650  41.217  1.00 38.81           C  
ANISOU 2927  CB  LYS B 392     4688   4806   5254    121   -136    105       C  
ATOM   2928  CG  LYS B 392      -0.259  54.063  42.345  1.00 41.15           C  
ANISOU 2928  CG  LYS B 392     4953   5104   5579    112   -130    267       C  
ATOM   2929  CD  LYS B 392       0.335  52.776  42.891  1.00 41.68           C  
ANISOU 2929  CD  LYS B 392     4992   5057   5787    101   -174    324       C  
ATOM   2930  CE  LYS B 392       1.067  52.995  44.201  1.00 42.97           C  
ANISOU 2930  CE  LYS B 392     5190   5248   5887    160   -172    411       C  
ATOM   2931  NZ  LYS B 392       1.413  51.698  44.848  1.00 39.30           N  
ANISOU 2931  NZ  LYS B 392     4692   4680   5560    148   -211    504       N  
ATOM   2932  N   THR B 393       3.289  56.175  40.246  1.00 29.91           N  
ANISOU 2932  N   THR B 393     3646   3696   4022    188   -138   -130       N  
ATOM   2933  CA  THR B 393       4.111  56.693  39.166  1.00 30.31           C  
ANISOU 2933  CA  THR B 393     3707   3758   4051    191   -133   -256       C  
ATOM   2934  C   THR B 393       4.706  55.544  38.369  1.00 32.29           C  
ANISOU 2934  C   THR B 393     3917   3926   4426    169   -169   -346       C  
ATOM   2935  O   THR B 393       5.324  54.645  38.937  1.00 38.65           O  
ANISOU 2935  O   THR B 393     4709   4649   5325    175   -206   -328       O  
ATOM   2936  CB  THR B 393       5.239  57.597  39.700  1.00 28.18           C  
ANISOU 2936  CB  THR B 393     3479   3510   3717    235   -128   -270       C  
ATOM   2937  OG1 THR B 393       4.670  58.665  40.467  1.00 29.25           O  
ANISOU 2937  OG1 THR B 393     3650   3720   3743    263   -103   -199       O  
ATOM   2938  CG2 THR B 393       6.056  58.181  38.556  1.00 26.74           C  
ANISOU 2938  CG2 THR B 393     3299   3349   3514    232   -115   -384       C  
ATOM   2939  N   THR B 394       4.505  55.567  37.055  1.00 30.02           N  
ANISOU 2939  N   THR B 394     3606   3663   4137    148   -163   -446       N  
ATOM   2940  CA  THR B 394       5.100  54.564  36.182  1.00 27.09           C  
ANISOU 2940  CA  THR B 394     3192   3230   3871    139   -200   -557       C  
ATOM   2941  C   THR B 394       6.620  54.645  36.244  1.00 30.27           C  
ANISOU 2941  C   THR B 394     3606   3611   4284    171   -209   -616       C  
ATOM   2942  O   THR B 394       7.172  55.699  36.554  1.00 31.89           O  
ANISOU 2942  O   THR B 394     3850   3870   4398    194   -179   -598       O  
ATOM   2943  CB  THR B 394       4.650  54.740  34.717  1.00 30.83           C  
ANISOU 2943  CB  THR B 394     3639   3765   4311    124   -188   -662       C  
ATOM   2944  OG1 THR B 394       5.418  55.782  34.104  1.00 33.19           O  
ANISOU 2944  OG1 THR B 394     3959   4144   4507    148   -151   -719       O  
ATOM   2945  CG2 THR B 394       3.164  55.069  34.637  1.00 31.23           C  
ANISOU 2945  CG2 THR B 394     3687   3867   4314     99   -169   -602       C  
ATOM   2946  N   PRO B 395       7.303  53.527  35.959  1.00 32.20           N  
ANISOU 2946  N   PRO B 395     3814   3774   4648    174   -254   -690       N  
ATOM   2947  CA  PRO B 395       8.761  53.593  35.859  1.00 31.34           C  
ANISOU 2947  CA  PRO B 395     3706   3655   4548    206   -261   -762       C  
ATOM   2948  C   PRO B 395       9.153  54.492  34.696  1.00 34.15           C  
ANISOU 2948  C   PRO B 395     4057   4112   4807    213   -220   -855       C  
ATOM   2949  O   PRO B 395       8.308  54.763  33.844  1.00 27.37           O  
ANISOU 2949  O   PRO B 395     3188   3315   3898    195   -199   -882       O  
ATOM   2950  CB  PRO B 395       9.172  52.137  35.600  1.00 30.25           C  
ANISOU 2950  CB  PRO B 395     3519   3411   4564    208   -322   -836       C  
ATOM   2951  CG  PRO B 395       8.017  51.319  36.064  1.00 21.87           C  
ANISOU 2951  CG  PRO B 395     2442   2278   3588    176   -352   -754       C  
ATOM   2952  CD  PRO B 395       6.797  52.151  35.817  1.00 24.42           C  
ANISOU 2952  CD  PRO B 395     2781   2691   3805    150   -306   -706       C  
ATOM   2953  N   PRO B 396      10.408  54.961  34.665  1.00 33.34           N  
ANISOU 2953  N   PRO B 396     3959   4031   4679    238   -207   -896       N  
ATOM   2954  CA  PRO B 396      10.847  55.717  33.487  1.00 25.98           C  
ANISOU 2954  CA  PRO B 396     3010   3196   3665    243   -166   -976       C  
ATOM   2955  C   PRO B 396      10.838  54.833  32.242  1.00 31.97           C  
ANISOU 2955  C   PRO B 396     3711   3967   4469    247   -185  -1104       C  
ATOM   2956  O   PRO B 396      11.179  53.652  32.327  1.00 41.68           O  
ANISOU 2956  O   PRO B 396     4910   5112   5815    258   -237  -1160       O  
ATOM   2957  CB  PRO B 396      12.270  56.151  33.850  1.00 24.42           C  
ANISOU 2957  CB  PRO B 396     2816   2998   3465    268   -160   -990       C  
ATOM   2958  CG  PRO B 396      12.347  56.037  35.344  1.00 25.74           C  
ANISOU 2958  CG  PRO B 396     3021   3090   3671    277   -189   -895       C  
ATOM   2959  CD  PRO B 396      11.441  54.908  35.714  1.00 22.82           C  
ANISOU 2959  CD  PRO B 396     2644   2644   3383    264   -228   -861       C  
ATOM   2960  N   VAL B 397      10.435  55.387  31.106  1.00 31.23           N  
ANISOU 2960  N   VAL B 397     3602   3979   4287    243   -148  -1150       N  
ATOM   2961  CA  VAL B 397      10.397  54.619  29.868  1.00 36.79           C  
ANISOU 2961  CA  VAL B 397     4248   4717   5015    257   -168  -1283       C  
ATOM   2962  C   VAL B 397      11.250  55.288  28.799  1.00 41.17           C  
ANISOU 2962  C   VAL B 397     4773   5394   5475    281   -120  -1354       C  
ATOM   2963  O   VAL B 397      11.144  56.492  28.566  1.00 39.01           O  
ANISOU 2963  O   VAL B 397     4523   5210   5090    272    -65  -1292       O  
ATOM   2964  CB  VAL B 397       8.956  54.449  29.345  1.00 36.38           C  
ANISOU 2964  CB  VAL B 397     4188   4691   4944    236   -176  -1285       C  
ATOM   2965  CG1 VAL B 397       8.955  53.651  28.051  1.00 31.40           C  
ANISOU 2965  CG1 VAL B 397     3493   4102   4336    259   -204  -1441       C  
ATOM   2966  CG2 VAL B 397       8.089  53.766  30.385  1.00 33.83           C  
ANISOU 2966  CG2 VAL B 397     3883   4251   4720    207   -218  -1203       C  
ATOM   2967  N   LEU B 398      12.105  54.496  28.161  1.00 42.67           N  
ANISOU 2967  N   LEU B 398     4907   5590   5715    315   -144  -1480       N  
ATOM   2968  CA  LEU B 398      12.989  54.999  27.122  1.00 33.15           C  
ANISOU 2968  CA  LEU B 398     3659   4513   4422    343    -98  -1551       C  
ATOM   2969  C   LEU B 398      12.185  55.462  25.911  1.00 37.92           C  
ANISOU 2969  C   LEU B 398     4244   5253   4910    347    -64  -1580       C  
ATOM   2970  O   LEU B 398      11.375  54.709  25.376  1.00 46.15           O  
ANISOU 2970  O   LEU B 398     5262   6294   5978    354   -103  -1656       O  
ATOM   2971  CB  LEU B 398      13.998  53.920  26.721  1.00 32.49           C  
ANISOU 2971  CB  LEU B 398     3514   4409   4422    388   -138  -1692       C  
ATOM   2972  CG  LEU B 398      15.192  54.331  25.858  1.00 36.89           C  
ANISOU 2972  CG  LEU B 398     4019   5091   4906    415    -93  -1731       C  
ATOM   2973  CD1 LEU B 398      15.984  55.428  26.544  1.00 28.86           C  
ANISOU 2973  CD1 LEU B 398     3031   4082   3853    402    -41  -1648       C  
ATOM   2974  CD2 LEU B 398      16.078  53.128  25.581  1.00 29.47           C  
ANISOU 2974  CD2 LEU B 398     3021   4117   4061    448   -149  -1823       C  
ATOM   2975  N   ASP B 399      12.405  56.707  25.495  1.00 32.20           N  
ANISOU 2975  N   ASP B 399     3528   4641   4064    341      5  -1515       N  
ATOM   2976  CA  ASP B 399      11.699  57.268  24.348  1.00 39.07           C  
ANISOU 2976  CA  ASP B 399     4381   5653   4811    348     43  -1525       C  
ATOM   2977  C   ASP B 399      12.519  57.104  23.066  1.00 46.16           C  
ANISOU 2977  C   ASP B 399     5207   6679   5651    385     62  -1603       C  
ATOM   2978  O   ASP B 399      13.644  56.604  23.103  1.00 47.01           O  
ANISOU 2978  O   ASP B 399     5279   6767   5815    404     49  -1653       O  
ATOM   2979  CB  ASP B 399      11.375  58.748  24.587  1.00 31.39           C  
ANISOU 2979  CB  ASP B 399     3458   4723   3745    317    102  -1378       C  
ATOM   2980  CG  ASP B 399       9.964  59.108  24.164  1.00 35.67           C  
ANISOU 2980  CG  ASP B 399     4021   5318   4215    305    106  -1342       C  
ATOM   2981  OD1 ASP B 399       9.458  58.490  23.206  1.00 35.11           O  
ANISOU 2981  OD1 ASP B 399     3908   5317   4116    330     87  -1440       O  
ATOM   2982  OD2 ASP B 399       9.351  59.996  24.794  1.00 36.66           O  
ANISOU 2982  OD2 ASP B 399     4202   5415   4313    276    124  -1222       O  
ATOM   2983  N   SER B 400      11.944  57.525  21.943  1.00 45.57           N  
ANISOU 2983  N   SER B 400     5113   6735   5468    392     86  -1589       N  
ATOM   2984  CA  SER B 400      12.586  57.399  20.641  1.00 43.03           C  
ANISOU 2984  CA  SER B 400     4723   6546   5080    426     98  -1636       C  
ATOM   2985  C   SER B 400      13.949  58.086  20.604  1.00 46.38           C  
ANISOU 2985  C   SER B 400     5126   7026   5469    429    156  -1595       C  
ATOM   2986  O   SER B 400      14.895  57.576  20.007  1.00 48.59           O  
ANISOU 2986  O   SER B 400     5347   7360   5755    459    148  -1662       O  
ATOM   2987  CB  SER B 400      11.689  57.989  19.549  1.00 42.89           C  
ANISOU 2987  CB  SER B 400     4698   6660   4938    432    121  -1597       C  
ATOM   2988  OG  SER B 400      10.323  57.935  19.924  1.00 49.85           O  
ANISOU 2988  OG  SER B 400     5621   7486   5834    412     94  -1581       O  
ATOM   2989  N   ASP B 401      14.046  59.236  21.261  1.00 39.25           N  
ANISOU 2989  N   ASP B 401     4265   6111   4535    398    211  -1488       N  
ATOM   2990  CA  ASP B 401      15.231  60.073  21.137  1.00 30.75           C  
ANISOU 2990  CA  ASP B 401     3160   5102   3422    395    275  -1434       C  
ATOM   2991  C   ASP B 401      16.284  59.809  22.216  1.00 35.50           C  
ANISOU 2991  C   ASP B 401     3761   5596   4131    392    264  -1463       C  
ATOM   2992  O   ASP B 401      17.200  60.607  22.399  1.00 41.81           O  
ANISOU 2992  O   ASP B 401     4540   6427   4920    382    317  -1412       O  
ATOM   2993  CB  ASP B 401      14.819  61.548  21.148  1.00 31.52           C  
ANISOU 2993  CB  ASP B 401     3290   5255   3433    365    341  -1300       C  
ATOM   2994  CG  ASP B 401      14.190  61.980  22.463  1.00 43.63           C  
ANISOU 2994  CG  ASP B 401     4901   6651   5025    329    323  -1229       C  
ATOM   2995  OD1 ASP B 401      13.983  61.117  23.347  1.00 39.43           O  
ANISOU 2995  OD1 ASP B 401     4400   5988   4592    326    263  -1276       O  
ATOM   2996  OD2 ASP B 401      13.895  63.184  22.610  1.00 43.56           O  
ANISOU 2996  OD2 ASP B 401     4928   6650   4974    298    358  -1102       O  
ATOM   2997  N   GLY B 402      16.154  58.694  22.929  1.00 33.67           N  
ANISOU 2997  N   GLY B 402     3547   5236   4010    401    194  -1539       N  
ATOM   2998  CA  GLY B 402      17.122  58.331  23.951  1.00 31.02           C  
ANISOU 2998  CA  GLY B 402     3212   4790   3784    404    170  -1566       C  
ATOM   2999  C   GLY B 402      16.881  58.986  25.300  1.00 36.58           C  
ANISOU 2999  C   GLY B 402     3993   5368   4539    360    161  -1445       C  
ATOM   3000  O   GLY B 402      17.536  58.648  26.288  1.00 42.29           O  
ANISOU 3000  O   GLY B 402     4729   5980   5357    358    125  -1444       O  
ATOM   3001  N   SER B 403      15.953  59.933  25.346  1.00 39.12           N  
ANISOU 3001  N   SER B 403     4363   5708   4792    328    187  -1340       N  
ATOM   3002  CA  SER B 403      15.545  60.522  26.616  1.00 39.59           C  
ANISOU 3002  CA  SER B 403     4498   5654   4893    293    169  -1230       C  
ATOM   3003  C   SER B 403      14.466  59.654  27.249  1.00 37.98           C  
ANISOU 3003  C   SER B 403     4336   5352   4742    291    111  -1243       C  
ATOM   3004  O   SER B 403      13.917  58.762  26.603  1.00 37.43           O  
ANISOU 3004  O   SER B 403     4240   5304   4676    309     87  -1328       O  
ATOM   3005  CB  SER B 403      15.033  61.949  26.422  1.00 33.50           C  
ANISOU 3005  CB  SER B 403     3756   4939   4033    265    218  -1114       C  
ATOM   3006  OG  SER B 403      13.720  61.943  25.896  1.00 35.33           O  
ANISOU 3006  OG  SER B 403     4007   5216   4199    264    220  -1105       O  
ATOM   3007  N   PHE B 404      14.155  59.920  28.511  1.00 29.47           N  
ANISOU 3007  N   PHE B 404     3319   4171   3708    271     86  -1159       N  
ATOM   3008  CA  PHE B 404      13.133  59.149  29.207  1.00 27.41           C  
ANISOU 3008  CA  PHE B 404     3094   3821   3500    266     37  -1148       C  
ATOM   3009  C   PHE B 404      11.862  59.954  29.420  1.00 30.30           C  
ANISOU 3009  C   PHE B 404     3510   4204   3799    243     54  -1053       C  
ATOM   3010  O   PHE B 404      11.878  61.185  29.384  1.00 32.43           O  
ANISOU 3010  O   PHE B 404     3801   4521   4002    232     94   -982       O  
ATOM   3011  CB  PHE B 404      13.654  58.648  30.555  1.00 33.09           C  
ANISOU 3011  CB  PHE B 404     3839   4418   4318    270     -8  -1123       C  
ATOM   3012  CG  PHE B 404      14.700  57.579  30.442  1.00 36.62           C  
ANISOU 3012  CG  PHE B 404     4237   4826   4852    297    -42  -1222       C  
ATOM   3013  CD1 PHE B 404      16.041  57.911  30.328  1.00 33.63           C  
ANISOU 3013  CD1 PHE B 404     3826   4475   4477    312    -23  -1252       C  
ATOM   3014  CD2 PHE B 404      14.345  56.240  30.465  1.00 29.51           C  
ANISOU 3014  CD2 PHE B 404     3318   3854   4038    309    -96  -1285       C  
ATOM   3015  CE1 PHE B 404      17.007  56.927  30.233  1.00 30.64           C  
ANISOU 3015  CE1 PHE B 404     3400   4063   4179    343    -56  -1348       C  
ATOM   3016  CE2 PHE B 404      15.308  55.251  30.372  1.00 30.61           C  
ANISOU 3016  CE2 PHE B 404     3413   3950   4268    340   -133  -1381       C  
ATOM   3017  CZ  PHE B 404      16.640  55.596  30.253  1.00 26.97           C  
ANISOU 3017  CZ  PHE B 404     2921   3526   3800    359   -112  -1416       C  
ATOM   3018  N   PHE B 405      10.761  59.245  29.634  1.00 32.49           N  
ANISOU 3018  N   PHE B 405     3800   4439   4105    236     22  -1053       N  
ATOM   3019  CA  PHE B 405       9.521  59.876  30.048  1.00 26.49           C  
ANISOU 3019  CA  PHE B 405     3085   3683   3296    218     30   -961       C  
ATOM   3020  C   PHE B 405       8.819  58.997  31.076  1.00 26.99           C  
ANISOU 3020  C   PHE B 405     3169   3647   3440    209    -16   -928       C  
ATOM   3021  O   PHE B 405       9.146  57.819  31.229  1.00 22.64           O  
ANISOU 3021  O   PHE B 405     2591   3026   2984    215    -58   -983       O  
ATOM   3022  CB  PHE B 405       8.604  60.142  28.850  1.00 28.29           C  
ANISOU 3022  CB  PHE B 405     3295   4012   3442    214     55   -985       C  
ATOM   3023  CG  PHE B 405       7.863  58.927  28.366  1.00 29.68           C  
ANISOU 3023  CG  PHE B 405     3436   4175   3666    215     15  -1064       C  
ATOM   3024  CD1 PHE B 405       6.596  58.633  28.847  1.00 28.52           C  
ANISOU 3024  CD1 PHE B 405     3308   3986   3542    196     -8  -1017       C  
ATOM   3025  CD2 PHE B 405       8.428  58.082  27.426  1.00 27.84           C  
ANISOU 3025  CD2 PHE B 405     3146   3973   3461    237     -1  -1189       C  
ATOM   3026  CE1 PHE B 405       5.912  57.519  28.405  1.00 32.96           C  
ANISOU 3026  CE1 PHE B 405     3831   4525   4167    191    -51  -1090       C  
ATOM   3027  CE2 PHE B 405       7.748  56.965  26.980  1.00 21.23           C  
ANISOU 3027  CE2 PHE B 405     2273   3113   2682    240    -48  -1274       C  
ATOM   3028  CZ  PHE B 405       6.488  56.683  27.469  1.00 27.03           C  
ANISOU 3028  CZ  PHE B 405     3025   3794   3452    213    -75  -1223       C  
ATOM   3029  N   LEU B 406       7.868  59.580  31.792  1.00 27.32           N  
ANISOU 3029  N   LEU B 406     3253   3683   3444    198    -10   -832       N  
ATOM   3030  CA  LEU B 406       6.992  58.799  32.649  1.00 29.55           C  
ANISOU 3030  CA  LEU B 406     3545   3896   3787    187    -44   -784       C  
ATOM   3031  C   LEU B 406       5.653  59.491  32.807  1.00 31.82           C  
ANISOU 3031  C   LEU B 406     3858   4228   4003    176    -24   -708       C  
ATOM   3032  O   LEU B 406       5.465  60.622  32.355  1.00 31.43           O  
ANISOU 3032  O   LEU B 406     3827   4253   3861    181     12   -689       O  
ATOM   3033  CB  LEU B 406       7.628  58.549  34.025  1.00 23.97           C  
ANISOU 3033  CB  LEU B 406     2863   3106   3139    200    -69   -729       C  
ATOM   3034  CG  LEU B 406       8.143  59.671  34.933  1.00 23.39           C  
ANISOU 3034  CG  LEU B 406     2833   3041   3010    219    -53   -664       C  
ATOM   3035  CD1 LEU B 406       7.033  60.542  35.507  1.00 14.80           C  
ANISOU 3035  CD1 LEU B 406     1785   1992   1848    220    -35   -574       C  
ATOM   3036  CD2 LEU B 406       8.955  59.062  36.064  1.00 16.71           C  
ANISOU 3036  CD2 LEU B 406     1995   2117   2238    238    -90   -643       C  
ATOM   3037  N   TYR B 407       4.724  58.791  33.441  1.00 22.15           N  
ANISOU 3037  N   TYR B 407     2630   2958   2827    162    -48   -659       N  
ATOM   3038  CA  TYR B 407       3.476  59.387  33.875  1.00 26.49           C  
ANISOU 3038  CA  TYR B 407     3203   3546   3317    157    -31   -574       C  
ATOM   3039  C   TYR B 407       3.289  59.153  35.370  1.00 28.58           C  
ANISOU 3039  C   TYR B 407     3489   3757   3613    164    -45   -476       C  
ATOM   3040  O   TYR B 407       3.622  58.088  35.892  1.00 21.93           O  
ANISOU 3040  O   TYR B 407     2628   2837   2867    158    -78   -469       O  
ATOM   3041  CB  TYR B 407       2.288  58.801  33.110  1.00 28.44           C  
ANISOU 3041  CB  TYR B 407     3411   3814   3581    132    -40   -601       C  
ATOM   3042  CG  TYR B 407       2.145  59.249  31.670  1.00 33.86           C  
ANISOU 3042  CG  TYR B 407     4078   4587   4199    134    -22   -680       C  
ATOM   3043  CD1 TYR B 407       2.891  58.661  30.656  1.00 33.27           C  
ANISOU 3043  CD1 TYR B 407     3966   4519   4155    139    -35   -793       C  
ATOM   3044  CD2 TYR B 407       1.236  60.241  31.319  1.00 34.47           C  
ANISOU 3044  CD2 TYR B 407     4172   4748   4177    137      8   -642       C  
ATOM   3045  CE1 TYR B 407       2.743  59.061  29.335  1.00 33.23           C  
ANISOU 3045  CE1 TYR B 407     3940   4613   4075    148    -16   -860       C  
ATOM   3046  CE2 TYR B 407       1.084  60.645  30.004  1.00 30.68           C  
ANISOU 3046  CE2 TYR B 407     3672   4355   3628    144     25   -703       C  
ATOM   3047  CZ  TYR B 407       1.838  60.054  29.017  1.00 33.46           C  
ANISOU 3047  CZ  TYR B 407     3987   4723   4002    150     14   -809       C  
ATOM   3048  OH  TYR B 407       1.679  60.462  27.712  1.00 28.78           O  
ANISOU 3048  OH  TYR B 407     3371   4237   3326    164     33   -865       O  
ATOM   3049  N   SER B 408       2.755  60.150  36.060  1.00 23.27           N  
ANISOU 3049  N   SER B 408     2852   3130   2857    182    -23   -399       N  
ATOM   3050  CA  SER B 408       2.333  59.954  37.436  1.00 26.98           C  
ANISOU 3050  CA  SER B 408     3336   3581   3335    196    -31   -301       C  
ATOM   3051  C   SER B 408       0.829  60.168  37.531  1.00 22.87           C  
ANISOU 3051  C   SER B 408     2806   3114   2768    186    -14   -238       C  
ATOM   3052  O   SER B 408       0.295  61.131  36.986  1.00 26.51           O  
ANISOU 3052  O   SER B 408     3281   3643   3148    193     10   -250       O  
ATOM   3053  CB  SER B 408       3.076  60.894  38.382  1.00 21.83           C  
ANISOU 3053  CB  SER B 408     2729   2941   2626    239    -28   -271       C  
ATOM   3054  OG  SER B 408       2.728  60.621  39.726  1.00 20.25           O  
ANISOU 3054  OG  SER B 408     2536   2734   2422    262    -38   -179       O  
ATOM   3055  N   LYS B 409       0.143  59.257  38.208  1.00 25.36           N  
ANISOU 3055  N   LYS B 409     3094   3401   3141    170    -26   -167       N  
ATOM   3056  CA  LYS B 409      -1.308  59.338  38.298  1.00 21.92           C  
ANISOU 3056  CA  LYS B 409     2637   3019   2675    157    -10   -104       C  
ATOM   3057  C   LYS B 409      -1.773  59.570  39.728  1.00 29.32           C  
ANISOU 3057  C   LYS B 409     3585   3990   3563    189      3     13       C  
ATOM   3058  O   LYS B 409      -1.533  58.750  40.608  1.00 16.34           O  
ANISOU 3058  O   LYS B 409     1928   2301   1979    188    -12     80       O  
ATOM   3059  CB  LYS B 409      -1.953  58.068  37.735  1.00 21.05           C  
ANISOU 3059  CB  LYS B 409     2465   2856   2676    105    -33   -117       C  
ATOM   3060  CG  LYS B 409      -3.474  58.083  37.755  1.00 21.58           C  
ANISOU 3060  CG  LYS B 409     2498   2977   2724     85    -18    -55       C  
ATOM   3061  CD  LYS B 409      -4.049  56.910  36.978  1.00 26.52           C  
ANISOU 3061  CD  LYS B 409     3059   3547   3472     30    -49    -95       C  
ATOM   3062  CE  LYS B 409      -3.800  55.590  37.689  1.00 24.62           C  
ANISOU 3062  CE  LYS B 409     2782   3201   3373      2    -82    -36       C  
ATOM   3063  NZ  LYS B 409      -4.628  55.442  38.916  1.00 19.13           N  
ANISOU 3063  NZ  LYS B 409     2067   2528   2674     -1    -62    119       N  
ATOM   3064  N   LEU B 410      -2.439  60.699  39.948  1.00 25.32           N  
ANISOU 3064  N   LEU B 410     3102   3571   2947    222     30     39       N  
ATOM   3065  CA  LEU B 410      -3.038  60.991  41.239  1.00 28.94           C  
ANISOU 3065  CA  LEU B 410     3565   4090   3342    261     44    142       C  
ATOM   3066  C   LEU B 410      -4.538  60.738  41.201  1.00 34.46           C  
ANISOU 3066  C   LEU B 410     4216   4841   4034    238     64    206       C  
ATOM   3067  O   LEU B 410      -5.232  61.198  40.290  1.00 31.44           O  
ANISOU 3067  O   LEU B 410     3826   4496   3624    223     75    162       O  
ATOM   3068  CB  LEU B 410      -2.756  62.436  41.652  1.00 29.14           C  
ANISOU 3068  CB  LEU B 410     3643   4177   3252    325     53    122       C  
ATOM   3069  CG  LEU B 410      -3.487  62.887  42.918  1.00 25.17           C  
ANISOU 3069  CG  LEU B 410     3141   3760   2662    381     68    209       C  
ATOM   3070  CD1 LEU B 410      -2.992  62.118  44.138  1.00 19.78           C  
ANISOU 3070  CD1 LEU B 410     2451   3062   2003    402     56    285       C  
ATOM   3071  CD2 LEU B 410      -3.353  64.386  43.126  1.00 26.00           C  
ANISOU 3071  CD2 LEU B 410     3294   3920   2665    445     68    166       C  
ATOM   3072  N   THR B 411      -5.035  59.996  42.187  1.00 36.00           N  
ANISOU 3072  N   THR B 411     4375   5045   4258    234     69    317       N  
ATOM   3073  CA  THR B 411      -6.463  59.722  42.281  1.00 33.63           C  
ANISOU 3073  CA  THR B 411     4020   4801   3958    211     91    395       C  
ATOM   3074  C   THR B 411      -7.089  60.543  43.405  1.00 36.26           C  
ANISOU 3074  C   THR B 411     4361   5252   4165    276    122    477       C  
ATOM   3075  O   THR B 411      -6.662  60.469  44.558  1.00 45.53           O  
ANISOU 3075  O   THR B 411     5545   6448   5305    320    124    545       O  
ATOM   3076  CB  THR B 411      -6.747  58.224  42.523  1.00 28.82           C  
ANISOU 3076  CB  THR B 411     3345   4120   3486    151     77    477       C  
ATOM   3077  OG1 THR B 411      -6.133  57.444  41.491  1.00 29.33           O  
ANISOU 3077  OG1 THR B 411     3400   4072   3673    100     40    384       O  
ATOM   3078  CG2 THR B 411      -8.247  57.961  42.515  1.00 22.95           C  
ANISOU 3078  CG2 THR B 411     2533   3431   2755    118    100    554       C  
ATOM   3079  N   VAL B 412      -8.097  61.338  43.065  1.00 34.94           N  
ANISOU 3079  N   VAL B 412     4186   5168   3923    291    144    465       N  
ATOM   3080  CA  VAL B 412      -8.812  62.126  44.058  1.00 35.22           C  
ANISOU 3080  CA  VAL B 412     4220   5327   3837    359    172    531       C  
ATOM   3081  C   VAL B 412     -10.312  61.892  43.936  1.00 37.63           C  
ANISOU 3081  C   VAL B 412     4456   5702   4141    332    200    597       C  
ATOM   3082  O   VAL B 412     -10.794  61.437  42.899  1.00 36.66           O  
ANISOU 3082  O   VAL B 412     4298   5534   4095    268    192    561       O  
ATOM   3083  CB  VAL B 412      -8.523  63.636  43.914  1.00 27.54           C  
ANISOU 3083  CB  VAL B 412     3311   4400   2754    427    168    443       C  
ATOM   3084  CG1 VAL B 412      -7.023  63.900  43.910  1.00 26.74           C  
ANISOU 3084  CG1 VAL B 412     3271   4223   2668    445    139    371       C  
ATOM   3085  CG2 VAL B 412      -9.165  64.181  42.650  1.00 17.41           C  
ANISOU 3085  CG2 VAL B 412     2026   3122   1466    402    170    372       C  
ATOM   3086  N   ASP B 413     -11.046  62.188  45.003  1.00 40.55           N  
ANISOU 3086  N   ASP B 413     4798   6186   4422    385    230    689       N  
ATOM   3087  CA  ASP B 413     -12.499  62.186  44.936  1.00 37.04           C  
ANISOU 3087  CA  ASP B 413     4286   5830   3957    372    261    747       C  
ATOM   3088  C   ASP B 413     -12.933  63.240  43.934  1.00 30.38           C  
ANISOU 3088  C   ASP B 413     3470   5012   3061    388    255    640       C  
ATOM   3089  O   ASP B 413     -12.366  64.334  43.900  1.00 33.71           O  
ANISOU 3089  O   ASP B 413     3960   5446   3403    449    243    562       O  
ATOM   3090  CB  ASP B 413     -13.121  62.461  46.306  1.00 34.30           C  
ANISOU 3090  CB  ASP B 413     3908   5624   3501    443    298    857       C  
ATOM   3091  CG  ASP B 413     -12.995  61.283  47.251  1.00 46.32           C  
ANISOU 3091  CG  ASP B 413     5380   7139   5081    418    312    999       C  
ATOM   3092  OD1 ASP B 413     -12.977  60.131  46.765  1.00 53.92           O  
ANISOU 3092  OD1 ASP B 413     6301   7996   6191    327    299   1034       O  
ATOM   3093  OD2 ASP B 413     -12.920  61.508  48.479  1.00 49.37           O  
ANISOU 3093  OD2 ASP B 413     5765   7627   5368    492    332   1074       O  
ATOM   3094  N   LYS B 414     -13.923  62.909  43.110  1.00 29.92           N  
ANISOU 3094  N   LYS B 414     3356   4958   3054    333    259    638       N  
ATOM   3095  CA  LYS B 414     -14.435  63.848  42.117  1.00 28.24           C  
ANISOU 3095  CA  LYS B 414     3162   4777   2791    349    253    548       C  
ATOM   3096  C   LYS B 414     -14.859  65.159  42.765  1.00 31.67           C  
ANISOU 3096  C   LYS B 414     3623   5327   3083    446    270    547       C  
ATOM   3097  O   LYS B 414     -14.603  66.235  42.229  1.00 28.75           O  
ANISOU 3097  O   LYS B 414     3310   4956   2658    487    254    460       O  
ATOM   3098  CB  LYS B 414     -15.613  63.238  41.352  1.00 31.33           C  
ANISOU 3098  CB  LYS B 414     3474   5181   3250    284    256    562       C  
ATOM   3099  CG  LYS B 414     -16.331  64.229  40.446  1.00 30.91           C  
ANISOU 3099  CG  LYS B 414     3429   5185   3130    310    252    487       C  
ATOM   3100  CD  LYS B 414     -17.220  63.524  39.436  1.00 39.80           C  
ANISOU 3100  CD  LYS B 414     4484   6297   4343    238    239    469       C  
ATOM   3101  CE  LYS B 414     -18.401  62.842  40.108  1.00 37.60           C  
ANISOU 3101  CE  LYS B 414     4105   6081   4099    210    265    582       C  
ATOM   3102  NZ  LYS B 414     -19.264  62.129  39.122  1.00 43.49           N  
ANISOU 3102  NZ  LYS B 414     4774   6806   4945    136    244    556       N  
ATOM   3103  N   SER B 415     -15.494  65.054  43.929  1.00 32.10           N  
ANISOU 3103  N   SER B 415     3631   5482   3082    486    302    647       N  
ATOM   3104  CA  SER B 415     -15.975  66.219  44.664  1.00 36.73           C  
ANISOU 3104  CA  SER B 415     4231   6193   3531    589    316    644       C  
ATOM   3105  C   SER B 415     -14.855  67.217  44.951  1.00 38.38           C  
ANISOU 3105  C   SER B 415     4529   6343   3709    653    279    550       C  
ATOM   3106  O   SER B 415     -15.034  68.423  44.780  1.00 31.62           O  
ANISOU 3106  O   SER B 415     3703   5471   2839    700    253    463       O  
ATOM   3107  CB  SER B 415     -16.634  65.789  45.979  1.00 31.75           C  
ANISOU 3107  CB  SER B 415     3532   5659   2872    618    349    760       C  
ATOM   3108  OG  SER B 415     -15.674  65.307  46.901  1.00 34.14           O  
ANISOU 3108  OG  SER B 415     3857   5939   3178    633    347    808       O  
ATOM   3109  N   ARG B 416     -13.703  66.710  45.386  1.00 38.87           N  
ANISOU 3109  N   ARG B 416     4626   6362   3781    649    273    569       N  
ATOM   3110  CA  ARG B 416     -12.552  67.566  45.675  1.00 35.40           C  
ANISOU 3110  CA  ARG B 416     4262   5855   3334    700    234    478       C  
ATOM   3111  C   ARG B 416     -12.103  68.319  44.433  1.00 29.81           C  
ANISOU 3111  C   ARG B 416     3609   5072   2644    683    208    374       C  
ATOM   3112  O   ARG B 416     -11.680  69.472  44.508  1.00 26.41           O  
ANISOU 3112  O   ARG B 416     3224   4599   2212    729    176    295       O  
ATOM   3113  CB  ARG B 416     -11.390  66.746  46.243  1.00 35.05           C  
ANISOU 3113  CB  ARG B 416     4239   5773   3305    691    229    520       C  
ATOM   3114  CG  ARG B 416     -11.490  66.494  47.735  1.00 31.91           C  
ANISOU 3114  CG  ARG B 416     3810   5443   2873    743    240    594       C  
ATOM   3115  CD  ARG B 416     -10.153  66.697  48.419  1.00 35.02           C  
ANISOU 3115  CD  ARG B 416     4257   5791   3256    787    207    553       C  
ATOM   3116  NE  ARG B 416      -9.198  65.649  48.077  1.00 36.44           N  
ANISOU 3116  NE  ARG B 416     4454   5888   3505    727    200    586       N  
ATOM   3117  CZ  ARG B 416      -7.879  65.794  48.133  1.00 36.83           C  
ANISOU 3117  CZ  ARG B 416     4557   5857   3580    739    163    521       C  
ATOM   3118  NH1 ARG B 416      -7.086  64.786  47.805  1.00 33.71           N  
ANISOU 3118  NH1 ARG B 416     4162   5354   3292    671    152    534       N  
ATOM   3119  NH2 ARG B 416      -7.352  66.949  48.510  1.00 37.42           N  
ANISOU 3119  NH2 ARG B 416     4682   5955   3582    819    135    438       N  
ATOM   3120  N   TRP B 417     -12.208  67.655  43.288  1.00 25.58           N  
ANISOU 3120  N   TRP B 417     3057   4489   2172    603    214    369       N  
ATOM   3121  CA  TRP B 417     -11.871  68.272  42.013  1.00 27.61           C  
ANISOU 3121  CA  TRP B 417     3355   4684   2453    581    193    280       C  
ATOM   3122  C   TRP B 417     -12.901  69.328  41.633  1.00 30.56           C  
ANISOU 3122  C   TRP B 417     3724   5121   2768    623    194    255       C  
ATOM   3123  O   TRP B 417     -12.545  70.430  41.221  1.00 30.03           O  
ANISOU 3123  O   TRP B 417     3701   5000   2710    647    166    188       O  
ATOM   3124  CB  TRP B 417     -11.772  67.212  40.917  1.00 22.01           C  
ANISOU 3124  CB  TRP B 417     2618   3901   1844    485    192    267       C  
ATOM   3125  CG  TRP B 417     -11.544  67.771  39.545  1.00 20.53           C  
ANISOU 3125  CG  TRP B 417     2459   3675   1666    465    176    186       C  
ATOM   3126  CD1 TRP B 417     -12.456  67.860  38.537  1.00 18.48           C  
ANISOU 3126  CD1 TRP B 417     2170   3449   1404    442    179    166       C  
ATOM   3127  CD2 TRP B 417     -10.324  68.315  39.031  1.00 20.19           C  
ANISOU 3127  CD2 TRP B 417     2475   3562   1633    468    157    120       C  
ATOM   3128  NE1 TRP B 417     -11.882  68.424  37.423  1.00 23.08           N  
ANISOU 3128  NE1 TRP B 417     2790   3993   1985    434    164     97       N  
ATOM   3129  CE2 TRP B 417     -10.572  68.714  37.703  1.00 26.68           C  
ANISOU 3129  CE2 TRP B 417     3299   4385   2452    447    153     72       C  
ATOM   3130  CE3 TRP B 417      -9.047  68.506  39.566  1.00 20.61           C  
ANISOU 3130  CE3 TRP B 417     2575   3558   1699    487    143    100       C  
ATOM   3131  CZ2 TRP B 417      -9.588  69.292  36.902  1.00 19.16           C  
ANISOU 3131  CZ2 TRP B 417     2391   3382   1507    443    142     16       C  
ATOM   3132  CZ3 TRP B 417      -8.072  69.081  38.770  1.00 25.88           C  
ANISOU 3132  CZ3 TRP B 417     3284   4167   2383    479    129     38       C  
ATOM   3133  CH2 TRP B 417      -8.349  69.468  37.454  1.00 19.99           C  
ANISOU 3133  CH2 TRP B 417     2536   3427   1631    456    131      2       C  
ATOM   3134  N   GLN B 418     -14.176  68.982  41.785  1.00 28.13           N  
ANISOU 3134  N   GLN B 418     3350   4893   2446    617    217    309       N  
ATOM   3135  CA  GLN B 418     -15.275  69.879  41.446  1.00 29.20           C  
ANISOU 3135  CA  GLN B 418     3465   5059   2569    645    208    283       C  
ATOM   3136  C   GLN B 418     -15.259  71.160  42.272  1.00 36.12           C  
ANISOU 3136  C   GLN B 418     4369   5924   3432    724    183    246       C  
ATOM   3137  O   GLN B 418     -15.750  72.196  41.826  1.00 31.51           O  
ANISOU 3137  O   GLN B 418     3794   5333   2845    755    164    203       O  
ATOM   3138  CB  GLN B 418     -16.617  69.172  41.635  1.00 30.59           C  
ANISOU 3138  CB  GLN B 418     3556   5337   2730    627    241    358       C  
ATOM   3139  CG  GLN B 418     -16.837  67.950  40.759  1.00 46.29           C  
ANISOU 3139  CG  GLN B 418     5498   7321   4770    538    257    385       C  
ATOM   3140  CD  GLN B 418     -17.297  68.299  39.355  1.00 66.92           C  
ANISOU 3140  CD  GLN B 418     8109   9922   7394    513    239    319       C  
ATOM   3141  OE1 GLN B 418     -17.017  69.383  38.842  1.00 71.33           O  
ANISOU 3141  OE1 GLN B 418     8725  10473   7906    557    221    257       O  
ATOM   3142  NE2 GLN B 418     -18.015  67.375  38.727  1.00 75.78           N  
ANISOU 3142  NE2 GLN B 418     9162  11044   8586    443    240    333       N  
ATOM   3143  N   GLN B 419     -14.701  71.085  43.476  1.00 35.74           N  
ANISOU 3143  N   GLN B 419     4328   5879   3371    761    182    264       N  
ATOM   3144  CA  GLN B 419     -14.724  72.209  44.408  1.00 30.07           C  
ANISOU 3144  CA  GLN B 419     3622   5171   2632    846    158    226       C  
ATOM   3145  C   GLN B 419     -13.562  73.178  44.203  1.00 34.95           C  
ANISOU 3145  C   GLN B 419     4312   5699   3269    871    120    149       C  
ATOM   3146  O   GLN B 419     -13.412  74.138  44.957  1.00 30.99           O  
ANISOU 3146  O   GLN B 419     3824   5201   2751    945     93    108       O  
ATOM   3147  CB  GLN B 419     -14.731  71.687  45.848  1.00 30.02           C  
ANISOU 3147  CB  GLN B 419     3580   5230   2595    884    174    280       C  
ATOM   3148  CG  GLN B 419     -16.029  71.005  46.226  1.00 37.18           C  
ANISOU 3148  CG  GLN B 419     4404   6242   3479    878    211    363       C  
ATOM   3149  CD  GLN B 419     -15.905  70.131  47.457  1.00 37.26           C  
ANISOU 3149  CD  GLN B 419     4375   6314   3467    890    236    445       C  
ATOM   3150  OE1 GLN B 419     -14.913  70.197  48.184  1.00 35.53           O  
ANISOU 3150  OE1 GLN B 419     4191   6068   3241    922    220    427       O  
ATOM   3151  NE2 GLN B 419     -16.914  69.301  47.696  1.00 28.42           N  
ANISOU 3151  NE2 GLN B 419     3178   5281   2338    865    274    541       N  
ATOM   3152  N   GLY B 420     -12.747  72.923  43.188  1.00 24.40           N  
ANISOU 3152  N   GLY B 420     3016   4292   1963    813    115    129       N  
ATOM   3153  CA  GLY B 420     -11.702  73.852  42.822  1.00 24.54           C  
ANISOU 3153  CA  GLY B 420     3095   4229   2000    829     82     66       C  
ATOM   3154  C   GLY B 420     -10.404  73.704  43.591  1.00 26.10           C  
ANISOU 3154  C   GLY B 420     3327   4388   2201    847     65     48       C  
ATOM   3155  O   GLY B 420      -9.568  74.604  43.581  1.00 29.48           O  
ANISOU 3155  O   GLY B 420     3800   4762   2641    879     31     -7       O  
ATOM   3156  N   ASN B 421     -10.229  72.573  44.262  1.00 25.94           N  
ANISOU 3156  N   ASN B 421     3285   4400   2171    830     86     97       N  
ATOM   3157  CA  ASN B 421      -8.968  72.303  44.942  1.00 27.56           C  
ANISOU 3157  CA  ASN B 421     3521   4572   2378    846     69     84       C  
ATOM   3158  C   ASN B 421      -7.796  72.229  43.959  1.00 30.90           C  
ANISOU 3158  C   ASN B 421     3993   4915   2834    801     57     44       C  
ATOM   3159  O   ASN B 421      -7.886  71.589  42.911  1.00 24.26           O  
ANISOU 3159  O   ASN B 421     3147   4064   2009    738     79     59       O  
ATOM   3160  CB  ASN B 421      -9.061  71.006  45.757  1.00 24.01           C  
ANISOU 3160  CB  ASN B 421     3035   4177   1908    834     97    163       C  
ATOM   3161  CG  ASN B 421      -9.864  71.182  47.038  1.00 28.71           C  
ANISOU 3161  CG  ASN B 421     3585   4858   2465    898    104    196       C  
ATOM   3162  OD1 ASN B 421      -9.387  71.781  48.005  1.00 34.71           O  
ANISOU 3162  OD1 ASN B 421     4357   5626   3205    967     78    159       O  
ATOM   3163  ND2 ASN B 421     -11.084  70.656  47.054  1.00 22.70           N  
ANISOU 3163  ND2 ASN B 421     2766   4169   1691    879    139    263       N  
ATOM   3164  N   VAL B 422      -6.704  72.903  44.304  1.00 28.92           N  
ANISOU 3164  N   VAL B 422     3784   4613   2591    838     20    -11       N  
ATOM   3165  CA  VAL B 422      -5.526  72.935  43.451  1.00 25.78           C  
ANISOU 3165  CA  VAL B 422     3430   4143   2222    803      8    -53       C  
ATOM   3166  C   VAL B 422      -4.570  71.796  43.782  1.00 29.05           C  
ANISOU 3166  C   VAL B 422     3839   4518   2681    764     11    -36       C  
ATOM   3167  O   VAL B 422      -4.260  71.547  44.942  1.00 34.73           O  
ANISOU 3167  O   VAL B 422     4558   5267   3372    811     -3    -23       O  
ATOM   3168  CB  VAL B 422      -4.796  74.281  43.574  1.00 27.39           C  
ANISOU 3168  CB  VAL B 422     3675   4295   2437    855    -40   -123       C  
ATOM   3169  CG1 VAL B 422      -3.502  74.268  42.778  1.00 27.29           C  
ANISOU 3169  CG1 VAL B 422     3682   4177   2509    793    -50   -154       C  
ATOM   3170  CG2 VAL B 422      -5.702  75.394  43.091  1.00 28.22           C  
ANISOU 3170  CG2 VAL B 422     3778   4407   2539    877    -47   -134       C  
ATOM   3171  N   PHE B 423      -4.113  71.099  42.747  1.00 23.70           N  
ANISOU 3171  N   PHE B 423     3154   3776   2074    682     27    -37       N  
ATOM   3172  CA  PHE B 423      -3.198  69.979  42.922  1.00 22.25           C  
ANISOU 3172  CA  PHE B 423     2962   3542   1950    640     27    -27       C  
ATOM   3173  C   PHE B 423      -1.893  70.244  42.196  1.00 23.65           C  
ANISOU 3173  C   PHE B 423     3162   3630   2193    606     10    -87       C  
ATOM   3174  O   PHE B 423      -1.889  70.771  41.086  1.00 31.74           O  
ANISOU 3174  O   PHE B 423     4193   4632   3235    575     18   -114       O  
ATOM   3175  CB  PHE B 423      -3.840  68.683  42.432  1.00 17.45           C  
ANISOU 3175  CB  PHE B 423     2311   2942   1377    575     58     23       C  
ATOM   3176  CG  PHE B 423      -5.095  68.319  43.166  1.00 20.34           C  
ANISOU 3176  CG  PHE B 423     2642   3396   1689    600     79     97       C  
ATOM   3177  CD1 PHE B 423      -5.050  67.483  44.268  1.00 20.47           C  
ANISOU 3177  CD1 PHE B 423     2638   3437   1703    616     81    162       C  
ATOM   3178  CD2 PHE B 423      -6.322  68.822  42.762  1.00 27.90           C  
ANISOU 3178  CD2 PHE B 423     3583   4418   2599    609     97    108       C  
ATOM   3179  CE1 PHE B 423      -6.205  67.146  44.948  1.00 26.67           C  
ANISOU 3179  CE1 PHE B 423     3382   4314   2438    636    106    244       C  
ATOM   3180  CE2 PHE B 423      -7.480  68.490  43.438  1.00 17.37           C  
ANISOU 3180  CE2 PHE B 423     2208   3173   1217    631    119    179       C  
ATOM   3181  CZ  PHE B 423      -7.424  67.653  44.531  1.00 23.71           C  
ANISOU 3181  CZ  PHE B 423     2986   4005   2017    643    126    250       C  
ATOM   3182  N   SER B 424      -0.782  69.870  42.827  1.00 21.03           N  
ANISOU 3182  N   SER B 424     2839   3254   1897    613    -12   -103       N  
ATOM   3183  CA  SER B 424       0.530  70.152  42.265  1.00 21.02           C  
ANISOU 3183  CA  SER B 424     2853   3174   1961    586    -29   -159       C  
ATOM   3184  C   SER B 424       1.363  68.902  42.015  1.00 29.69           C  
ANISOU 3184  C   SER B 424     3932   4222   3128    534    -24   -161       C  
ATOM   3185  O   SER B 424       1.434  68.004  42.852  1.00 25.22           O  
ANISOU 3185  O   SER B 424     3354   3661   2568    546    -31   -127       O  
ATOM   3186  CB  SER B 424       1.303  71.106  43.176  1.00 20.63           C  
ANISOU 3186  CB  SER B 424     2830   3105   1904    648    -74   -200       C  
ATOM   3187  OG  SER B 424       0.754  72.409  43.124  1.00 38.72           O  
ANISOU 3187  OG  SER B 424     5139   5415   4157    689    -87   -220       O  
ATOM   3188  N   CYS B 425       1.995  68.859  40.848  1.00 29.19           N  
ANISOU 3188  N   CYS B 425     3861   4113   3116    482    -13   -199       N  
ATOM   3189  CA  CYS B 425       2.938  67.800  40.523  1.00 20.11           C  
ANISOU 3189  CA  CYS B 425     2691   2911   2037    441    -13   -222       C  
ATOM   3190  C   CYS B 425       4.360  68.327  40.667  1.00 21.58           C  
ANISOU 3190  C   CYS B 425     2890   3046   2265    451    -38   -270       C  
ATOM   3191  O   CYS B 425       4.797  69.175  39.895  1.00 30.10           O  
ANISOU 3191  O   CYS B 425     3972   4110   3356    435    -32   -300       O  
ATOM   3192  CB  CYS B 425       2.683  67.276  39.104  1.00 20.88           C  
ANISOU 3192  CB  CYS B 425     2762   3011   2162    382     16   -240       C  
ATOM   3193  SG  CYS B 425       3.870  66.042  38.533  1.00 29.40           S  
ANISOU 3193  SG  CYS B 425     3811   4030   3330    339     12   -290       S  
ATOM   3194  N   SER B 426       5.074  67.831  41.674  1.00 20.22           N  
ANISOU 3194  N   SER B 426     2719   2848   2115    477    -67   -272       N  
ATOM   3195  CA  SER B 426       6.444  68.260  41.914  1.00 23.25           C  
ANISOU 3195  CA  SER B 426     3107   3182   2544    489    -97   -322       C  
ATOM   3196  C   SER B 426       7.431  67.253  41.330  1.00 24.04           C  
ANISOU 3196  C   SER B 426     3179   3235   2719    446    -92   -352       C  
ATOM   3197  O   SER B 426       7.318  66.048  41.558  1.00 27.22           O  
ANISOU 3197  O   SER B 426     3568   3629   3146    437    -93   -331       O  
ATOM   3198  CB  SER B 426       6.697  68.448  43.411  1.00 22.03           C  
ANISOU 3198  CB  SER B 426     2970   3037   2362    557   -140   -317       C  
ATOM   3199  OG  SER B 426       5.790  69.385  43.963  1.00 29.58           O  
ANISOU 3199  OG  SER B 426     3948   4045   3245    607   -148   -301       O  
ATOM   3200  N   VAL B 427       8.394  67.754  40.567  1.00 26.21           N  
ANISOU 3200  N   VAL B 427     3442   3480   3036    420    -88   -399       N  
ATOM   3201  CA  VAL B 427       9.377  66.895  39.933  1.00 25.76           C  
ANISOU 3201  CA  VAL B 427     3353   3390   3045    385    -82   -439       C  
ATOM   3202  C   VAL B 427      10.788  67.284  40.352  1.00 29.43           C  
ANISOU 3202  C   VAL B 427     3810   3812   3561    399   -113   -481       C  
ATOM   3203  O   VAL B 427      11.138  68.464  40.375  1.00 37.97           O  
ANISOU 3203  O   VAL B 427     4898   4885   4643    406   -122   -493       O  
ATOM   3204  CB  VAL B 427       9.253  66.946  38.399  1.00 16.52           C  
ANISOU 3204  CB  VAL B 427     2158   2244   1876    337    -38   -458       C  
ATOM   3205  CG1 VAL B 427      10.195  65.942  37.763  1.00 17.71           C  
ANISOU 3205  CG1 VAL B 427     2268   2372   2088    311    -33   -509       C  
ATOM   3206  CG2 VAL B 427       7.827  66.662  37.973  1.00 16.69           C  
ANISOU 3206  CG2 VAL B 427     2184   2311   1848    326    -14   -423       C  
ATOM   3207  N   MET B 428      11.592  66.282  40.695  1.00 30.04           N  
ANISOU 3207  N   MET B 428     3868   3856   3690    404   -133   -504       N  
ATOM   3208  CA  MET B 428      12.976  66.511  41.088  1.00 26.66           C  
ANISOU 3208  CA  MET B 428     3425   3388   3316    417   -165   -549       C  
ATOM   3209  C   MET B 428      13.955  65.756  40.188  1.00 17.16           C  
ANISOU 3209  C   MET B 428     2176   2165   2179    382   -149   -598       C  
ATOM   3210  O   MET B 428      13.876  64.538  40.040  1.00 18.12           O  
ANISOU 3210  O   MET B 428     2284   2276   2326    377   -148   -604       O  
ATOM   3211  CB  MET B 428      13.167  66.123  42.554  1.00 23.93           C  
ANISOU 3211  CB  MET B 428     3098   3029   2966    473   -216   -536       C  
ATOM   3212  CG  MET B 428      12.514  67.104  43.514  1.00 25.82           C  
ANISOU 3212  CG  MET B 428     3373   3298   3138    522   -240   -511       C  
ATOM   3213  SD  MET B 428      12.068  66.371  45.091  1.00 35.40           S  
ANISOU 3213  SD  MET B 428     4608   4542   4300    591   -277   -460       S  
ATOM   3214  CE  MET B 428      10.579  65.484  44.632  1.00 22.73           C  
ANISOU 3214  CE  MET B 428     3005   2971   2661    559   -227   -384       C  
ATOM   3215  N   HIS B 429      14.875  66.496  39.579  1.00 17.93           N  
ANISOU 3215  N   HIS B 429     2247   2258   2310    361   -138   -633       N  
ATOM   3216  CA  HIS B 429      15.806  65.936  38.603  1.00 20.29           C  
ANISOU 3216  CA  HIS B 429     2493   2557   2659    331   -115   -681       C  
ATOM   3217  C   HIS B 429      17.020  66.853  38.491  1.00 26.55           C  
ANISOU 3217  C   HIS B 429     3254   3336   3499    320   -120   -708       C  
ATOM   3218  O   HIS B 429      16.895  68.065  38.654  1.00 31.27           O  
ANISOU 3218  O   HIS B 429     3866   3929   4087    317   -125   -683       O  
ATOM   3219  CB  HIS B 429      15.120  65.765  37.245  1.00 20.06           C  
ANISOU 3219  CB  HIS B 429     2448   2581   2593    294    -60   -677       C  
ATOM   3220  CG  HIS B 429      15.981  65.130  36.197  1.00 24.60           C  
ANISOU 3220  CG  HIS B 429     2965   3177   3204    274    -34   -735       C  
ATOM   3221  ND1 HIS B 429      16.853  65.853  35.413  1.00 29.35           N  
ANISOU 3221  ND1 HIS B 429     3523   3809   3819    251     -3   -749       N  
ATOM   3222  CD2 HIS B 429      16.102  63.840  35.801  1.00 19.59           C  
ANISOU 3222  CD2 HIS B 429     2303   2541   2598    277    -36   -784       C  
ATOM   3223  CE1 HIS B 429      17.477  65.037  34.583  1.00 28.46           C  
ANISOU 3223  CE1 HIS B 429     3358   3727   3728    245     17   -806       C  
ATOM   3224  NE2 HIS B 429      17.038  63.810  34.796  1.00 27.72           N  
ANISOU 3224  NE2 HIS B 429     3275   3611   3647    263     -6   -836       N  
ATOM   3225  N   GLU B 430      18.189  66.281  38.214  1.00 29.99           N  
ANISOU 3225  N   GLU B 430     3641   3761   3995    314   -122   -759       N  
ATOM   3226  CA  GLU B 430      19.428  67.051  38.272  1.00 29.47           C  
ANISOU 3226  CA  GLU B 430     3535   3675   3988    305   -134   -783       C  
ATOM   3227  C   GLU B 430      19.527  68.117  37.182  1.00 32.29           C  
ANISOU 3227  C   GLU B 430     3860   4067   4340    259    -83   -756       C  
ATOM   3228  O   GLU B 430      20.217  69.124  37.354  1.00 34.24           O  
ANISOU 3228  O   GLU B 430     4085   4288   4636    245    -97   -750       O  
ATOM   3229  CB  GLU B 430      20.642  66.123  38.208  1.00 27.79           C  
ANISOU 3229  CB  GLU B 430     3270   3450   3839    313   -146   -845       C  
ATOM   3230  CG  GLU B 430      20.838  65.411  36.883  1.00 48.02           C  
ANISOU 3230  CG  GLU B 430     5783   6065   6399    288    -93   -876       C  
ATOM   3231  CD  GLU B 430      22.163  64.663  36.814  1.00 54.80           C  
ANISOU 3231  CD  GLU B 430     6580   6913   7327    300   -107   -945       C  
ATOM   3232  OE1 GLU B 430      23.206  65.315  36.584  1.00 60.10           O  
ANISOU 3232  OE1 GLU B 430     7200   7594   8042    283    -98   -959       O  
ATOM   3233  OE2 GLU B 430      22.162  63.427  36.989  1.00 47.14           O  
ANISOU 3233  OE2 GLU B 430     5612   5923   6376    328   -130   -983       O  
ATOM   3234  N   ALA B 431      18.826  67.914  36.072  1.00 30.57           N  
ANISOU 3234  N   ALA B 431     3638   3910   4069    235    -28   -736       N  
ATOM   3235  CA  ALA B 431      18.899  68.849  34.948  1.00 33.30           C  
ANISOU 3235  CA  ALA B 431     3949   4304   4400    194     25   -697       C  
ATOM   3236  C   ALA B 431      17.921  70.015  35.110  1.00 34.37           C  
ANISOU 3236  C   ALA B 431     4132   4428   4500    189     23   -631       C  
ATOM   3237  O   ALA B 431      17.793  70.856  34.215  1.00 36.89           O  
ANISOU 3237  O   ALA B 431     4430   4782   4804    157     65   -581       O  
ATOM   3238  CB  ALA B 431      18.642  68.126  33.641  1.00 20.52           C  
ANISOU 3238  CB  ALA B 431     2297   2770   2730    180     83   -712       C  
ATOM   3239  N   LEU B 432      17.236  70.059  36.251  1.00 30.53           N  
ANISOU 3239  N   LEU B 432     3704   3897   3999    225    -26   -628       N  
ATOM   3240  CA  LEU B 432      16.336  71.164  36.567  1.00 25.41           C  
ANISOU 3240  CA  LEU B 432     3101   3233   3322    232    -39   -579       C  
ATOM   3241  C   LEU B 432      17.018  72.178  37.470  1.00 26.05           C  
ANISOU 3241  C   LEU B 432     3182   3244   3473    245    -95   -590       C  
ATOM   3242  O   LEU B 432      17.836  71.815  38.310  1.00 25.23           O  
ANISOU 3242  O   LEU B 432     3069   3103   3416    268   -139   -638       O  
ATOM   3243  CB  LEU B 432      15.064  70.649  37.238  1.00 21.36           C  
ANISOU 3243  CB  LEU B 432     2646   2729   2740    269    -57   -570       C  
ATOM   3244  CG  LEU B 432      14.041  69.916  36.370  1.00 30.02           C  
ANISOU 3244  CG  LEU B 432     3749   3889   3769    256    -11   -552       C  
ATOM   3245  CD1 LEU B 432      13.036  69.182  37.246  1.00 31.68           C  
ANISOU 3245  CD1 LEU B 432     4003   4097   3936    291    -36   -546       C  
ATOM   3246  CD2 LEU B 432      13.331  70.880  35.441  1.00 24.80           C  
ANISOU 3246  CD2 LEU B 432     3092   3267   3066    233     27   -500       C  
ATOM   3247  N   HIS B 433      16.680  73.449  37.286  1.00 32.24           N  
ANISOU 3247  N   HIS B 433     3974   4007   4270    233    -97   -547       N  
ATOM   3248  CA  HIS B 433      17.136  74.500  38.185  1.00 26.84           C  
ANISOU 3248  CA  HIS B 433     3293   3247   3657    251   -162   -565       C  
ATOM   3249  C   HIS B 433      16.671  74.164  39.596  1.00 34.17           C  
ANISOU 3249  C   HIS B 433     4273   4160   4548    319   -224   -609       C  
ATOM   3250  O   HIS B 433      15.515  73.785  39.800  1.00 32.71           O  
ANISOU 3250  O   HIS B 433     4134   4015   4278    347   -214   -590       O  
ATOM   3251  CB  HIS B 433      16.600  75.862  37.741  1.00 27.76           C  
ANISOU 3251  CB  HIS B 433     3417   3338   3791    233   -159   -509       C  
ATOM   3252  CG  HIS B 433      17.253  77.029  38.418  1.00 43.23           C  
ANISOU 3252  CG  HIS B 433     5362   5207   5857    239   -227   -531       C  
ATOM   3253  ND1 HIS B 433      18.482  77.521  38.034  1.00 48.26           N  
ANISOU 3253  ND1 HIS B 433     5932   5801   6605    191   -227   -525       N  
ATOM   3254  CD2 HIS B 433      16.832  77.822  39.432  1.00 43.13           C  
ANISOU 3254  CD2 HIS B 433     5386   5140   5861    289   -299   -563       C  
ATOM   3255  CE1 HIS B 433      18.797  78.557  38.792  1.00 46.56           C  
ANISOU 3255  CE1 HIS B 433     5714   5496   6482    207   -302   -554       C  
ATOM   3256  NE2 HIS B 433      17.811  78.761  39.648  1.00 46.33           N  
ANISOU 3256  NE2 HIS B 433     5748   5460   6394    270   -349   -583       N  
ATOM   3257  N   ASN B 434      17.585  74.281  40.558  1.00 30.39           N  
ANISOU 3257  N   ASN B 434     3781   3633   4131    347   -287   -666       N  
ATOM   3258  CA  ASN B 434      17.334  73.909  41.949  1.00 30.93           C  
ANISOU 3258  CA  ASN B 434     3889   3702   4160    419   -348   -709       C  
ATOM   3259  C   ASN B 434      16.961  72.437  42.122  1.00 29.03           C  
ANISOU 3259  C   ASN B 434     3667   3514   3849    437   -323   -701       C  
ATOM   3260  O   ASN B 434      16.468  72.048  43.182  1.00 35.32           O  
ANISOU 3260  O   ASN B 434     4501   4330   4590    497   -358   -709       O  
ATOM   3261  CB  ASN B 434      16.219  74.769  42.557  1.00 23.85           C  
ANISOU 3261  CB  ASN B 434     3043   2807   3213    467   -380   -700       C  
ATOM   3262  CG  ASN B 434      16.525  76.248  42.510  1.00 28.97           C  
ANISOU 3262  CG  ASN B 434     3675   3387   3945    458   -421   -714       C  
ATOM   3263  OD1 ASN B 434      17.680  76.663  42.555  1.00 36.76           O  
ANISOU 3263  OD1 ASN B 434     4616   4315   5034    436   -454   -749       O  
ATOM   3264  ND2 ASN B 434      15.477  77.061  42.421  1.00 28.18           N  
ANISOU 3264  ND2 ASN B 434     3607   3288   3811    474   -423   -686       N  
ATOM   3265  N   HIS B 435      17.191  71.632  41.082  1.00 22.97           N  
ANISOU 3265  N   HIS B 435     2870   2770   3086    389   -263   -685       N  
ATOM   3266  CA  HIS B 435      16.767  70.225  41.043  1.00 18.13           C  
ANISOU 3266  CA  HIS B 435     2268   2194   2424    397   -239   -676       C  
ATOM   3267  C   HIS B 435      15.263  70.069  41.265  1.00 25.65           C  
ANISOU 3267  C   HIS B 435     3270   3186   3288    419   -225   -630       C  
ATOM   3268  O   HIS B 435      14.805  68.997  41.650  1.00 31.68           O  
ANISOU 3268  O   HIS B 435     4049   3970   4018    439   -224   -616       O  
ATOM   3269  CB  HIS B 435      17.514  69.391  42.091  1.00 22.55           C  
ANISOU 3269  CB  HIS B 435     2824   2734   3009    440   -289   -714       C  
ATOM   3270  CG  HIS B 435      18.997  69.322  41.886  1.00 27.42           C  
ANISOU 3270  CG  HIS B 435     3386   3319   3714    421   -302   -764       C  
ATOM   3271  ND1 HIS B 435      19.871  69.033  42.912  1.00 27.73           N  
ANISOU 3271  ND1 HIS B 435     3416   3330   3790    464   -363   -808       N  
ATOM   3272  CD2 HIS B 435      19.759  69.484  40.778  1.00 30.64           C  
ANISOU 3272  CD2 HIS B 435     3740   3727   4176    367   -262   -775       C  
ATOM   3273  CE1 HIS B 435      21.107  69.029  42.447  1.00 30.23           C  
ANISOU 3273  CE1 HIS B 435     3675   3625   4187    435   -361   -848       C  
ATOM   3274  NE2 HIS B 435      21.067  69.300  41.155  1.00 33.52           N  
ANISOU 3274  NE2 HIS B 435     4061   4061   4614    375   -298   -827       N  
ATOM   3275  N   TYR B 436      14.499  71.130  41.026  1.00 18.86           N  
ANISOU 3275  N   TYR B 436     2431   2335   2399    416   -216   -602       N  
ATOM   3276  CA  TYR B 436      13.089  71.125  41.392  1.00 20.48           C  
ANISOU 3276  CA  TYR B 436     2681   2581   2521    447   -211   -563       C  
ATOM   3277  C   TYR B 436      12.245  72.023  40.488  1.00 33.51           C  
ANISOU 3277  C   TYR B 436     4339   4250   4143    420   -176   -526       C  
ATOM   3278  O   TYR B 436      12.611  73.166  40.199  1.00 44.18           O  
ANISOU 3278  O   TYR B 436     5681   5568   5537    407   -186   -528       O  
ATOM   3279  CB  TYR B 436      12.930  71.554  42.862  1.00 21.73           C  
ANISOU 3279  CB  TYR B 436     2868   2735   2652    519   -274   -581       C  
ATOM   3280  CG  TYR B 436      11.514  71.490  43.401  1.00 24.04           C  
ANISOU 3280  CG  TYR B 436     3198   3083   2851    561   -269   -541       C  
ATOM   3281  CD1 TYR B 436      10.659  72.585  43.303  1.00 20.17           C  
ANISOU 3281  CD1 TYR B 436     2729   2607   2327    577   -271   -529       C  
ATOM   3282  CD2 TYR B 436      11.037  70.341  44.022  1.00 28.62           C  
ANISOU 3282  CD2 TYR B 436     3787   3703   3384    585   -264   -510       C  
ATOM   3283  CE1 TYR B 436       9.362  72.532  43.801  1.00 21.82           C  
ANISOU 3283  CE1 TYR B 436     2966   2876   2449    619   -264   -495       C  
ATOM   3284  CE2 TYR B 436       9.744  70.279  44.522  1.00 27.54           C  
ANISOU 3284  CE2 TYR B 436     3674   3625   3163    621   -255   -465       C  
ATOM   3285  CZ  TYR B 436       8.912  71.375  44.409  1.00 27.44           C  
ANISOU 3285  CZ  TYR B 436     3681   3635   3111    639   -254   -461       C  
ATOM   3286  OH  TYR B 436       7.631  71.306  44.909  1.00 31.04           O  
ANISOU 3286  OH  TYR B 436     4153   4159   3481    678   -243   -418       O  
ATOM   3287  N   THR B 437      11.117  71.485  40.036  1.00 25.34           N  
ANISOU 3287  N   THR B 437     3318   3265   3043    412   -137   -488       N  
ATOM   3288  CA  THR B 437      10.094  72.290  39.393  1.00 23.84           C  
ANISOU 3288  CA  THR B 437     3143   3104   2811    403   -111   -450       C  
ATOM   3289  C   THR B 437       8.731  71.768  39.799  1.00 20.76           C  
ANISOU 3289  C   THR B 437     2781   2766   2343    431   -103   -419       C  
ATOM   3290  O   THR B 437       8.614  70.660  40.312  1.00 28.21           O  
ANISOU 3290  O   THR B 437     3723   3723   3273    441   -105   -418       O  
ATOM   3291  CB  THR B 437      10.225  72.291  37.859  1.00 29.63           C  
ANISOU 3291  CB  THR B 437     3845   3859   3553    344    -56   -431       C  
ATOM   3292  OG1 THR B 437       9.418  73.340  37.305  1.00 35.70           O  
ANISOU 3292  OG1 THR B 437     4628   4645   4292    341    -42   -389       O  
ATOM   3293  CG2 THR B 437       9.787  70.960  37.278  1.00 18.75           C  
ANISOU 3293  CG2 THR B 437     2454   2528   2141    323    -20   -432       C  
ATOM   3294  N   GLN B 438       7.700  72.569  39.572  1.00 23.33           N  
ANISOU 3294  N   GLN B 438     3125   3118   2621    443    -94   -390       N  
ATOM   3295  CA  GLN B 438       6.354  72.195  39.976  1.00 21.77           C  
ANISOU 3295  CA  GLN B 438     2946   2976   2349    472    -86   -358       C  
ATOM   3296  C   GLN B 438       5.309  72.711  38.992  1.00 23.40           C  
ANISOU 3296  C   GLN B 438     3155   3221   2514    454    -52   -324       C  
ATOM   3297  O   GLN B 438       5.437  73.808  38.454  1.00 24.84           O  
ANISOU 3297  O   GLN B 438     3340   3383   2714    448    -54   -319       O  
ATOM   3298  CB  GLN B 438       6.072  72.720  41.391  1.00 29.44           C  
ANISOU 3298  CB  GLN B 438     3944   3954   3289    545   -133   -368       C  
ATOM   3299  CG  GLN B 438       4.854  72.109  42.055  1.00 30.48           C  
ANISOU 3299  CG  GLN B 438     4084   4154   3344    580   -124   -330       C  
ATOM   3300  CD  GLN B 438       4.469  72.840  43.321  1.00 32.02           C  
ANISOU 3300  CD  GLN B 438     4300   4377   3488    663   -167   -343       C  
ATOM   3301  OE1 GLN B 438       4.846  72.440  44.423  1.00 39.91           O  
ANISOU 3301  OE1 GLN B 438     5302   5389   4473    707   -196   -353       O  
ATOM   3302  NE2 GLN B 438       3.717  73.921  43.172  1.00 24.52           N  
ANISOU 3302  NE2 GLN B 438     3365   3444   2509    690   -173   -346       N  
ATOM   3303  N   LYS B 439       4.281  71.907  38.753  1.00 25.61           N  
ANISOU 3303  N   LYS B 439     3429   3554   2746    445    -24   -297       N  
ATOM   3304  CA  LYS B 439       3.159  72.318  37.920  1.00 32.16           C  
ANISOU 3304  CA  LYS B 439     4260   4433   3528    436      3   -267       C  
ATOM   3305  C   LYS B 439       1.866  72.121  38.692  1.00 34.29           C  
ANISOU 3305  C   LYS B 439     4540   4754   3736    476     -1   -239       C  
ATOM   3306  O   LYS B 439       1.725  71.154  39.440  1.00 33.43           O  
ANISOU 3306  O   LYS B 439     4423   4656   3621    484     -4   -230       O  
ATOM   3307  CB  LYS B 439       3.131  71.530  36.605  1.00 29.59           C  
ANISOU 3307  CB  LYS B 439     3904   4133   3206    381     43   -268       C  
ATOM   3308  CG  LYS B 439       4.285  71.815  35.664  1.00 35.74           C  
ANISOU 3308  CG  LYS B 439     4663   4887   4028    344     58   -287       C  
ATOM   3309  CD  LYS B 439       4.233  73.227  35.108  1.00 34.65           C  
ANISOU 3309  CD  LYS B 439     4535   4747   3885    348     61   -257       C  
ATOM   3310  CE  LYS B 439       5.288  73.413  34.032  1.00 34.52           C  
ANISOU 3310  CE  LYS B 439     4487   4725   3903    306     88   -258       C  
ATOM   3311  NZ  LYS B 439       5.348  74.821  33.568  1.00 39.31           N  
ANISOU 3311  NZ  LYS B 439     5098   5316   4521    306     88   -212       N  
ATOM   3312  N   SER B 440       0.925  73.042  38.516  1.00 33.79           N  
ANISOU 3312  N   SER B 440     4489   4722   3627    502      0   -220       N  
ATOM   3313  CA  SER B 440      -0.347  72.945  39.219  1.00 28.30           C  
ANISOU 3313  CA  SER B 440     3797   4089   2868    544     -1   -193       C  
ATOM   3314  C   SER B 440      -1.491  72.613  38.272  1.00 21.61           C  
ANISOU 3314  C   SER B 440     2928   3298   1985    516     34   -164       C  
ATOM   3315  O   SER B 440      -1.364  72.729  37.052  1.00 31.75           O  
ANISOU 3315  O   SER B 440     4203   4579   3281    476     53   -168       O  
ATOM   3316  CB  SER B 440      -0.642  74.236  39.978  1.00 24.12           C  
ANISOU 3316  CB  SER B 440     3293   3562   2311    615    -37   -204       C  
ATOM   3317  OG  SER B 440       0.114  74.294  41.174  1.00 36.21           O  
ANISOU 3317  OG  SER B 440     4835   5066   3855    658    -74   -234       O  
ATOM   3318  N   LEU B 441      -2.613  72.203  38.855  1.00 23.43           N  
ANISOU 3318  N   LEU B 441     3146   3587   2167    539     41   -134       N  
ATOM   3319  CA  LEU B 441      -3.739  71.678  38.101  1.00 32.92           C  
ANISOU 3319  CA  LEU B 441     4320   4845   3344    510     69   -110       C  
ATOM   3320  C   LEU B 441      -5.034  71.823  38.899  1.00 28.65           C  
ANISOU 3320  C   LEU B 441     3769   4376   2742    558     70    -74       C  
ATOM   3321  O   LEU B 441      -5.108  71.405  40.056  1.00 32.62           O  
ANISOU 3321  O   LEU B 441     4267   4898   3230    588     65    -52       O  
ATOM   3322  CB  LEU B 441      -3.478  70.208  37.751  1.00 37.92           C  
ANISOU 3322  CB  LEU B 441     4921   5462   4025    451     84   -112       C  
ATOM   3323  CG  LEU B 441      -4.551  69.392  37.040  1.00 34.24           C  
ANISOU 3323  CG  LEU B 441     4414   5040   3555    414    104    -97       C  
ATOM   3324  CD1 LEU B 441      -4.670  69.818  35.591  1.00 35.39           C  
ANISOU 3324  CD1 LEU B 441     4554   5204   3687    390    114   -125       C  
ATOM   3325  CD2 LEU B 441      -4.224  67.912  37.143  1.00 43.63           C  
ANISOU 3325  CD2 LEU B 441     5571   6194   4811    369    104    -99       C  
ATOM   3326  N   SER B 442      -6.044  72.431  38.286  1.00 26.46           N  
ANISOU 3326  N   SER B 442     3485   4145   2423    570     78    -64       N  
ATOM   3327  CA  SER B 442      -7.344  72.603  38.927  1.00 35.99           C  
ANISOU 3327  CA  SER B 442     4673   5431   3568    617     83    -32       C  
ATOM   3328  C   SER B 442      -8.434  72.803  37.891  1.00 32.45           C  
ANISOU 3328  C   SER B 442     4204   5032   3096    601     97    -23       C  
ATOM   3329  O   SER B 442      -8.153  73.139  36.743  1.00 29.47           O  
ANISOU 3329  O   SER B 442     3835   4631   2731    574     99    -41       O  
ATOM   3330  CB  SER B 442      -7.329  73.788  39.898  1.00 31.10           C  
ANISOU 3330  CB  SER B 442     4082   4814   2920    696     53    -47       C  
ATOM   3331  OG  SER B 442      -7.266  75.020  39.209  1.00 27.29           O  
ANISOU 3331  OG  SER B 442     3626   4301   2440    716     34    -72       O  
ATOM   3332  N   LEU B 443      -9.676  72.584  38.303  1.00 38.21           N  
ANISOU 3332  N   LEU B 443     4894   5817   3809    612    106     10       N  
ATOM   3333  CA  LEU B 443     -10.821  72.814  37.440  1.00 40.85           C  
ANISOU 3333  CA  LEU B 443     5198   6188   4135    600    112     18       C  
ATOM   3334  C   LEU B 443     -10.817  74.271  36.990  1.00 40.34           C  
ANISOU 3334  C   LEU B 443     5165   6094   4069    636     90     -2       C  
ATOM   3335  O   LEU B 443     -10.883  75.188  37.810  1.00 49.36           O  
ANISOU 3335  O   LEU B 443     6324   7227   5204    696     69     -8       O  
ATOM   3336  CB  LEU B 443     -12.118  72.462  38.168  1.00 33.40           C  
ANISOU 3336  CB  LEU B 443     4205   5315   3172    618    124     57       C  
ATOM   3337  CG  LEU B 443     -13.422  72.536  37.379  1.00 39.77           C  
ANISOU 3337  CG  LEU B 443     4970   6175   3966    608    130     66       C  
ATOM   3338  CD1 LEU B 443     -13.301  71.731  36.099  1.00 42.19           C  
ANISOU 3338  CD1 LEU B 443     5261   6491   4279    547    140     48       C  
ATOM   3339  CD2 LEU B 443     -14.580  72.032  38.227  1.00 47.56           C  
ANISOU 3339  CD2 LEU B 443     5899   7240   4933    624    147    112       C  
ATOM   3340  N   SER B 444     -10.716  74.479  35.681  1.00 35.94           N  
ANISOU 3340  N   SER B 444     4613   5528   3514    606     93    -11       N  
ATOM   3341  CA  SER B 444     -10.472  75.811  35.138  1.00 42.29           C  
ANISOU 3341  CA  SER B 444     5451   6304   4312    638     74    -16       C  
ATOM   3342  C   SER B 444     -11.002  75.956  33.707  1.00 32.26           C  
ANISOU 3342  C   SER B 444     4164   5063   3030    611     81     -7       C  
ATOM   3343  O   SER B 444     -11.283  74.955  33.047  1.00 27.12           O  
ANISOU 3343  O   SER B 444     3479   4444   2381    563     98    -13       O  
ATOM   3344  CB  SER B 444      -8.971  76.109  35.181  1.00 46.64           C  
ANISOU 3344  CB  SER B 444     6047   6799   4873    638     66    -34       C  
ATOM   3345  OG  SER B 444      -8.248  75.151  34.425  1.00 44.09           O  
ANISOU 3345  OG  SER B 444     5716   6474   4563    578     90    -45       O  
ATOM   3346  N   PRO B 445     -11.154  77.210  33.234  1.00 36.66           N  
ANISOU 3346  N   PRO B 445     4744   5614   3572    650     65      6       N  
ATOM   3347  CA  PRO B 445     -11.575  77.493  31.856  1.00 40.40           C  
ANISOU 3347  CA  PRO B 445     5205   6119   4028    635     69     24       C  
ATOM   3348  C   PRO B 445     -10.760  76.749  30.815  1.00 39.06           C  
ANISOU 3348  C   PRO B 445     5027   5953   3861    575     91     16       C  
ATOM   3349  O   PRO B 445      -9.532  76.836  30.820  1.00 44.80           O  
ANISOU 3349  O   PRO B 445     5782   6645   4595    565     97     13       O  
ATOM   3350  CB  PRO B 445     -11.336  78.996  31.719  1.00 40.07           C  
ANISOU 3350  CB  PRO B 445     5205   6054   3967    693     46     49       C  
ATOM   3351  CG  PRO B 445     -11.487  79.523  33.072  1.00 37.32           C  
ANISOU 3351  CG  PRO B 445     4875   5681   3623    755     21     31       C  
ATOM   3352  CD  PRO B 445     -11.067  78.445  34.037  1.00 31.71           C  
ANISOU 3352  CD  PRO B 445     4153   4959   2936    725     35      5       C  
ATOM   3353  N   GLY B 446     -11.438  76.034  29.925  1.00 44.76           N  
ANISOU 3353  N   GLY B 446     5707   6725   4574    542    100      5       N  
ATOM   3354  CA  GLY B 446     -10.764  75.341  28.846  1.00 42.79           C  
ANISOU 3354  CA  GLY B 446     5444   6495   4322    496    116    -15       C  
ATOM   3355  C   GLY B 446     -10.340  76.307  27.759  1.00 35.71           C  
ANISOU 3355  C   GLY B 446     4562   5609   3399    506    119     20       C  
ATOM   3356  O   GLY B 446      -9.251  76.186  27.199  1.00 42.73           O  
ANISOU 3356  O   GLY B 446     5456   6494   4285    483    136     18       O  
TER    3357      GLY B 446                                                      
ATOM   3358  N   PHE C 103      -8.021  42.870  11.276  1.00 60.03           N  
ANISOU 3358  N   PHE C 103     8079   8230   6498  -1770    732  -1460       N  
ATOM   3359  CA  PHE C 103      -8.607  41.582  11.642  1.00 63.93           C  
ANISOU 3359  CA  PHE C 103     8508   8665   7119  -1729    709  -1465       C  
ATOM   3360  C   PHE C 103     -10.114  41.545  11.400  1.00 64.28           C  
ANISOU 3360  C   PHE C 103     8591   8723   7108  -1720    683  -1421       C  
ATOM   3361  O   PHE C 103     -10.782  42.581  11.362  1.00 68.79           O  
ANISOU 3361  O   PHE C 103     9244   9335   7557  -1723    668  -1355       O  
ATOM   3362  CB  PHE C 103      -8.298  41.235  13.097  1.00 61.00           C  
ANISOU 3362  CB  PHE C 103     8105   8221   6853  -1671    671  -1392       C  
ATOM   3363  CG  PHE C 103      -9.039  42.069  14.106  1.00 56.50           C  
ANISOU 3363  CG  PHE C 103     7606   7647   6215  -1633    627  -1261       C  
ATOM   3364  CD1 PHE C 103      -8.515  43.276  14.537  1.00 54.17           C  
ANISOU 3364  CD1 PHE C 103     7373   7375   5833  -1637    626  -1206       C  
ATOM   3365  CD2 PHE C 103     -10.250  41.645  14.636  1.00 56.00           C  
ANISOU 3365  CD2 PHE C 103     7546   7557   6173  -1595    587  -1195       C  
ATOM   3366  CE1 PHE C 103      -9.182  44.052  15.463  1.00 53.47           C  
ANISOU 3366  CE1 PHE C 103     7350   7283   5684  -1601    588  -1093       C  
ATOM   3367  CE2 PHE C 103     -10.928  42.419  15.564  1.00 57.63           C  
ANISOU 3367  CE2 PHE C 103     7816   7766   6317  -1560    550  -1081       C  
ATOM   3368  CZ  PHE C 103     -10.391  43.624  15.979  1.00 59.05           C  
ANISOU 3368  CZ  PHE C 103     8057   7967   6413  -1562    551  -1032       C  
ATOM   3369  N   ASN C 104     -10.630  40.331  11.233  1.00 59.98           N  
ANISOU 3369  N   ASN C 104     7986   8143   6659  -1707    676  -1461       N  
ATOM   3370  CA  ASN C 104     -12.043  40.077  10.952  1.00 48.44           C  
ANISOU 3370  CA  ASN C 104     6546   6693   5165  -1701    653  -1431       C  
ATOM   3371  C   ASN C 104     -12.897  40.271  12.210  1.00 44.93           C  
ANISOU 3371  C   ASN C 104     6131   6217   4725  -1643    599  -1304       C  
ATOM   3372  O   ASN C 104     -12.757  39.528  13.180  1.00 47.40           O  
ANISOU 3372  O   ASN C 104     6394   6466   5151  -1604    573  -1273       O  
ATOM   3373  CB  ASN C 104     -12.203  38.655  10.395  1.00 40.64           C  
ANISOU 3373  CB  ASN C 104     5480   5673   4287  -1710    663  -1519       C  
ATOM   3374  CG  ASN C 104     -13.632  38.328   9.960  1.00 47.82           C  
ANISOU 3374  CG  ASN C 104     6408   6599   5161  -1712    643  -1500       C  
ATOM   3375  OD1 ASN C 104     -14.603  38.873  10.487  1.00 53.18           O  
ANISOU 3375  OD1 ASN C 104     7138   7289   5777  -1685    607  -1401       O  
ATOM   3376  ND2 ASN C 104     -13.758  37.419   9.000  1.00 54.69           N  
ANISOU 3376  ND2 ASN C 104     7233   7471   6075  -1744    666  -1597       N  
ATOM   3377  N   LYS C 105     -13.777  41.271  12.188  1.00 37.16           N  
ANISOU 3377  N   LYS C 105     5224   5277   3617  -1639    582  -1233       N  
ATOM   3378  CA  LYS C 105     -14.584  41.608  13.353  1.00 41.19           C  
ANISOU 3378  CA  LYS C 105     5766   5769   4115  -1586    536  -1116       C  
ATOM   3379  C   LYS C 105     -15.601  40.533  13.713  1.00 43.89           C  
ANISOU 3379  C   LYS C 105     6063   6076   4537  -1559    505  -1092       C  
ATOM   3380  O   LYS C 105     -15.736  40.166  14.880  1.00 50.09           O  
ANISOU 3380  O   LYS C 105     6826   6815   5392  -1517    471  -1025       O  
ATOM   3381  CB  LYS C 105     -15.301  42.945  13.130  1.00 45.95           C  
ANISOU 3381  CB  LYS C 105     6463   6431   4567  -1589    526  -1057       C  
ATOM   3382  CG  LYS C 105     -14.362  44.132  13.015  1.00 57.50           C  
ANISOU 3382  CG  LYS C 105     7981   7922   5944  -1612    545  -1056       C  
ATOM   3383  CD  LYS C 105     -14.022  44.695  14.381  1.00 63.60           C  
ANISOU 3383  CD  LYS C 105     8776   8663   6725  -1567    520   -968       C  
ATOM   3384  CE  LYS C 105     -13.524  46.127  14.276  1.00 65.56           C  
ANISOU 3384  CE  LYS C 105     9106   8949   6855  -1585    527   -942       C  
ATOM   3385  NZ  LYS C 105     -14.468  46.987  13.511  1.00 62.51           N  
ANISOU 3385  NZ  LYS C 105     8759   8592   6400  -1565    508   -888       N  
ATOM   3386  N   GLU C 106     -16.307  40.017  12.711  1.00 48.79           N  
ANISOU 3386  N   GLU C 106     6671   6721   5145  -1586    514  -1146       N  
ATOM   3387  CA  GLU C 106     -17.341  39.008  12.943  1.00 52.24           C  
ANISOU 3387  CA  GLU C 106     7069   7132   5649  -1567    484  -1125       C  
ATOM   3388  C   GLU C 106     -16.737  37.738  13.523  1.00 49.14           C  
ANISOU 3388  C   GLU C 106     6594   6663   5414  -1552    475  -1154       C  
ATOM   3389  O   GLU C 106     -17.313  37.116  14.416  1.00 43.65           O  
ANISOU 3389  O   GLU C 106     5872   5926   4785  -1519    436  -1092       O  
ATOM   3390  CB  GLU C 106     -18.090  38.685  11.648  1.00 57.55           C  
ANISOU 3390  CB  GLU C 106     7743   7846   6278  -1607    500  -1189       C  
ATOM   3391  CG  GLU C 106     -19.000  39.793  11.164  1.00 69.68           C  
ANISOU 3391  CG  GLU C 106     9356   9450   7667  -1616    494  -1144       C  
ATOM   3392  CD  GLU C 106     -18.543  40.387   9.847  1.00 80.79           C  
ANISOU 3392  CD  GLU C 106    10798  10913   8985  -1674    534  -1222       C  
ATOM   3393  OE1 GLU C 106     -17.383  40.848   9.769  1.00 80.24           O  
ANISOU 3393  OE1 GLU C 106    10736  10845   8906  -1692    562  -1256       O  
ATOM   3394  OE2 GLU C 106     -19.343  40.386   8.888  1.00 83.76           O  
ANISOU 3394  OE2 GLU C 106    11193  11332   9299  -1706    537  -1247       O  
ATOM   3395  N   GLN C 107     -15.573  37.357  13.001  1.00 45.12           N  
ANISOU 3395  N   GLN C 107     6045   6136   4964  -1577    510  -1248       N  
ATOM   3396  CA  GLN C 107     -14.861  36.191  13.512  1.00 41.02           C  
ANISOU 3396  CA  GLN C 107     5445   5540   4600  -1562    500  -1283       C  
ATOM   3397  C   GLN C 107     -14.455  36.387  14.967  1.00 38.15           C  
ANISOU 3397  C   GLN C 107     5081   5131   4285  -1519    466  -1191       C  
ATOM   3398  O   GLN C 107     -14.709  35.526  15.812  1.00 31.19           O  
ANISOU 3398  O   GLN C 107     4157   4190   3505  -1492    426  -1150       O  
ATOM   3399  CB  GLN C 107     -13.625  35.897  12.661  1.00 38.41           C  
ANISOU 3399  CB  GLN C 107     5073   5207   4315  -1595    548  -1405       C  
ATOM   3400  CG  GLN C 107     -12.897  34.621  13.058  1.00 37.96           C  
ANISOU 3400  CG  GLN C 107     4928   5068   4428  -1578    537  -1454       C  
ATOM   3401  CD  GLN C 107     -11.505  34.532  12.468  1.00 47.11           C  
ANISOU 3401  CD  GLN C 107     6045   6225   5629  -1602    584  -1563       C  
ATOM   3402  OE1 GLN C 107     -10.835  35.548  12.264  1.00 55.53           O  
ANISOU 3402  OE1 GLN C 107     7149   7340   6611  -1621    614  -1568       O  
ATOM   3403  NE2 GLN C 107     -11.056  33.313  12.201  1.00 46.15           N  
ANISOU 3403  NE2 GLN C 107     5845   6049   5642  -1602    588  -1650       N  
ATOM   3404  N   GLN C 108     -13.804  37.515  15.250  1.00 32.48           N  
ANISOU 3404  N   GLN C 108     4409   4441   3492  -1517    480  -1160       N  
ATOM   3405  CA  GLN C 108     -13.372  37.833  16.609  1.00 28.93           C  
ANISOU 3405  CA  GLN C 108     3964   3954   3073  -1481    450  -1073       C  
ATOM   3406  C   GLN C 108     -14.544  37.853  17.585  1.00 34.32           C  
ANISOU 3406  C   GLN C 108     4670   4629   3739  -1447    402   -962       C  
ATOM   3407  O   GLN C 108     -14.443  37.352  18.708  1.00 34.10           O  
ANISOU 3407  O   GLN C 108     4612   4548   3797  -1420    366   -904       O  
ATOM   3408  CB  GLN C 108     -12.639  39.177  16.638  1.00 29.74           C  
ANISOU 3408  CB  GLN C 108     4127   4099   3074  -1491    473  -1056       C  
ATOM   3409  CG  GLN C 108     -12.216  39.602  18.037  1.00 28.48           C  
ANISOU 3409  CG  GLN C 108     3981   3907   2934  -1457    443   -963       C  
ATOM   3410  CD  GLN C 108     -11.164  38.687  18.639  1.00 32.60           C  
ANISOU 3410  CD  GLN C 108     4427   4358   3603  -1447    433   -987       C  
ATOM   3411  OE1 GLN C 108     -10.484  37.944  17.930  1.00 40.81           O  
ANISOU 3411  OE1 GLN C 108     5408   5379   4721  -1466    458  -1085       O  
ATOM   3412  NE2 GLN C 108     -11.036  38.728  19.959  1.00 36.94           N  
ANISOU 3412  NE2 GLN C 108     4976   4868   4193  -1416    395   -898       N  
ATOM   3413  N   ASN C 109     -15.660  38.423  17.143  1.00 41.45           N  
ANISOU 3413  N   ASN C 109     5626   5589   4534  -1450    402   -935       N  
ATOM   3414  CA  ASN C 109     -16.857  38.507  17.967  1.00 42.81           C  
ANISOU 3414  CA  ASN C 109     5820   5766   4679  -1419    361   -836       C  
ATOM   3415  C   ASN C 109     -17.451  37.130  18.252  1.00 42.09           C  
ANISOU 3415  C   ASN C 109     5665   5628   4699  -1413    330   -834       C  
ATOM   3416  O   ASN C 109     -17.825  36.833  19.387  1.00 37.72           O  
ANISOU 3416  O   ASN C 109     5098   5044   4189  -1387    290   -754       O  
ATOM   3417  CB  ASN C 109     -17.910  39.390  17.297  1.00 54.29           C  
ANISOU 3417  CB  ASN C 109     7340   7293   5996  -1425    368   -819       C  
ATOM   3418  CG  ASN C 109     -19.273  39.262  17.946  1.00 70.29           C  
ANISOU 3418  CG  ASN C 109     9372   9329   8004  -1396    329   -736       C  
ATOM   3419  OD1 ASN C 109     -20.188  38.664  17.380  1.00 70.23           O  
ANISOU 3419  OD1 ASN C 109     9346   9336   8000  -1407    323   -755       O  
ATOM   3420  ND2 ASN C 109     -19.410  39.809  19.148  1.00 77.39           N  
ANISOU 3420  ND2 ASN C 109    10298  10225   8883  -1361    304   -644       N  
ATOM   3421  N   ALA C 110     -17.532  36.300  17.215  1.00 37.56           N  
ANISOU 3421  N   ALA C 110     5053   5049   4170  -1441    347   -922       N  
ATOM   3422  CA  ALA C 110     -18.070  34.951  17.344  1.00 36.63           C  
ANISOU 3422  CA  ALA C 110     4875   4884   4159  -1441    318   -931       C  
ATOM   3423  C   ALA C 110     -17.209  34.116  18.284  1.00 37.97           C  
ANISOU 3423  C   ALA C 110     4987   4971   4469  -1425    291   -921       C  
ATOM   3424  O   ALA C 110     -17.726  33.374  19.119  1.00 51.08           O  
ANISOU 3424  O   ALA C 110     6619   6591   6200  -1410    246   -862       O  
ATOM   3425  CB  ALA C 110     -18.174  34.278  15.976  1.00 49.49           C  
ANISOU 3425  CB  ALA C 110     6477   6522   5806  -1477    347  -1039       C  
ATOM   3426  N   PHE C 111     -15.895  34.253  18.146  1.00 34.01           N  
ANISOU 3426  N   PHE C 111     4468   4447   4006  -1430    318   -976       N  
ATOM   3427  CA  PHE C 111     -14.954  33.581  19.035  1.00 31.76           C  
ANISOU 3427  CA  PHE C 111     4129   4085   3852  -1414    292   -966       C  
ATOM   3428  C   PHE C 111     -15.173  33.970  20.494  1.00 37.10           C  
ANISOU 3428  C   PHE C 111     4828   4747   4520  -1385    249   -842       C  
ATOM   3429  O   PHE C 111     -15.215  33.103  21.368  1.00 37.46           O  
ANISOU 3429  O   PHE C 111     4832   4731   4670  -1374    203   -799       O  
ATOM   3430  CB  PHE C 111     -13.513  33.889  18.623  1.00 37.83           C  
ANISOU 3430  CB  PHE C 111     4883   4848   4642  -1424    332  -1043       C  
ATOM   3431  CG  PHE C 111     -12.505  33.639  19.713  1.00 37.13           C  
ANISOU 3431  CG  PHE C 111     4758   4695   4655  -1403    304  -1008       C  
ATOM   3432  CD1 PHE C 111     -12.287  32.356  20.193  1.00 34.84           C  
ANISOU 3432  CD1 PHE C 111     4398   4322   4518  -1392    265  -1015       C  
ATOM   3433  CD2 PHE C 111     -11.763  34.682  20.244  1.00 33.81           C  
ANISOU 3433  CD2 PHE C 111     4374   4295   4176  -1396    315   -966       C  
ATOM   3434  CE1 PHE C 111     -11.363  32.120  21.193  1.00 31.13           C  
ANISOU 3434  CE1 PHE C 111     3894   3791   4143  -1375    235   -980       C  
ATOM   3435  CE2 PHE C 111     -10.837  34.453  21.242  1.00 37.83           C  
ANISOU 3435  CE2 PHE C 111     4850   4746   4777  -1379    288   -932       C  
ATOM   3436  CZ  PHE C 111     -10.636  33.171  21.718  1.00 36.54           C  
ANISOU 3436  CZ  PHE C 111     4615   4501   4768  -1368    248   -938       C  
ATOM   3437  N   TYR C 112     -15.311  35.270  20.747  1.00 35.22           N  
ANISOU 3437  N   TYR C 112     4659   4566   4157  -1377    262   -787       N  
ATOM   3438  CA  TYR C 112     -15.473  35.784  22.105  1.00 28.86           C  
ANISOU 3438  CA  TYR C 112     3882   3757   3329  -1352    228   -674       C  
ATOM   3439  C   TYR C 112     -16.690  35.180  22.793  1.00 39.20           C  
ANISOU 3439  C   TYR C 112     5179   5057   4658  -1341    183   -600       C  
ATOM   3440  O   TYR C 112     -16.603  34.703  23.925  1.00 47.16           O  
ANISOU 3440  O   TYR C 112     6162   6018   5738  -1330    141   -534       O  
ATOM   3441  CB  TYR C 112     -15.583  37.313  22.096  1.00 31.18           C  
ANISOU 3441  CB  TYR C 112     4255   4117   3473  -1345    252   -636       C  
ATOM   3442  CG  TYR C 112     -15.834  37.882  23.474  1.00 31.40           C  
ANISOU 3442  CG  TYR C 112     4316   4146   3469  -1319    220   -524       C  
ATOM   3443  CD1 TYR C 112     -14.799  38.003  24.389  1.00 27.67           C  
ANISOU 3443  CD1 TYR C 112     3834   3633   3046  -1311    207   -491       C  
ATOM   3444  CD2 TYR C 112     -17.109  38.273  23.870  1.00 33.32           C  
ANISOU 3444  CD2 TYR C 112     4596   4431   3633  -1302    201   -452       C  
ATOM   3445  CE1 TYR C 112     -15.017  38.504  25.654  1.00 25.44           C  
ANISOU 3445  CE1 TYR C 112     3581   3352   2733  -1292    178   -391       C  
ATOM   3446  CE2 TYR C 112     -17.337  38.778  25.139  1.00 29.11           C  
ANISOU 3446  CE2 TYR C 112     4089   3901   3069  -1280    174   -355       C  
ATOM   3447  CZ  TYR C 112     -16.285  38.890  26.024  1.00 30.72           C  
ANISOU 3447  CZ  TYR C 112     4286   4064   3321  -1277    163   -325       C  
ATOM   3448  OH  TYR C 112     -16.497  39.390  27.289  1.00 33.00           O  
ANISOU 3448  OH  TYR C 112     4603   4358   3578  -1259    136   -230       O  
ATOM   3449  N   GLU C 113     -17.823  35.200  22.104  1.00 42.69           N  
ANISOU 3449  N   GLU C 113     5640   5546   5034  -1348    190   -609       N  
ATOM   3450  CA  GLU C 113     -19.089  34.770  22.688  1.00 46.56           C  
ANISOU 3450  CA  GLU C 113     6124   6044   5521  -1340    151   -537       C  
ATOM   3451  C   GLU C 113     -19.130  33.277  22.960  1.00 38.68           C  
ANISOU 3451  C   GLU C 113     5057   4975   4664  -1351    113   -546       C  
ATOM   3452  O   GLU C 113     -19.610  32.832  24.003  1.00 41.19           O  
ANISOU 3452  O   GLU C 113     5359   5271   5022  -1345     68   -467       O  
ATOM   3453  CB  GLU C 113     -20.232  35.113  21.752  1.00 51.74           C  
ANISOU 3453  CB  GLU C 113     6813   6768   6079  -1347    169   -556       C  
ATOM   3454  CG  GLU C 113     -20.852  36.437  22.007  1.00 61.92           C  
ANISOU 3454  CG  GLU C 113     8170   8126   7230  -1327    177   -494       C  
ATOM   3455  CD  GLU C 113     -21.519  36.958  20.768  1.00 74.20           C  
ANISOU 3455  CD  GLU C 113     9761   9744   8687  -1339    206   -541       C  
ATOM   3456  OE1 GLU C 113     -22.600  36.440  20.411  1.00 72.59           O  
ANISOU 3456  OE1 GLU C 113     9543   9561   8477  -1346    193   -539       O  
ATOM   3457  OE2 GLU C 113     -20.946  37.862  20.130  1.00 84.15           O  
ANISOU 3457  OE2 GLU C 113    11064  11033   9876  -1345    240   -580       O  
ATOM   3458  N   ILE C 114     -18.617  32.515  22.000  1.00 38.54           N  
ANISOU 3458  N   ILE C 114     4999   4924   4722  -1370    131   -646       N  
ATOM   3459  CA  ILE C 114     -18.552  31.069  22.106  1.00 41.87           C  
ANISOU 3459  CA  ILE C 114     5353   5270   5284  -1380     95   -671       C  
ATOM   3460  C   ILE C 114     -17.655  30.686  23.274  1.00 44.25           C  
ANISOU 3460  C   ILE C 114     5622   5500   5690  -1368     58   -624       C  
ATOM   3461  O   ILE C 114     -17.902  29.703  23.980  1.00 48.96           O  
ANISOU 3461  O   ILE C 114     6181   6040   6383  -1372      6   -582       O  
ATOM   3462  CB  ILE C 114     -18.046  30.434  20.787  1.00 38.43           C  
ANISOU 3462  CB  ILE C 114     4883   4815   4905  -1400    129   -800       C  
ATOM   3463  CG1 ILE C 114     -19.124  30.552  19.710  1.00 38.57           C  
ANISOU 3463  CG1 ILE C 114     4925   4895   4834  -1419    153   -835       C  
ATOM   3464  CG2 ILE C 114     -17.646  28.972  20.984  1.00 41.62           C  
ANISOU 3464  CG2 ILE C 114     5215   5124   5475  -1406     91   -833       C  
ATOM   3465  CD1 ILE C 114     -18.647  30.186  18.327  1.00 30.67           C  
ANISOU 3465  CD1 ILE C 114     3903   3894   3855  -1444    196   -964       C  
ATOM   3466  N   LEU C 115     -16.621  31.491  23.488  1.00 38.70           N  
ANISOU 3466  N   LEU C 115     4939   4801   4965  -1357     81   -629       N  
ATOM   3467  CA  LEU C 115     -15.712  31.302  24.609  1.00 37.49           C  
ANISOU 3467  CA  LEU C 115     4761   4587   4896  -1346     48   -580       C  
ATOM   3468  C   LEU C 115     -16.449  31.402  25.942  1.00 39.00           C  
ANISOU 3468  C   LEU C 115     4970   4782   5064  -1339     -1   -454       C  
ATOM   3469  O   LEU C 115     -16.077  30.752  26.916  1.00 40.33           O  
ANISOU 3469  O   LEU C 115     5104   4887   5331  -1339    -49   -404       O  
ATOM   3470  CB  LEU C 115     -14.592  32.340  24.553  1.00 39.64           C  
ANISOU 3470  CB  LEU C 115     5061   4880   5120  -1338     87   -601       C  
ATOM   3471  CG  LEU C 115     -13.499  32.297  25.622  1.00 41.19           C  
ANISOU 3471  CG  LEU C 115     5235   5020   5394  -1328     58   -558       C  
ATOM   3472  CD1 LEU C 115     -12.714  31.007  25.520  1.00 34.94           C  
ANISOU 3472  CD1 LEU C 115     4365   4140   4771  -1332     33   -618       C  
ATOM   3473  CD2 LEU C 115     -12.574  33.498  25.498  1.00 44.00           C  
ANISOU 3473  CD2 LEU C 115     5631   5415   5673  -1324    101   -574       C  
ATOM   3474  N   HIS C 116     -17.500  32.215  25.970  1.00 41.21           N  
ANISOU 3474  N   HIS C 116     5304   5138   5215  -1334     12   -405       N  
ATOM   3475  CA  HIS C 116     -18.211  32.494  27.215  1.00 41.03           C  
ANISOU 3475  CA  HIS C 116     5304   5135   5151  -1327    -25   -290       C  
ATOM   3476  C   HIS C 116     -19.582  31.820  27.342  1.00 40.45           C  
ANISOU 3476  C   HIS C 116     5217   5078   5075  -1338    -57   -249       C  
ATOM   3477  O   HIS C 116     -20.284  32.023  28.338  1.00 35.87           O  
ANISOU 3477  O   HIS C 116     4652   4523   4454  -1336    -85   -156       O  
ATOM   3478  CB  HIS C 116     -18.375  34.003  27.389  1.00 33.70           C  
ANISOU 3478  CB  HIS C 116     4447   4282   4077  -1309      7   -251       C  
ATOM   3479  CG  HIS C 116     -17.107  34.702  27.766  1.00 39.14           C  
ANISOU 3479  CG  HIS C 116     5154   4954   4766  -1300     22   -251       C  
ATOM   3480  ND1 HIS C 116     -16.579  34.652  29.039  1.00 52.65           N  
ANISOU 3480  ND1 HIS C 116     6855   6626   6523  -1298    -13   -178       N  
ATOM   3481  CD2 HIS C 116     -16.256  35.463  27.036  1.00 41.61           C  
ANISOU 3481  CD2 HIS C 116     5491   5283   5035  -1298     68   -314       C  
ATOM   3482  CE1 HIS C 116     -15.462  35.357  29.077  1.00 50.40           C  
ANISOU 3482  CE1 HIS C 116     6590   6335   6224  -1292     10   -196       C  
ATOM   3483  NE2 HIS C 116     -15.243  35.858  27.875  1.00 49.82           N  
ANISOU 3483  NE2 HIS C 116     6536   6295   6096  -1292     59   -278       N  
ATOM   3484  N   LEU C 117     -19.976  31.029  26.347  1.00 38.39           N  
ANISOU 3484  N   LEU C 117     4926   4806   4854  -1353    -51   -318       N  
ATOM   3485  CA  LEU C 117     -21.251  30.327  26.442  1.00 46.67           C  
ANISOU 3485  CA  LEU C 117     5959   5868   5904  -1368    -83   -282       C  
ATOM   3486  C   LEU C 117     -21.169  29.304  27.568  1.00 49.56           C  
ANISOU 3486  C   LEU C 117     6282   6165   6383  -1382   -148   -216       C  
ATOM   3487  O   LEU C 117     -20.360  28.377  27.510  1.00 45.00           O  
ANISOU 3487  O   LEU C 117     5658   5505   5935  -1391   -171   -257       O  
ATOM   3488  CB  LEU C 117     -21.618  29.660  25.113  1.00 44.34           C  
ANISOU 3488  CB  LEU C 117     5643   5572   5633  -1384    -65   -374       C  
ATOM   3489  CG  LEU C 117     -22.101  30.635  24.038  1.00 41.83           C  
ANISOU 3489  CG  LEU C 117     5372   5337   5186  -1379    -11   -419       C  
ATOM   3490  CD1 LEU C 117     -22.204  29.946  22.691  1.00 37.76           C  
ANISOU 3490  CD1 LEU C 117     4832   4811   4704  -1400     10   -522       C  
ATOM   3491  CD2 LEU C 117     -23.435  31.235  24.439  1.00 27.39           C  
ANISOU 3491  CD2 LEU C 117     3578   3584   3245  -1371    -19   -340       C  
ATOM   3492  N   PRO C 118     -22.013  29.474  28.600  1.00 48.19           N  
ANISOU 3492  N   PRO C 118     6122   6026   6162  -1386   -179   -114       N  
ATOM   3493  CA  PRO C 118     -21.855  28.752  29.870  1.00 46.78           C  
ANISOU 3493  CA  PRO C 118     5913   5791   6069  -1403   -241    -34       C  
ATOM   3494  C   PRO C 118     -22.263  27.277  29.833  1.00 45.18           C  
ANISOU 3494  C   PRO C 118     5658   5527   5980  -1433   -294    -37       C  
ATOM   3495  O   PRO C 118     -21.788  26.517  30.678  1.00 45.66           O  
ANISOU 3495  O   PRO C 118     5688   5517   6145  -1449   -348      7       O  
ATOM   3496  CB  PRO C 118     -22.779  29.518  30.819  1.00 43.33           C  
ANISOU 3496  CB  PRO C 118     5513   5430   5520  -1400   -248     65       C  
ATOM   3497  CG  PRO C 118     -23.809  30.127  29.942  1.00 39.97           C  
ANISOU 3497  CG  PRO C 118     5118   5090   4981  -1388   -206     36       C  
ATOM   3498  CD  PRO C 118     -23.162  30.390  28.611  1.00 42.54           C  
ANISOU 3498  CD  PRO C 118     5451   5407   5304  -1375   -157    -72       C  
ATOM   3499  N   ASN C 119     -23.101  26.875  28.881  1.00 43.33           N  
ANISOU 3499  N   ASN C 119     5417   5318   5728  -1444   -281    -85       N  
ATOM   3500  CA  ASN C 119     -23.644  25.521  28.893  1.00 47.38           C  
ANISOU 3500  CA  ASN C 119     5886   5781   6336  -1476   -334    -78       C  
ATOM   3501  C   ASN C 119     -23.025  24.569  27.875  1.00 54.09           C  
ANISOU 3501  C   ASN C 119     6698   6554   7300  -1482   -333   -184       C  
ATOM   3502  O   ASN C 119     -23.434  23.408  27.776  1.00 60.12           O  
ANISOU 3502  O   ASN C 119     7426   7268   8148  -1508   -376   -189       O  
ATOM   3503  CB  ASN C 119     -25.162  25.565  28.694  1.00 42.62           C  
ANISOU 3503  CB  ASN C 119     5296   5256   5641  -1491   -333    -45       C  
ATOM   3504  CG  ASN C 119     -25.862  26.429  29.729  1.00 44.88           C  
ANISOU 3504  CG  ASN C 119     5614   5621   5818  -1486   -335     57       C  
ATOM   3505  OD1 ASN C 119     -25.460  26.473  30.894  1.00 40.55           O  
ANISOU 3505  OD1 ASN C 119     5064   5049   5294  -1490   -367    129       O  
ATOM   3506  ND2 ASN C 119     -26.920  27.113  29.311  1.00 48.34           N  
ANISOU 3506  ND2 ASN C 119     6080   6153   6136  -1477   -303     61       N  
ATOM   3507  N   LEU C 120     -22.038  25.038  27.122  1.00 48.21           N  
ANISOU 3507  N   LEU C 120     5959   5799   6560  -1459   -284   -271       N  
ATOM   3508  CA  LEU C 120     -21.268  24.146  26.261  1.00 44.33           C  
ANISOU 3508  CA  LEU C 120     5426   5231   6188  -1461   -282   -376       C  
ATOM   3509  C   LEU C 120     -20.244  23.415  27.116  1.00 44.23           C  
ANISOU 3509  C   LEU C 120     5373   5116   6318  -1461   -335   -354       C  
ATOM   3510  O   LEU C 120     -19.799  23.946  28.137  1.00 42.35           O  
ANISOU 3510  O   LEU C 120     5147   4878   6066  -1452   -350   -280       O  
ATOM   3511  CB  LEU C 120     -20.559  24.919  25.146  1.00 39.47           C  
ANISOU 3511  CB  LEU C 120     4827   4647   5522  -1442   -208   -478       C  
ATOM   3512  CG  LEU C 120     -21.364  25.801  24.194  1.00 41.55           C  
ANISOU 3512  CG  LEU C 120     5136   5011   5641  -1441   -151   -509       C  
ATOM   3513  CD1 LEU C 120     -20.424  26.439  23.178  1.00 35.93           C  
ANISOU 3513  CD1 LEU C 120     4436   4315   4901  -1428    -87   -611       C  
ATOM   3514  CD2 LEU C 120     -22.462  25.011  23.497  1.00 36.88           C  
ANISOU 3514  CD2 LEU C 120     4531   4430   5053  -1466   -163   -535       C  
ATOM   3515  N   ASN C 121     -19.873  22.200  26.722  1.00 47.48           N  
ANISOU 3515  N   ASN C 121     5734   5438   6867  -1471   -367   -416       N  
ATOM   3516  CA  ASN C 121     -18.760  21.525  27.383  1.00 51.42           C  
ANISOU 3516  CA  ASN C 121     6191   5833   7512  -1465   -415   -411       C  
ATOM   3517  C   ASN C 121     -17.486  21.817  26.604  1.00 53.56           C  
ANISOU 3517  C   ASN C 121     6445   6082   7822  -1437   -364   -522       C  
ATOM   3518  O   ASN C 121     -17.551  22.351  25.497  1.00 59.64           O  
ANISOU 3518  O   ASN C 121     7233   6910   8516  -1431   -297   -605       O  
ATOM   3519  CB  ASN C 121     -19.015  20.012  27.530  1.00 48.37           C  
ANISOU 3519  CB  ASN C 121     5759   5353   7267  -1489   -489   -409       C  
ATOM   3520  CG  ASN C 121     -19.085  19.266  26.202  1.00 53.90           C  
ANISOU 3520  CG  ASN C 121     6434   6024   8023  -1492   -467   -532       C  
ATOM   3521  OD1 ASN C 121     -18.304  19.503  25.285  1.00 51.93           O  
ANISOU 3521  OD1 ASN C 121     6173   5773   7786  -1471   -413   -641       O  
ATOM   3522  ND2 ASN C 121     -20.030  18.335  26.111  1.00 53.41           N  
ANISOU 3522  ND2 ASN C 121     6360   5939   7995  -1523   -511   -516       N  
ATOM   3523  N   GLU C 122     -16.340  21.479  27.185  1.00 49.73           N  
ANISOU 3523  N   GLU C 122     5925   5517   7452  -1424   -397   -521       N  
ATOM   3524  CA  GLU C 122     -15.045  21.779  26.580  1.00 49.64           C  
ANISOU 3524  CA  GLU C 122     5892   5487   7482  -1399   -351   -619       C  
ATOM   3525  C   GLU C 122     -14.938  21.301  25.132  1.00 49.25           C  
ANISOU 3525  C   GLU C 122     5817   5429   7467  -1398   -306   -760       C  
ATOM   3526  O   GLU C 122     -14.437  22.025  24.271  1.00 55.02           O  
ANISOU 3526  O   GLU C 122     6560   6211   8136  -1386   -235   -843       O  
ATOM   3527  CB  GLU C 122     -13.920  21.168  27.414  1.00 58.87           C  
ANISOU 3527  CB  GLU C 122     7013   6553   8801  -1387   -408   -600       C  
ATOM   3528  CG  GLU C 122     -12.543  21.373  26.812  1.00 70.07           C  
ANISOU 3528  CG  GLU C 122     8400   7948  10276  -1361   -364   -705       C  
ATOM   3529  CD  GLU C 122     -11.430  21.228  27.829  1.00 74.06           C  
ANISOU 3529  CD  GLU C 122     8873   8382  10886  -1347   -412   -659       C  
ATOM   3530  OE1 GLU C 122     -10.309  21.706  27.552  1.00 71.35           O  
ANISOU 3530  OE1 GLU C 122     8513   8040  10557  -1326   -372   -720       O  
ATOM   3531  OE2 GLU C 122     -11.669  20.631  28.897  1.00 80.67           O  
ANISOU 3531  OE2 GLU C 122     9700   9161  11789  -1360   -491   -562       O  
ATOM   3532  N   GLU C 123     -15.413  20.088  24.866  1.00 50.36           N  
ANISOU 3532  N   GLU C 123     5924   5507   7703  -1413   -349   -788       N  
ATOM   3533  CA  GLU C 123     -15.268  19.485  23.544  1.00 54.45           C  
ANISOU 3533  CA  GLU C 123     6412   6005   8271  -1414   -314   -926       C  
ATOM   3534  C   GLU C 123     -16.099  20.229  22.515  1.00 56.86           C  
ANISOU 3534  C   GLU C 123     6764   6419   8424  -1427   -244   -966       C  
ATOM   3535  O   GLU C 123     -15.652  20.462  21.392  1.00 58.88           O  
ANISOU 3535  O   GLU C 123     7013   6701   8657  -1424   -181  -1080       O  
ATOM   3536  CB  GLU C 123     -15.668  18.005  23.568  1.00 59.08           C  
ANISOU 3536  CB  GLU C 123     6957   6496   8993  -1429   -383   -937       C  
ATOM   3537  CG  GLU C 123     -14.679  17.092  24.287  1.00 72.82           C  
ANISOU 3537  CG  GLU C 123     8642   8112  10915  -1414   -452   -933       C  
ATOM   3538  CD  GLU C 123     -14.568  17.388  25.771  1.00 82.83           C  
ANISOU 3538  CD  GLU C 123     9924   9366  12183  -1415   -509   -792       C  
ATOM   3539  OE1 GLU C 123     -13.430  17.409  26.289  1.00 75.25           O  
ANISOU 3539  OE1 GLU C 123     8934   8352  11306  -1392   -527   -792       O  
ATOM   3540  OE2 GLU C 123     -15.624  17.585  26.415  1.00 85.41           O  
ANISOU 3540  OE2 GLU C 123    10289   9738  12426  -1439   -536   -683       O  
ATOM   3541  N   GLN C 124     -17.313  20.602  22.904  1.00 59.94           N  
ANISOU 3541  N   GLN C 124     7197   6871   8705  -1444   -257   -871       N  
ATOM   3542  CA  GLN C 124     -18.209  21.330  22.011  1.00 55.78           C  
ANISOU 3542  CA  GLN C 124     6717   6448   8031  -1457   -199   -894       C  
ATOM   3543  C   GLN C 124     -17.626  22.703  21.702  1.00 56.79           C  
ANISOU 3543  C   GLN C 124     6881   6652   8044  -1440   -130   -916       C  
ATOM   3544  O   GLN C 124     -17.561  23.111  20.542  1.00 64.19           O  
ANISOU 3544  O   GLN C 124     7831   7640   8917  -1446    -68  -1007       O  
ATOM   3545  CB  GLN C 124     -19.601  21.473  22.630  1.00 48.66           C  
ANISOU 3545  CB  GLN C 124     5850   5597   7042  -1475   -232   -780       C  
ATOM   3546  CG  GLN C 124     -20.308  20.156  22.895  1.00 48.16           C  
ANISOU 3546  CG  GLN C 124     5755   5469   7075  -1500   -300   -753       C  
ATOM   3547  CD  GLN C 124     -21.611  20.330  23.651  1.00 55.73           C  
ANISOU 3547  CD  GLN C 124     6744   6483   7949  -1520   -335   -632       C  
ATOM   3548  OE1 GLN C 124     -21.675  21.059  24.644  1.00 62.23           O  
ANISOU 3548  OE1 GLN C 124     7592   7341   8710  -1511   -344   -535       O  
ATOM   3549  NE2 GLN C 124     -22.657  19.663  23.185  1.00 54.51           N  
ANISOU 3549  NE2 GLN C 124     6585   6337   7787  -1548   -352   -638       N  
ATOM   3550  N   ARG C 125     -17.209  23.404  22.755  1.00 47.26           N  
ANISOU 3550  N   ARG C 125     5693   5453   6811  -1423   -143   -830       N  
ATOM   3551  CA  ARG C 125     -16.613  24.727  22.614  1.00 46.23           C  
ANISOU 3551  CA  ARG C 125     5601   5388   6576  -1408    -86   -838       C  
ATOM   3552  C   ARG C 125     -15.371  24.712  21.725  1.00 45.78           C  
ANISOU 3552  C   ARG C 125     5513   5310   6571  -1401    -38   -964       C  
ATOM   3553  O   ARG C 125     -15.239  25.534  20.816  1.00 47.36           O  
ANISOU 3553  O   ARG C 125     5742   5579   6672  -1405     26  -1025       O  
ATOM   3554  CB  ARG C 125     -16.255  25.308  23.983  1.00 47.23           C  
ANISOU 3554  CB  ARG C 125     5745   5509   6690  -1393   -116   -727       C  
ATOM   3555  CG  ARG C 125     -15.616  26.694  23.917  1.00 44.87           C  
ANISOU 3555  CG  ARG C 125     5490   5276   6285  -1378    -62   -729       C  
ATOM   3556  CD  ARG C 125     -15.562  27.343  25.284  1.00 49.62           C  
ANISOU 3556  CD  ARG C 125     6121   5886   6849  -1367    -92   -608       C  
ATOM   3557  NE  ARG C 125     -14.956  26.463  26.277  1.00 58.99           N  
ANISOU 3557  NE  ARG C 125     7259   6979   8175  -1366   -156   -566       N  
ATOM   3558  CZ  ARG C 125     -15.603  25.988  27.336  1.00 60.79           C  
ANISOU 3558  CZ  ARG C 125     7484   7181   8431  -1376   -219   -464       C  
ATOM   3559  NH1 ARG C 125     -14.982  25.189  28.194  1.00 57.56           N  
ANISOU 3559  NH1 ARG C 125     7032   6684   8153  -1378   -280   -427       N  
ATOM   3560  NH2 ARG C 125     -16.873  26.326  27.540  1.00 59.67           N  
ANISOU 3560  NH2 ARG C 125     7381   7105   8186  -1386   -222   -398       N  
ATOM   3561  N   ASN C 126     -14.464  23.777  21.994  1.00 42.67           N  
ANISOU 3561  N   ASN C 126     5058   4820   6334  -1391    -72  -1001       N  
ATOM   3562  CA  ASN C 126     -13.239  23.653  21.216  1.00 46.35           C  
ANISOU 3562  CA  ASN C 126     5483   5260   6866  -1382    -30  -1124       C  
ATOM   3563  C   ASN C 126     -13.520  23.402  19.741  1.00 42.60           C  
ANISOU 3563  C   ASN C 126     5003   4818   6365  -1401     22  -1247       C  
ATOM   3564  O   ASN C 126     -12.787  23.872  18.868  1.00 52.62           O  
ANISOU 3564  O   ASN C 126     6267   6123   7602  -1403     85  -1344       O  
ATOM   3565  CB  ASN C 126     -12.352  22.530  21.767  1.00 42.00           C  
ANISOU 3565  CB  ASN C 126     4863   4592   6505  -1366    -86  -1143       C  
ATOM   3566  CG  ASN C 126     -11.748  22.871  23.110  1.00 46.75           C  
ANISOU 3566  CG  ASN C 126     5465   5162   7135  -1349   -128  -1041       C  
ATOM   3567  OD1 ASN C 126     -11.695  24.036  23.504  1.00 46.75           O  
ANISOU 3567  OD1 ASN C 126     5513   5229   7019  -1346   -102   -980       O  
ATOM   3568  ND2 ASN C 126     -11.271  21.855  23.815  1.00 49.28           N  
ANISOU 3568  ND2 ASN C 126     5733   5378   7613  -1339   -196  -1021       N  
ATOM   3569  N   ALA C 127     -14.592  22.669  19.463  1.00 36.55           N  
ANISOU 3569  N   ALA C 127     4237   4042   5609  -1418     -4  -1243       N  
ATOM   3570  CA  ALA C 127     -14.914  22.275  18.101  1.00 38.17           C  
ANISOU 3570  CA  ALA C 127     4433   4269   5801  -1440     38  -1358       C  
ATOM   3571  C   ALA C 127     -15.438  23.456  17.289  1.00 40.27           C  
ANISOU 3571  C   ALA C 127     4760   4652   5887  -1458    103  -1370       C  
ATOM   3572  O   ALA C 127     -15.046  23.642  16.138  1.00 43.45           O  
ANISOU 3572  O   ALA C 127     5159   5092   6259  -1473    163  -1481       O  
ATOM   3573  CB  ALA C 127     -15.929  21.143  18.105  1.00 34.16           C  
ANISOU 3573  CB  ALA C 127     3909   3714   5355  -1456    -14  -1341       C  
ATOM   3574  N   PHE C 128     -16.328  24.243  17.891  1.00 38.08           N  
ANISOU 3574  N   PHE C 128     4539   4435   5496  -1458     90  -1255       N  
ATOM   3575  CA  PHE C 128     -16.811  25.458  17.249  1.00 42.56           C  
ANISOU 3575  CA  PHE C 128     5168   5110   5894  -1471    144  -1253       C  
ATOM   3576  C   PHE C 128     -15.659  26.411  16.949  1.00 40.55           C  
ANISOU 3576  C   PHE C 128     4925   4888   5592  -1464    198  -1301       C  
ATOM   3577  O   PHE C 128     -15.567  26.974  15.859  1.00 40.61           O  
ANISOU 3577  O   PHE C 128     4956   4960   5514  -1485    256  -1377       O  
ATOM   3578  CB  PHE C 128     -17.856  26.170  18.118  1.00 47.04           C  
ANISOU 3578  CB  PHE C 128     5788   5727   6357  -1463    116  -1117       C  
ATOM   3579  CG  PHE C 128     -19.198  25.492  18.145  1.00 49.84           C  
ANISOU 3579  CG  PHE C 128     6144   6084   6710  -1479     78  -1074       C  
ATOM   3580  CD1 PHE C 128     -19.989  25.455  17.007  1.00 51.43           C  
ANISOU 3580  CD1 PHE C 128     6360   6337   6843  -1505    107  -1130       C  
ATOM   3581  CD2 PHE C 128     -19.684  24.923  19.312  1.00 47.27           C  
ANISOU 3581  CD2 PHE C 128     5804   5714   6444  -1472     12   -974       C  
ATOM   3582  CE1 PHE C 128     -21.229  24.845  17.025  1.00 48.98           C  
ANISOU 3582  CE1 PHE C 128     6050   6032   6527  -1522     71  -1090       C  
ATOM   3583  CE2 PHE C 128     -20.926  24.311  19.337  1.00 43.52           C  
ANISOU 3583  CE2 PHE C 128     5328   5245   5962  -1490    -23   -934       C  
ATOM   3584  CZ  PHE C 128     -21.699  24.274  18.190  1.00 45.74           C  
ANISOU 3584  CZ  PHE C 128     5623   5577   6177  -1514      7   -992       C  
ATOM   3585  N   ILE C 129     -14.787  26.592  17.937  1.00 36.48           N  
ANISOU 3585  N   ILE C 129     4396   4333   5133  -1439    177  -1254       N  
ATOM   3586  CA  ILE C 129     -13.647  27.497  17.811  1.00 39.81           C  
ANISOU 3586  CA  ILE C 129     4827   4782   5516  -1433    222  -1288       C  
ATOM   3587  C   ILE C 129     -12.686  27.051  16.711  1.00 46.50           C  
ANISOU 3587  C   ILE C 129     5626   5614   6426  -1447    268  -1436       C  
ATOM   3588  O   ILE C 129     -12.219  27.872  15.921  1.00 49.80           O  
ANISOU 3588  O   ILE C 129     6068   6098   6755  -1464    328  -1496       O  
ATOM   3589  CB  ILE C 129     -12.881  27.614  19.145  1.00 39.66           C  
ANISOU 3589  CB  ILE C 129     4795   4712   5563  -1406    183  -1208       C  
ATOM   3590  CG1 ILE C 129     -13.721  28.380  20.172  1.00 36.79           C  
ANISOU 3590  CG1 ILE C 129     4490   4385   5103  -1396    152  -1068       C  
ATOM   3591  CG2 ILE C 129     -11.547  28.316  18.944  1.00 31.28           C  
ANISOU 3591  CG2 ILE C 129     3728   3667   4490  -1402    227  -1262       C  
ATOM   3592  CD1 ILE C 129     -13.117  28.431  21.558  1.00 30.34           C  
ANISOU 3592  CD1 ILE C 129     3662   3519   4347  -1374    107   -979       C  
ATOM   3593  N   GLN C 130     -12.396  25.752  16.661  1.00 49.11           N  
ANISOU 3593  N   GLN C 130     5890   5861   6910  -1441    241  -1495       N  
ATOM   3594  CA  GLN C 130     -11.566  25.194  15.596  1.00 46.31           C  
ANISOU 3594  CA  GLN C 130     5482   5488   6627  -1452    283  -1645       C  
ATOM   3595  C   GLN C 130     -12.138  25.516  14.218  1.00 47.15           C  
ANISOU 3595  C   GLN C 130     5619   5676   6620  -1490    342  -1725       C  
ATOM   3596  O   GLN C 130     -11.413  25.946  13.320  1.00 52.77           O  
ANISOU 3596  O   GLN C 130     6326   6434   7290  -1509    403  -1823       O  
ATOM   3597  CB  GLN C 130     -11.432  23.679  15.760  1.00 52.10           C  
ANISOU 3597  CB  GLN C 130     6143   6112   7539  -1438    235  -1689       C  
ATOM   3598  CG  GLN C 130     -10.404  23.048  14.834  1.00 60.10           C  
ANISOU 3598  CG  GLN C 130     7090   7094   8649  -1441    275  -1846       C  
ATOM   3599  CD  GLN C 130      -9.012  23.617  15.044  1.00 72.60           C  
ANISOU 3599  CD  GLN C 130     8648   8682  10254  -1424    304  -1877       C  
ATOM   3600  OE1 GLN C 130      -8.544  23.747  16.178  1.00 75.98           O  
ANISOU 3600  OE1 GLN C 130     9069   9068  10733  -1397    262  -1792       O  
ATOM   3601  NE2 GLN C 130      -8.348  23.969  13.952  1.00 77.62           N  
ANISOU 3601  NE2 GLN C 130     9272   9373  10848  -1445    377  -1998       N  
ATOM   3602  N   SER C 131     -13.437  25.296  14.058  1.00 50.15           N  
ANISOU 3602  N   SER C 131     6030   6075   6950  -1504    321  -1682       N  
ATOM   3603  CA  SER C 131     -14.124  25.604  12.804  1.00 52.33           C  
ANISOU 3603  CA  SER C 131     6341   6430   7113  -1543    368  -1743       C  
ATOM   3604  C   SER C 131     -14.014  27.091  12.453  1.00 49.54           C  
ANISOU 3604  C   SER C 131     6052   6177   6595  -1559    417  -1724       C  
ATOM   3605  O   SER C 131     -13.819  27.444  11.290  1.00 43.64           O  
ANISOU 3605  O   SER C 131     5315   5489   5776  -1594    474  -1816       O  
ATOM   3606  CB  SER C 131     -15.595  25.186  12.885  1.00 54.84           C  
ANISOU 3606  CB  SER C 131     6682   6752   7402  -1553    328  -1678       C  
ATOM   3607  OG  SER C 131     -15.727  23.887  13.437  1.00 56.01           O  
ANISOU 3607  OG  SER C 131     6779   6803   7699  -1538    270  -1670       O  
ATOM   3608  N   LEU C 132     -14.152  27.950  13.462  1.00 48.95           N  
ANISOU 3608  N   LEU C 132     6020   6119   6460  -1536    393  -1605       N  
ATOM   3609  CA  LEU C 132     -13.914  29.385  13.307  1.00 57.59           C  
ANISOU 3609  CA  LEU C 132     7175   7295   7411  -1545    432  -1578       C  
ATOM   3610  C   LEU C 132     -12.525  29.680  12.755  1.00 54.36           C  
ANISOU 3610  C   LEU C 132     6741   6897   7016  -1557    484  -1676       C  
ATOM   3611  O   LEU C 132     -12.375  30.464  11.814  1.00 49.96           O  
ANISOU 3611  O   LEU C 132     6219   6416   6348  -1592    536  -1729       O  
ATOM   3612  CB  LEU C 132     -14.091  30.111  14.644  1.00 68.79           C  
ANISOU 3612  CB  LEU C 132     8632   8711   8793  -1512    393  -1439       C  
ATOM   3613  CG  LEU C 132     -15.480  30.657  14.948  1.00 73.12           C  
ANISOU 3613  CG  LEU C 132     9241   9308   9233  -1508    368  -1336       C  
ATOM   3614  CD1 LEU C 132     -15.467  31.355  16.289  1.00 78.46           C  
ANISOU 3614  CD1 LEU C 132     9949   9979   9883  -1476    335  -1213       C  
ATOM   3615  CD2 LEU C 132     -15.911  31.616  13.859  1.00 67.57           C  
ANISOU 3615  CD2 LEU C 132     8596   8697   8378  -1539    414  -1368       C  
ATOM   3616  N   LYS C 133     -11.514  29.057  13.355  1.00 48.44           N  
ANISOU 3616  N   LYS C 133     5929   6073   6402  -1532    468  -1699       N  
ATOM   3617  CA  LYS C 133     -10.133  29.232  12.915  1.00 46.40           C  
ANISOU 3617  CA  LYS C 133     5635   5821   6175  -1541    515  -1795       C  
ATOM   3618  C   LYS C 133      -9.989  28.796  11.459  1.00 52.04           C  
ANISOU 3618  C   LYS C 133     6321   6565   6886  -1580    569  -1941       C  
ATOM   3619  O   LYS C 133      -9.436  29.523  10.642  1.00 61.45           O  
ANISOU 3619  O   LYS C 133     7530   7827   7991  -1614    626  -2007       O  
ATOM   3620  CB  LYS C 133      -9.170  28.443  13.805  1.00 45.73           C  
ANISOU 3620  CB  LYS C 133     5479   5641   6257  -1504    479  -1798       C  
ATOM   3621  CG  LYS C 133      -8.948  29.027  15.191  1.00 51.37           C  
ANISOU 3621  CG  LYS C 133     6217   6332   6968  -1472    437  -1669       C  
ATOM   3622  CD  LYS C 133      -7.650  28.517  15.808  1.00 63.33           C  
ANISOU 3622  CD  LYS C 133     7662   7774   8627  -1445    421  -1696       C  
ATOM   3623  CE  LYS C 133      -7.870  27.269  16.650  1.00 75.68           C  
ANISOU 3623  CE  LYS C 133     9175   9233  10349  -1415    350  -1657       C  
ATOM   3624  NZ  LYS C 133      -7.725  27.545  18.111  1.00 81.00           N  
ANISOU 3624  NZ  LYS C 133     9861   9867  11046  -1387    294  -1526       N  
ATOM   3625  N   ASP C 134     -10.505  27.611  11.151  1.00 52.15           N  
ANISOU 3625  N   ASP C 134     6294   6528   6992  -1580    549  -1989       N  
ATOM   3626  CA  ASP C 134     -10.352  27.016   9.832  1.00 61.29           C  
ANISOU 3626  CA  ASP C 134     7416   7703   8168  -1616    596  -2134       C  
ATOM   3627  C   ASP C 134     -11.105  27.768   8.727  1.00 58.35           C  
ANISOU 3627  C   ASP C 134     7107   7433   7629  -1667    640  -2156       C  
ATOM   3628  O   ASP C 134     -10.629  27.862   7.597  1.00 60.95           O  
ANISOU 3628  O   ASP C 134     7426   7813   7921  -1708    699  -2273       O  
ATOM   3629  CB  ASP C 134     -10.801  25.550   9.861  1.00 67.01           C  
ANISOU 3629  CB  ASP C 134     8086   8340   9033  -1602    555  -2170       C  
ATOM   3630  CG  ASP C 134      -9.927  24.686  10.757  1.00 69.56           C  
ANISOU 3630  CG  ASP C 134     8337   8557   9535  -1556    514  -2174       C  
ATOM   3631  OD1 ASP C 134      -8.734  25.028  10.917  1.00 68.72           O  
ANISOU 3631  OD1 ASP C 134     8201   8450   9459  -1544    538  -2210       O  
ATOM   3632  OD2 ASP C 134     -10.417  23.670  11.296  1.00 73.92           O  
ANISOU 3632  OD2 ASP C 134     8862   9027  10197  -1534    455  -2141       O  
ATOM   3633  N   ASP C 135     -12.276  28.305   9.050  1.00 51.85           N  
ANISOU 3633  N   ASP C 135     6351   6644   6708  -1667    610  -2044       N  
ATOM   3634  CA  ASP C 135     -13.067  29.041   8.065  1.00 48.12           C  
ANISOU 3634  CA  ASP C 135     5942   6265   6078  -1713    642  -2052       C  
ATOM   3635  C   ASP C 135     -13.733  30.284   8.655  1.00 47.76           C  
ANISOU 3635  C   ASP C 135     5976   6271   5898  -1703    622  -1918       C  
ATOM   3636  O   ASP C 135     -14.866  30.218   9.126  1.00 52.73           O  
ANISOU 3636  O   ASP C 135     6635   6896   6506  -1687    579  -1827       O  
ATOM   3637  CB  ASP C 135     -14.135  28.132   7.444  1.00 45.85           C  
ANISOU 3637  CB  ASP C 135     5645   5967   5811  -1733    628  -2085       C  
ATOM   3638  CG  ASP C 135     -14.796  28.751   6.222  1.00 52.26           C  
ANISOU 3638  CG  ASP C 135     6509   6873   6473  -1789    667  -2120       C  
ATOM   3639  OD1 ASP C 135     -14.547  29.939   5.918  1.00 55.31           O  
ANISOU 3639  OD1 ASP C 135     6948   7334   6734  -1811    698  -2105       O  
ATOM   3640  OD2 ASP C 135     -15.584  28.038   5.567  1.00 49.40           O  
ANISOU 3640  OD2 ASP C 135     6139   6511   6120  -1813    663  -2161       O  
ATOM   3641  N   PRO C 136     -13.030  31.424   8.619  1.00 47.37           N  
ANISOU 3641  N   PRO C 136     5965   6275   5761  -1713    653  -1909       N  
ATOM   3642  CA  PRO C 136     -13.520  32.714   9.126  1.00 47.34           C  
ANISOU 3642  CA  PRO C 136     6041   6321   5626  -1704    638  -1792       C  
ATOM   3643  C   PRO C 136     -14.888  33.124   8.570  1.00 48.65           C  
ANISOU 3643  C   PRO C 136     6266   6546   5672  -1726    629  -1751       C  
ATOM   3644  O   PRO C 136     -15.622  33.850   9.240  1.00 44.09           O  
ANISOU 3644  O   PRO C 136     5743   5988   5023  -1702    597  -1638       O  
ATOM   3645  CB  PRO C 136     -12.439  33.701   8.667  1.00 46.93           C  
ANISOU 3645  CB  PRO C 136     6011   6324   5497  -1733    687  -1838       C  
ATOM   3646  CG  PRO C 136     -11.205  32.877   8.552  1.00 47.83           C  
ANISOU 3646  CG  PRO C 136     6043   6390   5741  -1732    712  -1943       C  
ATOM   3647  CD  PRO C 136     -11.657  31.522   8.087  1.00 49.05           C  
ANISOU 3647  CD  PRO C 136     6140   6499   5997  -1735    705  -2015       C  
ATOM   3648  N   SER C 137     -15.213  32.677   7.360  1.00 47.30           N  
ANISOU 3648  N   SER C 137     6085   6406   5480  -1772    657  -1842       N  
ATOM   3649  CA  SER C 137     -16.471  33.062   6.711  1.00 44.86           C  
ANISOU 3649  CA  SER C 137     5831   6158   5055  -1799    651  -1811       C  
ATOM   3650  C   SER C 137     -17.694  32.400   7.346  1.00 42.54           C  
ANISOU 3650  C   SER C 137     5530   5827   4806  -1767    596  -1732       C  
ATOM   3651  O   SER C 137     -18.831  32.796   7.083  1.00 48.28           O  
ANISOU 3651  O   SER C 137     6304   6601   5440  -1777    580  -1680       O  
ATOM   3652  CB  SER C 137     -16.428  32.726   5.216  1.00 48.31           C  
ANISOU 3652  CB  SER C 137     6257   6639   5458  -1864    697  -1936       C  
ATOM   3653  OG  SER C 137     -16.614  31.338   4.997  1.00 37.72           O  
ANISOU 3653  OG  SER C 137     4852   5243   4237  -1864    691  -2003       O  
ATOM   3654  N   GLN C 138     -17.453  31.398   8.187  1.00 46.45           N  
ANISOU 3654  N   GLN C 138     5967   6239   5444  -1730    566  -1723       N  
ATOM   3655  CA  GLN C 138     -18.547  30.648   8.805  1.00 48.12           C  
ANISOU 3655  CA  GLN C 138     6165   6411   5708  -1706    513  -1653       C  
ATOM   3656  C   GLN C 138     -18.922  31.158  10.190  1.00 46.61           C  
ANISOU 3656  C   GLN C 138     5999   6205   5507  -1657    467  -1516       C  
ATOM   3657  O   GLN C 138     -19.600  30.470  10.945  1.00 41.34           O  
ANISOU 3657  O   GLN C 138     5310   5493   4904  -1633    420  -1454       O  
ATOM   3658  CB  GLN C 138     -18.188  29.159   8.896  1.00 44.51           C  
ANISOU 3658  CB  GLN C 138     5629   5867   5416  -1699    499  -1721       C  
ATOM   3659  CG  GLN C 138     -18.528  28.358   7.647  1.00 50.12           C  
ANISOU 3659  CG  GLN C 138     6316   6587   6139  -1745    522  -1829       C  
ATOM   3660  CD  GLN C 138     -18.221  26.884   7.804  1.00 53.60           C  
ANISOU 3660  CD  GLN C 138     6683   6936   6748  -1734    502  -1891       C  
ATOM   3661  OE1 GLN C 138     -18.670  26.240   8.752  1.00 52.24           O  
ANISOU 3661  OE1 GLN C 138     6490   6701   6657  -1703    446  -1818       O  
ATOM   3662  NE2 GLN C 138     -17.442  26.344   6.878  1.00 56.87           N  
ANISOU 3662  NE2 GLN C 138     7056   7338   7213  -1761    545  -2028       N  
ATOM   3663  N   SER C 139     -18.494  32.369  10.516  1.00 49.11           N  
ANISOU 3663  N   SER C 139     6363   6559   5738  -1646    480  -1469       N  
ATOM   3664  CA  SER C 139     -18.643  32.875  11.872  1.00 46.43           C  
ANISOU 3664  CA  SER C 139     6046   6202   5395  -1599    441  -1349       C  
ATOM   3665  C   SER C 139     -20.100  33.019  12.292  1.00 43.95           C  
ANISOU 3665  C   SER C 139     5762   5914   5023  -1584    402  -1252       C  
ATOM   3666  O   SER C 139     -20.497  32.542  13.355  1.00 52.96           O  
ANISOU 3666  O   SER C 139     6883   7013   6228  -1553    358  -1177       O  
ATOM   3667  CB  SER C 139     -17.942  34.218  12.002  1.00 57.12           C  
ANISOU 3667  CB  SER C 139     7451   7598   6654  -1596    466  -1325       C  
ATOM   3668  OG  SER C 139     -16.546  34.059  11.854  1.00 69.29           O  
ANISOU 3668  OG  SER C 139     8956   9110   8260  -1605    497  -1402       O  
ATOM   3669  N   ALA C 140     -20.879  33.699  11.456  1.00 46.76           N  
ANISOU 3669  N   ALA C 140     6168   6343   5256  -1607    416  -1253       N  
ATOM   3670  CA  ALA C 140     -22.305  33.882  11.701  1.00 54.15           C  
ANISOU 3670  CA  ALA C 140     7132   7314   6129  -1595    382  -1170       C  
ATOM   3671  C   ALA C 140     -23.062  32.580  11.983  1.00 52.30           C  
ANISOU 3671  C   ALA C 140     6845   7035   5990  -1592    346  -1159       C  
ATOM   3672  O   ALA C 140     -23.767  32.480  12.988  1.00 53.45           O  
ANISOU 3672  O   ALA C 140     6989   7171   6150  -1562    305  -1066       O  
ATOM   3673  CB  ALA C 140     -22.944  34.600  10.519  1.00 56.22           C  
ANISOU 3673  CB  ALA C 140     7444   7654   6262  -1629    404  -1196       C  
ATOM   3674  N   ASN C 141     -22.934  31.597  11.096  1.00 43.60           N  
ANISOU 3674  N   ASN C 141     5703   5911   4951  -1627    361  -1255       N  
ATOM   3675  CA  ASN C 141     -23.638  30.329  11.290  1.00 52.48           C  
ANISOU 3675  CA  ASN C 141     6780   6991   6168  -1631    325  -1250       C  
ATOM   3676  C   ASN C 141     -23.121  29.578  12.518  1.00 53.72           C  
ANISOU 3676  C   ASN C 141     6890   7063   6456  -1598    289  -1210       C  
ATOM   3677  O   ASN C 141     -23.912  29.039  13.292  1.00 53.68           O  
ANISOU 3677  O   ASN C 141     6870   7036   6490  -1584    243  -1137       O  
ATOM   3678  CB  ASN C 141     -23.562  29.447  10.033  1.00 58.90           C  
ANISOU 3678  CB  ASN C 141     7563   7796   7021  -1677    351  -1369       C  
ATOM   3679  CG  ASN C 141     -22.152  29.290   9.496  1.00 67.26           C  
ANISOU 3679  CG  ASN C 141     8596   8826   8135  -1691    395  -1479       C  
ATOM   3680  OD1 ASN C 141     -21.665  30.138   8.747  1.00 71.74           O  
ANISOU 3680  OD1 ASN C 141     9196   9447   8616  -1713    439  -1526       O  
ATOM   3681  ND2 ASN C 141     -21.500  28.193   9.857  1.00 56.89           N  
ANISOU 3681  ND2 ASN C 141     7221   7428   6967  -1680    381  -1521       N  
ATOM   3682  N   LEU C 142     -21.801  29.538  12.700  1.00 46.68           N  
ANISOU 3682  N   LEU C 142     5976   6127   5633  -1589    308  -1258       N  
ATOM   3683  CA  LEU C 142     -21.214  28.834  13.837  1.00 45.55           C  
ANISOU 3683  CA  LEU C 142     5788   5900   5620  -1560    271  -1223       C  
ATOM   3684  C   LEU C 142     -21.638  29.447  15.171  1.00 44.95           C  
ANISOU 3684  C   LEU C 142     5739   5832   5506  -1525    234  -1090       C  
ATOM   3685  O   LEU C 142     -21.787  28.739  16.165  1.00 49.08           O  
ANISOU 3685  O   LEU C 142     6230   6299   6117  -1510    186  -1031       O  
ATOM   3686  CB  LEU C 142     -19.682  28.819  13.740  1.00 47.94           C  
ANISOU 3686  CB  LEU C 142     6063   6162   5992  -1556    301  -1298       C  
ATOM   3687  CG  LEU C 142     -19.065  27.899  12.682  1.00 49.97           C  
ANISOU 3687  CG  LEU C 142     6270   6385   6332  -1584    331  -1436       C  
ATOM   3688  CD1 LEU C 142     -17.589  28.214  12.491  1.00 33.21           C  
ANISOU 3688  CD1 LEU C 142     4128   4248   4240  -1581    371  -1509       C  
ATOM   3689  CD2 LEU C 142     -19.265  26.443  13.066  1.00 32.03           C  
ANISOU 3689  CD2 LEU C 142     3939   4025   4206  -1579    284  -1443       C  
ATOM   3690  N   LEU C 143     -21.829  30.766  15.193  1.00 37.09           N  
ANISOU 3690  N   LEU C 143     4804   4908   4382  -1515    254  -1045       N  
ATOM   3691  CA  LEU C 143     -22.252  31.443  16.414  1.00 42.07           C  
ANISOU 3691  CA  LEU C 143     5464   5553   4966  -1482    223   -925       C  
ATOM   3692  C   LEU C 143     -23.721  31.165  16.705  1.00 40.39           C  
ANISOU 3692  C   LEU C 143     5256   5369   4723  -1481    187   -854       C  
ATOM   3693  O   LEU C 143     -24.104  30.933  17.850  1.00 42.75           O  
ANISOU 3693  O   LEU C 143     5542   5646   5054  -1461    146   -768       O  
ATOM   3694  CB  LEU C 143     -22.013  32.954  16.310  1.00 49.18           C  
ANISOU 3694  CB  LEU C 143     6430   6518   5739  -1471    254   -903       C  
ATOM   3695  CG  LEU C 143     -22.600  33.817  17.431  1.00 48.56           C  
ANISOU 3695  CG  LEU C 143     6392   6470   5590  -1436    228   -786       C  
ATOM   3696  CD1 LEU C 143     -22.003  33.443  18.776  1.00 41.38           C  
ANISOU 3696  CD1 LEU C 143     5452   5497   4772  -1413    196   -727       C  
ATOM   3697  CD2 LEU C 143     -22.401  35.292  17.140  1.00 47.30           C  
ANISOU 3697  CD2 LEU C 143     6300   6371   5301  -1428    259   -776       C  
ATOM   3698  N   ALA C 144     -24.540  31.183  15.655  1.00 42.99           N  
ANISOU 3698  N   ALA C 144     5599   5748   4986  -1506    202   -892       N  
ATOM   3699  CA  ALA C 144     -25.956  30.857  15.775  1.00 47.07           C  
ANISOU 3699  CA  ALA C 144     6115   6297   5474  -1509    170   -836       C  
ATOM   3700  C   ALA C 144     -26.129  29.411  16.219  1.00 49.04           C  
ANISOU 3700  C   ALA C 144     6305   6477   5853  -1521    129   -833       C  
ATOM   3701  O   ALA C 144     -26.966  29.102  17.069  1.00 47.35           O  
ANISOU 3701  O   ALA C 144     6079   6263   5648  -1512     88   -749       O  
ATOM   3702  CB  ALA C 144     -26.674  31.099  14.458  1.00 42.11           C  
ANISOU 3702  CB  ALA C 144     5510   5731   4757  -1539    195   -888       C  
ATOM   3703  N   GLU C 145     -25.333  28.533  15.620  1.00 42.01           N  
ANISOU 3703  N   GLU C 145     5376   5527   5061  -1541    141   -927       N  
ATOM   3704  CA  GLU C 145     -25.333  27.118  15.954  1.00 41.29           C  
ANISOU 3704  CA  GLU C 145     5227   5356   5105  -1553    101   -937       C  
ATOM   3705  C   GLU C 145     -24.961  26.896  17.415  1.00 46.25           C  
ANISOU 3705  C   GLU C 145     5836   5929   5809  -1526     58   -853       C  
ATOM   3706  O   GLU C 145     -25.609  26.120  18.118  1.00 44.97           O  
ANISOU 3706  O   GLU C 145     5648   5737   5701  -1532      8   -792       O  
ATOM   3707  CB  GLU C 145     -24.360  26.367  15.044  1.00 40.21           C  
ANISOU 3707  CB  GLU C 145     5055   5164   5060  -1573    128  -1063       C  
ATOM   3708  CG  GLU C 145     -24.587  24.870  14.970  1.00 43.96           C  
ANISOU 3708  CG  GLU C 145     5476   5565   5659  -1593     90  -1097       C  
ATOM   3709  CD  GLU C 145     -23.421  24.140  14.332  1.00 53.74           C  
ANISOU 3709  CD  GLU C 145     6674   6737   7010  -1601    112  -1218       C  
ATOM   3710  OE1 GLU C 145     -22.788  24.718  13.423  1.00 51.83           O  
ANISOU 3710  OE1 GLU C 145     6446   6529   6717  -1610    169  -1301       O  
ATOM   3711  OE2 GLU C 145     -23.137  22.996  14.743  1.00 58.21           O  
ANISOU 3711  OE2 GLU C 145     7192   7214   7712  -1600     72  -1230       O  
ATOM   3712  N   ALA C 146     -23.917  27.582  17.865  1.00 34.66           N  
ANISOU 3712  N   ALA C 146     4379   4448   4340  -1502     76   -848       N  
ATOM   3713  CA  ALA C 146     -23.429  27.434  19.238  1.00 38.39           C  
ANISOU 3713  CA  ALA C 146     4835   4868   4882  -1480     37   -771       C  
ATOM   3714  C   ALA C 146     -24.413  28.014  20.255  1.00 42.91           C  
ANISOU 3714  C   ALA C 146     5437   5491   5375  -1466      8   -649       C  
ATOM   3715  O   ALA C 146     -24.591  27.453  21.335  1.00 46.30           O  
ANISOU 3715  O   ALA C 146     5843   5881   5867  -1464    -41   -575       O  
ATOM   3716  CB  ALA C 146     -22.068  28.093  19.387  1.00 29.51           C  
ANISOU 3716  CB  ALA C 146     3719   3726   3768  -1461     66   -800       C  
ATOM   3717  N   LYS C 147     -25.042  29.133  19.901  1.00 39.83           N  
ANISOU 3717  N   LYS C 147     5098   5188   4847  -1457     38   -629       N  
ATOM   3718  CA  LYS C 147     -26.052  29.746  20.760  1.00 45.04           C  
ANISOU 3718  CA  LYS C 147     5786   5906   5423  -1441     16   -523       C  
ATOM   3719  C   LYS C 147     -27.217  28.805  21.055  1.00 49.63           C  
ANISOU 3719  C   LYS C 147     6336   6486   6036  -1460    -28   -477       C  
ATOM   3720  O   LYS C 147     -27.639  28.664  22.204  1.00 47.50           O  
ANISOU 3720  O   LYS C 147     6057   6214   5777  -1455    -67   -388       O  
ATOM   3721  CB  LYS C 147     -26.595  31.033  20.132  1.00 44.64           C  
ANISOU 3721  CB  LYS C 147     5792   5945   5224  -1428     54   -524       C  
ATOM   3722  CG  LYS C 147     -25.761  32.271  20.409  1.00 44.51           C  
ANISOU 3722  CG  LYS C 147     5820   5946   5145  -1401     82   -513       C  
ATOM   3723  CD  LYS C 147     -26.622  33.520  20.335  1.00 48.92           C  
ANISOU 3723  CD  LYS C 147     6435   6593   5561  -1381     96   -467       C  
ATOM   3724  CE  LYS C 147     -25.899  34.676  19.661  1.00 57.52           C  
ANISOU 3724  CE  LYS C 147     7575   7710   6569  -1374    139   -512       C  
ATOM   3725  NZ  LYS C 147     -25.367  35.650  20.659  1.00 69.67           N  
ANISOU 3725  NZ  LYS C 147     9149   9252   8070  -1342    139   -451       N  
ATOM   3726  N   LYS C 148     -27.734  28.162  20.011  1.00 53.25           N  
ANISOU 3726  N   LYS C 148     6779   6950   6505  -1488    -22   -540       N  
ATOM   3727  CA  LYS C 148     -28.871  27.258  20.162  1.00 59.86           C  
ANISOU 3727  CA  LYS C 148     7587   7790   7366  -1512    -63   -502       C  
ATOM   3728  C   LYS C 148     -28.508  26.042  21.000  1.00 55.92           C  
ANISOU 3728  C   LYS C 148     7040   7201   7005  -1526   -115   -476       C  
ATOM   3729  O   LYS C 148     -29.277  25.633  21.870  1.00 58.35           O  
ANISOU 3729  O   LYS C 148     7334   7515   7324  -1536   -159   -393       O  
ATOM   3730  CB  LYS C 148     -29.402  26.828  18.790  1.00 67.44           C  
ANISOU 3730  CB  LYS C 148     8543   8771   8310  -1541    -44   -582       C  
ATOM   3731  CG  LYS C 148     -30.199  27.920  18.098  1.00 77.89           C  
ANISOU 3731  CG  LYS C 148     9912  10193   9489  -1534    -12   -579       C  
ATOM   3732  CD  LYS C 148     -30.651  27.506  16.713  1.00 89.17           C  
ANISOU 3732  CD  LYS C 148    11338  11642  10902  -1569      7   -660       C  
ATOM   3733  CE  LYS C 148     -31.221  28.697  15.956  1.00 93.58           C  
ANISOU 3733  CE  LYS C 148    11946  12293  11318  -1561     41   -664       C  
ATOM   3734  NZ  LYS C 148     -32.115  28.297  14.830  1.00 95.10           N  
ANISOU 3734  NZ  LYS C 148    12135  12522  11475  -1598     44   -708       N  
ATOM   3735  N   LEU C 149     -27.332  25.472  20.742  1.00 49.32           N  
ANISOU 3735  N   LEU C 149     6180   6285   6276  -1528   -111   -548       N  
ATOM   3736  CA  LEU C 149     -26.857  24.322  21.503  1.00 48.51           C  
ANISOU 3736  CA  LEU C 149     6031   6085   6314  -1539   -164   -529       C  
ATOM   3737  C   LEU C 149     -26.734  24.688  22.976  1.00 48.11           C  
ANISOU 3737  C   LEU C 149     5986   6031   6261  -1522   -196   -420       C  
ATOM   3738  O   LEU C 149     -27.113  23.910  23.851  1.00 54.66           O  
ANISOU 3738  O   LEU C 149     6790   6825   7153  -1540   -253   -352       O  
ATOM   3739  CB  LEU C 149     -25.514  23.832  20.959  1.00 42.07           C  
ANISOU 3739  CB  LEU C 149     5188   5188   5607  -1535   -147   -630       C  
ATOM   3740  CG  LEU C 149     -24.940  22.559  21.584  1.00 43.92           C  
ANISOU 3740  CG  LEU C 149     5372   5312   6004  -1545   -205   -626       C  
ATOM   3741  CD1 LEU C 149     -25.945  21.435  21.484  1.00 35.23           C  
ANISOU 3741  CD1 LEU C 149     4248   4190   4949  -1580   -251   -612       C  
ATOM   3742  CD2 LEU C 149     -23.635  22.175  20.915  1.00 35.90           C  
ANISOU 3742  CD2 LEU C 149     4328   4226   5087  -1536   -181   -739       C  
ATOM   3743  N   ASN C 150     -26.205  25.882  23.240  1.00 48.03           N  
ANISOU 3743  N   ASN C 150     6013   6060   6177  -1492   -161   -404       N  
ATOM   3744  CA  ASN C 150     -26.102  26.400  24.603  1.00 50.29           C  
ANISOU 3744  CA  ASN C 150     6312   6355   6443  -1476   -185   -303       C  
ATOM   3745  C   ASN C 150     -27.460  26.548  25.276  1.00 51.13           C  
ANISOU 3745  C   ASN C 150     6428   6528   6472  -1484   -211   -208       C  
ATOM   3746  O   ASN C 150     -27.640  26.178  26.438  1.00 45.78           O  
ANISOU 3746  O   ASN C 150     5734   5831   5830  -1495   -257   -124       O  
ATOM   3747  CB  ASN C 150     -25.378  27.754  24.612  1.00 39.76           C  
ANISOU 3747  CB  ASN C 150     5021   5059   5026  -1443   -137   -310       C  
ATOM   3748  CG  ASN C 150     -25.314  28.375  26.001  1.00 37.95           C  
ANISOU 3748  CG  ASN C 150     4811   4845   4763  -1427   -158   -208       C  
ATOM   3749  OD1 ASN C 150     -24.428  28.065  26.800  1.00 33.29           O  
ANISOU 3749  OD1 ASN C 150     4202   4191   4256  -1426   -185   -183       O  
ATOM   3750  ND2 ASN C 150     -26.263  29.257  26.295  1.00 31.39           N  
ANISOU 3750  ND2 ASN C 150     4016   4100   3811  -1414   -147   -149       N  
ATOM   3751  N   ASP C 151     -28.421  27.094  24.535  1.00 54.25           N  
ANISOU 3751  N   ASP C 151     6848   7005   6761  -1482   -181   -222       N  
ATOM   3752  CA  ASP C 151     -29.777  27.287  25.053  1.00 54.97           C  
ANISOU 3752  CA  ASP C 151     6945   7170   6772  -1488   -200   -141       C  
ATOM   3753  C   ASP C 151     -30.488  25.946  25.232  1.00 51.67           C  
ANISOU 3753  C   ASP C 151     6482   6719   6430  -1529   -252   -118       C  
ATOM   3754  O   ASP C 151     -31.251  25.763  26.180  1.00 45.98           O  
ANISOU 3754  O   ASP C 151     5750   6026   5693  -1543   -288    -30       O  
ATOM   3755  CB  ASP C 151     -30.582  28.194  24.123  1.00 59.11           C  
ANISOU 3755  CB  ASP C 151     7504   7785   7169  -1473   -157   -169       C  
ATOM   3756  CG  ASP C 151     -30.044  29.613  24.091  1.00 63.46           C  
ANISOU 3756  CG  ASP C 151     8106   8377   7631  -1434   -113   -174       C  
ATOM   3757  OD1 ASP C 151     -29.107  29.909  24.861  1.00 64.77           O  
ANISOU 3757  OD1 ASP C 151     8279   8505   7827  -1418   -115   -151       O  
ATOM   3758  OD2 ASP C 151     -30.553  30.432  23.295  1.00 64.42           O  
ANISOU 3758  OD2 ASP C 151     8260   8565   7651  -1420    -79   -201       O  
ATOM   3759  N   ALA C 152     -30.253  25.028  24.297  1.00 52.58           N  
ANISOU 3759  N   ALA C 152     6573   6779   6625  -1551   -255   -197       N  
ATOM   3760  CA  ALA C 152     -30.805  23.678  24.391  1.00 48.59           C  
ANISOU 3760  CA  ALA C 152     6027   6229   6206  -1593   -308   -184       C  
ATOM   3761  C   ALA C 152     -30.293  22.945  25.630  1.00 54.88           C  
ANISOU 3761  C   ALA C 152     6796   6949   7107  -1607   -366   -119       C  
ATOM   3762  O   ALA C 152     -30.999  22.120  26.207  1.00 56.97           O  
ANISOU 3762  O   ALA C 152     7036   7203   7408  -1642   -419    -59       O  
ATOM   3763  CB  ALA C 152     -30.473  22.881  23.140  1.00 38.94           C  
ANISOU 3763  CB  ALA C 152     4787   4953   5056  -1610   -296   -293       C  
ATOM   3764  N   GLN C 153     -29.070  23.260  26.043  1.00 51.06           N  
ANISOU 3764  N   GLN C 153     6317   6415   6670  -1583   -358   -129       N  
ATOM   3765  CA  GLN C 153     -28.477  22.596  27.195  1.00 52.10           C  
ANISOU 3765  CA  GLN C 153     6423   6468   6904  -1596   -416    -69       C  
ATOM   3766  C   GLN C 153     -28.596  23.435  28.465  1.00 49.84           C  
ANISOU 3766  C   GLN C 153     6159   6232   6547  -1585   -423     33       C  
ATOM   3767  O   GLN C 153     -27.836  23.251  29.412  1.00 44.25           O  
ANISOU 3767  O   GLN C 153     5440   5467   5904  -1587   -456     78       O  
ATOM   3768  CB  GLN C 153     -27.015  22.263  26.907  1.00 50.11           C  
ANISOU 3768  CB  GLN C 153     6154   6120   6767  -1580   -412   -143       C  
ATOM   3769  CG  GLN C 153     -26.848  21.330  25.717  1.00 52.26           C  
ANISOU 3769  CG  GLN C 153     6400   6335   7123  -1594   -408   -249       C  
ATOM   3770  CD  GLN C 153     -25.397  21.058  25.368  1.00 54.87           C  
ANISOU 3770  CD  GLN C 153     6709   6577   7561  -1574   -397   -333       C  
ATOM   3771  OE1 GLN C 153     -25.094  20.150  24.589  1.00 56.60           O  
ANISOU 3771  OE1 GLN C 153     6899   6732   7876  -1585   -404   -418       O  
ATOM   3772  NE2 GLN C 153     -24.492  21.839  25.943  1.00 51.10           N  
ANISOU 3772  NE2 GLN C 153     6246   6099   7072  -1546   -381   -312       N  
ATOM   3773  N   ALA C 154     -29.551  24.361  28.475  1.00 51.71           N  
ANISOU 3773  N   ALA C 154     6425   6575   6649  -1572   -391     68       N  
ATOM   3774  CA  ALA C 154     -29.904  25.102  29.680  1.00 51.34           C  
ANISOU 3774  CA  ALA C 154     6396   6586   6524  -1565   -399    166       C  
ATOM   3775  C   ALA C 154     -30.742  24.181  30.565  1.00 62.46           C  
ANISOU 3775  C   ALA C 154     7774   7994   7966  -1613   -462    250       C  
ATOM   3776  O   ALA C 154     -31.478  23.337  30.047  1.00 64.00           O  
ANISOU 3776  O   ALA C 154     7945   8185   8187  -1643   -484    234       O  
ATOM   3777  CB  ALA C 154     -30.662  26.377  29.333  1.00 40.94           C  
ANISOU 3777  CB  ALA C 154     5118   5380   5056  -1534   -346    167       C  
ATOM   3778  N   PRO C 155     -30.633  24.317  31.898  1.00 69.99           N  
ANISOU 3778  N   PRO C 155     8727   8950   8916  -1624   -494    340       N  
ATOM   3779  CA  PRO C 155     -31.490  23.525  32.788  1.00 77.20           C  
ANISOU 3779  CA  PRO C 155     9613   9875   9845  -1675   -553    427       C  
ATOM   3780  C   PRO C 155     -32.981  23.750  32.535  1.00 75.96           C  
ANISOU 3780  C   PRO C 155     9456   9825   9581  -1685   -538    448       C  
ATOM   3781  O   PRO C 155     -33.738  22.780  32.457  1.00 72.77           O  
ANISOU 3781  O   PRO C 155     9022   9416   9212  -1730   -578    467       O  
ATOM   3782  CB  PRO C 155     -31.081  24.005  34.187  1.00 72.71           C  
ANISOU 3782  CB  PRO C 155     9055   9314   9258  -1677   -571    513       C  
ATOM   3783  CG  PRO C 155     -30.600  25.384  33.981  1.00 67.87           C  
ANISOU 3783  CG  PRO C 155     8484   8746   8558  -1621   -507    481       C  
ATOM   3784  CD  PRO C 155     -29.931  25.390  32.628  1.00 69.43           C  
ANISOU 3784  CD  PRO C 155     8688   8898   8796  -1591   -469    371       C  
TER    3785      PRO C 155                                                      
ATOM   3786  N   MET D 101       7.757  69.550  49.979  1.00 67.95           N  
ANISOU 3786  N   MET D 101     9246   9199   7375    661   -140    222       N  
ATOM   3787  CA  MET D 101       8.301  68.730  51.057  1.00 81.86           C  
ANISOU 3787  CA  MET D 101    11026  11054   9022    718   -219    310       C  
ATOM   3788  C   MET D 101       8.756  69.572  52.234  1.00 82.28           C  
ANISOU 3788  C   MET D 101    11091  11234   8940    798   -324    187       C  
ATOM   3789  O   MET D 101       9.776  69.276  52.861  1.00 86.61           O  
ANISOU 3789  O   MET D 101    11633  11807   9469    841   -436    187       O  
ATOM   3790  CB  MET D 101       9.476  67.892  50.559  1.00 90.65           C  
ANISOU 3790  CB  MET D 101    12104  12052  10286    695   -281    363       C  
ATOM   3791  CG  MET D 101       9.091  66.474  50.225  1.00 95.25           C  
ANISOU 3791  CG  MET D 101    12698  12593  10901    664   -221    551       C  
ATOM   3792  SD  MET D 101       7.999  65.767  51.473  1.00147.54           S  
ANISOU 3792  SD  MET D 101    19384  19388  17285    707   -182    709       S  
ATOM   3793  CE  MET D 101       6.452  65.769  50.573  1.00109.92           C  
ANISOU 3793  CE  MET D 101    14630  14585  12552    643    -13    762       C  
ATOM   3794  N   LYS D 102       8.000  70.628  52.521  1.00 78.77           N  
ANISOU 3794  N   LYS D 102    10658  10864   8406    820   -295     77       N  
ATOM   3795  CA  LYS D 102       8.325  71.594  53.570  1.00 71.90           C  
ANISOU 3795  CA  LYS D 102     9794  10113   7414    899   -394    -69       C  
ATOM   3796  C   LYS D 102       9.722  72.219  53.393  1.00 67.22           C  
ANISOU 3796  C   LYS D 102     9155   9430   6955    906   -522   -204       C  
ATOM   3797  O   LYS D 102      10.114  73.083  54.177  1.00 74.65           O  
ANISOU 3797  O   LYS D 102    10092  10447   7824    970   -619   -342       O  
ATOM   3798  CB  LYS D 102       8.243  70.948  54.964  1.00 77.08           C  
ANISOU 3798  CB  LYS D 102    10493  10949   7846    975   -435     20       C  
ATOM   3799  CG  LYS D 102       7.275  69.773  55.117  1.00 80.22           C  
ANISOU 3799  CG  LYS D 102    10928  11410   8144    954   -328    225       C  
ATOM   3800  CD  LYS D 102       8.043  68.499  55.475  1.00 83.41           C  
ANISOU 3800  CD  LYS D 102    11342  11805   8543    962   -390    380       C  
ATOM   3801  CE  LYS D 102       7.130  67.367  55.932  1.00 81.98           C  
ANISOU 3801  CE  LYS D 102    11203  11718   8229    955   -309    589       C  
ATOM   3802  NZ  LYS D 102       6.588  66.564  54.799  1.00 78.09           N  
ANISOU 3802  NZ  LYS D 102    10697  11087   7886    871   -203    715       N  
ATOM   3803  N   PHE D 103      10.455  71.796  52.365  1.00 49.75           N  
ANISOU 3803  N   PHE D 103     6904   7061   4939    841   -521   -168       N  
ATOM   3804  CA  PHE D 103      11.889  72.039  52.324  1.00 38.60           C  
ANISOU 3804  CA  PHE D 103     5446   5578   3643    850   -644   -255       C  
ATOM   3805  C   PHE D 103      12.229  73.510  52.108  1.00 37.38           C  
ANISOU 3805  C   PHE D 103     5254   5380   3570    848   -700   -451       C  
ATOM   3806  O   PHE D 103      11.454  74.279  51.535  1.00 39.87           O  
ANISOU 3806  O   PHE D 103     5568   5659   3920    811   -631   -510       O  
ATOM   3807  CB  PHE D 103      12.573  71.178  51.251  1.00 32.00           C  
ANISOU 3807  CB  PHE D 103     4570   4593   2996    781   -623   -170       C  
ATOM   3808  CG  PHE D 103      12.333  71.624  49.834  1.00 35.65           C  
ANISOU 3808  CG  PHE D 103     4996   4916   3632    693   -536   -206       C  
ATOM   3809  CD1 PHE D 103      11.226  71.182  49.118  1.00 33.90           C  
ANISOU 3809  CD1 PHE D 103     4798   4664   3418    642   -402   -107       C  
ATOM   3810  CD2 PHE D 103      13.239  72.460  49.202  1.00 30.02           C  
ANISOU 3810  CD2 PHE D 103     4224   4102   3078    658   -590   -333       C  
ATOM   3811  CE1 PHE D 103      11.026  71.591  47.805  1.00 32.49           C  
ANISOU 3811  CE1 PHE D 103     4589   4360   3394    562   -328   -139       C  
ATOM   3812  CE2 PHE D 103      13.041  72.875  47.900  1.00 27.94           C  
ANISOU 3812  CE2 PHE D 103     3929   3718   2967    574   -512   -358       C  
ATOM   3813  CZ  PHE D 103      11.933  72.438  47.199  1.00 24.65           C  
ANISOU 3813  CZ  PHE D 103     3541   3275   2548    528   -382   -262       C  
ATOM   3814  N   ASN D 104      13.413  73.872  52.578  1.00 41.47           N  
ANISOU 3814  N   ASN D 104     5740   5893   4124    888   -835   -547       N  
ATOM   3815  CA  ASN D 104      13.893  75.237  52.532  1.00 39.52           C  
ANISOU 3815  CA  ASN D 104     5453   5607   3957    894   -915   -734       C  
ATOM   3816  C   ASN D 104      14.334  75.595  51.116  1.00 37.81           C  
ANISOU 3816  C   ASN D 104     5176   5213   3975    795   -879   -764       C  
ATOM   3817  O   ASN D 104      15.321  75.054  50.618  1.00 36.95           O  
ANISOU 3817  O   ASN D 104     5024   5018   3996    760   -907   -728       O  
ATOM   3818  CB  ASN D 104      15.044  75.397  53.534  1.00 30.94           C  
ANISOU 3818  CB  ASN D 104     4348   4575   2833    971  -1076   -817       C  
ATOM   3819  CG  ASN D 104      15.542  76.825  53.658  1.00 30.36           C  
ANISOU 3819  CG  ASN D 104     4232   4471   2832    989  -1178  -1017       C  
ATOM   3820  OD1 ASN D 104      15.465  77.622  52.724  1.00 38.33           O  
ANISOU 3820  OD1 ASN D 104     5204   5367   3993    921  -1145  -1087       O  
ATOM   3821  ND2 ASN D 104      16.076  77.149  54.829  1.00 47.27           N  
ANISOU 3821  ND2 ASN D 104     6379   6713   4870   1082  -1310  -1110       N  
ATOM   3822  N   LYS D 105      13.609  76.509  50.475  1.00 37.88           N  
ANISOU 3822  N   LYS D 105     5182   5172   4037    750   -819   -831       N  
ATOM   3823  CA  LYS D 105      13.898  76.878  49.096  1.00 36.53           C  
ANISOU 3823  CA  LYS D 105     4962   4843   4075    651   -774   -848       C  
ATOM   3824  C   LYS D 105      15.234  77.587  48.991  1.00 32.58           C  
ANISOU 3824  C   LYS D 105     4393   4268   3719    639   -893   -967       C  
ATOM   3825  O   LYS D 105      16.019  77.316  48.086  1.00 26.93           O  
ANISOU 3825  O   LYS D 105     3624   3444   3165    572   -881   -939       O  
ATOM   3826  CB  LYS D 105      12.801  77.773  48.509  1.00 33.85           C  
ANISOU 3826  CB  LYS D 105     4638   4469   3752    610   -697   -897       C  
ATOM   3827  CG  LYS D 105      11.443  77.124  48.331  1.00 41.08           C  
ANISOU 3827  CG  LYS D 105     5611   5432   4567    601   -563   -780       C  
ATOM   3828  CD  LYS D 105      11.361  76.404  46.995  1.00 53.41           C  
ANISOU 3828  CD  LYS D 105     7157   6875   6260    508   -456   -665       C  
ATOM   3829  CE  LYS D 105       9.913  76.218  46.535  1.00 52.77           C  
ANISOU 3829  CE  LYS D 105     7121   6800   6127    481   -326   -593       C  
ATOM   3830  NZ  LYS D 105       9.008  75.752  47.622  1.00 52.97           N  
ANISOU 3830  NZ  LYS D 105     7202   6976   5949    554   -299   -539       N  
ATOM   3831  N   GLU D 106      15.484  78.506  49.915  1.00 32.88           N  
ANISOU 3831  N   GLU D 106     4427   4366   3701    707  -1008  -1104       N  
ATOM   3832  CA  GLU D 106      16.710  79.302  49.899  1.00 37.78           C  
ANISOU 3832  CA  GLU D 106     4978   4915   4461    700  -1133  -1231       C  
ATOM   3833  C   GLU D 106      17.946  78.425  50.081  1.00 38.84           C  
ANISOU 3833  C   GLU D 106     5075   5038   4643    713  -1198  -1185       C  
ATOM   3834  O   GLU D 106      18.951  78.606  49.393  1.00 36.69           O  
ANISOU 3834  O   GLU D 106     4731   4658   4550    655  -1231  -1217       O  
ATOM   3835  CB  GLU D 106      16.658  80.376  50.984  1.00 35.44           C  
ANISOU 3835  CB  GLU D 106     4690   4698   4079    786  -1253  -1389       C  
ATOM   3836  CG  GLU D 106      17.921  81.212  51.089  1.00 40.11           C  
ANISOU 3836  CG  GLU D 106     5208   5220   4813    787  -1397  -1527       C  
ATOM   3837  CD  GLU D 106      17.823  82.282  52.160  1.00 52.95           C  
ANISOU 3837  CD  GLU D 106     6841   6923   6357    878  -1522  -1693       C  
ATOM   3838  OE1 GLU D 106      17.640  81.927  53.347  1.00 54.42           O  
ANISOU 3838  OE1 GLU D 106     7072   7254   6350    981  -1570  -1701       O  
ATOM   3839  OE2 GLU D 106      17.927  83.477  51.815  1.00 57.66           O  
ANISOU 3839  OE2 GLU D 106     7395   7434   7079    847  -1576  -1816       O  
ATOM   3840  N   GLN D 107      17.855  77.471  51.001  1.00 28.75           N  
ANISOU 3840  N   GLN D 107     3844   3872   3205    788  -1214  -1106       N  
ATOM   3841  CA  GLN D 107      18.935  76.518  51.222  1.00 31.35           C  
ANISOU 3841  CA  GLN D 107     4147   4195   3569    807  -1277  -1049       C  
ATOM   3842  C   GLN D 107      19.174  75.662  49.984  1.00 35.37           C  
ANISOU 3842  C   GLN D 107     4621   4595   4224    717  -1180   -937       C  
ATOM   3843  O   GLN D 107      20.306  75.537  49.513  1.00 33.40           O  
ANISOU 3843  O   GLN D 107     4300   4262   4128    684  -1228   -962       O  
ATOM   3844  CB  GLN D 107      18.625  75.607  52.411  1.00 40.15           C  
ANISOU 3844  CB  GLN D 107     5329   5452   4473    898  -1304   -963       C  
ATOM   3845  CG  GLN D 107      19.763  74.662  52.756  1.00 39.72           C  
ANISOU 3845  CG  GLN D 107     5250   5392   4451    928  -1391   -912       C  
ATOM   3846  CD  GLN D 107      19.330  73.532  53.663  1.00 40.53           C  
ANISOU 3846  CD  GLN D 107     5423   5614   4362    993  -1388   -777       C  
ATOM   3847  OE1 GLN D 107      18.191  73.068  53.599  1.00 42.01           O  
ANISOU 3847  OE1 GLN D 107     5667   5852   4443    981  -1275   -667       O  
ATOM   3848  NE2 GLN D 107      20.237  73.085  54.521  1.00 38.75           N  
ANISOU 3848  NE2 GLN D 107     5194   5435   4095   1060  -1515   -780       N  
ATOM   3849  N   GLN D 108      18.096  75.070  49.475  1.00 26.76           N  
ANISOU 3849  N   GLN D 108     3577   3509   3082    682  -1046   -818       N  
ATOM   3850  CA  GLN D 108      18.155  74.227  48.282  1.00 30.51           C  
ANISOU 3850  CA  GLN D 108     4025   3887   3681    603   -946   -711       C  
ATOM   3851  C   GLN D 108      18.753  74.973  47.096  1.00 30.06           C  
ANISOU 3851  C   GLN D 108     3891   3702   3827    513   -929   -787       C  
ATOM   3852  O   GLN D 108      19.557  74.417  46.343  1.00 32.42           O  
ANISOU 3852  O   GLN D 108     4131   3925   4262    466   -917   -755       O  
ATOM   3853  CB  GLN D 108      16.757  73.713  47.924  1.00 25.08           C  
ANISOU 3853  CB  GLN D 108     3401   3223   2907    580   -807   -594       C  
ATOM   3854  CG  GLN D 108      16.703  72.873  46.653  1.00 28.89           C  
ANISOU 3854  CG  GLN D 108     3857   3606   3513    501   -701   -492       C  
ATOM   3855  CD  GLN D 108      17.450  71.559  46.782  1.00 32.80           C  
ANISOU 3855  CD  GLN D 108     4333   4095   4035    522   -736   -399       C  
ATOM   3856  OE1 GLN D 108      17.735  71.100  47.890  1.00 29.46           O  
ANISOU 3856  OE1 GLN D 108     3936   3754   3504    598   -821   -375       O  
ATOM   3857  NE2 GLN D 108      17.767  70.945  45.649  1.00 29.84           N  
ANISOU 3857  NE2 GLN D 108     3912   3624   3804    458   -675   -349       N  
ATOM   3858  N   ASN D 109      18.374  76.240  46.945  1.00 29.43           N  
ANISOU 3858  N   ASN D 109     3810   3602   3769    490   -931   -889       N  
ATOM   3859  CA  ASN D 109      18.872  77.073  45.856  1.00 32.18           C  
ANISOU 3859  CA  ASN D 109     4089   3833   4303    400   -919   -956       C  
ATOM   3860  C   ASN D 109      20.359  77.352  46.003  1.00 32.40           C  
ANISOU 3860  C   ASN D 109     4035   3822   4455    402  -1038  -1043       C  
ATOM   3861  O   ASN D 109      21.107  77.281  45.032  1.00 38.48           O  
ANISOU 3861  O   ASN D 109     4732   4502   5385    326  -1013  -1038       O  
ATOM   3862  CB  ASN D 109      18.105  78.397  45.787  1.00 38.08           C  
ANISOU 3862  CB  ASN D 109     4858   4568   5044    383   -914  -1046       C  
ATOM   3863  CG  ASN D 109      18.769  79.413  44.871  1.00 35.62           C  
ANISOU 3863  CG  ASN D 109     4472   4140   4924    296   -936  -1128       C  
ATOM   3864  OD1 ASN D 109      19.351  80.395  45.333  1.00 33.89           O  
ANISOU 3864  OD1 ASN D 109     4216   3907   4754    314  -1050  -1250       O  
ATOM   3865  ND2 ASN D 109      18.684  79.179  43.565  1.00 34.62           N  
ANISOU 3865  ND2 ASN D 109     4319   3928   4907    200   -829  -1058       N  
ATOM   3866  N   ALA D 110      20.776  77.673  47.225  1.00 27.84           N  
ANISOU 3866  N   ALA D 110     3465   3315   3799    489  -1167  -1126       N  
ATOM   3867  CA  ALA D 110      22.179  77.960  47.498  1.00 31.97           C  
ANISOU 3867  CA  ALA D 110     3909   3805   4433    501  -1295  -1218       C  
ATOM   3868  C   ALA D 110      23.033  76.726  47.225  1.00 35.45           C  
ANISOU 3868  C   ALA D 110     4309   4226   4935    495  -1290  -1136       C  
ATOM   3869  O   ALA D 110      24.112  76.825  46.641  1.00 35.15           O  
ANISOU 3869  O   ALA D 110     4181   4111   5063    445  -1321  -1177       O  
ATOM   3870  CB  ALA D 110      22.365  78.430  48.935  1.00 32.64           C  
ANISOU 3870  CB  ALA D 110     4021   3983   4398    609  -1436  -1317       C  
ATOM   3871  N   PHE D 111      22.530  75.567  47.647  1.00 30.32           N  
ANISOU 3871  N   PHE D 111     3722   3644   4154    544  -1252  -1021       N  
ATOM   3872  CA  PHE D 111      23.183  74.294  47.366  1.00 35.51           C  
ANISOU 3872  CA  PHE D 111     4347   4278   4866    541  -1244   -932       C  
ATOM   3873  C   PHE D 111      23.331  74.059  45.862  1.00 35.76           C  
ANISOU 3873  C   PHE D 111     4319   4208   5062    436  -1132   -891       C  
ATOM   3874  O   PHE D 111      24.413  73.710  45.390  1.00 42.22           O  
ANISOU 3874  O   PHE D 111     5053   4970   6018    408  -1161   -909       O  
ATOM   3875  CB  PHE D 111      22.408  73.140  48.009  1.00 37.39           C  
ANISOU 3875  CB  PHE D 111     4671   4601   4936    601  -1212   -801       C  
ATOM   3876  CG  PHE D 111      22.721  71.795  47.410  1.00 36.64           C  
ANISOU 3876  CG  PHE D 111     4551   4460   4910    579  -1166   -688       C  
ATOM   3877  CD1 PHE D 111      23.986  71.246  47.528  1.00 35.97           C  
ANISOU 3877  CD1 PHE D 111     4399   4345   4922    599  -1260   -709       C  
ATOM   3878  CD2 PHE D 111      21.751  71.079  46.726  1.00 40.18           C  
ANISOU 3878  CD2 PHE D 111     5039   4894   5334    539  -1034   -567       C  
ATOM   3879  CE1 PHE D 111      24.280  70.015  46.973  1.00 43.20           C  
ANISOU 3879  CE1 PHE D 111     5287   5217   5910    583  -1226   -616       C  
ATOM   3880  CE2 PHE D 111      22.038  69.848  46.170  1.00 40.38           C  
ANISOU 3880  CE2 PHE D 111     5038   4873   5433    523  -1001   -473       C  
ATOM   3881  CZ  PHE D 111      23.304  69.316  46.291  1.00 42.33           C  
ANISOU 3881  CZ  PHE D 111     5217   5091   5777    546  -1097   -499       C  
ATOM   3882  N   TYR D 112      22.249  74.256  45.112  1.00 31.84           N  
ANISOU 3882  N   TYR D 112     3862   3690   4546    380  -1006   -841       N  
ATOM   3883  CA  TYR D 112      22.274  74.022  43.670  1.00 35.65           C  
ANISOU 3883  CA  TYR D 112     4296   4086   5164    284   -893   -797       C  
ATOM   3884  C   TYR D 112      23.299  74.895  42.954  1.00 36.14           C  
ANISOU 3884  C   TYR D 112     4257   4072   5404    212   -923   -896       C  
ATOM   3885  O   TYR D 112      24.108  74.394  42.175  1.00 42.23           O  
ANISOU 3885  O   TYR D 112     4951   4793   6302    167   -899   -883       O  
ATOM   3886  CB  TYR D 112      20.893  74.253  43.059  1.00 33.64           C  
ANISOU 3886  CB  TYR D 112     4105   3824   4853    240   -766   -740       C  
ATOM   3887  CG  TYR D 112      20.898  74.118  41.556  1.00 28.97           C  
ANISOU 3887  CG  TYR D 112     3466   3148   4394    141   -654   -703       C  
ATOM   3888  CD1 TYR D 112      20.909  72.871  40.958  1.00 27.59           C  
ANISOU 3888  CD1 TYR D 112     3279   2956   4246    130   -586   -607       C  
ATOM   3889  CD2 TYR D 112      20.907  75.239  40.737  1.00 24.77           C  
ANISOU 3889  CD2 TYR D 112     2899   2553   3958     60   -622   -765       C  
ATOM   3890  CE1 TYR D 112      20.924  72.738  39.586  1.00 23.89           C  
ANISOU 3890  CE1 TYR D 112     2766   2420   3890     45   -485   -581       C  
ATOM   3891  CE2 TYR D 112      20.924  75.118  39.366  1.00 25.25           C  
ANISOU 3891  CE2 TYR D 112     2918   2548   4128    -31   -519   -727       C  
ATOM   3892  CZ  TYR D 112      20.931  73.864  38.797  1.00 34.09           C  
ANISOU 3892  CZ  TYR D 112     4026   3661   5264    -35   -449   -639       C  
ATOM   3893  OH  TYR D 112      20.945  73.736  37.421  1.00 40.13           O  
ANISOU 3893  OH  TYR D 112     4749   4371   6130   -120   -347   -610       O  
ATOM   3894  N   GLU D 113      23.260  76.198  43.209  1.00 37.27           N  
ANISOU 3894  N   GLU D 113     4397   4205   5558    202   -975   -994       N  
ATOM   3895  CA  GLU D 113      24.128  77.133  42.499  1.00 36.57           C  
ANISOU 3895  CA  GLU D 113     4215   4038   5643    123   -999  -1079       C  
ATOM   3896  C   GLU D 113      25.595  76.930  42.879  1.00 42.19           C  
ANISOU 3896  C   GLU D 113     4837   4742   6450    148  -1111  -1143       C  
ATOM   3897  O   GLU D 113      26.473  77.003  42.021  1.00 51.59           O  
ANISOU 3897  O   GLU D 113     5932   5873   7798     75  -1093  -1163       O  
ATOM   3898  CB  GLU D 113      23.695  78.582  42.749  1.00 36.32           C  
ANISOU 3898  CB  GLU D 113     4203   3990   5605    110  -1042  -1169       C  
ATOM   3899  CG  GLU D 113      22.820  79.156  41.635  1.00 45.86           C  
ANISOU 3899  CG  GLU D 113     5430   5141   6855     18   -926  -1134       C  
ATOM   3900  CD  GLU D 113      21.947  80.316  42.088  1.00 63.97           C  
ANISOU 3900  CD  GLU D 113     7781   7440   9087     35   -960  -1200       C  
ATOM   3901  OE1 GLU D 113      22.501  81.407  42.359  1.00 74.71           O  
ANISOU 3901  OE1 GLU D 113     9095   8764  10528     26  -1062  -1308       O  
ATOM   3902  OE2 GLU D 113      20.711  80.146  42.147  1.00 61.32           O  
ANISOU 3902  OE2 GLU D 113     7528   7139   8630     55   -887  -1147       O  
ATOM   3903  N   ILE D 114      25.853  76.668  44.161  1.00 38.02           N  
ANISOU 3903  N   ILE D 114     4340   4280   5825    251  -1227  -1174       N  
ATOM   3904  CA  ILE D 114      27.213  76.394  44.616  1.00 43.77           C  
ANISOU 3904  CA  ILE D 114     4990   5004   6635    287  -1344  -1234       C  
ATOM   3905  C   ILE D 114      27.754  75.120  43.959  1.00 43.97           C  
ANISOU 3905  C   ILE D 114     4966   5008   6731    267  -1290  -1156       C  
ATOM   3906  O   ILE D 114      28.939  75.028  43.628  1.00 45.27           O  
ANISOU 3906  O   ILE D 114     5028   5133   7041    241  -1334  -1206       O  
ATOM   3907  CB  ILE D 114      27.270  76.262  46.161  1.00 41.47           C  
ANISOU 3907  CB  ILE D 114     4756   4799   6202    410  -1478  -1271       C  
ATOM   3908  CG1 ILE D 114      27.149  77.640  46.807  1.00 39.13           C  
ANISOU 3908  CG1 ILE D 114     4471   4513   5884    433  -1567  -1392       C  
ATOM   3909  CG2 ILE D 114      28.570  75.611  46.626  1.00 37.61           C  
ANISOU 3909  CG2 ILE D 114     4200   4310   5779    457  -1591  -1301       C  
ATOM   3910  CD1 ILE D 114      26.949  77.583  48.296  1.00 39.40           C  
ANISOU 3910  CD1 ILE D 114     4577   4650   5745    555  -1681  -1426       C  
ATOM   3911  N   LEU D 115      26.871  74.151  43.741  1.00 40.65           N  
ANISOU 3911  N   LEU D 115     4614   4614   6217    278  -1195  -1039       N  
ATOM   3912  CA  LEU D 115      27.239  72.910  43.067  1.00 43.87           C  
ANISOU 3912  CA  LEU D 115     4981   4999   6691    261  -1140   -964       C  
ATOM   3913  C   LEU D 115      27.741  73.166  41.648  1.00 42.57           C  
ANISOU 3913  C   LEU D 115     4717   4761   6697    154  -1052   -985       C  
ATOM   3914  O   LEU D 115      28.582  72.430  41.134  1.00 39.92           O  
ANISOU 3914  O   LEU D 115     4300   4401   6468    139  -1048   -982       O  
ATOM   3915  CB  LEU D 115      26.044  71.953  43.041  1.00 43.72           C  
ANISOU 3915  CB  LEU D 115     5056   5012   6544    285  -1049   -833       C  
ATOM   3916  CG  LEU D 115      26.219  70.571  42.407  1.00 45.35           C  
ANISOU 3916  CG  LEU D 115     5234   5193   6803    279   -995   -747       C  
ATOM   3917  CD1 LEU D 115      27.240  69.744  43.167  1.00 37.70           C  
ANISOU 3917  CD1 LEU D 115     4227   4239   5857    353  -1120   -758       C  
ATOM   3918  CD2 LEU D 115      24.878  69.852  42.336  1.00 44.19           C  
ANISOU 3918  CD2 LEU D 115     5184   5070   6535    291   -899   -621       C  
ATOM   3919  N   HIS D 116      27.229  74.226  41.027  1.00 44.00           N  
ANISOU 3919  N   HIS D 116     4904   4912   6902     79   -986  -1008       N  
ATOM   3920  CA  HIS D 116      27.535  74.511  39.629  1.00 42.41           C  
ANISOU 3920  CA  HIS D 116     4621   4651   6840    -31   -888  -1010       C  
ATOM   3921  C   HIS D 116      28.514  75.661  39.403  1.00 41.26           C  
ANISOU 3921  C   HIS D 116     4378   4463   6835    -92   -945  -1114       C  
ATOM   3922  O   HIS D 116      28.796  76.019  38.257  1.00 40.46           O  
ANISOU 3922  O   HIS D 116     4206   4318   6848   -191   -866  -1114       O  
ATOM   3923  CB  HIS D 116      26.244  74.796  38.865  1.00 32.85           C  
ANISOU 3923  CB  HIS D 116     3482   3427   5573    -87   -758   -942       C  
ATOM   3924  CG  HIS D 116      25.431  73.569  38.588  1.00 38.03           C  
ANISOU 3924  CG  HIS D 116     4198   4103   6147    -61   -669   -833       C  
ATOM   3925  ND1 HIS D 116      25.760  72.666  37.600  1.00 39.95           N  
ANISOU 3925  ND1 HIS D 116     4384   4325   6471    -98   -592   -789       N  
ATOM   3926  CD2 HIS D 116      24.312  73.087  39.180  1.00 36.38           C  
ANISOU 3926  CD2 HIS D 116     4097   3935   5789     -2   -648   -760       C  
ATOM   3927  CE1 HIS D 116      24.873  71.687  37.586  1.00 35.07           C  
ANISOU 3927  CE1 HIS D 116     3837   3725   5764    -62   -533   -695       C  
ATOM   3928  NE2 HIS D 116      23.984  71.918  38.536  1.00 41.83           N  
ANISOU 3928  NE2 HIS D 116     4794   4619   6482     -7   -563   -670       N  
ATOM   3929  N   LEU D 117      29.020  76.255  40.479  1.00 41.30           N  
ANISOU 3929  N   LEU D 117     4378   4482   6833    -35  -1083  -1199       N  
ATOM   3930  CA  LEU D 117      30.015  77.318  40.337  1.00 43.60           C  
ANISOU 3930  CA  LEU D 117     4568   4726   7270    -89  -1152  -1301       C  
ATOM   3931  C   LEU D 117      31.289  76.717  39.760  1.00 45.98           C  
ANISOU 3931  C   LEU D 117     4743   5010   7718   -122  -1152  -1320       C  
ATOM   3932  O   LEU D 117      31.902  75.848  40.377  1.00 48.28           O  
ANISOU 3932  O   LEU D 117     5015   5329   8000    -46  -1225  -1331       O  
ATOM   3933  CB  LEU D 117      30.289  78.010  41.675  1.00 38.98           C  
ANISOU 3933  CB  LEU D 117     4004   4162   6644     -9  -1312  -1396       C  
ATOM   3934  CG  LEU D 117      29.191  78.966  42.153  1.00 40.21           C  
ANISOU 3934  CG  LEU D 117     4257   4328   6694      8  -1324  -1414       C  
ATOM   3935  CD1 LEU D 117      29.427  79.403  43.589  1.00 44.02           C  
ANISOU 3935  CD1 LEU D 117     4768   4852   7107    112  -1485  -1509       C  
ATOM   3936  CD2 LEU D 117      29.095  80.174  41.231  1.00 32.60           C  
ANISOU 3936  CD2 LEU D 117     3265   3307   5814    -89  -1246  -1406       C  
ATOM   3937  N   PRO D 118      31.685  77.181  38.564  1.00 48.31           N  
ANISOU 3937  N   PRO D 118     4990   5285   8079   -203  -1023  -1272       N  
ATOM   3938  CA  PRO D 118      32.713  76.503  37.765  1.00 43.48           C  
ANISOU 3938  CA  PRO D 118     4285   4678   7558   -227   -962  -1254       C  
ATOM   3939  C   PRO D 118      34.147  76.682  38.269  1.00 47.63           C  
ANISOU 3939  C   PRO D 118     4727   5200   8173   -191  -1059  -1328       C  
ATOM   3940  O   PRO D 118      34.994  75.852  37.937  1.00 53.86           O  
ANISOU 3940  O   PRO D 118     5442   5995   9027   -182  -1045  -1334       O  
ATOM   3941  CB  PRO D 118      32.567  77.153  36.389  1.00 44.09           C  
ANISOU 3941  CB  PRO D 118     4360   4750   7641   -320   -806  -1181       C  
ATOM   3942  CG  PRO D 118      31.995  78.495  36.656  1.00 48.49           C  
ANISOU 3942  CG  PRO D 118     4978   5290   8156   -339   -825  -1184       C  
ATOM   3943  CD  PRO D 118      31.155  78.381  37.900  1.00 50.88           C  
ANISOU 3943  CD  PRO D 118     5354   5594   8384   -269   -935  -1230       C  
ATOM   3944  N   ASN D 119      34.413  77.717  39.058  1.00 46.56           N  
ANISOU 3944  N   ASN D 119     4601   5050   8040   -166  -1154  -1387       N  
ATOM   3945  CA  ASN D 119      35.786  78.027  39.436  1.00 49.48           C  
ANISOU 3945  CA  ASN D 119     4892   5407   8503   -140  -1233  -1455       C  
ATOM   3946  C   ASN D 119      36.165  77.657  40.866  1.00 58.16           C  
ANISOU 3946  C   ASN D 119     5997   6517   9584    -33  -1406  -1537       C  
ATOM   3947  O   ASN D 119      37.294  77.906  41.298  1.00 60.92           O  
ANISOU 3947  O   ASN D 119     6287   6852  10008     -1  -1483  -1599       O  
ATOM   3948  CB  ASN D 119      36.061  79.517  39.205  1.00 51.04           C  
ANISOU 3948  CB  ASN D 119     5079   5576   8740   -190  -1218  -1462       C  
ATOM   3949  CG  ASN D 119      35.788  79.935  37.777  1.00 55.59           C  
ANISOU 3949  CG  ASN D 119     5651   6148   9321   -293  -1058  -1374       C  
ATOM   3950  OD1 ASN D 119      36.033  79.171  36.842  1.00 55.83           O  
ANISOU 3950  OD1 ASN D 119     5645   6199   9371   -331   -958  -1329       O  
ATOM   3951  ND2 ASN D 119      35.283  81.149  37.597  1.00 57.29           N  
ANISOU 3951  ND2 ASN D 119     5910   6344   9515   -335  -1038  -1351       N  
ATOM   3952  N   LEU D 120      35.245  77.054  41.607  1.00 56.40           N  
ANISOU 3952  N   LEU D 120     5850   6324   9254     26  -1472  -1535       N  
ATOM   3953  CA  LEU D 120      35.601  76.503  42.911  1.00 57.17           C  
ANISOU 3953  CA  LEU D 120     5962   6451   9309    135  -1636  -1595       C  
ATOM   3954  C   LEU D 120      36.287  75.155  42.715  1.00 58.83           C  
ANISOU 3954  C   LEU D 120     6111   6669   9574    161  -1645  -1579       C  
ATOM   3955  O   LEU D 120      36.013  74.455  41.739  1.00 61.28           O  
ANISOU 3955  O   LEU D 120     6398   6976   9911    109  -1531  -1515       O  
ATOM   3956  CB  LEU D 120      34.368  76.336  43.804  1.00 53.76           C  
ANISOU 3956  CB  LEU D 120     5640   6066   8719    197  -1712  -1592       C  
ATOM   3957  CG  LEU D 120      33.477  77.535  44.126  1.00 56.33           C  
ANISOU 3957  CG  LEU D 120     6044   6394   8963    190  -1712  -1614       C  
ATOM   3958  CD1 LEU D 120      32.345  77.102  45.046  1.00 55.37           C  
ANISOU 3958  CD1 LEU D 120     6060   6346   8632    281  -1733  -1566       C  
ATOM   3959  CD2 LEU D 120      34.285  78.653  44.759  1.00 50.00           C  
ANISOU 3959  CD2 LEU D 120     5218   5573   8207    222  -1794  -1694       C  
ATOM   3960  N   ASN D 121      37.177  74.784  43.630  1.00 53.53           N  
ANISOU 3960  N   ASN D 121     5416   6006   8918    246  -1777  -1635       N  
ATOM   3961  CA  ASN D 121      37.726  73.429  43.616  1.00 59.02           C  
ANISOU 3961  CA  ASN D 121     6068   6709   9649    289  -1806  -1616       C  
ATOM   3962  C   ASN D 121      36.894  72.547  44.543  1.00 62.82           C  
ANISOU 3962  C   ASN D 121     6638   7245   9988    380  -1903  -1572       C  
ATOM   3963  O   ASN D 121      36.065  73.056  45.294  1.00 65.45           O  
ANISOU 3963  O   ASN D 121     7081   7614  10175    421  -1930  -1557       O  
ATOM   3964  CB  ASN D 121      39.216  73.428  43.996  1.00 54.45           C  
ANISOU 3964  CB  ASN D 121     5416   6103   9168    329  -1883  -1689       C  
ATOM   3965  CG  ASN D 121      39.481  73.883  45.425  1.00 56.91           C  
ANISOU 3965  CG  ASN D 121     5777   6430   9415    423  -2047  -1756       C  
ATOM   3966  OD1 ASN D 121      38.774  73.520  46.362  1.00 62.42           O  
ANISOU 3966  OD1 ASN D 121     6562   7178   9978    500  -2142  -1738       O  
ATOM   3967  ND2 ASN D 121      40.520  74.695  45.589  1.00 62.41           N  
ANISOU 3967  ND2 ASN D 121     6420   7090  10205    419  -2079  -1831       N  
ATOM   3968  N   GLU D 122      37.105  71.236  44.476  1.00 60.68           N  
ANISOU 3968  N   GLU D 122     6358   6978   9719    423  -1904  -1516       N  
ATOM   3969  CA  GLU D 122      36.316  70.285  45.254  1.00 63.67           C  
ANISOU 3969  CA  GLU D 122     6863   7402   9926    511  -1930  -1414       C  
ATOM   3970  C   GLU D 122      36.259  70.629  46.743  1.00 61.98           C  
ANISOU 3970  C   GLU D 122     6732   7238   9581    610  -2080  -1445       C  
ATOM   3971  O   GLU D 122      35.192  70.565  47.360  1.00 62.67           O  
ANISOU 3971  O   GLU D 122     6947   7379   9487    653  -2065  -1369       O  
ATOM   3972  CB  GLU D 122      36.869  68.868  45.081  1.00 66.25           C  
ANISOU 3972  CB  GLU D 122     7144   7713  10316    550  -1954  -1374       C  
ATOM   3973  CG  GLU D 122      36.144  67.840  45.930  1.00 68.72           C  
ANISOU 3973  CG  GLU D 122     7580   8065  10465    639  -1997  -1260       C  
ATOM   3974  CD  GLU D 122      36.331  66.422  45.436  1.00 72.90           C  
ANISOU 3974  CD  GLU D 122     8076   8564  11057    654  -1976  -1192       C  
ATOM   3975  OE1 GLU D 122      35.519  65.552  45.821  1.00 70.54           O  
ANISOU 3975  OE1 GLU D 122     7879   8288  10636    700  -1968  -1073       O  
ATOM   3976  OE2 GLU D 122      37.290  66.177  44.673  1.00 74.49           O  
ANISOU 3976  OE2 GLU D 122     8147   8722  11434    619  -1969  -1260       O  
ATOM   3977  N   GLU D 123      37.401  70.998  47.314  1.00 50.79           N  
ANISOU 3977  N   GLU D 123     5237   5807   8254    646  -2224  -1558       N  
ATOM   3978  CA  GLU D 123      37.495  71.242  48.751  1.00 56.44           C  
ANISOU 3978  CA  GLU D 123     6021   6572   8851    750  -2384  -1599       C  
ATOM   3979  C   GLU D 123      36.691  72.471  49.157  1.00 56.34           C  
ANISOU 3979  C   GLU D 123     6083   6594   8729    744  -2373  -1632       C  
ATOM   3980  O   GLU D 123      36.007  72.468  50.185  1.00 53.28           O  
ANISOU 3980  O   GLU D 123     5810   6279   8155    823  -2427  -1601       O  
ATOM   3981  CB  GLU D 123      38.958  71.404  49.181  1.00 64.63           C  
ANISOU 3981  CB  GLU D 123     6990   7568  10000    780  -2476  -1695       C  
ATOM   3982  CG  GLU D 123      39.768  70.106  49.180  1.00 83.61           C  
ANISOU 3982  CG  GLU D 123     9354   9946  12468    819  -2516  -1665       C  
ATOM   3983  CD  GLU D 123      39.927  69.502  47.795  1.00 91.77           C  
ANISOU 3983  CD  GLU D 123    10297  10932  13640    736  -2387  -1631       C  
ATOM   3984  OE1 GLU D 123      39.779  68.268  47.662  1.00 84.60           O  
ANISOU 3984  OE1 GLU D 123     9397  10025  12723    766  -2389  -1554       O  
ATOM   3985  OE2 GLU D 123      40.212  70.266  46.844  1.00 99.09           O  
ANISOU 3985  OE2 GLU D 123    11150  11819  14680    643  -2279  -1676       O  
ATOM   3986  N   GLN D 124      36.772  73.519  48.342  1.00 54.47           N  
ANISOU 3986  N   GLN D 124     5778   6309   8609    649  -2304  -1695       N  
ATOM   3987  CA  GLN D 124      36.046  74.756  48.614  1.00 57.05           C  
ANISOU 3987  CA  GLN D 124     6163   6653   8860    636  -2296  -1737       C  
ATOM   3988  C   GLN D 124      34.545  74.508  48.519  1.00 57.11           C  
ANISOU 3988  C   GLN D 124     6299   6709   8691    633  -2173  -1620       C  
ATOM   3989  O   GLN D 124      33.787  74.870  49.416  1.00 57.88           O  
ANISOU 3989  O   GLN D 124     6497   6872   8622    697  -2214  -1621       O  
ATOM   3990  CB  GLN D 124      36.458  75.861  47.641  1.00 55.91           C  
ANISOU 3990  CB  GLN D 124     5944   6430   8870    528  -2192  -1779       C  
ATOM   3991  CG  GLN D 124      37.923  76.249  47.704  1.00 56.07           C  
ANISOU 3991  CG  GLN D 124     5876   6394   9033    530  -2230  -1850       C  
ATOM   3992  CD  GLN D 124      38.305  77.231  46.618  1.00 58.78           C  
ANISOU 3992  CD  GLN D 124     6144   6671   9519    422  -2113  -1859       C  
ATOM   3993  OE1 GLN D 124      37.950  77.054  45.451  1.00 63.24           O  
ANISOU 3993  OE1 GLN D 124     6680   7218  10129    332  -1977  -1794       O  
ATOM   3994  NE2 GLN D 124      39.026  78.279  46.996  1.00 57.02           N  
ANISOU 3994  NE2 GLN D 124     5890   6413   9361    433  -2164  -1931       N  
ATOM   3995  N   ARG D 125      34.136  73.869  47.426  1.00 50.67           N  
ANISOU 3995  N   ARG D 125     5474   5865   7912    562  -2023  -1524       N  
ATOM   3996  CA  ARG D 125      32.737  73.538  47.200  1.00 49.50           C  
ANISOU 3996  CA  ARG D 125     5437   5753   7617    552  -1896  -1406       C  
ATOM   3997  C   ARG D 125      32.160  72.680  48.330  1.00 48.27           C  
ANISOU 3997  C   ARG D 125     5394   5680   7265    659  -1952  -1327       C  
ATOM   3998  O   ARG D 125      31.089  72.983  48.856  1.00 46.54           O  
ANISOU 3998  O   ARG D 125     5280   5523   6881    689  -1925  -1291       O  
ATOM   3999  CB  ARG D 125      32.572  72.819  45.862  1.00 47.62           C  
ANISOU 3999  CB  ARG D 125     5158   5468   7467    468  -1746  -1322       C  
ATOM   4000  CG  ARG D 125      31.146  72.413  45.542  1.00 53.05           C  
ANISOU 4000  CG  ARG D 125     5952   6183   8020    454  -1613  -1200       C  
ATOM   4001  CD  ARG D 125      31.011  71.981  44.095  1.00 57.02           C  
ANISOU 4001  CD  ARG D 125     6403   6633   8628    361  -1464  -1143       C  
ATOM   4002  NE  ARG D 125      32.003  70.977  43.718  1.00 59.68           N  
ANISOU 4002  NE  ARG D 125     6650   6941   9084    366  -1487  -1141       N  
ATOM   4003  CZ  ARG D 125      32.944  71.170  42.800  1.00 58.37           C  
ANISOU 4003  CZ  ARG D 125     6357   6725   9095    296  -1461  -1204       C  
ATOM   4004  NH1 ARG D 125      33.808  70.203  42.523  1.00 57.42           N  
ANISOU 4004  NH1 ARG D 125     6155   6586   9076    312  -1487  -1209       N  
ATOM   4005  NH2 ARG D 125      33.013  72.327  42.148  1.00 48.06           N  
ANISOU 4005  NH2 ARG D 125     5004   5389   7868    209  -1410  -1261       N  
ATOM   4006  N   ASN D 126      32.872  71.618  48.696  1.00 40.98           N  
ANISOU 4006  N   ASN D 126     4448   4760   6362    714  -2030  -1298       N  
ATOM   4007  CA  ASN D 126      32.438  70.733  49.770  1.00 45.14           C  
ANISOU 4007  CA  ASN D 126     5076   5362   6712    812  -2093  -1211       C  
ATOM   4008  C   ASN D 126      32.283  71.465  51.100  1.00 47.93           C  
ANISOU 4008  C   ASN D 126     5498   5797   6917    897  -2213  -1275       C  
ATOM   4009  O   ASN D 126      31.409  71.139  51.905  1.00 43.29           O  
ANISOU 4009  O   ASN D 126     5022   5296   6132    958  -2215  -1197       O  
ATOM   4010  CB  ASN D 126      33.412  69.559  49.939  1.00 50.28           C  
ANISOU 4010  CB  ASN D 126     5677   5989   7440    857  -2183  -1186       C  
ATOM   4011  CG  ASN D 126      33.351  68.586  48.785  1.00 48.42           C  
ANISOU 4011  CG  ASN D 126     5396   5693   7308    796  -2067  -1102       C  
ATOM   4012  OD1 ASN D 126      32.385  68.569  48.023  1.00 48.54           O  
ANISOU 4012  OD1 ASN D 126     5449   5702   7293    736  -1920  -1030       O  
ATOM   4013  ND2 ASN D 126      34.379  67.761  48.652  1.00 45.49           N  
ANISOU 4013  ND2 ASN D 126     4943   5278   7062    816  -2138  -1117       N  
ATOM   4014  N   ALA D 127      33.129  72.462  51.328  1.00 43.02           N  
ANISOU 4014  N   ALA D 127     4805   5150   6389    900  -2314  -1421       N  
ATOM   4015  CA  ALA D 127      33.129  73.172  52.597  1.00 43.13           C  
ANISOU 4015  CA  ALA D 127     4870   5238   6279    988  -2447  -1505       C  
ATOM   4016  C   ALA D 127      31.913  74.084  52.719  1.00 43.87           C  
ANISOU 4016  C   ALA D 127     5043   5382   6242    978  -2374  -1512       C  
ATOM   4017  O   ALA D 127      31.270  74.129  53.764  1.00 53.87           O  
ANISOU 4017  O   ALA D 127     6406   6752   7311   1060  -2420  -1498       O  
ATOM   4018  CB  ALA D 127      34.409  73.971  52.754  1.00 44.47           C  
ANISOU 4018  CB  ALA D 127     4933   5356   6609    993  -2581  -1664       C  
ATOM   4019  N   PHE D 128      31.613  74.811  51.643  1.00 35.29           N  
ANISOU 4019  N   PHE D 128     3914   4226   5267    877  -2261  -1535       N  
ATOM   4020  CA  PHE D 128      30.416  75.640  51.602  1.00 47.03           C  
ANISOU 4020  CA  PHE D 128     5471   5747   6651    857  -2181  -1538       C  
ATOM   4021  C   PHE D 128      29.160  74.800  51.796  1.00 50.55           C  
ANISOU 4021  C   PHE D 128     6030   6271   6905    882  -2079  -1392       C  
ATOM   4022  O   PHE D 128      28.263  75.160  52.557  1.00 52.44           O  
ANISOU 4022  O   PHE D 128     6357   6601   6968    937  -2083  -1394       O  
ATOM   4023  CB  PHE D 128      30.318  76.412  50.280  1.00 41.16           C  
ANISOU 4023  CB  PHE D 128     4661   4905   6072    734  -2071  -1564       C  
ATOM   4024  CG  PHE D 128      31.290  77.553  50.164  1.00 46.93           C  
ANISOU 4024  CG  PHE D 128     5290   5567   6973    703  -2166  -1712       C  
ATOM   4025  CD1 PHE D 128      31.165  78.671  50.970  1.00 53.19           C  
ANISOU 4025  CD1 PHE D 128     6104   6388   7718    752  -2270  -1830       C  
ATOM   4026  CD2 PHE D 128      32.306  77.524  49.225  1.00 49.18           C  
ANISOU 4026  CD2 PHE D 128     5456   5760   7472    621  -2149  -1734       C  
ATOM   4027  CE1 PHE D 128      32.048  79.729  50.858  1.00 51.92           C  
ANISOU 4027  CE1 PHE D 128     5861   6151   7717    722  -2319  -1932       C  
ATOM   4028  CE2 PHE D 128      33.192  78.580  49.108  1.00 52.22           C  
ANISOU 4028  CE2 PHE D 128     5752   6078   8013    586  -2213  -1846       C  
ATOM   4029  CZ  PHE D 128      33.061  79.684  49.927  1.00 47.52           C  
ANISOU 4029  CZ  PHE D 128     5195   5498   7361    639  -2273  -1923       C  
ATOM   4030  N   ILE D 129      29.108  73.672  51.094  1.00 33.26           N  
ANISOU 4030  N   ILE D 129     3834   4047   4756    843  -1989  -1270       N  
ATOM   4031  CA  ILE D 129      27.959  72.772  51.160  1.00 41.40           C  
ANISOU 4031  CA  ILE D 129     4962   5136   5632    856  -1887  -1119       C  
ATOM   4032  C   ILE D 129      27.769  72.222  52.575  1.00 45.39           C  
ANISOU 4032  C   ILE D 129     5551   5757   5936    969  -1986  -1075       C  
ATOM   4033  O   ILE D 129      26.646  72.161  53.072  1.00 49.18           O  
ANISOU 4033  O   ILE D 129     6127   6327   6234    999  -1933  -1007       O  
ATOM   4034  CB  ILE D 129      28.113  71.607  50.158  1.00 38.61           C  
ANISOU 4034  CB  ILE D 129     4572   4714   5385    799  -1796  -1008       C  
ATOM   4035  CG1 ILE D 129      27.982  72.129  48.726  1.00 33.49           C  
ANISOU 4035  CG1 ILE D 129     3861   3975   4890    685  -1668  -1029       C  
ATOM   4036  CG2 ILE D 129      27.074  70.517  50.413  1.00 36.33           C  
ANISOU 4036  CG2 ILE D 129     4379   4483   4941    827  -1724   -847       C  
ATOM   4037  CD1 ILE D 129      28.252  71.088  47.672  1.00 32.02           C  
ANISOU 4037  CD1 ILE D 129     3622   3720   4824    630  -1585   -947       C  
ATOM   4038  N   GLN D 130      28.866  71.821  53.218  1.00 50.67           N  
ANISOU 4038  N   GLN D 130     6185   6430   6638   1029  -2129  -1111       N  
ATOM   4039  CA  GLN D 130      28.818  71.375  54.610  1.00 52.98           C  
ANISOU 4039  CA  GLN D 130     6555   6836   6741   1139  -2242  -1077       C  
ATOM   4040  C   GLN D 130      28.234  72.449  55.522  1.00 49.14           C  
ANISOU 4040  C   GLN D 130     6127   6451   6093   1197  -2286  -1167       C  
ATOM   4041  O   GLN D 130      27.376  72.166  56.362  1.00 48.57           O  
ANISOU 4041  O   GLN D 130     6151   6498   5805   1256  -2276  -1094       O  
ATOM   4042  CB  GLN D 130      30.211  70.977  55.104  1.00 53.05           C  
ANISOU 4042  CB  GLN D 130     6503   6817   6836   1193  -2406  -1132       C  
ATOM   4043  CG  GLN D 130      30.188  70.292  56.464  1.00 55.61           C  
ANISOU 4043  CG  GLN D 130     6910   7253   6965   1302  -2521  -1068       C  
ATOM   4044  CD  GLN D 130      29.339  69.028  56.463  1.00 62.05           C  
ANISOU 4044  CD  GLN D 130     7803   8105   7666   1300  -2435   -870       C  
ATOM   4045  OE1 GLN D 130      29.450  68.189  55.564  1.00 61.50           O  
ANISOU 4045  OE1 GLN D 130     7696   7948   7722   1242  -2364   -786       O  
ATOM   4046  NE2 GLN D 130      28.469  68.901  57.455  1.00 61.86           N  
ANISOU 4046  NE2 GLN D 130     7886   8214   7404   1362  -2439   -797       N  
ATOM   4047  N   SER D 131      28.714  73.680  55.357  1.00 48.36           N  
ANISOU 4047  N   SER D 131     5965   6307   6103   1179  -2336  -1327       N  
ATOM   4048  CA  SER D 131      28.220  74.813  56.137  1.00 47.12           C  
ANISOU 4048  CA  SER D 131     5848   6231   5822   1232  -2387  -1439       C  
ATOM   4049  C   SER D 131      26.725  75.010  55.928  1.00 50.84           C  
ANISOU 4049  C   SER D 131     6398   6759   6161   1206  -2241  -1372       C  
ATOM   4050  O   SER D 131      25.985  75.273  56.875  1.00 56.11           O  
ANISOU 4050  O   SER D 131     7141   7552   6625   1279  -2262  -1384       O  
ATOM   4051  CB  SER D 131      28.972  76.089  55.753  1.00 43.21           C  
ANISOU 4051  CB  SER D 131     5259   5646   5512   1196  -2453  -1613       C  
ATOM   4052  OG  SER D 131      30.368  75.871  55.691  1.00 43.47           O  
ANISOU 4052  OG  SER D 131     5203   5607   5708   1198  -2563  -1668       O  
ATOM   4053  N   LEU D 132      26.294  74.863  54.678  1.00 44.32           N  
ANISOU 4053  N   LEU D 132     5548   5843   5448   1103  -2094  -1303       N  
ATOM   4054  CA  LEU D 132      24.881  74.872  54.326  1.00 49.65           C  
ANISOU 4054  CA  LEU D 132     6291   6555   6018   1069  -1944  -1220       C  
ATOM   4055  C   LEU D 132      24.088  73.828  55.115  1.00 48.61           C  
ANISOU 4055  C   LEU D 132     6256   6546   5667   1130  -1913  -1076       C  
ATOM   4056  O   LEU D 132      23.025  74.126  55.663  1.00 41.07           O  
ANISOU 4056  O   LEU D 132     5374   5696   4536   1165  -1869  -1065       O  
ATOM   4057  CB  LEU D 132      24.714  74.622  52.826  1.00 43.84           C  
ANISOU 4057  CB  LEU D 132     5511   5697   5449    951  -1802  -1152       C  
ATOM   4058  CG  LEU D 132      24.700  75.854  51.935  1.00 44.07           C  
ANISOU 4058  CG  LEU D 132     5484   5635   5628    872  -1763  -1259       C  
ATOM   4059  CD1 LEU D 132      24.515  75.442  50.492  1.00 40.20           C  
ANISOU 4059  CD1 LEU D 132     4957   5041   5275    762  -1619  -1173       C  
ATOM   4060  CD2 LEU D 132      23.591  76.781  52.373  1.00 52.25           C  
ANISOU 4060  CD2 LEU D 132     6582   6741   6531    899  -1738  -1314       C  
ATOM   4061  N   LYS D 133      24.598  72.599  55.149  1.00 47.32           N  
ANISOU 4061  N   LYS D 133     6090   6367   5520   1139  -1934   -963       N  
ATOM   4062  CA  LYS D 133      23.951  71.521  55.892  1.00 50.81           C  
ANISOU 4062  CA  LYS D 133     6619   6915   5770   1190  -1916   -809       C  
ATOM   4063  C   LYS D 133      23.872  71.891  57.371  1.00 55.74           C  
ANISOU 4063  C   LYS D 133     7303   7692   6184   1300  -2031   -865       C  
ATOM   4064  O   LYS D 133      22.817  71.783  57.990  1.00 56.85           O  
ANISOU 4064  O   LYS D 133     7523   7956   6121   1336  -1977   -797       O  
ATOM   4065  CB  LYS D 133      24.704  70.201  55.710  1.00 56.16           C  
ANISOU 4065  CB  LYS D 133     7273   7535   6531   1186  -1952   -698       C  
ATOM   4066  CG  LYS D 133      24.549  69.544  54.342  1.00 55.69           C  
ANISOU 4066  CG  LYS D 133     7172   7353   6633   1090  -1824   -609       C  
ATOM   4067  CD  LYS D 133      24.887  68.055  54.407  1.00 55.71           C  
ANISOU 4067  CD  LYS D 133     7181   7334   6651   1104  -1851   -464       C  
ATOM   4068  CE  LYS D 133      26.349  67.784  54.091  1.00 52.85           C  
ANISOU 4068  CE  LYS D 133     6725   6874   6481   1103  -1956   -532       C  
ATOM   4069  NZ  LYS D 133      26.520  67.122  52.767  1.00 55.09           N  
ANISOU 4069  NZ  LYS D 133     6945   7035   6953   1022  -1863   -481       N  
ATOM   4070  N   ASP D 134      24.998  72.337  57.919  1.00 57.73           N  
ANISOU 4070  N   ASP D 134     7510   7937   6486   1354  -2188   -992       N  
ATOM   4071  CA  ASP D 134      25.099  72.618  59.342  1.00 65.38           C  
ANISOU 4071  CA  ASP D 134     8530   9049   7264   1467  -2318  -1052       C  
ATOM   4072  C   ASP D 134      24.260  73.806  59.812  1.00 67.94           C  
ANISOU 4072  C   ASP D 134     8888   9471   7457   1502  -2302  -1167       C  
ATOM   4073  O   ASP D 134      23.691  73.771  60.901  1.00 71.60           O  
ANISOU 4073  O   ASP D 134     9424  10093   7686   1584  -2331  -1150       O  
ATOM   4074  CB  ASP D 134      26.563  72.857  59.731  1.00 65.42           C  
ANISOU 4074  CB  ASP D 134     8469   9008   7381   1514  -2498  -1175       C  
ATOM   4075  CG  ASP D 134      27.424  71.624  59.547  1.00 71.74           C  
ANISOU 4075  CG  ASP D 134     9243   9739   8277   1506  -2545  -1070       C  
ATOM   4076  OD1 ASP D 134      26.868  70.506  59.650  1.00 72.08           O  
ANISOU 4076  OD1 ASP D 134     9346   9823   8219   1505  -2483   -894       O  
ATOM   4077  OD2 ASP D 134      28.645  71.767  59.313  1.00 74.27           O  
ANISOU 4077  OD2 ASP D 134     9479   9964   8778   1502  -2646  -1163       O  
ATOM   4078  N   ASP D 135      24.171  74.854  58.999  1.00 65.78           N  
ANISOU 4078  N   ASP D 135     8560   9104   7330   1441  -2256  -1283       N  
ATOM   4079  CA  ASP D 135      23.379  76.021  59.378  1.00 62.43           C  
ANISOU 4079  CA  ASP D 135     8159   8756   6804   1473  -2247  -1403       C  
ATOM   4080  C   ASP D 135      22.612  76.611  58.188  1.00 56.32           C  
ANISOU 4080  C   ASP D 135     7363   7887   6149   1373  -2103  -1411       C  
ATOM   4081  O   ASP D 135      23.115  77.507  57.510  1.00 51.25           O  
ANISOU 4081  O   ASP D 135     6649   7127   5697   1321  -2129  -1529       O  
ATOM   4082  CB  ASP D 135      24.275  77.096  60.011  1.00 57.57           C  
ANISOU 4082  CB  ASP D 135     7495   8132   6248   1530  -2398  -1596       C  
ATOM   4083  CG  ASP D 135      23.476  78.197  60.692  1.00 63.24           C  
ANISOU 4083  CG  ASP D 135     8240   8931   6859   1570  -2360  -1693       C  
ATOM   4084  OD1 ASP D 135      22.237  78.223  60.566  1.00 62.02           O  
ANISOU 4084  OD1 ASP D 135     8136   8847   6581   1560  -2252  -1645       O  
ATOM   4085  OD2 ASP D 135      24.098  79.046  61.367  1.00 66.69           O  
ANISOU 4085  OD2 ASP D 135     8643   9358   7341   1616  -2440  -1819       O  
ATOM   4086  N   PRO D 136      21.389  76.112  57.942  1.00 57.09           N  
ANISOU 4086  N   PRO D 136     7522   8035   6135   1343  -1955  -1282       N  
ATOM   4087  CA  PRO D 136      20.509  76.572  56.855  1.00 56.59           C  
ANISOU 4087  CA  PRO D 136     7449   7893   6159   1253  -1811  -1272       C  
ATOM   4088  C   PRO D 136      20.286  78.086  56.850  1.00 57.84           C  
ANISOU 4088  C   PRO D 136     7582   8037   6359   1260  -1850  -1456       C  
ATOM   4089  O   PRO D 136      20.058  78.660  55.786  1.00 57.24           O  
ANISOU 4089  O   PRO D 136     7468   7843   6437   1173  -1778  -1484       O  
ATOM   4090  CB  PRO D 136      19.194  75.834  57.139  1.00 52.58           C  
ANISOU 4090  CB  PRO D 136     7025   7501   5452   1265  -1687  -1125       C  
ATOM   4091  CG  PRO D 136      19.603  74.614  57.879  1.00 53.12           C  
ANISOU 4091  CG  PRO D 136     7129   7644   5410   1317  -1737   -999       C  
ATOM   4092  CD  PRO D 136      20.783  75.013  58.718  1.00 50.45           C  
ANISOU 4092  CD  PRO D 136     6761   7331   5076   1394  -1919  -1125       C  
ATOM   4093  N   SER D 137      20.366  78.718  58.017  1.00 57.14           N  
ANISOU 4093  N   SER D 137     7511   8064   6137   1363  -1970  -1581       N  
ATOM   4094  CA  SER D 137      20.110  80.158  58.129  1.00 59.75           C  
ANISOU 4094  CA  SER D 137     7816   8385   6501   1381  -2017  -1762       C  
ATOM   4095  C   SER D 137      21.220  81.008  57.501  1.00 55.64           C  
ANISOU 4095  C   SER D 137     7201   7697   6244   1326  -2094  -1876       C  
ATOM   4096  O   SER D 137      21.046  82.209  57.294  1.00 51.58           O  
ANISOU 4096  O   SER D 137     6648   7115   5835   1303  -2084  -1976       O  
ATOM   4097  CB  SER D 137      19.923  80.549  59.602  1.00 58.69           C  
ANISOU 4097  CB  SER D 137     7709   8389   6202   1485  -2052  -1811       C  
ATOM   4098  OG  SER D 137      21.158  80.586  60.295  1.00 60.27           O  
ANISOU 4098  OG  SER D 137     7873   8576   6451   1535  -2179  -1866       O  
ATOM   4099  N   GLN D 138      22.354  80.379  57.205  1.00 47.26           N  
ANISOU 4099  N   GLN D 138     6095   6565   5296   1303  -2162  -1846       N  
ATOM   4100  CA  GLN D 138      23.487  81.091  56.613  1.00 47.76           C  
ANISOU 4100  CA  GLN D 138     6061   6474   5613   1246  -2228  -1939       C  
ATOM   4101  C   GLN D 138      23.560  80.958  55.094  1.00 50.86           C  
ANISOU 4101  C   GLN D 138     6404   6718   6203   1114  -2126  -1875       C  
ATOM   4102  O   GLN D 138      24.587  81.269  54.491  1.00 51.42           O  
ANISOU 4102  O   GLN D 138     6388   6668   6480   1056  -2176  -1925       O  
ATOM   4103  CB  GLN D 138      24.804  80.606  57.233  1.00 45.78           C  
ANISOU 4103  CB  GLN D 138     5774   6220   5399   1296  -2345  -1947       C  
ATOM   4104  CG  GLN D 138      25.526  81.661  58.062  1.00 53.66           C  
ANISOU 4104  CG  GLN D 138     6731   7201   6455   1353  -2435  -2077       C  
ATOM   4105  CD  GLN D 138      24.662  82.272  59.147  1.00 61.36           C  
ANISOU 4105  CD  GLN D 138     7766   8302   7247   1441  -2427  -2127       C  
ATOM   4106  OE1 GLN D 138      24.359  83.464  59.113  1.00 66.09           O  
ANISOU 4106  OE1 GLN D 138     8337   8860   7913   1436  -2417  -2219       O  
ATOM   4107  NE2 GLN D 138      24.263  81.457  60.118  1.00 59.83           N  
ANISOU 4107  NE2 GLN D 138     7647   8261   6825   1520  -2430  -2058       N  
ATOM   4108  N   SER D 139      22.467  80.520  54.479  1.00 44.58           N  
ANISOU 4108  N   SER D 139     5659   5931   5350   1062  -1966  -1754       N  
ATOM   4109  CA  SER D 139      22.481  80.177  53.056  1.00 37.37           C  
ANISOU 4109  CA  SER D 139     4708   4888   4603    939  -1840  -1657       C  
ATOM   4110  C   SER D 139      22.799  81.383  52.179  1.00 42.74           C  
ANISOU 4110  C   SER D 139     5314   5434   5490    856  -1854  -1762       C  
ATOM   4111  O   SER D 139      23.676  81.312  51.318  1.00 53.70           O  
ANISOU 4111  O   SER D 139     6626   6710   7068    777  -1848  -1749       O  
ATOM   4112  CB  SER D 139      21.142  79.579  52.646  1.00 35.80           C  
ANISOU 4112  CB  SER D 139     4581   4729   4292    910  -1676  -1521       C  
ATOM   4113  OG  SER D 139      20.935  78.324  53.266  1.00 42.16           O  
ANISOU 4113  OG  SER D 139     5445   5636   4939    964  -1651  -1394       O  
ATOM   4114  N   ALA D 140      22.061  82.474  52.394  1.00 40.92           N  
ANISOU 4114  N   ALA D 140     5104   5219   5223    873  -1872  -1863       N  
ATOM   4115  CA  ALA D 140      22.297  83.730  51.692  1.00 45.36           C  
ANISOU 4115  CA  ALA D 140     5602   5657   5977    801  -1899  -1963       C  
ATOM   4116  C   ALA D 140      23.759  84.155  51.767  1.00 46.94           C  
ANISOU 4116  C   ALA D 140     5708   5779   6349    793  -1989  -2012       C  
ATOM   4117  O   ALA D 140      24.371  84.482  50.747  1.00 48.01           O  
ANISOU 4117  O   ALA D 140     5770   5790   6683    693  -1953  -1991       O  
ATOM   4118  CB  ALA D 140      21.396  84.820  52.252  1.00 32.95           C  
ANISOU 4118  CB  ALA D 140     4061   4129   4331    850  -1887  -2022       C  
ATOM   4119  N   ASN D 141      24.310  84.164  52.975  1.00 51.94           N  
ANISOU 4119  N   ASN D 141     6345   6489   6901    899  -2098  -2071       N  
ATOM   4120  CA  ASN D 141      25.699  84.567  53.180  1.00 51.55           C  
ANISOU 4120  CA  ASN D 141     6212   6371   7004    906  -2190  -2127       C  
ATOM   4121  C   ASN D 141      26.673  83.623  52.487  1.00 59.00           C  
ANISOU 4121  C   ASN D 141     7099   7254   8063    844  -2191  -2070       C  
ATOM   4122  O   ASN D 141      27.603  84.066  51.814  1.00 67.79           O  
ANISOU 4122  O   ASN D 141     8125   8256   9378    774  -2189  -2079       O  
ATOM   4123  CB  ASN D 141      26.031  84.610  54.671  1.00 59.72           C  
ANISOU 4123  CB  ASN D 141     7274   7509   7907   1039  -2302  -2198       C  
ATOM   4124  CG  ASN D 141      25.211  85.635  55.436  1.00 64.66           C  
ANISOU 4124  CG  ASN D 141     7936   8195   8438   1108  -2310  -2270       C  
ATOM   4125  OD1 ASN D 141      24.851  86.682  54.897  1.00 62.55           O  
ANISOU 4125  OD1 ASN D 141     7639   7850   8277   1058  -2271  -2298       O  
ATOM   4126  ND2 ASN D 141      24.910  85.335  56.694  1.00 65.21           N  
ANISOU 4126  ND2 ASN D 141     8066   8404   8305   1223  -2358  -2295       N  
ATOM   4127  N   LEU D 142      26.443  82.324  52.650  1.00 54.34           N  
ANISOU 4127  N   LEU D 142     6557   6743   7345    872  -2191  -2003       N  
ATOM   4128  CA  LEU D 142      27.311  81.303  52.069  1.00 51.84           C  
ANISOU 4128  CA  LEU D 142     6188   6380   7130    826  -2185  -1933       C  
ATOM   4129  C   LEU D 142      27.295  81.328  50.540  1.00 52.50           C  
ANISOU 4129  C   LEU D 142     6216   6344   7386    688  -2050  -1864       C  
ATOM   4130  O   LEU D 142      28.307  81.048  49.898  1.00 53.26           O  
ANISOU 4130  O   LEU D 142     6226   6363   7647    628  -2053  -1853       O  
ATOM   4131  CB  LEU D 142      26.908  79.917  52.580  1.00 46.87           C  
ANISOU 4131  CB  LEU D 142     5637   5854   6318    888  -2137  -1799       C  
ATOM   4132  CG  LEU D 142      27.250  79.641  54.046  1.00 41.69           C  
ANISOU 4132  CG  LEU D 142     5020   5313   5506   1020  -2281  -1847       C  
ATOM   4133  CD1 LEU D 142      26.533  78.397  54.545  1.00 42.72           C  
ANISOU 4133  CD1 LEU D 142     5246   5555   5432   1072  -2216  -1698       C  
ATOM   4134  CD2 LEU D 142      28.755  79.517  54.226  1.00 36.88           C  
ANISOU 4134  CD2 LEU D 142     4323   4650   5039   1035  -2415  -1914       C  
ATOM   4135  N   LEU D 143      26.145  81.659  49.964  1.00 52.47           N  
ANISOU 4135  N   LEU D 143     6263   6332   7343    638  -1932  -1819       N  
ATOM   4136  CA  LEU D 143      26.017  81.728  48.514  1.00 43.47           C  
ANISOU 4136  CA  LEU D 143     5082   5088   6349    510  -1802  -1751       C  
ATOM   4137  C   LEU D 143      26.722  82.970  47.979  1.00 50.36           C  
ANISOU 4137  C   LEU D 143     5864   5853   7417    439  -1840  -1834       C  
ATOM   4138  O   LEU D 143      27.401  82.913  46.953  1.00 52.64           O  
ANISOU 4138  O   LEU D 143     6076   6060   7866    345  -1775  -1785       O  
ATOM   4139  CB  LEU D 143      24.542  81.733  48.102  1.00 38.94           C  
ANISOU 4139  CB  LEU D 143     4592   4536   5667    485  -1667  -1674       C  
ATOM   4140  CG  LEU D 143      24.246  82.016  46.629  1.00 40.16           C  
ANISOU 4140  CG  LEU D 143     4715   4585   5957    355  -1540  -1617       C  
ATOM   4141  CD1 LEU D 143      24.873  80.958  45.734  1.00 33.88           C  
ANISOU 4141  CD1 LEU D 143     3870   3751   5251    292  -1456  -1513       C  
ATOM   4142  CD2 LEU D 143      22.749  82.103  46.392  1.00 31.19           C  
ANISOU 4142  CD2 LEU D 143     3667   3477   4705    347  -1429  -1559       C  
ATOM   4143  N   ALA D 144      26.562  84.087  48.684  1.00 49.89           N  
ANISOU 4143  N   ALA D 144     5819   5809   7329    493  -1895  -1904       N  
ATOM   4144  CA  ALA D 144      27.255  85.324  48.331  1.00 54.16           C  
ANISOU 4144  CA  ALA D 144     6285   6262   8034    448  -1901  -1931       C  
ATOM   4145  C   ALA D 144      28.766  85.152  48.462  1.00 52.70           C  
ANISOU 4145  C   ALA D 144     6012   6041   7971    454  -1972  -1958       C  
ATOM   4146  O   ALA D 144      29.530  85.596  47.606  1.00 55.21           O  
ANISOU 4146  O   ALA D 144     6249   6274   8453    372  -1929  -1928       O  
ATOM   4147  CB  ALA D 144      26.773  86.472  49.206  1.00 49.55           C  
ANISOU 4147  CB  ALA D 144     5732   5706   7388    523  -1964  -2011       C  
ATOM   4148  N   GLU D 145      29.179  84.504  49.548  1.00 48.98           N  
ANISOU 4148  N   GLU D 145     5560   5642   7409    556  -2079  -2008       N  
ATOM   4149  CA  GLU D 145      30.589  84.225  49.803  1.00 56.44           C  
ANISOU 4149  CA  GLU D 145     6429   6559   8455    576  -2156  -2039       C  
ATOM   4150  C   GLU D 145      31.192  83.358  48.702  1.00 58.94           C  
ANISOU 4150  C   GLU D 145     6680   6826   8889    484  -2079  -1962       C  
ATOM   4151  O   GLU D 145      32.286  83.637  48.207  1.00 60.21           O  
ANISOU 4151  O   GLU D 145     6749   6916   9210    436  -2072  -1964       O  
ATOM   4152  CB  GLU D 145      30.752  83.536  51.160  1.00 58.24           C  
ANISOU 4152  CB  GLU D 145     6708   6888   8534    706  -2276  -2088       C  
ATOM   4153  CG  GLU D 145      32.158  83.613  51.733  1.00 57.81           C  
ANISOU 4153  CG  GLU D 145     6586   6805   8573    753  -2381  -2150       C  
ATOM   4154  CD  GLU D 145      32.361  82.667  52.901  1.00 59.90           C  
ANISOU 4154  CD  GLU D 145     6903   7169   8689    868  -2484  -2166       C  
ATOM   4155  OE1 GLU D 145      31.394  82.449  53.662  1.00 61.57           O  
ANISOU 4155  OE1 GLU D 145     7209   7485   8699    941  -2501  -2162       O  
ATOM   4156  OE2 GLU D 145      33.483  82.147  53.063  1.00 62.79           O  
ANISOU 4156  OE2 GLU D 145     7215   7511   9132    885  -2545  -2177       O  
ATOM   4157  N   ALA D 146      30.467  82.310  48.319  1.00 60.91           N  
ANISOU 4157  N   ALA D 146     6974   7112   9056    463  -2018  -1894       N  
ATOM   4158  CA  ALA D 146      30.932  81.372  47.298  1.00 65.53           C  
ANISOU 4158  CA  ALA D 146     7499   7659   9742    384  -1940  -1821       C  
ATOM   4159  C   ALA D 146      30.969  82.028  45.916  1.00 65.67           C  
ANISOU 4159  C   ALA D 146     7462   7591   9900    257  -1803  -1764       C  
ATOM   4160  O   ALA D 146      31.875  81.762  45.128  1.00 61.25           O  
ANISOU 4160  O   ALA D 146     6816   6986   9470    195  -1751  -1730       O  
ATOM   4161  CB  ALA D 146      30.041  80.137  47.269  1.00 68.24           C  
ANISOU 4161  CB  ALA D 146     7914   8064   9950    403  -1894  -1742       C  
ATOM   4162  N   LYS D 147      29.985  82.882  45.634  1.00 60.50           N  
ANISOU 4162  N   LYS D 147     6858   6923   9205    224  -1742  -1748       N  
ATOM   4163  CA  LYS D 147      29.949  83.612  44.370  1.00 63.51           C  
ANISOU 4163  CA  LYS D 147     7201   7236   9695    112  -1618  -1682       C  
ATOM   4164  C   LYS D 147      31.196  84.471  44.157  1.00 63.47           C  
ANISOU 4164  C   LYS D 147     7103   7175   9836     83  -1644  -1706       C  
ATOM   4165  O   LYS D 147      31.789  84.464  43.073  1.00 67.85           O  
ANISOU 4165  O   LYS D 147     7593   7690  10496     -5  -1553  -1644       O  
ATOM   4166  CB  LYS D 147      28.699  84.499  44.290  1.00 64.67           C  
ANISOU 4166  CB  LYS D 147     7422   7380   9769     99  -1575  -1671       C  
ATOM   4167  CG  LYS D 147      27.453  83.783  43.792  1.00 62.18           C  
ANISOU 4167  CG  LYS D 147     7181   7087   9357     69  -1477  -1604       C  
ATOM   4168  CD  LYS D 147      26.483  84.765  43.148  1.00 67.18           C  
ANISOU 4168  CD  LYS D 147     7856   7689   9981     13  -1390  -1560       C  
ATOM   4169  CE  LYS D 147      25.032  84.457  43.500  1.00 78.98           C  
ANISOU 4169  CE  LYS D 147     9455   9229  11325     51  -1366  -1559       C  
ATOM   4170  NZ  LYS D 147      24.339  83.739  42.392  1.00 84.49           N  
ANISOU 4170  NZ  LYS D 147    10180   9905  12017    -27  -1225  -1458       N  
ATOM   4171  N   LYS D 148      31.589  85.216  45.187  1.00 56.50           N  
ANISOU 4171  N   LYS D 148     6217   6295   8954    160  -1767  -1796       N  
ATOM   4172  CA  LYS D 148      32.756  86.091  45.088  1.00 65.72           C  
ANISOU 4172  CA  LYS D 148     7301   7406  10264    141  -1806  -1828       C  
ATOM   4173  C   LYS D 148      34.044  85.297  44.908  1.00 65.42           C  
ANISOU 4173  C   LYS D 148     7180   7358  10319    132  -1817  -1830       C  
ATOM   4174  O   LYS D 148      34.886  85.651  44.082  1.00 73.16           O  
ANISOU 4174  O   LYS D 148     8082   8289  11425     59  -1763  -1798       O  
ATOM   4175  CB  LYS D 148      32.856  86.993  46.321  1.00 70.34           C  
ANISOU 4175  CB  LYS D 148     7904   7996  10827    237  -1942  -1932       C  
ATOM   4176  CG  LYS D 148      31.845  88.128  46.306  1.00 77.59           C  
ANISOU 4176  CG  LYS D 148     8872   8900  11708    230  -1926  -1934       C  
ATOM   4177  CD  LYS D 148      31.894  88.967  47.566  1.00 80.37           C  
ANISOU 4177  CD  LYS D 148     9241   9265  12031    336  -2060  -2044       C  
ATOM   4178  CE  LYS D 148      30.712  89.923  47.616  1.00 83.91           C  
ANISOU 4178  CE  LYS D 148     9746   9714  12420    342  -2043  -2048       C  
ATOM   4179  NZ  LYS D 148      30.956  91.081  48.523  1.00 89.91           N  
ANISOU 4179  NZ  LYS D 148    10492  10455  13214    419  -2159  -2148       N  
ATOM   4180  N   LEU D 149      34.191  84.220  45.676  1.00 58.24           N  
ANISOU 4180  N   LEU D 149     6289   6500   9341    210  -1888  -1864       N  
ATOM   4181  CA  LEU D 149      35.364  83.359  45.571  1.00 60.34           C  
ANISOU 4181  CA  LEU D 149     6479   6759   9687    214  -1907  -1869       C  
ATOM   4182  C   LEU D 149      35.467  82.779  44.167  1.00 61.26           C  
ANISOU 4182  C   LEU D 149     6548   6857   9872    108  -1760  -1775       C  
ATOM   4183  O   LEU D 149      36.550  82.714  43.585  1.00 66.82           O  
ANISOU 4183  O   LEU D 149     7164   7531  10695     65  -1727  -1767       O  
ATOM   4184  CB  LEU D 149      35.306  82.236  46.610  1.00 66.12           C  
ANISOU 4184  CB  LEU D 149     7256   7557  10311    317  -2008  -1905       C  
ATOM   4185  CG  LEU D 149      36.518  81.303  46.708  1.00 73.00           C  
ANISOU 4185  CG  LEU D 149     8056   8424  11257    342  -2054  -1920       C  
ATOM   4186  CD1 LEU D 149      37.797  82.087  46.947  1.00 74.09           C  
ANISOU 4186  CD1 LEU D 149     8115   8510  11525    353  -2116  -1988       C  
ATOM   4187  CD2 LEU D 149      36.308  80.278  47.808  1.00 75.79           C  
ANISOU 4187  CD2 LEU D 149     8471   8848  11477    451  -2164  -1942       C  
ATOM   4188  N   ASN D 150      34.324  82.358  43.632  1.00 59.92           N  
ANISOU 4188  N   ASN D 150     6439   6709   9619     70  -1668  -1707       N  
ATOM   4189  CA  ASN D 150      34.246  81.849  42.269  1.00 63.61           C  
ANISOU 4189  CA  ASN D 150     6874   7164  10130    -27  -1517  -1613       C  
ATOM   4190  C   ASN D 150      34.674  82.891  41.245  1.00 61.60           C  
ANISOU 4190  C   ASN D 150     6569   6864   9971   -121  -1428  -1571       C  
ATOM   4191  O   ASN D 150      35.402  82.594  40.297  1.00 54.08           O  
ANISOU 4191  O   ASN D 150     5548   5903   9097   -183  -1343  -1528       O  
ATOM   4192  CB  ASN D 150      32.822  81.373  41.961  1.00 55.69           C  
ANISOU 4192  CB  ASN D 150     5957   6187   9016    -45  -1441  -1552       C  
ATOM   4193  CG  ASN D 150      32.666  80.894  40.532  1.00 52.41           C  
ANISOU 4193  CG  ASN D 150     5517   5760   8636   -141  -1279  -1454       C  
ATOM   4194  OD1 ASN D 150      32.976  79.747  40.215  1.00 57.55           O  
ANISOU 4194  OD1 ASN D 150     6133   6427   9307   -141  -1248  -1431       O  
ATOM   4195  ND2 ASN D 150      32.174  81.770  39.660  1.00 47.65           N  
ANISOU 4195  ND2 ASN D 150     4935   5136   8035   -217  -1179  -1395       N  
ATOM   4196  N   ASP D 151      34.209  84.119  41.442  1.00 63.10           N  
ANISOU 4196  N   ASP D 151     6796   7031  10147   -127  -1450  -1584       N  
ATOM   4197  CA  ASP D 151      34.550  85.212  40.536  1.00 67.40           C  
ANISOU 4197  CA  ASP D 151     7303   7533  10772   -213  -1383  -1540       C  
ATOM   4198  C   ASP D 151      36.020  85.608  40.665  1.00 67.92           C  
ANISOU 4198  C   ASP D 151     7273   7568  10965   -213  -1443  -1589       C  
ATOM   4199  O   ASP D 151      36.677  85.923  39.670  1.00 67.43           O  
ANISOU 4199  O   ASP D 151     7152   7487  10982   -295  -1364  -1539       O  
ATOM   4200  CB  ASP D 151      33.657  86.422  40.800  1.00 67.70           C  
ANISOU 4200  CB  ASP D 151     7405   7550  10767   -210  -1409  -1546       C  
ATOM   4201  CG  ASP D 151      32.207  86.165  40.441  1.00 64.77           C  
ANISOU 4201  CG  ASP D 151     7125   7204  10282   -230  -1327  -1485       C  
ATOM   4202  OD1 ASP D 151      31.902  85.080  39.910  1.00 65.11           O  
ANISOU 4202  OD1 ASP D 151     7180   7276  10285   -252  -1245  -1432       O  
ATOM   4203  OD2 ASP D 151      31.370  87.063  40.685  1.00 59.64           O  
ANISOU 4203  OD2 ASP D 151     6532   6542   9588   -220  -1347  -1493       O  
ATOM   4204  N   ALA D 152      36.520  85.598  41.898  1.00 65.22           N  
ANISOU 4204  N   ALA D 152     6920   7225  10635   -118  -1583  -1687       N  
ATOM   4205  CA  ALA D 152      37.926  85.889  42.166  1.00 66.62           C  
ANISOU 4205  CA  ALA D 152     7009   7371  10934   -103  -1654  -1745       C  
ATOM   4206  C   ALA D 152      38.865  84.883  41.500  1.00 69.46           C  
ANISOU 4206  C   ALA D 152     7291   7743  11356   -137  -1592  -1720       C  
ATOM   4207  O   ALA D 152      39.981  85.224  41.114  1.00 76.26           O  
ANISOU 4207  O   ALA D 152     8070   8577  12330   -175  -1585  -1730       O  
ATOM   4208  CB  ALA D 152      38.176  85.918  43.668  1.00 67.09           C  
ANISOU 4208  CB  ALA D 152     7086   7436  10970     18  -1817  -1855       C  
ATOM   4209  N   GLN D 153      38.398  83.648  41.366  1.00 64.33           N  
ANISOU 4209  N   GLN D 153     6670   7137  10636   -122  -1548  -1690       N  
ATOM   4210  CA  GLN D 153      39.202  82.582  40.785  1.00 62.58           C  
ANISOU 4210  CA  GLN D 153     6379   6931  10467   -142  -1493  -1672       C  
ATOM   4211  C   GLN D 153      38.860  82.325  39.316  1.00 67.00           C  
ANISOU 4211  C   GLN D 153     6931   7507  11019   -243  -1324  -1571       C  
ATOM   4212  O   GLN D 153      39.113  81.244  38.792  1.00 63.11           O  
ANISOU 4212  O   GLN D 153     6407   7041  10533   -251  -1262  -1546       O  
ATOM   4213  CB  GLN D 153      39.025  81.299  41.597  1.00 55.65           C  
ANISOU 4213  CB  GLN D 153     5529   6090   9526    -52  -1567  -1707       C  
ATOM   4214  CG  GLN D 153      39.453  81.448  43.050  1.00 55.68           C  
ANISOU 4214  CG  GLN D 153     5545   6090   9521     56  -1738  -1806       C  
ATOM   4215  CD  GLN D 153      39.189  80.205  43.874  1.00 61.76           C  
ANISOU 4215  CD  GLN D 153     6358   6904  10204    146  -1819  -1826       C  
ATOM   4216  OE1 GLN D 153      39.685  80.071  44.992  1.00 60.26           O  
ANISOU 4216  OE1 GLN D 153     6175   6721  10000    238  -1956  -1900       O  
ATOM   4217  NE2 GLN D 153      38.401  79.289  43.324  1.00 70.54           N  
ANISOU 4217  NE2 GLN D 153     7501   8045  11254    120  -1738  -1758       N  
ATOM   4218  N   ALA D 154      38.287  83.327  38.661  1.00 83.38           N  
ANISOU 4218  N   ALA D 154     9038   9566  13076   -314  -1254  -1513       N  
ATOM   4219  CA  ALA D 154      38.009  83.249  37.225  1.00 89.31           C  
ANISOU 4219  CA  ALA D 154     9789  10336  13810   -412  -1097  -1414       C  
ATOM   4220  C   ALA D 154      39.270  83.438  36.376  1.00 89.83           C  
ANISOU 4220  C   ALA D 154     9759  10400  13974   -477  -1043  -1402       C  
ATOM   4221  O   ALA D 154      40.190  84.158  36.770  1.00 91.24           O  
ANISOU 4221  O   ALA D 154     9880  10545  14241   -472  -1118  -1454       O  
ATOM   4222  CB  ALA D 154      36.957  84.282  36.848  1.00 90.29           C  
ANISOU 4222  CB  ALA D 154     9989  10445  13873   -461  -1052  -1356       C  
ATOM   4223  N   PRO D 155      39.314  82.765  35.215  1.00 79.02           N  
ANISOU 4223  N   PRO D 155     8371   9069  12585   -534   -916  -1337       N  
ATOM   4224  CA  PRO D 155      40.387  82.948  34.233  1.00 79.75           C  
ANISOU 4224  CA  PRO D 155     8378   9175  12747   -608   -846  -1314       C  
ATOM   4225  C   PRO D 155      40.545  84.402  33.786  1.00 86.35           C  
ANISOU 4225  C   PRO D 155     9212   9985  13614   -686   -837  -1276       C  
ATOM   4226  O   PRO D 155      41.674  84.902  33.821  1.00 91.75           O  
ANISOU 4226  O   PRO D 155     9814  10649  14396   -707   -875  -1311       O  
ATOM   4227  CB  PRO D 155      39.942  82.063  33.072  1.00 72.51           C  
ANISOU 4227  CB  PRO D 155     7480   8312  11761   -650   -709  -1240       C  
ATOM   4228  CG  PRO D 155      39.134  80.995  33.705  1.00 62.20           C  
ANISOU 4228  CG  PRO D 155     6225   7013  10394   -572   -734  -1258       C  
ATOM   4229  CD  PRO D 155      38.419  81.648  34.856  1.00 66.19           C  
ANISOU 4229  CD  PRO D 155     6796   7480  10872   -521   -841  -1292       C  
TER    4230      PRO D 155                                                      
HETATM 4231  C1  NAG E   1      26.613  32.047  26.958  1.00121.41           C  
ANISOU 4231  C1  NAG E   1    11989  13762  20380    329   -130  -3130       C  
HETATM 4232  C2  NAG E   1      26.125  32.134  28.414  1.00114.85           C  
ANISOU 4232  C2  NAG E   1    11226  12932  19481    446   -410  -2964       C  
HETATM 4233  C3  NAG E   1      24.593  32.089  28.492  1.00105.26           C  
ANISOU 4233  C3  NAG E   1    10171  11805  18018    455   -400  -2816       C  
HETATM 4234  C4  NAG E   1      23.949  33.122  27.575  1.00100.43           C  
ANISOU 4234  C4  NAG E   1     9634  11331  17194    333   -155  -2830       C  
HETATM 4235  C5  NAG E   1      24.503  32.919  26.162  1.00108.32           C  
ANISOU 4235  C5  NAG E   1    10575  12315  18268    225    101  -2993       C  
HETATM 4236  C6  NAG E   1      23.979  33.898  25.137  1.00111.89           C  
ANISOU 4236  C6  NAG E   1    11117  12887  18508     91    351  -3018       C  
HETATM 4237  C7  NAG E   1      27.005  31.186  30.510  1.00117.15           C  
ANISOU 4237  C7  NAG E   1    11459  13039  20014    652   -908  -2871       C  
HETATM 4238  C8  NAG E   1      27.596  29.967  31.161  1.00113.67           C  
ANISOU 4238  C8  NAG E   1    10963  12450  19777    755  -1126  -2872       C  
HETATM 4239  N2  NAG E   1      26.704  31.066  29.211  1.00118.09           N  
ANISOU 4239  N2  NAG E   1    11571  13206  20092    557   -641  -2954       N  
HETATM 4240  O3  NAG E   1      24.185  32.301  29.838  1.00102.89           O  
ANISOU 4240  O3  NAG E   1     9943  11508  17644    550   -650  -2664       O  
HETATM 4241  O4  NAG E   1      22.522  32.994  27.581  1.00 97.19           O  
ANISOU 4241  O4  NAG E   1     9363  10993  16573    341   -139  -2708       O  
HETATM 4242  O5  NAG E   1      25.935  33.049  26.158  1.00115.05           O  
ANISOU 4242  O5  NAG E   1    11281  13087  19346    216     91  -3123       O  
HETATM 4243  O6  NAG E   1      23.134  34.889  25.705  1.00120.92           O  
ANISOU 4243  O6  NAG E   1    12362  14139  19441     93    302  -2894       O  
HETATM 4244  O7  NAG E   1      26.804  32.224  31.135  1.00116.56           O  
ANISOU 4244  O7  NAG E   1    11442  13036  19810    652   -976  -2796       O  
HETATM 4245  C1  NAG E   2      21.745  33.815  28.537  1.00108.27           C  
ANISOU 4245  C1  NAG E   2    10856  12479  17802    377   -270  -2560       C  
HETATM 4246  C2  NAG E   2      20.306  34.001  28.062  1.00109.99           C  
ANISOU 4246  C2  NAG E   2    11205  12800  17785    331   -144  -2483       C  
HETATM 4247  C3  NAG E   2      19.575  34.950  28.992  1.00110.01           C  
ANISOU 4247  C3  NAG E   2    11354  12893  17552    327   -267  -2315       C  
HETATM 4248  C4  NAG E   2      19.581  34.407  30.419  1.00114.09           C  
ANISOU 4248  C4  NAG E   2    11908  13328  18114    452   -561  -2188       C  
HETATM 4249  C5  NAG E   2      20.991  33.978  30.874  1.00116.13           C  
ANISOU 4249  C5  NAG E   2    11965  13466  18693    542   -706  -2296       C  
HETATM 4250  C6  NAG E   2      20.947  33.091  32.101  1.00114.66           C  
ANISOU 4250  C6  NAG E   2    11827  13168  18570    675   -989  -2182       C  
HETATM 4251  C7  NAG E   2      19.160  34.178  25.907  1.00109.84           C  
ANISOU 4251  C7  NAG E   2    11321  12899  17514    150    281  -2565       C  
HETATM 4252  C8  NAG E   2      19.219  34.706  24.504  1.00109.15           C  
ANISOU 4252  C8  NAG E   2    11272  12874  17327      7    552  -2672       C  
HETATM 4253  N2  NAG E   2      20.222  34.438  26.680  1.00111.43           N  
ANISOU 4253  N2  NAG E   2    11410  13051  17876    199    137  -2585       N  
HETATM 4254  O3  NAG E   2      18.242  35.134  28.544  1.00104.06           O  
ANISOU 4254  O3  NAG E   2    10807  12227  16505    250   -157  -2210       O  
HETATM 4255  O4  NAG E   2      19.160  35.413  31.347  1.00115.94           O  
ANISOU 4255  O4  NAG E   2    12270  13638  18143    440   -677  -2051       O  
HETATM 4256  O5  NAG E   2      21.733  33.243  29.873  1.00116.90           O  
ANISOU 4256  O5  NAG E   2    11964  13492  18960    508   -559  -2447       O  
HETATM 4257  O6  NAG E   2      22.061  33.296  32.956  1.00115.78           O  
ANISOU 4257  O6  NAG E   2    11907  13242  18842    723  -1178  -2198       O  
HETATM 4258  O7  NAG E   2      18.191  33.549  26.322  1.00111.80           O  
ANISOU 4258  O7  NAG E   2    11711  13133  17634    190    180  -2430       O  
HETATM 4259  C1  MAN E   3      17.752  35.795  31.559  1.00106.98           C  
ANISOU 4259  C1  MAN E   3    11375  12593  16680    389   -655  -1882       C  
HETATM 4260  C2  MAN E   3      17.324  35.436  33.058  1.00 90.79           C  
ANISOU 4260  C2  MAN E   3     9461  10488  14546    483   -916  -1706       C  
HETATM 4261  C3  MAN E   3      15.784  35.486  33.252  1.00 98.69           C  
ANISOU 4261  C3  MAN E   3    10700  11554  15243    441   -882  -1537       C  
HETATM 4262  C4  MAN E   3      15.079  36.287  32.124  1.00 81.72           C  
ANISOU 4262  C4  MAN E   3     8602   9531  12915    316   -640  -1567       C  
HETATM 4263  C5  MAN E   3      15.485  35.829  30.699  1.00 94.83           C  
ANISOU 4263  C5  MAN E   3    10134  11178  14718    269   -442  -1732       C  
HETATM 4264  C6  MAN E   3      15.496  37.004  29.775  1.00 89.30           C  
ANISOU 4264  C6  MAN E   3     9426  10589  13915    157   -249  -1805       C  
HETATM 4265  O2  MAN E   3      17.865  36.351  34.015  1.00 92.37           O  
ANISOU 4265  O2  MAN E   3     9651  10709  14738    507  -1068  -1674       O  
HETATM 4266  O3  MAN E   3      15.454  36.050  34.548  1.00 98.56           O  
ANISOU 4266  O3  MAN E   3    10819  11557  15073    471  -1054  -1392       O  
HETATM 4267  O4  MAN E   3      13.653  36.207  32.229  1.00 80.72           O  
ANISOU 4267  O4  MAN E   3     8671   9452  12546    283   -609  -1428       O  
HETATM 4268  O5  MAN E   3      16.815  35.215  30.651  1.00 99.70           O  
ANISOU 4268  O5  MAN E   3    10544  11691  15646    337   -493  -1871       O  
HETATM 4269  O6  MAN E   3      15.537  36.527  28.454  1.00 90.96           O  
ANISOU 4269  O6  MAN E   3     9584  10791  14184    102    -54  -1927       O  
HETATM 4270  C1  MAN E   4      14.503  37.194  27.710  1.00 87.89           C  
ANISOU 4270  C1  MAN E   4     9343  10507  13545      0     96  -1884       C  
HETATM 4271  C2  MAN E   4      14.480  36.544  26.330  1.00 88.62           C  
ANISOU 4271  C2  MAN E   4     9405  10578  13687    -55    288  -2007       C  
HETATM 4272  C3  MAN E   4      15.827  36.816  25.646  1.00 85.26           C  
ANISOU 4272  C3  MAN E   4     8798  10131  13466    -86    412  -2195       C  
HETATM 4273  C4  MAN E   4      16.167  38.326  25.608  1.00 85.55           C  
ANISOU 4273  C4  MAN E   4     8837  10258  13412   -161    474  -2208       C  
HETATM 4274  C5  MAN E   4      16.017  38.981  26.999  1.00 86.61           C  
ANISOU 4274  C5  MAN E   4     9017  10421  13472   -106    268  -2069       C  
HETATM 4275  C6  MAN E   4      16.038  40.501  26.946  1.00 81.01           C  
ANISOU 4275  C6  MAN E   4     8355   9808  12616   -188    330  -2055       C  
HETATM 4276  O2  MAN E   4      13.501  37.152  25.497  1.00 94.29           O  
ANISOU 4276  O2  MAN E   4    10270  11389  14166   -155    428  -1976       O  
HETATM 4277  O3  MAN E   4      15.878  36.272  24.331  1.00 80.98           O  
ANISOU 4277  O3  MAN E   4     8234   9568  12965   -144    609  -2323       O  
HETATM 4278  O4  MAN E   4      17.508  38.489  25.175  1.00 88.74           O  
ANISOU 4278  O4  MAN E   4     9049  10624  14044   -178    568  -2381       O  
HETATM 4279  O5  MAN E   4      14.758  38.586  27.627  1.00 88.48           O  
ANISOU 4279  O5  MAN E   4     9422  10668  13527    -68    155  -1899       O  
HETATM 4280  O6  MAN E   4      14.791  40.975  27.452  1.00 76.54           O  
ANISOU 4280  O6  MAN E   4     7981   9312  11790   -196    261  -1888       O  
HETATM 4281  C1  NAG E   5      12.240  36.455  25.513  1.00 93.54           C  
ANISOU 4281  C1  NAG E   5    10314  11291  13937   -146    395  -1870       C  
HETATM 4282  C2  NAG E   5      11.157  37.531  25.226  1.00105.74           C  
ANISOU 4282  C2  NAG E   5    12023  12949  15205   -229    454  -1782       C  
HETATM 4283  C3  NAG E   5       9.853  36.963  24.611  1.00 91.63           C  
ANISOU 4283  C3  NAG E   5    10370  11174  13273   -264    503  -1731       C  
HETATM 4284  C4  NAG E   5       9.979  35.605  23.921  1.00 99.08           C  
ANISOU 4284  C4  NAG E   5    11263  12030  14354   -248    558  -1822       C  
HETATM 4285  C5  NAG E   5      11.048  34.763  24.585  1.00 95.05           C  
ANISOU 4285  C5  NAG E   5    10600  11417  14098   -153    463  -1871       C  
HETATM 4286  C6  NAG E   5      11.336  33.452  23.886  1.00 89.34           C  
ANISOU 4286  C6  NAG E   5     9808  10598  13539   -132    525  -1980       C  
HETATM 4287  C7  NAG E   5      11.599  39.236  26.958  1.00110.87           C  
ANISOU 4287  C7  NAG E   5    12674  13670  15781   -193    272  -1658       C  
HETATM 4288  C8  NAG E   5      11.121  39.821  28.254  1.00108.92           C  
ANISOU 4288  C8  NAG E   5    12513  13456  15417   -152    117  -1510       C  
HETATM 4289  N2  NAG E   5      10.854  38.244  26.458  1.00107.13           N  
ANISOU 4289  N2  NAG E   5    12255  13164  15285   -192    309  -1647       N  
HETATM 4290  O3  NAG E   5       9.340  37.910  23.678  1.00 84.66           O  
ANISOU 4290  O3  NAG E   5     9585  10376  12205   -364    631  -1748       O  
HETATM 4291  O4  NAG E   5       8.725  34.931  24.004  1.00110.45           O  
ANISOU 4291  O4  NAG E   5    12817  13460  15689   -242    512  -1724       O  
HETATM 4292  O5  NAG E   5      12.245  35.528  24.543  1.00 95.05           O  
ANISOU 4292  O5  NAG E   5    10478  11431  14205   -164    504  -1968       O  
HETATM 4293  O6  NAG E   5      11.382  33.606  22.475  1.00 85.31           O  
ANISOU 4293  O6  NAG E   5     9312  10116  12985   -225    724  -2107       O  
HETATM 4294  O7  NAG E   5      12.598  39.650  26.386  1.00114.86           O  
ANISOU 4294  O7  NAG E   5    13071  14176  16395   -230    368  -1785       O  
HETATM 4295  C1  GAL E   6       8.283  34.437  22.716  1.00117.12           C  
ANISOU 4295  C1  GAL E   6    13709  14299  16493   -306    645  -1807       C  
HETATM 4296  C2  GAL E   6       6.738  34.150  22.790  1.00128.61           C  
ANISOU 4296  C2  GAL E   6    15306  15776  17784   -322    597  -1687       C  
HETATM 4297  C3  GAL E   6       6.158  33.804  21.418  1.00125.28           C  
ANISOU 4297  C3  GAL E   6    14955  15359  17287   -398    721  -1767       C  
HETATM 4298  C4  GAL E   6       6.561  34.879  20.415  1.00128.56           C  
ANISOU 4298  C4  GAL E   6    15399  15844  17603   -484    858  -1858       C  
HETATM 4299  C5  GAL E   6       8.070  34.951  20.366  1.00125.64           C  
ANISOU 4299  C5  GAL E   6    14887  15439  17411   -467    922  -1978       C  
HETATM 4300  C6  GAL E   6       8.603  35.964  19.363  1.00122.26           C  
ANISOU 4300  C6  GAL E   6    14483  15066  16904   -560   1081  -2081       C  
HETATM 4301  O2  GAL E   6       6.433  33.059  23.659  1.00128.24           O  
ANISOU 4301  O2  GAL E   6    15247  15649  17830   -245    477  -1609       O  
HETATM 4302  O3  GAL E   6       4.731  33.762  21.451  1.00116.77           O  
ANISOU 4302  O3  GAL E   6    14000  14313  16055   -421    675  -1662       O  
HETATM 4303  O4  GAL E   6       6.079  36.125  20.848  1.00129.29           O  
ANISOU 4303  O4  GAL E   6    15566  16026  17533   -507    817  -1758       O  
HETATM 4304  O5  GAL E   6       8.593  35.353  21.645  1.00121.59           O  
ANISOU 4304  O5  GAL E   6    14295  14929  16974   -397    799  -1904       O  
HETATM 4305  O6  GAL E   6       9.986  35.769  19.155  1.00121.05           O  
ANISOU 4305  O6  GAL E   6    14181  14862  16950   -551   1167  -2221       O  
HETATM 4306  C1  MAN E   7      14.234  35.506  35.118  1.00102.18           C  
ANISOU 4306  C1  MAN E   7    11479  12003  15344    484  -1101  -1230       C  
HETATM 4307  C2  MAN E   7      13.630  36.571  36.074  1.00100.61           C  
ANISOU 4307  C2  MAN E   7    11441  11882  14906    460  -1170  -1097       C  
HETATM 4308  C3  MAN E   7      14.592  36.818  37.226  1.00 97.75           C  
ANISOU 4308  C3  MAN E   7    11046  11459  14635    539  -1397  -1085       C  
HETATM 4309  C4  MAN E   7      14.961  35.498  37.929  1.00102.34           C  
ANISOU 4309  C4  MAN E   7    11631  11888  15365    649  -1588  -1049       C  
HETATM 4310  C5  MAN E   7      15.441  34.436  36.914  1.00107.29           C  
ANISOU 4310  C5  MAN E   7    12095  12442  16228    671  -1504  -1176       C  
HETATM 4311  C6  MAN E   7      15.582  33.063  37.544  1.00111.70           C  
ANISOU 4311  C6  MAN E   7    12686  12847  16909    774  -1676  -1124       C  
HETATM 4312  O2  MAN E   7      12.417  36.104  36.681  1.00102.41           O  
ANISOU 4312  O2  MAN E   7    11867  12098  14948    465  -1202   -941       O  
HETATM 4313  O3  MAN E   7      14.055  37.739  38.171  1.00 90.43           O  
ANISOU 4313  O3  MAN E   7    10279  10593  13486    522  -1468   -964       O  
HETATM 4314  O4  MAN E   7      15.996  35.734  38.876  1.00103.86           O  
ANISOU 4314  O4  MAN E   7    11771  12019  15674    726  -1809  -1061       O  
HETATM 4315  O5  MAN E   7      14.498  34.316  35.821  1.00107.24           O  
ANISOU 4315  O5  MAN E   7    12127  12507  16113    584  -1273  -1188       O  
HETATM 4316  O6  MAN E   7      16.436  32.280  36.718  1.00113.11           O  
ANISOU 4316  O6  MAN E   7    12662  12947  17366    811  -1635  -1278       O  
HETATM 4317  C1  FUC E   8      23.884  36.118  25.822  1.00133.71           C  
ANISOU 4317  C1  FUC E   8    13942  15797  21066     42    332  -2938       C  
HETATM 4318  C2  FUC E   8      23.130  37.275  25.079  1.00125.15           C  
ANISOU 4318  C2  FUC E   8    12983  14847  19720    -79    532  -2915       C  
HETATM 4319  C3  FUC E   8      23.713  38.691  25.391  1.00134.36           C  
ANISOU 4319  C3  FUC E   8    14131  16064  20854   -124    538  -2926       C  
HETATM 4320  C4  FUC E   8      24.786  38.658  26.501  1.00139.92           C  
ANISOU 4320  C4  FUC E   8    14704  16684  21776    -26    321  -2942       C  
HETATM 4321  C5  FUC E   8      24.319  37.734  27.637  1.00139.91           C  
ANISOU 4321  C5  FUC E   8    14703  16635  21819    110     60  -2825       C  
HETATM 4322  C6  FUC E   8      25.319  37.636  28.783  1.00138.70           C  
ANISOU 4322  C6  FUC E   8    14448  16390  21862    210   -182  -2828       C  
HETATM 4323  O2  FUC E   8      21.716  37.236  25.287  1.00120.49           O  
ANISOU 4323  O2  FUC E   8    12519  14340  18923    -63    502  -2781       O  
HETATM 4324  O3  FUC E   8      24.288  39.285  24.223  1.00132.32           O  
ANISOU 4324  O3  FUC E   8    13880  15816  20582   -252    779  -3049       O  
HETATM 4325  O4  FUC E   8      26.057  38.248  25.985  1.00144.94           O  
ANISOU 4325  O4  FUC E   8    15211  17213  22647    -44    392  -3100       O  
HETATM 4326  O5  FUC E   8      24.087  36.379  27.206  1.00140.88           O  
ANISOU 4326  O5  FUC E   8    14817  16687  22024    144     79  -2849       O  
HETATM 4327  C1  NAG F   1      16.286  33.095  50.310  1.00 85.76           C  
ANISOU 4327  C1  NAG F   1    10216   8409  13960    481  -1379    830       C  
HETATM 4328  C2  NAG F   1      16.694  33.168  48.837  1.00 83.19           C  
ANISOU 4328  C2  NAG F   1     9872   8053  13684    475  -1406    548       C  
HETATM 4329  C3  NAG F   1      17.253  34.554  48.508  1.00 74.54           C  
ANISOU 4329  C3  NAG F   1     8832   7091  12399    528  -1355    415       C  
HETATM 4330  C4  NAG F   1      16.310  35.670  48.975  1.00 71.28           C  
ANISOU 4330  C4  NAG F   1     8460   6785  11839    519  -1279    546       C  
HETATM 4331  C5  NAG F   1      15.959  35.433  50.445  1.00 77.91           C  
ANISOU 4331  C5  NAG F   1     9311   7651  12642    529  -1265    820       C  
HETATM 4332  C6  NAG F   1      14.961  36.402  51.042  1.00 82.68           C  
ANISOU 4332  C6  NAG F   1     9943   8375  13096    523  -1192    979       C  
HETATM 4333  C7  NAG F   1      17.380  30.977  47.987  1.00 88.71           C  
ANISOU 4333  C7  NAG F   1    10466   8530  14708    451  -1549    393       C  
HETATM 4334  C8  NAG F   1      18.535  30.045  47.749  1.00 84.91           C  
ANISOU 4334  C8  NAG F   1     9953   7972  14338    490  -1629    275       C  
HETATM 4335  N2  NAG F   1      17.685  32.157  48.531  1.00 87.74           N  
ANISOU 4335  N2  NAG F   1    10412   8536  14390    498  -1484    435       N  
HETATM 4336  O3  NAG F   1      17.465  34.635  47.094  1.00 73.76           O  
ANISOU 4336  O3  NAG F   1     8709   6984  12332    514  -1367    167       O  
HETATM 4337  O4  NAG F   1      16.933  36.955  48.813  1.00 62.39           O  
ANISOU 4337  O4  NAG F   1     7383   5781  10540    577  -1239    434       O  
HETATM 4338  O5  NAG F   1      15.382  34.134  50.598  1.00 84.70           O  
ANISOU 4338  O5  NAG F   1    10114   8387  13683    468  -1304    931       O  
HETATM 4339  O6  NAG F   1      14.583  37.469  50.194  1.00 89.66           O  
ANISOU 4339  O6  NAG F   1    10848   9321  13897    514  -1151    849       O  
HETATM 4340  O7  NAG F   1      16.225  30.672  47.691  1.00 91.91           O  
ANISOU 4340  O7  NAG F   1    10834   8888  15201    382  -1547    446       O  
HETATM 4341  C1  NAG F   2      16.796  37.512  47.470  1.00 55.91           C  
ANISOU 4341  C1  NAG F   2     6557   4981   9704    554  -1219    222       C  
HETATM 4342  C2  NAG F   2      16.911  39.044  47.486  1.00 56.77           C  
ANISOU 4342  C2  NAG F   2     6718   5241   9611    592  -1153    178       C  
HETATM 4343  C3  NAG F   2      16.745  39.592  46.067  1.00 49.65           C  
ANISOU 4343  C3  NAG F   2     5810   4388   8669    557  -1117    -37       C  
HETATM 4344  C4  NAG F   2      17.714  38.917  45.098  1.00 56.39           C  
ANISOU 4344  C4  NAG F   2     6622   5173   9629    574  -1170   -243       C  
HETATM 4345  C5  NAG F   2      17.657  37.396  45.238  1.00 62.49           C  
ANISOU 4345  C5  NAG F   2     7345   5810  10586    546  -1241   -190       C  
HETATM 4346  C6  NAG F   2      18.750  36.681  44.466  1.00 61.51           C  
ANISOU 4346  C6  NAG F   2     7179   5660  10531    567  -1292   -377       C  
HETATM 4347  C7  NAG F   2      16.271  40.563  49.292  1.00 68.43           C  
ANISOU 4347  C7  NAG F   2     8271   6972  10758    616  -1048    443       C  
HETATM 4348  C8  NAG F   2      15.147  41.078  50.142  1.00 64.63           C  
ANISOU 4348  C8  NAG F   2     7809   6602  10144    594   -985    636       C  
HETATM 4349  N2  NAG F   2      15.939  39.642  48.384  1.00 65.38           N  
ANISOU 4349  N2  NAG F   2     7839   6441  10563    568  -1089    372       N  
HETATM 4350  O3  NAG F   2      16.989  40.998  46.098  1.00 53.43           O  
ANISOU 4350  O3  NAG F   2     6335   5047   8920    573  -1041    -84       O  
HETATM 4351  O4  NAG F   2      17.368  39.201  43.734  1.00 59.35           O  
ANISOU 4351  O4  NAG F   2     6977   5581   9992    540  -1146   -423       O  
HETATM 4352  O5  NAG F   2      17.796  36.976  46.603  1.00 58.88           O  
ANISOU 4352  O5  NAG F   2     6904   5318  10151    569  -1263     16       O  
HETATM 4353  O6  NAG F   2      18.754  35.285  44.741  1.00 62.66           O  
ANISOU 4353  O6  NAG F   2     7279   5676  10851    550  -1365   -315       O  
HETATM 4354  O7  NAG F   2      17.424  40.963  49.427  1.00 70.16           O  
ANISOU 4354  O7  NAG F   2     8508   7234  10914    678  -1063    352       O  
HETATM 4355  C1  MAN F   3      17.337  40.544  43.138  1.00 57.77           C  
ANISOU 4355  C1  MAN F   3     6808   5525   9616    543  -1070   -524       C  
HETATM 4356  C2  MAN F   3      18.273  40.486  41.851  1.00 66.55           C  
ANISOU 4356  C2  MAN F   3     7883   6680  10722    561  -1077   -763       C  
HETATM 4357  C3  MAN F   3      18.562  41.902  41.287  1.00 65.49           C  
ANISOU 4357  C3  MAN F   3     7777   6694  10412    576  -1002   -869       C  
HETATM 4358  C4  MAN F   3      17.555  42.904  41.835  1.00 59.89           C  
ANISOU 4358  C4  MAN F   3     7119   6090   9546    532   -928   -725       C  
HETATM 4359  C5  MAN F   3      17.655  43.004  43.357  1.00 62.52           C  
ANISOU 4359  C5  MAN F   3     7491   6423   9843    555   -933   -534       C  
HETATM 4360  C6  MAN F   3      16.466  43.755  43.867  1.00 61.82           C  
ANISOU 4360  C6  MAN F   3     7439   6422   9627    513   -870   -392       C  
HETATM 4361  O2  MAN F   3      17.721  39.689  40.746  1.00 77.08           O  
ANISOU 4361  O2  MAN F   3     9163   7976  12149    518  -1104   -868       O  
HETATM 4362  O3  MAN F   3      18.546  41.979  39.839  1.00 72.72           O  
ANISOU 4362  O3  MAN F   3     8655   7684  11291    553   -979  -1043       O  
HETATM 4363  O4  MAN F   3      17.804  44.178  41.261  1.00 61.11           O  
ANISOU 4363  O4  MAN F   3     7295   6396   9528    530   -855   -811       O  
HETATM 4364  O5  MAN F   3      17.708  41.656  43.996  1.00 61.47           O  
ANISOU 4364  O5  MAN F   3     7330   6129   9896    569  -1014   -441       O  
HETATM 4365  O6  MAN F   3      16.439  43.775  45.283  1.00 64.94           O  
ANISOU 4365  O6  MAN F   3     7863   6827   9983    539   -876   -211       O  
HETATM 4366  C1  MAN F   4      15.611  44.911  45.635  1.00 74.37           C  
ANISOU 4366  C1  MAN F   4     9098   8157  11000    518   -802   -131       C  
HETATM 4367  C2  MAN F   4      15.549  45.046  47.187  1.00 88.37           C  
ANISOU 4367  C2  MAN F   4    10901   9974  12701    557   -803     60       C  
HETATM 4368  C3  MAN F   4      14.717  43.927  47.803  1.00 86.17           C  
ANISOU 4368  C3  MAN F   4    10596   9598  12546    532   -833    235       C  
HETATM 4369  C4  MAN F   4      13.342  43.810  47.121  1.00 85.17           C  
ANISOU 4369  C4  MAN F   4    10448   9459  12454    455   -800    253       C  
HETATM 4370  C5  MAN F   4      13.514  43.668  45.601  1.00 86.71           C  
ANISOU 4370  C5  MAN F   4    10617   9603  12726    424   -812     44       C  
HETATM 4371  C6  MAN F   4      12.208  43.681  44.841  1.00 86.05           C  
ANISOU 4371  C6  MAN F   4    10512   9524  12657    354   -781     37       C  
HETATM 4372  O2  MAN F   4      14.865  46.240  47.551  1.00 86.09           O  
ANISOU 4372  O2  MAN F   4    10651   9829  12230    551   -735    115       O  
HETATM 4373  O3  MAN F   4      14.550  44.117  49.211  1.00 84.75           O  
ANISOU 4373  O3  MAN F   4    10440   9488  12274    571   -823    422       O  
HETATM 4374  O4  MAN F   4      12.662  42.668  47.612  1.00 77.40           O  
ANISOU 4374  O4  MAN F   4     9426   8363  11618    426   -837    411       O  
HETATM 4375  O5  MAN F   4      14.304  44.769  45.085  1.00 79.99           O  
ANISOU 4375  O5  MAN F   4     9795   8860  11737    453   -775   -103       O  
HETATM 4376  O6  MAN F   4      12.406  44.466  43.665  1.00 83.55           O  
ANISOU 4376  O6  MAN F   4    10205   9283  12258    347   -747   -147       O  
HETATM 4377  C1  NAG F   5      15.772  47.346  47.513  1.00 81.83           C  
ANISOU 4377  C1  NAG F   5    10141   9384  11566    590   -716      9       C  
HETATM 4378  C2  NAG F   5      14.966  48.624  47.234  1.00 80.23           C  
ANISOU 4378  C2  NAG F   5     9969   9307  11207    563   -644     -5       C  
HETATM 4379  C3  NAG F   5      15.840  49.871  47.381  1.00 73.16           C  
ANISOU 4379  C3  NAG F   5     9104   8509  10184    604   -627    -88       C  
HETATM 4380  C4  NAG F   5      16.656  49.840  48.667  1.00 71.56           C  
ANISOU 4380  C4  NAG F   5     8916   8324   9950    677   -669    -21       C  
HETATM 4381  C5  NAG F   5      17.392  48.515  48.768  1.00 73.03           C  
ANISOU 4381  C5  NAG F   5     9069   8387  10293    696   -734    -14       C  
HETATM 4382  C6  NAG F   5      18.175  48.361  50.048  1.00 67.54           C  
ANISOU 4382  C6  NAG F   5     8382   7705   9573    772   -781     64       C  
HETATM 4383  C7  NAG F   5      13.136  48.180  45.647  1.00 73.89           C  
ANISOU 4383  C7  NAG F   5     9130   8460  10484    451   -602    -37       C  
HETATM 4384  C8  NAG F   5      12.728  48.193  44.206  1.00 70.18           C  
ANISOU 4384  C8  NAG F   5     8638   7978  10051    400   -584   -167       C  
HETATM 4385  N2  NAG F   5      14.389  48.572  45.900  1.00 77.68           N  
ANISOU 4385  N2  NAG F   5     9625   8961  10928    502   -619   -103       N  
HETATM 4386  O3  NAG F   5      15.003  51.026  47.371  1.00 70.81           O  
ANISOU 4386  O3  NAG F   5     8837   8321   9746    588   -569    -70       O  
HETATM 4387  O4  NAG F   5      17.607  50.901  48.665  1.00 67.39           O  
ANISOU 4387  O4  NAG F   5     8404   7864   9337    710   -665   -125       O  
HETATM 4388  O5  NAG F   5      16.430  47.456  48.753  1.00 80.04           O  
ANISOU 4388  O5  NAG F   5     9934   9192  11285    657   -742     93       O  
HETATM 4389  O6  NAG F   5      17.314  48.239  51.173  1.00 69.92           O  
ANISOU 4389  O6  NAG F   5     8699   8057   9810    791   -773    247       O  
HETATM 4390  O7  NAG F   5      12.369  47.833  46.539  1.00 70.55           O  
ANISOU 4390  O7  NAG F   5     8706   8035  10062    447   -601    123       O  
HETATM 4391  C1  MAN F   6      19.694  41.354  39.226  1.00 80.55           C  
ANISOU 4391  C1  MAN F   6     9595   8699  12311    580  -1012  -1170       C  
HETATM 4392  C2  MAN F   6      20.612  42.416  38.565  1.00 92.28           C  
ANISOU 4392  C2  MAN F   6    11079  10342  13642    603   -949  -1285       C  
HETATM 4393  C3  MAN F   6      21.265  41.824  37.313  1.00 87.64           C  
ANISOU 4393  C3  MAN F   6    10420   9810  13071    615   -967  -1444       C  
HETATM 4394  C4  MAN F   6      21.567  40.338  37.534  1.00 91.05           C  
ANISOU 4394  C4  MAN F   6    10809  10117  13670    630  -1059  -1446       C  
HETATM 4395  C5  MAN F   6      20.224  39.573  37.626  1.00 87.44           C  
ANISOU 4395  C5  MAN F   6    10349   9542  13334    589  -1098  -1379       C  
HETATM 4396  C6  MAN F   6      20.291  38.244  38.381  1.00 84.14           C  
ANISOU 4396  C6  MAN F   6     9910   8966  13096    592  -1187  -1301       C  
HETATM 4397  O2  MAN F   6      21.700  42.762  39.428  1.00 94.72           O  
ANISOU 4397  O2  MAN F   6    11408  10666  13917    644   -952  -1245       O  
HETATM 4398  O3  MAN F   6      22.455  42.524  36.934  1.00 79.73           O  
ANISOU 4398  O3  MAN F   6     9401   8929  11961    644   -928  -1524       O  
HETATM 4399  O4  MAN F   6      22.342  39.834  36.457  1.00 95.10           O  
ANISOU 4399  O4  MAN F   6    11252  10689  14192    657  -1081  -1598       O  
HETATM 4400  O5  MAN F   6      19.228  40.403  38.274  1.00 83.99           O  
ANISOU 4400  O5  MAN F   6     9973   9096  12841    557  -1051  -1255       O  
HETATM 4401  O6  MAN F   6      20.566  38.487  39.762  1.00 77.50           O  
ANISOU 4401  O6  MAN F   6     9121   8074  12250    606  -1186  -1148       O  
HETATM 4402  C1  FUC F   7      13.296  37.282  49.528  1.00 93.68           C  
ANISOU 4402  C1  FUC F   7    11323   9780  14492    430  -1133    865       C  
HETATM 4403  C2  FUC F   7      12.270  36.217  50.155  1.00 87.02           C  
ANISOU 4403  C2  FUC F   7    10427   8866  13771    359  -1138   1086       C  
HETATM 4404  C3  FUC F   7      10.836  36.471  49.567  1.00 80.15           C  
ANISOU 4404  C3  FUC F   7     9530   7996  12928    280  -1099   1113       C  
HETATM 4405  C4  FUC F   7      10.861  37.293  48.242  1.00105.77           C  
ANISOU 4405  C4  FUC F   7    12795  11276  16117    275  -1081    863       C  
HETATM 4406  C5  FUC F   7      11.632  38.624  48.455  1.00 95.68           C  
ANISOU 4406  C5  FUC F   7    11588  10188  14576    342  -1021    778       C  
HETATM 4407  C6  FUC F   7      12.411  39.090  47.251  1.00 92.28           C  
ANISOU 4407  C6  FUC F   7    11173   9774  14113    361  -1027    504       C  
HETATM 4408  O2  FUC F   7      12.179  36.104  51.569  1.00 86.12           O  
ANISOU 4408  O2  FUC F   7    10322   8825  13576    385  -1113   1327       O  
HETATM 4409  O3  FUC F   7      10.086  35.256  49.314  1.00 78.30           O  
ANISOU 4409  O3  FUC F   7     9221   7634  12895    197  -1137   1164       O  
HETATM 4410  O4  FUC F   7      11.459  36.519  47.183  1.00104.27           O  
ANISOU 4410  O4  FUC F   7    12572  10954  16092    268  -1154    654       O  
HETATM 4411  O5  FUC F   7      12.626  38.537  49.503  1.00 95.25           O  
ANISOU 4411  O5  FUC F   7    11559  10149  14483    418  -1046    868       O  
HETATM 4412  O   HOH A 601      -7.070  36.210  36.392  1.00 42.22           O  
HETATM 4413  O   HOH A 602      -3.267  28.045  18.635  1.00 59.74           O  
HETATM 4414  O   HOH A 603      11.494  40.667  24.377  1.00 54.74           O  
HETATM 4415  O   HOH A 604       0.582  71.763  31.876  1.00 51.87           O  
HETATM 4416  O   HOH A 605     -10.273  25.817  27.689  1.00 43.49           O  
HETATM 4417  O   HOH A 606       5.660  58.867  22.695  1.00 40.61           O  
HETATM 4418  O   HOH A 607       2.198  34.109  21.309  1.00 33.74           O  
HETATM 4419  O   HOH A 608       6.293  67.544  23.258  1.00 20.95           O  
HETATM 4420  O   HOH A 609     -12.122  54.465  35.501  1.00 37.79           O  
HETATM 4421  O   HOH A 610      -6.195  40.217  28.833  1.00 33.90           O  
HETATM 4422  O   HOH A 611       1.450  49.151  23.676  1.00 42.91           O  
HETATM 4423  O   HOH A 612      -6.297  50.926  38.431  1.00 31.12           O  
HETATM 4424  O   HOH A 613       5.571  48.779  36.288  1.00 37.63           O  
HETATM 4425  O   HOH A 614       7.761  50.254  26.895  1.00 38.67           O  
HETATM 4426  O   HOH A 615      -3.360  29.665  31.881  1.00 43.65           O  
HETATM 4427  O   HOH A 616       2.894  50.018  42.288  1.00 35.64           O  
HETATM 4428  O   HOH A 617      -8.848  41.039  40.722  1.00 33.54           O  
HETATM 4429  O   HOH A 618      -1.323  64.194  26.463  1.00 28.69           O  
HETATM 4430  O   HOH A 619       5.704  63.006  23.254  1.00 34.17           O  
HETATM 4431  O   HOH A 620       4.941  11.788  20.375  1.00 45.45           O  
HETATM 4432  O   HOH A 621       0.861  43.104  29.539  1.00 39.46           O  
HETATM 4433  O   HOH A 622      -8.964  57.806  12.835  1.00 50.78           O  
HETATM 4434  O   HOH A 623      -9.256  66.516  22.690  1.00 39.37           O  
HETATM 4435  O   HOH A 624     -13.608  50.079  28.820  1.00 50.40           O  
HETATM 4436  O   HOH A 625      -8.942  38.269  15.452  1.00 39.41           O  
HETATM 4437  O   HOH A 626      -9.035  51.147  39.679  1.00 48.91           O  
HETATM 4438  O   HOH A 627      -5.126  66.609  28.783  1.00 32.53           O  
HETATM 4439  O   HOH A 628       1.001  46.632  23.318  1.00 41.99           O  
HETATM 4440  O   HOH A 629       0.500  66.519  27.200  1.00 35.08           O  
HETATM 4441  O   HOH A 630      -7.163  66.559  16.227  1.00 49.59           O  
HETATM 4442  O   HOH A 631     -12.614  62.216  18.757  1.00 46.40           O  
HETATM 4443  O   HOH A 632       6.105  50.548  24.264  1.00 33.64           O  
HETATM 4444  O   HOH A 633      -7.360  43.157  40.743  1.00 39.70           O  
HETATM 4445  O   HOH A 634      -8.688  55.000  12.626  1.00 52.25           O  
HETATM 4446  O   HOH A 635       5.109  18.146  22.333  1.00 53.26           O  
HETATM 4447  O   HOH A 636       1.323  20.598  33.081  1.00 46.67           O  
HETATM 4448  O   HOH A 637       5.361  50.875  17.140  1.00 52.97           O  
HETATM 4449  O   HOH A 638       0.108  35.256  15.436  1.00 43.09           O  
HETATM 4450  O   HOH A 639       8.428  27.247  37.013  1.00 52.45           O  
HETATM 4451  O   HOH A 640     -13.800  53.011  28.963  1.00 33.63           O  
HETATM 4452  O   HOH A 641      -1.178  39.734  36.523  1.00 37.47           O  
HETATM 4453  O   HOH A 642     -20.965  37.741  24.982  1.00 39.16           O  
HETATM 4454  O   HOH A 643     -13.090  43.646  18.146  1.00 42.91           O  
HETATM 4455  O   HOH B 601      37.606  59.004  47.410  1.00 52.28           O  
HETATM 4456  O   HOH B 602      30.991  57.928  37.076  1.00 38.51           O  
HETATM 4457  O   HOH B 603      14.029  57.206  38.268  1.00 34.65           O  
HETATM 4458  O   HOH B 604       2.051  75.244  44.491  1.00 51.17           O  
HETATM 4459  O   HOH B 605       0.000  76.126  42.910  0.50 69.19           O  
HETATM 4460  O   HOH B 606      24.267  61.466  33.678  1.00 56.27           O  
HETATM 4461  O   HOH B 607      -8.908  76.941  39.281  1.00 46.19           O  
HETATM 4462  O   HOH B 608       7.729  68.802  25.629  1.00 33.69           O  
HETATM 4463  O   HOH B 609      -3.223  56.914  41.120  1.00 29.95           O  
HETATM 4464  O   HOH B 610       6.606  59.188  42.239  1.00 27.66           O  
HETATM 4465  O   HOH B 611      20.597  61.811  38.267  1.00 32.39           O  
HETATM 4466  O   HOH B 612      -7.166  56.773  38.949  1.00 30.53           O  
HETATM 4467  O   HOH B 613      22.224  56.270  37.953  1.00 42.31           O  
HETATM 4468  O   HOH B 614      22.870  69.193  39.262  1.00 45.57           O  
HETATM 4469  O   HOH B 615       7.209  72.114  31.060  1.00 52.62           O  
HETATM 4470  O   HOH B 616      16.898  52.000  50.978  1.00 46.01           O  
HETATM 4471  O   HOH B 617      27.989  58.432  40.888  1.00 32.48           O  
HETATM 4472  O   HOH B 618       3.627  63.891  48.298  1.00 45.48           O  
HETATM 4473  O   HOH B 619      30.319  60.646  49.045  1.00 25.12           O  
HETATM 4474  O   HOH B 620      18.242  63.176  38.586  1.00 32.45           O  
HETATM 4475  O   HOH B 621      35.831  50.436  54.561  1.00 39.67           O  
HETATM 4476  O   HOH B 622     -11.706  56.456  37.564  1.00 36.55           O  
HETATM 4477  O   HOH B 623      -8.684  60.848  32.787  1.00 30.25           O  
HETATM 4478  O   HOH B 624      30.382  52.371  38.226  1.00 44.29           O  
HETATM 4479  O   HOH B 625      -5.953  62.532  33.706  1.00 21.13           O  
HETATM 4480  O   HOH B 626      16.271  70.573  50.231  1.00 31.91           O  
HETATM 4481  O   HOH B 627     -15.127  76.134  45.623  1.00 26.23           O  
HETATM 4482  O   HOH B 628      28.359  59.394  36.366  1.00 49.39           O  
HETATM 4483  O   HOH B 629      35.404  53.336  44.793  1.00 46.15           O  
HETATM 4484  O   HOH B 630      -7.077  65.484  29.895  1.00 28.28           O  
HETATM 4485  O   HOH B 631      32.041  65.778  44.209  1.00 32.09           O  
HETATM 4486  O   HOH B 632      20.241  52.818  48.821  1.00 54.66           O  
HETATM 4487  O   HOH B 633      34.275  32.813  64.518  1.00 58.24           O  
HETATM 4488  O   HOH B 634      -7.873  71.827  34.329  1.00 40.75           O  
HETATM 4489  O   HOH B 635      10.810  61.961  26.088  1.00 26.75           O  
HETATM 4490  O   HOH B 636     -10.147  71.794  40.971  1.00 27.02           O  
HETATM 4491  O   HOH B 637      12.960  75.612  41.455  1.00 32.17           O  
HETATM 4492  O   HOH B 638       2.810  74.770  40.688  1.00 23.31           O  
HETATM 4493  O   HOH B 639      33.786  46.108  41.922  1.00 40.00           O  
HETATM 4494  O   HOH B 640       0.229  73.420  34.866  1.00 36.09           O  
HETATM 4495  O   HOH B 641     -16.603  62.544  44.510  1.00 37.63           O  
HETATM 4496  O   HOH B 642       8.793  56.182  38.807  1.00 29.29           O  
HETATM 4497  O   HOH B 643       7.130  73.842  46.057  1.00 36.97           O  
HETATM 4498  O   HOH B 644       1.214  75.343  36.859  1.00 31.04           O  
HETATM 4499  O   HOH B 645      -7.319  69.918  48.745  1.00 43.60           O  
HETATM 4500  O   HOH B 646      -9.027  62.703  47.339  1.00 40.26           O  
HETATM 4501  O   HOH B 647     -12.294  69.050  34.632  1.00 41.05           O  
HETATM 4502  O   HOH B 648       9.900  51.078  31.912  1.00 37.62           O  
HETATM 4503  O   HOH B 649      -0.298  72.852  45.845  1.00 37.47           O  
HETATM 4504  O   HOH B 650      21.179  60.357  40.175  1.00 39.76           O  
HETATM 4505  O   HOH B 651      30.952  58.775  51.819  1.00 48.61           O  
HETATM 4506  O   HOH B 652      26.253  54.785  32.461  1.00 42.38           O  
HETATM 4507  O   HOH B 653      19.766  56.582  33.588  1.00 46.70           O  
HETATM 4508  O   HOH B 654       4.731  54.553  42.276  1.00 32.39           O  
HETATM 4509  O   HOH B 655      13.295  74.635  37.683  1.00 43.71           O  
HETATM 4510  O   HOH B 656     -16.855  55.150  40.916  1.00 49.01           O  
HETATM 4511  O   HOH B 657      20.435  58.393  41.443  1.00 53.04           O  
HETATM 4512  O   HOH B 658      13.504  59.295  45.156  1.00 33.91           O  
HETATM 4513  O   HOH B 659      12.219  51.421  28.363  1.00 43.49           O  
HETATM 4514  O   HOH B 660      28.057  54.749  35.107  1.00 56.26           O  
HETATM 4515  O   HOH B 661       9.407  59.380  43.216  1.00 46.10           O  
HETATM 4516  O   HOH B 662      17.779  69.952  27.990  1.00 36.53           O  
HETATM 4517  O   HOH B 663      -5.688  75.326  36.359  1.00 59.66           O  
HETATM 4518  O   HOH B 664     -14.697  75.875  30.055  1.00 50.35           O  
HETATM 4519  O   HOH B 665      34.143  65.708  42.293  1.00 44.91           O  
HETATM 4520  O   HOH B 666      18.602  54.371  50.164  1.00 29.14           O  
HETATM 4521  O   HOH B 667      -7.038  53.896  42.609  1.00 39.64           O  
HETATM 4522  O   HOH B 668       4.824  52.081  41.861  1.00 39.29           O  
HETATM 4523  O   HOH C 201     -14.144  29.515  27.952  1.00 41.45           O  
HETATM 4524  O   HOH C 202     -12.753  36.281  27.977  1.00 30.41           O  
HETATM 4525  O   HOH C 203     -10.694  37.956  13.521  1.00 44.31           O  
HETATM 4526  O   HOH C 204     -21.710  30.740   6.179  1.00 44.45           O  
HETATM 4527  O   HOH C 205     -20.090  37.774  14.898  1.00 41.24           O  
HETATM 4528  O   HOH C 206     -10.379  24.803  19.471  1.00 57.78           O  
HETATM 4529  O   HOH C 207     -12.470  24.796  26.027  1.00 41.85           O  
HETATM 4530  O   HOH D 201      31.357  74.359  42.022  1.00 49.37           O  
HETATM 4531  O   HOH D 202      19.514  80.667  47.842  1.00 34.47           O  
HETATM 4532  O   HOH D 203      21.034  71.425  36.350  1.00 32.47           O  
HETATM 4533  O   HOH D 204      16.411  72.719  51.781  1.00 35.93           O  
HETATM 4534  O   HOH D 205      23.432  85.186  48.416  1.00 49.38           O  
HETATM 4535  O   HOH D 206       9.345  74.074  49.907  1.00 37.23           O  
HETATM 4536  O   HOH D 207      30.057  68.834  51.971  1.00 45.11           O  
HETATM 4537  O   HOH D 208      20.330  70.927  56.260  1.00 50.42           O  
HETATM 4538  O   HOH D 209      17.228  79.761  55.055  1.00 55.39           O  
HETATM 4539  O   HOH D 210      13.295  79.672  51.365  1.00 35.46           O  
HETATM 4540  O   HOH D 211      32.803  68.343  45.188  1.00 44.88           O  
HETATM 4541  O   HOH D 212      38.675  74.324  40.230  1.00 57.41           O  
CONECT  192  692                                                                
CONECT  493 4231                                                                
CONECT  692  192                                                                
CONECT 1055 1521                                                                
CONECT 1521 1055                                                                
CONECT 1872 2372                                                                
CONECT 2173 4327                                                                
CONECT 2372 1872                                                                
CONECT 2727 3193                                                                
CONECT 3193 2727                                                                
CONECT 4231  493 4232 4242                                                      
CONECT 4232 4231 4233 4239                                                      
CONECT 4233 4232 4234 4240                                                      
CONECT 4234 4233 4235 4241                                                      
CONECT 4235 4234 4236 4242                                                      
CONECT 4236 4235 4243                                                           
CONECT 4237 4238 4239 4244                                                      
CONECT 4238 4237                                                                
CONECT 4239 4232 4237                                                           
CONECT 4240 4233                                                                
CONECT 4241 4234 4245                                                           
CONECT 4242 4231 4235                                                           
CONECT 4243 4236 4317                                                           
CONECT 4244 4237                                                                
CONECT 4245 4241 4246 4256                                                      
CONECT 4246 4245 4247 4253                                                      
CONECT 4247 4246 4248 4254                                                      
CONECT 4248 4247 4249 4255                                                      
CONECT 4249 4248 4250 4256                                                      
CONECT 4250 4249 4257                                                           
CONECT 4251 4252 4253 4258                                                      
CONECT 4252 4251                                                                
CONECT 4253 4246 4251                                                           
CONECT 4254 4247                                                                
CONECT 4255 4248 4259                                                           
CONECT 4256 4245 4249                                                           
CONECT 4257 4250                                                                
CONECT 4258 4251                                                                
CONECT 4259 4255 4260 4268                                                      
CONECT 4260 4259 4261 4265                                                      
CONECT 4261 4260 4262 4266                                                      
CONECT 4262 4261 4263 4267                                                      
CONECT 4263 4262 4264 4268                                                      
CONECT 4264 4263 4269                                                           
CONECT 4265 4260                                                                
CONECT 4266 4261 4306                                                           
CONECT 4267 4262                                                                
CONECT 4268 4259 4263                                                           
CONECT 4269 4264 4270                                                           
CONECT 4270 4269 4271 4279                                                      
CONECT 4271 4270 4272 4276                                                      
CONECT 4272 4271 4273 4277                                                      
CONECT 4273 4272 4274 4278                                                      
CONECT 4274 4273 4275 4279                                                      
CONECT 4275 4274 4280                                                           
CONECT 4276 4271 4281                                                           
CONECT 4277 4272                                                                
CONECT 4278 4273                                                                
CONECT 4279 4270 4274                                                           
CONECT 4280 4275                                                                
CONECT 4281 4276 4282 4292                                                      
CONECT 4282 4281 4283 4289                                                      
CONECT 4283 4282 4284 4290                                                      
CONECT 4284 4283 4285 4291                                                      
CONECT 4285 4284 4286 4292                                                      
CONECT 4286 4285 4293                                                           
CONECT 4287 4288 4289 4294                                                      
CONECT 4288 4287                                                                
CONECT 4289 4282 4287                                                           
CONECT 4290 4283                                                                
CONECT 4291 4284 4295                                                           
CONECT 4292 4281 4285                                                           
CONECT 4293 4286                                                                
CONECT 4294 4287                                                                
CONECT 4295 4291 4296 4304                                                      
CONECT 4296 4295 4297 4301                                                      
CONECT 4297 4296 4298 4302                                                      
CONECT 4298 4297 4299 4303                                                      
CONECT 4299 4298 4300 4304                                                      
CONECT 4300 4299 4305                                                           
CONECT 4301 4296                                                                
CONECT 4302 4297                                                                
CONECT 4303 4298                                                                
CONECT 4304 4295 4299                                                           
CONECT 4305 4300                                                                
CONECT 4306 4266 4307 4315                                                      
CONECT 4307 4306 4308 4312                                                      
CONECT 4308 4307 4309 4313                                                      
CONECT 4309 4308 4310 4314                                                      
CONECT 4310 4309 4311 4315                                                      
CONECT 4311 4310 4316                                                           
CONECT 4312 4307                                                                
CONECT 4313 4308                                                                
CONECT 4314 4309                                                                
CONECT 4315 4306 4310                                                           
CONECT 4316 4311                                                                
CONECT 4317 4243 4318 4326                                                      
CONECT 4318 4317 4319 4323                                                      
CONECT 4319 4318 4320 4324                                                      
CONECT 4320 4319 4321 4325                                                      
CONECT 4321 4320 4322 4326                                                      
CONECT 4322 4321                                                                
CONECT 4323 4318                                                                
CONECT 4324 4319                                                                
CONECT 4325 4320                                                                
CONECT 4326 4317 4321                                                           
CONECT 4327 2173 4328 4338                                                      
CONECT 4328 4327 4329 4335                                                      
CONECT 4329 4328 4330 4336                                                      
CONECT 4330 4329 4331 4337                                                      
CONECT 4331 4330 4332 4338                                                      
CONECT 4332 4331 4339                                                           
CONECT 4333 4334 4335 4340                                                      
CONECT 4334 4333                                                                
CONECT 4335 4328 4333                                                           
CONECT 4336 4329                                                                
CONECT 4337 4330 4341                                                           
CONECT 4338 4327 4331                                                           
CONECT 4339 4332 4402                                                           
CONECT 4340 4333                                                                
CONECT 4341 4337 4342 4352                                                      
CONECT 4342 4341 4343 4349                                                      
CONECT 4343 4342 4344 4350                                                      
CONECT 4344 4343 4345 4351                                                      
CONECT 4345 4344 4346 4352                                                      
CONECT 4346 4345 4353                                                           
CONECT 4347 4348 4349 4354                                                      
CONECT 4348 4347                                                                
CONECT 4349 4342 4347                                                           
CONECT 4350 4343                                                                
CONECT 4351 4344 4355                                                           
CONECT 4352 4341 4345                                                           
CONECT 4353 4346                                                                
CONECT 4354 4347                                                                
CONECT 4355 4351 4356 4364                                                      
CONECT 4356 4355 4357 4361                                                      
CONECT 4357 4356 4358 4362                                                      
CONECT 4358 4357 4359 4363                                                      
CONECT 4359 4358 4360 4364                                                      
CONECT 4360 4359 4365                                                           
CONECT 4361 4356                                                                
CONECT 4362 4357 4391                                                           
CONECT 4363 4358                                                                
CONECT 4364 4355 4359                                                           
CONECT 4365 4360 4366                                                           
CONECT 4366 4365 4367 4375                                                      
CONECT 4367 4366 4368 4372                                                      
CONECT 4368 4367 4369 4373                                                      
CONECT 4369 4368 4370 4374                                                      
CONECT 4370 4369 4371 4375                                                      
CONECT 4371 4370 4376                                                           
CONECT 4372 4367 4377                                                           
CONECT 4373 4368                                                                
CONECT 4374 4369                                                                
CONECT 4375 4366 4370                                                           
CONECT 4376 4371                                                                
CONECT 4377 4372 4378 4388                                                      
CONECT 4378 4377 4379 4385                                                      
CONECT 4379 4378 4380 4386                                                      
CONECT 4380 4379 4381 4387                                                      
CONECT 4381 4380 4382 4388                                                      
CONECT 4382 4381 4389                                                           
CONECT 4383 4384 4385 4390                                                      
CONECT 4384 4383                                                                
CONECT 4385 4378 4383                                                           
CONECT 4386 4379                                                                
CONECT 4387 4380                                                                
CONECT 4388 4377 4381                                                           
CONECT 4389 4382                                                                
CONECT 4390 4383                                                                
CONECT 4391 4362 4392 4400                                                      
CONECT 4392 4391 4393 4397                                                      
CONECT 4393 4392 4394 4398                                                      
CONECT 4394 4393 4395 4399                                                      
CONECT 4395 4394 4396 4400                                                      
CONECT 4396 4395 4401                                                           
CONECT 4397 4392                                                                
CONECT 4398 4393                                                                
CONECT 4399 4394                                                                
CONECT 4400 4391 4395                                                           
CONECT 4401 4396                                                                
CONECT 4402 4339 4403 4411                                                      
CONECT 4403 4402 4404 4408                                                      
CONECT 4404 4403 4405 4409                                                      
CONECT 4405 4404 4406 4410                                                      
CONECT 4406 4405 4407 4411                                                      
CONECT 4407 4406                                                                
CONECT 4408 4403                                                                
CONECT 4409 4404                                                                
CONECT 4410 4405                                                                
CONECT 4411 4402 4406                                                           
MASTER      341    0   15   16   48    0    0    6 4529    4  191   44          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.