CNRS Nantes University US2B US2B
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***  TRANSCRIPTION 31-MAR-22 7UJO  ***

elNémo ID: 2407252150121255009

Job options:

ID        	=	 2407252150121255009
JOBID     	=	 TRANSCRIPTION 31-MAR-22 7UJO
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSCRIPTION                           31-MAR-22   7UJO              
TITLE     ESTROGEN RECEPTOR ALPHA LIGAND BINDING DOMAIN IN COMPLEX WITH RU39411 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTROGEN RECEPTOR;                                         
COMPND   3 CHAIN: B, D, C, A;                                                   
COMPND   4 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3 
COMPND   5 GROUP A MEMBER 1;                                                    
COMPND   6 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: ESR1, ESR, NR3A1;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA HELICAL BUNDLE, HORMONE, BREAST CANCER, ESTROGEN, TRANSCRIPTION 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.HOSFIELD,G.L.GREENE,S.W.FANNING                                   
REVDAT   2   18-OCT-23 7UJO    1       REMARK                                   
REVDAT   1   15-JUN-22 7UJO    0                                                
SPRSDE     15-JUN-22 7UJO      6VIG                                             
JRNL        AUTH   D.J.HOSFIELD,S.WEBER,N.S.LI,M.SUAVAGE,C.F.JOINER,            
JRNL        AUTH 2 G.R.HANCOCK,E.A.SULLIVAN,E.NDUKWE,R.HAN,S.CUSH,M.LAINE,      
JRNL        AUTH 3 S.C.MADER,G.L.GREENE,S.W.FANNING                             
JRNL        TITL   STEREOSPECIFIC LASOFOXIFENE DERIVATIVES REVEAL THE INTERPLAY 
JRNL        TITL 2 BETWEEN ESTROGEN RECEPTOR ALPHA STABILITY AND ANTAGONISTIC   
JRNL        TITL 3 ACTIVITY IN ESR1 MUTANT BREAST CANCER CELLS.                 
JRNL        REF    ELIFE                         V.  11       2022              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   35575456                                                     
JRNL        DOI    10.7554/ELIFE.72512                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.82                                          
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 144095                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.58                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 7UJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1000264295.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 144124                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.449                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 5UFX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8,000, TRIS PH 6.5, MGCL2, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      183.51333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.75667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       29.11700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       50.43212            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS B   292                                                      
REMARK 465     HIS B   293                                                      
REMARK 465     HIS B   294                                                      
REMARK 465     HIS B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     ASN B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     TYR B   301                                                      
REMARK 465     GLN B   302                                                      
REMARK 465     PHE B   303                                                      
REMARK 465     SER B   304                                                      
REMARK 465     MET B   305                                                      
REMARK 465     LEU B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     SER B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     ALA B   546                                                      
REMARK 465     HIS B   547                                                      
REMARK 465     ARG B   548                                                      
REMARK 465     LEU B   549                                                      
REMARK 465     HIS B   550                                                      
REMARK 465     ALA B   551                                                      
REMARK 465     PRO B   552                                                      
REMARK 465     THR B   553                                                      
REMARK 465     SER B   554                                                      
REMARK 465     HIS D   292                                                      
REMARK 465     HIS D   293                                                      
REMARK 465     HIS D   294                                                      
REMARK 465     HIS D   295                                                      
REMARK 465     HIS D   296                                                      
REMARK 465     HIS D   297                                                      
REMARK 465     GLU D   298                                                      
REMARK 465     ASN D   299                                                      
REMARK 465     LEU D   300                                                      
REMARK 465     TYR D   301                                                      
REMARK 465     GLN D   302                                                      
REMARK 465     PHE D   303                                                      
REMARK 465     SER D   304                                                      
REMARK 465     MET D   305                                                      
REMARK 465     SER D   417                                                      
REMARK 465     VAL D   418                                                      
REMARK 465     ARG D   548                                                      
REMARK 465     LEU D   549                                                      
REMARK 465     HIS D   550                                                      
REMARK 465     ALA D   551                                                      
REMARK 465     PRO D   552                                                      
REMARK 465     THR D   553                                                      
REMARK 465     SER D   554                                                      
REMARK 465     HIS C   292                                                      
REMARK 465     HIS C   293                                                      
REMARK 465     HIS C   294                                                      
REMARK 465     HIS C   295                                                      
REMARK 465     HIS C   296                                                      
REMARK 465     HIS C   297                                                      
REMARK 465     GLU C   298                                                      
REMARK 465     ASN C   299                                                      
REMARK 465     LEU C   300                                                      
REMARK 465     TYR C   301                                                      
REMARK 465     GLN C   302                                                      
REMARK 465     PHE C   303                                                      
REMARK 465     SER C   304                                                      
REMARK 465     MET C   305                                                      
REMARK 465     LEU C   306                                                      
REMARK 465     ALA C   307                                                      
REMARK 465     LEU C   308                                                      
REMARK 465     GLN C   414                                                      
REMARK 465     GLY C   415                                                      
REMARK 465     LYS C   416                                                      
REMARK 465     SER C   417                                                      
REMARK 465     VAL C   418                                                      
REMARK 465     HIS C   547                                                      
REMARK 465     ARG C   548                                                      
REMARK 465     LEU C   549                                                      
REMARK 465     HIS C   550                                                      
REMARK 465     ALA C   551                                                      
REMARK 465     PRO C   552                                                      
REMARK 465     THR C   553                                                      
REMARK 465     SER C   554                                                      
REMARK 465     HIS A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     ASN A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     TYR A   301                                                      
REMARK 465     GLN A   302                                                      
REMARK 465     PHE A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     MET A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     PHE A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     SER A   417                                                      
REMARK 465     VAL A   418                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     HIS A   547                                                      
REMARK 465     ARG A   548                                                      
REMARK 465     LEU A   549                                                      
REMARK 465     HIS A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     PRO A   552                                                      
REMARK 465     THR A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP B 332    CG   OD1  OD2                                       
REMARK 470     ARG B 335    CD   NE   CZ   NH1  NH2                             
REMARK 470     PHE B 337    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B 413    CG   OD1  ND2                                       
REMARK 470     LYS B 416    CG   CD   CE   NZ                                                        
ATOM      1  N   SER B 309      15.390   1.168 -39.447  1.00 44.35           N  
ANISOU    1  N   SER B 309     8170   4627   4056  -1058   -687   1083       N  
ATOM      2  CA  SER B 309      14.918   2.544 -39.389  1.00 44.74           C  
ANISOU    2  CA  SER B 309     8082   4562   4354   -983   -992   1331       C  
ATOM      3  C   SER B 309      14.313   2.849 -38.021  1.00 42.78           C  
ANISOU    3  C   SER B 309     7307   4329   4619   -639  -1091   1275       C  
ATOM      4  O   SER B 309      14.077   4.010 -37.682  1.00 45.03           O  
ANISOU    4  O   SER B 309     7412   4476   5222   -512  -1201   1403       O  
ATOM      5  CB  SER B 309      13.891   2.804 -40.492  1.00 47.57           C  
ANISOU    5  CB  SER B 309     8665   4882   4527  -1218  -1447   1631       C  
ATOM      6  OG  SER B 309      12.732   2.006 -40.310  1.00 48.38           O  
ANISOU    6  OG  SER B 309     8589   5089   4705  -1190  -1732   1652       O  
ATOM      7  N   LEU B 310      14.075   1.796 -37.239  1.00 39.60           N  
ANISOU    7  N   LEU B 310     6692   4066   4288   -509  -1010   1073       N  
ATOM      8  CA  LEU B 310      13.432   1.920 -35.931  1.00 37.27           C  
ANISOU    8  CA  LEU B 310     5961   3786   4414   -234  -1062    992       C  
ATOM      9  C   LEU B 310      14.207   2.791 -34.955  1.00 33.80           C  
ANISOU    9  C   LEU B 310     5321   3282   4240    -86   -817    854       C  
ATOM     10  O   LEU B 310      15.428   2.687 -34.842  1.00 35.09           O  
ANISOU   10  O   LEU B 310     5543   3494   4295   -139   -534    713       O  
ATOM     11  CB  LEU B 310      13.229   0.543 -35.293  1.00 35.20           C  
ANISOU   11  CB  LEU B 310     5568   3693   4113   -168   -973    787       C  
ATOM     12  CG  LEU B 310      12.138  -0.384 -35.825  1.00 37.76           C  
ANISOU   12  CG  LEU B 310     5977   4084   4287   -275  -1253    889       C  
ATOM     13  CD1 LEU B 310      11.998  -1.586 -34.903  1.00 35.93           C  
ANISOU   13  CD1 LEU B 310     5547   3993   4112   -157  -1114    662       C  
ATOM     14  CD2 LEU B 310      10.812   0.348 -35.958  1.00 41.71           C  
ANISOU   14  CD2 LEU B 310     6300   4479   5069   -231  -1664   1182       C  
ATOM     15  N   THR B 311      13.479   3.644 -34.243  1.00 32.64           N  
ANISOU   15  N   THR B 311     4934   3002   4466     78   -912    904       N  
ATOM     16  CA  THR B 311      14.039   4.367 -33.111  1.00 31.62           C  
ANISOU   16  CA  THR B 311     4643   2803   4568    179   -676    726       C  
ATOM     17  C   THR B 311      14.182   3.414 -31.927  1.00 28.98           C  
ANISOU   17  C   THR B 311     4128   2640   4244    248   -522    470       C  
ATOM     18  O   THR B 311      13.643   2.304 -31.948  1.00 27.57           O  
ANISOU   18  O   THR B 311     3902   2597   3978    272   -603    444       O  
ATOM     19  CB  THR B 311      13.160   5.563 -32.704  1.00 31.34           C  
ANISOU   19  CB  THR B 311     4453   2507   4947    319   -741    833       C  
ATOM     20  OG1 THR B 311      11.965   5.087 -32.073  1.00 30.17           O  
ANISOU   20  OG1 THR B 311     4060   2355   5048    470   -813    813       O  
ATOM     21  CG2 THR B 311      12.796   6.409 -33.923  1.00 36.17           C  
ANISOU   21  CG2 THR B 311     5206   2937   5599    259   -985   1176       C  
ATOM     22  N   ALA B 312      14.907   3.847 -30.899  1.00 27.60           N  
ANISOU   22  N   ALA B 312     3876   2454   4157    242   -323    299       N  
ATOM     23  CA  ALA B 312      15.104   3.029 -29.708  1.00 24.95           C  
ANISOU   23  CA  ALA B 312     3397   2274   3810    253   -216     95       C  
ATOM     24  C   ALA B 312      13.775   2.717 -29.034  1.00 22.75           C  
ANISOU   24  C   ALA B 312     2968   1964   3712    386   -268     40       C  
ATOM     25  O   ALA B 312      13.499   1.570 -28.702  1.00 21.27           O  
ANISOU   25  O   ALA B 312     2700   1938   3442    411   -291    -30       O  
ATOM     26  CB  ALA B 312      16.041   3.720 -28.733  1.00 22.88           C  
ANISOU   26  CB  ALA B 312     3125   1981   3588    144    -60    -33       C  
ATOM     27  N   ASP B 313      12.949   3.739 -28.837  1.00 24.77           N  
ANISOU   27  N   ASP B 313     3172   1983   4257    476   -253     82       N  
ATOM     28  CA  ASP B 313      11.640   3.531 -28.229  1.00 25.35           C  
ANISOU   28  CA  ASP B 313     3062   1976   4596    614   -241     49       C  
ATOM     29  C   ASP B 313      10.791   2.556 -29.045  1.00 25.23           C  
ANISOU   29  C   ASP B 313     2962   2077   4549    669   -496    220       C  
ATOM     30  O   ASP B 313      10.125   1.680 -28.488  1.00 25.02           O  
ANISOU   30  O   ASP B 313     2799   2145   4563    719   -490    138       O  
ATOM     31  CB  ASP B 313      10.906   4.856 -28.068  1.00 28.87           C  
ANISOU   31  CB  ASP B 313     3436   2074   5458    724   -136    117       C  
ATOM     32  CG  ASP B 313      11.449   5.682 -26.921  1.00 30.36           C  
ANISOU   32  CG  ASP B 313     3733   2113   5689    640    186   -133       C  
ATOM     33  OD1 ASP B 313      12.301   5.163 -26.171  1.00 32.29           O  
ANISOU   33  OD1 ASP B 313     4077   2554   5636    479    266   -330       O  
ATOM     34  OD2 ASP B 313      11.013   6.839 -26.761  1.00 34.33           O  
ANISOU   34  OD2 ASP B 313     4229   2281   6532    710    356   -114       O  
ATOM     35  N   GLN B 314      10.830   2.701 -30.365  1.00 27.72           N  
ANISOU   35  N   GLN B 314     3396   2382   4755    612   -727    460       N  
ATOM     36  CA  GLN B 314      10.082   1.810 -31.242  1.00 26.86           C  
ANISOU   36  CA  GLN B 314     3289   2379   4539    572  -1011    638       C  
ATOM     37  C   GLN B 314      10.607   0.377 -31.182  1.00 24.43           C  
ANISOU   37  C   GLN B 314     3081   2326   3874    482   -953    470       C  
ATOM     38  O   GLN B 314       9.830  -0.571 -31.276  1.00 24.33           O  
ANISOU   38  O   GLN B 314     3003   2407   3834    476  -1091    498       O  
ATOM     39  CB  GLN B 314      10.116   2.324 -32.682  1.00 30.50           C  
ANISOU   39  CB  GLN B 314     3954   2764   4869    443  -1274    936       C  
ATOM     40  CG  GLN B 314       9.270   3.564 -32.921  1.00 32.52           C  
ANISOU   40  CG  GLN B 314     4052   2744   5559    542  -1439   1219       C  
ATOM     41  CD  GLN B 314       9.578   4.225 -34.245  1.00 36.64           C  
ANISOU   41  CD  GLN B 314     4835   3184   5902    375  -1676   1512       C  
ATOM     42  OE1 GLN B 314      10.500   3.822 -34.953  1.00 34.36           O  
ANISOU   42  OE1 GLN B 314     4878   3034   5144    176  -1646   1457       O  
ATOM     43  NE2 GLN B 314       8.794   5.238 -34.596  1.00 42.29           N  
ANISOU   43  NE2 GLN B 314     5392   3759   6915    408  -1773   1720       N  
ATOM     44  N   MET B 315      11.921   0.225 -31.024  1.00 23.49           N  
ANISOU   44  N   MET B 315     3096   2296   3532    411   -744    318       N  
ATOM     45  CA  MET B 315      12.528  -1.098 -30.904  1.00 22.97           C  
ANISOU   45  CA  MET B 315     3083   2418   3225    354   -634    181       C  
ATOM     46  C   MET B 315      12.034  -1.780 -29.630  1.00 20.11           C  
ANISOU   46  C   MET B 315     2505   2141   2994    449   -571     25       C  
ATOM     47  O   MET B 315      11.645  -2.947 -29.650  1.00 19.38           O  
ANISOU   47  O   MET B 315     2398   2160   2807    441   -614     -7       O  
ATOM     48  CB  MET B 315      14.060  -0.997 -30.908  1.00 21.94           C  
ANISOU   48  CB  MET B 315     3046   2324   2967    279   -411    108       C  
ATOM     49  CG  MET B 315      14.787  -2.306 -30.622  1.00 21.80           C  
ANISOU   49  CG  MET B 315     2999   2450   2834    257   -250     -1       C  
ATOM     50  SD  MET B 315      14.550  -3.559 -31.896  1.00 28.38           S  
ANISOU   50  SD  MET B 315     4083   3310   3391    158   -248     34       S  
ATOM     51  CE  MET B 315      15.516  -2.858 -33.227  1.00 36.57           C  
ANISOU   51  CE  MET B 315     5424   4232   4239     -1   -109    130       C  
ATOM     52  N   VAL B 316      12.034  -1.035 -28.528  1.00 21.41           N  
ANISOU   52  N   VAL B 316     2546   2234   3354    505   -452    -78       N  
ATOM     53  CA  VAL B 316      11.550  -1.546 -27.247  1.00 22.11           C  
ANISOU   53  CA  VAL B 316     2489   2376   3535    547   -358   -234       C  
ATOM     54  C   VAL B 316      10.079  -1.925 -27.327  1.00 23.32           C  
ANISOU   54  C   VAL B 316     2499   2490   3871    642   -471   -173       C  
ATOM     55  O   VAL B 316       9.687  -3.021 -26.918  1.00 22.48           O  
ANISOU   55  O   VAL B 316     2325   2506   3709    644   -475   -240       O  
ATOM     56  CB  VAL B 316      11.736  -0.512 -26.116  1.00 23.03           C  
ANISOU   56  CB  VAL B 316     2595   2367   3787    522   -173   -368       C  
ATOM     57  CG1 VAL B 316      11.056  -0.986 -24.837  1.00 23.79           C  
ANISOU   57  CG1 VAL B 316     2605   2482   3950    523    -45   -532       C  
ATOM     58  CG2 VAL B 316      13.211  -0.249 -25.874  1.00 21.56           C  
ANISOU   58  CG2 VAL B 316     2515   2249   3427    376   -107   -410       C  
ATOM     59  N   SER B 317       9.276  -1.007 -27.857  1.00 23.83           N  
ANISOU   59  N   SER B 317     2491   2368   4195    716   -572    -12       N  
ATOM     60  CA  SER B 317       7.847  -1.232 -28.033  1.00 25.03           C  
ANISOU   60  CA  SER B 317     2433   2452   4625    802   -721    127       C  
ATOM     61  C   SER B 317       7.599  -2.512 -28.819  1.00 23.88           C  
ANISOU   61  C   SER B 317     2350   2492   4231    706   -960    215       C  
ATOM     62  O   SER B 317       6.758  -3.327 -28.444  1.00 22.38           O  
ANISOU   62  O   SER B 317     2021   2369   4114    717   -981    191       O  
ATOM     63  CB  SER B 317       7.196  -0.043 -28.742  1.00 29.59           C  
ANISOU   63  CB  SER B 317     2933   2815   5496    849   -844    379       C  
ATOM     64  OG  SER B 317       5.877  -0.355 -29.154  1.00 37.89           O  
ANISOU   64  OG  SER B 317     3829   3889   6679    818  -1003    559       O  
ATOM     65  N   ALA B 318       8.356  -2.687 -29.898  1.00 24.15           N  
ANISOU   65  N   ALA B 318     2643   2597   3938    574  -1080    294       N  
ATOM     66  CA  ALA B 318       8.236  -3.863 -30.752  1.00 23.58           C  
ANISOU   66  CA  ALA B 318     2739   2657   3565    423  -1250    347       C  
ATOM     67  C   ALA B 318       8.561  -5.148 -29.991  1.00 20.97           C  
ANISOU   67  C   ALA B 318     2399   2476   3091    429  -1063    124       C  
ATOM     68  O   ALA B 318       7.853  -6.150 -30.114  1.00 24.68           O  
ANISOU   68  O   ALA B 318     2851   3017   3508    372  -1177    136       O  
ATOM     69  CB  ALA B 318       9.142  -3.724 -31.970  1.00 23.10           C  
ANISOU   69  CB  ALA B 318     3025   2594   3159    253  -1284    422       C  
ATOM     70  N   LEU B 319       9.627  -5.115 -29.200  1.00 18.44           N  
ANISOU   70  N   LEU B 319     2084   2197   2726    476   -805    -48       N  
ATOM     71  CA  LEU B 319      10.050  -6.305 -28.470  1.00 20.81           C  
ANISOU   71  CA  LEU B 319     2363   2622   2922    475   -655   -200       C  
ATOM     72  C   LEU B 319       9.094  -6.642 -27.334  1.00 23.22           C  
ANISOU   72  C   LEU B 319     2452   2954   3416    547   -638   -279       C  
ATOM     73  O   LEU B 319       8.833  -7.817 -27.069  1.00 25.32           O  
ANISOU   73  O   LEU B 319     2702   3311   3610    524   -630   -334       O  
ATOM     74  CB  LEU B 319      11.466  -6.129 -27.929  1.00 17.98           C  
ANISOU   74  CB  LEU B 319     2026   2295   2510    471   -451   -283       C  
ATOM     75  CG  LEU B 319      12.528  -6.030 -29.027  1.00 20.03           C  
ANISOU   75  CG  LEU B 319     2484   2522   2606    395   -378   -222       C  
ATOM     76  CD1 LEU B 319      13.908  -5.835 -28.421  1.00 18.07           C  
ANISOU   76  CD1 LEU B 319     2166   2297   2402    390   -198   -255       C  
ATOM     77  CD2 LEU B 319      12.487  -7.261 -29.919  1.00 19.42           C  
ANISOU   77  CD2 LEU B 319     2588   2461   2329    314   -347   -220       C  
ATOM     78  N   LEU B 320       8.575  -5.615 -26.665  1.00 21.23           N  
ANISOU   78  N   LEU B 320     2055   2594   3416    625   -586   -294       N  
ATOM     79  CA  LEU B 320       7.613  -5.830 -25.589  1.00 22.64           C  
ANISOU   79  CA  LEU B 320     2054   2752   3796    676   -486   -383       C  
ATOM     80  C   LEU B 320       6.348  -6.473 -26.123  1.00 23.37           C  
ANISOU   80  C   LEU B 320     2065   2856   3958    649   -634   -244       C  
ATOM     81  O   LEU B 320       5.764  -7.342 -25.476  1.00 26.37           O  
ANISOU   81  O   LEU B 320     2395   3298   4327    617   -558   -300       O  
ATOM     82  CB  LEU B 320       7.274  -4.516 -24.875  1.00 20.79           C  
ANISOU   82  CB  LEU B 320     1756   2336   3806    720   -298   -423       C  
ATOM     83  CG  LEU B 320       8.407  -3.960 -24.014  1.00 21.58           C  
ANISOU   83  CG  LEU B 320     1978   2426   3793    661   -113   -595       C  
ATOM     84  CD1 LEU B 320       8.014  -2.636 -23.378  1.00 25.36           C  
ANISOU   84  CD1 LEU B 320     2443   2667   4527    688    114   -673       C  
ATOM     85  CD2 LEU B 320       8.798  -4.974 -22.949  1.00 21.60           C  
ANISOU   85  CD2 LEU B 320     2032   2590   3584    553    -26   -733       C  
ATOM     86  N   ASP B 321       5.941  -6.052 -27.314  1.00 24.27           N  
ANISOU   86  N   ASP B 321     2183   2910   4129    632   -869    -41       N  
ATOM     87  CA  ASP B 321       4.702  -6.530 -27.909  1.00 27.16           C  
ANISOU   87  CA  ASP B 321     2470   3285   4564    559  -1053    128       C  
ATOM     88  C   ASP B 321       4.872  -7.962 -28.415  1.00 23.17           C  
ANISOU   88  C   ASP B 321     2114   2925   3765    431  -1189     97       C  
ATOM     89  O   ASP B 321       3.912  -8.728 -28.464  1.00 29.29           O  
ANISOU   89  O   ASP B 321     2821   3740   4566    358  -1261    149       O  
ATOM     90  CB  ASP B 321       4.261  -5.590 -29.039  1.00 28.33           C  
ANISOU   90  CB  ASP B 321     2616   3321   4829    517  -1290    383       C  
ATOM     91  CG  ASP B 321       3.012  -6.073 -29.753  1.00 37.69           C  
ANISOU   91  CG  ASP B 321     3732   4514   6076    390  -1528    584       C  
ATOM     92  OD1 ASP B 321       2.141  -6.678 -29.096  1.00 44.02           O  
ANISOU   92  OD1 ASP B 321     4370   5337   7018    411  -1442    541       O  
ATOM     93  OD2 ASP B 321       2.887  -5.825 -30.973  1.00 44.59           O  
ANISOU   93  OD2 ASP B 321     4731   5359   6853    242  -1807    796       O  
ATOM     94  N   ALA B 322       6.101  -8.330 -28.762  1.00 22.90           N  
ANISOU   94  N   ALA B 322     2296   2948   3456    399  -1194     -4       N  
ATOM     95  CA  ALA B 322       6.378  -9.661 -29.300  1.00 22.35           C  
ANISOU   95  CA  ALA B 322     2461   2965   3064    248  -1206    -61       C  
ATOM     96  C   ALA B 322       6.484 -10.739 -28.222  1.00 21.61           C  
ANISOU   96  C   ALA B 322     2286   2953   2974    303  -1003   -237       C  
ATOM     97  O   ALA B 322       6.618 -11.920 -28.544  1.00 22.87           O  
ANISOU   97  O   ALA B 322     2611   3149   2931    198   -975   -290       O  
ATOM     98  CB  ALA B 322       7.660  -9.633 -30.125  1.00 21.55           C  
ANISOU   98  CB  ALA B 322     2683   2846   2659    163  -1086    -95       C  
ATOM     99  N   GLU B 323       6.434 -10.336 -26.953  1.00 18.34           N  
ANISOU   99  N   GLU B 323     1655   2542   2769    437   -847   -325       N  
ATOM    100  CA  GLU B 323       6.677 -11.265 -25.849  1.00 18.80           C  
ANISOU  100  CA  GLU B 323     1683   2673   2787    449   -659   -458       C  
ATOM    101  C   GLU B 323       5.709 -12.440 -25.863  1.00 18.06           C  
ANISOU  101  C   GLU B 323     1565   2612   2686    372   -723   -445       C  
ATOM    102  O   GLU B 323       4.501 -12.249 -26.001  1.00 17.95           O  
ANISOU  102  O   GLU B 323     1436   2556   2827    339   -815   -335       O  
ATOM    103  CB  GLU B 323       6.591 -10.547 -24.503  1.00 20.67           C  
ANISOU  103  CB  GLU B 323     1835   2867   3153    482   -461   -515       C  
ATOM    104  CG  GLU B 323       7.898  -9.927 -24.067  1.00 21.92           C  
ANISOU  104  CG  GLU B 323     2055   3041   3233    496   -362   -578       C  
ATOM    105  CD  GLU B 323       8.951 -10.978 -23.766  1.00 20.47           C  
ANISOU  105  CD  GLU B 323     1936   2954   2888    458   -313   -602       C  
ATOM    106  OE1 GLU B 323       9.758 -11.278 -24.672  1.00 19.47           O  
ANISOU  106  OE1 GLU B 323     1882   2835   2680    474   -331   -561       O  
ATOM    107  OE2 GLU B 323       8.968 -11.502 -22.631  1.00 22.72           O  
ANISOU  107  OE2 GLU B 323     2202   3285   3147    404   -243   -643       O  
ATOM    108  N   PRO B 324       6.250 -13.663 -25.731  1.00 15.74           N  
ANISOU  108  N   PRO B 324     1371   2379   2232    337   -653   -531       N  
ATOM    109  CA  PRO B 324       5.430 -14.877 -25.700  1.00 16.39           C  
ANISOU  109  CA  PRO B 324     1449   2486   2292    250   -703   -545       C  
ATOM    110  C   PRO B 324       4.737 -15.010 -24.355  1.00 15.12           C  
ANISOU  110  C   PRO B 324     1125   2332   2289    283   -570   -569       C  
ATOM    111  O   PRO B 324       5.176 -14.409 -23.373  1.00 17.14           O  
ANISOU  111  O   PRO B 324     1361   2576   2576    333   -415   -609       O  
ATOM    112  CB  PRO B 324       6.451 -15.997 -25.919  1.00 18.52           C  
ANISOU  112  CB  PRO B 324     1936   2738   2365    212   -549   -602       C  
ATOM    113  CG  PRO B 324       7.712 -15.453 -25.352  1.00 22.39           C  
ANISOU  113  CG  PRO B 324     2393   3233   2882    320   -394   -612       C  
ATOM    114  CD  PRO B 324       7.687 -13.966 -25.609  1.00 17.91           C  
ANISOU  114  CD  PRO B 324     1772   2656   2378    363   -478   -573       C  
ATOM    115  N   PRO B 325       3.649 -15.781 -24.304  1.00 15.62           N  
ANISOU  115  N   PRO B 325     1118   2401   2416    208   -630   -541       N  
ATOM    116  CA  PRO B 325       2.985 -15.950 -23.011  1.00 18.47           C  
ANISOU  116  CA  PRO B 325     1359   2756   2902    222   -470   -579       C  
ATOM    117  C   PRO B 325       3.746 -16.861 -22.063  1.00 15.40           C  
ANISOU  117  C   PRO B 325     1044   2427   2379    211   -334   -685       C  
ATOM    118  O   PRO B 325       4.614 -17.619 -22.488  1.00 16.00           O  
ANISOU  118  O   PRO B 325     1214   2544   2323    206   -362   -712       O  
ATOM    119  CB  PRO B 325       1.657 -16.586 -23.391  1.00 18.02           C  
ANISOU  119  CB  PRO B 325     1188   2698   2959    131   -596   -493       C  
ATOM    120  CG  PRO B 325       1.968 -17.360 -24.634  1.00 17.65           C  
ANISOU  120  CG  PRO B 325     1306   2682   2720     13   -802   -477       C  
ATOM    121  CD  PRO B 325       2.963 -16.513 -25.383  1.00 19.20           C  
ANISOU  121  CD  PRO B 325     1630   2861   2804     62   -850   -473       C  
ATOM    122  N   ILE B 326       3.405 -16.783 -20.783  1.00 17.52           N  
ANISOU  122  N   ILE B 326     1254   2700   2701    193   -184   -742       N  
ATOM    123  CA  ILE B 326       3.894 -17.741 -19.807  1.00 16.79           C  
ANISOU  123  CA  ILE B 326     1199   2684   2495    135    -99   -801       C  
ATOM    124  C   ILE B 326       2.960 -18.949 -19.813  1.00 16.70           C  
ANISOU  124  C   ILE B 326     1127   2687   2532     66   -114   -808       C  
ATOM    125  O   ILE B 326       1.766 -18.819 -19.547  1.00 18.58           O  
ANISOU  125  O   ILE B 326     1250   2885   2925     36    -64   -810       O  
ATOM    126  CB  ILE B 326       3.973 -17.121 -18.401  1.00 18.28           C  
ANISOU  126  CB  ILE B 326     1370   2905   2671     75     73   -895       C  
ATOM    127  CG1 ILE B 326       5.013 -15.996 -18.377  1.00 23.18           C  
ANISOU  127  CG1 ILE B 326     2044   3533   3229    104     69   -905       C  
ATOM    128  CG2 ILE B 326       4.298 -18.182 -17.360  1.00 20.12           C  
ANISOU  128  CG2 ILE B 326     1690   3208   2747    -53    125   -887       C  
ATOM    129  CD1 ILE B 326       4.669 -14.874 -17.416  1.00 26.68           C  
ANISOU  129  CD1 ILE B 326     2507   3920   3710     37    275  -1030       C  
ATOM    130  N   LEU B 327       3.502 -20.117 -20.142  1.00 14.96           N  
ANISOU  130  N   LEU B 327      999   2484   2202     36   -159   -788       N  
ATOM    131  CA  LEU B 327       2.704 -21.333 -20.221  1.00 14.29           C  
ANISOU  131  CA  LEU B 327      920   2379   2130    -61   -173   -789       C  
ATOM    132  C   LEU B 327       2.669 -22.095 -18.902  1.00 14.52           C  
ANISOU  132  C   LEU B 327      967   2431   2118   -133    -40   -792       C  
ATOM    133  O   LEU B 327       3.528 -21.917 -18.034  1.00 14.13           O  
ANISOU  133  O   LEU B 327      980   2411   1976   -134     19   -758       O  
ATOM    134  CB  LEU B 327       3.235 -22.247 -21.327  1.00 14.31           C  
ANISOU  134  CB  LEU B 327     1114   2304   2021    -86   -228   -763       C  
ATOM    135  CG  LEU B 327       3.330 -21.605 -22.714  1.00 14.60           C  
ANISOU  135  CG  LEU B 327     1231   2308   2009    -86   -359   -755       C  
ATOM    136  CD1 LEU B 327       3.723 -22.644 -23.751  1.00 15.43           C  
ANISOU  136  CD1 LEU B 327     1610   2294   1958   -184   -329   -776       C  
ATOM    137  CD2 LEU B 327       2.007 -20.930 -23.085  1.00 15.83           C  
ANISOU  137  CD2 LEU B 327     1208   2503   2305   -149   -545   -720       C  
ATOM    138  N   TYR B 328       1.661 -22.947 -18.764  1.00 16.49           N  
ANISOU  138  N   TYR B 328     1173   2667   2427   -233    -22   -808       N  
ATOM    139  CA  TYR B 328       1.526 -23.793 -17.591  1.00 16.10           C  
ANISOU  139  CA  TYR B 328     1170   2626   2321   -335    101   -797       C  
ATOM    140  C   TYR B 328       1.998 -25.214 -17.867  1.00 16.17           C  
ANISOU  140  C   TYR B 328     1325   2559   2258   -368     75   -727       C  
ATOM    141  O   TYR B 328       1.945 -25.695 -19.001  1.00 16.32           O  
ANISOU  141  O   TYR B 328     1412   2503   2285   -366      6   -739       O  
ATOM    142  CB  TYR B 328       0.075 -23.815 -17.111  1.00 17.63           C  
ANISOU  142  CB  TYR B 328     1202   2828   2668   -433    204   -859       C  
ATOM    143  CG  TYR B 328      -0.378 -22.517 -16.478  1.00 19.94           C  
ANISOU  143  CG  TYR B 328     1362   3130   3084   -407    366   -936       C  
ATOM    144  CD1 TYR B 328      -0.670 -21.404 -17.255  1.00 28.93           C  
ANISOU  144  CD1 TYR B 328     2372   4225   4395   -283    290   -919       C  
ATOM    145  CD2 TYR B 328      -0.512 -22.407 -15.100  1.00 23.09           C  
ANISOU  145  CD2 TYR B 328     1841   3532   3402   -524    613  -1002       C  
ATOM    146  CE1 TYR B 328      -1.087 -20.214 -16.677  1.00 33.40           C  
ANISOU  146  CE1 TYR B 328     2895   4709   5087   -236    469   -954       C  
ATOM    147  CE2 TYR B 328      -0.927 -21.223 -14.512  1.00 23.00           C  
ANISOU  147  CE2 TYR B 328     1784   3461   3494   -519    840  -1101       C  
ATOM    148  CZ  TYR B 328      -1.212 -20.130 -15.305  1.00 30.37           C  
ANISOU  148  CZ  TYR B 328     2601   4304   4635   -350    758  -1063       C  
ATOM    149  OH  TYR B 328      -1.625 -18.949 -14.731  1.00 39.11           O  
ANISOU  149  OH  TYR B 328     3720   5279   5861   -329    977  -1121       O  
ATOM    150  N   SER B 329       2.467 -25.882 -16.821  1.00 16.53           N  
ANISOU  150  N   SER B 329     1451   2600   2231   -426    141   -643       N  
ATOM    151  CA  SER B 329       2.746 -27.306 -16.906  1.00 17.84           C  
ANISOU  151  CA  SER B 329     1727   2650   2402   -458    160   -556       C  
ATOM    152  C   SER B 329       1.433 -28.062 -17.087  1.00 18.25           C  
ANISOU  152  C   SER B 329     1763   2673   2498   -589    190   -637       C  
ATOM    153  O   SER B 329       0.404 -27.654 -16.550  1.00 18.83           O  
ANISOU  153  O   SER B 329     1714   2828   2612   -674    235   -703       O  
ATOM    154  CB  SER B 329       3.481 -27.787 -15.655  1.00 23.60           C  
ANISOU  154  CB  SER B 329     2516   3380   3071   -516    170   -384       C  
ATOM    155  OG  SER B 329       3.777 -29.168 -15.747  1.00 28.03           O  
ANISOU  155  OG  SER B 329     3157   3787   3708   -520    203   -265       O  
ATOM    156  N   GLU B 330       1.459 -29.142 -17.862  1.00 18.91           N  
ANISOU  156  N   GLU B 330     1971   2616   2598   -620    196   -634       N  
ATOM    157  CA  GLU B 330       0.279 -29.987 -18.006  1.00 20.28           C  
ANISOU  157  CA  GLU B 330     2153   2751   2801   -791    200   -690       C  
ATOM    158  C   GLU B 330       0.320 -31.135 -17.033  1.00 24.90           C  
ANISOU  158  C   GLU B 330     2820   3261   3382   -872    308   -600       C  
ATOM    159  O   GLU B 330       0.869 -32.193 -17.340  1.00 26.25           O  
ANISOU  159  O   GLU B 330     3153   3249   3572   -866    372   -545       O  
ATOM    160  CB  GLU B 330       0.148 -30.576 -19.406  1.00 25.62           C  
ANISOU  160  CB  GLU B 330     2996   3293   3444   -869    149   -758       C  
ATOM    161  CG  GLU B 330       0.101 -29.609 -20.538  1.00 27.66           C  
ANISOU  161  CG  GLU B 330     3246   3602   3663   -851      4   -815       C  
ATOM    162  CD  GLU B 330      -0.213 -30.320 -21.829  1.00 30.19           C  
ANISOU  162  CD  GLU B 330     3815   3786   3868  -1048    -58   -884       C  
ATOM    163  OE1 GLU B 330      -1.093 -31.210 -21.826  1.00 38.55           O  
ANISOU  163  OE1 GLU B 330     4918   4800   4931  -1255    -88   -902       O  
ATOM    164  OE2 GLU B 330       0.449 -30.010 -22.830  1.00 34.63           O  
ANISOU  164  OE2 GLU B 330     4567   4275   4315  -1030    -58   -926       O  
ATOM    165  N   TYR B 331      -0.258 -30.931 -15.862  1.00 26.31           N  
ANISOU  165  N   TYR B 331     2905   3547   3544   -960    364   -584       N  
ATOM    166  CA  TYR B 331      -0.552 -32.040 -14.975  1.00 30.97           C  
ANISOU  166  CA  TYR B 331     3582   4074   4111  -1104    454   -504       C  
ATOM    167  C   TYR B 331      -1.838 -31.712 -14.237  1.00 31.68           C  
ANISOU  167  C   TYR B 331     3538   4273   4226  -1259    558   -588       C  
ATOM    168  O   TYR B 331      -2.177 -30.542 -14.073  1.00 33.97           O  
ANISOU  168  O   TYR B 331     3683   4672   4553  -1222    597   -670       O  
ATOM    169  CB  TYR B 331       0.598 -32.294 -13.999  1.00 28.54           C  
ANISOU  169  CB  TYR B 331     3383   3740   3720  -1074    450   -304       C  
ATOM    170  CG  TYR B 331       0.836 -31.172 -13.013  1.00 29.85           C  
ANISOU  170  CG  TYR B 331     3524   4071   3747  -1111    443   -287       C  
ATOM    171  CD1 TYR B 331       0.180 -31.151 -11.789  1.00 30.61           C  
ANISOU  171  CD1 TYR B 331     3684   4239   3707  -1324    559   -295       C  
ATOM    172  CD2 TYR B 331       1.711 -30.135 -13.305  1.00 27.29           C  
ANISOU  172  CD2 TYR B 331     3155   3809   3406   -971    353   -278       C  
ATOM    173  CE1 TYR B 331       0.390 -30.131 -10.880  1.00 31.30           C  
ANISOU  173  CE1 TYR B 331     3838   4442   3614  -1421    602   -313       C  
ATOM    174  CE2 TYR B 331       1.928 -29.105 -12.400  1.00 25.42           C  
ANISOU  174  CE2 TYR B 331     2948   3699   3010  -1053    357   -281       C  
ATOM    175  CZ  TYR B 331       1.262 -29.111 -11.188  1.00 29.96           C  
ANISOU  175  CZ  TYR B 331     3633   4329   3421  -1291    490   -308       C  
ATOM    176  OH  TYR B 331       1.462 -28.099 -10.277  1.00 34.39           O  
ANISOU  176  OH  TYR B 331     4311   4983   3774  -1435    545   -345       O  
ATOM    177  N   ASP B 332      -2.561 -32.737 -13.805  1.00 34.48           N  
ANISOU  177  N   ASP B 332     3933   4566   4600  -1430    644   -568       N  
ATOM    178  CA  ASP B 332      -3.771 -32.510 -13.031  1.00 38.15           C  
ANISOU  178  CA  ASP B 332     4262   5103   5132  -1590    816   -638       C  
ATOM    179  C   ASP B 332      -3.404 -32.207 -11.583  1.00 33.04           C  
ANISOU  179  C   ASP B 332     3757   4510   4286  -1681    974   -590       C  
ATOM    180  O   ASP B 332      -2.843 -33.057 -10.889  1.00 34.08           O  
ANISOU  180  O   ASP B 332     4102   4588   4258  -1778    958   -441       O  
ATOM    181  CB  ASP B 332      -4.708 -33.715 -13.113  1.00 43.10           C  
ANISOU  181  CB  ASP B 332     4885   5642   5851  -1775    858   -632       C  
ATOM    182  N   PRO B 333      -3.726 -30.990 -11.120  1.00 33.03           N  
ANISOU  182  N   PRO B 333     3663   4592   4293  -1681   1129   -702       N  
ATOM    183  CA  PRO B 333      -3.282 -30.526  -9.801  1.00 33.08           C  
ANISOU  183  CA  PRO B 333     3894   4644   4030  -1827   1281   -685       C  
ATOM    184  C   PRO B 333      -4.009 -31.210  -8.647  1.00 35.20           C  
ANISOU  184  C   PRO B 333     4317   4876   4181  -2099   1525   -679       C  
ATOM    185  O   PRO B 333      -3.632 -31.010  -7.493  1.00 35.91           O  
ANISOU  185  O   PRO B 333     4694   4983   3969  -2266   1600   -644       O  
ATOM    186  CB  PRO B 333      -3.597 -29.027  -9.837  1.00 34.73           C  
ANISOU  186  CB  PRO B 333     3960   4894   4342  -1747   1446   -857       C  
ATOM    187  CG  PRO B 333      -4.758 -28.918 -10.767  1.00 32.77           C  
ANISOU  187  CG  PRO B 333     3374   4598   4480  -1605   1452   -928       C  
ATOM    188  CD  PRO B 333      -4.552 -29.984 -11.814  1.00 31.81           C  
ANISOU  188  CD  PRO B 333     3204   4466   4417  -1575   1179   -834       C  
ATOM    189  N   THR B 334      -5.032 -32.002  -8.951  1.00 33.55           N  
ANISOU  189  N   THR B 334     3965   4600   4182  -2105   1574   -700       N  
ATOM    190  CA  THR B 334      -5.745 -32.741  -7.914  1.00 35.99           C  
ANISOU  190  CA  THR B 334     4428   4852   4395  -2289   1756   -682       C  
ATOM    191  C   THR B 334      -5.156 -34.135  -7.728  1.00 36.54           C  
ANISOU  191  C   THR B 334     4706   4870   4306  -2426   1603   -477       C  
ATOM    192  O   THR B 334      -5.505 -34.847  -6.788  1.00 38.56           O  
ANISOU  192  O   THR B 334     5149   5081   4419  -2599   1704   -416       O  
ATOM    193  CB  THR B 334      -7.254 -32.868  -8.229  1.00 40.66           C  
ANISOU  193  CB  THR B 334     4735   5386   5329  -2244   1902   -776       C  
ATOM    194  OG1 THR B 334      -7.441 -33.686  -9.390  1.00 39.72           O  
ANISOU  194  OG1 THR B 334     4441   5245   5407  -2201   1680   -710       O  
ATOM    195  CG2 THR B 334      -7.881 -31.497  -8.450  1.00 38.17           C  
ANISOU  195  CG2 THR B 334     4173   5064   5266  -2077   2040   -909       C  
ATOM    196  N   ARG B 335      -4.260 -34.516  -8.630  1.00 36.92           N  
ANISOU  196  N   ARG B 335     4729   4891   4408  -2329   1364   -366       N  
ATOM    197  CA  ARG B 335      -3.644 -35.836  -8.592  1.00 39.37           C  
ANISOU  197  CA  ARG B 335     5214   5076   4670  -2359   1206   -145       C  
ATOM    198  C   ARG B 335      -2.373 -35.801  -7.754  1.00 38.77           C  
ANISOU  198  C   ARG B 335     5370   5014   4347  -2403   1044    103       C  
ATOM    199  O   ARG B 335      -1.774 -34.741  -7.598  1.00 37.50           O  
ANISOU  199  O   ARG B 335     5217   4963   4070  -2349    980     84       O  
ATOM    200  CB  ARG B 335      -3.330 -36.316 -10.011  1.00 39.97           C  
ANISOU  200  CB  ARG B 335     5176   5040   4969  -2136   1033   -155       C  
ATOM    201  CG  ARG B 335      -4.533 -36.844 -10.765  1.00 43.03           C  
ANISOU  201  CG  ARG B 335     5421   5373   5555  -2210   1102   -300       C  
ATOM    202  N   PRO B 336      -1.962 -36.957  -7.203  1.00 37.77           N  
ANISOU  202  N   PRO B 336     5425   4767   4159  -2523    953    369       N  
ATOM    203  CA  PRO B 336      -0.669 -37.020  -6.510  1.00 40.23           C  
ANISOU  203  CA  PRO B 336     5899   5071   4315  -2567    702    705       C  
ATOM    204  C   PRO B 336       0.480 -36.602  -7.424  1.00 40.27           C  
ANISOU  204  C   PRO B 336     5734   5049   4518  -2248    493    782       C  
ATOM    205  O   PRO B 336       0.427 -36.879  -8.621  1.00 40.71           O  
ANISOU  205  O   PRO B 336     5631   4994   4845  -2006    531    659       O  
ATOM    206  CB  PRO B 336      -0.550 -38.497  -6.122  1.00 42.40           C  
ANISOU  206  CB  PRO B 336     6304   5155   4653  -2675    641    993       C  
ATOM    207  CG  PRO B 336      -1.954 -38.971  -6.025  1.00 44.66           C  
ANISOU  207  CG  PRO B 336     6602   5427   4940  -2804    910    760       C  
ATOM    208  CD  PRO B 336      -2.709 -38.223  -7.089  1.00 42.57           C  
ANISOU  208  CD  PRO B 336     6093   5234   4847  -2665   1066    408       C  
ATOM    209  N   PHE B 337       1.491 -35.939  -6.872  1.00 41.75           N  
ANISOU  209  N   PHE B 337     5979   5328   4556  -2290    282    980       N  
ATOM    210  CA  PHE B 337       2.617 -35.463  -7.668  1.00 41.74           C  
ANISOU  210  CA  PHE B 337     5795   5304   4762  -2005    105   1069       C  
ATOM    211  C   PHE B 337       3.813 -36.386  -7.502  1.00 47.14           C  
ANISOU  211  C   PHE B 337     6440   5804   5668  -1937   -134   1529       C  
ATOM    212  O   PHE B 337       4.199 -36.720  -6.381  1.00 48.27           O  
ANISOU  212  O   PHE B 337     6732   5962   5646  -2192   -337   1871       O  
ATOM    213  CB  PHE B 337       2.992 -34.033  -7.274  1.00 38.76           C  
ANISOU  213  CB  PHE B 337     5451   5133   4141  -2085     22    995       C  
ATOM    214  N   SER B 341       8.060 -37.991 -12.641  1.00 40.80           N  
ANISOU  214  N   SER B 341     5507   4648   5347   -562    721   1283       N  
ATOM    215  CA  SER B 341       7.429 -37.420 -13.826  1.00 32.80           C  
ANISOU  215  CA  SER B 341     4415   3665   4381   -622    719   1039       C  
ATOM    216  C   SER B 341       7.955 -36.050 -14.228  1.00 27.13           C  
ANISOU  216  C   SER B 341     3584   3115   3611   -530    585    939       C  
ATOM    217  O   SER B 341       7.444 -35.450 -15.173  1.00 27.51           O  
ANISOU  217  O   SER B 341     3560   3211   3682   -568    568    758       O  
ATOM    218  CB  SER B 341       5.920 -37.311 -13.609  1.00 34.34           C  
ANISOU  218  CB  SER B 341     4581   3949   4516   -803    790    924       C  
ATOM    219  OG  SER B 341       5.622 -37.005 -12.257  1.00 40.24           O  
ANISOU  219  OG  SER B 341     5331   4839   5119   -842    786   1024       O  
ATOM    220  N   MET B 342       8.962 -35.548 -13.523  1.00 25.56           N  
ANISOU  220  N   MET B 342     3367   3011   3335   -419    490   1059       N  
ATOM    221  CA  MET B 342       9.357 -34.157 -13.708  1.00 24.93           C  
ANISOU  221  CA  MET B 342     3189   3101   3183   -364    376    960       C  
ATOM    222  C   MET B 342       9.954 -33.870 -15.082  1.00 24.46           C  
ANISOU  222  C   MET B 342     3085   2976   3231   -287    338    850       C  
ATOM    223  O   MET B 342       9.638 -32.848 -15.686  1.00 21.37           O  
ANISOU  223  O   MET B 342     2622   2679   2817   -300    293    701       O  
ATOM    224  CB  MET B 342      10.340 -33.725 -12.622  1.00 28.73           C  
ANISOU  224  CB  MET B 342     3659   3713   3543   -292    284   1108       C  
ATOM    225  CG  MET B 342      10.466 -32.216 -12.514  1.00 32.32           C  
ANISOU  225  CG  MET B 342     4032   4357   3891   -291    197    988       C  
ATOM    226  SD  MET B 342       8.984 -31.415 -11.858  1.00 50.50           S  
ANISOU  226  SD  MET B 342     6312   6798   6077   -430    257    854       S  
ATOM    227  CE  MET B 342       8.364 -32.645 -10.707  1.00 39.40           C  
ANISOU  227  CE  MET B 342     4998   5360   4611   -527    352   1015       C  
ATOM    228  N   MET B 343      10.811 -34.756 -15.579  1.00 21.98           N  
ANISOU  228  N   MET B 343     2817   2500   3035   -203    365    928       N  
ATOM    229  CA  MET B 343      11.405 -34.540 -16.894  1.00 19.33           C  
ANISOU  229  CA  MET B 343     2446   2104   2793   -141    347    818       C  
ATOM    230  C   MET B 343      10.328 -34.538 -17.973  1.00 18.75           C  
ANISOU  230  C   MET B 343     2368   1997   2759   -257    402    629       C  
ATOM    231  O   MET B 343      10.384 -33.748 -18.916  1.00 20.28           O  
ANISOU  231  O   MET B 343     2501   2253   2951   -250    351    500       O  
ATOM    232  CB  MET B 343      12.455 -35.603 -17.206  1.00 20.51           C  
ANISOU  232  CB  MET B 343     2647   2067   3079    -30    399    930       C  
ATOM    233  CG  MET B 343      13.159 -35.380 -18.535  1.00 21.50           C  
ANISOU  233  CG  MET B 343     2736   2141   3292     31    393    812       C  
ATOM    234  SD  MET B 343      14.001 -33.783 -18.558  1.00 23.52           S  
ANISOU  234  SD  MET B 343     2872   2619   3444    103    238    776       S  
ATOM    235  CE  MET B 343      14.989 -33.918 -20.043  1.00 22.55           C  
ANISOU  235  CE  MET B 343     2728   2391   3447    181    268    685       C  
ATOM    236  N   GLY B 344       9.344 -35.420 -17.818  1.00 19.93           N  
ANISOU  236  N   GLY B 344     2578   2060   2936   -374    505    621       N  
ATOM    237  CA  GLY B 344       8.220 -35.481 -18.733  1.00 18.81           C  
ANISOU  237  CA  GLY B 344     2414   1920   2812   -513    552    449       C  
ATOM    238  C   GLY B 344       7.438 -34.180 -18.739  1.00 22.97           C  
ANISOU  238  C   GLY B 344     2827   2661   3240   -548    470    349       C  
ATOM    239  O   GLY B 344       7.061 -33.679 -19.799  1.00 19.55           O  
ANISOU  239  O   GLY B 344     2331   2285   2813   -582    437    216       O  
ATOM    240  N   LEU B 345       7.199 -33.628 -17.552  1.00 18.22           N  
ANISOU  240  N   LEU B 345     2200   2177   2545   -539    442    418       N  
ATOM    241  CA  LEU B 345       6.470 -32.370 -17.435  1.00 19.32           C  
ANISOU  241  CA  LEU B 345     2236   2498   2608   -555    388    328       C  
ATOM    242  C   LEU B 345       7.248 -31.226 -18.075  1.00 17.87           C  
ANISOU  242  C   LEU B 345     1998   2375   2415   -447    286    278       C  
ATOM    243  O   LEU B 345       6.694 -30.434 -18.839  1.00 19.61           O  
ANISOU  243  O   LEU B 345     2140   2673   2637   -456    251    170       O  
ATOM    244  CB  LEU B 345       6.177 -32.042 -15.967  1.00 20.14           C  
ANISOU  244  CB  LEU B 345     2343   2703   2608   -571    402    403       C  
ATOM    245  CG  LEU B 345       5.221 -32.944 -15.183  1.00 24.89           C  
ANISOU  245  CG  LEU B 345     2984   3284   3189   -697    509    449       C  
ATOM    246  CD1 LEU B 345       5.073 -32.445 -13.751  1.00 23.61           C  
ANISOU  246  CD1 LEU B 345     2824   3248   2897   -709    517    515       C  
ATOM    247  CD2 LEU B 345       3.864 -33.018 -15.866  1.00 25.91           C  
ANISOU  247  CD2 LEU B 345     3036   3452   3358   -816    563    314       C  
ATOM    248  N   LEU B 346       8.538 -31.154 -17.758  1.00 15.16           N  
ANISOU  248  N   LEU B 346     1693   2003   2065   -346    240    368       N  
ATOM    249  CA  LEU B 346       9.406 -30.089 -18.253  1.00 14.88           C  
ANISOU  249  CA  LEU B 346     1615   2024   2016   -257    151    331       C  
ATOM    250  C   LEU B 346       9.593 -30.154 -19.765  1.00 13.49           C  
ANISOU  250  C   LEU B 346     1425   1784   1916   -248    142    240       C  
ATOM    251  O   LEU B 346       9.654 -29.126 -20.434  1.00 14.42           O  
ANISOU  251  O   LEU B 346     1490   1970   2017   -221     84    166       O  
ATOM    252  CB  LEU B 346      10.768 -30.151 -17.562  1.00 17.62           C  
ANISOU  252  CB  LEU B 346     1990   2370   2337   -169    106    455       C  
ATOM    253  CG  LEU B 346      10.783 -29.825 -16.067  1.00 18.98           C  
ANISOU  253  CG  LEU B 346     2169   2652   2389   -185     89    541       C  
ATOM    254  CD1 LEU B 346      12.199 -29.846 -15.523  1.00 22.68           C  
ANISOU  254  CD1 LEU B 346     2640   3155   2823   -103     21    667       C  
ATOM    255  CD2 LEU B 346      10.130 -28.477 -15.814  1.00 22.20           C  
ANISOU  255  CD2 LEU B 346     2528   3191   2718   -220     70    429       C  
ATOM    256  N   THR B 347       9.694 -31.367 -20.295  1.00 14.42           N  
ANISOU  256  N   THR B 347     1599   1764   2114   -277    210    248       N  
ATOM    257  CA  THR B 347       9.851 -31.562 -21.731  1.00 14.20           C  
ANISOU  257  CA  THR B 347     1573   1678   2145   -296    221    148       C  
ATOM    258  C   THR B 347       8.599 -31.130 -22.493  1.00 16.64           C  
ANISOU  258  C   THR B 347     1820   2080   2422   -398    208     27       C  
ATOM    259  O   THR B 347       8.690 -30.458 -23.523  1.00 15.36           O  
ANISOU  259  O   THR B 347     1616   1974   2245   -391    155    -47       O  
ATOM    260  CB  THR B 347      10.175 -33.026 -22.052  1.00 17.75           C  
ANISOU  260  CB  THR B 347     2112   1940   2693   -319    328    167       C  
ATOM    261  OG1 THR B 347      11.437 -33.371 -21.463  1.00 17.35           O  
ANISOU  261  OG1 THR B 347     2094   1811   2686   -192    330    299       O  
ATOM    262  CG2 THR B 347      10.255 -33.239 -23.550  1.00 16.98           C  
ANISOU  262  CG2 THR B 347     2024   1793   2636   -368    357     36       C  
ATOM    263  N   ASN B 348       7.431 -31.507 -21.982  1.00 14.41           N  
ANISOU  263  N   ASN B 348     1522   1828   2125   -495    254     18       N  
ATOM    264  CA  ASN B 348       6.177 -31.113 -22.618  1.00 14.49           C  
ANISOU  264  CA  ASN B 348     1443   1957   2107   -589    235    -80       C  
ATOM    265  C   ASN B 348       5.989 -29.599 -22.572  1.00 15.25           C  
ANISOU  265  C   ASN B 348     1443   2198   2152   -508    145    -89       C  
ATOM    266  O   ASN B 348       5.503 -28.999 -23.529  1.00 14.43           O  
ANISOU  266  O   ASN B 348     1264   2185   2036   -523     92   -151       O  
ATOM    267  CB  ASN B 348       4.991 -31.813 -21.959  1.00 17.65           C  
ANISOU  267  CB  ASN B 348     1831   2373   2504   -712    312    -83       C  
ATOM    268  CG  ASN B 348       3.665 -31.350 -22.515  1.00 22.95           C  
ANISOU  268  CG  ASN B 348     2372   3202   3146   -801    284   -171       C  
ATOM    269  OD1 ASN B 348       3.070 -30.407 -22.006  1.00 20.15           O  
ANISOU  269  OD1 ASN B 348     1921   2974   2760   -756    250   -161       O  
ATOM    270  ND2 ASN B 348       3.206 -31.999 -23.579  1.00 29.80           N  
ANISOU  270  ND2 ASN B 348     3230   4070   4024   -930    303   -259       N  
ATOM    271  N   LEU B 349       6.386 -28.990 -21.457  1.00 13.84           N  
ANISOU  271  N   LEU B 349     1274   2041   1944   -426    132    -22       N  
ATOM    272  CA  LEU B 349       6.370 -27.539 -21.312  1.00 12.14           C  
ANISOU  272  CA  LEU B 349      996   1924   1694   -345     71    -35       C  
ATOM    273  C   LEU B 349       7.240 -26.862 -22.369  1.00 14.22           C  
ANISOU  273  C   LEU B 349     1262   2175   1964   -278      1    -56       C  
ATOM    274  O   LEU B 349       6.790 -25.962 -23.088  1.00 12.69           O  
ANISOU  274  O   LEU B 349     1002   2053   1766   -256    -46    -95       O  
ATOM    275  CB  LEU B 349       6.836 -27.151 -19.908  1.00 12.10           C  
ANISOU  275  CB  LEU B 349     1026   1931   1639   -298     84     27       C  
ATOM    276  CG  LEU B 349       6.988 -25.663 -19.596  1.00 14.91           C  
ANISOU  276  CG  LEU B 349     1348   2357   1959   -225     47      2       C  
ATOM    277  CD1 LEU B 349       5.663 -24.933 -19.740  1.00 14.56           C  
ANISOU  277  CD1 LEU B 349     1206   2396   1931   -229     67    -59       C  
ATOM    278  CD2 LEU B 349       7.560 -25.488 -18.190  1.00 15.22           C  
ANISOU  278  CD2 LEU B 349     1440   2418   1925   -217     65     52       C  
ATOM    279  N   ALA B 350       8.484 -27.315 -22.465  1.00 11.74           N  
ANISOU  279  N   ALA B 350     1021   1774   1666   -242     -2    -21       N  
ATOM    280  CA  ALA B 350       9.426 -26.783 -23.444  1.00 11.09           C  
ANISOU  280  CA  ALA B 350      947   1678   1590   -191    -52    -42       C  
ATOM    281  C   ALA B 350       8.942 -27.013 -24.878  1.00 14.42           C  
ANISOU  281  C   ALA B 350     1346   2113   2021   -255    -61   -114       C  
ATOM    282  O   ALA B 350       9.130 -26.160 -25.746  1.00 12.47           O  
ANISOU  282  O   ALA B 350     1074   1913   1752   -229   -115   -138       O  
ATOM    283  CB  ALA B 350      10.792 -27.404 -23.245  1.00 12.00           C  
ANISOU  283  CB  ALA B 350     1123   1704   1732   -144    -36     12       C  
ATOM    284  N   ASP B 351       8.316 -28.159 -25.123  1.00 12.34           N  
ANISOU  284  N   ASP B 351     1098   1812   1780   -352     -4   -147       N  
ATOM    285  CA  ASP B 351       7.764 -28.437 -26.446  1.00 14.05           C  
ANISOU  285  CA  ASP B 351     1290   2069   1981   -448    -11   -229       C  
ATOM    286  C   ASP B 351       6.772 -27.355 -26.844  1.00 15.16           C  
ANISOU  286  C   ASP B 351     1322   2365   2075   -447    -90   -239       C  
ATOM    287  O   ASP B 351       6.792 -26.873 -27.976  1.00 13.13           O  
ANISOU  287  O   ASP B 351     1037   2173   1778   -460   -146   -265       O  
ATOM    288  CB  ASP B 351       7.073 -29.797 -26.496  1.00 14.10           C  
ANISOU  288  CB  ASP B 351     1327   2021   2012   -583     73   -277       C  
ATOM    289  CG  ASP B 351       8.049 -30.959 -26.488  1.00 15.78           C  
ANISOU  289  CG  ASP B 351     1654   2052   2289   -583    167   -276       C  
ATOM    290  OD1 ASP B 351       9.268 -30.740 -26.655  1.00 17.92           O  
ANISOU  290  OD1 ASP B 351     1963   2263   2583   -485    158   -248       O  
ATOM    291  OD2 ASP B 351       7.585 -32.109 -26.335  1.00 21.24           O  
ANISOU  291  OD2 ASP B 351     2396   2655   3018   -685    259   -302       O  
ATOM    292  N   ARG B 352       5.911 -26.967 -25.908  1.00 12.25           N  
ANISOU  292  N   ARG B 352      888   2057   1710   -427    -87   -208       N  
ATOM    293  CA  ARG B 352       4.876 -25.987 -26.207  1.00 12.55           C  
ANISOU  293  CA  ARG B 352      833   2206   1728   -390   -142   -195       C  
ATOM    294  C   ARG B 352       5.446 -24.571 -26.249  1.00 13.68           C  
ANISOU  294  C   ARG B 352      986   2341   1870   -257   -192   -150       C  
ATOM    295  O   ARG B 352       4.990 -23.745 -27.038  1.00 12.82           O  
ANISOU  295  O   ARG B 352      855   2265   1752   -213   -241   -125       O  
ATOM    296  CB  ARG B 352       3.731 -26.087 -25.192  1.00 13.21           C  
ANISOU  296  CB  ARG B 352      851   2338   1829   -408    -96   -186       C  
ATOM    297  CG  ARG B 352       2.841 -27.306 -25.411  1.00 14.33           C  
ANISOU  297  CG  ARG B 352      981   2498   1965   -548    -52   -228       C  
ATOM    298  CD  ARG B 352       1.756 -27.433 -24.353  1.00 15.08           C  
ANISOU  298  CD  ARG B 352     1013   2642   2075   -573      4   -220       C  
ATOM    299  NE  ARG B 352       2.294 -27.911 -23.080  1.00 14.79           N  
ANISOU  299  NE  ARG B 352     1022   2547   2053   -601     84   -203       N  
ATOM    300  CZ  ARG B 352       2.307 -27.200 -21.958  1.00 14.52           C  
ANISOU  300  CZ  ARG B 352      969   2535   2014   -525    110   -170       C  
ATOM    301  NH1 ARG B 352       1.807 -25.972 -21.941  1.00 14.99           N  
ANISOU  301  NH1 ARG B 352      955   2660   2080   -421     76   -166       N  
ATOM    302  NH2 ARG B 352       2.822 -27.718 -20.851  1.00 14.49           N  
ANISOU  302  NH2 ARG B 352     1065   2448   1994   -532    171   -126       N  
ATOM    303  N   GLU B 353       6.447 -24.296 -25.417  1.00 12.52           N  
ANISOU  303  N   GLU B 353      876   2148   1733   -203   -176   -137       N  
ATOM    304  CA  GLU B 353       7.107 -22.995 -25.437  1.00 10.67           C  
ANISOU  304  CA  GLU B 353      670   1888   1495   -101   -209   -108       C  
ATOM    305  C   GLU B 353       7.794 -22.714 -26.770  1.00 14.26           C  
ANISOU  305  C   GLU B 353     1170   2318   1929    -97   -256   -104       C  
ATOM    306  O   GLU B 353       7.817 -21.571 -27.235  1.00 12.42           O  
ANISOU  306  O   GLU B 353      945   2080   1695    -38   -288    -73       O  
ATOM    307  CB  GLU B 353       8.135 -22.881 -24.313  1.00 10.23           C  
ANISOU  307  CB  GLU B 353      678   1775   1434    -65   -180    -94       C  
ATOM    308  CG  GLU B 353       7.552 -22.762 -22.917  1.00 11.08           C  
ANISOU  308  CG  GLU B 353      771   1902   1537    -60   -127    -90       C  
ATOM    309  CD  GLU B 353       8.643 -22.659 -21.868  1.00 17.89           C  
ANISOU  309  CD  GLU B 353     1706   2727   2364    -43   -113    -68       C  
ATOM    310  OE1 GLU B 353       9.193 -23.710 -21.484  1.00 15.01           O  
ANISOU  310  OE1 GLU B 353     1385   2329   1990    -75   -100    -32       O  
ATOM    311  OE2 GLU B 353       8.966 -21.526 -21.453  1.00 16.96           O  
ANISOU  311  OE2 GLU B 353     1602   2615   2229     -1   -113    -82       O  
ATOM    312  N   LEU B 354       8.354 -23.754 -27.382  1.00 12.90           N  
ANISOU  312  N   LEU B 354     1024   2133   1745   -169   -249   -141       N  
ATOM    313  CA  LEU B 354       9.121 -23.581 -28.608  1.00 16.70           C  
ANISOU  313  CA  LEU B 354     1547   2602   2195   -180   -277   -153       C  
ATOM    314  C   LEU B 354       8.232 -23.086 -29.743  1.00 14.47           C  
ANISOU  314  C   LEU B 354     1245   2377   1874   -196   -322   -134       C  
ATOM    315  O   LEU B 354       8.651 -22.268 -30.557  1.00 12.55           O  
ANISOU  315  O   LEU B 354     1027   2138   1602   -166   -357   -107       O  
ATOM    316  CB  LEU B 354       9.821 -24.890 -28.994  1.00 14.86           C  
ANISOU  316  CB  LEU B 354     1364   2312   1971   -254   -227   -210       C  
ATOM    317  CG  LEU B 354      10.682 -24.854 -30.268  1.00 15.02           C  
ANISOU  317  CG  LEU B 354     1425   2327   1954   -283   -232   -245       C  
ATOM    318  CD1 LEU B 354      11.874 -23.935 -30.083  1.00 13.60           C  
ANISOU  318  CD1 LEU B 354     1274   2113   1782   -195   -247   -206       C  
ATOM    319  CD2 LEU B 354      11.147 -26.246 -30.650  1.00 15.84           C  
ANISOU  319  CD2 LEU B 354     1589   2347   2084   -356   -147   -315       C  
ATOM    320  N   VAL B 355       6.992 -23.565 -29.780  1.00 14.21           N  
ANISOU  320  N   VAL B 355     1160   2401   1838   -245   -321   -143       N  
ATOM    321  CA  VAL B 355       6.046 -23.101 -30.785  1.00 13.47           C  
ANISOU  321  CA  VAL B 355     1024   2387   1707   -254   -372   -115       C  
ATOM    322  C   VAL B 355       5.830 -21.591 -30.677  1.00 13.23           C  
ANISOU  322  C   VAL B 355      966   2354   1705   -137   -410    -42       C  
ATOM    323  O   VAL B 355       5.848 -20.883 -31.685  1.00 14.73           O  
ANISOU  323  O   VAL B 355     1158   2578   1860   -117   -459     -2       O  
ATOM    324  CB  VAL B 355       4.699 -23.822 -30.661  1.00 18.64           C  
ANISOU  324  CB  VAL B 355     1608   3114   2359   -323   -362   -136       C  
ATOM    325  CG1 VAL B 355       3.773 -23.402 -31.789  1.00 19.51           C  
ANISOU  325  CG1 VAL B 355     1662   3333   2420   -339   -424   -103       C  
ATOM    326  CG2 VAL B 355       4.918 -25.326 -30.685  1.00 16.37           C  
ANISOU  326  CG2 VAL B 355     1361   2805   2055   -452   -305   -218       C  
ATOM    327  N   HIS B 356       5.643 -21.102 -29.455  1.00 11.94           N  
ANISOU  327  N   HIS B 356      780   2154   1604    -66   -380    -26       N  
ATOM    328  CA  HIS B 356       5.492 -19.667 -29.235  1.00 12.12           C  
ANISOU  328  CA  HIS B 356      779   2157   1669     43   -393     29       C  
ATOM    329  C   HIS B 356       6.787 -18.899 -29.504  1.00 13.35           C  
ANISOU  329  C   HIS B 356     1011   2249   1811     81   -404     44       C  
ATOM    330  O   HIS B 356       6.742 -17.747 -29.930  1.00 14.47           O  
ANISOU  330  O   HIS B 356     1146   2386   1966    152   -431     97       O  
ATOM    331  CB  HIS B 356       5.011 -19.394 -27.810  1.00 12.11           C  
ANISOU  331  CB  HIS B 356      735   2140   1728     96   -336     22       C  
ATOM    332  CG  HIS B 356       3.612 -19.854 -27.550  1.00 13.09           C  
ANISOU  332  CG  HIS B 356      764   2336   1875     73   -323     17       C  
ATOM    333  ND1 HIS B 356       2.513 -19.048 -27.747  1.00 20.83           N  
ANISOU  333  ND1 HIS B 356     1651   3361   2903    142   -339     59       N  
ATOM    334  CD2 HIS B 356       3.134 -21.043 -27.110  1.00 13.23           C  
ANISOU  334  CD2 HIS B 356      758   2392   1878    -14   -290    -24       C  
ATOM    335  CE1 HIS B 356       1.416 -19.719 -27.441  1.00 20.94           C  
ANISOU  335  CE1 HIS B 356     1582   3446   2927     96   -320     41       C  
ATOM    336  NE2 HIS B 356       1.767 -20.932 -27.054  1.00 15.17           N  
ANISOU  336  NE2 HIS B 356      898   2712   2155     -6   -289    -10       N  
ATOM    337  N   MET B 357       7.929 -19.538 -29.256  1.00 11.80           N  
ANISOU  337  N   MET B 357      881   2011   1593     37   -379      3       N  
ATOM    338  CA  MET B 357       9.227 -18.910 -29.497  1.00  9.50           C  
ANISOU  338  CA  MET B 357      652   1674   1284     57   -385      9       C  
ATOM    339  C   MET B 357       9.412 -18.570 -30.968  1.00  9.96           C  
ANISOU  339  C   MET B 357      728   1766   1289     36   -433     37       C  
ATOM    340  O   MET B 357      10.016 -17.552 -31.308  1.00 12.02           O  
ANISOU  340  O   MET B 357     1015   2011   1540     75   -451     76       O  
ATOM    341  CB  MET B 357      10.373 -19.816 -29.045  1.00  8.88           C  
ANISOU  341  CB  MET B 357      621   1560   1195     13   -351    -40       C  
ATOM    342  CG  MET B 357      11.727 -19.121 -29.071  1.00 12.55           C  
ANISOU  342  CG  MET B 357     1133   1989   1647     32   -350    -41       C  
ATOM    343  SD  MET B 357      13.110 -20.246 -28.859  1.00 13.59           S  
ANISOU  343  SD  MET B 357     1293   2095   1776     -8   -319    -87       S  
ATOM    344  CE  MET B 357      12.752 -20.917 -27.239  1.00 10.20           C  
ANISOU  344  CE  MET B 357      839   1656   1379     10   -289    -89       C  
ATOM    345  N   ILE B 358       8.905 -19.429 -31.842  1.00 11.72           N  
ANISOU  345  N   ILE B 358      938   2049   1468    -37   -450     18       N  
ATOM    346  CA  ILE B 358       9.043 -19.190 -33.273  1.00 14.69           C  
ANISOU  346  CA  ILE B 358     1332   2483   1768    -75   -491     42       C  
ATOM    347  C   ILE B 358       8.229 -17.958 -33.665  1.00 15.63           C  
ANISOU  347  C   ILE B 358     1409   2640   1891      1   -543    136       C  
ATOM    348  O   ILE B 358       8.693 -17.119 -34.438  1.00 14.63           O  
ANISOU  348  O   ILE B 358     1312   2523   1722     19   -573    196       O  
ATOM    349  CB  ILE B 358       8.621 -20.430 -34.104  1.00 18.48           C  
ANISOU  349  CB  ILE B 358     1804   3034   2185   -188   -489    -12       C  
ATOM    350  CG1 ILE B 358       9.818 -21.374 -34.311  1.00 20.29           C  
ANISOU  350  CG1 ILE B 358     2094   3227   2388   -264   -437    -93       C  
ATOM    351  CG2 ILE B 358       8.088 -20.019 -35.474  1.00 18.60           C  
ANISOU  351  CG2 ILE B 358     1801   3151   2113   -222   -544     38       C  
ATOM    352  CD1 ILE B 358      10.610 -21.734 -33.058  1.00 23.49           C  
ANISOU  352  CD1 ILE B 358     2514   3544   2868   -227   -388   -126       C  
ATOM    353  N   ASN B 359       7.030 -17.830 -33.107  1.00 15.34           N  
ANISOU  353  N   ASN B 359     1298   2623   1908     50   -548    157       N  
ATOM    354  CA  ASN B 359       6.218 -16.638 -33.345  1.00 14.43           C  
ANISOU  354  CA  ASN B 359     1129   2531   1821    148   -586    253       C  
ATOM    355  C   ASN B 359       6.916 -15.377 -32.854  1.00 17.75           C  
ANISOU  355  C   ASN B 359     1591   2858   2296    250   -564    303       C  
ATOM    356  O   ASN B 359       6.888 -14.344 -33.522  1.00 17.34           O  
ANISOU  356  O   ASN B 359     1548   2803   2238    312   -595    401       O  
ATOM    357  CB  ASN B 359       4.854 -16.760 -32.672  1.00 19.75           C  
ANISOU  357  CB  ASN B 359     1704   3240   2561    186   -578    254       C  
ATOM    358  CG  ASN B 359       3.959 -17.763 -33.352  1.00 28.70           C  
ANISOU  358  CG  ASN B 359     2780   4491   3636     91   -611    234       C  
ATOM    359  OD1 ASN B 359       4.136 -18.081 -34.530  1.00 37.22           O  
ANISOU  359  OD1 ASN B 359     3879   5641   4620     15   -652    243       O  
ATOM    360  ND2 ASN B 359       2.971 -18.254 -32.619  1.00 33.57           N  
ANISOU  360  ND2 ASN B 359     3318   5138   4300     85   -588    205       N  
ATOM    361  N   TRP B 360       7.538 -15.474 -31.683  1.00 15.12           N  
ANISOU  361  N   TRP B 360     1283   2449   2011    262   -507    244       N  
ATOM    362  CA  TRP B 360       8.257 -14.351 -31.096  1.00 15.63           C  
ANISOU  362  CA  TRP B 360     1385   2426   2126    346   -472    280       C  
ATOM    363  C   TRP B 360       9.425 -13.951 -31.990  1.00 17.73           C  
ANISOU  363  C   TRP B 360     1725   2681   2331    311   -500    326       C  
ATOM    364  O   TRP B 360       9.623 -12.772 -32.285  1.00 16.65           O  
ANISOU  364  O   TRP B 360     1639   2465   2222    373   -488    405       O  
ATOM    365  CB  TRP B 360       8.760 -14.706 -29.693  1.00 12.87           C  
ANISOU  365  CB  TRP B 360     1046   2034   1811    338   -407    195       C  
ATOM    366  CG  TRP B 360       9.882 -13.837 -29.224  1.00 12.24           C  
ANISOU  366  CG  TRP B 360     1078   1825   1746    341   -348    166       C  
ATOM    367  CD1 TRP B 360       9.785 -12.583 -28.695  1.00 15.10           C  
ANISOU  367  CD1 TRP B 360     1484   2076   2179    417   -282    179       C  
ATOM    368  CD2 TRP B 360      11.280 -14.153 -29.258  1.00 12.36           C  
ANISOU  368  CD2 TRP B 360     1172   1814   1708    255   -340    112       C  
ATOM    369  NE1 TRP B 360      11.039 -12.100 -28.392  1.00 14.54           N  
ANISOU  369  NE1 TRP B 360     1520   1917   2088    360   -237    128       N  
ATOM    370  CE2 TRP B 360      11.972 -13.044 -28.726  1.00 13.54           C  
ANISOU  370  CE2 TRP B 360     1405   1855   1886    265   -279     92       C  
ATOM    371  CE3 TRP B 360      12.012 -15.266 -29.682  1.00 13.47           C  
ANISOU  371  CE3 TRP B 360     1316   2011   1788    170   -367     74       C  
ATOM    372  CZ2 TRP B 360      13.362 -13.017 -28.613  1.00 12.84           C  
ANISOU  372  CZ2 TRP B 360     1383   1740   1757    185   -261     42       C  
ATOM    373  CZ3 TRP B 360      13.391 -15.239 -29.563  1.00 14.46           C  
ANISOU  373  CZ3 TRP B 360     1505   2100   1890    117   -342     32       C  
ATOM    374  CH2 TRP B 360      14.052 -14.120 -29.033  1.00 13.83           C  
ANISOU  374  CH2 TRP B 360     1488   1939   1829    120   -298     20       C  
ATOM    375  N   ALA B 361      10.188 -14.951 -32.418  1.00 15.31           N  
ANISOU  375  N   ALA B 361     1452   2416   1948    199   -511    256       N  
ATOM    376  CA  ALA B 361      11.368 -14.738 -33.244  1.00 15.82           C  
ANISOU  376  CA  ALA B 361     1598   2465   1947    136   -513    262       C  
ATOM    377  C   ALA B 361      11.020 -13.970 -34.513  1.00 15.76           C  
ANISOU  377  C   ALA B 361     1595   2509   1885    152   -574    387       C  
ATOM    378  O   ALA B 361      11.744 -13.063 -34.932  1.00 15.60           O  
ANISOU  378  O   ALA B 361     1658   2417   1852    154   -554    437       O  
ATOM    379  CB  ALA B 361      12.009 -16.071 -33.589  1.00 12.78           C  
ANISOU  379  CB  ALA B 361     1221   2136   1501     27   -508    169       C  
ATOM    380  N   LYS B 362       9.894 -14.326 -35.117  1.00 14.70           N  
ANISOU  380  N   LYS B 362     1407   2454   1724    150   -610    403       N  
ATOM    381  CA  LYS B 362       9.481 -13.693 -36.360  1.00 16.99           C  
ANISOU  381  CA  LYS B 362     1702   2803   1950    156   -663    515       C  
ATOM    382  C   LYS B 362       9.088 -12.235 -36.157  1.00 16.80           C  
ANISOU  382  C   LYS B 362     1681   2696   2007    296   -664    650       C  
ATOM    383  O   LYS B 362       8.985 -11.483 -37.119  1.00 20.01           O  
ANISOU  383  O   LYS B 362     2115   3118   2371    317   -699    769       O  
ATOM    384  CB  LYS B 362       8.329 -14.470 -36.999  1.00 17.61           C  
ANISOU  384  CB  LYS B 362     1709   3001   1981    109   -703    497       C  
ATOM    385  CG  LYS B 362       8.716 -15.873 -37.452  1.00 22.04           C  
ANISOU  385  CG  LYS B 362     2288   3625   2462    -34   -685    378       C  
ATOM    386  CD  LYS B 362       7.518 -16.629 -38.003  1.00 24.07           C  
ANISOU  386  CD  LYS B 362     2472   3998   2675    -92   -719    364       C  
ATOM    387  CE  LYS B 362       6.949 -15.933 -39.230  1.00 30.53           C  
ANISOU  387  CE  LYS B 362     3264   4925   3413    -91   -790    485       C  
ATOM    388  NZ  LYS B 362       5.615 -16.469 -39.620  1.00 37.17           N  
ANISOU  388  NZ  LYS B 362     4007   5895   4222   -129   -834    492       N  
ATOM    389  N   ARG B 363       8.891 -11.835 -34.905  1.00 15.85           N  
ANISOU  389  N   ARG B 363     1540   2474   2007    392   -611    632       N  
ATOM    390  CA  ARG B 363       8.494 -10.466 -34.605  1.00 17.03           C  
ANISOU  390  CA  ARG B 363     1704   2502   2264    535   -575    741       C  
ATOM    391  C   ARG B 363       9.660  -9.626 -34.082  1.00 20.43           C  
ANISOU  391  C   ARG B 363     2254   2759   2751    549   -494    743       C  
ATOM    392  O   ARG B 363       9.516  -8.424 -33.847  1.00 25.08           O  
ANISOU  392  O   ARG B 363     2895   3195   3439    653   -430    816       O  
ATOM    393  CB  ARG B 363       7.354 -10.458 -33.595  1.00 22.56           C  
ANISOU  393  CB  ARG B 363     2318   3184   3071    625   -535    698       C  
ATOM    394  CG  ARG B 363       6.103 -11.154 -34.088  1.00 24.29           C  
ANISOU  394  CG  ARG B 363     2431   3550   3250    600   -600    691       C  
ATOM    395  CD  ARG B 363       4.986 -10.977 -33.090  1.00 27.35           C  
ANISOU  395  CD  ARG B 363     2730   3914   3749    694   -553    666       C  
ATOM    396  NE  ARG B 363       4.626  -9.572 -32.949  1.00 31.35           N  
ANISOU  396  NE  ARG B 363     3247   4300   4363    845   -506    765       N  
ATOM    397  CZ  ARG B 363       3.650  -9.129 -32.168  1.00 33.53           C  
ANISOU  397  CZ  ARG B 363     3453   4536   4752    951   -448    758       C  
ATOM    398  NH1 ARG B 363       2.936  -9.979 -31.441  1.00 33.76           N  
ANISOU  398  NH1 ARG B 363     3389   4646   4792    917   -437    662       N  
ATOM    399  NH2 ARG B 363       3.397  -7.833 -32.109  1.00 35.19           N  
ANISOU  399  NH2 ARG B 363     3691   4615   5067   1086   -389    844       N  
ATOM    400  N   VAL B 364      10.811 -10.257 -33.888  1.00 18.26           N  
ANISOU  400  N   VAL B 364     2045   2481   2412    419   -467    613       N  
ATOM    401  CA  VAL B 364      12.015  -9.516 -33.549  1.00 18.22           C  
ANISOU  401  CA  VAL B 364     2170   2327   2426    373   -381    562       C  
ATOM    402  C   VAL B 364      12.449  -8.769 -34.799  1.00 20.06           C  
ANISOU  402  C   VAL B 364     2482   2539   2601    350   -401    686       C  
ATOM    403  O   VAL B 364      12.706  -9.400 -35.827  1.00 19.94           O  
ANISOU  403  O   VAL B 364     2453   2655   2468    266   -468    709       O  
ATOM    404  CB  VAL B 364      13.155 -10.432 -33.074  1.00 14.44           C  
ANISOU  404  CB  VAL B 364     1711   1881   1893    247   -358    411       C  
ATOM    405  CG1 VAL B 364      14.458  -9.643 -32.974  1.00 16.17           C  
ANISOU  405  CG1 VAL B 364     2045   1990   2109    175   -286    373       C  
ATOM    406  CG2 VAL B 364      12.800 -11.111 -31.754  1.00 14.64           C  
ANISOU  406  CG2 VAL B 364     1676   1918   1967    265   -333    306       C  
ATOM    407  N   PRO B 365      12.502  -7.429 -34.733  1.00 19.57           N  
ANISOU  407  N   PRO B 365     2509   2308   2618    417   -334    768       N  
ATOM    408  CA  PRO B 365      12.824  -6.625 -35.915  1.00 21.80           C  
ANISOU  408  CA  PRO B 365     2878   2555   2851    404   -347    917       C  
ATOM    409  C   PRO B 365      14.095  -7.084 -36.615  1.00 20.12           C  
ANISOU  409  C   PRO B 365     2725   2413   2506    234   -352    854       C  
ATOM    410  O   PRO B 365      15.123  -7.262 -35.966  1.00 23.88           O  
ANISOU  410  O   PRO B 365     3242   2843   2987    140   -284    709       O  
ATOM    411  CB  PRO B 365      12.994  -5.221 -35.337  1.00 24.97           C  
ANISOU  411  CB  PRO B 365     3396   2710   3382    469   -224    946       C  
ATOM    412  CG  PRO B 365      12.049  -5.202 -34.195  1.00 23.30           C  
ANISOU  412  CG  PRO B 365     3110   2446   3296    592   -184    892       C  
ATOM    413  CD  PRO B 365      12.171  -6.576 -33.577  1.00 20.84           C  
ANISOU  413  CD  PRO B 365     2704   2293   2923    510   -229    731       C  
ATOM    414  N   GLY B 366      14.012  -7.303 -37.921  1.00 22.81           N  
ANISOU  414  N   GLY B 366     3060   2884   2724    190   -431    963       N  
ATOM    415  CA  GLY B 366      15.168  -7.722 -38.687  1.00 23.85           C  
ANISOU  415  CA  GLY B 366     3245   3088   2727     29   -419    904       C  
ATOM    416  C   GLY B 366      15.273  -9.218 -38.917  1.00 24.29           C  
ANISOU  416  C   GLY B 366     3214   3327   2690    -58   -468    781       C  
ATOM    417  O   GLY B 366      15.936  -9.653 -39.857  1.00 24.20           O  
ANISOU  417  O   GLY B 366     3229   3413   2553   -178   -471    759       O  
ATOM    418  N   PHE B 367      14.620 -10.011 -38.073  1.00 21.40           N  
ANISOU  418  N   PHE B 367     2750   2996   2384     -4   -492    698       N  
ATOM    419  CA  PHE B 367      14.772 -11.463 -38.140  1.00 17.71           C  
ANISOU  419  CA  PHE B 367     2216   2659   1855    -86   -512    568       C  
ATOM    420  C   PHE B 367      14.178 -12.079 -39.413  1.00 17.31           C  
ANISOU  420  C   PHE B 367     2125   2789   1663   -151   -596    621       C  
ATOM    421  O   PHE B 367      14.803 -12.936 -40.032  1.00 18.35           O  
ANISOU  421  O   PHE B 367     2269   3005   1699   -271   -577    527       O  
ATOM    422  CB  PHE B 367      14.148 -12.129 -36.909  1.00 16.56           C  
ANISOU  422  CB  PHE B 367     1986   2499   1807    -18   -511    482       C  
ATOM    423  CG  PHE B 367      14.424 -13.607 -36.813  1.00 16.23           C  
ANISOU  423  CG  PHE B 367     1895   2541   1729    -97   -506    348       C  
ATOM    424  CD1 PHE B 367      15.656 -14.069 -36.383  1.00 16.50           C  
ANISOU  424  CD1 PHE B 367     1958   2530   1780   -153   -435    235       C  
ATOM    425  CD2 PHE B 367      13.454 -14.533 -37.151  1.00 16.74           C  
ANISOU  425  CD2 PHE B 367     1882   2728   1750   -116   -565    338       C  
ATOM    426  CE1 PHE B 367      15.916 -15.431 -36.295  1.00 13.59           C  
ANISOU  426  CE1 PHE B 367     1550   2213   1402   -204   -415    127       C  
ATOM    427  CE2 PHE B 367      13.706 -15.897 -37.061  1.00 14.31           C  
ANISOU  427  CE2 PHE B 367     1548   2464   1423   -191   -538    211       C  
ATOM    428  CZ  PHE B 367      14.938 -16.341 -36.632  1.00 12.69           C  
ANISOU  428  CZ  PHE B 367     1381   2188   1252   -224   -459    112       C  
ATOM    429  N   VAL B 368      12.983 -11.657 -39.813  1.00 18.57           N  
ANISOU  429  N   VAL B 368     2233   3012   1811    -75   -678    761       N  
ATOM    430  CA  VAL B 368      12.369 -12.270 -40.991  1.00 20.89           C  
ANISOU  430  CA  VAL B 368     2488   3450   1999   -145   -717    748       C  
ATOM    431  C   VAL B 368      12.923 -11.694 -42.292  1.00 22.91           C  
ANISOU  431  C   VAL B 368     2826   3750   2127   -224   -721    837       C  
ATOM    432  O   VAL B 368      12.537 -12.126 -43.378  1.00 25.86           O  
ANISOU  432  O   VAL B 368     3179   4252   2395   -302   -752    834       O  
ATOM    433  CB  VAL B 368      10.833 -12.126 -40.988  1.00 24.96           C  
ANISOU  433  CB  VAL B 368     2907   4010   2566    -45   -774    816       C  
ATOM    434  CG1 VAL B 368      10.243 -12.866 -39.804  1.00 25.47           C  
ANISOU  434  CG1 VAL B 368     2893   4049   2736      1   -755    709       C  
ATOM    435  CG2 VAL B 368      10.422 -10.662 -40.981  1.00 24.89           C  
ANISOU  435  CG2 VAL B 368     2920   3913   2625     95   -792    995       C  
ATOM    436  N   ASP B 369      13.832 -10.728 -42.181  1.00 20.94           N  
ANISOU  436  N   ASP B 369     2678   3392   1887   -218   -683    914       N  
ATOM    437  CA  ASP B 369      14.554 -10.221 -43.343  1.00 24.25           C  
ANISOU  437  CA  ASP B 369     3192   3837   2183   -314   -661    980       C  
ATOM    438  C   ASP B 369      15.559 -11.260 -43.814  1.00 23.34           C  
ANISOU  438  C   ASP B 369     3100   3809   1961   -483   -604    814       C  
ATOM    439  O   ASP B 369      16.008 -11.237 -44.958  1.00 23.34           O  
ANISOU  439  O   ASP B 369     3149   3880   1840   -590   -583    820       O  
ATOM    440  CB  ASP B 369      15.281  -8.912 -43.023  1.00 27.72           C  
ANISOU  440  CB  ASP B 369     3750   4106   2676   -279   -607   1097       C  
ATOM    441  CG  ASP B 369      14.333  -7.775 -42.705  1.00 32.86           C  
ANISOU  441  CG  ASP B 369     4399   4638   3450   -102   -631   1263       C  
ATOM    442  OD1 ASP B 369      13.250  -7.709 -43.320  1.00 37.32           O  
ANISOU  442  OD1 ASP B 369     4896   5290   3994    -32   -701   1339       O  
ATOM    443  OD2 ASP B 369      14.683  -6.937 -41.848  1.00 34.58           O  
ANISOU  443  OD2 ASP B 369     4684   4662   3793    -39   -566   1303       O  
ATOM    444  N   LEU B 370      15.912 -12.168 -42.911  1.00 19.63           N  
ANISOU  444  N   LEU B 370     2591   3322   1547   -498   -570    662       N  
ATOM    445  CA  LEU B 370      16.893 -13.207 -43.196  1.00 17.84           C  
ANISOU  445  CA  LEU B 370     2376   3146   1258   -629   -490    487       C  
ATOM    446  C   LEU B 370      16.283 -14.323 -44.031  1.00 18.49           C  
ANISOU  446  C   LEU B 370     2403   3343   1280   -697   -496    401       C  
ATOM    447  O   LEU B 370      15.063 -14.481 -44.068  1.00 21.42           O  
ANISOU  447  O   LEU B 370     2708   3760   1671   -642   -567    448       O  
ATOM    448  CB  LEU B 370      17.442 -13.780 -41.890  1.00 16.12           C  
ANISOU  448  CB  LEU B 370     2118   2816   1192   -576   -423    345       C  
ATOM    449  CG  LEU B 370      18.163 -12.794 -40.961  1.00 15.54           C  
ANISOU  449  CG  LEU B 370     2081   2580   1242   -509   -368    365       C  
ATOM    450  CD1 LEU B 370      18.474 -13.450 -39.627  1.00 14.08           C  
ANISOU  450  CD1 LEU B 370     1834   2323   1190   -453   -329    241       C  
ATOM    451  CD2 LEU B 370      19.435 -12.251 -41.604  1.00 20.76           C  
ANISOU  451  CD2 LEU B 370     2820   3224   1843   -611   -287    359       C  
ATOM    452  N   THR B 371      17.132 -15.101 -44.694  1.00 18.67           N  
ANISOU  452  N   THR B 371     2453   3407   1232   -822   -409    271       N  
ATOM    453  CA  THR B 371      16.665 -16.295 -45.391  1.00 19.34           C  
ANISOU  453  CA  THR B 371     2501   3577   1269   -906   -387    167       C  
ATOM    454  C   THR B 371      16.083 -17.272 -44.379  1.00 18.18           C  
ANISOU  454  C   THR B 371     2287   3386   1233   -844   -386     77       C  
ATOM    455  O   THR B 371      16.476 -17.268 -43.214  1.00 16.76           O  
ANISOU  455  O   THR B 371     2095   3113   1160   -765   -370     45       O  
ATOM    456  CB  THR B 371      17.800 -16.987 -46.168  1.00 19.81           C  
ANISOU  456  CB  THR B 371     2605   3659   1262  -1042   -263     28       C  
ATOM    457  OG1 THR B 371      18.750 -17.525 -45.236  1.00 19.97           O  
ANISOU  457  OG1 THR B 371     2620   3586   1382  -1012   -172    -96       O  
ATOM    458  CG2 THR B 371      18.493 -16.005 -47.104  1.00 20.97           C  
ANISOU  458  CG2 THR B 371     2822   3840   1304  -1111   -248    110       C  
ATOM    459  N   LEU B 372      15.146 -18.108 -44.806  1.00 18.28           N  
ANISOU  459  N   LEU B 372     2259   3471   1218   -890   -402     38       N  
ATOM    460  CA  LEU B 372      14.595 -19.085 -43.885  1.00 17.38           C  
ANISOU  460  CA  LEU B 372     2093   3307   1203   -847   -387    -46       C  
ATOM    461  C   LEU B 372      15.667 -20.057 -43.375  1.00 18.09           C  
ANISOU  461  C   LEU B 372     2208   3306   1358   -871   -269   -203       C  
ATOM    462  O   LEU B 372      15.642 -20.438 -42.208  1.00 15.95           O  
ANISOU  462  O   LEU B 372     1908   2950   1203   -791   -261   -239       O  
ATOM    463  CB  LEU B 372      13.414 -19.828 -44.518  1.00 18.66           C  
ANISOU  463  CB  LEU B 372     2212   3571   1307   -919   -414    -64       C  
ATOM    464  CG  LEU B 372      12.126 -19.181 -43.989  1.00 32.63           C  
ANISOU  464  CG  LEU B 372     3907   5364   3125   -809   -526     62       C  
ATOM    465  CD1 LEU B 372      10.922 -19.361 -44.895  1.00 37.54           C  
ANISOU  465  CD1 LEU B 372     4476   6136   3653   -880   -587    107       C  
ATOM    466  CD2 LEU B 372      11.841 -19.749 -42.611  1.00 30.17           C  
ANISOU  466  CD2 LEU B 372     3560   4954   2952   -725   -507      3       C  
ATOM    467  N   HIS B 373      16.634 -20.414 -44.214  1.00 20.01           N  
ANISOU  467  N   HIS B 373     2501   3566   1537   -973   -171   -290       N  
ATOM    468  CA  HIS B 373      17.748 -21.235 -43.737  1.00 19.25           C  
ANISOU  468  CA  HIS B 373     2418   3376   1519   -974    -47   -431       C  
ATOM    469  C   HIS B 373      18.501 -20.569 -42.587  1.00 17.98           C  
ANISOU  469  C   HIS B 373     2242   3137   1453   -868    -61   -402       C  
ATOM    470  O   HIS B 373      18.818 -21.208 -41.580  1.00 15.60           O  
ANISOU  470  O   HIS B 373     1909   2752   1267   -808    -21   -475       O  
ATOM    471  CB  HIS B 373      18.734 -21.538 -44.862  1.00 22.77           C  
ANISOU  471  CB  HIS B 373     2910   3850   1890  -1091     72   -522       C  
ATOM    472  CG  HIS B 373      20.039 -22.084 -44.372  1.00 27.47           C  
ANISOU  472  CG  HIS B 373     3505   4350   2583  -1064    205   -646       C  
ATOM    473  ND1 HIS B 373      20.188 -23.387 -43.949  1.00 32.59           N  
ANISOU  473  ND1 HIS B 373     4140   4908   3335  -1049    308   -777       N  
ATOM    474  CD2 HIS B 373      21.248 -21.495 -44.206  1.00 29.41           C  
ANISOU  474  CD2 HIS B 373     3752   4574   2848  -1042    258   -654       C  
ATOM    475  CE1 HIS B 373      21.435 -23.583 -43.560  1.00 32.73           C  
ANISOU  475  CE1 HIS B 373     4142   4851   3442  -1001    418   -855       C  
ATOM    476  NE2 HIS B 373      22.099 -22.450 -43.705  1.00 33.12           N  
ANISOU  476  NE2 HIS B 373     4193   4953   3437  -1001    390   -788       N  
ATOM    477  N   ASP B 374      18.799 -19.283 -42.737  1.00 17.63           N  
ANISOU  477  N   ASP B 374     2221   3119   1358   -855   -115   -293       N  
ATOM    478  CA  ASP B 374      19.542 -18.581 -41.700  1.00 15.77           C  
ANISOU  478  CA  ASP B 374     1970   2794   1227   -761   -113   -256       C  
ATOM    479  C   ASP B 374      18.701 -18.395 -40.435  1.00 13.68           C  
ANISOU  479  C   ASP B 374     1656   2465   1077   -636   -195   -191       C  
ATOM    480  O   ASP B 374      19.239 -18.413 -39.328  1.00 14.59           O  
ANISOU  480  O   ASP B 374     1738   2488   1319   -552   -166   -207       O  
ATOM    481  CB  ASP B 374      20.051 -17.238 -42.218  1.00 16.00           C  
ANISOU  481  CB  ASP B 374     2053   2839   1187   -788   -127   -153       C  
ATOM    482  CG  ASP B 374      21.261 -17.390 -43.122  1.00 19.78           C  
ANISOU  482  CG  ASP B 374     2567   3355   1593   -897    -10   -234       C  
ATOM    483  OD1 ASP B 374      21.838 -18.498 -43.169  1.00 20.50           O  
ANISOU  483  OD1 ASP B 374     2630   3435   1726   -922     93   -375       O  
ATOM    484  OD2 ASP B 374      21.648 -16.403 -43.782  1.00 21.44           O  
ANISOU  484  OD2 ASP B 374     2836   3597   1715   -957     -9   -155       O  
ATOM    485  N   GLN B 375      17.387 -18.230 -40.597  1.00 14.60           N  
ANISOU  485  N   GLN B 375     1758   2648   1143   -630   -294   -118       N  
ATOM    486  CA  GLN B 375      16.483 -18.178 -39.447  1.00 13.04           C  
ANISOU  486  CA  GLN B 375     1504   2401   1049   -521   -354    -73       C  
ATOM    487  C   GLN B 375      16.500 -19.489 -38.671  1.00 12.39           C  
ANISOU  487  C   GLN B 375     1383   2265   1058   -507   -299   -185       C  
ATOM    488  O   GLN B 375      16.548 -19.492 -37.436  1.00 12.81           O  
ANISOU  488  O   GLN B 375     1406   2235   1227   -414   -295   -177       O  
ATOM    489  CB  GLN B 375      15.050 -17.868 -39.877  1.00 13.92           C  
ANISOU  489  CB  GLN B 375     1587   2578   1122   -499   -439     23       C  
ATOM    490  CG  GLN B 375      14.849 -16.508 -40.496  1.00 14.70           C  
ANISOU  490  CG  GLN B 375     1715   2713   1157   -477   -503    171       C  
ATOM    491  CD  GLN B 375      13.428 -16.308 -40.980  1.00 15.82           C  
ANISOU  491  CD  GLN B 375     1808   2924   1278   -443   -576    262       C  
ATOM    492  OE1 GLN B 375      12.474 -16.774 -40.356  1.00 21.46           O  
ANISOU  492  OE1 GLN B 375     2458   3634   2063   -391   -594    242       O  
ATOM    493  NE2 GLN B 375      13.277 -15.607 -42.093  1.00 17.22           N  
ANISOU  493  NE2 GLN B 375     2013   3173   1357   -476   -615    364       N  
ATOM    494  N   VAL B 376      16.451 -20.603 -39.394  1.00 13.80           N  
ANISOU  494  N   VAL B 376     1576   2478   1190   -599   -242   -283       N  
ATOM    495  CA  VAL B 376      16.500 -21.906 -38.749  1.00 15.52           C  
ANISOU  495  CA  VAL B 376     1773   2630   1493   -599   -176   -390       C  
ATOM    496  C   VAL B 376      17.829 -22.077 -38.022  1.00 13.50           C  
ANISOU  496  C   VAL B 376     1514   2263   1354   -520    -90   -418       C  
ATOM    497  O   VAL B 376      17.866 -22.533 -36.878  1.00 14.81           O  
ANISOU  497  O   VAL B 376     1645   2348   1633   -437    -77   -413       O  
ATOM    498  CB  VAL B 376      16.312 -23.055 -39.751  1.00 14.48           C  
ANISOU  498  CB  VAL B 376     1678   2522   1303   -713    -95   -495       C  
ATOM    499  CG1 VAL B 376      16.412 -24.395 -39.040  1.00 17.45           C  
ANISOU  499  CG1 VAL B 376     2048   2796   1785   -713     -8   -607       C  
ATOM    500  CG2 VAL B 376      14.973 -22.930 -40.456  1.00 18.25           C  
ANISOU  500  CG2 VAL B 376     2145   3095   1692   -758   -166   -431       C  
ATOM    501  N   HIS B 377      18.921 -21.690 -38.671  1.00 12.83           N  
ANISOU  501  N   HIS B 377     1452   2188   1233   -551    -35   -438       N  
ATOM    502  CA  HIS B 377      20.229 -21.829 -38.047  1.00 12.50           C  
ANISOU  502  CA  HIS B 377     1379   2072   1298   -482     41   -459       C  
ATOM    503  C   HIS B 377      20.330 -21.041 -36.747  1.00 11.51           C  
ANISOU  503  C   HIS B 377     1214   1911   1249   -381    -27   -368       C  
ATOM    504  O   HIS B 377      20.864 -21.538 -35.756  1.00 12.25           O  
ANISOU  504  O   HIS B 377     1259   1950   1446   -305      0   -370       O  
ATOM    505  CB  HIS B 377      21.340 -21.376 -38.985  1.00 17.10           C  
ANISOU  505  CB  HIS B 377     1982   2694   1821   -546    108   -490       C  
ATOM    506  CG  HIS B 377      22.700 -21.455 -38.369  1.00 21.18           C  
ANISOU  506  CG  HIS B 377     2436   3164   2445   -478    179   -504       C  
ATOM    507  ND1 HIS B 377      23.379 -22.646 -38.220  1.00 24.77           N  
ANISOU  507  ND1 HIS B 377     2849   3562   3002   -435    289   -581       N  
ATOM    508  CD2 HIS B 377      23.491 -20.500 -37.827  1.00 22.59           C  
ANISOU  508  CD2 HIS B 377     2579   3352   2651   -447    155   -446       C  
ATOM    509  CE1 HIS B 377      24.540 -22.416 -37.633  1.00 26.19           C  
ANISOU  509  CE1 HIS B 377     2950   3737   3263   -371    317   -557       C  
ATOM    510  NE2 HIS B 377      24.634 -21.123 -37.385  1.00 23.91           N  
ANISOU  510  NE2 HIS B 377     2665   3498   2923   -391    235   -484       N  
ATOM    511  N   LEU B 378      19.827 -19.809 -36.754  1.00 12.24           N  
ANISOU  511  N   LEU B 378     1329   2034   1287   -381   -109   -285       N  
ATOM    512  CA  LEU B 378      19.872 -18.979 -35.553  1.00 13.16           C  
ANISOU  512  CA  LEU B 378     1424   2110   1464   -306   -156   -221       C  
ATOM    513  C   LEU B 378      19.050 -19.590 -34.423  1.00 10.11           C  
ANISOU  513  C   LEU B 378     1002   1691   1147   -238   -187   -213       C  
ATOM    514  O   LEU B 378      19.504 -19.644 -33.277  1.00 11.95           O  
ANISOU  514  O   LEU B 378     1201   1892   1448   -183   -183   -203       O  
ATOM    515  CB  LEU B 378      19.384 -17.564 -35.852  1.00 13.61           C  
ANISOU  515  CB  LEU B 378     1528   2178   1466   -314   -214   -137       C  
ATOM    516  CG  LEU B 378      20.329 -16.705 -36.696  1.00 13.80           C  
ANISOU  516  CG  LEU B 378     1598   2215   1429   -382   -179   -122       C  
ATOM    517  CD1 LEU B 378      19.740 -15.312 -36.899  1.00 16.21           C  
ANISOU  517  CD1 LEU B 378     1962   2497   1699   -372   -231    -17       C  
ATOM    518  CD2 LEU B 378      21.727 -16.632 -36.082  1.00 14.77           C  
ANISOU  518  CD2 LEU B 378     1686   2317   1611   -386   -120   -167       C  
ATOM    519  N   LEU B 379      17.846 -20.057 -34.740  1.00 10.18           N  
ANISOU  519  N   LEU B 379     1016   1725   1128   -255   -219   -214       N  
ATOM    520  CA  LEU B 379      16.996 -20.652 -33.714  1.00 10.17           C  
ANISOU  520  CA  LEU B 379      981   1698   1186   -207   -238   -208       C  
ATOM    521  C   LEU B 379      17.553 -21.983 -33.208  1.00 13.24           C  
ANISOU  521  C   LEU B 379     1353   2030   1648   -190   -168   -259       C  
ATOM    522  O   LEU B 379      17.503 -22.263 -32.010  1.00 13.28           O  
ANISOU  522  O   LEU B 379     1332   1998   1715   -131   -172   -231       O  
ATOM    523  CB  LEU B 379      15.572 -20.825 -34.242  1.00 17.11           C  
ANISOU  523  CB  LEU B 379     1851   2637   2014   -245   -287   -198       C  
ATOM    524  CG  LEU B 379      14.725 -19.588 -33.949  1.00 22.25           C  
ANISOU  524  CG  LEU B 379     2484   3312   2656   -191   -360   -110       C  
ATOM    525  CD1 LEU B 379      13.510 -19.512 -34.862  1.00 25.08           C  
ANISOU  525  CD1 LEU B 379     2828   3749   2952   -224   -411    -74       C  
ATOM    526  CD2 LEU B 379      14.319 -19.561 -32.469  1.00 20.57           C  
ANISOU  526  CD2 LEU B 379     2240   3052   2523   -117   -359    -96       C  
ATOM    527  N   GLU B 380      18.094 -22.791 -34.114  1.00 12.42           N  
ANISOU  527  N   GLU B 380     1268   1915   1536   -241    -96   -329       N  
ATOM    528  CA  GLU B 380      18.765 -24.032 -33.733  1.00 11.37           C  
ANISOU  528  CA  GLU B 380     1123   1703   1497   -206     -7   -369       C  
ATOM    529  C   GLU B 380      19.866 -23.784 -32.701  1.00 13.10           C  
ANISOU  529  C   GLU B 380     1289   1901   1786   -114     -7   -313       C  
ATOM    530  O   GLU B 380      20.026 -24.544 -31.744  1.00 15.39           O  
ANISOU  530  O   GLU B 380     1552   2140   2158    -47     12   -279       O  
ATOM    531  CB  GLU B 380      19.366 -24.713 -34.959  1.00 19.46           C  
ANISOU  531  CB  GLU B 380     2176   2711   2505   -272     95   -466       C  
ATOM    532  CG  GLU B 380      19.657 -26.185 -34.764  1.00 23.37           C  
ANISOU  532  CG  GLU B 380     2678   3095   3106   -244    209   -521       C  
ATOM    533  CD  GLU B 380      20.072 -26.875 -36.050  1.00 29.10           C  
ANISOU  533  CD  GLU B 380     3450   3796   3812   -327    333   -646       C  
ATOM    534  OE1 GLU B 380      20.622 -26.201 -36.949  1.00 31.69           O  
ANISOU  534  OE1 GLU B 380     3783   4198   4058   -380    341   -676       O  
ATOM    535  OE2 GLU B 380      19.852 -28.097 -36.159  1.00 34.07           O  
ANISOU  535  OE2 GLU B 380     4118   4325   4504   -349    436   -719       O  
ATOM    536  N   SER B 381      20.614 -22.707 -32.899  1.00 11.73           N  
ANISOU  536  N   SER B 381     1103   1780   1575   -123    -32   -295       N  
ATOM    537  CA  SER B 381      21.707 -22.363 -32.008  1.00 11.75           C  
ANISOU  537  CA  SER B 381     1043   1800   1623    -67    -40   -251       C  
ATOM    538  C   SER B 381      21.234 -21.799 -30.673  1.00 11.67           C  
ANISOU  538  C   SER B 381     1020   1805   1609    -33   -118   -187       C  
ATOM    539  O   SER B 381      21.874 -22.007 -29.639  1.00 13.26           O  
ANISOU  539  O   SER B 381     1165   2024   1850     17   -129   -143       O  
ATOM    540  CB  SER B 381      22.632 -21.352 -32.682  1.00 18.06           C  
ANISOU  540  CB  SER B 381     1837   2652   2374   -118    -31   -266       C  
ATOM    541  OG  SER B 381      23.739 -21.054 -31.848  1.00 23.71           O  
ANISOU  541  OG  SER B 381     2475   3407   3126    -85    -39   -234       O  
ATOM    542  N   ALA B 382      20.108 -21.094 -30.695  1.00 10.84           N  
ANISOU  542  N   ALA B 382      962   1704   1453    -59   -168   -178       N  
ATOM    543  CA  ALA B 382      19.735 -20.246 -29.572  1.00  9.70           C  
ANISOU  543  CA  ALA B 382      817   1574   1295    -41   -220   -140       C  
ATOM    544  C   ALA B 382      18.567 -20.738 -28.716  1.00  9.76           C  
ANISOU  544  C   ALA B 382      826   1563   1318    -11   -240   -118       C  
ATOM    545  O   ALA B 382      18.353 -20.206 -27.634  1.00 10.73           O  
ANISOU  545  O   ALA B 382      945   1701   1430      2   -265    -96       O  
ATOM    546  CB  ALA B 382      19.417 -18.851 -30.086  1.00 11.97           C  
ANISOU  546  CB  ALA B 382     1152   1865   1532    -77   -244   -137       C  
ATOM    547  N   TRP B 383      17.807 -21.722 -29.186  1.00 11.03           N  
ANISOU  547  N   TRP B 383      995   1698   1496    -17   -219   -135       N  
ATOM    548  CA  TRP B 383      16.495 -21.973 -28.583  1.00 11.19           C  
ANISOU  548  CA  TRP B 383     1016   1715   1519    -12   -236   -122       C  
ATOM    549  C   TRP B 383      16.568 -22.328 -27.087  1.00  8.35           C  
ANISOU  549  C   TRP B 383      638   1351   1183     25   -236    -80       C  
ATOM    550  O   TRP B 383      15.753 -21.840 -26.303  1.00 10.39           O  
ANISOU  550  O   TRP B 383      896   1630   1423     29   -255    -67       O  
ATOM    551  CB  TRP B 383      15.729 -23.063 -29.357  1.00 14.30           C  
ANISOU  551  CB  TRP B 383     1420   2091   1924    -55   -206   -160       C  
ATOM    552  CG  TRP B 383      16.282 -24.449 -29.232  1.00 13.52           C  
ANISOU  552  CG  TRP B 383     1329   1923   1886    -47   -138   -173       C  
ATOM    553  CD1 TRP B 383      17.247 -25.025 -30.010  1.00 18.85           C  
ANISOU  553  CD1 TRP B 383     2015   2558   2591    -51    -77   -211       C  
ATOM    554  CD2 TRP B 383      15.906 -25.436 -28.265  1.00 10.52           C  
ANISOU  554  CD2 TRP B 383      951   1492   1556    -27   -107   -140       C  
ATOM    555  NE1 TRP B 383      17.494 -26.310 -29.586  1.00 17.76           N  
ANISOU  555  NE1 TRP B 383     1884   2332   2534    -19     -6   -202       N  
ATOM    556  CE2 TRP B 383      16.683 -26.585 -28.513  1.00 15.30           C  
ANISOU  556  CE2 TRP B 383     1572   2010   2232     -7    -28   -150       C  
ATOM    557  CE3 TRP B 383      14.991 -25.459 -27.208  1.00 11.34           C  
ANISOU  557  CE3 TRP B 383     1045   1609   1653    -24   -128   -101       C  
ATOM    558  CZ2 TRP B 383      16.578 -27.741 -27.739  1.00 14.05           C  
ANISOU  558  CZ2 TRP B 383     1429   1765   2143     21     26   -106       C  
ATOM    559  CZ3 TRP B 383      14.882 -26.612 -26.447  1.00 13.33           C  
ANISOU  559  CZ3 TRP B 383     1313   1795   1956    -13    -79    -62       C  
ATOM    560  CH2 TRP B 383      15.668 -27.735 -26.717  1.00 13.21           C  
ANISOU  560  CH2 TRP B 383     1323   1681   2016     12     -5    -57       C  
ATOM    561  N   LEU B 384      17.539 -23.140 -26.680  1.00  9.00           N  
ANISOU  561  N   LEU B 384      701   1415   1302     55   -211    -51       N  
ATOM    562  CA  LEU B 384      17.611 -23.526 -25.272  1.00 10.56           C  
ANISOU  562  CA  LEU B 384      881   1627   1503     85   -221     13       C  
ATOM    563  C   LEU B 384      18.104 -22.360 -24.408  1.00 10.66           C  
ANISOU  563  C   LEU B 384      878   1717   1455     76   -267     26       C  
ATOM    564  O   LEU B 384      17.649 -22.193 -23.278  1.00 10.03           O  
ANISOU  564  O   LEU B 384      802   1673   1335     67   -282     50       O  
ATOM    565  CB  LEU B 384      18.502 -24.755 -25.080  1.00 10.00           C  
ANISOU  565  CB  LEU B 384      786   1516   1498    138   -185     69       C  
ATOM    566  CG  LEU B 384      18.574 -25.259 -23.635  1.00 10.05           C  
ANISOU  566  CG  LEU B 384      775   1548   1496    171   -203    167       C  
ATOM    567  CD1 LEU B 384      17.155 -25.580 -23.141  1.00 11.41           C  
ANISOU  567  CD1 LEU B 384      992   1692   1650    134   -187    164       C  
ATOM    568  CD2 LEU B 384      19.500 -26.465 -23.531  1.00 11.04           C  
ANISOU  568  CD2 LEU B 384      869   1620   1707    249   -165    250       C  
ATOM    569  N   GLU B 385      19.018 -21.551 -24.944  1.00  9.06           N  
ANISOU  569  N   GLU B 385      663   1543   1238     59   -280     -1       N  
ATOM    570  CA  GLU B 385      19.413 -20.308 -24.273  1.00  8.88           C  
ANISOU  570  CA  GLU B 385      661   1555   1157     17   -299    -15       C  
ATOM    571  C   GLU B 385      18.202 -19.415 -24.017  1.00  8.62           C  
ANISOU  571  C   GLU B 385      666   1514   1094     -2   -299    -53       C  
ATOM    572  O   GLU B 385      18.054 -18.840 -22.941  1.00 10.78           O  
ANISOU  572  O   GLU B 385      946   1831   1319    -29   -305    -65       O  
ATOM    573  CB  GLU B 385      20.434 -19.524 -25.101  1.00 10.14           C  
ANISOU  573  CB  GLU B 385      816   1724   1311    -15   -295    -46       C  
ATOM    574  CG  GLU B 385      21.797 -20.160 -25.229  1.00 14.90           C  
ANISOU  574  CG  GLU B 385     1357   2360   1943      3   -290    -17       C  
ATOM    575  CD  GLU B 385      22.699 -19.388 -26.172  1.00 26.38           C  
ANISOU  575  CD  GLU B 385     2798   3837   3389    -42   -274    -57       C  
ATOM    576  OE1 GLU B 385      23.420 -18.487 -25.697  1.00 20.48           O  
ANISOU  576  OE1 GLU B 385     2049   3134   2600    -97   -285    -69       O  
ATOM    577  OE2 GLU B 385      22.681 -19.683 -27.385  1.00 31.59           O  
ANISOU  577  OE2 GLU B 385     3446   4480   4075    -36   -247    -86       O  
ATOM    578  N   ILE B 386      17.349 -19.288 -25.031  1.00  9.59           N  
ANISOU  578  N   ILE B 386      808   1592   1244     12   -290    -74       N  
ATOM    579  CA AILE B 386      16.143 -18.466 -24.954  0.35  9.76           C  
ANISOU  579  CA AILE B 386      857   1589   1264     19   -281    -93       C  
ATOM    580  CA BILE B 386      16.176 -18.431 -24.920  0.65  8.98           C  
ANISOU  580  CA BILE B 386      758   1489   1163     18   -281    -94       C  
ATOM    581  C   ILE B 386      15.194 -18.985 -23.879  1.00 10.21           C  
ANISOU  581  C   ILE B 386      900   1662   1318     30   -267    -85       C  
ATOM    582  O   ILE B 386      14.659 -18.221 -23.074  1.00 10.57           O  
ANISOU  582  O   ILE B 386      960   1710   1345     27   -243   -109       O  
ATOM    583  CB AILE B 386      15.409 -18.426 -26.307  0.35 11.65           C  
ANISOU  583  CB AILE B 386     1099   1801   1525     34   -289    -90       C  
ATOM    584  CB BILE B 386      15.492 -18.245 -26.287  0.65 11.15           C  
ANISOU  584  CB BILE B 386     1041   1737   1460     33   -288    -91       C  
ATOM    585  CG1AILE B 386      16.271 -17.720 -27.355  0.35 11.70           C  
ANISOU  585  CG1AILE B 386     1133   1794   1517     12   -294    -93       C  
ATOM    586  CG1BILE B 386      16.429 -17.481 -27.234  0.65 10.57           C  
ANISOU  586  CG1BILE B 386      997   1649   1372      9   -292    -96       C  
ATOM    587  CG2AILE B 386      14.066 -17.724 -26.172  0.35 12.86           C  
ANISOU  587  CG2AILE B 386     1249   1943   1695     67   -283    -85       C  
ATOM    588  CG2BILE B 386      14.178 -17.499 -26.139  0.65 14.29           C  
ANISOU  588  CG2BILE B 386     1438   2119   1874     67   -281    -87       C  
ATOM    589  CD1AILE B 386      16.630 -16.308 -26.989  0.35 10.29           C  
ANISOU  589  CD1AILE B 386      998   1585   1328     -1   -279   -105       C  
ATOM    590  CD1BILE B 386      16.055 -17.577 -28.697  0.65 12.46           C  
ANISOU  590  CD1BILE B 386     1242   1888   1603      3   -307    -81       C  
ATOM    591  N   LEU B 387      14.974 -20.299 -23.870  1.00 10.02           N  
ANISOU  591  N   LEU B 387      853   1639   1313     37   -265    -56       N  
ATOM    592  CA  LEU B 387      14.159 -20.903 -22.815  1.00 11.84           C  
ANISOU  592  CA  LEU B 387     1076   1888   1536     32   -244    -38       C  
ATOM    593  C   LEU B 387      14.770 -20.629 -21.441  1.00  9.52           C  
ANISOU  593  C   LEU B 387      790   1646   1179     11   -246    -22       C  
ATOM    594  O   LEU B 387      14.054 -20.361 -20.477  1.00 10.85           O  
ANISOU  594  O   LEU B 387      968   1843   1311     -8   -218    -36       O  
ATOM    595  CB  LEU B 387      14.018 -22.414 -23.008  1.00 11.77           C  
ANISOU  595  CB  LEU B 387     1059   1851   1563     31   -229     -2       C  
ATOM    596  CG  LEU B 387      13.129 -22.908 -24.150  1.00 12.50           C  
ANISOU  596  CG  LEU B 387     1142   1914   1693     13   -217    -33       C  
ATOM    597  CD1 LEU B 387      13.039 -24.428 -24.134  1.00 15.38           C  
ANISOU  597  CD1 LEU B 387     1519   2229   2096     -9   -177    -12       C  
ATOM    598  CD2 LEU B 387      11.752 -22.285 -24.049  1.00 13.76           C  
ANISOU  598  CD2 LEU B 387     1272   2110   1847      6   -215    -57       C  
ATOM    599  N   MET B 388      16.094 -20.704 -21.347  1.00  7.78           N  
ANISOU  599  N   MET B 388      559   1457    939      6   -277      6       N  
ATOM    600  CA  MET B 388      16.757 -20.535 -20.056  1.00  8.39           C  
ANISOU  600  CA  MET B 388      630   1621    936    -31   -297     32       C  
ATOM    601  C   MET B 388      16.690 -19.100 -19.538  1.00  9.05           C  
ANISOU  601  C   MET B 388      748   1733    957    -88   -280    -48       C  
ATOM    602  O   MET B 388      16.430 -18.888 -18.355  1.00  9.73           O  
ANISOU  602  O   MET B 388      851   1881    966   -137   -264    -62       O  
ATOM    603  CB  MET B 388      18.209 -20.999 -20.140  1.00  8.71           C  
ANISOU  603  CB  MET B 388      632   1697    980    -16   -335     90       C  
ATOM    604  CG  MET B 388      18.354 -22.506 -20.111  1.00  9.05           C  
ANISOU  604  CG  MET B 388      642   1721   1074     44   -338    189       C  
ATOM    605  SD  MET B 388      20.060 -23.030 -20.311  1.00 17.31           S  
ANISOU  605  SD  MET B 388     1644   2773   2159     88   -353    248       S  
ATOM    606  CE  MET B 388      19.931 -24.779 -19.947  1.00 12.23           C  
ANISOU  606  CE  MET B 388      970   2095   1582    173   -341    389       C  
ATOM    607  N   ILE B 389      16.920 -18.114 -20.401  1.00 10.85           N  
ANISOU  607  N   ILE B 389      996   1910   1215    -92   -271   -104       N  
ATOM    608  CA  ILE B 389      16.848 -16.739 -19.927  1.00 11.17           C  
ANISOU  608  CA  ILE B 389     1087   1943   1216   -148   -231   -186       C  
ATOM    609  C   ILE B 389      15.401 -16.391 -19.560  1.00 12.15           C  
ANISOU  609  C   ILE B 389     1238   2015   1362   -121   -166   -225       C  
ATOM    610  O   ILE B 389      15.165 -15.633 -18.622  1.00 12.71           O  
ANISOU  610  O   ILE B 389     1349   2097   1382   -172   -112   -293       O  
ATOM    611  CB  ILE B 389      17.423 -15.724 -20.950  1.00 11.28           C  
ANISOU  611  CB  ILE B 389     1129   1891   1264   -160   -223   -224       C  
ATOM    612  CG1 ILE B 389      17.668 -14.377 -20.257  1.00 12.37           C  
ANISOU  612  CG1 ILE B 389     1330   2018   1353   -246   -171   -313       C  
ATOM    613  CG2 ILE B 389      16.537 -15.582 -22.192  1.00 13.03           C  
ANISOU  613  CG2 ILE B 389     1364   2016   1573    -83   -209   -208       C  
ATOM    614  CD1 ILE B 389      18.266 -13.333 -21.152  1.00 11.18           C  
ANISOU  614  CD1 ILE B 389     1223   1791   1233   -275   -149   -346       C  
ATOM    615  N   GLY B 390      14.437 -16.981 -20.262  1.00 11.37           N  
ANISOU  615  N   GLY B 390     1112   1872   1334    -50   -166   -190       N  
ATOM    616  CA  GLY B 390      13.040 -16.811 -19.902  1.00 13.90           C  
ANISOU  616  CA  GLY B 390     1426   2171   1684    -19   -108   -215       C  
ATOM    617  C   GLY B 390      12.780 -17.337 -18.504  1.00 10.68           C  
ANISOU  617  C   GLY B 390     1019   1838   1201    -69    -79   -220       C  
ATOM    618  O   GLY B 390      12.161 -16.668 -17.674  1.00 12.27           O  
ANISOU  618  O   GLY B 390     1243   2042   1377    -91     -5   -285       O  
ATOM    619  N   LEU B 391      13.272 -18.543 -18.247  1.00 10.28           N  
ANISOU  619  N   LEU B 391      948   1843   1115    -86   -128   -146       N  
ATOM    620  CA  LEU B 391      13.141 -19.180 -16.935  1.00 10.95           C  
ANISOU  620  CA  LEU B 391     1037   2009   1112   -138   -113   -117       C  
ATOM    621  C   LEU B 391      13.766 -18.345 -15.824  1.00 12.13           C  
ANISOU  621  C   LEU B 391     1226   2238   1145   -224    -99   -170       C  
ATOM    622  O   LEU B 391      13.194 -18.176 -14.742  1.00 14.33           O  
ANISOU  622  O   LEU B 391     1529   2569   1346   -280    -40   -210       O  
ATOM    623  CB  LEU B 391      13.788 -20.564 -16.963  1.00 12.41           C  
ANISOU  623  CB  LEU B 391     1200   2220   1296   -125   -172     -3       C  
ATOM    624  CG  LEU B 391      13.859 -21.316 -15.639  1.00 13.76           C  
ANISOU  624  CG  LEU B 391     1381   2481   1368   -174   -174     71       C  
ATOM    625  CD1 LEU B 391      12.461 -21.536 -15.074  1.00 12.83           C  
ANISOU  625  CD1 LEU B 391     1274   2360   1241   -199    -96     46       C  
ATOM    626  CD2 LEU B 391      14.604 -22.638 -15.815  1.00 13.01           C  
ANISOU  626  CD2 LEU B 391     1263   2377   1304   -131   -226    204       C  
ATOM    627  N   VAL B 392      14.956 -17.833 -16.094  1.00 11.36           N  
ANISOU  627  N   VAL B 392     1132   2160   1024   -251   -147   -180       N  
ATOM    628  CA  VAL B 392      15.671 -17.059 -15.099  1.00 12.33           C  
ANISOU  628  CA  VAL B 392     1287   2378   1022   -361   -142   -241       C  
ATOM    629  C   VAL B 392      14.933 -15.752 -14.801  1.00 13.94           C  
ANISOU  629  C   VAL B 392     1556   2513   1226   -399    -31   -382       C  
ATOM    630  O   VAL B 392      14.829 -15.339 -13.646  1.00 16.67           O  
ANISOU  630  O   VAL B 392     1944   2932   1459   -498     23   -454       O  
ATOM    631  CB  VAL B 392      17.105 -16.790 -15.563  1.00 16.96           C  
ANISOU  631  CB  VAL B 392     1846   3003   1593   -391   -215   -226       C  
ATOM    632  CG1 VAL B 392      17.746 -15.722 -14.732  1.00 20.76           C  
ANISOU  632  CG1 VAL B 392     2366   3568   1953   -530   -195   -325       C  
ATOM    633  CG2 VAL B 392      17.915 -18.076 -15.486  1.00 18.47           C  
ANISOU  633  CG2 VAL B 392     1964   3286   1768   -357   -308    -83       C  
ATOM    634  N   TRP B 393      14.391 -15.129 -15.845  1.00 13.53           N  
ANISOU  634  N   TRP B 393     1515   2321   1304   -316     10   -416       N  
ATOM    635  CA  TRP B 393      13.601 -13.905 -15.698  1.00 14.21           C  
ANISOU  635  CA  TRP B 393     1658   2306   1434   -311    130   -530       C  
ATOM    636  C   TRP B 393      12.352 -14.119 -14.834  1.00 14.35           C  
ANISOU  636  C   TRP B 393     1669   2344   1439   -302    218   -564       C  
ATOM    637  O   TRP B 393      12.068 -13.325 -13.938  1.00 17.08           O  
ANISOU  637  O   TRP B 393     2071   2684   1733   -368    326   -678       O  
ATOM    638  CB  TRP B 393      13.210 -13.358 -17.079  1.00 13.13           C  
ANISOU  638  CB  TRP B 393     1516   2027   1447   -198    138   -510       C  
ATOM    639  CG  TRP B 393      12.233 -12.216 -17.038  1.00 16.70           C  
ANISOU  639  CG  TRP B 393     2007   2354   1983   -145    265   -590       C  
ATOM    640  CD1 TRP B 393      10.915 -12.255 -17.395  1.00 17.00           C  
ANISOU  640  CD1 TRP B 393     1993   2340   2128    -28    310   -563       C  
ATOM    641  CD2 TRP B 393      12.491 -10.872 -16.613  1.00 16.59           C  
ANISOU  641  CD2 TRP B 393     2089   2249   1967   -204    375   -708       C  
ATOM    642  NE1 TRP B 393      10.338 -11.022 -17.218  1.00 19.47           N  
ANISOU  642  NE1 TRP B 393     2352   2528   2516     14    440   -644       N  
ATOM    643  CE2 TRP B 393      11.283 -10.155 -16.738  1.00 19.60           C  
ANISOU  643  CE2 TRP B 393     2473   2502   2470    -95    492   -740       C  
ATOM    644  CE3 TRP B 393      13.623 -10.204 -16.140  1.00 18.37           C  
ANISOU  644  CE3 TRP B 393     2394   2488   2100   -346    391   -794       C  
ATOM    645  CZ2 TRP B 393      11.177  -8.803 -16.405  1.00 22.99           C  
ANISOU  645  CZ2 TRP B 393     2999   2789   2949   -110    641   -855       C  
ATOM    646  CZ3 TRP B 393      13.516  -8.863 -15.802  1.00 20.56           C  
ANISOU  646  CZ3 TRP B 393     2772   2631   2407   -389    536   -923       C  
ATOM    647  CH2 TRP B 393      12.301  -8.177 -15.939  1.00 22.86           C  
ANISOU  647  CH2 TRP B 393     3082   2767   2838   -265    667   -952       C  
ATOM    648  N   ARG B 394      11.603 -15.189 -15.085  1.00 13.07           N  
ANISOU  648  N   ARG B 394     1441   2204   1321   -234    186   -478       N  
ATOM    649  CA  ARG B 394      10.388 -15.402 -14.300  1.00 19.79           C  
ANISOU  649  CA  ARG B 394     2274   3082   2163   -233    278   -511       C  
ATOM    650  C   ARG B 394      10.669 -16.090 -12.953  1.00 22.33           C  
ANISOU  650  C   ARG B 394     2619   3546   2320   -350    276   -497       C  
ATOM    651  O   ARG B 394       9.746 -16.368 -12.190  1.00 26.26           O  
ANISOU  651  O   ARG B 394     3107   4085   2784   -374    356   -520       O  
ATOM    652  CB  ARG B 394       9.343 -16.175 -15.125  1.00 25.74           C  
ANISOU  652  CB  ARG B 394     2942   3807   3031   -133    259   -436       C  
ATOM    653  CG  ARG B 394       9.659 -17.626 -15.445  1.00 23.68           C  
ANISOU  653  CG  ARG B 394     2646   3598   2752   -140    159   -320       C  
ATOM    654  CD  ARG B 394       8.536 -18.256 -16.285  1.00 20.16           C  
ANISOU  654  CD  ARG B 394     2122   3125   2413    -72    158   -280       C  
ATOM    655  NE  ARG B 394       8.874 -19.610 -16.708  1.00 14.73           N  
ANISOU  655  NE  ARG B 394     1420   2452   1724    -86     82   -187       N  
ATOM    656  CZ  ARG B 394       9.493 -19.910 -17.846  1.00 11.36           C  
ANISOU  656  CZ  ARG B 394      987   1982   1348    -51      6   -146       C  
ATOM    657  NH1 ARG B 394       9.824 -18.951 -18.700  1.00 15.34           N  
ANISOU  657  NH1 ARG B 394     1495   2436   1896     -4    -16   -175       N  
ATOM    658  NH2 ARG B 394       9.767 -21.174 -18.133  1.00 17.86           N  
ANISOU  658  NH2 ARG B 394     1807   2801   2177    -66    -33    -76       N  
ATOM    659  N   SER B 395      11.944 -16.317 -12.644  1.00 18.65           N  
ANISOU  659  N   SER B 395     1806   3476   1804     19    250   -519       N  
ATOM    660  CA  SER B 395      12.319 -16.858 -11.339  1.00 32.07           C  
ANISOU  660  CA  SER B 395     3560   5215   3409    -60    245   -514       C  
ATOM    661  C   SER B 395      12.957 -15.799 -10.437  1.00 23.85           C  
ANISOU  661  C   SER B 395     2610   4152   2302    -99    243   -574       C  
ATOM    662  O   SER B 395      13.299 -16.078  -9.286  1.00 18.62           O  
ANISOU  662  O   SER B 395     1988   3547   1539   -173    240   -576       O  
ATOM    663  CB  SER B 395      13.277 -18.043 -11.497  1.00 18.02           C  
ANISOU  663  CB  SER B 395     1762   3448   1636   -110    171   -426       C  
ATOM    664  OG  SER B 395      12.705 -19.061 -12.297  1.00 16.29           O  
ANISOU  664  OG  SER B 395     1464   3241   1486    -86    178   -392       O  
ATOM    665  N   MET B 396      13.106 -14.586 -10.959  1.00 18.17           N  
ANISOU  665  N   MET B 396     1914   3352   1638    -55    246   -621       N  
ATOM    666  CA  MET B 396      13.833 -13.528 -10.258  1.00 22.67           C  
ANISOU  666  CA  MET B 396     2571   3878   2165   -103    239   -690       C  
ATOM    667  C   MET B 396      13.293 -13.210  -8.873  1.00 24.30           C  
ANISOU  667  C   MET B 396     2827   4133   2273   -140    311   -790       C  
ATOM    668  O   MET B 396      14.062 -12.966  -7.946  1.00 30.02           O  
ANISOU  668  O   MET B 396     3611   4890   2905   -229    291   -829       O  
ATOM    669  CB  MET B 396      13.838 -12.246 -11.082  1.00 27.44           C  
ANISOU  669  CB  MET B 396     3188   4366   2874    -41    246   -722       C  
ATOM    670  CG  MET B 396      14.990 -12.138 -12.045  1.00 30.97           C  
ANISOU  670  CG  MET B 396     3623   4775   3369    -58    155   -645       C  
ATOM    671  SD  MET B 396      14.748 -10.732 -13.127  1.00 54.67           S  
ANISOU  671  SD  MET B 396     6614   7651   6508     22    170   -645       S  
ATOM    672  CE  MET B 396      15.215  -9.389 -12.044  1.00 20.16           C  
ANISOU  672  CE  MET B 396     2366   3174   2118    -39    199   -766       C  
ATOM    673  N   GLU B 397      11.974 -13.206  -8.737  1.00 30.79           N  
ANISOU  673  N   GLU B 397     3614   4980   3107    -78    395   -834       N  
ATOM    674  CA  GLU B 397      11.353 -12.855  -7.469  1.00 29.89           C  
ANISOU  674  CA  GLU B 397     3533   4928   2897   -105    474   -944       C  
ATOM    675  C   GLU B 397      11.071 -14.095  -6.630  1.00 29.85           C  
ANISOU  675  C   GLU B 397     3494   5072   2776   -173    478   -888       C  
ATOM    676  O   GLU B 397      10.268 -14.060  -5.702  1.00 32.02           O  
ANISOU  676  O   GLU B 397     3763   5438   2967   -186    551   -958       O  
ATOM    677  CB  GLU B 397      10.077 -12.052  -7.725  1.00 32.03           C  
ANISOU  677  CB  GLU B 397     3778   5151   3243      6    571  -1028       C  
ATOM    678  CG  GLU B 397      10.376 -10.615  -8.134  1.00 35.90           C  
ANISOU  678  CG  GLU B 397     4320   5484   3836     57    584  -1103       C  
ATOM    679  CD  GLU B 397       9.315  -9.999  -9.025  1.00 40.14           C  
ANISOU  679  CD  GLU B 397     4800   5943   4507    197    644  -1102       C  
ATOM    680  OE1 GLU B 397       8.117 -10.301  -8.844  1.00 41.01           O  
ANISOU  680  OE1 GLU B 397     4850   6132   4600    255    716  -1121       O  
ATOM    681  OE2 GLU B 397       9.689  -9.202  -9.913  1.00 47.54           O  
ANISOU  681  OE2 GLU B 397     5746   6752   5565    246    616  -1072       O  
ATOM    682  N   HIS B 398      11.753 -15.187  -6.962  1.00 26.64           N  
ANISOU  682  N   HIS B 398     3061   4690   2372   -214    399   -760       N  
ATOM    683  CA  HIS B 398      11.646 -16.425  -6.198  1.00 26.46           C  
ANISOU  683  CA  HIS B 398     3006   4786   2260   -284    390   -675       C  
ATOM    684  C   HIS B 398      13.026 -16.976  -5.842  1.00 24.38           C  
ANISOU  684  C   HIS B 398     2766   4552   1945   -369    299   -583       C  
ATOM    685  O   HIS B 398      13.458 -17.983  -6.402  1.00 24.67           O  
ANISOU  685  O   HIS B 398     2766   4568   2041   -368    241   -466       O  
ATOM    686  CB  HIS B 398      10.851 -17.467  -6.985  1.00 27.14           C  
ANISOU  686  CB  HIS B 398     3015   4869   2427   -239    398   -594       C  
ATOM    687  CG  HIS B 398       9.470 -17.019  -7.343  1.00 29.36           C  
ANISOU  687  CG  HIS B 398     3255   5151   2749   -158    484   -666       C  
ATOM    688  ND1 HIS B 398       9.190 -16.337  -8.507  1.00 32.50           N  
ANISOU  688  ND1 HIS B 398     3631   5459   3259    -63    493   -695       N  
ATOM    689  CD2 HIS B 398       8.292 -17.148  -6.688  1.00 29.62           C  
ANISOU  689  CD2 HIS B 398     3254   5280   2720   -156    564   -703       C  
ATOM    690  CE1 HIS B 398       7.898 -16.065  -8.555  1.00 27.24           C  
ANISOU  690  CE1 HIS B 398     2918   4830   2603      0    576   -746       C  
ATOM    691  NE2 HIS B 398       7.330 -16.549  -7.465  1.00 33.68           N  
ANISOU  691  NE2 HIS B 398     3727   5758   3313    -54    621   -758       N  
ATOM    692  N   PRO B 399      13.718 -16.312  -4.901  1.00 25.24           N  
ANISOU  692  N   PRO B 399     2931   4716   1945   -444    290   -642       N  
ATOM    693  CA  PRO B 399      15.068 -16.713  -4.493  1.00 25.84           C  
ANISOU  693  CA  PRO B 399     3020   4845   1953   -528    204   -553       C  
ATOM    694  C   PRO B 399      15.146 -18.180  -4.072  1.00 23.71           C  
ANISOU  694  C   PRO B 399     2695   4664   1650   -569    171   -393       C  
ATOM    695  O   PRO B 399      14.319 -18.636  -3.284  1.00 24.45           O  
ANISOU  695  O   PRO B 399     2762   4858   1671   -600    221   -378       O  
ATOM    696  CB  PRO B 399      15.366 -15.790  -3.305  1.00 27.72           C  
ANISOU  696  CB  PRO B 399     3311   5175   2045   -616    230   -668       C  
ATOM    697  CG  PRO B 399      14.466 -14.618  -3.498  1.00 29.58           C  
ANISOU  697  CG  PRO B 399     3580   5327   2331   -552    317   -837       C  
ATOM    698  CD  PRO B 399      13.223 -15.161  -4.127  1.00 28.88           C  
ANISOU  698  CD  PRO B 399     3436   5204   2333   -456    367   -804       C  
ATOM    699  N   GLY B 400      16.125 -18.901  -4.609  1.00 23.49           N  
ANISOU  699  N   GLY B 400     2646   4596   1682   -567     88   -271       N  
ATOM    700  CA  GLY B 400      16.344 -20.291  -4.253  1.00 25.04           C  
ANISOU  700  CA  GLY B 400     2791   4847   1876   -598     52   -106       C  
ATOM    701  C   GLY B 400      15.476 -21.274  -5.015  1.00 25.27           C  
ANISOU  701  C   GLY B 400     2771   4796   2036   -536     77    -53       C  
ATOM    702  O   GLY B 400      15.584 -22.490  -4.822  1.00 27.38           O  
ANISOU  702  O   GLY B 400     2996   5072   2337   -556     52     84       O  
ATOM    703  N   LYS B 401      14.607 -20.758  -5.878  1.00 21.08           N  
ANISOU  703  N   LYS B 401     2239   4187   1584   -465    127   -159       N  
ATOM    704  CA  LYS B 401      13.684 -21.612  -6.621  1.00 20.62           C  
ANISOU  704  CA  LYS B 401     2126   4073   1636   -418    159   -131       C  
ATOM    705  C   LYS B 401      13.620 -21.250  -8.101  1.00 21.37           C  
ANISOU  705  C   LYS B 401     2203   4061   1856   -333    152   -193       C  
ATOM    706  O   LYS B 401      14.025 -20.160  -8.506  1.00 19.20           O  
ANISOU  706  O   LYS B 401     1962   3753   1581   -303    141   -267       O  
ATOM    707  CB  LYS B 401      12.284 -21.536  -6.006  1.00 21.31           C  
ANISOU  707  CB  LYS B 401     2199   4237   1661   -431    246   -179       C  
ATOM    708  CG  LYS B 401      12.240 -21.963  -4.541  1.00 22.54           C  
ANISOU  708  CG  LYS B 401     2354   4531   1680   -524    256   -108       C  
ATOM    709  CD  LYS B 401      10.821 -22.207  -4.049  1.00 23.61           C  
ANISOU  709  CD  LYS B 401     2452   4752   1768   -541    338   -128       C  
ATOM    710  CE  LYS B 401      10.808 -22.672  -2.586  1.00 27.74           C  
ANISOU  710  CE  LYS B 401     2960   5438   2140   -645    344    -40       C  
ATOM    711  NZ  LYS B 401       9.728 -22.049  -1.767  1.00 35.96           N  
ANISOU  711  NZ  LYS B 401     3991   6620   3053   -666    431   -143       N  
ATOM    712  N   LEU B 402      13.106 -22.173  -8.906  1.00 18.16           N  
ANISOU  712  N   LEU B 402     1738   3607   1554   -304    161   -161       N  
ATOM    713  CA  LEU B 402      12.954 -21.925 -10.332  1.00 17.27           C  
ANISOU  713  CA  LEU B 402     1588   3429   1544   -234    158   -217       C  
ATOM    714  C   LEU B 402      11.494 -22.075 -10.728  1.00 17.32           C  
ANISOU  714  C   LEU B 402     1542   3456   1581   -208    232   -263       C  
ATOM    715  O   LEU B 402      10.891 -23.130 -10.522  1.00 18.17           O  
ANISOU  715  O   LEU B 402     1614   3579   1711   -244    256   -218       O  
ATOM    716  CB  LEU B 402      13.836 -22.875 -11.143  1.00 16.77           C  
ANISOU  716  CB  LEU B 402     1487   3304   1582   -225     96   -158       C  
ATOM    717  CG  LEU B 402      15.348 -22.627 -11.037  1.00 17.75           C  
ANISOU  717  CG  LEU B 402     1643   3415   1685   -234     18   -116       C  
ATOM    718  CD1 LEU B 402      16.126 -23.651 -11.843  1.00 17.74           C  
ANISOU  718  CD1 LEU B 402     1591   3358   1792   -213    -33    -65       C  
ATOM    719  CD2 LEU B 402      15.693 -21.219 -11.493  1.00 16.66           C  
ANISOU  719  CD2 LEU B 402     1536   3277   1519   -205      5   -191       C  
ATOM    720  N   LEU B 403      10.923 -21.007 -11.274  1.00 17.21           N  
ANISOU  720  N   LEU B 403     1520   3447   1570   -148    268   -345       N  
ATOM    721  CA  LEU B 403       9.527 -21.018 -11.690  1.00 19.64           C  
ANISOU  721  CA  LEU B 403     1767   3797   1899   -114    338   -385       C  
ATOM    722  C   LEU B 403       9.453 -21.492 -13.132  1.00 16.65           C  
ANISOU  722  C   LEU B 403     1310   3398   1620    -83    318   -386       C  
ATOM    723  O   LEU B 403       9.453 -20.683 -14.056  1.00 16.25           O  
ANISOU  723  O   LEU B 403     1231   3343   1603    -22    313   -420       O  
ATOM    724  CB  LEU B 403       8.901 -19.625 -11.533  1.00 17.80           C  
ANISOU  724  CB  LEU B 403     1552   3584   1627    -54    393   -464       C  
ATOM    725  CG  LEU B 403       7.386 -19.428 -11.690  1.00 18.12           C  
ANISOU  725  CG  LEU B 403     1529   3692   1665     -8    477   -505       C  
ATOM    726  CD1 LEU B 403       6.953 -18.200 -10.923  1.00 26.10           C  
ANISOU  726  CD1 LEU B 403     2582   4716   2618     34    535   -580       C  
ATOM    727  CD2 LEU B 403       6.941 -19.281 -13.139  1.00 24.69           C  
ANISOU  727  CD2 LEU B 403     2274   4526   2581     57    478   -509       C  
ATOM    728  N   PHE B 404       9.427 -22.806 -13.323  1.00 16.56           N  
ANISOU  728  N   PHE B 404     1259   3374   1659   -129    307   -348       N  
ATOM    729  CA  PHE B 404       9.331 -23.374 -14.664  1.00 16.11           C  
ANISOU  729  CA  PHE B 404     1120   3311   1691   -115    296   -371       C  
ATOM    730  C   PHE B 404       7.988 -22.997 -15.267  1.00 16.24           C  
ANISOU  730  C   PHE B 404     1059   3410   1699    -83    359   -421       C  
ATOM    731  O   PHE B 404       7.884 -22.699 -16.457  1.00 15.86           O  
ANISOU  731  O   PHE B 404      997   3333   1694    -43    327   -435       O  
ATOM    732  CB  PHE B 404       9.510 -24.892 -14.626  1.00 16.40           C  
ANISOU  732  CB  PHE B 404     1135   3298   1797   -178    283   -334       C  
ATOM    733  CG  PHE B 404      10.927 -25.327 -14.376  1.00 16.29           C  
ANISOU  733  CG  PHE B 404     1167   3204   1818   -188    214   -279       C  
ATOM    734  CD1 PHE B 404      11.824 -25.443 -15.425  1.00 15.77           C  
ANISOU  734  CD1 PHE B 404     1067   3104   1820   -157    165   -305       C  
ATOM    735  CD2 PHE B 404      11.366 -25.606 -13.092  1.00 17.33           C  
ANISOU  735  CD2 PHE B 404     1363   3315   1904   -229    199   -195       C  
ATOM    736  CE1 PHE B 404      13.130 -25.841 -15.200  1.00 16.58           C  
ANISOU  736  CE1 PHE B 404     1202   3145   1954   -158    103   -251       C  
ATOM    737  CE2 PHE B 404      12.673 -26.000 -12.860  1.00 19.46           C  
ANISOU  737  CE2 PHE B 404     1662   3528   2203   -233    134   -130       C  
ATOM    738  CZ  PHE B 404      13.553 -26.118 -13.914  1.00 18.14           C  
ANISOU  738  CZ  PHE B 404     1463   3318   2112   -193     87   -159       C  
ATOM    739  N   ALA B 405       6.968 -23.009 -14.417  1.00 16.88           N  
ANISOU  739  N   ALA B 405     1146   3543   1723   -102    420   -419       N  
ATOM    740  CA  ALA B 405       5.622 -22.570 -14.761  1.00 17.19           C  
ANISOU  740  CA  ALA B 405     1179   3597   1757    -65    448   -434       C  
ATOM    741  C   ALA B 405       4.973 -22.069 -13.474  1.00 18.06           C  
ANISOU  741  C   ALA B 405     1319   3762   1780    -64    507   -440       C  
ATOM    742  O   ALA B 405       5.475 -22.364 -12.387  1.00 18.23           O  
ANISOU  742  O   ALA B 405     1363   3824   1738   -116    528   -426       O  
ATOM    743  CB  ALA B 405       4.824 -23.706 -15.386  1.00 17.41           C  
ANISOU  743  CB  ALA B 405     1163   3622   1830   -115    449   -429       C  
ATOM    744  N   PRO B 406       3.878 -21.292 -13.580  1.00 18.93           N  
ANISOU  744  N   PRO B 406     1429   3881   1882     -7    535   -456       N  
ATOM    745  CA  PRO B 406       3.241 -20.804 -12.352  1.00 19.20           C  
ANISOU  745  CA  PRO B 406     1491   3966   1838     -1    592   -477       C  
ATOM    746  C   PRO B 406       2.754 -21.940 -11.458  1.00 19.81           C  
ANISOU  746  C   PRO B 406     1552   4113   1860    -93    620   -445       C  
ATOM    747  O   PRO B 406       2.638 -21.760 -10.245  1.00 20.51           O  
ANISOU  747  O   PRO B 406     1671   4260   1863   -119    655   -452       O  
ATOM    748  CB  PRO B 406       2.062 -19.975 -12.871  1.00 19.61           C  
ANISOU  748  CB  PRO B 406     1520   4012   1919     79    615   -487       C  
ATOM    749  CG  PRO B 406       2.510 -19.511 -14.214  1.00 18.90           C  
ANISOU  749  CG  PRO B 406     1415   3862   1906    130    568   -473       C  
ATOM    750  CD  PRO B 406       3.301 -20.658 -14.780  1.00 19.00           C  
ANISOU  750  CD  PRO B 406     1413   3858   1947     60    516   -452       C  
ATOM    751  N   ASN B 407       2.470 -23.093 -12.057  1.00 19.75           N  
ANISOU  751  N   ASN B 407     1498   4105   1903   -150    604   -411       N  
ATOM    752  CA  ASN B 407       2.070 -24.272 -11.301  1.00 20.43           C  
ANISOU  752  CA  ASN B 407     1559   4248   1955   -252    632   -365       C  
ATOM    753  C   ASN B 407       3.204 -25.286 -11.212  1.00 20.17           C  
ANISOU  753  C   ASN B 407     1514   4191   1958   -332    612   -316       C  
ATOM    754  O   ASN B 407       2.976 -26.467 -10.969  1.00 20.69           O  
ANISOU  754  O   ASN B 407     1543   4271   2048   -428    627   -261       O  
ATOM    755  CB  ASN B 407       0.831 -24.917 -11.929  1.00 20.81           C  
ANISOU  755  CB  ASN B 407     1555   4313   2040   -276    641   -361       C  
ATOM    756  CG  ASN B 407       1.094 -25.449 -13.325  1.00 20.19           C  
ANISOU  756  CG  ASN B 407     1447   4165   2059   -278    601   -378       C  
ATOM    757  OD1 ASN B 407       2.037 -25.025 -13.993  1.00 19.40           O  
ANISOU  757  OD1 ASN B 407     1364   4005   2001   -230    561   -397       O  
ATOM    758  ND2 ASN B 407       0.253 -26.374 -13.776  1.00 20.80           N  
ANISOU  758  ND2 ASN B 407     1479   4258   2165   -338    611   -376       N  
ATOM    759  N   LEU B 408       4.431 -24.822 -11.416  1.00 19.40           N  
ANISOU  759  N   LEU B 408     1458   4032   1882   -294    568   -324       N  
ATOM    760  CA  LEU B 408       5.580 -25.705 -11.294  1.00 19.25           C  
ANISOU  760  CA  LEU B 408     1483   3905   1927   -343    501   -255       C  
ATOM    761  C   LEU B 408       6.788 -24.933 -10.785  1.00 18.93           C  
ANISOU  761  C   LEU B 408     1524   3824   1844   -310    451   -243       C  
ATOM    762  O   LEU B 408       7.699 -24.596 -11.544  1.00 18.18           O  
ANISOU  762  O   LEU B 408     1443   3662   1803   -264    400   -265       O  
ATOM    763  CB  LEU B 408       5.893 -26.378 -12.633  1.00 18.71           C  
ANISOU  763  CB  LEU B 408     1363   3761   1984   -338    471   -282       C  
ATOM    764  CG  LEU B 408       6.847 -27.572 -12.565  1.00 23.58           C  
ANISOU  764  CG  LEU B 408     2004   4259   2698   -390    419   -214       C  
ATOM    765  CD1 LEU B 408       6.343 -28.599 -11.572  1.00 24.12           C  
ANISOU  765  CD1 LEU B 408     2075   4324   2765   -482    443   -122       C  
ATOM    766  CD2 LEU B 408       7.011 -28.204 -13.935  1.00 21.84           C  
ANISOU  766  CD2 LEU B 408     1721   3980   2598   -385    404   -276       C  
ATOM    767  N   LEU B 409       6.770 -24.648  -9.489  1.00 19.61           N  
ANISOU  767  N   LEU B 409     1658   3972   1823   -343    467   -212       N  
ATOM    768  CA  LEU B 409       7.840 -23.932  -8.815  1.00 23.74           C  
ANISOU  768  CA  LEU B 409     2255   4484   2281   -336    426   -206       C  
ATOM    769  C   LEU B 409       8.690 -24.931  -8.041  1.00 24.44           C  
ANISOU  769  C   LEU B 409     2369   4551   2368   -411    374    -80       C  
ATOM    770  O   LEU B 409       8.213 -25.546  -7.089  1.00 24.81           O  
ANISOU  770  O   LEU B 409     2403   4667   2356   -482    398     -6       O  
ATOM    771  CB  LEU B 409       7.257 -22.873  -7.877  1.00 22.91           C  
ANISOU  771  CB  LEU B 409     2176   4481   2047   -326    483   -273       C  
ATOM    772  CG  LEU B 409       8.182 -21.942  -7.090  1.00 26.53           C  
ANISOU  772  CG  LEU B 409     2711   4952   2418   -331    458   -303       C  
ATOM    773  CD1 LEU B 409       9.084 -21.148  -8.007  1.00 26.74           C  
ANISOU  773  CD1 LEU B 409     2769   4876   2513   -267    410   -351       C  
ATOM    774  CD2 LEU B 409       7.345 -21.012  -6.226  1.00 26.88           C  
ANISOU  774  CD2 LEU B 409     2765   5101   2349   -322    536   -398       C  
ATOM    775  N   LEU B 410       9.942 -25.101  -8.453  1.00 19.53           N  
ANISOU  775  N   LEU B 410     1770   3842   1809   -395    302    -45       N  
ATOM    776  CA  LEU B 410      10.796 -26.130  -7.869  1.00 21.96           C  
ANISOU  776  CA  LEU B 410     2086   4116   2143   -449    250     91       C  
ATOM    777  C   LEU B 410      11.943 -25.520  -7.074  1.00 22.44           C  
ANISOU  777  C   LEU B 410     2200   4221   2106   -463    199    126       C  
ATOM    778  O   LEU B 410      12.519 -24.515  -7.488  1.00 22.49           O  
ANISOU  778  O   LEU B 410     2238   4214   2092   -418    177     45       O  
ATOM    779  CB  LEU B 410      11.353 -27.040  -8.965  1.00 24.52           C  
ANISOU  779  CB  LEU B 410     2378   4309   2631   -421    209    113       C  
ATOM    780  CG  LEU B 410      10.319 -27.764  -9.831  1.00 27.06           C  
ANISOU  780  CG  LEU B 410     2639   4587   3056   -424    256     68       C  
ATOM    781  CD1 LEU B 410      11.012 -28.742 -10.771  1.00 28.30           C  
ANISOU  781  CD1 LEU B 410     2765   4614   3374   -407    217     81       C  
ATOM    782  CD2 LEU B 410       9.277 -28.462  -8.964  1.00 29.42           C  
ANISOU  782  CD2 LEU B 410     2918   4938   3322   -503    306    138       C  
ATOM    783  N   ASP B 411      12.271 -26.115  -5.930  1.00 25.77           N  
ANISOU  783  N   ASP B 411     2624   4706   2461   -533    179    254       N  
ATOM    784  CA  ASP B 411      13.450 -25.673  -5.196  1.00 27.79           C  
ANISOU  784  CA  ASP B 411     2915   5022   2620   -559    123    302       C  
ATOM    785  C   ASP B 411      14.630 -26.554  -5.556  1.00 29.33           C  
ANISOU  785  C   ASP B 411     3093   5125   2924   -542     49    421       C  
ATOM    786  O   ASP B 411      14.523 -27.438  -6.405  1.00 28.38           O  
ANISOU  786  O   ASP B 411     2940   4883   2961   -507     46    444       O  
ATOM    787  CB  ASP B 411      13.224 -25.669  -3.673  1.00 31.71           C  
ANISOU  787  CB  ASP B 411     3412   5685   2950   -650    141    374       C  
ATOM    788  CG  ASP B 411      12.938 -27.054  -3.092  1.00 33.08           C  
ANISOU  788  CG  ASP B 411     3536   5871   3160   -709    138    556       C  
ATOM    789  OD1 ASP B 411      13.166 -28.086  -3.757  1.00 36.34           O  
ANISOU  789  OD1 ASP B 411     3923   6145   3738   -683    112    640       O  
ATOM    790  OD2 ASP B 411      12.499 -27.104  -1.923  1.00 37.68           O  
ANISOU  790  OD2 ASP B 411     4103   6610   3605   -788    164    617       O  
ATOM    791  N   ARG B 412      15.746 -26.322  -4.881  1.00 32.50           N  
ANISOU  791  N   ARG B 412     3511   5596   3240   -571     -8    493       N  
ATOM    792  CA  ARG B 412      16.987 -27.001  -5.198  1.00 33.38           C  
ANISOU  792  CA  ARG B 412     3601   5638   3443   -542    -82    604       C  
ATOM    793  C   ARG B 412      16.900 -28.509  -4.966  1.00 34.62           C  
ANISOU  793  C   ARG B 412     3709   5727   3717   -555    -89    775       C  
ATOM    794  O   ARG B 412      17.435 -29.298  -5.748  1.00 34.47           O  
ANISOU  794  O   ARG B 412     3663   5573   3862   -498   -118    815       O  
ATOM    795  CB  ARG B 412      18.122 -26.404  -4.374  1.00 32.52           C  
ANISOU  795  CB  ARG B 412     3510   5655   3191   -584   -138    655       C  
ATOM    796  CG  ARG B 412      19.479 -26.717  -4.927  1.00 34.76           C  
ANISOU  796  CG  ARG B 412     3772   5879   3555   -536   -214    723       C  
ATOM    797  CD  ARG B 412      20.568 -26.066  -4.115  1.00 30.40           C  
ANISOU  797  CD  ARG B 412     3231   5475   2846   -590   -269    768       C  
ATOM    798  NE  ARG B 412      21.871 -26.513  -4.582  1.00 35.40           N  
ANISOU  798  NE  ARG B 412     3826   6068   3556   -541   -343    859       N  
ATOM    799  CZ  ARG B 412      22.493 -27.587  -4.112  1.00 36.00           C  
ANISOU  799  CZ  ARG B 412     3845   6154   3678   -537   -385   1056       C  
ATOM    800  NH1 ARG B 412      21.927 -28.319  -3.162  1.00 41.55           N  
ANISOU  800  NH1 ARG B 412     4525   6907   4357   -588   -363   1192       N  
ATOM    801  NH2 ARG B 412      23.679 -27.932  -4.593  1.00 38.37           N  
ANISOU  801  NH2 ARG B 412     4106   6420   4054   -479   -447   1126       N  
ATOM    802  N   ASN B 413      16.221 -28.903  -3.893  1.00 33.00           N  
ANISOU  802  N   ASN B 413     3491   5616   3433   -631    -59    873       N  
ATOM    803  CA  ASN B 413      16.024 -30.315  -3.588  1.00 35.29           C  
ANISOU  803  CA  ASN B 413     3734   5837   3838   -656    -61   1053       C  
ATOM    804  C   ASN B 413      15.238 -31.028  -4.684  1.00 35.11           C  
ANISOU  804  C   ASN B 413     3697   5636   4008   -617    -19    983       C  
ATOM    805  O   ASN B 413      15.620 -32.109  -5.130  1.00 37.52           O  
ANISOU  805  O   ASN B 413     3973   5790   4494   -586    -39   1068       O  
ATOM    806  CB  ASN B 413      15.313 -30.472  -2.243  1.00 38.49           C  
ANISOU  806  CB  ASN B 413     4121   6406   4099   -758    -32   1164       C  
ATOM    807  N   GLN B 414      14.141 -30.414  -5.117  1.00 34.63           N  
ANISOU  807  N   GLN B 414     3651   5599   3909   -618     43    822       N  
ATOM    808  CA  GLN B 414      13.336 -30.959  -6.205  1.00 34.65           C  
ANISOU  808  CA  GLN B 414     3631   5470   4066   -592     86    732       C  
ATOM    809  C   GLN B 414      14.126 -30.990  -7.507  1.00 33.76           C  
ANISOU  809  C   GLN B 414     3513   5226   4089   -506     53    643       C  
ATOM    810  O   GLN B 414      13.896 -31.846  -8.360  1.00 36.27           O  
ANISOU  810  O   GLN B 414     3799   5410   4574   -488     69    613       O  
ATOM    811  CB  GLN B 414      12.048 -30.151  -6.389  1.00 32.96           C  
ANISOU  811  CB  GLN B 414     3422   5342   3760   -604    155    584       C  
ATOM    812  CG  GLN B 414      11.049 -30.320  -5.258  1.00 34.72           C  
ANISOU  812  CG  GLN B 414     3631   5691   3871   -691    202    658       C  
ATOM    813  CD  GLN B 414       9.982 -29.245  -5.252  1.00 36.28           C  
ANISOU  813  CD  GLN B 414     3834   6009   3942   -685    267    507       C  
ATOM    814  OE1 GLN B 414      10.282 -28.052  -5.298  1.00 32.07           O  
ANISOU  814  OE1 GLN B 414     3336   5532   3316   -640    264    399       O  
ATOM    815  NE2 GLN B 414       8.723 -29.665  -5.205  1.00 36.64           N  
ANISOU  815  NE2 GLN B 414     3840   6089   3992   -730    328    501       N  
ATOM    816  N   GLY B 415      15.059 -30.056  -7.652  1.00 33.49           N  
ANISOU  816  N   GLY B 415     3504   5241   3978   -461      9    594       N  
ATOM    817  CA  GLY B 415      15.908 -30.003  -8.827  1.00 34.98           C  
ANISOU  817  CA  GLY B 415     3679   5339   4270   -384    -28    518       C  
ATOM    818  C   GLY B 415      16.688 -31.287  -9.041  1.00 36.54           C  
ANISOU  818  C   GLY B 415     3840   5404   4639   -357    -62    625       C  
ATOM    819  O   GLY B 415      16.930 -31.696 -10.176  1.00 35.57           O  
ANISOU  819  O   GLY B 415     3685   5174   4655   -302    -63    542       O  
ATOM    820  N   LYS B 416      17.071 -31.930  -7.942  1.00 37.81           N  
ANISOU  820  N   LYS B 416     3997   5578   4791   -393    -87    812       N  
ATOM    821  CA  LYS B 416      17.810 -33.185  -8.001  1.00 38.23           C  
ANISOU  821  CA  LYS B 416     4012   5493   5022   -360   -117    944       C  
ATOM    822  C   LYS B 416      16.973 -34.309  -8.601  1.00 39.15           C  
ANISOU  822  C   LYS B 416     4101   5441   5333   -369    -65    914       C  
ATOM    823  O   LYS B 416      17.515 -35.294  -9.100  1.00 42.76           O  
ANISOU  823  O   LYS B 416     4524   5737   5984   -321    -75    946       O  
ATOM    824  CB  LYS B 416      18.294 -33.587  -6.606  1.00 39.39           C  
ANISOU  824  CB  LYS B 416     4149   5711   5104   -404   -154   1179       C  
ATOM    825  N   SER B 417      15.652 -34.159  -8.547  1.00 43.04           N  
ANISOU  825  N   SER B 417     4604   5972   5776   -434     -5    845       N  
ATOM    826  CA  SER B 417      14.742 -35.129  -9.149  1.00 40.57           C  
ANISOU  826  CA  SER B 417     4264   5522   5628   -464     50    794       C  
ATOM    827  C   SER B 417      14.783 -35.042 -10.669  1.00 41.69           C  
ANISOU  827  C   SER B 417     4382   5590   5868   -405     66    587       C  
ATOM    828  O   SER B 417      14.278 -35.927 -11.366  1.00 40.86           O  
ANISOU  828  O   SER B 417     4245   5356   5924   -423    106    518       O  
ATOM    829  CB  SER B 417      13.311 -34.909  -8.655  1.00 41.33           C  
ANISOU  829  CB  SER B 417     4368   5717   5619   -553    108    779       C  
ATOM    830  OG  SER B 417      12.571 -34.123  -9.576  1.00 43.60           O  
ANISOU  830  OG  SER B 417     4651   6065   5850   -539    147    577       O  
ATOM    831  N   VAL B 418      15.387 -33.972 -11.179  1.00 37.33           N  
ANISOU  831  N   VAL B 418     3838   5130   5214   -345     34    488       N  
ATOM    832  CA  VAL B 418      15.428 -33.733 -12.614  1.00 32.16           C  
ANISOU  832  CA  VAL B 418     3148   4453   4616   -296     45    299       C  
ATOM    833  C   VAL B 418      16.751 -34.183 -13.218  1.00 30.64           C  
ANISOU  833  C   VAL B 418     2926   4170   4546   -217     -1    295       C  
ATOM    834  O   VAL B 418      17.812 -33.646 -12.893  1.00 26.91           O  
ANISOU  834  O   VAL B 418     2469   3757   4000   -173    -58    361       O  
ATOM    835  CB  VAL B 418      15.214 -32.245 -12.947  1.00 32.20           C  
ANISOU  835  CB  VAL B 418     3171   4616   4448   -278     42    191       C  
ATOM    836  CG1 VAL B 418      15.127 -32.051 -14.453  1.00 33.22           C  
ANISOU  836  CG1 VAL B 418     3246   4746   4630   -239     55     15       C  
ATOM    837  CG2 VAL B 418      13.966 -31.718 -12.259  1.00 32.06           C  
ANISOU  837  CG2 VAL B 418     3179   4699   4304   -340     89    196       C  
ATOM    838  N   GLU B 419      16.673 -35.175 -14.097  1.00 27.10           N  
ANISOU  838  N   GLU B 419     2430   3584   4282   -203     29    208       N  
ATOM    839  CA  GLU B 419      17.829 -35.629 -14.850  1.00 27.89           C  
ANISOU  839  CA  GLU B 419     2486   3601   4509   -121     -1    163       C  
ATOM    840  C   GLU B 419      18.460 -34.471 -15.626  1.00 27.02           C  
ANISOU  840  C   GLU B 419     2359   3635   4273    -69    -38     55       C  
ATOM    841  O   GLU B 419      17.759 -33.634 -16.205  1.00 25.37           O  
ANISOU  841  O   GLU B 419     2145   3538   3958    -93    -18    -62       O  
ATOM    842  CB  GLU B 419      17.436 -36.768 -15.800  1.00 27.73           C  
ANISOU  842  CB  GLU B 419     2413   3427   4697   -128     53     30       C  
ATOM    843  CG  GLU B 419      16.451 -36.359 -16.880  1.00 29.46           C  
ANISOU  843  CG  GLU B 419     2596   3734   4865   -171    100   -174       C  
ATOM    844  CD  GLU B 419      16.140 -37.480 -17.850  1.00 31.09           C  
ANISOU  844  CD  GLU B 419     2742   3806   5266   -191    155   -329       C  
ATOM    845  OE1 GLU B 419      16.732 -37.498 -18.951  1.00 32.13           O  
ANISOU  845  OE1 GLU B 419     2811   3955   5442   -139    151   -479       O  
ATOM    846  OE2 GLU B 419      15.300 -38.338 -17.512  1.00 34.73           O  
ANISOU  846  OE2 GLU B 419     3213   4150   5832   -266    202   -305       O  
ATOM    847  N   GLY B 420      19.788 -34.413 -15.606  1.00 30.88           N  
ANISOU  847  N   GLY B 420     2833   4126   4773      2    -95    112       N  
ATOM    848  CA  GLY B 420      20.526 -33.392 -16.329  1.00 29.32           C  
ANISOU  848  CA  GLY B 420     2613   4060   4467     46   -137     30       C  
ATOM    849  C   GLY B 420      20.775 -32.097 -15.573  1.00 27.02           C  
ANISOU  849  C   GLY B 420     2380   3914   3973     25   -182    111       C  
ATOM    850  O   GLY B 420      21.517 -31.240 -16.046  1.00 23.53           O  
ANISOU  850  O   GLY B 420     1925   3572   3445     55   -224     71       O  
ATOM    851  N   MET B 421      20.176 -31.955 -14.393  1.00 28.10           N  
ANISOU  851  N   MET B 421     2578   4067   4032    -33   -170    221       N  
ATOM    852  CA  MET B 421      20.192 -30.672 -13.693  1.00 23.14           C  
ANISOU  852  CA  MET B 421     2007   3576   3209    -67   -195    257       C  
ATOM    853  C   MET B 421      21.071 -30.662 -12.444  1.00 24.51           C  
ANISOU  853  C   MET B 421     2210   3792   3310    -79   -247    430       C  
ATOM    854  O   MET B 421      20.923 -29.784 -11.596  1.00 25.69           O  
ANISOU  854  O   MET B 421     2412   4049   3301   -130   -255    467       O  
ATOM    855  CB  MET B 421      18.765 -30.272 -13.313  1.00 27.33           C  
ANISOU  855  CB  MET B 421     2576   4143   3665   -129   -137    220       C  
ATOM    856  CG  MET B 421      17.922 -29.857 -14.508  1.00 22.88           C  
ANISOU  856  CG  MET B 421     1980   3601   3112   -121    -95     54       C  
ATOM    857  SD  MET B 421      16.558 -28.715 -14.185  1.00 28.20           S  
ANISOU  857  SD  MET B 421     2694   4377   3642   -164    -44      0       S  
ATOM    858  CE  MET B 421      17.398 -27.139 -14.331  1.00 22.76           C  
ANISOU  858  CE  MET B 421     2037   3786   2823   -134    -95    -28       C  
ATOM    859  N   VAL B 422      21.984 -31.627 -12.332  1.00 27.12           N  
ANISOU  859  N   VAL B 422     2501   4047   3756    -33   -279    532       N  
ATOM    860  CA  VAL B 422      22.839 -31.741 -11.144  1.00 28.97           C  
ANISOU  860  CA  VAL B 422     2743   4338   3927    -44   -330    722       C  
ATOM    861  C   VAL B 422      23.663 -30.471 -10.916  1.00 28.51           C  
ANISOU  861  C   VAL B 422     2708   4441   3684    -60   -385    716       C  
ATOM    862  O   VAL B 422      23.894 -30.065  -9.775  1.00 31.43           O  
ANISOU  862  O   VAL B 422     3107   4919   3915   -117   -411    825       O  
ATOM    863  CB  VAL B 422      23.797 -32.967 -11.236  1.00 29.73           C  
ANISOU  863  CB  VAL B 422     2776   4322   4200     32   -357    834       C  
ATOM    864  CG1 VAL B 422      24.595 -32.945 -12.530  1.00 28.72           C  
ANISOU  864  CG1 VAL B 422     2592   4168   4152    116   -375    706       C  
ATOM    865  CG2 VAL B 422      24.729 -33.044 -10.020  1.00 30.57           C  
ANISOU  865  CG2 VAL B 422     2872   4516   4226     23   -416   1051       C  
ATOM    866  N   GLU B 423      24.093 -29.840 -12.004  1.00 26.79           N  
ANISOU  866  N   GLU B 423     2471   4248   3462    -21   -402    585       N  
ATOM    867  CA  GLU B 423      24.872 -28.614 -11.917  1.00 23.74           C  
ANISOU  867  CA  GLU B 423     2106   3998   2917    -44   -453    569       C  
ATOM    868  C   GLU B 423      24.080 -27.424 -12.455  1.00 22.52           C  
ANISOU  868  C   GLU B 423     1996   3882   2680    -76   -423    418       C  
ATOM    869  O   GLU B 423      24.245 -26.296 -11.993  1.00 19.84           O  
ANISOU  869  O   GLU B 423     1705   3637   2196   -128   -442    407       O  
ATOM    870  CB  GLU B 423      26.193 -28.764 -12.680  1.00 26.83           C  
ANISOU  870  CB  GLU B 423     2429   4408   3359     24   -509    571       C  
ATOM    871  N   ILE B 424      23.203 -27.683 -13.420  1.00 20.65           N  
ANISOU  871  N   ILE B 424     1735   3571   2538    -49   -372    305       N  
ATOM    872  CA  ILE B 424      22.537 -26.607 -14.147  1.00 17.56           C  
ANISOU  872  CA  ILE B 424     1362   3220   2091    -60   -347    175       C  
ATOM    873  C   ILE B 424      21.555 -25.825 -13.271  1.00 17.49           C  
ANISOU  873  C   ILE B 424     1427   3246   1973   -120   -307    167       C  
ATOM    874  O   ILE B 424      21.440 -24.605 -13.397  1.00 16.97           O  
ANISOU  874  O   ILE B 424     1396   3233   1818   -137   -308    105       O  
ATOM    875  CB  ILE B 424      21.811 -27.160 -15.391  1.00 19.16           C  
ANISOU  875  CB  ILE B 424     1503   3362   2414    -22   -302     63       C  
ATOM    876  CG1 ILE B 424      22.830 -27.635 -16.433  1.00 21.77           C  
ANISOU  876  CG1 ILE B 424     1752   3688   2830     38   -339     28       C  
ATOM    877  CG2 ILE B 424      20.907 -26.114 -16.006  1.00 19.95           C  
ANISOU  877  CG2 ILE B 424     1614   3512   2456    -35   -269    -41       C  
ATOM    878  CD1 ILE B 424      22.237 -28.529 -17.500  1.00 20.95           C  
ANISOU  878  CD1 ILE B 424     1578   3521   2861     67   -292    -81       C  
ATOM    879  N   PHE B 425      20.864 -26.524 -12.376  1.00 18.03           N  
ANISOU  879  N   PHE B 425     1515   3284   2051   -151   -271    231       N  
ATOM    880  CA  PHE B 425      19.893 -25.883 -11.490  1.00 18.15           C  
ANISOU  880  CA  PHE B 425     1588   3348   1958   -206   -226    218       C  
ATOM    881  C   PHE B 425      20.536 -24.736 -10.702  1.00 18.22           C  
ANISOU  881  C   PHE B 425     1653   3455   1815   -250   -260    230       C  
ATOM    882  O   PHE B 425      20.011 -23.622 -10.668  1.00 17.89           O  
ANISOU  882  O   PHE B 425     1654   3445   1698   -267   -231    141       O  
ATOM    883  CB  PHE B 425      19.290 -26.910 -10.527  1.00 21.39           C  
ANISOU  883  CB  PHE B 425     1999   3737   2390   -244   -195    318       C  
ATOM    884  CG  PHE B 425      17.949 -26.516  -9.981  1.00 19.35           C  
ANISOU  884  CG  PHE B 425     1774   3520   2060   -287   -127    273       C  
ATOM    885  CD1 PHE B 425      17.848 -25.620  -8.932  1.00 26.07           C  
ANISOU  885  CD1 PHE B 425     2676   4475   2754   -339   -120    275       C  
ATOM    886  CD2 PHE B 425      16.788 -27.047 -10.517  1.00 20.54           C  
ANISOU  886  CD2 PHE B 425     1894   3614   2294   -280    -69    220       C  
ATOM    887  CE1 PHE B 425      16.614 -25.259  -8.428  1.00 24.51           C  
ANISOU  887  CE1 PHE B 425     2499   4324   2490   -371    -52    223       C  
ATOM    888  CE2 PHE B 425      15.550 -26.688 -10.019  1.00 23.11           C  
ANISOU  888  CE2 PHE B 425     2238   3993   2548   -315     -5    181       C  
ATOM    889  CZ  PHE B 425      15.468 -25.791  -8.970  1.00 24.67           C  
ANISOU  889  CZ  PHE B 425     2485   4293   2593   -355      4    183       C  
ATOM    890  N   ASP B 426      21.680 -25.017 -10.086  1.00 18.32           N  
ANISOU  890  N   ASP B 426     1660   3514   1789   -269   -319    338       N  
ATOM    891  CA  ASP B 426      22.409 -24.009  -9.323  1.00 18.58           C  
ANISOU  891  CA  ASP B 426     1736   3654   1670   -328   -357    348       C  
ATOM    892  C   ASP B 426      22.919 -22.889 -10.220  1.00 17.85           C  
ANISOU  892  C   ASP B 426     1656   3562   1562   -312   -383    249       C  
ATOM    893  O   ASP B 426      22.967 -21.731  -9.806  1.00 20.14           O  
ANISOU  893  O   ASP B 426     2002   3904   1747   -364   -382    189       O  
ATOM    894  CB  ASP B 426      23.581 -24.641  -8.570  1.00 21.60           C  
ANISOU  894  CB  ASP B 426     2087   4104   2014   -349   -420    501       C  
ATOM    895  CG  ASP B 426      23.135 -25.441  -7.365  1.00 27.24           C  
ANISOU  895  CG  ASP B 426     2797   4859   2693   -394   -400    623       C  
ATOM    896  OD1 ASP B 426      22.032 -25.173  -6.852  1.00 26.05           O  
ANISOU  896  OD1 ASP B 426     2683   4726   2487   -435   -340    573       O  
ATOM    897  OD2 ASP B 426      23.896 -26.328  -6.919  1.00 28.45           O  
ANISOU  897  OD2 ASP B 426     2903   5035   2873   -387   -443    780       O  
ATOM    898  N   MET B 427      23.306 -23.236 -11.443  1.00 18.68           N  
ANISOU  898  N   MET B 427     1706   3616   1778   -246   -406    229       N  
ATOM    899  CA  MET B 427      23.777 -22.240 -12.396  1.00 18.00           C  
ANISOU  899  CA  MET B 427     1615   3541   1683   -234   -434    154       C  
ATOM    900  C   MET B 427      22.653 -21.254 -12.723  1.00 17.54           C  
ANISOU  900  C   MET B 427     1598   3451   1617   -235   -377     45       C  
ATOM    901  O   MET B 427      22.872 -20.038 -12.760  1.00 17.46           O  
ANISOU  901  O   MET B 427     1629   3458   1545   -265   -388     -2       O  
ATOM    902  CB  MET B 427      24.294 -22.915 -13.671  1.00 17.58           C  
ANISOU  902  CB  MET B 427     1476   3459   1743   -163   -462    148       C  
ATOM    903  CG  MET B 427      25.673 -23.548 -13.537  1.00 18.05           C  
ANISOU  903  CG  MET B 427     1488   3563   1809   -149   -529    244       C  
ATOM    904  SD  MET B 427      26.120 -24.539 -14.977  1.00 20.76           S  
ANISOU  904  SD  MET B 427     1748   3828   2311    -53   -523    206       S  
ATOM    905  CE  MET B 427      27.741 -25.124 -14.510  1.00 32.92           C  
ANISOU  905  CE  MET B 427     3273   5385   3850    -34   -575    319       C  
ATOM    906  N   LEU B 428      21.453 -21.786 -12.952  1.00 15.40           N  
ANISOU  906  N   LEU B 428     1310   3129   1411   -203   -314     11       N  
ATOM    907  CA  LEU B 428      20.289 -20.957 -13.251  1.00 15.11           C  
ANISOU  907  CA  LEU B 428     1296   3070   1373   -191   -254    -79       C  
ATOM    908  C   LEU B 428      19.932 -20.057 -12.072  1.00 15.67           C  
ANISOU  908  C   LEU B 428     1449   3167   1338   -244   -223   -106       C  
ATOM    909  O   LEU B 428      19.652 -18.871 -12.257  1.00 15.61           O  
ANISOU  909  O   LEU B 428     1477   3144   1310   -243   -203   -176       O  
ATOM    910  CB  LEU B 428      19.092 -21.828 -13.639  1.00 15.00           C  
ANISOU  910  CB  LEU B 428     1237   3020   1440   -156   -194   -102       C  
ATOM    911  CG  LEU B 428      19.232 -22.548 -14.982  1.00 14.53           C  
ANISOU  911  CG  LEU B 428     1090   2940   1490   -107   -208   -122       C  
ATOM    912  CD1 LEU B 428      18.268 -23.702 -15.075  1.00 14.75           C  
ANISOU  912  CD1 LEU B 428     1079   2929   1595   -100   -156   -132       C  
ATOM    913  CD2 LEU B 428      19.004 -21.589 -16.135  1.00 13.95           C  
ANISOU  913  CD2 LEU B 428      983   2892   1427    -75   -206   -189       C  
ATOM    914  N   LEU B 429      19.950 -20.623 -10.867  1.00 16.66           N  
ANISOU  914  N   LEU B 429     1599   3334   1398   -293   -217    -49       N  
ATOM    915  CA  LEU B 429      19.681 -19.855  -9.652  1.00 17.41           C  
ANISOU  915  CA  LEU B 429     1761   3484   1371   -356   -187    -85       C  
ATOM    916  C   LEU B 429      20.650 -18.691  -9.502  1.00 17.59           C  
ANISOU  916  C   LEU B 429     1831   3531   1322   -402   -229   -123       C  
ATOM    917  O   LEU B 429      20.260 -17.585  -9.126  1.00 17.99           O  
ANISOU  917  O   LEU B 429     1938   3573   1322   -428   -190   -218       O  
ATOM    918  CB  LEU B 429      19.763 -20.746  -8.411  1.00 18.27           C  
ANISOU  918  CB  LEU B 429     1867   3669   1406   -413   -189     11       C  
ATOM    919  CG  LEU B 429      18.608 -21.723  -8.189  1.00 18.51           C  
ANISOU  919  CG  LEU B 429     1868   3686   1480   -398   -132     43       C  
ATOM    920  CD1 LEU B 429      18.890 -22.601  -6.976  1.00 19.49           C  
ANISOU  920  CD1 LEU B 429     1980   3893   1533   -461   -150    172       C  
ATOM    921  CD2 LEU B 429      17.286 -20.986  -8.031  1.00 18.99           C  
ANISOU  921  CD2 LEU B 429     1955   3750   1510   -391    -49    -69       C  
ATOM    922  N   ALA B 430      21.918 -18.954  -9.792  1.00 17.51           N  
ANISOU  922  N   ALA B 430     1793   3546   1312   -414   -306    -52       N  
ATOM    923  CA  ALA B 430      22.946 -17.930  -9.695  1.00 19.52           C  
ANISOU  923  CA  ALA B 430     2084   3834   1497   -471   -355    -76       C  
ATOM    924  C   ALA B 430      22.674 -16.802 -10.686  1.00 17.25           C  
ANISOU  924  C   ALA B 430     1816   3464   1275   -439   -340   -165       C  
ATOM    925  O   ALA B 430      22.953 -15.640 -10.407  1.00 20.42           O  
ANISOU  925  O   ALA B 430     2276   3855   1628   -494   -341   -229       O  
ATOM    926  CB  ALA B 430      24.318 -18.531  -9.934  1.00 20.12           C  
ANISOU  926  CB  ALA B 430     2109   3968   1569   -478   -441     27       C  
ATOM    927  N   THR B 431      22.108 -17.147 -11.838  1.00 16.83           N  
ANISOU  927  N   THR B 431     1709   3352   1334   -355   -324   -166       N  
ATOM    928  CA  THR B 431      21.817 -16.146 -12.856  1.00 21.20           C  
ANISOU  928  CA  THR B 431     2261   3842   1953   -318   -313   -220       C  
ATOM    929  C   THR B 431      20.650 -15.258 -12.420  1.00 16.21           C  
ANISOU  929  C   THR B 431     1686   3151   1322   -309   -232   -309       C  
ATOM    930  O   THR B 431      20.696 -14.038 -12.578  1.00 16.55           O  
ANISOU  930  O   THR B 431     1772   3138   1379   -320   -224   -360       O  
ATOM    931  CB  THR B 431      21.503 -16.802 -14.212  1.00 18.70           C  
ANISOU  931  CB  THR B 431     1852   3515   1739   -238   -317   -195       C  
ATOM    932  OG1 THR B 431      22.539 -17.736 -14.541  1.00 18.27           O  
ANISOU  932  OG1 THR B 431     1739   3511   1692   -237   -381   -128       O  
ATOM    933  CG2 THR B 431      21.402 -15.752 -15.309  1.00 14.67           C  
ANISOU  933  CG2 THR B 431     1321   2970   1283   -209   -322   -218       C  
ATOM    934  N   SER B 432      19.612 -15.871 -11.863  1.00 19.40           N  
ANISOU  934  N   SER B 432     2088   3567   1717   -287   -170   -327       N  
ATOM    935  CA  SER B 432      18.465 -15.107 -11.391  1.00 17.30           C  
ANISOU  935  CA  SER B 432     1865   3262   1447   -269    -86   -416       C  
ATOM    936  C   SER B 432      18.878 -14.208 -10.232  1.00 20.08           C  
ANISOU  936  C   SER B 432     2303   3625   1703   -351    -77   -486       C  
ATOM    937  O   SER B 432      18.443 -13.060 -10.140  1.00 19.75           O  
ANISOU  937  O   SER B 432     2309   3512   1683   -341    -29   -578       O  
ATOM    938  CB  SER B 432      17.322 -16.040 -10.982  1.00 21.04           C  
ANISOU  938  CB  SER B 432     2307   3772   1914   -242    -25   -412       C  
ATOM    939  OG  SER B 432      17.650 -16.763  -9.810  1.00 32.65           O  
ANISOU  939  OG  SER B 432     3796   5320   3287   -312    -36   -374       O  
ATOM    940  N   SER B 433      19.732 -14.732  -9.359  1.00 18.47           N  
ANISOU  940  N   SER B 433     2112   3510   1395   -432   -121   -443       N  
ATOM    941  CA  SER B 433      20.300 -13.938  -8.278  1.00 22.71           C  
ANISOU  941  CA  SER B 433     2718   4090   1820   -532   -123   -510       C  
ATOM    942  C   SER B 433      21.026 -12.718  -8.837  1.00 24.40           C  
ANISOU  942  C   SER B 433     2973   4223   2075   -556   -155   -557       C  
ATOM    943  O   SER B 433      20.883 -11.610  -8.319  1.00 28.71           O  
ANISOU  943  O   SER B 433     3588   4722   2601   -600   -113   -672       O  
ATOM    944  CB  SER B 433      21.257 -14.783  -7.429  1.00 24.59           C  
ANISOU  944  CB  SER B 433     2939   4464   1940   -614   -183   -420       C  
ATOM    945  OG  SER B 433      22.180 -13.968  -6.722  1.00 36.20           O  
ANISOU  945  OG  SER B 433     4460   5990   3305   -723   -213   -470       O  
ATOM    946  N   ARG B 434      21.794 -12.926  -9.903  1.00 21.07           N  
ANISOU  946  N   ARG B 434     2505   3784   1715   -532   -226   -470       N  
ATOM    947  CA  ARG B 434      22.569 -11.847 -10.512  1.00 21.72           C  
ANISOU  947  CA  ARG B 434     2613   3803   1836   -565   -268   -486       C  
ATOM    948  C   ARG B 434      21.646 -10.814 -11.159  1.00 19.31           C  
ANISOU  948  C   ARG B 434     2330   3356   1649   -497   -207   -552       C  
ATOM    949  O   ARG B 434      21.873  -9.613 -11.029  1.00 20.17           O  
ANISOU  949  O   ARG B 434     2502   3381   1780   -543   -196   -622       O  
ATOM    950  CB  ARG B 434      23.558 -12.408 -11.538  1.00 21.45           C  
ANISOU  950  CB  ARG B 434     2505   3812   1832   -550   -356   -371       C  
ATOM    951  CG  ARG B 434      24.346 -11.360 -12.325  1.00 22.97           C  
ANISOU  951  CG  ARG B 434     2706   3953   2068   -584   -405   -363       C  
ATOM    952  CD  ARG B 434      25.378 -10.638 -11.466  1.00 24.31           C  
ANISOU  952  CD  ARG B 434     2941   4159   2138   -718   -441   -401       C  
ATOM    953  NE  ARG B 434      26.127  -9.645 -12.234  1.00 21.51           N  
ANISOU  953  NE  ARG B 434     2593   3751   1830   -763   -490   -384       N  
ATOM    954  CZ  ARG B 434      26.635  -8.525 -11.725  1.00 26.46           C  
ANISOU  954  CZ  ARG B 434     3296   4331   2427   -873   -494   -455       C  
ATOM    955  NH1 ARG B 434      26.476  -8.243 -10.438  1.00 26.62           N  
ANISOU  955  NH1 ARG B 434     3389   4364   2360   -950   -449   -565       N  
ATOM    956  NH2 ARG B 434      27.306  -7.686 -12.504  1.00 25.72           N  
ANISOU  956  NH2 ARG B 434     3200   4185   2388   -916   -541   -420       N  
ATOM    957  N   PHE B 435      20.609 -11.282 -11.855  1.00 18.32           N  
ANISOU  957  N   PHE B 435     2148   3206   1606   -390   -166   -526       N  
ATOM    958  CA  PHE B 435      19.585 -10.384 -12.389  1.00 18.63           C  
ANISOU  958  CA  PHE B 435     2193   3130   1754   -311   -101   -574       C  
ATOM    959  C   PHE B 435      18.965  -9.514 -11.297  1.00 20.82           C  
ANISOU  959  C   PHE B 435     2556   3344   2010   -332    -18   -708       C  
ATOM    960  O   PHE B 435      18.741  -8.319 -11.488  1.00 20.75           O  
ANISOU  960  O   PHE B 435     2588   3208   2086   -313     16   -766       O  
ATOM    961  CB  PHE B 435      18.475 -11.171 -13.093  1.00 18.69           C  
ANISOU  961  CB  PHE B 435     2118   3163   1822   -205    -63   -532       C  
ATOM    962  CG  PHE B 435      18.812 -11.594 -14.495  1.00 21.61           C  
ANISOU  962  CG  PHE B 435     2395   3563   2254   -163   -122   -432       C  
ATOM    963  CD1 PHE B 435      20.003 -11.217 -15.088  1.00 22.88           C  
ANISOU  963  CD1 PHE B 435     2547   3726   2420   -209   -201   -378       C  
ATOM    964  CD2 PHE B 435      17.909 -12.335 -15.234  1.00 23.75           C  
ANISOU  964  CD2 PHE B 435     2579   3874   2571    -84    -94   -401       C  
ATOM    965  CE1 PHE B 435      20.301 -11.602 -16.387  1.00 26.68           C  
ANISOU  965  CE1 PHE B 435     2931   4261   2946   -172   -251   -295       C  
ATOM    966  CE2 PHE B 435      18.195 -12.721 -16.533  1.00 22.34           C  
ANISOU  966  CE2 PHE B 435     2305   3745   2438    -53   -143   -328       C  
ATOM    967  CZ  PHE B 435      19.391 -12.354 -17.105  1.00 20.23           C  
ANISOU  967  CZ  PHE B 435     2027   3489   2171    -95   -220   -277       C  
ATOM    968  N   ARG B 436      18.681 -10.130 -10.155  1.00 24.61           N  
ANISOU  968  N   ARG B 436     3055   3915   2382   -371     15   -757       N  
ATOM    969  CA  ARG B 436      18.078  -9.419  -9.038  1.00 25.86           C  
ANISOU  969  CA  ARG B 436     3281   4049   2496   -397     99   -901       C  
ATOM    970  C   ARG B 436      19.025  -8.371  -8.481  1.00 24.43           C  
ANISOU  970  C   ARG B 436     3183   3821   2277   -506     80   -989       C  
ATOM    971  O   ARG B 436      18.622  -7.244  -8.199  1.00 33.94           O  
ANISOU  971  O   ARG B 436     4448   4910   3539   -501    146  -1116       O  
ATOM    972  CB  ARG B 436      17.673 -10.397  -7.938  1.00 29.18           C  
ANISOU  972  CB  ARG B 436     3687   4615   2783   -432    128   -914       C  
ATOM    973  CG  ARG B 436      16.763  -9.803  -6.876  1.00 33.70           C  
ANISOU  973  CG  ARG B 436     4304   5193   3308   -437    231  -1068       C  
ATOM    974  CD  ARG B 436      16.446 -10.845  -5.825  1.00 38.84           C  
ANISOU  974  CD  ARG B 436     4926   6017   3813   -486    248  -1051       C  
ATOM    975  NE  ARG B 436      16.135 -12.120  -6.452  1.00 40.36           N  
ANISOU  975  NE  ARG B 436     5041   6255   4038   -429    217   -905       N  
ATOM    976  CZ  ARG B 436      16.854 -13.228  -6.302  1.00 33.76           C  
ANISOU  976  CZ  ARG B 436     4171   5518   3140   -481    146   -782       C  
ATOM    977  NH1 ARG B 436      17.931 -13.221  -5.529  1.00 32.23           N  
ANISOU  977  NH1 ARG B 436     4005   5410   2830   -591     94   -771       N  
ATOM    978  NH2 ARG B 436      16.493 -14.343  -6.927  1.00 26.32           N  
ANISOU  978  NH2 ARG B 436     3162   4586   2254   -425    129   -670       N  
ATOM    979  N   MET B 437      20.291  -8.746  -8.337  1.00 22.83           N  
ANISOU  979  N   MET B 437     2979   3708   1987   -606     -9   -925       N  
ATOM    980  CA  MET B 437      21.289  -7.845  -7.784  1.00 29.41           C  
ANISOU  980  CA  MET B 437     3883   4528   2764   -733    -36  -1003       C  
ATOM    981  C   MET B 437      21.478  -6.642  -8.705  1.00 29.26           C  
ANISOU  981  C   MET B 437     3897   4326   2895   -713    -42  -1016       C  
ATOM    982  O   MET B 437      21.752  -5.533  -8.248  1.00 28.63           O  
ANISOU  982  O   MET B 437     3894   4154   2829   -790    -15  -1137       O  
ATOM    983  CB  MET B 437      22.611  -8.586  -7.560  1.00 29.36           C  
ANISOU  983  CB  MET B 437     3847   4677   2633   -833   -136   -901       C  
ATOM    984  CG  MET B 437      23.858  -7.746  -7.745  1.00 33.34           C  
ANISOU  984  CG  MET B 437     4387   5153   3128   -941   -202   -908       C  
ATOM    985  SD  MET B 437      25.303  -8.594  -7.096  1.00 59.90           S  
ANISOU  985  SD  MET B 437     7710   8743   6305  -1068   -303   -813       S  
ATOM    986  CE  MET B 437      25.035  -8.317  -5.354  1.00 30.95           C  
ANISOU  986  CE  MET B 437     4090   5148   2520  -1150   -225   -938       C  
ATOM    987  N   MET B 438      21.293  -6.860 -10.003  1.00 25.82           N  
ANISOU  987  N   MET B 438     3801   3194   2815   -882    -54   -643       N  
ATOM    988  CA  MET B 438      21.429  -5.786 -10.980  1.00 26.10           C  
ANISOU  988  CA  MET B 438     3794   3126   2997   -712    -47   -655       C  
ATOM    989  C   MET B 438      20.130  -5.014 -11.181  1.00 22.22           C  
ANISOU  989  C   MET B 438     3232   2678   2533   -572     91   -790       C  
ATOM    990  O   MET B 438      20.114  -3.990 -11.864  1.00 23.31           O  
ANISOU  990  O   MET B 438     3344   2720   2790   -435     95   -814       O  
ATOM    991  CB  MET B 438      21.884  -6.341 -12.325  1.00 22.32           C  
ANISOU  991  CB  MET B 438     3213   2622   2644   -636   -120   -522       C  
ATOM    992  CG  MET B 438      23.280  -6.915 -12.342  1.00 28.22           C  
ANISOU  992  CG  MET B 438     4003   3301   3419   -729   -255   -391       C  
ATOM    993  SD  MET B 438      23.686  -7.308 -14.042  1.00 20.87           S  
ANISOU  993  SD  MET B 438     2947   2346   2636   -605   -296   -277       S  
ATOM    994  CE  MET B 438      23.733  -5.658 -14.735  1.00 24.93           C  
ANISOU  994  CE  MET B 438     3460   2762   3251   -469   -270   -312       C  
ATOM    995  N   ASN B 439      19.053  -5.514 -10.582  1.00 19.60           N  
ANISOU  995  N   ASN B 439     2860   2488   2098   -613    197   -868       N  
ATOM    996  CA  ASN B 439      17.704  -4.996 -10.811  1.00 22.01           C  
ANISOU  996  CA  ASN B 439     3056   2861   2444   -478    335   -985       C  
ATOM    997  C   ASN B 439      17.393  -4.904 -12.308  1.00 22.08           C  
ANISOU  997  C   ASN B 439     2930   2839   2622   -318    305   -910       C  
ATOM    998  O   ASN B 439      17.042  -3.841 -12.829  1.00 23.51           O  
ANISOU  998  O   ASN B 439     3070   2942   2921   -170    334   -967       O  
ATOM    999  CB  ASN B 439      17.518  -3.633 -10.139  1.00 27.24           C  
ANISOU  999  CB  ASN B 439     3797   3448   3105   -416    416  -1149       C  
ATOM   1000  CG  ASN B 439      16.068  -3.190 -10.126  1.00 30.14           C  
ANISOU 1000  CG  ASN B 439     4044   3901   3507   -288    575  -1289       C  
ATOM   1001  OD1 ASN B 439      15.158  -4.021 -10.096  1.00 35.72           O  
ANISOU 1001  OD1 ASN B 439     4638   4769   4164   -316    649  -1284       O  
ATOM   1002  ND2 ASN B 439      15.841  -1.881 -10.160  1.00 36.29           N  
ANISOU 1002  ND2 ASN B 439     4837   4569   4383   -148    621  -1411       N  
ATOM   1003  N   LEU B 440      17.539  -6.029 -12.996  1.00 18.10           N  
ANISOU 1003  N   LEU B 440     2365   2386   2126   -357    237   -782       N  
ATOM   1004  CA  LEU B 440      17.265  -6.084 -14.425  1.00 17.19           C  
ANISOU 1004  CA  LEU B 440     2137   2253   2140   -234    203   -704       C  
ATOM   1005  C   LEU B 440      15.830  -5.673 -14.729  1.00 21.75           C  
ANISOU 1005  C   LEU B 440     2586   2901   2776   -115    305   -782       C  
ATOM   1006  O   LEU B 440      14.893  -6.127 -14.076  1.00 22.12           O  
ANISOU 1006  O   LEU B 440     2580   3080   2744   -160    396   -844       O  
ATOM   1007  CB  LEU B 440      17.532  -7.488 -14.962  1.00 16.39           C  
ANISOU 1007  CB  LEU B 440     2006   2210   2012   -308    128   -579       C  
ATOM   1008  CG  LEU B 440      17.325  -7.675 -16.465  1.00 17.59           C  
ANISOU 1008  CG  LEU B 440     2063   2350   2270   -205     86   -496       C  
ATOM   1009  CD1 LEU B 440      18.407  -6.942 -17.221  1.00 18.16           C  
ANISOU 1009  CD1 LEU B 440     2177   2288   2434   -143     15   -440       C  
ATOM   1010  CD2 LEU B 440      17.306  -9.155 -16.828  1.00 14.23           C  
ANISOU 1010  CD2 LEU B 440     1611   1998   1799   -283     32   -408       C  
ATOM   1011  N   GLN B 441      15.667  -4.810 -15.725  1.00 16.66           N  
ANISOU 1011  N   GLN B 441     1885   2170   2275     29    282   -769       N  
ATOM   1012  CA  GLN B 441      14.349  -4.327 -16.107  1.00 17.69           C  
ANISOU 1012  CA  GLN B 441     1880   2344   2498    156    356   -829       C  
ATOM   1013  C   GLN B 441      13.795  -5.089 -17.306  1.00 20.00           C  
ANISOU 1013  C   GLN B 441     2056   2700   2842    184    307   -714       C  
ATOM   1014  O   GLN B 441      14.555  -5.642 -18.103  1.00 20.18           O  
ANISOU 1014  O   GLN B 441     2114   2690   2864    147    210   -598       O  
ATOM   1015  CB  GLN B 441      14.411  -2.831 -16.405  1.00 20.03           C  
ANISOU 1015  CB  GLN B 441     2189   2491   2931    295    346   -887       C  
ATOM   1016  CG  GLN B 441      14.992  -2.030 -15.254  1.00 21.81           C  
ANISOU 1016  CG  GLN B 441     2550   2633   3103    266    381  -1005       C  
ATOM   1017  CD  GLN B 441      14.026  -1.930 -14.093  1.00 27.17           C  
ANISOU 1017  CD  GLN B 441     3201   3411   3709    264    535  -1171       C  
ATOM   1018  OE1 GLN B 441      12.961  -1.322 -14.206  1.00 29.09           O  
ANISOU 1018  OE1 GLN B 441     3333   3667   4054    396    616  -1262       O  
ATOM   1019  NE2 GLN B 441      14.380  -2.554 -12.975  1.00 27.05           N  
ANISOU 1019  NE2 GLN B 441     3284   3476   3519    109    575  -1208       N  
ATOM   1020  N   GLY B 442      12.469  -5.121 -17.418  1.00 20.10           N  
ANISOU 1020  N   GLY B 442     1929   2808   2901    245    377   -752       N  
ATOM   1021  CA  GLY B 442      11.798  -5.843 -18.485  1.00 21.51           C  
ANISOU 1021  CA  GLY B 442     1997   3054   3122    259    326   -646       C  
ATOM   1022  C   GLY B 442      12.257  -5.417 -19.864  1.00 19.98           C  
ANISOU 1022  C   GLY B 442     1810   2747   3035    333    213   -544       C  
ATOM   1023  O   GLY B 442      12.471  -6.248 -20.745  1.00 16.29           O  
ANISOU 1023  O   GLY B 442     1345   2303   2542    287    136   -433       O  
ATOM   1024  N   GLU B 443      12.416  -4.111 -20.045  1.00 20.45           N  
ANISOU 1024  N   GLU B 443     1882   2681   3209    441    201   -583       N  
ATOM   1025  CA  GLU B 443      12.902  -3.563 -21.305  1.00 20.93           C  
ANISOU 1025  CA  GLU B 443     1959   2630   3363    497     90   -481       C  
ATOM   1026  C   GLU B 443      14.310  -4.052 -21.638  1.00 14.94           C  
ANISOU 1026  C   GLU B 443     1323   1831   2524    406     20   -396       C  
ATOM   1027  O   GLU B 443      14.619  -4.350 -22.794  1.00 18.53           O  
ANISOU 1027  O   GLU B 443     1777   2275   2989    397    -58   -286       O  
ATOM   1028  CB  GLU B 443      12.867  -2.037 -21.256  1.00 20.87           C  
ANISOU 1028  CB  GLU B 443     1957   2482   3492    616     81   -543       C  
ATOM   1029  CG  GLU B 443      11.460  -1.475 -21.166  1.00 25.59           C  
ANISOU 1029  CG  GLU B 443     2408   3100   4215    736    137   -618       C  
ATOM   1030  CD  GLU B 443      10.928  -1.430 -19.748  1.00 29.38           C  
ANISOU 1030  CD  GLU B 443     2869   3650   4645    742    285   -784       C  
ATOM   1031  OE1 GLU B 443      11.692  -1.727 -18.803  1.00 35.38           O  
ANISOU 1031  OE1 GLU B 443     3749   4426   5269    645    330   -838       O  
ATOM   1032  OE2 GLU B 443       9.724  -1.135 -19.579  1.00 37.05           O  
ANISOU 1032  OE2 GLU B 443     3719   4670   5687    820    352   -836       O  
ATOM   1033  N   GLU B 444      15.161  -4.146 -20.625  1.00 16.97           N  
ANISOU 1033  N   GLU B 444     1681   2070   2698    334     48   -447       N  
ATOM   1034  CA  GLU B 444      16.507  -4.673 -20.832  1.00 15.60           C  
ANISOU 1034  CA  GLU B 444     1603   1863   2463    248    -15   -367       C  
ATOM   1035  C   GLU B 444      16.461  -6.166 -21.148  1.00 12.57           C  
ANISOU 1035  C   GLU B 444     1198   1583   1995    168    -29   -304       C  
ATOM   1036  O   GLU B 444      17.189  -6.641 -22.020  1.00 14.70           O  
ANISOU 1036  O   GLU B 444     1493   1836   2258    146    -90   -216       O  
ATOM   1037  CB  GLU B 444      17.386  -4.423 -19.609  1.00 16.03           C  
ANISOU 1037  CB  GLU B 444     1765   1869   2457    180      3   -428       C  
ATOM   1038  CG  GLU B 444      17.592  -2.951 -19.281  1.00 17.20           C  
ANISOU 1038  CG  GLU B 444     1964   1891   2682    248      1   -492       C  
ATOM   1039  CD  GLU B 444      18.271  -2.741 -17.939  1.00 21.02           C  
ANISOU 1039  CD  GLU B 444     2563   2337   3086    167     22   -568       C  
ATOM   1040  OE1 GLU B 444      17.901  -3.436 -16.967  1.00 21.22           O  
ANISOU 1040  OE1 GLU B 444     2599   2458   3006     92     88   -632       O  
ATOM   1041  OE2 GLU B 444      19.170  -1.877 -17.865  1.00 20.97           O  
ANISOU 1041  OE2 GLU B 444     2643   2208   3118    165    -35   -556       O  
ATOM   1042  N   PHE B 445      15.594  -6.892 -20.445  1.00 13.66           N  
ANISOU 1042  N   PHE B 445     1291   1829   2068    124     27   -353       N  
ATOM   1043  CA  PHE B 445      15.440  -8.335 -20.641  1.00 12.99           C  
ANISOU 1043  CA  PHE B 445     1194   1837   1907     39      1   -296       C  
ATOM   1044  C   PHE B 445      15.071  -8.697 -22.086  1.00 12.59           C  
ANISOU 1044  C   PHE B 445     1088   1798   1897     80    -56   -210       C  
ATOM   1045  O   PHE B 445      15.675  -9.591 -22.679  1.00 13.69           O  
ANISOU 1045  O   PHE B 445     1269   1936   1996     32   -112   -146       O  
ATOM   1046  CB  PHE B 445      14.391  -8.884 -19.667  1.00 15.13           C  
ANISOU 1046  CB  PHE B 445     1411   2230   2109    -19     72   -356       C  
ATOM   1047  CG  PHE B 445      13.825 -10.222 -20.067  1.00 13.44           C  
ANISOU 1047  CG  PHE B 445     1153   2112   1841    -89     34   -291       C  
ATOM   1048  CD1 PHE B 445      14.596 -11.370 -19.982  1.00 13.38           C  
ANISOU 1048  CD1 PHE B 445     1222   2100   1760   -191    -31   -237       C  
ATOM   1049  CD2 PHE B 445      12.519 -10.332 -20.520  1.00 15.68           C  
ANISOU 1049  CD2 PHE B 445     1318   2480   2159    -54     53   -279       C  
ATOM   1050  CE1 PHE B 445      14.078 -12.603 -20.350  1.00 13.44           C  
ANISOU 1050  CE1 PHE B 445     1204   2178   1723   -257    -80   -180       C  
ATOM   1051  CE2 PHE B 445      11.995 -11.561 -20.889  1.00 17.83           C  
ANISOU 1051  CE2 PHE B 445     1561   2834   2381   -131      3   -212       C  
ATOM   1052  CZ  PHE B 445      12.781 -12.696 -20.806  1.00 16.73           C  
ANISOU 1052  CZ  PHE B 445     1515   2681   2161   -233    -65   -166       C  
ATOM   1053  N   VAL B 446      14.087  -8.007 -22.658  1.00 13.30           N  
ANISOU 1053  N   VAL B 446     1089   1895   2070    167    -48   -211       N  
ATOM   1054  CA  VAL B 446      13.679  -8.332 -24.024  1.00 13.10           C  
ANISOU 1054  CA  VAL B 446     1021   1883   2072    188   -116   -122       C  
ATOM   1055  C   VAL B 446      14.797  -8.007 -25.018  1.00 13.75           C  
ANISOU 1055  C   VAL B 446     1178   1877   2169    202   -177    -56       C  
ATOM   1056  O   VAL B 446      14.952  -8.702 -26.025  1.00 13.81           O  
ANISOU 1056  O   VAL B 446     1205   1903   2139    173   -228     13       O  
ATOM   1057  CB  VAL B 446      12.374  -7.609 -24.435  1.00 14.22           C  
ANISOU 1057  CB  VAL B 446     1041   2044   2319    274   -113   -121       C  
ATOM   1058  CG1 VAL B 446      11.205  -8.125 -23.606  1.00 17.71           C  
ANISOU 1058  CG1 VAL B 446     1384   2605   2739    248    -46   -172       C  
ATOM   1059  CG2 VAL B 446      12.514  -6.096 -24.322  1.00 14.95           C  
ANISOU 1059  CG2 VAL B 446     1127   2030   2524    376   -101   -163       C  
ATOM   1060  N   CYS B 447      15.584  -6.972 -24.728  1.00 13.91           N  
ANISOU 1060  N   CYS B 447     1245   1806   2236    239   -169    -78       N  
ATOM   1061  CA  CYS B 447      16.747  -6.653 -25.553  1.00 12.59           C  
ANISOU 1061  CA  CYS B 447     1142   1566   2074    235   -218    -10       C  
ATOM   1062  C   CYS B 447      17.764  -7.783 -25.516  1.00 11.62           C  
ANISOU 1062  C   CYS B 447     1082   1466   1866    158   -221     10       C  
ATOM   1063  O   CYS B 447      18.268  -8.206 -26.557  1.00 12.72           O  
ANISOU 1063  O   CYS B 447     1243   1611   1980    144   -253     71       O  
ATOM   1064  CB  CYS B 447      17.410  -5.353 -25.103  1.00 16.17           C  
ANISOU 1064  CB  CYS B 447     1636   1915   2593    272   -219    -34       C  
ATOM   1065  SG  CYS B 447      16.531  -3.860 -25.598  1.00 18.00           S  
ANISOU 1065  SG  CYS B 447     1808   2070   2960    379   -255    -29       S  
ATOM   1066  N   LEU B 448      18.062  -8.262 -24.313  1.00 12.59           N  
ANISOU 1066  N   LEU B 448     1235   1602   1947    106   -190    -44       N  
ATOM   1067  CA  LEU B 448      19.023  -9.341 -24.139  1.00  9.88           C  
ANISOU 1067  CA  LEU B 448      943   1265   1547     36   -207    -25       C  
ATOM   1068  C   LEU B 448      18.569 -10.608 -24.849  1.00 10.04           C  
ANISOU 1068  C   LEU B 448      949   1349   1517      9   -232      3       C  
ATOM   1069  O   LEU B 448      19.381 -11.322 -25.439  1.00 12.46           O  
ANISOU 1069  O   LEU B 448     1290   1641   1804     -9   -256     34       O  
ATOM   1070  CB  LEU B 448      19.249  -9.625 -22.652  1.00 12.21           C  
ANISOU 1070  CB  LEU B 448     1273   1562   1804    -32   -189    -78       C  
ATOM   1071  CG  LEU B 448      19.944  -8.525 -21.852  1.00 15.44           C  
ANISOU 1071  CG  LEU B 448     1728   1895   2244    -29   -178   -108       C  
ATOM   1072  CD1 LEU B 448      19.996  -8.903 -20.376  1.00 15.43           C  
ANISOU 1072  CD1 LEU B 448     1773   1913   2178   -117   -163   -162       C  
ATOM   1073  CD2 LEU B 448      21.339  -8.272 -22.409  1.00 16.70           C  
ANISOU 1073  CD2 LEU B 448     1922   1981   2443    -28   -219    -43       C  
ATOM   1074  N   LYS B 449      17.271 -10.882 -24.800  1.00 10.58           N  
ANISOU 1074  N   LYS B 449      964   1486   1570      7   -226    -12       N  
ATOM   1075  CA  LYS B 449      16.758 -12.102 -25.406  1.00 13.71           C  
ANISOU 1075  CA  LYS B 449     1356   1937   1914    -32   -264     18       C  
ATOM   1076  C   LYS B 449      16.893 -12.030 -26.927  1.00 11.63           C  
ANISOU 1076  C   LYS B 449     1104   1658   1655      4   -298     71       C  
ATOM   1077  O   LYS B 449      17.225 -13.024 -27.574  1.00 12.93           O  
ANISOU 1077  O   LYS B 449     1313   1828   1770    -26   -328     88       O  
ATOM   1078  CB  LYS B 449      15.303 -12.354 -24.990  1.00 16.68           C  
ANISOU 1078  CB  LYS B 449     1660   2400   2278    -54   -254      3       C  
ATOM   1079  CG  LYS B 449      14.812 -13.753 -25.343  1.00 20.66           C  
ANISOU 1079  CG  LYS B 449     2173   2958   2718   -125   -308     35       C  
ATOM   1080  CD  LYS B 449      13.517 -14.127 -24.631  1.00 17.54           C  
ANISOU 1080  CD  LYS B 449     1702   2662   2300   -177   -296     27       C  
ATOM   1081  CE  LYS B 449      12.502 -13.006 -24.643  1.00 19.65           C  
ANISOU 1081  CE  LYS B 449     1861   2965   2639   -104   -247     13       C  
ATOM   1082  NZ  LYS B 449      11.142 -13.541 -24.382  1.00 15.03           N  
ANISOU 1082  NZ  LYS B 449     1181   2493   2039   -153   -247     29       N  
ATOM   1083  N   SER B 450      16.665 -10.851 -27.500  1.00 11.87           N  
ANISOU 1083  N   SER B 450     1103   1664   1741     65   -296     96       N  
ATOM   1084  CA ASER B 450      16.808 -10.668 -28.939  0.58 10.83           C  
ANISOU 1084  CA ASER B 450      992   1524   1601     81   -333    157       C  
ATOM   1085  CA BSER B 450      16.800 -10.688 -28.942  0.42 10.83           C  
ANISOU 1085  CA BSER B 450      992   1525   1600     80   -333    157       C  
ATOM   1086  C   SER B 450      18.265 -10.766 -29.363  1.00 10.43           C  
ANISOU 1086  C   SER B 450     1006   1433   1525     72   -317    169       C  
ATOM   1087  O   SER B 450      18.574 -11.227 -30.464  1.00 12.86           O  
ANISOU 1087  O   SER B 450     1352   1756   1779     57   -331    198       O  
ATOM   1088  CB ASER B 450      16.228  -9.322 -29.375  0.58 16.34           C  
ANISOU 1088  CB ASER B 450     1640   2194   2376    137   -354    194       C  
ATOM   1089  CB BSER B 450      16.181  -9.366 -29.406  0.42 15.86           C  
ANISOU 1089  CB BSER B 450     1578   2136   2313    136   -355    195       C  
ATOM   1090  OG ASER B 450      14.815  -9.386 -29.438  0.58 16.35           O  
ANISOU 1090  OG ASER B 450     1565   2242   2404    148   -380    204       O  
ATOM   1091  OG BSER B 450      16.794  -8.257 -28.780  0.42 16.11           O  
ANISOU 1091  OG BSER B 450     1612   2100   2411    175   -329    174       O  
ATOM   1092  N   ILE B 451      19.160 -10.316 -28.488  1.00  9.91           N  
ANISOU 1092  N   ILE B 451      950   1319   1495     78   -287    144       N  
ATOM   1093  CA  ILE B 451      20.587 -10.386 -28.765  1.00  9.66           C  
ANISOU 1093  CA  ILE B 451      957   1254   1460     70   -270    161       C  
ATOM   1094  C   ILE B 451      21.022 -11.849 -28.839  1.00  9.38           C  
ANISOU 1094  C   ILE B 451      952   1239   1375     38   -269    135       C  
ATOM   1095  O   ILE B 451      21.785 -12.231 -29.726  1.00 13.10           O  
ANISOU 1095  O   ILE B 451     1446   1712   1819     42   -253    147       O  
ATOM   1096  CB  ILE B 451      21.406  -9.626 -27.698  1.00  9.65           C  
ANISOU 1096  CB  ILE B 451      958   1192   1514     69   -256    148       C  
ATOM   1097  CG1 ILE B 451      21.285  -8.115 -27.917  1.00 11.00           C  
ANISOU 1097  CG1 ILE B 451     1117   1319   1743    106   -268    181       C  
ATOM   1098  CG2 ILE B 451      22.868 -10.044 -27.735  1.00  9.32           C  
ANISOU 1098  CG2 ILE B 451      937   1127   1478     48   -243    164       C  
ATOM   1099  CD1 ILE B 451      21.841  -7.295 -26.775  1.00 11.61           C  
ANISOU 1099  CD1 ILE B 451     1211   1328   1871    102   -266    157       C  
ATOM   1100  N   ILE B 452      20.500 -12.675 -27.931  1.00 10.03           N  
ANISOU 1100  N   ILE B 452     1034   1334   1442      5   -285     97       N  
ATOM   1101  CA  ILE B 452      20.807 -14.106 -27.938  1.00  9.68           C  
ANISOU 1101  CA  ILE B 452     1024   1290   1364    -28   -308     75       C  
ATOM   1102  C   ILE B 452      20.377 -14.749 -29.252  1.00 10.54           C  
ANISOU 1102  C   ILE B 452     1160   1430   1413    -23   -323     81       C  
ATOM   1103  O   ILE B 452      21.123 -15.516 -29.853  1.00 12.28           O  
ANISOU 1103  O   ILE B 452     1419   1632   1615    -16   -317     62       O  
ATOM   1104  CB  ILE B 452      20.125 -14.849 -26.770  1.00 11.77           C  
ANISOU 1104  CB  ILE B 452     1287   1571   1613    -86   -341     51       C  
ATOM   1105  CG1 ILE B 452      20.742 -14.437 -25.433  1.00  9.61           C  
ANISOU 1105  CG1 ILE B 452     1012   1263   1376   -113   -333     39       C  
ATOM   1106  CG2 ILE B 452      20.257 -16.357 -26.941  1.00 13.35           C  
ANISOU 1106  CG2 ILE B 452     1529   1759   1782   -122   -391     37       C  
ATOM   1107  CD1 ILE B 452      19.981 -14.975 -24.233  1.00 14.99           C  
ANISOU 1107  CD1 ILE B 452     1693   1980   2021   -188   -356     19       C  
ATOM   1108  N   LEU B 453      19.166 -14.429 -29.691  1.00 10.71           N  
ANISOU 1108  N   LEU B 453     1163   1497   1410    -26   -345    105       N  
ATOM   1109  CA  LEU B 453      18.636 -14.961 -30.942  1.00 10.59           C  
ANISOU 1109  CA  LEU B 453     1184   1513   1328    -40   -376    120       C  
ATOM   1110  C   LEU B 453      19.524 -14.632 -32.143  1.00 12.06           C  
ANISOU 1110  C   LEU B 453     1408   1692   1481    -16   -341    133       C  
ATOM   1111  O   LEU B 453      19.792 -15.485 -32.987  1.00 12.37           O  
ANISOU 1111  O   LEU B 453     1509   1737   1455    -28   -340    109       O  
ATOM   1112  CB  LEU B 453      17.225 -14.424 -31.181  1.00 11.16           C  
ANISOU 1112  CB  LEU B 453     1209   1630   1401    -47   -415    164       C  
ATOM   1113  CG  LEU B 453      16.609 -14.814 -32.519  1.00 12.26           C  
ANISOU 1113  CG  LEU B 453     1391   1800   1468    -76   -467    199       C  
ATOM   1114  CD1 LEU B 453      16.312 -16.306 -32.537  1.00 13.58           C  
ANISOU 1114  CD1 LEU B 453     1613   1973   1572   -129   -513    168       C  
ATOM   1115  CD2 LEU B 453      15.356 -14.012 -32.787  1.00 11.13           C  
ANISOU 1115  CD2 LEU B 453     1181   1691   1359    -75   -513    261       C  
ATOM   1116  N   LEU B 454      19.993 -13.391 -32.200  1.00 11.68           N  
ANISOU 1116  N   LEU B 454     1329   1633   1477     12   -309    170       N  
ATOM   1117  CA  LEU B 454      20.726 -12.920 -33.368  1.00 10.87           C  
ANISOU 1117  CA  LEU B 454     1254   1543   1335     15   -277    201       C  
ATOM   1118  C   LEU B 454      22.213 -13.266 -33.322  1.00 10.93           C  
ANISOU 1118  C   LEU B 454     1268   1531   1353     32   -210    168       C  
ATOM   1119  O   LEU B 454      22.845 -13.450 -34.362  1.00 13.82           O  
ANISOU 1119  O   LEU B 454     1666   1927   1658     27   -165    164       O  
ATOM   1120  CB  LEU B 454      20.545 -11.411 -33.513  1.00 11.07           C  
ANISOU 1120  CB  LEU B 454     1242   1559   1406     25   -291    271       C  
ATOM   1121  CG  LEU B 454      19.134 -10.989 -33.934  1.00 12.72           C  
ANISOU 1121  CG  LEU B 454     1433   1786   1613     16   -362    318       C  
ATOM   1122  CD1 LEU B 454      18.967  -9.483 -33.790  1.00 21.53           C  
ANISOU 1122  CD1 LEU B 454     2503   2863   2815     43   -388    375       C  
ATOM   1123  CD2 LEU B 454      18.816 -11.448 -35.358  1.00 15.09           C  
ANISOU 1123  CD2 LEU B 454     1795   2133   1805    -32   -392    350       C  
ATOM   1124  N   ASN B 455      22.763 -13.373 -32.116  1.00 11.29           N  
ANISOU 1124  N   ASN B 455     1281   1532   1475     46   -203    143       N  
ATOM   1125  CA  ASN B 455      24.205 -13.525 -31.952  1.00 13.50           C  
ANISOU 1125  CA  ASN B 455     1543   1787   1799     63   -152    130       C  
ATOM   1126  C   ASN B 455      24.686 -14.967 -31.830  1.00 14.12           C  
ANISOU 1126  C   ASN B 455     1641   1842   1881     76   -147     63       C  
ATOM   1127  O   ASN B 455      25.806 -15.282 -32.221  1.00 15.66           O  
ANISOU 1127  O   ASN B 455     1821   2032   2098    103    -92     42       O  
ATOM   1128  CB  ASN B 455      24.678 -12.744 -30.722  1.00 13.16           C  
ANISOU 1128  CB  ASN B 455     1458   1696   1846     62   -164    155       C  
ATOM   1129  CG  ASN B 455      26.179 -12.809 -30.537  1.00 14.98           C  
ANISOU 1129  CG  ASN B 455     1654   1901   2138     72   -126    162       C  
ATOM   1130  OD1 ASN B 455      26.936 -12.231 -31.318  1.00 17.73           O  
ANISOU 1130  OD1 ASN B 455     1981   2276   2482     76    -78    200       O  
ATOM   1131  ND2 ASN B 455      26.620 -13.531 -29.513  1.00 13.53           N  
ANISOU 1131  ND2 ASN B 455     1460   1668   2013     66   -154    135       N  
ATOM   1132  N   SER B 456      23.850 -15.839 -31.280  1.00 12.71           N  
ANISOU 1132  N   SER B 456     1491   1647   1692     55   -207     32       N  
ATOM   1133  CA  SER B 456      24.311 -17.173 -30.905  1.00 14.53           C  
ANISOU 1133  CA  SER B 456     1741   1827   1952     61   -231    -23       C  
ATOM   1134  C   SER B 456      24.835 -17.985 -32.087  1.00 17.32           C  
ANISOU 1134  C   SER B 456     2134   2183   2265     97   -186    -81       C  
ATOM   1135  O   SER B 456      25.844 -18.674 -31.964  1.00 20.31           O  
ANISOU 1135  O   SER B 456     2497   2513   2709    135   -166   -124       O  
ATOM   1136  CB  SER B 456      23.192 -17.941 -30.207  1.00 21.82           C  
ANISOU 1136  CB  SER B 456     2695   2740   2854     12   -315    -33       C  
ATOM   1137  OG  SER B 456      22.917 -17.375 -28.935  1.00 24.44           O  
ANISOU 1137  OG  SER B 456     2991   3069   3227    -22   -342      0       O  
ATOM   1138  N   GLY B 457      24.166 -17.896 -33.232  1.00 17.15           N  
ANISOU 1138  N   GLY B 457     2163   2215   2137     85   -171    -84       N  
ATOM   1139  CA  GLY B 457      24.557 -18.689 -34.385  1.00 17.45           C  
ANISOU 1139  CA  GLY B 457     2260   2261   2109    109   -123   -155       C  
ATOM   1140  C   GLY B 457      25.229 -17.930 -35.516  1.00 18.56           C  
ANISOU 1140  C   GLY B 457     2392   2470   2188    121    -20   -144       C  
ATOM   1141  O   GLY B 457      25.505 -18.505 -36.568  1.00 19.88           O  
ANISOU 1141  O   GLY B 457     2618   2662   2275    133     37   -210       O  
ATOM   1142  N   VAL B 458      25.517 -16.649 -35.298  1.00 18.24           N  
ANISOU 1142  N   VAL B 458     2287   2460   2183    111      3    -63       N  
ATOM   1143  CA  VAL B 458      25.984 -15.779 -36.379  1.00 20.85           C  
ANISOU 1143  CA  VAL B 458     2614   2867   2442     93     80    -24       C  
ATOM   1144  C   VAL B 458      27.429 -16.060 -36.811  1.00 25.08           C  
ANISOU 1144  C   VAL B 458     3106   3424   2998    136    198    -73       C  
ATOM   1145  O   VAL B 458      27.853 -15.632 -37.884  1.00 24.19           O  
ANISOU 1145  O   VAL B 458     3002   3392   2796    112    281    -61       O  
ATOM   1146  CB  VAL B 458      25.852 -14.286 -35.987  1.00 20.95           C  
ANISOU 1146  CB  VAL B 458     2573   2889   2498     64     51     84       C  
ATOM   1147  CG1 VAL B 458      26.924 -13.895 -34.994  1.00 18.40           C  
ANISOU 1147  CG1 VAL B 458     2164   2525   2300     92     73    105       C  
ATOM   1148  CG2 VAL B 458      25.917 -13.391 -37.221  1.00 21.01           C  
ANISOU 1148  CG2 VAL B 458     2603   2975   2407     16     88    148       C  
ATOM   1149  N   TYR B 459      28.179 -16.787 -35.990  1.00 21.31           N  
ANISOU 1149  N   TYR B 459     2576   2880   2639    192    204   -124       N  
ATOM   1150  CA  TYR B 459      29.551 -17.127 -36.349  1.00 19.32           C  
ANISOU 1150  CA  TYR B 459     2260   2645   2437    247    316   -175       C  
ATOM   1151  C   TYR B 459      29.669 -18.572 -36.839  1.00 24.17           C  
ANISOU 1151  C   TYR B 459     2928   3225   3031    304    350   -310       C  
ATOM   1152  O   TYR B 459      30.767 -19.037 -37.132  1.00 26.38           O  
ANISOU 1152  O   TYR B 459     3149   3508   3367    370    448   -377       O  
ATOM   1153  CB  TYR B 459      30.505 -16.873 -35.166  1.00 20.94           C  
ANISOU 1153  CB  TYR B 459     2351   2792   2812    274    297   -129       C  
ATOM   1154  CG  TYR B 459      30.171 -15.628 -34.363  1.00 26.43           C  
ANISOU 1154  CG  TYR B 459     3022   3480   3538    218    226    -15       C  
ATOM   1155  CD1 TYR B 459      30.616 -14.376 -34.775  1.00 28.40           C  
ANISOU 1155  CD1 TYR B 459     3230   3794   3767    179    270     71       C  
ATOM   1156  CD2 TYR B 459      29.437 -15.706 -33.186  1.00 28.79           C  
ANISOU 1156  CD2 TYR B 459     3344   3707   3887    198    114      3       C  
ATOM   1157  CE1 TYR B 459      30.319 -13.234 -34.054  1.00 27.42           C  
ANISOU 1157  CE1 TYR B 459     3095   3645   3679    135    198    164       C  
ATOM   1158  CE2 TYR B 459      29.139 -14.568 -32.452  1.00 26.17           C  
ANISOU 1158  CE2 TYR B 459     2997   3364   3581    155     61     85       C  
ATOM   1159  CZ  TYR B 459      29.583 -13.334 -32.893  1.00 27.51           C  
ANISOU 1159  CZ  TYR B 459     3132   3580   3739    130     99    161       C  
ATOM   1160  OH  TYR B 459      29.293 -12.192 -32.179  1.00 31.09           O  
ANISOU 1160  OH  TYR B 459     3582   4005   4225     94     40    232       O  
ATOM   1161  N   THR B 460      28.542 -19.271 -36.965  1.00 23.08           N  
ANISOU 1161  N   THR B 460     2899   3052   2817    281    268   -351       N  
ATOM   1162  CA  THR B 460      28.571 -20.669 -37.390  1.00 19.60           C  
ANISOU 1162  CA  THR B 460     2531   2556   2358    331    276   -482       C  
ATOM   1163  C   THR B 460      27.714 -20.973 -38.628  1.00 24.03           C  
ANISOU 1163  C   THR B 460     3232   3169   2731    284    285   -532       C  
ATOM   1164  O   THR B 460      27.234 -22.096 -38.786  1.00 23.92           O  
ANISOU 1164  O   THR B 460     3314   3088   2687    294    229   -619       O  
ATOM   1165  CB  THR B 460      28.104 -21.600 -36.257  1.00 26.55           C  
ANISOU 1165  CB  THR B 460     3430   3314   3342    340    138   -495       C  
ATOM   1166  OG1 THR B 460      26.859 -21.119 -35.739  1.00 23.80           O  
ANISOU 1166  OG1 THR B 460     3115   2978   2948    259     30   -406       O  
ATOM   1167  CG2 THR B 460      29.135 -21.650 -35.127  1.00 24.72           C  
ANISOU 1167  CG2 THR B 460     3079   3013   3300    390    125   -472       C  
ATOM   1168  N   PHE B 461      27.525 -19.995 -39.510  1.00 25.32           N  
ANISOU 1168  N   PHE B 461     3414   3441   2764    221    340   -473       N  
ATOM   1169  CA  PHE B 461      26.762 -20.240 -40.739  1.00 26.84           C  
ANISOU 1169  CA  PHE B 461     3746   3687   2765    158    340   -509       C  
ATOM   1170  C   PHE B 461      27.465 -21.191 -41.707  1.00 29.89           C  
ANISOU 1170  C   PHE B 461     4199   4084   3073    207    461   -667       C  
ATOM   1171  O   PHE B 461      26.817 -21.791 -42.569  1.00 27.96           O  
ANISOU 1171  O   PHE B 461     4098   3845   2680    164    440   -733       O  
ATOM   1172  CB  PHE B 461      26.450 -18.923 -41.459  1.00 24.38           C  
ANISOU 1172  CB  PHE B 461     3438   3487   2338     68    357   -393       C  
ATOM   1173  CG  PHE B 461      25.343 -18.134 -40.825  1.00 22.12           C  
ANISOU 1173  CG  PHE B 461     3134   3184   2088     12    218   -262       C  
ATOM   1174  CD1 PHE B 461      24.073 -18.676 -40.711  1.00 25.39           C  
ANISOU 1174  CD1 PHE B 461     3625   3554   2466    -26     92   -257       C  
ATOM   1175  CD2 PHE B 461      25.564 -16.853 -40.351  1.00 25.87           C  
ANISOU 1175  CD2 PHE B 461     3510   3683   2635     -1    215   -147       C  
ATOM   1176  CE1 PHE B 461      23.046 -17.957 -40.131  1.00 23.41           C  
ANISOU 1176  CE1 PHE B 461     3338   3295   2260    -67    -20   -146       C  
ATOM   1177  CE2 PHE B 461      24.539 -16.128 -39.770  1.00 27.06           C  
ANISOU 1177  CE2 PHE B 461     3641   3811   2829    -37     98    -45       C  
ATOM   1178  CZ  PHE B 461      23.279 -16.681 -39.659  1.00 27.53           C  
ANISOU 1178  CZ  PHE B 461     3762   3837   2860    -65    -12    -48       C  
ATOM   1179  N   LEU B 462      28.782 -21.324 -41.556  1.00 29.76           N  
ANISOU 1179  N   LEU B 462     4077   4068   3161    297    586   -729       N  
ATOM   1180  CA  LEU B 462      29.606 -22.158 -42.436  1.00 29.54           C  
ANISOU 1180  CA  LEU B 462     4083   4057   3083    365    732   -894       C  
ATOM   1181  C   LEU B 462      29.337 -21.865 -43.906  1.00 33.66           C  
ANISOU 1181  C   LEU B 462     4725   4706   3357    278    821   -922       C  
ATOM   1182  O   LEU B 462      29.184 -22.779 -44.718  1.00 36.56           O  
ANISOU 1182  O   LEU B 462     5225   5060   3606    287    861  -1064       O  
ATOM   1183  CB  LEU B 462      29.377 -23.644 -42.155  1.00 30.12           C  
ANISOU 1183  CB  LEU B 462     4238   3985   3222    439    660  -1031       C  
ATOM   1184  CG  LEU B 462      29.591 -24.116 -40.717  1.00 31.75           C  
ANISOU 1184  CG  LEU B 462     4348   4053   3661    508    549  -1005       C  
ATOM   1185  CD1 LEU B 462      29.403 -25.623 -40.632  1.00 33.30           C  
ANISOU 1185  CD1 LEU B 462     4642   4103   3908    571    474  -1143       C  
ATOM   1186  CD2 LEU B 462      30.971 -23.705 -40.212  1.00 33.31           C  
ANISOU 1186  CD2 LEU B 462     4360   4266   4030    590    652   -986       C  
ATOM   1187  N   SER B 463      29.269 -20.582 -44.236  1.00 36.33           N  
ANISOU 1187  N   SER B 463     5027   5162   3615    185    841   -784       N  
ATOM   1188  CA  SER B 463      29.040 -20.162 -45.610  1.00 35.64           C  
ANISOU 1188  CA  SER B 463     5050   5205   3285     75    911   -780       C  
ATOM   1189  C   SER B 463      29.574 -18.757 -45.843  1.00 33.61           C  
ANISOU 1189  C   SER B 463     4693   5075   3001      4    977   -637       C  
ATOM   1190  O   SER B 463      29.449 -17.874 -44.988  1.00 39.57           O  
ANISOU 1190  O   SER B 463     5349   5802   3882     -7    887   -494       O  
ATOM   1191  CB  SER B 463      27.547 -20.226 -45.955  1.00 33.99           C  
ANISOU 1191  CB  SER B 463     5000   4970   2945    -31    746   -725       C  
ATOM   1192  OG  SER B 463      27.294 -19.701 -47.247  1.00 36.83           O  
ANISOU 1192  OG  SER B 463     5468   5456   3070   -159    788   -690       O  
ATOM   1193  N   SER B 464      30.181 -18.566 -47.005  1.00 38.77           N  
ANISOU 1193  N   SER B 464     5379   5868   3484    -50   1135   -680       N  
ATOM   1194  CA  SER B 464      30.668 -17.260 -47.397  1.00 37.99           C  
ANISOU 1194  CA  SER B 464     5205   5903   3327   -146   1193   -537       C  
ATOM   1195  C   SER B 464      30.250 -16.986 -48.838  1.00 36.76           C  
ANISOU 1195  C   SER B 464     5200   5861   2905   -289   1215   -514       C  
ATOM   1196  O   SER B 464      30.991 -16.392 -49.623  1.00 36.92           O  
ANISOU 1196  O   SER B 464     5182   5988   2856   -337   1313   -462       O  
ATOM   1197  CB  SER B 464      32.182 -17.174 -47.227  1.00 37.20           C  
ANISOU 1197  CB  SER B 464     4932   5868   3334    -67   1376   -578       C  
ATOM   1198  OG  SER B 464      32.812 -18.337 -47.741  1.00 45.32           O  
ANISOU 1198  OG  SER B 464     5983   6893   4344     35   1517   -770       O  
ATOM   1199  N   THR B 465      29.056 -17.458 -49.183  1.00 37.13           N  
ANISOU 1199  N   THR B 465     5408   5848   2850   -339   1081   -529       N  
ATOM   1200  CA  THR B 465      28.370 -16.988 -50.375  1.00 33.79           C  
ANISOU 1200  CA  THR B 465     5110   5481   2249   -476   1003   -436       C  
ATOM   1201  C   THR B 465      28.138 -15.494 -50.203  1.00 30.71           C  
ANISOU 1201  C   THR B 465     4654   5133   1883   -583    909   -220       C  
ATOM   1202  O   THR B 465      28.117 -14.993 -49.074  1.00 33.53           O  
ANISOU 1202  O   THR B 465     4907   5453   2379   -553    860   -148       O  
ATOM   1203  CB  THR B 465      27.022 -17.706 -50.596  1.00 32.69           C  
ANISOU 1203  CB  THR B 465     5127   5252   2042   -512    839   -462       C  
ATOM   1204  OG1 THR B 465      26.151 -17.445 -49.486  1.00 29.12           O  
ANISOU 1204  OG1 THR B 465     4645   4714   1704   -512    683   -375       O  
ATOM   1205  CG2 THR B 465      27.224 -19.210 -50.745  1.00 32.91           C  
ANISOU 1205  CG2 THR B 465     5229   5216   2057   -406    906   -674       C  
ATOM   1206  N   LEU B 466      27.968 -14.782 -51.312  1.00 33.22           N  
ANISOU 1206  N   LEU B 466     5031   5519   2072   -707    876   -118       N  
ATOM   1207  CA  LEU B 466      27.667 -13.356 -51.252  1.00 33.30           C  
ANISOU 1207  CA  LEU B 466     4991   5542   2118   -811    757     89       C  
ATOM   1208  C   LEU B 466      26.442 -13.095 -50.377  1.00 29.47           C  
ANISOU 1208  C   LEU B 466     4511   4949   1739   -810    556    181       C  
ATOM   1209  O   LEU B 466      26.412 -12.137 -49.602  1.00 27.01           O  
ANISOU 1209  O   LEU B 466     4102   4611   1548   -813    483    309       O  
ATOM   1210  CB  LEU B 466      27.441 -12.794 -52.653  1.00 34.34           C  
ANISOU 1210  CB  LEU B 466     5213   5739   2094   -955    717    170       C  
ATOM   1211  CG  LEU B 466      27.232 -11.280 -52.732  1.00 36.31           C  
ANISOU 1211  CG  LEU B 466     5413   5994   2391  -1065    589    378       C  
ATOM   1212  CD1 LEU B 466      28.250 -10.530 -51.884  1.00 34.86           C  
ANISOU 1212  CD1 LEU B 466     5075   5833   2338  -1021    661    439       C  
ATOM   1213  CD2 LEU B 466      27.278 -10.807 -54.176  1.00 36.71           C  
ANISOU 1213  CD2 LEU B 466     5543   6126   2279  -1213    584    436       C  
ATOM   1214  N   LYS B 467      25.444 -13.966 -50.498  1.00 29.19           N  
ANISOU 1214  N   LYS B 467     4581   4846   1665   -801    465    115       N  
ATOM   1215  CA  LYS B 467      24.219 -13.848 -49.722  1.00 27.33           C  
ANISOU 1215  CA  LYS B 467     4343   4509   1533   -794    277    193       C  
ATOM   1216  C   LYS B 467      24.510 -13.894 -48.227  1.00 29.73           C  
ANISOU 1216  C   LYS B 467     4528   4757   2011   -679    292    174       C  
ATOM   1217  O   LYS B 467      24.001 -13.080 -47.460  1.00 26.36           O  
ANISOU 1217  O   LYS B 467     4015   4263   1736   -662    171    292       O  
ATOM   1218  CB  LYS B 467      23.238 -14.959 -50.099  1.00 28.03           C  
ANISOU 1218  CB  LYS B 467     4553   4536   1562   -797    196    109       C  
ATOM   1219  CG  LYS B 467      21.869 -14.780 -49.480  1.00 29.76           C  
ANISOU 1219  CG  LYS B 467     4755   4660   1894   -804     -5    208       C  
ATOM   1220  CD  LYS B 467      21.311 -13.408 -49.817  1.00 32.13           C  
ANISOU 1220  CD  LYS B 467     5006   4957   2242   -889   -129    393       C  
ATOM   1221  CE  LYS B 467      20.078 -13.104 -48.992  1.00 31.79           C  
ANISOU 1221  CE  LYS B 467     4898   4819   2361   -862   -302    484       C  
ATOM   1222  NZ  LYS B 467      19.393 -11.874 -49.482  1.00 36.74           N  
ANISOU 1222  NZ  LYS B 467     5487   5424   3048   -942   -432    643       N  
ATOM   1223  N   SER B 468      25.344 -14.848 -47.829  1.00 28.29           N  
ANISOU 1223  N   SER B 468     4311   4558   1880   -565    430     13       N  
ATOM   1224  CA  SER B 468      25.677 -15.048 -46.424  1.00 25.58           C  
ANISOU 1224  CA  SER B 468     3834   4116   1771   -425    429    -21       C  
ATOM   1225  C   SER B 468      26.476 -13.876 -45.855  1.00 24.05           C  
ANISOU 1225  C   SER B 468     3495   3940   1703   -410    462     87       C  
ATOM   1226  O   SER B 468      26.294 -13.498 -44.698  1.00 21.80           O  
ANISOU 1226  O   SER B 468     3117   3567   1600   -347    384    138       O  
ATOM   1227  CB  SER B 468      26.450 -16.355 -46.249  1.00 29.22           C  
ANISOU 1227  CB  SER B 468     4296   4549   2258   -315    558   -211       C  
ATOM   1228  OG  SER B 468      25.581 -17.477 -46.369  1.00 32.85           O  
ANISOU 1228  OG  SER B 468     4877   4939   2663   -308    481   -303       O  
ATOM   1229  N   LEU B 469      27.362 -13.307 -46.670  1.00 28.48           N  
ANISOU 1229  N   LEU B 469     4043   4620   2158   -479    577    121       N  
ATOM   1230  CA  LEU B 469      28.088 -12.099 -46.285  1.00 23.10           C  
ANISOU 1230  CA  LEU B 469     3239   3963   1574   -497    589    247       C  
ATOM   1231  C   LEU B 469      27.110 -10.980 -45.956  1.00 23.69           C  
ANISOU 1231  C   LEU B 469     3315   3973   1714   -553    401    411       C  
ATOM   1232  O   LEU B 469      27.244 -10.294 -44.941  1.00 22.05           O  
ANISOU 1232  O   LEU B 469     3006   3690   1681   -502    344    477       O  
ATOM   1233  CB  LEU B 469      29.044 -11.657 -47.397  1.00 29.14           C  
ANISOU 1233  CB  LEU B 469     4007   4887   2178   -597    730    276       C  
ATOM   1234  CG  LEU B 469      30.499 -12.137 -47.316  1.00 34.14           C  
ANISOU 1234  CG  LEU B 469     4533   5589   2852   -521    936    170       C  
ATOM   1235  CD1 LEU B 469      30.597 -13.628 -46.996  1.00 34.34           C  
ANISOU 1235  CD1 LEU B 469     4574   5550   2925   -383   1010    -32       C  
ATOM   1236  CD2 LEU B 469      31.248 -11.808 -48.594  1.00 33.07           C  
ANISOU 1236  CD2 LEU B 469     4419   5607   2540   -624   1070    186       C  
ATOM   1237  N   GLU B 470      26.117 -10.816 -46.822  1.00 22.52           N  
ANISOU 1237  N   GLU B 470     3281   3847   1427   -658    300    472       N  
ATOM   1238  CA  GLU B 470      25.084  -9.808 -46.637  1.00 21.90           C  
ANISOU 1238  CA  GLU B 470     3203   3702   1416   -707    112    624       C  
ATOM   1239  C   GLU B 470      24.211 -10.107 -45.417  1.00 20.15           C  
ANISOU 1239  C   GLU B 470     2931   3349   1376   -595     10    592       C  
ATOM   1240  O   GLU B 470      23.817  -9.192 -44.692  1.00 20.08           O  
ANISOU 1240  O   GLU B 470     2853   3264   1514   -570    -93    684       O  
ATOM   1241  CB  GLU B 470      24.228  -9.709 -47.898  1.00 23.23           C  
ANISOU 1241  CB  GLU B 470     3500   3914   1413   -841     21    688       C  
ATOM   1242  CG  GLU B 470      24.962  -9.085 -49.076  1.00 25.08           C  
ANISOU 1242  CG  GLU B 470     3757   4234   1540   -944     83    734       C  
ATOM   1243  CD  GLU B 470      24.245  -9.293 -50.393  1.00 31.39           C  
ANISOU 1243  CD  GLU B 470     4674   5050   2202  -1044     20    735       C  
ATOM   1244  OE1 GLU B 470      23.220 -10.006 -50.411  1.00 32.04           O  
ANISOU 1244  OE1 GLU B 470     4820   5077   2276  -1028    -62    691       O  
ATOM   1245  OE2 GLU B 470      24.711  -8.744 -51.413  1.00 30.10           O  
ANISOU 1245  OE2 GLU B 470     4539   4958   1942  -1147     49    784       O  
ATOM   1246  N   GLU B 471      23.917 -11.386 -45.189  1.00 19.31           N  
ANISOU 1246  N   GLU B 471     2865   3218   1256   -532     40    458       N  
ATOM   1247  CA  GLU B 471      23.106 -11.783 -44.040  1.00 17.83           C  
ANISOU 1247  CA  GLU B 471     2631   2923   1219   -442    -46    425       C  
ATOM   1248  C   GLU B 471      23.819 -11.446 -42.732  1.00 16.62           C  
ANISOU 1248  C   GLU B 471     2353   2710   1251   -343     -6    412       C  
ATOM   1249  O   GLU B 471      23.203 -10.937 -41.795  1.00 16.30           O  
ANISOU 1249  O   GLU B 471     2252   2594   1346   -303    -96    458       O  
ATOM   1250  CB  GLU B 471      22.777 -13.274 -44.093  1.00 22.06           C  
ANISOU 1250  CB  GLU B 471     3242   3444   1694   -410    -25    290       C  
ATOM   1251  CG  GLU B 471      21.876 -13.665 -45.256  1.00 25.67           C  
ANISOU 1251  CG  GLU B 471     3836   3941   1975   -514    -98    304       C  
ATOM   1252  CD  GLU B 471      20.400 -13.582 -44.907  1.00 25.61           C  
ANISOU 1252  CD  GLU B 471     3826   3874   2033   -532   -271    380       C  
ATOM   1253  OE1 GLU B 471      19.893 -14.470 -44.194  1.00 17.62           O  
ANISOU 1253  OE1 GLU B 471     2805   2803   1086   -476   -305    310       O  
ATOM   1254  OE2 GLU B 471      19.742 -12.619 -45.346  1.00 25.51           O  
ANISOU 1254  OE2 GLU B 471     3810   3871   2013   -605   -379    516       O  
ATOM   1255  N   LYS B 472      25.122 -11.718 -42.679  1.00 17.73           N  
ANISOU 1255  N   LYS B 472     2455   2888   1396   -308    131    348       N  
ATOM   1256  CA  LYS B 472      25.911 -11.436 -41.483  1.00 16.78           C  
ANISOU 1256  CA  LYS B 472     2221   2712   1443   -230    163    343       C  
ATOM   1257  C   LYS B 472      25.994  -9.936 -41.191  1.00 16.55           C  
ANISOU 1257  C   LYS B 472     2134   2662   1492   -265     99    480       C  
ATOM   1258  O   LYS B 472      25.892  -9.518 -40.036  1.00 17.65           O  
ANISOU 1258  O   LYS B 472     2210   2718   1777   -212     46    497       O  
ATOM   1259  CB  LYS B 472      27.315 -12.019 -41.620  1.00 21.63           C  
ANISOU 1259  CB  LYS B 472     2791   3375   2051   -191    318    260       C  
ATOM   1260  CG  LYS B 472      27.373 -13.531 -41.494  1.00 20.34           C  
ANISOU 1260  CG  LYS B 472     2661   3183   1882   -119    370    108       C  
ATOM   1261  CD  LYS B 472      28.763 -14.063 -41.796  1.00 29.99           C  
ANISOU 1261  CD  LYS B 472     3831   4459   3105    -73    531     22       C  
ATOM   1262  CE  LYS B 472      28.703 -15.510 -42.252  1.00 29.86           C  
ANISOU 1262  CE  LYS B 472     3893   4432   3020    -25    587   -135       C  
ATOM   1263  NZ  LYS B 472      30.044 -16.031 -42.641  1.00 32.22           N  
ANISOU 1263  NZ  LYS B 472     4131   4785   3324     33    758   -235       N  
ATOM   1264  N   ASP B 473      26.182  -9.133 -42.237  1.00 18.21           N  
ANISOU 1264  N   ASP B 473     2375   2945   1598   -362    100    576       N  
ATOM   1265  CA  ASP B 473      26.188  -7.685 -42.085  1.00 18.23           C  
ANISOU 1265  CA  ASP B 473     2340   2915   1672   -408     13    716       C  
ATOM   1266  C   ASP B 473      24.864  -7.185 -41.526  1.00 17.44           C  
ANISOU 1266  C   ASP B 473     2245   2715   1668   -382   -140    761       C  
ATOM   1267  O   ASP B 473      24.845  -6.359 -40.616  1.00 17.64           O  
ANISOU 1267  O   ASP B 473     2212   2654   1835   -343   -199    803       O  
ATOM   1268  CB  ASP B 473      26.467  -6.989 -43.415  1.00 22.29           C  
ANISOU 1268  CB  ASP B 473     2904   3528   2039   -540     17    824       C  
ATOM   1269  CG  ASP B 473      26.447  -5.478 -43.285  1.00 30.35           C  
ANISOU 1269  CG  ASP B 473     3894   4496   3141   -595    -98    980       C  
ATOM   1270  OD1 ASP B 473      27.386  -4.923 -42.680  1.00 33.30           O  
ANISOU 1270  OD1 ASP B 473     4193   4849   3609   -579    -65   1011       O  
ATOM   1271  OD2 ASP B 473      25.469  -4.856 -43.750  1.00 35.52           O  
ANISOU 1271  OD2 ASP B 473     4599   5117   3779   -652   -235   1074       O  
ATOM   1272  N   HIS B 474      23.761  -7.680 -42.083  1.00 17.22           N  
ANISOU 1272  N   HIS B 474     2283   2696   1562   -406   -203    751       N  
ATOM   1273  CA  HIS B 474      22.437  -7.294 -41.612  1.00 17.94           C  
ANISOU 1273  CA  HIS B 474     2360   2704   1751   -377   -340    791       C  
ATOM   1274  C   HIS B 474      22.250  -7.631 -40.135  1.00 21.66           C  
ANISOU 1274  C   HIS B 474     2762   3098   2371   -266   -330    705       C  
ATOM   1275  O   HIS B 474      21.778  -6.800 -39.357  1.00 17.72           O  
ANISOU 1275  O   HIS B 474     2210   2520   2004   -224   -402    741       O  
ATOM   1276  CB  HIS B 474      21.345  -7.972 -42.444  1.00 19.86           C  
ANISOU 1276  CB  HIS B 474     2679   2981   1884   -427   -405    790       C  
ATOM   1277  CG  HIS B 474      19.961  -7.733 -41.925  1.00 22.48           C  
ANISOU 1277  CG  HIS B 474     2972   3239   2329   -389   -535    823       C  
ATOM   1278  ND1 HIS B 474      19.355  -6.495 -41.960  1.00 27.98           N  
ANISOU 1278  ND1 HIS B 474     3630   3877   3124   -401   -658    940       N  
ATOM   1279  CD2 HIS B 474      19.067  -8.572 -41.349  1.00 26.63           C  
ANISOU 1279  CD2 HIS B 474     3482   3743   2895   -339   -560    755       C  
ATOM   1280  CE1 HIS B 474      18.145  -6.583 -41.435  1.00 26.79           C  
ANISOU 1280  CE1 HIS B 474     3429   3675   3074   -350   -740    935       C  
ATOM   1281  NE2 HIS B 474      17.946  -7.833 -41.056  1.00 32.65           N  
ANISOU 1281  NE2 HIS B 474     4183   4447   3775   -319   -681    828       N  
ATOM   1282  N   ILE B 475      22.621  -8.851 -39.760  1.00 14.81           N  
ANISOU 1282  N   ILE B 475     1900   2250   1477   -223   -243    589       N  
ATOM   1283  CA  ILE B 475      22.493  -9.298 -38.379  1.00 14.32           C  
ANISOU 1283  CA  ILE B 475     1785   2125   1533   -140   -235    512       C  
ATOM   1284  C   ILE B 475      23.265  -8.377 -37.441  1.00 15.79           C  
ANISOU 1284  C   ILE B 475     1905   2255   1839   -107   -222    538       C  
ATOM   1285  O   ILE B 475      22.765  -7.997 -36.387  1.00 16.09           O  
ANISOU 1285  O   ILE B 475     1903   2225   1985    -61   -268    528       O  
ATOM   1286  CB  ILE B 475      22.987 -10.749 -38.211  1.00 16.21           C  
ANISOU 1286  CB  ILE B 475     2046   2384   1728   -110   -154    396       C  
ATOM   1287  CG1 ILE B 475      22.016 -11.719 -38.897  1.00 16.84           C  
ANISOU 1287  CG1 ILE B 475     2201   2492   1705   -140   -193    361       C  
ATOM   1288  CG2 ILE B 475      23.150 -11.103 -36.736  1.00 14.61           C  
ANISOU 1288  CG2 ILE B 475     1788   2117   1647    -45   -147    337       C  
ATOM   1289  CD1 ILE B 475      22.542 -13.133 -39.018  1.00 18.91           C  
ANISOU 1289  CD1 ILE B 475     2510   2767   1909   -119   -121    246       C  
ATOM   1290  N   HIS B 476      24.470  -7.987 -37.843  1.00 15.07           N  
ANISOU 1290  N   HIS B 476     1805   2197   1725   -137   -159    573       N  
ATOM   1291  CA  HIS B 476      25.302  -7.145 -36.988  1.00 15.18           C  
ANISOU 1291  CA  HIS B 476     1763   2157   1848   -121   -156    606       C  
ATOM   1292  C   HIS B 476      24.779  -5.707 -36.932  1.00 14.33           C  
ANISOU 1292  C   HIS B 476     1652   1986   1808   -140   -261    704       C  
ATOM   1293  O   HIS B 476      24.907  -5.043 -35.900  1.00 16.23           O  
ANISOU 1293  O   HIS B 476     1862   2144   2161   -106   -294    706       O  
ATOM   1294  CB  HIS B 476      26.758  -7.188 -37.452  1.00 21.67           C  
ANISOU 1294  CB  HIS B 476     2560   3042   2633   -154    -59    624       C  
ATOM   1295  CG  HIS B 476      27.477  -8.434 -37.028  1.00 23.71           C  
ANISOU 1295  CG  HIS B 476     2790   3317   2902   -104     34    520       C  
ATOM   1296  ND1 HIS B 476      27.661  -8.769 -35.704  1.00 26.07           N  
ANISOU 1296  ND1 HIS B 476     3050   3542   3313    -49     20    469       N  
ATOM   1297  CD2 HIS B 476      28.030  -9.438 -37.749  1.00 25.35           C  
ANISOU 1297  CD2 HIS B 476     3006   3598   3027    -99    134    454       C  
ATOM   1298  CE1 HIS B 476      28.310  -9.918 -35.626  1.00 25.35           C  
ANISOU 1298  CE1 HIS B 476     2940   3470   3222    -14     93    390       C  
ATOM   1299  NE2 HIS B 476      28.545 -10.345 -36.854  1.00 26.20           N  
ANISOU 1299  NE2 HIS B 476     3072   3663   3219    -34    168    370       N  
ATOM   1300  N   ARG B 477      24.169  -5.231 -38.016  1.00 18.46           N  
ANISOU 1300  N   ARG B 477     2213   2536   2265   -196   -323    784       N  
ATOM   1301  CA  ARG B 477      23.517  -3.925 -37.976  1.00 16.57           C  
ANISOU 1301  CA  ARG B 477     1968   2216   2111   -203   -445    876       C  
ATOM   1302  C   ARG B 477      22.340  -3.929 -37.006  1.00 16.15           C  
ANISOU 1302  C   ARG B 477     1885   2084   2168   -118   -500    815       C  
ATOM   1303  O   ARG B 477      22.147  -2.974 -36.255  1.00 20.26           O  
ANISOU 1303  O   ARG B 477     2379   2508   2811    -76   -557    828       O  
ATOM   1304  CB  ARG B 477      23.060  -3.498 -39.370  1.00 18.28           C  
ANISOU 1304  CB  ARG B 477     2233   2477   2236   -293   -519    985       C  
ATOM   1305  CG  ARG B 477      24.193  -3.050 -40.267  1.00 23.11           C  
ANISOU 1305  CG  ARG B 477     2869   3159   2754   -396   -482   1074       C  
ATOM   1306  CD  ARG B 477      23.659  -2.479 -41.562  1.00 31.52           C  
ANISOU 1306  CD  ARG B 477     3991   4256   3729   -503   -582   1201       C  
ATOM   1307  NE  ARG B 477      22.753  -3.420 -42.212  1.00 37.21           N  
ANISOU 1307  NE  ARG B 477     4759   5033   4345   -517   -587   1160       N  
ATOM   1308  CZ  ARG B 477      22.153  -3.202 -43.377  1.00 35.71           C  
ANISOU 1308  CZ  ARG B 477     4624   4872   4073   -607   -658   1218       C  
ATOM   1309  NH1 ARG B 477      22.361  -2.067 -44.035  1.00 41.35           N  
ANISOU 1309  NH1 ARG B 477     5341   5564   4804   -687   -724   1304       N  
ATOM   1310  NH2 ARG B 477      21.343  -4.124 -43.885  1.00 36.52           N  
ANISOU 1310  NH2 ARG B 477     4775   5018   4084   -620   -666   1175       N  
ATOM   1311  N   VAL B 478      21.558  -5.003 -37.009  1.00 14.24           N  
ANISOU 1311  N   VAL B 478     1647   1884   1880    -94   -481    746       N  
ATOM   1312  CA  VAL B 478      20.435  -5.102 -36.086  1.00 13.77           C  
ANISOU 1312  CA  VAL B 478     1544   1774   1913    -23   -517    688       C  
ATOM   1313  C   VAL B 478      20.938  -5.227 -34.646  1.00 17.91           C  
ANISOU 1313  C   VAL B 478     2039   2254   2511     33   -457    601       C  
ATOM   1314  O   VAL B 478      20.372  -4.630 -33.728  1.00 16.01           O  
ANISOU 1314  O   VAL B 478     1762   1946   2374     88   -486    571       O  
ATOM   1315  CB  VAL B 478      19.515  -6.297 -36.422  1.00 19.64           C  
ANISOU 1315  CB  VAL B 478     2299   2580   2583    -30   -517    647       C  
ATOM   1316  CG1 VAL B 478      18.389  -6.393 -35.418  1.00 19.20           C  
ANISOU 1316  CG1 VAL B 478     2181   2491   2623     35   -543    593       C  
ATOM   1317  CG2 VAL B 478      18.946  -6.149 -37.832  1.00 22.19           C  
ANISOU 1317  CG2 VAL B 478     2663   2942   2826   -100   -595    740       C  
ATOM   1318  N   LEU B 479      22.005  -5.994 -34.451  1.00 14.18           N  
ANISOU 1318  N   LEU B 479     1582   1819   1987     18   -374    557       N  
ATOM   1319  CA  LEU B 479      22.598  -6.125 -33.125  1.00 11.92           C  
ANISOU 1319  CA  LEU B 479     1275   1489   1764     49   -334    492       C  
ATOM   1320  C   LEU B 479      23.092  -4.770 -32.620  1.00 15.78           C  
ANISOU 1320  C   LEU B 479     1757   1895   2343     54   -370    536       C  
ATOM   1321  O   LEU B 479      22.964  -4.461 -31.434  1.00 16.88           O  
ANISOU 1321  O   LEU B 479     1887   1971   2553     88   -376    484       O  
ATOM   1322  CB  LEU B 479      23.741  -7.140 -33.136  1.00 11.59           C  
ANISOU 1322  CB  LEU B 479     1241   1493   1671     31   -256    456       C  
ATOM   1323  CG  LEU B 479      23.315  -8.606 -33.082  1.00 11.19           C  
ANISOU 1323  CG  LEU B 479     1204   1485   1564     41   -227    379       C  
ATOM   1324  CD1 LEU B 479      24.492  -9.527 -33.387  1.00 11.25           C  
ANISOU 1324  CD1 LEU B 479     1217   1527   1531     32   -156    348       C  
ATOM   1325  CD2 LEU B 479      22.709  -8.924 -31.719  1.00 14.53           C  
ANISOU 1325  CD2 LEU B 479     1608   1870   2042     67   -244    316       C  
ATOM   1326  N   ASP B 480      23.645  -3.966 -33.525  1.00 16.05           N  
ANISOU 1326  N   ASP B 480     1805   1929   2364      9   -399    632       N  
ATOM   1327  CA  ASP B 480      24.101  -2.624 -33.179  1.00 16.43           C  
ANISOU 1327  CA  ASP B 480     1858   1889   2498      0   -457    690       C  
ATOM   1328  C   ASP B 480      22.942  -1.742 -32.737  1.00 15.80           C  
ANISOU 1328  C   ASP B 480     1772   1715   2515     57   -538    677       C  
ATOM   1329  O   ASP B 480      23.080  -0.940 -31.816  1.00 16.02           O  
ANISOU 1329  O   ASP B 480     1807   1646   2632     86   -567    652       O  
ATOM   1330  CB  ASP B 480      24.821  -1.968 -34.355  1.00 16.36           C  
ANISOU 1330  CB  ASP B 480     1863   1908   2444    -78   -484    814       C  
ATOM   1331  CG  ASP B 480      26.218  -2.507 -34.552  1.00 18.84           C  
ANISOU 1331  CG  ASP B 480     2162   2297   2699   -128   -396    827       C  
ATOM   1332  OD1 ASP B 480      26.740  -3.154 -33.624  1.00 15.63           O  
ANISOU 1332  OD1 ASP B 480     1734   1884   2320    -98   -340    753       O  
ATOM   1333  OD2 ASP B 480      26.799  -2.273 -35.630  1.00 21.58           O  
ANISOU 1333  OD2 ASP B 480     2513   2711   2975   -201   -384    914       O  
ATOM   1334  N   LYS B 481      21.803  -1.891 -33.403  1.00 18.56           N  
ANISOU 1334  N   LYS B 481     2108   2091   2854     75   -576    690       N  
ATOM   1335  CA  LYS B 481      20.617  -1.127 -33.048  1.00 18.91           C  
ANISOU 1335  CA  LYS B 481     2129   2061   2997    137   -632    657       C  
ATOM   1336  C   LYS B 481      20.138  -1.493 -31.645  1.00 15.22           C  
ANISOU 1336  C   LYS B 481     1630   1569   2585    211   -584    539       C  
ATOM   1337  O   LYS B 481      19.724  -0.624 -30.881  1.00 17.21           O  
ANISOU 1337  O   LYS B 481     1877   1739   2924    262   -596    482       O  
ATOM   1338  CB  LYS B 481      19.501  -1.357 -34.067  1.00 16.54           C  
ANISOU 1338  CB  LYS B 481     1811   1807   2668    128   -677    697       C  
ATOM   1339  CG  LYS B 481      18.228  -0.592 -33.760  1.00 21.73           C  
ANISOU 1339  CG  LYS B 481     2426   2397   3432    192   -719    656       C  
ATOM   1340  CD  LYS B 481      18.473   0.903 -33.748  1.00 26.26           C  
ANISOU 1340  CD  LYS B 481     3023   2864   4091    193   -778    683       C  
ATOM   1341  CE  LYS B 481      18.553   1.452 -35.158  1.00 27.77           C  
ANISOU 1341  CE  LYS B 481     3241   3058   4250    109   -861    802       C  
ATOM   1342  NZ  LYS B 481      18.558   2.939 -35.174  1.00 31.68           N  
ANISOU 1342  NZ  LYS B 481     3750   3442   4847    109   -940    828       N  
ATOM   1343  N   ILE B 482      20.201  -2.776 -31.303  1.00 14.21           N  
ANISOU 1343  N   ILE B 482     1494   1524   2380    200   -509    479       N  
ATOM   1344  CA  ILE B 482      19.788  -3.210 -29.976  1.00 14.48           C  
ANISOU 1344  CA  ILE B 482     1508   1558   2435    240   -454    367       C  
ATOM   1345  C   ILE B 482      20.768  -2.717 -28.908  1.00 14.63           C  
ANISOU 1345  C   ILE B 482     1567   1508   2484    232   -433    328       C  
ATOM   1346  O   ILE B 482      20.362  -2.406 -27.789  1.00 16.35           O  
ANISOU 1346  O   ILE B 482     1783   1683   2747    270   -413    243       O  
ATOM   1347  CB  ILE B 482      19.645  -4.745 -29.899  1.00 16.05           C  
ANISOU 1347  CB  ILE B 482     1701   1857   2538    211   -397    323       C  
ATOM   1348  CG1 ILE B 482      18.666  -5.235 -30.963  1.00 17.50           C  
ANISOU 1348  CG1 ILE B 482     1860   2104   2686    205   -431    365       C  
ATOM   1349  CG2 ILE B 482      19.161  -5.170 -28.522  1.00 18.43           C  
ANISOU 1349  CG2 ILE B 482     1984   2168   2851    230   -349    222       C  
ATOM   1350  CD1 ILE B 482      18.586  -6.744 -31.077  1.00 22.45           C  
ANISOU 1350  CD1 ILE B 482     2499   2817   3215    167   -394    333       C  
ATOM   1351  N   THR B 483      22.052  -2.637 -29.252  1.00 12.53           N  
ANISOU 1351  N   THR B 483     1336   1236   2189    177   -436    390       N  
ATOM   1352  CA  THR B 483      23.029  -2.014 -28.363  1.00 13.01           C  
ANISOU 1352  CA  THR B 483     1435   1219   2288    155   -443    380       C  
ATOM   1353  C   THR B 483      22.658  -0.559 -28.105  1.00 13.38           C  
ANISOU 1353  C   THR B 483     1503   1147   2435    196   -512    382       C  
ATOM   1354  O   THR B 483      22.606  -0.119 -26.959  1.00 15.99           O  
ANISOU 1354  O   THR B 483     1863   1407   2805    218   -507    303       O  
ATOM   1355  CB  THR B 483      24.456  -2.068 -28.934  1.00 15.77           C  
ANISOU 1355  CB  THR B 483     1796   1589   2606     87   -443    469       C  
ATOM   1356  OG1 THR B 483      24.858  -3.433 -29.078  1.00 16.31           O  
ANISOU 1356  OG1 THR B 483     1845   1752   2602     65   -377    449       O  
ATOM   1357  CG2 THR B 483      25.426  -1.351 -28.004  1.00 18.31           C  
ANISOU 1357  CG2 THR B 483     2155   1823   2977     54   -472    475       C  
ATOM   1358  N   ASP B 484      22.393   0.177 -29.182  1.00 13.77           N  
ANISOU 1358  N   ASP B 484     1545   1179   2508    195   -572    462       N  
ATOM   1359  CA  ASP B 484      21.936   1.564 -29.080  1.00 15.07           C  
ANISOU 1359  CA  ASP B 484     1729   1245   2751    225   -630    448       C  
ATOM   1360  C   ASP B 484      20.699   1.686 -28.201  1.00 17.68           C  
ANISOU 1360  C   ASP B 484     2031   1536   3150    322   -609    332       C  
ATOM   1361  O   ASP B 484      20.554   2.635 -27.430  1.00 19.36           O  
ANISOU 1361  O   ASP B 484     2274   1651   3432    361   -627    267       O  
ATOM   1362  CB  ASP B 484      21.616   2.138 -30.464  1.00 17.50           C  
ANISOU 1362  CB  ASP B 484     2026   1566   3056    197   -693    543       C  
ATOM   1363  CG  ASP B 484      22.841   2.263 -31.352  1.00 25.73           C  
ANISOU 1363  CG  ASP B 484     3094   2646   4037     97   -713    655       C  
ATOM   1364  OD1 ASP B 484      23.976   2.175 -30.839  1.00 26.40           O  
ANISOU 1364  OD1 ASP B 484     3201   2729   4102     55   -688    661       O  
ATOM   1365  OD2 ASP B 484      22.658   2.465 -32.575  1.00 27.45           O  
ANISOU 1365  OD2 ASP B 484     3306   2898   4225     53   -756    742       O  
ATOM   1366  N   THR B 485      19.802   0.717 -28.343  1.00 15.48           N  
ANISOU 1366  N   THR B 485     1691   1340   2851    357   -569    304       N  
ATOM   1367  CA  THR B 485      18.548   0.708 -27.611  1.00 16.30           C  
ANISOU 1367  CA  THR B 485     1739   1440   3016    444   -532    198       C  
ATOM   1368  C   THR B 485      18.783   0.482 -26.116  1.00 18.21           C  
ANISOU 1368  C   THR B 485     2009   1663   3249    457   -462     76       C  
ATOM   1369  O   THR B 485      18.176   1.151 -25.280  1.00 18.37           O  
ANISOU 1369  O   THR B 485     2023   1618   3341    527   -440    -27       O  
ATOM   1370  CB  THR B 485      17.607  -0.369 -28.170  1.00 21.35           C  
ANISOU 1370  CB  THR B 485     2301   2195   3615    451   -508    212       C  
ATOM   1371  OG1 THR B 485      17.291  -0.057 -29.535  1.00 21.58           O  
ANISOU 1371  OG1 THR B 485     2326   2238   3635    423   -574    315       O  
ATOM   1372  CG2 THR B 485      16.324  -0.415 -27.379  1.00 20.83           C  
ANISOU 1372  CG2 THR B 485     2158   2147   3609    531   -457    106       C  
ATOM   1373  N   LEU B 486      19.668  -0.458 -25.787  1.00 16.76           N  
ANISOU 1373  N   LEU B 486     1864   1548   2957    375   -416     81       N  
ATOM   1374  CA  LEU B 486      20.033  -0.713 -24.394  1.00 17.11           C  
ANISOU 1374  CA  LEU B 486     1957   1590   2955    344   -357    -18       C  
ATOM   1375  C   LEU B 486      20.634   0.519 -23.732  1.00 16.43           C  
ANISOU 1375  C   LEU B 486     1949   1366   2927    349   -398    -48       C  
ATOM   1376  O   LEU B 486      20.252   0.885 -22.619  1.00 18.53           O  
ANISOU 1376  O   LEU B 486     2247   1593   3201    376   -357   -167       O  
ATOM   1377  CB  LEU B 486      21.015  -1.881 -24.293  1.00 18.44           C  
ANISOU 1377  CB  LEU B 486     2151   1834   3021    251   -334     20       C  
ATOM   1378  CG  LEU B 486      20.380  -3.264 -24.193  1.00 19.21           C  
ANISOU 1378  CG  LEU B 486     2202   2054   3042    233   -277    -11       C  
ATOM   1379  CD1 LEU B 486      21.444  -4.337 -24.297  1.00 18.66           C  
ANISOU 1379  CD1 LEU B 486     2157   2030   2902    155   -276     38       C  
ATOM   1380  CD2 LEU B 486      19.635  -3.388 -22.874  1.00 16.19           C  
ANISOU 1380  CD2 LEU B 486     1820   1695   2635    237   -215   -130       C  
ATOM   1381  N   ILE B 487      21.576   1.152 -24.423  1.00 15.39           N  
ANISOU 1381  N   ILE B 487     1854   1166   2827    315   -479     60       N  
ATOM   1382  CA  ILE B 487      22.210   2.362 -23.921  1.00 18.20           C  
ANISOU 1382  CA  ILE B 487     2293   1378   3244    306   -544     53       C  
ATOM   1383  C   ILE B 487      21.175   3.460 -23.694  1.00 17.22           C  
ANISOU 1383  C   ILE B 487     2165   1166   3210    404   -556    -31       C  
ATOM   1384  O   ILE B 487      21.234   4.185 -22.701  1.00 19.81           O  
ANISOU 1384  O   ILE B 487     2566   1405   3558    419   -553   -127       O  
ATOM   1385  CB  ILE B 487      23.310   2.860 -24.887  1.00 21.98           C  
ANISOU 1385  CB  ILE B 487     2788   1854   3709    230   -615    199       C  
ATOM   1386  CG1 ILE B 487      24.524   1.931 -24.826  1.00 21.90           C  
ANISOU 1386  CG1 ILE B 487     2784   1908   3628    138   -596    263       C  
ATOM   1387  CG2 ILE B 487      23.732   4.283 -24.547  1.00 21.56           C  
ANISOU 1387  CG2 ILE B 487     2805   1693   3693    214   -681    195       C  
ATOM   1388  CD1 ILE B 487      25.334   2.060 -23.546  1.00 21.56           C  
ANISOU 1388  CD1 ILE B 487     2818   1810   3565     79   -602    216       C  
ATOM   1389  N   HIS B 488      20.207   3.550 -24.601  1.00 17.49           N  
ANISOU 1389  N   HIS B 488     2118   1242   3285    463   -564      0       N  
ATOM   1390  CA  HIS B 488      19.170   4.575 -24.512  1.00 18.99           C  
ANISOU 1390  CA  HIS B 488     2285   1366   3564    554   -574    -66       C  
ATOM   1391  C   HIS B 488      18.257   4.364 -23.303  1.00 19.61           C  
ANISOU 1391  C   HIS B 488     2339   1448   3664    637   -474   -238       C  
ATOM   1392  O   HIS B 488      17.886   5.321 -22.623  1.00 21.22           O  
ANISOU 1392  O   HIS B 488     2576   1566   3921    696   -462   -336       O  
ATOM   1393  CB  HIS B 488      18.343   4.607 -25.799  1.00 22.81           C  
ANISOU 1393  CB  HIS B 488     2685   1901   4081    577   -613     22       C  
ATOM   1394  CG  HIS B 488      17.317   5.694 -25.821  1.00 25.99           C  
ANISOU 1394  CG  HIS B 488     3055   2228   4593    666   -641    -24       C  
ATOM   1395  ND1 HIS B 488      15.962   5.442 -25.784  1.00 30.93           N  
ANISOU 1395  ND1 HIS B 488     3582   2902   5269    750   -591    -83       N  
ATOM   1396  CD2 HIS B 488      17.450   7.041 -25.838  1.00 22.38           C  
ANISOU 1396  CD2 HIS B 488     2646   1647   4209    683   -716    -21       C  
ATOM   1397  CE1 HIS B 488      15.305   6.587 -25.801  1.00 30.49           C  
ANISOU 1397  CE1 HIS B 488     3511   2752   5319    822   -631   -112       C  
ATOM   1398  NE2 HIS B 488      16.183   7.573 -25.831  1.00 35.25           N  
ANISOU 1398  NE2 HIS B 488     4206   3245   5941    785   -711    -79       N  
ATOM   1399  N   LEU B 489      17.895   3.112 -23.040  1.00 18.95           N  
ANISOU 1399  N   LEU B 489     2194   1473   3531    636   -396   -280       N  
ATOM   1400  CA  LEU B 489      17.108   2.781 -21.856  1.00 21.91           C  
ANISOU 1400  CA  LEU B 489     2544   1899   3883    679   -278   -444       C  
ATOM   1401  C   LEU B 489      17.818   3.227 -20.580  1.00 19.86           C  
ANISOU 1401  C   LEU B 489     2412   1565   3569    635   -249   -550       C  
ATOM   1402  O   LEU B 489      17.197   3.757 -19.657  1.00 20.84           O  
ANISOU 1402  O   LEU B 489     2549   1650   3720    701   -179   -705       O  
ATOM   1403  CB  LEU B 489      16.828   1.279 -21.796  1.00 19.00           C  
ANISOU 1403  CB  LEU B 489     2116   1714   3390    611   -199   -430       C  
ATOM   1404  CG  LEU B 489      15.830   0.702 -22.799  1.00 18.22           C  
ANISOU 1404  CG  LEU B 489     1888   1708   3327    652   -206   -363       C  
ATOM   1405  CD1 LEU B 489      15.890  -0.830 -22.801  1.00 18.87           C  
ANISOU 1405  CD1 LEU B 489     1951   1948   3272    556   -159   -327       C  
ATOM   1406  CD2 LEU B 489      14.429   1.203 -22.477  1.00 23.76           C  
ANISOU 1406  CD2 LEU B 489     2481   2409   4138    772   -151   -467       C  
ATOM   1407  N   MET B 490      19.128   3.011 -20.544  1.00 18.26           N  
ANISOU 1407  N   MET B 490     2302   1345   3289    522   -302   -466       N  
ATOM   1408  CA  MET B 490      19.940   3.386 -19.397  1.00 19.96           C  
ANISOU 1408  CA  MET B 490     2651   1488   3446    453   -302   -537       C  
ATOM   1409  C   MET B 490      20.053   4.904 -19.261  1.00 20.14           C  
ANISOU 1409  C   MET B 490     2752   1329   3572    512   -373   -578       C  
ATOM   1410  O   MET B 490      20.045   5.437 -18.148  1.00 23.50           O  
ANISOU 1410  O   MET B 490     3270   1697   3961    508   -333   -705       O  
ATOM   1411  CB  MET B 490      21.324   2.750 -19.511  1.00 18.05           C  
ANISOU 1411  CB  MET B 490     2463   1276   3119    318   -357   -411       C  
ATOM   1412  CG  MET B 490      21.287   1.231 -19.419  1.00 16.56           C  
ANISOU 1412  CG  MET B 490     2220   1253   2819    250   -290   -387       C  
ATOM   1413  SD  MET B 490      22.854   0.459 -19.839  1.00 18.71           S  
ANISOU 1413  SD  MET B 490     2515   1554   3039    126   -358   -230       S  
ATOM   1414  CE  MET B 490      22.337  -1.233 -20.127  1.00 18.33           C  
ANISOU 1414  CE  MET B 490     2375   1680   2910    105   -288   -213       C  
ATOM   1415  N   ALA B 491      20.147   5.592 -20.396  1.00 20.69           N  
ANISOU 1415  N   ALA B 491     2784   1362   3714    536   -461   -447       N  
ATOM   1416  CA  ALA B 491      20.220   7.049 -20.415  1.00 22.36           C  
ANISOU 1416  CA  ALA B 491     3055   1452   3990    566   -528   -447       C  
ATOM   1417  C   ALA B 491      18.903   7.654 -19.938  1.00 23.49           C  
ANISOU 1417  C   ALA B 491     3160   1562   4203    695   -456   -593       C  
ATOM   1418  O   ALA B 491      18.894   8.624 -19.179  1.00 26.18           O  
ANISOU 1418  O   ALA B 491     3587   1799   4562    723   -452   -689       O  
ATOM   1419  CB  ALA B 491      20.564   7.546 -21.810  1.00 26.47           C  
ANISOU 1419  CB  ALA B 491     3534   1963   4560    543   -639   -274       C  
ATOM   1420  N   LYS B 492      17.796   7.070 -20.388  1.00 23.39           N  
ANISOU 1420  N   LYS B 492     3015   1645   4227    770   -397   -607       N  
ATOM   1421  CA  LYS B 492      16.470   7.452 -19.909  1.00 26.41           C  
ANISOU 1421  CA  LYS B 492     3330   2033   4670    890   -306   -742       C  
ATOM   1422  C   LYS B 492      16.378   7.357 -18.395  1.00 25.81           C  
ANISOU 1422  C   LYS B 492     3330   1965   4513    891   -183   -928       C  
ATOM   1423  O   LYS B 492      15.717   8.167 -17.747  1.00 29.52           O  
ANISOU 1423  O   LYS B 492     3816   2379   5020    973   -124  -1052       O  
ATOM   1424  CB  LYS B 492      15.389   6.560 -20.509  1.00 31.03           C  
ANISOU 1424  CB  LYS B 492     3756   2758   5277    937   -252   -716       C  
ATOM   1425  CG  LYS B 492      14.541   7.169 -21.603  1.00 33.53           C  
ANISOU 1425  CG  LYS B 492     3975   3051   5711   1008   -323   -628       C  
ATOM   1426  CD  LYS B 492      13.351   6.249 -21.867  1.00 35.30           C  
ANISOU 1426  CD  LYS B 492     4049   3421   5941   1050   -247   -632       C  
ATOM   1427  CE  LYS B 492      13.209   5.874 -23.323  1.00 32.87           C  
ANISOU 1427  CE  LYS B 492     3674   3160   5653   1013   -344   -460       C  
ATOM   1428  NZ  LYS B 492      12.507   6.927 -24.113  1.00 33.30           N  
ANISOU 1428  NZ  LYS B 492     3684   3133   5834   1076   -432   -403       N  
ATOM   1429  N   ALA B 493      17.026   6.336 -17.844  1.00 24.17           N  
ANISOU 1429  N   ALA B 493     3169   1830   4186    791   -143   -949       N  
ATOM   1430  CA  ALA B 493      16.983   6.083 -16.410  1.00 28.76           C  
ANISOU 1430  CA  ALA B 493     3832   2447   4650    752    -25  -1118       C  
ATOM   1431  C   ALA B 493      17.916   7.012 -15.647  1.00 30.12           C  
ANISOU 1431  C   ALA B 493     4189   2478   4779    691    -77  -1157       C  
ATOM   1432  O   ALA B 493      17.931   7.010 -14.417  1.00 34.24           O  
ANISOU 1432  O   ALA B 493     4812   3009   5189    646      9  -1296       O  
ATOM   1433  CB  ALA B 493      17.333   4.640 -16.121  1.00 25.19           C  
ANISOU 1433  CB  ALA B 493     3366   2125   4082    644     20  -1119       C  
ATOM   1434  N   GLY B 494      18.703   7.795 -16.376  1.00 25.81           N  
ANISOU 1434  N   GLY B 494     3689   1812   4304    673   -217  -1024       N  
ATOM   1435  CA  GLY B 494      19.549   8.797 -15.759  1.00 26.60           C  
ANISOU 1435  CA  GLY B 494     3950   1776   4381    615   -277  -1042       C  
ATOM   1436  C   GLY B 494      20.919   8.300 -15.339  1.00 25.78           C  
ANISOU 1436  C   GLY B 494     3955   1676   4165    447   -337   -969       C  
ATOM   1437  O   GLY B 494      21.597   8.940 -14.538  1.00 26.31           O  
ANISOU 1437  O   GLY B 494     4159   1659   4180    372   -365  -1005       O  
ATOM   1438  N   LEU B 495      21.327   7.155 -15.877  1.00 24.79           N  
ANISOU 1438  N   LEU B 495     3762   1651   4006    383   -360   -861       N  
ATOM   1439  CA  LEU B 495      22.668   6.645 -15.630  1.00 22.25           C  
ANISOU 1439  CA  LEU B 495     3514   1344   3594    225   -429   -755       C  
ATOM   1440  C   LEU B 495      23.700   7.537 -16.308  1.00 24.30           C  
ANISOU 1440  C   LEU B 495     3798   1527   3909    183   -559   -595       C  
ATOM   1441  O   LEU B 495      23.461   8.053 -17.399  1.00 22.36           O  
ANISOU 1441  O   LEU B 495     3476   1259   3761    254   -611   -512       O  
ATOM   1442  CB  LEU B 495      22.808   5.202 -16.125  1.00 21.60           C  
ANISOU 1442  CB  LEU B 495     3344   1385   3479    179   -421   -675       C  
ATOM   1443  CG  LEU B 495      22.444   4.071 -15.160  1.00 25.26           C  
ANISOU 1443  CG  LEU B 495     3814   1975   3809    117   -316   -775       C  
ATOM   1444  CD1 LEU B 495      20.990   4.139 -14.727  1.00 27.73           C  
ANISOU 1444  CD1 LEU B 495     4071   2344   4120    228   -178   -952       C  
ATOM   1445  CD2 LEU B 495      22.762   2.717 -15.783  1.00 21.62           C  
ANISOU 1445  CD2 LEU B 495     3251   1662   3303     55   -313   -636       C  
ATOM   1446  N   THR B 496      24.843   7.723 -15.655  1.00 22.64           N  
ANISOU 1446  N   THR B 496     3683   1292   3626     58   -614   -547       N  
ATOM   1447  CA  THR B 496      25.954   8.441 -16.267  1.00 25.60           C  
ANISOU 1447  CA  THR B 496     4062   1631   4035      1   -735   -387       C  
ATOM   1448  C   THR B 496      26.481   7.616 -17.439  1.00 27.69           C  
ANISOU 1448  C   THR B 496     4206   2004   4308    -28   -765   -219       C  
ATOM   1449  O   THR B 496      26.180   6.426 -17.541  1.00 22.45           O  
ANISOU 1449  O   THR B 496     3483   1432   3614    -28   -702   -226       O  
ATOM   1450  CB  THR B 496      27.092   8.710 -15.263  1.00 28.10           C  
ANISOU 1450  CB  THR B 496     4485   1924   4269   -127   -786   -365       C  
ATOM   1451  OG1 THR B 496      27.729   7.477 -14.910  1.00 23.72           O  
ANISOU 1451  OG1 THR B 496     3905   1484   3624   -225   -765   -308       O  
ATOM   1452  CG2 THR B 496      26.550   9.371 -13.998  1.00 30.87           C  
ANISOU 1452  CG2 THR B 496     4964   2181   4585   -114   -735   -552       C  
ATOM   1453  N   LEU B 497      27.255   8.240 -18.323  1.00 24.67           N  
ANISOU 1453  N   LEU B 497     2960   2690   3725     50   -226   -516       N  
ATOM   1454  CA  LEU B 497      27.849   7.512 -19.442  1.00 24.93           C  
ANISOU 1454  CA  LEU B 497     2953   2766   3753     14   -235   -437       C  
ATOM   1455  C   LEU B 497      28.713   6.354 -18.957  1.00 21.10           C  
ANISOU 1455  C   LEU B 497     2438   2373   3205    -19   -260   -454       C  
ATOM   1456  O   LEU B 497      28.687   5.274 -19.542  1.00 21.19           O  
ANISOU 1456  O   LEU B 497     2418   2453   3182    -16   -257   -401       O  
ATOM   1457  CB  LEU B 497      28.677   8.444 -20.330  1.00 24.91           C  
ANISOU 1457  CB  LEU B 497     2953   2685   3826    -39   -241   -403       C  
ATOM   1458  CG  LEU B 497      27.905   9.254 -21.368  1.00 25.39           C  
ANISOU 1458  CG  LEU B 497     3021   2677   3950    -10   -215   -335       C  
ATOM   1459  CD1 LEU B 497      28.854  10.157 -22.142  1.00 30.08           C  
ANISOU 1459  CD1 LEU B 497     3615   3198   4618    -69   -224   -301       C  
ATOM   1460  CD2 LEU B 497      27.163   8.313 -22.307  1.00 27.72           C  
ANISOU 1460  CD2 LEU B 497     3281   3046   4205     23   -200   -253       C  
ATOM   1461  N   GLN B 498      29.469   6.576 -17.885  1.00 20.86           N  
ANISOU 1461  N   GLN B 498     2421   2345   3161    -52   -283   -530       N  
ATOM   1462  CA  GLN B 498      30.307   5.518 -17.333  1.00 21.72           C  
ANISOU 1462  CA  GLN B 498     2498   2543   3211    -80   -308   -543       C  
ATOM   1463  C   GLN B 498      29.449   4.361 -16.819  1.00 19.72           C  
ANISOU 1463  C   GLN B 498     2230   2374   2888    -27   -298   -535       C  
ATOM   1464  O   GLN B 498      29.756   3.194 -17.069  1.00 20.91           O  
ANISOU 1464  O   GLN B 498     2345   2595   3004    -33   -303   -495       O  
ATOM   1465  CB  GLN B 498      31.199   6.056 -16.213  1.00 23.63           C  
ANISOU 1465  CB  GLN B 498     2754   2778   3447   -126   -338   -626       C  
ATOM   1466  CG  GLN B 498      32.018   4.979 -15.515  1.00 20.38           C  
ANISOU 1466  CG  GLN B 498     2304   2467   2971   -150   -365   -635       C  
ATOM   1467  CD  GLN B 498      32.793   5.504 -14.322  1.00 25.48           C  
ANISOU 1467  CD  GLN B 498     2962   3120   3599   -195   -398   -719       C  
ATOM   1468  OE1 GLN B 498      32.278   6.287 -13.524  1.00 31.48           O  
ANISOU 1468  OE1 GLN B 498     3763   3843   4355   -180   -395   -793       O  
ATOM   1469  NE2 GLN B 498      34.038   5.071 -14.194  1.00 24.98           N  
ANISOU 1469  NE2 GLN B 498     2861   3109   3522   -250   -429   -710       N  
ATOM   1470  N   GLN B 499      28.368   4.688 -16.115  1.00 18.03           N  
ANISOU 1470  N   GLN B 499     2042   2150   2657     25   -281   -573       N  
ATOM   1471  CA  GLN B 499      27.446   3.664 -15.633  1.00 18.41           C  
ANISOU 1471  CA  GLN B 499     2075   2277   2643     76   -269   -560       C  
ATOM   1472  C   GLN B 499      26.765   2.933 -16.785  1.00 17.86           C  
ANISOU 1472  C   GLN B 499     1982   2226   2577     99   -249   -475       C  
ATOM   1473  O   GLN B 499      26.520   1.728 -16.693  1.00 18.40           O  
ANISOU 1473  O   GLN B 499     2024   2368   2599    113   -249   -445       O  
ATOM   1474  CB  GLN B 499      26.387   4.264 -14.705  1.00 20.36           C  
ANISOU 1474  CB  GLN B 499     2354   2510   2874    130   -249   -615       C  
ATOM   1475  CG  GLN B 499      26.931   4.803 -13.389  1.00 20.91           C  
ANISOU 1475  CG  GLN B 499     2446   2582   2918    110   -267   -711       C  
ATOM   1476  CD  GLN B 499      25.892   5.583 -12.597  1.00 22.53           C  
ANISOU 1476  CD  GLN B 499     2688   2758   3115    166   -241   -772       C  
ATOM   1477  OE1 GLN B 499      24.945   6.136 -13.159  1.00 24.91           O  
ANISOU 1477  OE1 GLN B 499     3004   3002   3459    212   -210   -747       O  
ATOM   1478  NE2 GLN B 499      26.061   5.618 -11.281  1.00 29.31           N  
ANISOU 1478  NE2 GLN B 499     3558   3662   3917    164   -252   -852       N  
ATOM   1479  N   GLN B 500      26.456   3.651 -17.865  1.00 17.88           N  
ANISOU 1479  N   GLN B 500     1994   2163   2635    102   -234   -434       N  
ATOM   1480  CA  GLN B 500      25.859   3.016 -19.036  1.00 18.24           C  
ANISOU 1480  CA  GLN B 500     2016   2232   2680    116   -219   -354       C  
ATOM   1481  C   GLN B 500      26.771   1.941 -19.630  1.00 16.07           C  
ANISOU 1481  C   GLN B 500     1710   2010   2387     75   -233   -319       C  
ATOM   1482  O   GLN B 500      26.334   0.809 -19.845  1.00 16.35           O  
ANISOU 1482  O   GLN B 500     1723   2105   2384     90   -227   -286       O  
ATOM   1483  CB  GLN B 500      25.516   4.050 -20.119  1.00 16.94           C  
ANISOU 1483  CB  GLN B 500     1863   1993   2578    120   -204   -311       C  
ATOM   1484  CG  GLN B 500      24.414   5.044 -19.756  1.00 17.63           C  
ANISOU 1484  CG  GLN B 500     1978   2026   2694    175   -182   -328       C  
ATOM   1485  CD  GLN B 500      24.356   6.225 -20.716  1.00 18.27           C  
ANISOU 1485  CD  GLN B 500     2071   2020   2850    171   -170   -287       C  
ATOM   1486  OE1 GLN B 500      24.563   6.077 -21.925  1.00 21.93           O  
ANISOU 1486  OE1 GLN B 500     2513   2488   3329    147   -171   -217       O  
ATOM   1487  NE2 GLN B 500      24.066   7.407 -20.180  1.00 23.47           N  
ANISOU 1487  NE2 GLN B 500     2765   2597   3557    196   -158   -330       N  
ATOM   1488  N   HIS B 501      28.032   2.277 -19.897  1.00 14.75           N  
ANISOU 1488  N   HIS B 501     1538   1819   2248     23   -249   -326       N  
ATOM   1489  CA AHIS B 501      28.876   1.285 -20.550  0.55 15.11           C  
ANISOU 1489  CA AHIS B 501     1551   1912   2278     -9   -255   -290       C  
ATOM   1490  CA BHIS B 501      28.985   1.346 -20.499  0.45 15.51           C  
ANISOU 1490  CA BHIS B 501     1603   1961   2332    -13   -257   -294       C  
ATOM   1491  C   HIS B 501      29.234   0.154 -19.585  0.95 15.08           C  
ANISOU 1491  C   HIS B 501     1528   1977   2223     -6   -268   -315       C  
ATOM   1492  O   HIS B 501      29.409  -0.981 -20.031  0.91 15.91           O  
ANISOU 1492  O   HIS B 501     1608   2131   2307     -8   -264   -280       O  
ATOM   1493  CB AHIS B 501      30.135   1.916 -21.184  0.55 18.18           C  
ANISOU 1493  CB AHIS B 501     1932   2264   2711    -64   -265   -280       C  
ATOM   1494  CB BHIS B 501      30.314   2.048 -20.790  0.45 17.41           C  
ANISOU 1494  CB BHIS B 501     1839   2164   2614    -69   -272   -300       C  
ATOM   1495  CG AHIS B 501      31.139   2.465 -20.214  0.55 17.87           C  
ANISOU 1495  CG AHIS B 501     1899   2210   2683   -101   -291   -337       C  
ATOM   1496  CG BHIS B 501      30.186   3.257 -21.663  0.45 19.49           C  
ANISOU 1496  CG BHIS B 501     2118   2352   2936    -81   -263   -273       C  
ATOM   1497  ND1AHIS B 501      31.669   3.731 -20.345  0.55 20.61           N  
ANISOU 1497  ND1AHIS B 501     2263   2484   3084   -137   -300   -353       N  
ATOM   1498  ND1BHIS B 501      29.227   3.370 -22.646  0.45 19.47           N  
ANISOU 1498  ND1BHIS B 501     2117   2336   2943    -53   -240   -218       N  
ATOM   1499  CD2AHIS B 501      31.762   1.909 -19.147  0.55 15.84           C  
ANISOU 1499  CD2AHIS B 501     1629   2003   2388   -112   -312   -378       C  
ATOM   1500  CD2BHIS B 501      30.894   4.411 -21.695  0.45 19.51           C  
ANISOU 1500  CD2BHIS B 501     2133   2287   2991   -120   -273   -289       C  
ATOM   1501  CE1AHIS B 501      32.549   3.943 -19.383  0.55 19.15           C  
ANISOU 1501  CE1AHIS B 501     2077   2306   2893   -172   -326   -408       C  
ATOM   1502  CE1BHIS B 501      29.352   4.539 -23.250  0.45 18.10           C  
ANISOU 1502  CE1BHIS B 501     1957   2093   2829    -70   -236   -196       C  
ATOM   1503  NE2AHIS B 501      32.621   2.853 -18.640  0.55 15.34           N  
ANISOU 1503  NE2AHIS B 501     1575   1902   2352   -157   -335   -422       N  
ATOM   1504  NE2BHIS B 501      30.356   5.191 -22.688  0.45 22.16           N  
ANISOU 1504  NE2BHIS B 501     2479   2568   3373   -112   -255   -239       N  
ATOM   1505  N   GLN B 502      29.282   0.438 -18.285  1.00 16.80           N  
ANISOU 1505  N   GLN B 502     1759   2204   2422      0   -283   -372       N  
ATOM   1506  CA  GLN B 502      29.547  -0.605 -17.302  1.00 13.41           C  
ANISOU 1506  CA  GLN B 502     1309   1847   1941      6   -296   -388       C  
ATOM   1507  C   GLN B 502      28.381  -1.585 -17.243  1.00 13.94           C  
ANISOU 1507  C   GLN B 502     1368   1957   1971     52   -278   -358       C  
ATOM   1508  O   GLN B 502      28.587  -2.797 -17.238  1.00 15.54           O  
ANISOU 1508  O   GLN B 502     1544   2212   2149     53   -280   -330       O  
ATOM   1509  CB  GLN B 502      29.810  -0.013 -15.913  1.00 15.66           C  
ANISOU 1509  CB  GLN B 502     1608   2139   2203      0   -316   -458       C  
ATOM   1510  CG  GLN B 502      31.213   0.555 -15.727  1.00 14.43           C  
ANISOU 1510  CG  GLN B 502     1445   1967   2069    -58   -343   -487       C  
ATOM   1511  CD  GLN B 502      31.434   1.142 -14.341  1.00 16.75           C  
ANISOU 1511  CD  GLN B 502     1756   2275   2334    -69   -365   -564       C  
ATOM   1512  OE1 GLN B 502      30.568   1.055 -13.468  1.00 19.21           O  
ANISOU 1512  OE1 GLN B 502     2081   2613   2603    -29   -358   -595       O  
ATOM   1513  NE2 GLN B 502      32.599   1.744 -14.135  1.00 22.03           N  
ANISOU 1513  NE2 GLN B 502     2421   2929   3022   -126   -393   -595       N  
ATOM   1514  N   ARG B 503      27.160  -1.061 -17.211  1.00 14.26           N  
ANISOU 1514  N   ARG B 503     1431   1976   2013     91   -261   -361       N  
ATOM   1515  CA  ARG B 503      25.975  -1.914 -17.131  1.00 12.95           C  
ANISOU 1515  CA  ARG B 503     1254   1853   1813    132   -245   -331       C  
ATOM   1516  C   ARG B 503      25.773  -2.721 -18.414  1.00 13.56           C  
ANISOU 1516  C   ARG B 503     1314   1938   1900    124   -235   -269       C  
ATOM   1517  O   ARG B 503      25.392  -3.892 -18.366  1.00 13.65           O  
ANISOU 1517  O   ARG B 503     1307   1997   1884    135   -231   -242       O  
ATOM   1518  CB  ARG B 503      24.730  -1.076 -16.836  1.00 13.12           C  
ANISOU 1518  CB  ARG B 503     1299   1850   1837    177   -227   -345       C  
ATOM   1519  CG  ARG B 503      23.456  -1.897 -16.671  1.00 16.01           C  
ANISOU 1519  CG  ARG B 503     1649   2267   2167    219   -212   -311       C  
ATOM   1520  CD  ARG B 503      22.292  -1.036 -16.178  1.00 16.54           C  
ANISOU 1520  CD  ARG B 503     1734   2319   2233    270   -192   -330       C  
ATOM   1521  NE  ARG B 503      21.069  -1.813 -15.978  1.00 17.43           N  
ANISOU 1521  NE  ARG B 503     1826   2488   2309    307   -178   -293       N  
ATOM   1522  CZ  ARG B 503      20.795  -2.506 -14.875  1.00 19.60           C  
ANISOU 1522  CZ  ARG B 503     2086   2828   2533    325   -179   -306       C  
ATOM   1523  NH1 ARG B 503      21.658  -2.526 -13.871  1.00 18.36           N  
ANISOU 1523  NH1 ARG B 503     1934   2692   2351    310   -196   -355       N  
ATOM   1524  NH2 ARG B 503      19.654  -3.181 -14.773  1.00 21.27           N  
ANISOU 1524  NH2 ARG B 503     2275   3089   2717    356   -166   -264       N  
ATOM   1525  N   LEU B 504      26.028  -2.092 -19.558  1.00 14.88           N  
ANISOU 1525  N   LEU B 504     1488   2060   2108    104   -229   -247       N  
ATOM   1526  CA  LEU B 504      25.952  -2.783 -20.838  1.00 13.08           C  
ANISOU 1526  CA  LEU B 504     1244   1843   1883     90   -219   -195       C  
ATOM   1527  C   LEU B 504      26.887  -3.987 -20.831  1.00 11.32           C  
ANISOU 1527  C   LEU B 504      998   1660   1644     66   -226   -191       C  
ATOM   1528  O   LEU B 504      26.509  -5.087 -21.235  1.00 12.83           O  
ANISOU 1528  O   LEU B 504     1176   1883   1817     71   -218   -164       O  
ATOM   1529  CB  LEU B 504      26.305  -1.835 -21.985  1.00 15.22           C  
ANISOU 1529  CB  LEU B 504     1522   2065   2195     66   -214   -173       C  
ATOM   1530  CG  LEU B 504      26.453  -2.507 -23.350  1.00 15.16           C  
ANISOU 1530  CG  LEU B 504     1497   2078   2185     44   -204   -126       C  
ATOM   1531  CD1 LEU B 504      25.118  -3.077 -23.816  1.00 16.06           C  
ANISOU 1531  CD1 LEU B 504     1606   2222   2273     69   -193    -91       C  
ATOM   1532  CD2 LEU B 504      27.011  -1.532 -24.376  1.00 14.58           C  
ANISOU 1532  CD2 LEU B 504     1426   1964   2150     16   -201   -101       C  
ATOM   1533  N   ALA B 505      28.106  -3.768 -20.349  1.00 13.83           N  
ANISOU 1533  N   ALA B 505     1311   1973   1972     41   -241   -219       N  
ATOM   1534  CA  ALA B 505      29.095  -4.832 -20.266  1.00 12.91           C  
ANISOU 1534  CA  ALA B 505     1168   1893   1847     24   -246   -212       C  
ATOM   1535  C   ALA B 505      28.637  -5.928 -19.311  1.00 11.83           C  
ANISOU 1535  C   ALA B 505     1018   1802   1673     50   -249   -212       C  
ATOM   1536  O   ALA B 505      28.726  -7.109 -19.629  1.00 11.71           O  
ANISOU 1536  O   ALA B 505      986   1812   1652     52   -241   -186       O  
ATOM   1537  CB  ALA B 505      30.444  -4.274 -19.833  1.00 12.97           C  
ANISOU 1537  CB  ALA B 505     1166   1892   1870     -8   -265   -238       C  
ATOM   1538  N   GLN B 506      28.135  -5.534 -18.145  1.00 11.43           N  
ANISOU 1538  N   GLN B 506      978   1765   1600     72   -259   -240       N  
ATOM   1539  CA  GLN B 506      27.680  -6.505 -17.153  1.00 12.70           C  
ANISOU 1539  CA  GLN B 506     1123   1978   1723     96   -262   -234       C  
ATOM   1540  C   GLN B 506      26.583  -7.402 -17.725  1.00 11.60           C  
ANISOU 1540  C   GLN B 506      981   1850   1576    116   -244   -194       C  
ATOM   1541  O   GLN B 506      26.570  -8.611 -17.496  1.00 13.55           O  
ANISOU 1541  O   GLN B 506     1209   2129   1812    120   -242   -169       O  
ATOM   1542  CB  GLN B 506      27.160  -5.801 -15.900  1.00 13.45           C  
ANISOU 1542  CB  GLN B 506     1233   2090   1789    119   -270   -273       C  
ATOM   1543  CG  GLN B 506      28.227  -5.124 -15.050  1.00 14.26           C  
ANISOU 1543  CG  GLN B 506     1336   2197   1886     96   -293   -320       C  
ATOM   1544  CD  GLN B 506      27.667  -3.974 -14.231  1.00 24.28           C  
ANISOU 1544  CD  GLN B 506     2633   3453   3140    112   -295   -374       C  
ATOM   1545  OE1 GLN B 506      26.450  -3.788 -14.151  1.00 24.74           O  
ANISOU 1545  OE1 GLN B 506     2706   3508   3187    149   -277   -372       O  
ATOM   1546  NE2 GLN B 506      28.554  -3.208 -13.598  1.00 20.84           N  
ANISOU 1546  NE2 GLN B 506     2205   3011   2703     85   -316   -424       N  
ATOM   1547  N   LEU B 507      25.671  -6.798 -18.478  1.00 10.87           N  
ANISOU 1547  N   LEU B 507      906   1730   1494    124   -231   -185       N  
ATOM   1548  CA  LEU B 507      24.567  -7.535 -19.075  1.00 10.61           C  
ANISOU 1548  CA  LEU B 507      869   1712   1453    136   -218   -147       C  
ATOM   1549  C   LEU B 507      25.045  -8.527 -20.123  1.00 11.85           C  
ANISOU 1549  C   LEU B 507     1014   1866   1622    110   -211   -123       C  
ATOM   1550  O   LEU B 507      24.605  -9.672 -20.142  1.00 12.43           O  
ANISOU 1550  O   LEU B 507     1077   1962   1685    112   -206   -101       O  
ATOM   1551  CB  LEU B 507      23.553  -6.575 -19.703  1.00 13.90           C  
ANISOU 1551  CB  LEU B 507     1301   2104   1878    150   -207   -138       C  
ATOM   1552  CG  LEU B 507      22.749  -5.759 -18.694  1.00 16.63           C  
ANISOU 1552  CG  LEU B 507     1657   2454   2210    187   -205   -159       C  
ATOM   1553  CD1 LEU B 507      21.726  -4.899 -19.402  1.00 17.06           C  
ANISOU 1553  CD1 LEU B 507     1720   2483   2279    206   -192   -138       C  
ATOM   1554  CD2 LEU B 507      22.066  -6.682 -17.695  1.00 19.94           C  
ANISOU 1554  CD2 LEU B 507     2058   2928   2590    211   -205   -149       C  
ATOM   1555  N   LEU B 508      25.943  -8.089 -20.998  1.00 11.71           N  
ANISOU 1555  N   LEU B 508     1001   1821   1629     84   -209   -128       N  
ATOM   1556  CA  LEU B 508      26.406  -8.953 -22.078  1.00 10.28           C  
ANISOU 1556  CA  LEU B 508      811   1639   1456     62   -197   -111       C  
ATOM   1557  C   LEU B 508      27.303 -10.081 -21.580  1.00 10.24           C  
ANISOU 1557  C   LEU B 508      787   1650   1454     60   -198   -113       C  
ATOM   1558  O   LEU B 508      27.358 -11.146 -22.189  1.00 13.67           O  
ANISOU 1558  O   LEU B 508     1215   2086   1892     53   -185   -100       O  
ATOM   1559  CB  LEU B 508      27.140  -8.136 -23.140  1.00 10.38           C  
ANISOU 1559  CB  LEU B 508      828   1625   1490     36   -192   -111       C  
ATOM   1560  CG  LEU B 508      26.302  -7.028 -23.773  1.00 12.30           C  
ANISOU 1560  CG  LEU B 508     1086   1849   1737     39   -189    -97       C  
ATOM   1561  CD1 LEU B 508      27.121  -6.244 -24.778  1.00 11.39           C  
ANISOU 1561  CD1 LEU B 508      972   1711   1645     11   -185    -89       C  
ATOM   1562  CD2 LEU B 508      25.056  -7.616 -24.426  1.00 16.47           C  
ANISOU 1562  CD2 LEU B 508     1616   2399   2245     44   -181    -70       C  
ATOM   1563  N   LEU B 509      28.003  -9.849 -20.474  1.00 10.55           N  
ANISOU 1563  N   LEU B 509      816   1700   1492     66   -213   -129       N  
ATOM   1564  CA  LEU B 509      28.861 -10.886 -19.912  1.00 11.04           C  
ANISOU 1564  CA  LEU B 509      854   1783   1558     69   -215   -121       C  
ATOM   1565  C   LEU B 509      28.044 -12.022 -19.297  1.00 10.93           C  
ANISOU 1565  C   LEU B 509      832   1791   1529     90   -213    -99       C  
ATOM   1566  O   LEU B 509      28.512 -13.156 -19.221  1.00 14.69           O  
ANISOU 1566  O   LEU B 509     1291   2273   2018     93   -206    -81       O  
ATOM   1567  CB  LEU B 509      29.813 -10.290 -18.875  1.00 14.48           C  
ANISOU 1567  CB  LEU B 509     1277   2236   1991     65   -236   -140       C  
ATOM   1568  CG  LEU B 509      30.996  -9.550 -19.507  1.00 17.52           C  
ANISOU 1568  CG  LEU B 509     1657   2600   2400     37   -239   -152       C  
ATOM   1569  CD1 LEU B 509      31.959  -9.051 -18.451  1.00 21.53           C  
ANISOU 1569  CD1 LEU B 509     2147   3130   2903     26   -264   -171       C  
ATOM   1570  CD2 LEU B 509      31.717 -10.443 -20.500  1.00 18.04           C  
ANISOU 1570  CD2 LEU B 509     1706   2661   2488     29   -218   -132       C  
ATOM   1571  N   ILE B 510      26.823 -11.721 -18.862  1.00 11.12           N  
ANISOU 1571  N   ILE B 510      868   1828   1530    105   -216    -97       N  
ATOM   1572  CA  ILE B 510      25.942 -12.762 -18.332  1.00 11.12           C  
ANISOU 1572  CA  ILE B 510      857   1851   1516    121   -213    -69       C  
ATOM   1573  C   ILE B 510      25.514 -13.707 -19.461  1.00 14.27           C  
ANISOU 1573  C   ILE B 510     1261   2229   1932    106   -197    -51       C  
ATOM   1574  O   ILE B 510      25.289 -14.894 -19.236  1.00 12.89           O  
ANISOU 1574  O   ILE B 510     1075   2059   1764    108   -192    -27       O  
ATOM   1575  CB  ILE B 510      24.688 -12.168 -17.626  1.00 17.23           C  
ANISOU 1575  CB  ILE B 510     1637   2650   2258    142   -218    -69       C  
ATOM   1576  CG1 ILE B 510      25.092 -11.372 -16.383  1.00 20.55           C  
ANISOU 1576  CG1 ILE B 510     2055   3097   2656    157   -233    -95       C  
ATOM   1577  CG2 ILE B 510      23.686 -13.266 -17.226  1.00 21.29           C  
ANISOU 1577  CG2 ILE B 510     2137   3190   2760    153   -214    -31       C  
ATOM   1578  CD1 ILE B 510      23.960 -10.590 -15.783  1.00 24.03           C  
ANISOU 1578  CD1 ILE B 510     2506   3556   3067    183   -232   -106       C  
ATOM   1579  N   LEU B 511      25.423 -13.183 -20.682  1.00 12.61           N  
ANISOU 1579  N   LEU B 511     1068   1996   1729     88   -188    -61       N  
ATOM   1580  CA  LEU B 511      25.060 -14.015 -21.827  1.00 13.55           C  
ANISOU 1580  CA  LEU B 511     1193   2100   1856     68   -173    -53       C  
ATOM   1581  C   LEU B 511      26.064 -15.147 -22.066  1.00 15.86           C  
ANISOU 1581  C   LEU B 511     1477   2375   2174     61   -160    -55       C  
ATOM   1582  O   LEU B 511      25.698 -16.208 -22.558  1.00 15.48           O  
ANISOU 1582  O   LEU B 511     1433   2315   2136     51   -148    -49       O  
ATOM   1583  CB  LEU B 511      24.913 -13.167 -23.093  1.00 14.56           C  
ANISOU 1583  CB  LEU B 511     1336   2216   1979     49   -167    -62       C  
ATOM   1584  CG  LEU B 511      23.839 -12.081 -23.019  1.00 18.53           C  
ANISOU 1584  CG  LEU B 511     1847   2731   2465     59   -176    -53       C  
ATOM   1585  CD1 LEU B 511      23.636 -11.427 -24.375  1.00 19.67           C  
ANISOU 1585  CD1 LEU B 511     2000   2867   2605     38   -169    -48       C  
ATOM   1586  CD2 LEU B 511      22.540 -12.663 -22.507  1.00 20.39           C  
ANISOU 1586  CD2 LEU B 511     2075   2990   2682     70   -180    -30       C  
ATOM   1587  N   SER B 512      27.327 -14.941 -21.713  1.00 13.58           N  
ANISOU 1587  N   SER B 512     1175   2084   1900     68   -161    -64       N  
ATOM   1588  CA  SER B 512      28.290 -16.029 -21.823  1.00 13.33           C  
ANISOU 1588  CA  SER B 512     1129   2037   1897     71   -146    -60       C  
ATOM   1589  C   SER B 512      27.965 -17.159 -20.855  1.00 14.19           C  
ANISOU 1589  C   SER B 512     1225   2152   2016     89   -149    -32       C  
ATOM   1590  O   SER B 512      28.148 -18.332 -21.183  1.00 14.98           O  
ANISOU 1590  O   SER B 512     1321   2226   2143     89   -131    -24       O  
ATOM   1591  CB  SER B 512      29.710 -15.527 -21.579  1.00 22.39           C  
ANISOU 1591  CB  SER B 512     2258   3191   3057     74   -149    -67       C  
ATOM   1592  OG  SER B 512      30.295 -15.122 -22.797  1.00 36.64           O  
ANISOU 1592  OG  SER B 512     4070   4981   4870     56   -133    -85       O  
ATOM   1593  N   HIS B 513      27.492 -16.805 -19.663  1.00 14.08           N  
ANISOU 1593  N   HIS B 513     1201   2171   1979    104   -169    -16       N  
ATOM   1594  CA  HIS B 513      27.092 -17.811 -18.690  1.00 14.15           C  
ANISOU 1594  CA  HIS B 513     1192   2194   1992    120   -173     20       C  
ATOM   1595  C   HIS B 513      25.851 -18.562 -19.169  1.00 11.53           C  
ANISOU 1595  C   HIS B 513      874   1845   1664    107   -164     33       C  
ATOM   1596  O   HIS B 513      25.733 -19.768 -18.971  1.00 11.82           O  
ANISOU 1596  O   HIS B 513      901   1864   1725    109   -156     60       O  
ATOM   1597  CB  HIS B 513      26.833 -17.182 -17.317  1.00 13.17           C  
ANISOU 1597  CB  HIS B 513     1052   2119   1832    137   -195     31       C  
ATOM   1598  CG  HIS B 513      26.495 -18.183 -16.255  1.00 16.17           C  
ANISOU 1598  CG  HIS B 513     1409   2525   2212    154   -200     77       C  
ATOM   1599  ND1 HIS B 513      25.254 -18.249 -15.659  0.46 17.71           N  
ANISOU 1599  ND1 HIS B 513     1601   2748   2378    160   -205     99       N  
ATOM   1600  CD2 HIS B 513      27.229 -19.181 -15.705  0.92 21.94           C  
ANISOU 1600  CD2 HIS B 513     2111   3256   2967    167   -197    113       C  
ATOM   1601  CE1 HIS B 513      25.243 -19.230 -14.772  1.00 21.83           C  
ANISOU 1601  CE1 HIS B 513     2096   3290   2906    173   -207    147       C  
ATOM   1602  NE2 HIS B 513      26.430 -19.811 -14.782  0.75 20.71           N  
ANISOU 1602  NE2 HIS B 513     1939   3131   2799    178   -203    157       N  
ATOM   1603  N   ILE B 514      24.929 -17.848 -19.805  1.00 10.20           N  
ANISOU 1603  N   ILE B 514      724   1680   1470     92   -166     18       N  
ATOM   1604  CA  ILE B 514      23.710 -18.471 -20.316  1.00 10.61           C  
ANISOU 1604  CA  ILE B 514      785   1725   1520     73   -162     31       C  
ATOM   1605  C   ILE B 514      24.035 -19.448 -21.454  1.00  9.41           C  
ANISOU 1605  C   ILE B 514      648   1529   1400     49   -143     14       C  
ATOM   1606  O   ILE B 514      23.437 -20.520 -21.553  1.00 14.14           O  
ANISOU 1606  O   ILE B 514     1248   2109   2016     34   -137     29       O  
ATOM   1607  CB  ILE B 514      22.710 -17.399 -20.775  1.00 17.45           C  
ANISOU 1607  CB  ILE B 514     1663   2613   2354     66   -170     22       C  
ATOM   1608  CG1 ILE B 514      22.145 -16.667 -19.549  1.00 15.16           C  
ANISOU 1608  CG1 ILE B 514     1360   2364   2035     94   -184     38       C  
ATOM   1609  CG2 ILE B 514      21.589 -18.006 -21.605  1.00 22.69           C  
ANISOU 1609  CG2 ILE B 514     2335   3272   3015     37   -167     32       C  
ATOM   1610  CD1 ILE B 514      21.302 -15.467 -19.888  1.00 17.71           C  
ANISOU 1610  CD1 ILE B 514     1692   2703   2332     98   -188     31       C  
ATOM   1611  N   ARG B 515      25.000 -19.094 -22.297  1.00 10.70           N  
ANISOU 1611  N   ARG B 515      820   1673   1571     44   -130    -17       N  
ATOM   1612  CA  ARG B 515      25.466 -20.028 -23.311  1.00 12.96           C  
ANISOU 1612  CA  ARG B 515     1119   1919   1884     27   -106    -40       C  
ATOM   1613  C   ARG B 515      26.053 -21.282 -22.676  1.00 13.27           C  
ANISOU 1613  C   ARG B 515     1146   1929   1969     45    -94    -21       C  
ATOM   1614  O   ARG B 515      25.794 -22.396 -23.130  1.00 12.68           O  
ANISOU 1614  O   ARG B 515     1083   1815   1922     31    -79    -27       O  
ATOM   1615  CB  ARG B 515      26.518 -19.400 -24.219  1.00 16.67           C  
ANISOU 1615  CB  ARG B 515     1596   2386   2353     24    -92    -72       C  
ATOM   1616  CG  ARG B 515      27.093 -20.410 -25.198  1.00 16.32           C  
ANISOU 1616  CG  ARG B 515     1563   2303   2335     13    -62   -100       C  
ATOM   1617  CD  ARG B 515      26.350 -20.356 -26.516  1.00 24.53           C  
ANISOU 1617  CD  ARG B 515     2628   3347   3347    -24    -55   -129       C  
ATOM   1618  NE  ARG B 515      26.595 -19.062 -27.130  1.00 33.06           N  
ANISOU 1618  NE  ARG B 515     3708   4458   4394    -31    -60   -137       N  
ATOM   1619  CZ  ARG B 515      26.989 -18.892 -28.383  1.00 29.33           C  
ANISOU 1619  CZ  ARG B 515     3247   3990   3906    -51    -41   -165       C  
ATOM   1620  NH1 ARG B 515      27.151 -19.935 -29.188  1.00 33.34           N  
ANISOU 1620  NH1 ARG B 515     3770   4475   4422    -65    -15   -198       N  
ATOM   1621  NH2 ARG B 515      27.212 -17.672 -28.825  1.00 25.06           N  
ANISOU 1621  NH2 ARG B 515     2703   3478   3341    -56    -47   -160       N  
ATOM   1622  N   HIS B 516      26.857 -21.099 -21.635  1.00 13.10           N  
ANISOU 1622  N   HIS B 516     1098   1923   1956     75   -102      2       N  
ATOM   1623  CA  HIS B 516      27.445 -22.236 -20.940  1.00 11.55           C  
ANISOU 1623  CA  HIS B 516      882   1703   1803     98    -92     33       C  
ATOM   1624  C   HIS B 516      26.370 -23.186 -20.421  1.00 12.41           C  
ANISOU 1624  C   HIS B 516      990   1801   1926     91    -97     68       C  
ATOM   1625  O   HIS B 516      26.463 -24.404 -20.594  1.00 13.75           O  
ANISOU 1625  O   HIS B 516     1162   1920   2142     90    -79     78       O  
ATOM   1626  CB  HIS B 516      28.323 -21.770 -19.782  1.00 11.56           C  
ANISOU 1626  CB  HIS B 516      850   1743   1799    128   -108     60       C  
ATOM   1627  CG  HIS B 516      28.999 -22.891 -19.058  1.00 20.51           C  
ANISOU 1627  CG  HIS B 516     1955   2860   2977    155    -99    102       C  
ATOM   1628  ND1 HIS B 516      29.956 -23.684 -19.651  1.00 26.92           N  
ANISOU 1628  ND1 HIS B 516     2763   3626   3839    167    -70     95       N  
ATOM   1629  CD2 HIS B 516      28.841 -23.367 -17.801  1.00 32.54           C  
ANISOU 1629  CD2 HIS B 516     3450   4409   4504    174   -113    157       C  
ATOM   1630  CE1 HIS B 516      30.376 -24.589 -18.783  1.00 28.66           C  
ANISOU 1630  CE1 HIS B 516     2953   3839   4097    195    -67    147       C  
ATOM   1631  NE2 HIS B 516      29.715 -24.419 -17.653  1.00 33.54           N  
ANISOU 1631  NE2 HIS B 516     3555   4502   4686    198    -94    187       N  
ATOM   1632  N   MET B 517      25.339 -22.626 -19.798  1.00 10.34           N  
ANISOU 1632  N   MET B 517      723   1582   1624     86   -120     88       N  
ATOM   1633  CA  MET B 517      24.258 -23.443 -19.265  1.00 10.53           C  
ANISOU 1633  CA  MET B 517      740   1605   1655     77   -126    128       C  
ATOM   1634  C   MET B 517      23.537 -24.200 -20.371  1.00 10.69           C  
ANISOU 1634  C   MET B 517      787   1579   1696     38   -114    107       C  
ATOM   1635  O   MET B 517      23.162 -25.360 -20.194  1.00 11.05           O  
ANISOU 1635  O   MET B 517      830   1588   1779     27   -107    133       O  
ATOM   1636  CB  MET B 517      23.269 -22.585 -18.485  1.00 10.33           C  
ANISOU 1636  CB  MET B 517      703   1643   1578     81   -149    150       C  
ATOM   1637  CG  MET B 517      23.880 -21.928 -17.265  1.00 15.36           C  
ANISOU 1637  CG  MET B 517     1316   2331   2191    116   -163    167       C  
ATOM   1638  SD  MET B 517      22.624 -21.209 -16.210  1.00 16.24           S  
ANISOU 1638  SD  MET B 517     1412   2515   2245    126   -182    194       S  
ATOM   1639  CE  MET B 517      22.177 -19.752 -17.155  1.00 17.81           C  
ANISOU 1639  CE  MET B 517     1639   2719   2409    115   -185    140       C  
ATOM   1640  N   SER B 518      23.357 -23.546 -21.513  1.00 11.60           N  
ANISOU 1640  N   SER B 518      926   1696   1785     15   -111     60       N  
ATOM   1641  CA  SER B 518      22.668 -24.169 -22.633  1.00 19.03           C  
ANISOU 1641  CA  SER B 518     1893   2605   2733    -28   -102     32       C  
ATOM   1642  C   SER B 518      23.475 -25.342 -23.169  1.00 12.01           C  
ANISOU 1642  C   SER B 518     1018   1645   1898    -31    -74      7       C  
ATOM   1643  O   SER B 518      22.925 -26.400 -23.458  1.00 12.97           O  
ANISOU 1643  O   SER B 518     1153   1724   2050    -59    -67      5       O  
ATOM   1644  CB  SER B 518      22.410 -23.158 -23.745  1.00 10.70           C  
ANISOU 1644  CB  SER B 518      857   1577   1633    -50   -106     -8       C  
ATOM   1645  OG  SER B 518      21.911 -23.801 -24.910  1.00 12.08           O  
ANISOU 1645  OG  SER B 518     1055   1726   1809    -95    -97    -41       O  
ATOM   1646  N   ASN B 519      24.785 -25.149 -23.289  1.00 13.48           N  
ANISOU 1646  N   ASN B 519     1202   1820   2100     -1    -56    -12       N  
ATOM   1647  CA  ASN B 519      25.662 -26.206 -23.769  1.00 12.67           C  
ANISOU 1647  CA  ASN B 519     1110   1652   2053      7    -23    -36       C  
ATOM   1648  C   ASN B 519      25.574 -27.431 -22.861  1.00 12.38           C  
ANISOU 1648  C   ASN B 519     1059   1570   2074     22    -19     12       C  
ATOM   1649  O   ASN B 519      25.511 -28.563 -23.340  1.00 17.06           O  
ANISOU 1649  O   ASN B 519     1671   2094   2715      7      3     -6       O  
ATOM   1650  CB  ASN B 519      27.108 -25.711 -23.868  1.00 18.42           C  
ANISOU 1650  CB  ASN B 519     1825   2387   2786     43     -6    -50       C  
ATOM   1651  CG  ASN B 519      27.279 -24.596 -24.899  1.00 22.51           C  
ANISOU 1651  CG  ASN B 519     2358   2941   3255     26     -6    -95       C  
ATOM   1652  OD1 ASN B 519      26.455 -24.427 -25.799  1.00 36.23           O  
ANISOU 1652  OD1 ASN B 519     4120   4686   4960    -12     -9   -125       O  
ATOM   1653  ND2 ASN B 519      28.360 -23.838 -24.774  1.00 15.10           N  
ANISOU 1653  ND2 ASN B 519     1400   2027   2309     52     -3    -94       N  
ATOM   1654  N   LYS B 520      25.541 -27.205 -21.551  1.00 13.10           N  
ANISOU 1654  N   LYS B 520     1116   1699   2160     49    -39     74       N  
ATOM   1655  CA  LYS B 520      25.413 -28.312 -20.604  1.00 17.00           C  
ANISOU 1655  CA  LYS B 520     1590   2162   2707     62    -38    134       C  
ATOM   1656  C   LYS B 520      24.045 -28.976 -20.720  1.00 16.33           C  
ANISOU 1656  C   LYS B 520     1520   2056   2630     18    -47    146       C  
ATOM   1657  O   LYS B 520      23.924 -30.199 -20.620  1.00 17.17           O  
ANISOU 1657  O   LYS B 520     1630   2097   2799     11    -33    168       O  
ATOM   1658  CB  LYS B 520      25.652 -27.832 -19.170  1.00 13.97           C  
ANISOU 1658  CB  LYS B 520     1164   1843   2302     98    -61    198       C  
ATOM   1659  CG  LYS B 520      27.102 -27.462 -18.882  1.00 19.73           C  
ANISOU 1659  CG  LYS B 520     1870   2587   3038    140    -53    199       C  
ATOM   1660  CD  LYS B 520      27.948 -28.729 -18.752  1.00 23.95           C  
ANISOU 1660  CD  LYS B 520     2392   3056   3652    168    -25    229       C  
ATOM   1661  CE  LYS B 520      29.242 -28.503 -17.976  1.00 29.60           C  
ANISOU 1661  CE  LYS B 520     3064   3806   4375    215    -27    266       C  
ATOM   1662  NZ  LYS B 520      29.020 -27.935 -16.617  1.00 36.07           N  
ANISOU 1662  NZ  LYS B 520     3848   4710   5148    226    -62    322       N  
ATOM   1663  N   GLY B 521      23.013 -28.166 -20.932  1.00 16.35           N  
ANISOU 1663  N   GLY B 521     1528   2111   2572    -12    -70    136       N  
ATOM   1664  CA  GLY B 521      21.672 -28.688 -21.119  1.00 15.39           C  
ANISOU 1664  CA  GLY B 521     1414   1982   2451    -59    -82    148       C  
ATOM   1665  C   GLY B 521      21.566 -29.494 -22.400  1.00 14.55           C  
ANISOU 1665  C   GLY B 521     1348   1806   2376   -102    -63     88       C  
ATOM   1666  O   GLY B 521      20.951 -30.560 -22.421  1.00 15.66           O  
ANISOU 1666  O   GLY B 521     1496   1895   2560   -135    -61    102       O  
ATOM   1667  N   MET B 522      22.174 -28.988 -23.470  1.00 13.97           N  
ANISOU 1667  N   MET B 522     1299   1730   2280   -104    -48     21       N  
ATOM   1668  CA  MET B 522      22.150 -29.683 -24.752  1.00 18.73           C  
ANISOU 1668  CA  MET B 522     1941   2275   2900   -145    -27    -47       C  
ATOM   1669  C   MET B 522      22.898 -31.002 -24.662  1.00 16.58           C  
ANISOU 1669  C   MET B 522     1679   1907   2712   -127      6    -52       C  
ATOM   1670  O   MET B 522      22.494 -31.991 -25.272  1.00 19.05           O  
ANISOU 1670  O   MET B 522     2021   2154   3062   -168     18    -87       O  
ATOM   1671  CB  MET B 522      22.740 -28.811 -25.867  1.00 17.50           C  
ANISOU 1671  CB  MET B 522     1803   2148   2696   -145    -16   -111       C  
ATOM   1672  CG  MET B 522      21.889 -27.601 -26.234  1.00 19.98           C  
ANISOU 1672  CG  MET B 522     2114   2545   2934   -170    -45   -112       C  
ATOM   1673  SD  MET B 522      20.277 -28.047 -26.916  1.00 19.94           S  
ANISOU 1673  SD  MET B 522     2123   2549   2904   -247    -67   -123       S  
ATOM   1674  CE  MET B 522      20.761 -29.139 -28.245  1.00 27.49           C  
ANISOU 1674  CE  MET B 522     3126   3430   3889   -284    -33   -211       C  
ATOM   1675  N   GLU B 523      23.991 -31.016 -23.901  1.00 16.28           N  
ANISOU 1675  N   GLU B 523     1617   1861   2708    -68     20    -18       N  
ATOM   1676  CA  GLU B 523      24.716 -32.258 -23.666  1.00 19.58           C  
ANISOU 1676  CA  GLU B 523     2037   2189   3214    -40     52     -6       C  
ATOM   1677  C   GLU B 523      23.806 -33.334 -23.094  1.00 19.93           C  
ANISOU 1677  C   GLU B 523     2079   2183   3311    -69     43     42       C  
ATOM   1678  O   GLU B 523      23.869 -34.494 -23.509  1.00 21.58           O  
ANISOU 1678  O   GLU B 523     2315   2296   3590    -83     69     17       O  
ATOM   1679  CB  GLU B 523      25.907 -32.043 -22.727  1.00 19.57           C  
ANISOU 1679  CB  GLU B 523     1996   2206   3235     28     59     46       C  
ATOM   1680  CG  GLU B 523      27.086 -31.334 -23.361  1.00 25.48           C  
ANISOU 1680  CG  GLU B 523     2746   2977   3960     59     80     -2       C  
ATOM   1681  CD  GLU B 523      28.013 -30.726 -22.328  1.00 29.46           C  
ANISOU 1681  CD  GLU B 523     3203   3534   4457    112     69     55       C  
ATOM   1682  OE1 GLU B 523      28.102 -31.274 -21.210  1.00 31.07           O  
ANISOU 1682  OE1 GLU B 523     3375   3731   4700    139     62    128       O  
ATOM   1683  OE2 GLU B 523      28.648 -29.696 -22.634  1.00 37.26           O  
ANISOU 1683  OE2 GLU B 523     4184   4574   5399    124     67     28       O  
ATOM   1684  N   HIS B 524      22.956 -32.959 -22.143  1.00 18.83           N  
ANISOU 1684  N   HIS B 524     1909   2104   3140    -77      8    111       N  
ATOM   1685  CA  HIS B 524      22.061 -33.946 -21.561  1.00 18.00           C  
ANISOU 1685  CA  HIS B 524     1795   1959   3083   -107     -2    167       C  
ATOM   1686  C   HIS B 524      21.010 -34.411 -22.552  1.00 16.86           C  
ANISOU 1686  C   HIS B 524     1689   1780   2938   -182     -8    114       C  
ATOM   1687  O   HIS B 524      20.741 -35.605 -22.650  1.00 20.88           O  
ANISOU 1687  O   HIS B 524     2214   2200   3518   -212      5    117       O  
ATOM   1688  CB  HIS B 524      21.357 -33.427 -20.312  1.00 17.56           C  
ANISOU 1688  CB  HIS B 524     1694   1989   2987    -98    -36    254       C  
ATOM   1689  CG  HIS B 524      20.441 -34.441 -19.705  1.00 22.38           C  
ANISOU 1689  CG  HIS B 524     2292   2566   3647   -130    -45    320       C  
ATOM   1690  ND1 HIS B 524      20.905 -35.571 -19.067  1.00 23.99           N  
ANISOU 1690  ND1 HIS B 524     2482   2695   3938   -108    -27    378       N  
ATOM   1691  CD2 HIS B 524      19.089 -34.523 -19.679  1.00 20.20           C  
ANISOU 1691  CD2 HIS B 524     2010   2316   3349   -186    -70    343       C  
ATOM   1692  CE1 HIS B 524      19.881 -36.294 -18.653  1.00 22.75           C  
ANISOU 1692  CE1 HIS B 524     2313   2519   3812   -150    -41    434       C  
ATOM   1693  NE2 HIS B 524      18.767 -35.680 -19.013  1.00 24.03           N  
ANISOU 1693  NE2 HIS B 524     2479   2744   3907   -199    -67    413       N  
ATOM   1694  N   LEU B 525      20.405 -33.471 -23.272  1.00 14.74           N  
ANISOU 1694  N   LEU B 525     1432   1580   2590   -216    -27     69       N  
ATOM   1695  CA  LEU B 525      19.346 -33.816 -24.215  1.00 15.09           C  
ANISOU 1695  CA  LEU B 525     1504   1609   2619   -293    -39     23       C  
ATOM   1696  C   LEU B 525      19.831 -34.816 -25.266  1.00 19.79           C  
ANISOU 1696  C   LEU B 525     2149   2102   3269   -318     -5    -59       C  
ATOM   1697  O   LEU B 525      19.134 -35.781 -25.585  1.00 18.12           O  
ANISOU 1697  O   LEU B 525     1958   1828   3098   -376     -7    -75       O  
ATOM   1698  CB  LEU B 525      18.791 -32.557 -24.886  1.00 15.14           C  
ANISOU 1698  CB  LEU B 525     1511   1712   2529   -316    -62     -9       C  
ATOM   1699  CG  LEU B 525      18.026 -31.605 -23.960  1.00 15.74           C  
ANISOU 1699  CG  LEU B 525     1543   1885   2551   -301    -95     64       C  
ATOM   1700  CD1 LEU B 525      17.574 -30.357 -24.704  1.00 17.36           C  
ANISOU 1700  CD1 LEU B 525     1751   2175   2672   -317   -113     31       C  
ATOM   1701  CD2 LEU B 525      16.836 -32.334 -23.356  1.00 16.82           C  
ANISOU 1701  CD2 LEU B 525     1659   2019   2712   -344   -116    125       C  
ATOM   1702  N   TYR B 526      21.032 -34.591 -25.787  1.00 21.68           N  
ANISOU 1702  N   TYR B 526     2405   2324   3510   -274     27   -113       N  
ATOM   1703  CA  TYR B 526      21.625 -35.519 -26.741  1.00 21.03           C  
ANISOU 1703  CA  TYR B 526     2368   2145   3478   -285     67   -195       C  
ATOM   1704  C   TYR B 526      21.917 -36.870 -26.101  1.00 19.17           C  
ANISOU 1704  C   TYR B 526     2134   1794   3354   -267     92   -159       C  
ATOM   1705  O   TYR B 526      21.787 -37.907 -26.750  1.00 22.49           O  
ANISOU 1705  O   TYR B 526     2595   2120   3830   -304    114   -217       O  
ATOM   1706  CB  TYR B 526      22.906 -34.937 -27.345  1.00 18.88           C  
ANISOU 1706  CB  TYR B 526     2103   1888   3182   -233    100   -249       C  
ATOM   1707  CG  TYR B 526      22.645 -33.923 -28.430  1.00 19.37           C  
ANISOU 1707  CG  TYR B 526     2180   2031   3147   -267     88   -311       C  
ATOM   1708  CD1 TYR B 526      21.958 -34.284 -29.579  1.00 24.53           C  
ANISOU 1708  CD1 TYR B 526     2874   2673   3774   -338     87   -387       C  
ATOM   1709  CD2 TYR B 526      23.097 -32.615 -28.319  1.00 21.88           C  
ANISOU 1709  CD2 TYR B 526     2473   2438   3402   -231     77   -292       C  
ATOM   1710  CE1 TYR B 526      21.713 -33.373 -30.583  1.00 25.65           C  
ANISOU 1710  CE1 TYR B 526     3025   2896   3825   -369     75   -435       C  
ATOM   1711  CE2 TYR B 526      22.859 -31.692 -29.324  1.00 20.88           C  
ANISOU 1711  CE2 TYR B 526     2357   2383   3192   -261     67   -339       C  
ATOM   1712  CZ  TYR B 526      22.166 -32.080 -30.453  1.00 25.37           C  
ANISOU 1712  CZ  TYR B 526     2961   2945   3732   -328     66   -407       C  
ATOM   1713  OH  TYR B 526      21.922 -31.175 -31.460  1.00 33.71           O  
ANISOU 1713  OH  TYR B 526     4025   4080   4703   -358     55   -446       O  
ATOM   1714  N   SER B 527      22.297 -36.859 -24.826  1.00 20.40           N  
ANISOU 1714  N   SER B 527     2246   1960   3544   -211     87    -64       N  
ATOM   1715  CA  SER B 527      22.607 -38.101 -24.120  1.00 21.47           C  
ANISOU 1715  CA  SER B 527     2375   1993   3789   -187    109    -11       C  
ATOM   1716  C   SER B 527      21.385 -39.007 -23.986  1.00 21.97           C  
ANISOU 1716  C   SER B 527     2449   2002   3896   -258     90     13       C  
ATOM   1717  O   SER B 527      21.515 -40.223 -23.836  1.00 22.11           O  
ANISOU 1717  O   SER B 527     2481   1906   4015   -260    114     26       O  
ATOM   1718  CB  SER B 527      23.180 -37.799 -22.732  1.00 26.89           C  
ANISOU 1718  CB  SER B 527     3004   2726   4488   -118    101     96       C  
ATOM   1719  OG  SER B 527      22.148 -37.506 -21.804  1.00 27.49           O  
ANISOU 1719  OG  SER B 527     3044   2870   4530   -142     59    178       O  
ATOM   1720  N   MET B 528      20.200 -38.410 -24.039  1.00 20.46           N  
ANISOU 1720  N   MET B 528     2249   1894   3632   -315     48     23       N  
ATOM   1721  CA  MET B 528      18.968 -39.163 -23.847  1.00 20.05           C  
ANISOU 1721  CA  MET B 528     2197   1809   3613   -388     24     58       C  
ATOM   1722  C   MET B 528      18.676 -40.113 -25.001  1.00 22.10           C  
ANISOU 1722  C   MET B 528     2514   1967   3916   -457     41    -38       C  
ATOM   1723  O   MET B 528      17.971 -41.103 -24.820  1.00 24.29           O  
ANISOU 1723  O   MET B 528     2799   2171   4259   -510     34    -13       O  
ATOM   1724  CB  MET B 528      17.788 -38.212 -23.655  1.00 19.56           C  
ANISOU 1724  CB  MET B 528     2105   1872   3457   -428    -23     93       C  
ATOM   1725  CG  MET B 528      17.924 -37.296 -22.460  1.00 20.45           C  
ANISOU 1725  CG  MET B 528     2162   2085   3524   -366    -40    183       C  
ATOM   1726  SD  MET B 528      16.542 -36.154 -22.351  1.00 22.10           S  
ANISOU 1726  SD  MET B 528     2339   2433   3625   -406    -88    212       S  
ATOM   1727  CE  MET B 528      15.172 -37.285 -22.104  1.00 24.63           C  
ANISOU 1727  CE  MET B 528     2648   2711   3998   -490   -109    266       C  
ATOM   1728  N   LYS B 529      19.192 -39.802 -26.175  1.00 24.17           N  
ANISOU 1728  N   LYS B 529     4192   1261   3731    264    461   -510       N  
ATOM   1729  CA  LYS B 529      18.962 -40.608 -27.399  1.00 26.60           C  
ANISOU 1729  CA  LYS B 529     4606   1411   4090    103    349   -757       C  
ATOM   1730  C   LYS B 529      17.469 -40.772 -27.621  1.00 28.00           C  
ANISOU 1730  C   LYS B 529     4832   1403   4404   -157    322   -650       C  
ATOM   1731  O   LYS B 529      17.038 -41.849 -27.941  1.00 30.54           O  
ANISOU 1731  O   LYS B 529     5197   1520   4888   -315    206   -727       O  
ATOM   1732  CB  LYS B 529      19.699 -41.946 -27.386  1.00 28.87           C  
ANISOU 1732  CB  LYS B 529     4911   1542   4517    171    230   -892       C  
ATOM   1733  CG  LYS B 529      21.185 -41.810 -27.631  1.00 31.08           C  
ANISOU 1733  CG  LYS B 529     5104   2035   4672    346    199  -1086       C  
ATOM   1734  CD  LYS B 529      21.956 -42.844 -26.881  1.00 33.00           C  
ANISOU 1734  CD  LYS B 529     5314   2169   5055    468    120  -1087       C  
ATOM   1735  CE  LYS B 529      21.452 -44.259 -27.116  1.00 35.56           C  
ANISOU 1735  CE  LYS B 529     5782   2182   5546    371     -6  -1123       C  
ATOM   1736  NZ  LYS B 529      21.339 -44.638 -28.550  1.00 41.20           N  
ANISOU 1736  NZ  LYS B 529     6609   2887   6158    283   -105  -1364       N  
ATOM   1737  N   SER B 530      16.747 -39.678 -27.456  1.00 30.00           N  
ATOM   1738  CA  SER B 530      15.288 -39.612 -27.643  1.00 30.00           C  
ATOM   1739  C   SER B 530      15.032 -38.808 -28.905  1.00 30.00           C  
ATOM   1740  O   SER B 530      15.499 -37.695 -29.007  1.00 30.00           O  
ATOM   1741  CB  SER B 530      14.596 -38.980 -26.465  1.00 30.00           C  
ATOM   1742  OG  SER B 530      14.582 -39.804 -25.303  1.00 30.00           O  
ATOM   1743  N   LYS B 531      14.308 -39.397 -29.838  1.00 29.64           N  
ANISOU 1743  N   LYS B 531     4771   2088   4402   -770     15   -533       N  
ATOM   1744  CA  LYS B 531      13.954 -38.681 -31.091  1.00 32.69           C  
ANISOU 1744  CA  LYS B 531     5118   2718   4586   -911    -89   -633       C  
ATOM   1745  C   LYS B 531      13.130 -37.434 -30.762  1.00 32.65           C  
ANISOU 1745  C   LYS B 531     4940   2943   4522   -898    -81   -340       C  
ATOM   1746  O   LYS B 531      12.287 -37.484 -29.888  1.00 36.95           O  
ANISOU 1746  O   LYS B 531     5379   3431   5230   -877    -39    -89       O  
ATOM   1747  CB  LYS B 531      13.187 -39.587 -32.066  1.00 34.74           C  
ANISOU 1747  CB  LYS B 531     5392   2882   4926  -1176   -249   -774       C  
ATOM   1748  N   ASN B 532      13.438 -36.328 -31.421  1.00 36.36           N  
ANISOU 1748  N   ASN B 532     5385   3672   4757   -901   -116   -379       N  
ATOM   1749  CA  ASN B 532      12.669 -35.067 -31.238  1.00 34.11           C  
ANISOU 1749  CA  ASN B 532     4941   3618   4400   -892   -140   -138       C  
ATOM   1750  C   ASN B 532      12.767 -34.468 -29.819  1.00 35.35           C  
ANISOU 1750  C   ASN B 532     4996   3805   4628   -685      1    117       C  
ATOM   1751  O   ASN B 532      11.970 -33.620 -29.513  1.00 33.76           O  
ANISOU 1751  O   ASN B 532     4637   3761   4430   -690    -28    325       O  
ATOM   1752  CB  ASN B 532      11.239 -35.165 -31.788  1.00 35.90           C  
ANISOU 1752  CB  ASN B 532     5044   3872   4726  -1129   -299    -39       C  
ATOM   1753  N   VAL B 533      13.702 -34.893 -28.980  1.00 27.82           N  
ANISOU 1753  N   VAL B 533     4124   2717   3729   -499    149     92       N  
ATOM   1754  CA  VAL B 533      13.906 -34.161 -27.721  1.00 24.59           C  
ANISOU 1754  CA  VAL B 533     3624   2374   3346   -293    291    307       C  
ATOM   1755  C   VAL B 533      14.897 -33.020 -27.966  1.00 23.09           C  
ANISOU 1755  C   VAL B 533     3475   2374   2923   -131    361    234       C  
ATOM   1756  O   VAL B 533      15.063 -32.116 -27.145  1.00 21.64           O  
ANISOU 1756  O   VAL B 533     3206   2305   2712     33    462    392       O  
ATOM   1757  CB  VAL B 533      14.411 -35.071 -26.583  1.00 25.45           C  
ANISOU 1757  CB  VAL B 533     3788   2257   3627   -170    414    353       C  
ATOM   1758  CG1 VAL B 533      15.910 -35.328 -26.719  1.00 22.78           C  
ANISOU 1758  CG1 VAL B 533     3622   1843   3192     -5    503    124       C  
ATOM   1759  CG2 VAL B 533      14.074 -34.460 -25.222  1.00 24.80           C  
ANISOU 1759  CG2 VAL B 533     3552   2250   3619    -39    527    634       C  
ATOM   1760  N   VAL B 534      15.573 -33.089 -29.104  1.00 22.22           N  
ANISOU 1760  N   VAL B 534     3497   2301   2643   -187    310    -19       N  
ATOM   1761  CA  VAL B 534      16.238 -31.931 -29.674  1.00 20.95           C  
ANISOU 1761  CA  VAL B 534     3366   2362   2231   -121    325    -86       C  
ATOM   1762  C   VAL B 534      15.488 -31.645 -30.963  1.00 22.76           C  
ANISOU 1762  C   VAL B 534     3579   2723   2346   -348    142   -137       C  
ATOM   1763  O   VAL B 534      15.349 -32.534 -31.802  1.00 24.19           O  
ANISOU 1763  O   VAL B 534     3835   2820   2536   -514     49   -318       O  
ATOM   1764  CB  VAL B 534      17.738 -32.171 -29.957  1.00 25.26           C  
ANISOU 1764  CB  VAL B 534     4076   2885   2638     -5    423   -350       C  
ATOM   1765  CG1 VAL B 534      18.343 -30.960 -30.664  1.00 23.41           C  
ANISOU 1765  CG1 VAL B 534     3872   2898   2125     15    424   -418       C  
ATOM   1766  CG2 VAL B 534      18.497 -32.489 -28.670  1.00 22.62           C  
ANISOU 1766  CG2 VAL B 534     3758   2417   2421    226    594   -301       C  
ATOM   1767  N   PRO B 535      14.965 -30.421 -31.121  1.00 18.85           N  
ANISOU 1767  N   PRO B 535     2982   2428   1752   -358     81     24       N  
ATOM   1768  CA  PRO B 535      14.220 -30.163 -32.356  1.00 22.99           C  
ANISOU 1768  CA  PRO B 535     3491   3078   2166   -577   -110    -10       C  
ATOM   1769  C   PRO B 535      15.117 -30.231 -33.587  1.00 23.92           C  
ANISOU 1769  C   PRO B 535     3770   3277   2040   -663   -146   -283       C  
ATOM   1770  O   PRO B 535      16.188 -29.624 -33.609  1.00 22.75           O  
ANISOU 1770  O   PRO B 535     3701   3223   1720   -542    -49   -362       O  
ATOM   1771  CB  PRO B 535      13.668 -28.751 -32.144  1.00 23.92           C  
ANISOU 1771  CB  PRO B 535     3477   3381   2231   -522   -156    220       C  
ATOM   1772  CG  PRO B 535      14.633 -28.118 -31.198  1.00 24.41           C  
ANISOU 1772  CG  PRO B 535     3552   3463   2259   -276     25    271       C  
ATOM   1773  CD  PRO B 535      15.058 -29.225 -30.270  1.00 19.23           C  
ANISOU 1773  CD  PRO B 535     2931   2598   1777   -176    168    225       C  
ATOM   1774  N   SER B 536      14.684 -30.983 -34.594  1.00 23.56           N  
ANISOU 1774  N   SER B 536     3767   3207   1979   -879   -279   -437       N  
ATOM   1775  CA  SER B 536      15.471 -31.154 -35.808  1.00 27.17           C  
ANISOU 1775  CA  SER B 536     4365   3755   2204   -988   -317   -721       C  
ATOM   1776  C   SER B 536      15.478 -29.872 -36.627  1.00 26.85           C  
ANISOU 1776  C   SER B 536     4235   3924   2042   -951   -372   -603       C  
ATOM   1777  O   SER B 536      14.652 -28.986 -36.409  1.00 23.81           O  
ANISOU 1777  O   SER B 536     3770   3638   1637   -987   -455   -388       O  
ATOM   1778  CB  SER B 536      14.923 -32.307 -36.652  1.00 28.70           C  
ANISOU 1778  CB  SER B 536     4588   3856   2459  -1210   -442   -901       C  
ATOM   1779  OG  SER B 536      13.654 -31.981 -37.192  1.00 29.87           O  
ANISOU 1779  OG  SER B 536     4632   4106   2613  -1393   -620   -758       O  
ATOM   1780  N   TYR B 537      16.416 -29.777 -37.563  1.00 26.47           N  
ANISOU 1780  N   TYR B 537     4179   3908   1970   -851   -333   -720       N  
ATOM   1781  CA  TYR B 537      16.435 -28.667 -38.505  1.00 26.32           C  
ANISOU 1781  CA  TYR B 537     4099   4014   1886   -831   -385   -630       C  
ATOM   1782  C   TYR B 537      15.102 -28.591 -39.248  1.00 27.03           C  
ANISOU 1782  C   TYR B 537     4157   4181   1931  -1055   -549   -562       C  
ATOM   1783  O   TYR B 537      14.544 -27.509 -39.432  1.00 27.53           O  
ANISOU 1783  O   TYR B 537     4156   4327   1979  -1058   -609   -391       O  
ATOM   1784  CB  TYR B 537      17.599 -28.810 -39.498  1.00 28.78           C  
ANISOU 1784  CB  TYR B 537     4434   4329   2170   -740   -350   -776       C  
ATOM   1785  CG  TYR B 537      17.670 -27.705 -40.540  1.00 31.27           C  
ANISOU 1785  CG  TYR B 537     4724   4762   2394   -801   -385   -697       C  
ATOM   1786  CD1 TYR B 537      16.822 -27.706 -41.642  1.00 33.73           C  
ANISOU 1786  CD1 TYR B 537     5030   5151   2635   -969   -508   -701       C  
ATOM   1787  CD2 TYR B 537      18.583 -26.663 -40.422  1.00 29.59           C  
ANISOU 1787  CD2 TYR B 537     4493   4584   2165   -735   -294   -622       C  
ATOM   1788  CE1 TYR B 537      16.870 -26.703 -42.589  1.00 34.81           C  
ANISOU 1788  CE1 TYR B 537     5155   5402   2671  -1068   -532   -624       C  
ATOM   1789  CE2 TYR B 537      18.642 -25.651 -41.373  1.00 32.02           C  
ANISOU 1789  CE2 TYR B 537     4784   4995   2386   -844   -324   -558       C  
ATOM   1790  CZ  TYR B 537      17.781 -25.677 -42.452  1.00 32.43           C  
ANISOU 1790  CZ  TYR B 537     4841   5127   2353  -1009   -440   -554       C  
ATOM   1791  OH  TYR B 537      17.826 -24.680 -43.403  1.00 32.65           O  
ANISOU 1791  OH  TYR B 537     4860   5258   2289  -1124   -473   -483       O  
ATOM   1792  N   ASP B 538      14.586 -29.740 -39.670  1.00 29.61           N  
ANISOU 1792  N   ASP B 538     4515   4462   2274  -1224   -629   -697       N  
ATOM   1793  CA  ASP B 538      13.387 -29.746 -40.497  1.00 30.83           C  
ANISOU 1793  CA  ASP B 538     4619   4685   2410  -1416   -793   -645       C  
ATOM   1794  C   ASP B 538      12.131 -29.412 -39.698  1.00 28.58           C  
ANISOU 1794  C   ASP B 538     4250   4410   2199  -1503   -902   -429       C  
ATOM   1795  O   ASP B 538      11.178 -28.857 -40.247  1.00 29.55           O  
ANISOU 1795  O   ASP B 538     4292   4620   2316  -1583  -1025   -300       O  
ATOM   1796  CB  ASP B 538      13.215 -31.093 -41.199  1.00 34.57           C  
ANISOU 1796  CB  ASP B 538     5128   5087   2920  -1551   -848   -861       C  
ATOM   1797  N   LEU B 539      12.126 -29.744 -38.409  1.00 27.07           N  
ANISOU 1797  N   LEU B 539     4065   4129   2092  -1480   -863   -381       N  
ATOM   1798  CA  LEU B 539      11.011 -29.354 -37.552  1.00 26.56           C  
ANISOU 1798  CA  LEU B 539     3873   4089   2130  -1533   -977   -136       C  
ATOM   1799  C   LEU B 539      10.991 -27.842 -37.411  1.00 25.09           C  
ANISOU 1799  C   LEU B 539     3608   4025   1901  -1363   -952     74       C  
ATOM   1800  O   LEU B 539       9.946 -27.212 -37.570  1.00 25.53           O  
ANISOU 1800  O   LEU B 539     3535   4143   2020  -1393  -1066    245       O  
ATOM   1801  CB  LEU B 539      11.090 -30.007 -36.173  1.00 25.81           C  
ANISOU 1801  CB  LEU B 539     3730   3782   2294  -1368   -807    -68       C  
ATOM   1802  CG  LEU B 539      10.035 -29.460 -35.204  1.00 28.56           C  
ANISOU 1802  CG  LEU B 539     3880   4135   2835  -1290   -823    222       C  
ATOM   1803  CD1 LEU B 539       8.621 -29.710 -35.731  1.00 27.00           C  
ANISOU 1803  CD1 LEU B 539     3557   3974   2727  -1498  -1016    289       C  
ATOM   1804  CD2 LEU B 539      10.202 -30.033 -33.807  1.00 23.78           C  
ANISOU 1804  CD2 LEU B 539     3233   3349   2455  -1130   -643    300       C  
ATOM   1805  N   LEU B 540      12.153 -27.267 -37.115  1.00 23.75           N  
ANISOU 1805  N   LEU B 540     3503   3852   1671  -1164   -783     40       N  
ATOM   1806  CA  LEU B 540      12.281 -25.820 -37.006  1.00 22.26           C  
ANISOU 1806  CA  LEU B 540     3238   3708   1511   -985   -730    184       C  
ATOM   1807  C   LEU B 540      11.914 -25.107 -38.305  1.00 24.52           C  
ANISOU 1807  C   LEU B 540     3508   4056   1755  -1048   -818    187       C  
ATOM   1808  O   LEU B 540      11.270 -24.058 -38.283  1.00 23.42           O  
ANISOU 1808  O   LEU B 540     3280   3942   1678   -998   -867    335       O  
ATOM   1809  CB  LEU B 540      13.702 -25.441 -36.583  1.00 20.22           C  
ANISOU 1809  CB  LEU B 540     3039   3394   1248   -760   -536     98       C  
ATOM   1810  CG  LEU B 540      14.103 -25.932 -35.196  1.00 18.62           C  
ANISOU 1810  CG  LEU B 540     2852   3128   1095   -641   -413    124       C  
ATOM   1811  CD1 LEU B 540      15.569 -25.650 -34.918  1.00 16.88           C  
ANISOU 1811  CD1 LEU B 540     2676   2831    904   -400   -236     13       C  
ATOM   1812  CD2 LEU B 540      13.230 -25.261 -34.160  1.00 17.58           C  
ANISOU 1812  CD2 LEU B 540     2575   3010   1095   -555   -427    365       C  
ATOM   1813  N   LEU B 541      12.317 -25.677 -39.434  1.00 24.41           N  
ANISOU 1813  N   LEU B 541     3577   4057   1641  -1149   -832     18       N  
ATOM   1814  CA  LEU B 541      12.005 -25.076 -40.725  1.00 25.99           C  
ANISOU 1814  CA  LEU B 541     3771   4326   1776  -1219   -915     27       C  
ATOM   1815  C   LEU B 541      10.502 -25.134 -41.001  1.00 27.72           C  
ANISOU 1815  C   LEU B 541     3909   4590   2033  -1369  -1089    143       C  
ATOM   1816  O   LEU B 541       9.920 -24.162 -41.481  1.00 28.25           O  
ANISOU 1816  O   LEU B 541     3926   4702   2105  -1364  -1161    258       O  
ATOM   1817  CB  LEU B 541      12.787 -25.764 -41.845  1.00 28.34           C  
ANISOU 1817  CB  LEU B 541     4157   4641   1969  -1281   -887   -178       C  
ATOM   1818  CG  LEU B 541      12.595 -25.215 -43.263  1.00 31.73           C  
ANISOU 1818  CG  LEU B 541     4594   5157   2306  -1364   -965   -177       C  
ATOM   1819  CD1 LEU B 541      12.583 -23.691 -43.275  1.00 31.09           C  
ANISOU 1819  CD1 LEU B 541     4478   5101   2231  -1295   -963    -11       C  
ATOM   1820  CD2 LEU B 541      13.694 -25.738 -44.168  1.00 34.78           C  
ANISOU 1820  CD2 LEU B 541     5055   5563   2597  -1381   -897   -365       C  
ATOM   1821  N   GLU B 542       9.875 -26.262 -40.674  1.00 28.68           N  
ANISOU 1821  N   GLU B 542     4010   4684   2205  -1495  -1159    107       N  
ATOM   1822  CA  GLU B 542       8.436 -26.409 -40.874  1.00 30.40           C  
ANISOU 1822  CA  GLU B 542     4123   4930   2499  -1624  -1324    210       C  
ATOM   1823  C   GLU B 542       7.653 -25.389 -40.047  1.00 29.29           C  
ANISOU 1823  C   GLU B 542     3849   4800   2481  -1519  -1359    443       C  
ATOM   1824  O   GLU B 542       6.659 -24.839 -40.517  1.00 30.54           O  
ANISOU 1824  O   GLU B 542     3927   5001   2675  -1552  -1470    542       O  
ATOM   1825  CB  GLU B 542       7.981 -27.831 -40.532  1.00 39.26           C  
ANISOU 1825  CB  GLU B 542     5228   5981   3708  -1770  -1377    117       C  
ATOM   1826  CG  GLU B 542       6.462 -28.003 -40.415  1.00 34.67           C  
ANISOU 1826  CG  GLU B 542     4495   5407   3270  -1876  -1527    246       C  
ATOM   1827  CD  GLU B 542       5.793 -28.302 -41.744  1.00 37.39           C  
ANISOU 1827  CD  GLU B 542     4841   5807   3558  -2015  -1639    160       C  
ATOM   1828  OE1 GLU B 542       6.426 -28.952 -42.606  1.00 40.79           O  
ANISOU 1828  OE1 GLU B 542     5380   6234   3884  -2081  -1607    -43       O  
ATOM   1829  OE2 GLU B 542       4.628 -27.884 -41.936  1.00 36.81           O  
ANISOU 1829  OE2 GLU B 542     4652   5785   3549  -2048  -1755    289       O  
ATOM   1830  N   MET B 543       8.106 -25.120 -38.825  1.00 27.05           N  
ANISOU 1830  N   MET B 543     3536   4474   2269  -1376  -1256    518       N  
ATOM   1831  CA  MET B 543       7.412 -24.157 -37.974  1.00 26.00           C  
ANISOU 1831  CA  MET B 543     3260   4339   2281  -1243  -1257    712       C  
ATOM   1832  C   MET B 543       7.648 -22.713 -38.410  1.00 25.39           C  
ANISOU 1832  C   MET B 543     3199   4271   2179  -1113  -1215    741       C  
ATOM   1833  O   MET B 543       6.742 -21.885 -38.335  1.00 25.78           O  
ANISOU 1833  O   MET B 543     3149   4326   2322  -1066  -1276    854       O  
ATOM   1834  CB  MET B 543       7.821 -24.320 -36.510  1.00 23.92           C  
ANISOU 1834  CB  MET B 543     2943   4029   2116  -1112  -1142    780       C  
ATOM   1835  CG  MET B 543       6.960 -25.307 -35.738  1.00 26.26           C  
ANISOU 1835  CG  MET B 543     3109   4309   2558  -1209  -1223    870       C  
ATOM   1836  SD  MET B 543       7.376 -25.404 -33.991  1.00 53.76           S  
ANISOU 1836  SD  MET B 543     6497   7752   6179  -1025  -1078   1004       S  
ATOM   1837  CE  MET B 543       9.017 -26.112 -34.075  1.00 21.31           C  
ANISOU 1837  CE  MET B 543     2630   3553   1913   -984   -907    788       C  
ATOM   1838  N   LEU B 544       8.862 -22.408 -38.856  1.00 24.56           N  
ANISOU 1838  N   LEU B 544     3216   4155   1962  -1054  -1113    626       N  
ATOM   1839  CA  LEU B 544       9.179 -21.048 -39.275  1.00 24.07           C  
ANISOU 1839  CA  LEU B 544     3172   4083   1889   -944  -1080    642       C  
ATOM   1840  C   LEU B 544       8.487 -20.671 -40.583  1.00 28.10           C  
ANISOU 1840  C   LEU B 544     3692   4655   2330  -1068  -1221    666       C  
ATOM   1841  O   LEU B 544       8.209 -19.497 -40.834  1.00 26.85           O  
ANISOU 1841  O   LEU B 544     3508   4505   2190  -1046  -1262    759       O  
ATOM   1842  CB  LEU B 544      10.691 -20.873 -39.415  1.00 22.85           C  
ANISOU 1842  CB  LEU B 544     3126   3904   1652   -866   -940    523       C  
ATOM   1843  CG  LEU B 544      11.428 -20.629 -38.100  1.00 26.94           C  
ANISOU 1843  CG  LEU B 544     3624   4354   2258   -693   -791    528       C  
ATOM   1844  CD1 LEU B 544      12.900 -20.972 -38.229  1.00 27.42           C  
ANISOU 1844  CD1 LEU B 544     3785   4398   2234   -662   -668    391       C  
ATOM   1845  CD2 LEU B 544      11.245 -19.185 -37.653  1.00 25.48           C  
ANISOU 1845  CD2 LEU B 544     3362   4157   2161   -616   -778    641       C  
ATOM   1846  N   ASP B 545       8.202 -21.673 -41.404  1.00 28.33           N  
ANISOU 1846  N   ASP B 545     3758   4738   2269  -1245  -1309    599       N  
ATOM   1847  CA  ASP B 545       7.657 -21.432 -42.729  1.00 30.69           C  
ANISOU 1847  CA  ASP B 545     4076   5104   2480  -1368  -1435    601       C  
ATOM   1848  C   ASP B 545       6.141 -21.545 -42.740  1.00 32.32           C  
ANISOU 1848  C   ASP B 545     4171   5337   2773  -1446  -1592    708       C  
ATOM   1849  O   ASP B 545       5.439 -20.552 -42.917  1.00 34.61           O  
ANISOU 1849  O   ASP B 545     4403   5635   3111  -1401  -1668    815       O  
ATOM   1850  CB  ASP B 545       8.261 -22.409 -43.732  1.00 32.09           C  
ANISOU 1850  CB  ASP B 545     4354   5328   2511  -1504  -1429    435       C  
ATOM   1851  CG  ASP B 545       8.231 -21.878 -45.148  1.00 34.06           C  
ANISOU 1851  CG  ASP B 545     4651   5652   2639  -1589  -1502    424       C  
ATOM   1852  OD1 ASP B 545       7.738 -20.749 -45.349  1.00 34.69           O  
ANISOU 1852  OD1 ASP B 545     4697   5751   2731  -1592  -1574    572       O  
ATOM   1853  OD2 ASP B 545       8.709 -22.588 -46.053  1.00 35.45           O  
ANISOU 1853  OD2 ASP B 545     4898   5879   2694  -1698  -1495    286       O  
TER    1854      ASP B 545                                                      
ATOM   1855  N   LEU D 306      -6.171 -11.917 -50.206  1.00 53.77           N  
ANISOU 1855  N   LEU D 306     7034   7338   6057    903   1318  -1205       N  
ATOM   1856  CA  LEU D 306      -5.987 -10.944 -51.309  1.00 52.67           C  
ANISOU 1856  CA  LEU D 306     6750   7091   6171    960   1309  -1217       C  
ATOM   1857  C   LEU D 306      -5.797 -11.691 -52.629  1.00 49.77           C  
ANISOU 1857  C   LEU D 306     6299   6617   5995    827   1167  -1059       C  
ATOM   1858  O   LEU D 306      -6.594 -11.509 -53.521  1.00 50.30           O  
ANISOU 1858  O   LEU D 306     6240   6590   6281    852   1143  -1033       O  
ATOM   1859  CB  LEU D 306      -4.744 -10.107 -51.023  1.00 53.07           C  
ANISOU 1859  CB  LEU D 306     6892   6999   6273   1071   1220  -1426       C  
ATOM   1860  N   ALA D 307      -4.787 -12.556 -52.696  1.00 49.92           N  
ANISOU 1860  N   ALA D 307     6391   6650   5926    694   1070   -960       N  
ATOM   1861  CA  ALA D 307      -4.423 -13.353 -53.894  1.00 46.80           C  
ANISOU 1861  CA  ALA D 307     5943   6164   5675    573    926   -821       C  
ATOM   1862  C   ALA D 307      -5.643 -13.929 -54.635  1.00 44.82           C  
ANISOU 1862  C   ALA D 307     5502   5926   5601    563    985   -677       C  
ATOM   1863  O   ALA D 307      -5.682 -13.816 -55.859  1.00 47.23           O  
ANISOU 1863  O   ALA D 307     5749   6118   6080    512    866   -601       O  
ATOM   1864  CB  ALA D 307      -3.431 -14.423 -53.468  1.00 45.52           C  
ANISOU 1864  CB  ALA D 307     5872   6060   5364    450    851   -735       C  
ATOM   1865  N   LEU D 308      -6.586 -14.526 -53.911  1.00 44.62           N  
ANISOU 1865  N   LEU D 308     5382   6039   5532    614   1166   -637       N  
ATOM   1866  CA  LEU D 308      -7.823 -15.148 -54.452  1.00 45.38           C  
ANISOU 1866  CA  LEU D 308     5286   6161   5796    597   1227   -484       C  
ATOM   1867  C   LEU D 308      -8.977 -14.132 -54.492  1.00 46.93           C  
ANISOU 1867  C   LEU D 308     5351   6323   6158    728   1325   -562       C  
ATOM   1868  O   LEU D 308     -10.084 -14.550 -54.797  1.00 48.91           O  
ANISOU 1868  O   LEU D 308     5424   6586   6573    730   1381   -451       O  
ATOM   1869  CB  LEU D 308      -8.155 -16.353 -53.566  1.00 43.69           C  
ANISOU 1869  CB  LEU D 308     5025   6128   5449    545   1360   -349       C  
ATOM   1870  N   SER D 309      -8.710 -12.852 -54.200  1.00 45.58           N  
ANISOU 1870  N   SER D 309     5265   6099   5953    838   1331   -756       N  
ATOM   1871  CA  SER D 309      -9.778 -11.822 -54.263  1.00 43.99           C  
ANISOU 1871  CA  SER D 309     4954   5847   5914    977   1401   -858       C  
ATOM   1872  C   SER D 309      -9.667 -11.036 -55.561  1.00 41.85           C  
ANISOU 1872  C   SER D 309     4679   5360   5863    973   1213   -891       C  
ATOM   1873  O   SER D 309     -10.547 -10.219 -55.814  1.00 44.01           O  
ANISOU 1873  O   SER D 309     4861   5555   6304   1081   1229   -971       O  
ATOM   1874  CB  SER D 309      -9.719 -10.871 -53.094  1.00 45.33           C  
ANISOU 1874  CB  SER D 309     5218   6081   5926   1122   1512  -1063       C  
ATOM   1875  OG  SER D 309     -10.225 -11.459 -51.912  1.00 49.00           O  
ANISOU 1875  OG  SER D 309     5668   6758   6193   1147   1715  -1032       O  
ATOM   1876  N   LEU D 310      -8.645 -11.309 -56.368  1.00 41.23           N  
ANISOU 1876  N   LEU D 310     4699   5186   5781    852   1036   -828       N  
ATOM   1877  CA  LEU D 310      -8.471 -10.525 -57.615  1.00 37.31           C  
ANISOU 1877  CA  LEU D 310     4220   4491   5466    833    853   -842       C  
ATOM   1878  C   LEU D 310      -9.647 -10.752 -58.556  1.00 35.63           C  
ANISOU 1878  C   LEU D 310     3836   4206   5495    838    831   -734       C  
ATOM   1879  O   LEU D 310     -10.114 -11.855 -58.640  1.00 38.26           O  
ANISOU 1879  O   LEU D 310     4060   4620   5859    783    882   -583       O  
ATOM   1880  CB  LEU D 310      -7.188 -10.947 -58.341  1.00 34.72           C  
ANISOU 1880  CB  LEU D 310     4016   4107   5070    697    691   -774       C  
ATOM   1881  CG  LEU D 310      -5.853 -10.680 -57.652  1.00 35.22           C  
ANISOU 1881  CG  LEU D 310     4258   4185   4940    670    646   -875       C  
ATOM   1882  CD1 LEU D 310      -4.735 -11.377 -58.416  1.00 34.49           C  
ANISOU 1882  CD1 LEU D 310     4231   4090   4783    527    528   -761       C  
ATOM   1883  CD2 LEU D 310      -5.557  -9.201 -57.629  1.00 37.19           C  
ANISOU 1883  CD2 LEU D 310     4589   4282   5259    733    548  -1029       C  
ATOM   1884  N   THR D 311      -9.954  -9.743 -59.371  1.00 35.28           N  
ANISOU 1884  N   THR D 311     3775   3999   5630    900    737   -809       N  
ATOM   1885  CA  THR D 311     -10.856  -9.876 -60.504  1.00 35.10           C  
ANISOU 1885  CA  THR D 311     3620   3869   5848    895    664   -710       C  
ATOM   1886  C   THR D 311     -10.100 -10.556 -61.642  1.00 31.46           C  
ANISOU 1886  C   THR D 311     3220   3334   5398    757    498   -570       C  
ATOM   1887  O   THR D 311      -8.875 -10.693 -61.583  1.00 28.10           O  
ANISOU 1887  O   THR D 311     2936   2924   4816    679    437   -573       O  
ATOM   1888  CB  THR D 311     -11.394  -8.514 -60.988  1.00 33.64           C  
ANISOU 1888  CB  THR D 311     3418   3515   5850    999    586   -833       C  
ATOM   1889  OG1 THR D 311     -10.313  -7.734 -61.511  1.00 32.89           O  
ANISOU 1889  OG1 THR D 311     3488   3284   5723    952    422   -891       O  
ATOM   1890  CG2 THR D 311     -12.070  -7.749 -59.847  1.00 36.40           C  
ANISOU 1890  CG2 THR D 311     3719   3935   6179   1156    743  -1000       C  
ATOM   1891  N   ALA D 312     -10.826 -10.979 -62.673  1.00 28.79           N  
ANISOU 1891  N   ALA D 312     2778   2915   5246    735    421   -451       N  
ATOM   1892  CA  ALA D 312     -10.203 -11.598 -63.836  1.00 26.01           C  
ANISOU 1892  CA  ALA D 312     2486   2488   4908    624    258   -326       C  
ATOM   1893  C   ALA D 312      -9.267 -10.611 -64.520  1.00 25.25           C  
ANISOU 1893  C   ALA D 312     2538   2254   4803    600    114   -394       C  
ATOM   1894  O   ALA D 312      -8.134 -10.949 -64.855  1.00 23.84           O  
ANISOU 1894  O   ALA D 312     2472   2084   4502    508     38   -351       O  
ATOM   1895  CB  ALA D 312     -11.258 -12.098 -64.810  1.00 25.98           C  
ANISOU 1895  CB  ALA D 312     2349   2402   5118    625    188   -204       C  
ATOM   1896  N   ASP D 313      -9.744  -9.386 -64.713  1.00 26.59           N  
ANISOU 1896  N   ASP D 313     2701   2296   5106    683     76   -497       N  
ATOM   1897  CA  ASP D 313      -8.918  -8.343 -65.310  1.00 27.09           C  
ANISOU 1897  CA  ASP D 313     2900   2218   5174    658    -62   -558       C  
ATOM   1898  C   ASP D 313      -7.660  -8.072 -64.487  1.00 27.72           C  
ANISOU 1898  C   ASP D 313     3114   2368   5051    622    -35   -642       C  
ATOM   1899  O   ASP D 313      -6.575  -7.890 -65.040  1.00 24.60           O  
ANISOU 1899  O   ASP D 313     2833   1919   4596    535   -144   -615       O  
ATOM   1900  CB  ASP D 313      -9.717  -7.053 -65.475  1.00 29.43           C  
ANISOU 1900  CB  ASP D 313     3163   2366   5651    764   -107   -668       C  
ATOM   1901  CG  ASP D 313     -10.735  -7.138 -66.594  1.00 28.93           C  
ANISOU 1901  CG  ASP D 313     3004   2180   5809    781   -201   -580       C  
ATOM   1902  OD1 ASP D 313     -10.639  -8.062 -67.432  1.00 33.47           O  
ANISOU 1902  OD1 ASP D 313     3572   2755   6391    700   -267   -433       O  
ATOM   1903  OD2 ASP D 313     -11.617  -6.260 -66.647  1.00 35.95           O  
ANISOU 1903  OD2 ASP D 313     3840   2994   6827    862   -219   -652       O  
ATOM   1904  N   GLN D 314      -7.808  -8.047 -63.167  1.00 28.50           N  
ANISOU 1904  N   GLN D 314     3197   2589   5043    689    111   -742       N  
ATOM   1905  CA  GLN D 314      -6.661  -7.852 -62.286  1.00 28.13           C  
ANISOU 1905  CA  GLN D 314     3280   2610   4800    663    133   -827       C  
ATOM   1906  C   GLN D 314      -5.682  -9.022 -62.362  1.00 25.04           C  
ANISOU 1906  C   GLN D 314     2938   2321   4255    540    121   -712       C  
ATOM   1907  O   GLN D 314      -4.471  -8.822 -62.283  1.00 24.38           O  
ANISOU 1907  O   GLN D 314     2972   2228   4062    475     55   -739       O  
ATOM   1908  CB  GLN D 314      -7.114  -7.644 -60.842  1.00 33.16           C  
ANISOU 1908  CB  GLN D 314     3895   3363   5339    774    295   -957       C  
ATOM   1909  CG  GLN D 314      -7.673  -6.258 -60.551  1.00 34.99           C  
ANISOU 1909  CG  GLN D 314     4130   3490   5674    907    287  -1126       C  
ATOM   1910  CD  GLN D 314      -8.311  -6.173 -59.181  1.00 35.06           C  
ANISOU 1910  CD  GLN D 314     4098   3636   5588   1037    470  -1246       C  
ATOM   1911  OE1 GLN D 314      -8.676  -7.190 -58.589  1.00 33.05           O  
ANISOU 1911  OE1 GLN D 314     3770   3551   5238   1030    620  -1175       O  
ATOM   1912  NE2 GLN D 314      -8.435  -4.957 -58.659  1.00 37.00           N  
ANISOU 1912  NE2 GLN D 314     4396   3811   5853   1158    457  -1430       N  
ATOM   1913  N   MET D 315      -6.202 -10.237 -62.515  1.00 24.48           N  
ANISOU 1913  N   MET D 315     2772   2341   4187    509    176   -585       N  
ATOM   1914  CA  MET D 315      -5.348 -11.416 -62.659  1.00 24.73           C  
ANISOU 1914  CA  MET D 315     2845   2461   4091    401    148   -474       C  
ATOM   1915  C   MET D 315      -4.481 -11.304 -63.910  1.00 22.34           C  
ANISOU 1915  C   MET D 315     2615   2051   3822    316    -13   -412       C  
ATOM   1916  O   MET D 315      -3.267 -11.501 -63.851  1.00 20.65           O  
ANISOU 1916  O   MET D 315     2495   1871   3481    243    -58   -411       O  
ATOM   1917  CB  MET D 315      -6.187 -12.694 -62.713  1.00 23.46           C  
ANISOU 1917  CB  MET D 315     2562   2389   3964    386    209   -342       C  
ATOM   1918  CG  MET D 315      -5.373 -13.967 -62.934  1.00 23.23           C  
ANISOU 1918  CG  MET D 315     2572   2436   3819    282    157   -228       C  
ATOM   1919  SD  MET D 315      -4.140 -14.301 -61.657  1.00 29.16           S  
ANISOU 1919  SD  MET D 315     3440   3324   4314    239    215   -291       S  
ATOM   1920  CE  MET D 315      -5.198 -14.793 -60.298  1.00 29.15           C  
ANISOU 1920  CE  MET D 315     3348   3474   4255    301    409   -292       C  
ATOM   1921  N   VAL D 316      -5.116 -10.975 -65.034  1.00 23.05           N  
ANISOU 1921  N   VAL D 316     2659   2014   4083    330    -98   -361       N  
ATOM   1922  CA  VAL D 316      -4.419 -10.805 -66.308  1.00 25.41           C  
ANISOU 1922  CA  VAL D 316     3027   2210   4416    260   -244   -294       C  
ATOM   1923  C   VAL D 316      -3.360  -9.716 -66.231  1.00 24.81           C  
ANISOU 1923  C   VAL D 316     3067   2070   4291    230   -301   -381       C  
ATOM   1924  O   VAL D 316      -2.234  -9.903 -66.692  1.00 21.58           O  
ANISOU 1924  O   VAL D 316     2732   1670   3799    144   -367   -335       O  
ATOM   1925  CB  VAL D 316      -5.402 -10.464 -67.450  1.00 23.98           C  
ANISOU 1925  CB  VAL D 316     2790   1888   4433    294   -330   -239       C  
ATOM   1926  CG1 VAL D 316      -4.646 -10.045 -68.708  1.00 25.53           C  
ANISOU 1926  CG1 VAL D 316     3081   1973   4647    228   -474   -184       C  
ATOM   1927  CG2 VAL D 316      -6.292 -11.647 -67.745  1.00 21.61           C  
ANISOU 1927  CG2 VAL D 316     2382   1634   4194    302   -314   -128       C  
ATOM   1928  N   SER D 317      -3.727  -8.580 -65.648  1.00 23.72           N  
ANISOU 1928  N   SER D 317     2938   1865   4210    304   -279   -506       N  
ATOM   1929  CA  SER D 317      -2.799  -7.466 -65.496  1.00 24.48           C  
ANISOU 1929  CA  SER D 317     3140   1881   4280    281   -349   -595       C  
ATOM   1930  C   SER D 317      -1.576  -7.884 -64.693  1.00 23.15           C  
ANISOU 1930  C   SER D 317     3044   1826   3927    220   -318   -622       C  
ATOM   1931  O   SER D 317      -0.445  -7.563 -65.053  1.00 21.57           O  
ANISOU 1931  O   SER D 317     2921   1587   3689    139   -404   -607       O  
ATOM   1932  CB  SER D 317      -3.487  -6.278 -64.824  1.00 29.51           C  
ANISOU 1932  CB  SER D 317     3773   2437   5002    391   -330   -744       C  
ATOM   1933  OG  SER D 317      -4.582  -5.836 -65.602  1.00 37.89           O  
ANISOU 1933  OG  SER D 317     4767   3379   6252    448   -376   -724       O  
ATOM   1934  N   ALA D 318      -1.812  -8.612 -63.609  1.00 23.55           N  
ANISOU 1934  N   ALA D 318     3066   2017   3865    258   -197   -656       N  
ATOM   1935  CA  ALA D 318      -0.729  -9.089 -62.759  1.00 21.84           C  
ANISOU 1935  CA  ALA D 318     2921   1909   3470    208   -172   -684       C  
ATOM   1936  C   ALA D 318       0.222 -10.015 -63.520  1.00 21.28           C  
ANISOU 1936  C   ALA D 318     2864   1881   3338     96   -236   -561       C  
ATOM   1937  O   ALA D 318       1.446  -9.909 -63.393  1.00 23.59           O  
ANISOU 1937  O   ALA D 318     3231   2182   3549     29   -290   -578       O  
ATOM   1938  CB  ALA D 318      -1.295  -9.799 -61.545  1.00 22.49           C  
ANISOU 1938  CB  ALA D 318     2967   2136   3442    267    -29   -719       C  
ATOM   1939  N   LEU D 319      -0.348 -10.917 -64.312  1.00 19.81           N  
ANISOU 1939  N   LEU D 319     2606   1719   3201     82   -235   -440       N  
ATOM   1940  CA  LEU D 319       0.440 -11.886 -65.066  1.00 19.48           C  
ANISOU 1940  CA  LEU D 319     2575   1726   3102     -3   -295   -330       C  
ATOM   1941  C   LEU D 319       1.229 -11.223 -66.191  1.00 20.52           C  
ANISOU 1941  C   LEU D 319     2756   1756   3283    -64   -406   -294       C  
ATOM   1942  O   LEU D 319       2.380 -11.581 -66.446  1.00 21.53           O  
ANISOU 1942  O   LEU D 319     2925   1929   3328   -137   -449   -260       O  
ATOM   1943  CB  LEU D 319      -0.466 -12.981 -65.625  1.00 17.84           C  
ANISOU 1943  CB  LEU D 319     2282   1553   2944     10   -284   -218       C  
ATOM   1944  CG  LEU D 319      -1.055 -13.899 -64.552  1.00 18.71           C  
ANISOU 1944  CG  LEU D 319     2338   1788   2985     40   -177   -215       C  
ATOM   1945  CD1 LEU D 319      -1.858 -15.017 -65.191  1.00 17.66           C  
ANISOU 1945  CD1 LEU D 319     2118   1673   2917     38   -195    -89       C  
ATOM   1946  CD2 LEU D 319       0.049 -14.453 -63.668  1.00 20.41           C  
ANISOU 1946  CD2 LEU D 319     2619   2113   3021     -9   -159   -245       C  
ATOM   1947  N   LEU D 320       0.611 -10.251 -66.855  1.00 20.38           N  
ANISOU 1947  N   LEU D 320     2732   1605   3405    -33   -452   -299       N  
ATOM   1948  CA  LEU D 320       1.294  -9.514 -67.911  1.00 24.45           C  
ANISOU 1948  CA  LEU D 320     3300   2018   3971    -95   -554   -256       C  
ATOM   1949  C   LEU D 320       2.462  -8.727 -67.348  1.00 23.39           C  
ANISOU 1949  C   LEU D 320     3236   1869   3782   -145   -581   -330       C  
ATOM   1950  O   LEU D 320       3.527  -8.662 -67.957  1.00 24.74           O  
ANISOU 1950  O   LEU D 320     3441   2038   3921   -230   -639   -273       O  
ATOM   1951  CB  LEU D 320       0.333  -8.571 -68.635  1.00 25.93           C  
ANISOU 1951  CB  LEU D 320     3475   2052   4323    -49   -610   -251       C  
ATOM   1952  CG  LEU D 320      -0.742  -9.246 -69.478  1.00 26.09           C  
ANISOU 1952  CG  LEU D 320     3433   2054   4427    -11   -623   -161       C  
ATOM   1953  CD1 LEU D 320      -1.720  -8.223 -70.045  1.00 27.69           C  
ANISOU 1953  CD1 LEU D 320     3622   2109   4790     42   -679   -174       C  
ATOM   1954  CD2 LEU D 320      -0.082 -10.049 -70.585  1.00 22.89           C  
ANISOU 1954  CD2 LEU D 320     3054   1685   3959    -79   -681    -36       C  
ATOM   1955  N   ASP D 321       2.257  -8.132 -66.179  1.00 25.36           N  
ANISOU 1955  N   ASP D 321     3504   2110   4023    -90   -541   -457       N  
ATOM   1956  CA  ASP D 321       3.301  -7.342 -65.543  1.00 25.20           C  
ANISOU 1956  CA  ASP D 321     3555   2057   3961   -128   -585   -541       C  
ATOM   1957  C   ASP D 321       4.463  -8.219 -65.087  1.00 23.85           C  
ANISOU 1957  C   ASP D 321     3404   2013   3645   -195   -569   -524       C  
ATOM   1958  O   ASP D 321       5.598  -7.757 -64.985  1.00 27.61           O  
ANISOU 1958  O   ASP D 321     3926   2464   4100   -263   -633   -543       O  
ATOM   1959  CB  ASP D 321       2.739  -6.568 -64.349  1.00 25.13           C  
ANISOU 1959  CB  ASP D 321     3573   2013   3964    -32   -550   -695       C  
ATOM   1960  CG  ASP D 321       3.616  -5.405 -63.951  1.00 36.18           C  
ANISOU 1960  CG  ASP D 321     5054   3312   5381    -60   -643   -784       C  
ATOM   1961  OD1 ASP D 321       4.137  -4.717 -64.856  1.00 40.53           O  
ANISOU 1961  OD1 ASP D 321     5625   3753   6022   -135   -747   -723       O  
ATOM   1962  OD2 ASP D 321       3.794  -5.174 -62.733  1.00 40.45           O  
ANISOU 1962  OD2 ASP D 321     5644   3881   5845    -10   -619   -910       O  
ATOM   1963  N   ALA D 322       4.175  -9.485 -64.812  1.00 21.63           N  
ANISOU 1963  N   ALA D 322     3083   1861   3275   -178   -495   -486       N  
ATOM   1964  CA  ALA D 322       5.178 -10.387 -64.259  1.00 21.60           C  
ANISOU 1964  CA  ALA D 322     3098   1977   3132   -228   -485   -482       C  
ATOM   1965  C   ALA D 322       6.073 -11.011 -65.330  1.00 21.55           C  
ANISOU 1965  C   ALA D 322     3074   2005   3110   -312   -540   -370       C  
ATOM   1966  O   ALA D 322       7.025 -11.720 -65.003  1.00 21.15           O  
ANISOU 1966  O   ALA D 322     3033   2043   2959   -358   -549   -365       O  
ATOM   1967  CB  ALA D 322       4.500 -11.483 -63.446  1.00 22.08           C  
ANISOU 1967  CB  ALA D 322     3129   2158   3103   -177   -393   -486       C  
ATOM   1968  N   GLU D 323       5.770 -10.747 -66.598  1.00 18.80           N  
ANISOU 1968  N   GLU D 323     2703   1587   2853   -326   -578   -284       N  
ATOM   1969  CA  GLU D 323       6.462 -11.416 -67.699  1.00 18.19           C  
ANISOU 1969  CA  GLU D 323     2608   1555   2747   -385   -615   -175       C  
ATOM   1970  C   GLU D 323       7.963 -11.170 -67.669  1.00 16.74           C  
ANISOU 1970  C   GLU D 323     2447   1397   2517   -469   -656   -179       C  
ATOM   1971  O   GLU D 323       8.406 -10.028 -67.553  1.00 18.29           O  
ANISOU 1971  O   GLU D 323     2673   1504   2773   -506   -696   -216       O  
ATOM   1972  CB  GLU D 323       5.885 -10.973 -69.041  1.00 20.47           C  
ANISOU 1972  CB  GLU D 323     2889   1750   3137   -382   -656    -89       C  
ATOM   1973  CG  GLU D 323       4.658 -11.759 -69.434  1.00 23.38           C  
ANISOU 1973  CG  GLU D 323     3218   2129   3536   -315   -636    -40       C  
ATOM   1974  CD  GLU D 323       4.988 -13.204 -69.750  1.00 17.93           C  
ANISOU 1974  CD  GLU D 323     2505   1557   2749   -322   -636     26       C  
ATOM   1975  OE1 GLU D 323       4.857 -14.063 -68.853  1.00 18.09           O  
ANISOU 1975  OE1 GLU D 323     2504   1666   2704   -301   -594     -6       O  
ATOM   1976  OE2 GLU D 323       5.379 -13.480 -70.902  1.00 22.51           O  
ANISOU 1976  OE2 GLU D 323     3095   2142   3318   -346   -683    109       O  
ATOM   1977  N   PRO D 324       8.749 -12.254 -67.750  1.00 15.00           N  
ANISOU 1977  N   PRO D 324     2206   1292   2200   -498   -654   -144       N  
ATOM   1978  CA  PRO D 324      10.206 -12.133 -67.789  1.00 17.45           C  
ANISOU 1978  CA  PRO D 324     2515   1638   2476   -577   -690   -140       C  
ATOM   1979  C   PRO D 324      10.645 -11.602 -69.143  1.00 15.24           C  
ANISOU 1979  C   PRO D 324     2220   1316   2252   -632   -720    -42       C  
ATOM   1980  O   PRO D 324       9.884 -11.682 -70.109  1.00 17.77           O  
ANISOU 1980  O   PRO D 324     2539   1607   2606   -602   -718     30       O  
ATOM   1981  CB  PRO D 324      10.680 -13.570 -67.567  1.00 20.81           C  
ANISOU 1981  CB  PRO D 324     2917   2200   2791   -570   -681   -130       C  
ATOM   1982  CG  PRO D 324       9.607 -14.389 -68.184  1.00 21.60           C  
ANISOU 1982  CG  PRO D 324     2998   2321   2889   -510   -660    -68       C  
ATOM   1983  CD  PRO D 324       8.314 -13.654 -67.902  1.00 18.37           C  
ANISOU 1983  CD  PRO D 324     2603   1816   2562   -459   -631    -98       C  
ATOM   1984  N   PRO D 325      11.857 -11.051 -69.220  1.00 15.31           N  
ANISOU 1984  N   PRO D 325     2220   1322   2275   -713   -752    -32       N  
ATOM   1985  CA  PRO D 325      12.319 -10.542 -70.512  1.00 18.23           C  
ANISOU 1985  CA  PRO D 325     2573   1666   2688   -774   -768     78       C  
ATOM   1986  C   PRO D 325      12.728 -11.651 -71.466  1.00 17.75           C  
ANISOU 1986  C   PRO D 325     2474   1729   2540   -767   -741    160       C  
ATOM   1987  O   PRO D 325      12.944 -12.785 -71.043  1.00 17.25           O  
ANISOU 1987  O   PRO D 325     2389   1771   2392   -731   -727    125       O  
ATOM   1988  CB  PRO D 325      13.529  -9.700 -70.137  1.00 19.67           C  
ANISOU 1988  CB  PRO D 325     2735   1838   2902   -840   -783     62       C  
ATOM   1989  CG  PRO D 325      14.046 -10.332 -68.892  1.00 17.13           C  
ANISOU 1989  CG  PRO D 325     2407   1587   2517   -824   -782    -38       C  
ATOM   1990  CD  PRO D 325      12.837 -10.819 -68.145  1.00 17.99           C  
ANISOU 1990  CD  PRO D 325     2560   1679   2594   -748   -771   -113       C  
ATOM   1991  N   ILE D 326      12.838 -11.314 -72.745  1.00 15.81           N  
ANISOU 1991  N   ILE D 326     2227   1469   2312   -796   -741    267       N  
ATOM   1992  CA  ILE D 326      13.413 -12.226 -73.717  1.00 15.43           C  
ANISOU 1992  CA  ILE D 326     2147   1544   2173   -789   -716    341       C  
ATOM   1993  C   ILE D 326      14.923 -12.028 -73.710  1.00 16.63           C  
ANISOU 1993  C   ILE D 326     2238   1769   2313   -875   -703    361       C  
ATOM   1994  O   ILE D 326      15.414 -10.921 -73.938  1.00 19.23           O  
ANISOU 1994  O   ILE D 326     2559   2031   2716   -961   -714    410       O  
ATOM   1995  CB  ILE D 326      12.838 -11.993 -75.128  1.00 17.35           C  
ANISOU 1995  CB  ILE D 326     2426   1747   2418   -773   -718    450       C  
ATOM   1996  CG1 ILE D 326      11.347 -12.346 -75.156  1.00 20.87           C  
ANISOU 1996  CG1 ILE D 326     2917   2126   2886   -681   -741    430       C  
ATOM   1997  CG2 ILE D 326      13.596 -12.817 -76.158  1.00 22.63           C  
ANISOU 1997  CG2 ILE D 326     3067   2552   2978   -763   -688    522       C  
ATOM   1998  CD1 ILE D 326      10.670 -12.039 -76.479  1.00 24.76           C  
ANISOU 1998  CD1 ILE D 326     3460   2553   3396   -661   -766    528       C  
ATOM   1999  N   LEU D 327      15.660 -13.092 -73.413  1.00 15.00           N  
ANISOU 1999  N   LEU D 327     1983   1690   2024   -854   -690    324       N  
ATOM   2000  CA  LEU D 327      17.111 -13.002 -73.334  1.00 15.65           C  
ANISOU 2000  CA  LEU D 327     1990   1849   2107   -928   -680    333       C  
ATOM   2001  C   LEU D 327      17.789 -13.341 -74.653  1.00 16.67           C  
ANISOU 2001  C   LEU D 327     2071   2090   2174   -935   -631    435       C  
ATOM   2002  O   LEU D 327      17.204 -13.984 -75.529  1.00 15.56           O  
ANISOU 2002  O   LEU D 327     1964   1990   1959   -860   -614    476       O  
ATOM   2003  CB  LEU D 327      17.644 -13.921 -72.234  1.00 18.43           C  
ANISOU 2003  CB  LEU D 327     2313   2277   2414   -903   -703    229       C  
ATOM   2004  CG  LEU D 327      17.060 -13.712 -70.838  1.00 15.74           C  
ANISOU 2004  CG  LEU D 327     2027   1852   2103   -885   -741    123       C  
ATOM   2005  CD1 LEU D 327      17.808 -14.558 -69.823  1.00 18.78           C  
ANISOU 2005  CD1 LEU D 327     2386   2316   2434   -838   -738     35       C  
ATOM   2006  CD2 LEU D 327      17.120 -12.237 -70.459  1.00 18.57           C  
ANISOU 2006  CD2 LEU D 327     2406   2084   2567   -937   -753    114       C  
ATOM   2007  N   TYR D 328      19.036 -12.906 -74.780  1.00 24.19           N  
ANISOU 2007  N   TYR D 328     2943   3091   3158  -1022   -610    476       N  
ATOM   2008  CA  TYR D 328      19.836 -13.222 -75.950  1.00 17.65           C  
ANISOU 2008  CA  TYR D 328     2051   2393   2263  -1029   -544    569       C  
ATOM   2009  C   TYR D 328      20.809 -14.359 -75.686  1.00 17.43           C  
ANISOU 2009  C   TYR D 328     1938   2517   2168   -989   -532    508       C  
ATOM   2010  O   TYR D 328      21.234 -14.578 -74.550  1.00 17.19           O  
ANISOU 2010  O   TYR D 328     1876   2479   2175  -1004   -579    414       O  
ATOM   2011  CB  TYR D 328      20.614 -11.994 -76.418  1.00 19.18           C  
ANISOU 2011  CB  TYR D 328     2191   2557   2541  -1158   -517    679       C  
ATOM   2012  CG  TYR D 328      19.754 -10.953 -77.084  1.00 20.05           C  
ANISOU 2012  CG  TYR D 328     2385   2537   2697  -1193   -526    770       C  
ATOM   2013  CD1 TYR D 328      19.006 -10.060 -76.332  1.00 30.85           C  
ANISOU 2013  CD1 TYR D 328     3818   3731   4172  -1221   -599    725       C  
ATOM   2014  CD2 TYR D 328      19.687 -10.864 -78.468  1.00 22.07           C  
ANISOU 2014  CD2 TYR D 328     2660   2844   2883  -1192   -469    898       C  
ATOM   2015  CE1 TYR D 328      18.214  -9.099 -76.940  1.00 30.14           C  
ANISOU 2015  CE1 TYR D 328     3804   3512   4136  -1249   -623    802       C  
ATOM   2016  CE2 TYR D 328      18.899  -9.909 -79.085  1.00 24.88           C  
ANISOU 2016  CE2 TYR D 328     3101   3070   3283  -1226   -494    985       C  
ATOM   2017  CZ  TYR D 328      18.163  -9.030 -78.316  1.00 30.05           C  
ANISOU 2017  CZ  TYR D 328     3813   3544   4061  -1256   -575    935       C  
ATOM   2018  OH  TYR D 328      17.374  -8.074 -78.914  1.00 38.66           O  
ANISOU 2018  OH  TYR D 328     4984   4506   5199  -1261   -609    997       O  
ATOM   2019  N   SER D 329      21.157 -15.081 -76.744  1.00 19.40           N  
ANISOU 2019  N   SER D 329     2155   2901   2315   -932   -476    558       N  
ATOM   2020  CA  SER D 329      22.260 -16.023 -76.681  1.00 18.39           C  
ANISOU 2020  CA  SER D 329     1926   2926   2135   -898   -458    512       C  
ATOM   2021  C   SER D 329      23.562 -15.251 -76.492  1.00 19.18           C  
ANISOU 2021  C   SER D 329     1903   3055   2328  -1019   -425    552       C  
ATOM   2022  O   SER D 329      23.704 -14.137 -76.993  1.00 20.83           O  
ANISOU 2022  O   SER D 329     2098   3216   2598  -1115   -386    661       O  
ATOM   2023  CB  SER D 329      22.323 -16.876 -77.946  1.00 23.23           C  
ANISOU 2023  CB  SER D 329     2537   3676   2612   -798   -403    554       C  
ATOM   2024  OG  SER D 329      23.314 -17.878 -77.824  1.00 26.47           O  
ANISOU 2024  OG  SER D 329     2853   4231   2974   -744   -398    487       O  
ATOM   2025  N   GLU D 330      24.502 -15.834 -75.754  1.00 19.24           N  
ANISOU 2025  N   GLU D 330     1820   3133   2358  -1018   -454    470       N  
ATOM   2026  CA  GLU D 330      25.804 -15.211 -75.559  1.00 22.39           C  
ANISOU 2026  CA  GLU D 330     2084   3565   2860  -1128   -434    505       C  
ATOM   2027  C   GLU D 330      26.822 -15.791 -76.515  1.00 28.48           C  
ANISOU 2027  C   GLU D 330     2727   4527   3566  -1096   -341    553       C  
ATOM   2028  O   GLU D 330      27.427 -16.824 -76.228  1.00 28.48           O  
ANISOU 2028  O   GLU D 330     2661   4630   3529  -1024   -361    464       O  
ATOM   2029  CB  GLU D 330      26.313 -15.395 -74.129  1.00 27.08           C  
ANISOU 2029  CB  GLU D 330     2646   4108   3534  -1154   -534    385       C  
ATOM   2030  CG  GLU D 330      25.838 -14.359 -73.140  1.00 31.03           C  
ANISOU 2030  CG  GLU D 330     3226   4422   4140  -1227   -610    356       C  
ATOM   2031  CD  GLU D 330      26.361 -14.627 -71.739  1.00 31.38           C  
ANISOU 2031  CD  GLU D 330     3289   4402   4230  -1177   -677    216       C  
ATOM   2032  OE1 GLU D 330      27.529 -14.279 -71.464  1.00 38.05           O  
ANISOU 2032  OE1 GLU D 330     4041   5250   5168  -1224   -683    212       O  
ATOM   2033  OE2 GLU D 330      25.610 -15.179 -70.913  1.00 38.02           O  
ANISOU 2033  OE2 GLU D 330     4238   5190   5017  -1087   -719    116       O  
ATOM   2034  N   TYR D 331      27.004 -15.131 -77.650  1.00 28.30           N  
ANISOU 2034  N   TYR D 331     2672   4553   3527  -1146   -240    694       N  
ATOM   2035  CA  TYR D 331      28.087 -15.468 -78.560  1.00 31.85           C  
ANISOU 2035  CA  TYR D 331     2982   5195   3925  -1133   -128    758       C  
ATOM   2036  C   TYR D 331      28.458 -14.223 -79.352  1.00 32.37           C  
ANISOU 2036  C   TYR D 331     2994   5258   4046  -1267    -36    935       C  
ATOM   2037  O   TYR D 331      27.623 -13.345 -79.563  1.00 34.46           O  
ANISOU 2037  O   TYR D 331     3370   5390   4334  -1324    -55   1011       O  
ATOM   2038  CB  TYR D 331      27.690 -16.608 -79.503  1.00 29.71           C  
ANISOU 2038  CB  TYR D 331     2766   5056   3467   -969    -79    732       C  
ATOM   2039  CG  TYR D 331      26.606 -16.240 -80.498  1.00 29.46           C  
ANISOU 2039  CG  TYR D 331     2876   4976   3341   -942    -44    826       C  
ATOM   2040  CD1 TYR D 331      26.927 -15.680 -81.730  1.00 30.48           C  
ANISOU 2040  CD1 TYR D 331     2977   5194   3410   -980     79    976       C  
ATOM   2041  CD2 TYR D 331      25.264 -16.450 -80.206  1.00 27.75           C  
ANISOU 2041  CD2 TYR D 331     2819   4626   3098   -880   -134    771       C  
ATOM   2042  CE1 TYR D 331      25.943 -15.338 -82.645  1.00 31.14           C  
ANISOU 2042  CE1 TYR D 331     3202   5224   3405   -955     96   1063       C  
ATOM   2043  CE2 TYR D 331      24.269 -16.111 -81.115  1.00 28.39           C  
ANISOU 2043  CE2 TYR D 331     3027   4652   3109   -854   -117    854       C  
ATOM   2044  CZ  TYR D 331      24.615 -15.556 -82.334  1.00 27.51           C  
ANISOU 2044  CZ  TYR D 331     2900   4621   2934   -890     -9    997       C  
ATOM   2045  OH  TYR D 331      23.630 -15.218 -83.237  1.00 31.92           O  
ANISOU 2045  OH  TYR D 331     3596   5114   3419   -863     -6   1080       O  
ATOM   2046  N   ASP D 332      29.709 -14.145 -79.788  1.00 33.03           N  
ANISOU 2046  N   ASP D 332     3232   5500   3817      3    244   1398       N  
ATOM   2047  CA  ASP D 332      30.133 -13.032 -80.622  1.00 34.10           C  
ANISOU 2047  CA  ASP D 332     3292   5802   3862     86    274   1442       C  
ATOM   2048  C   ASP D 332      29.562 -13.198 -82.026  1.00 31.03           C  
ANISOU 2048  C   ASP D 332     2966   5395   3429    214    213   1303       C  
ATOM   2049  O   ASP D 332      29.876 -14.166 -82.719  1.00 31.73           O  
ANISOU 2049  O   ASP D 332     3147   5437   3471    373    186   1251       O  
ATOM   2050  CB  ASP D 332      31.658 -12.937 -80.667  1.00 41.18           C  
ANISOU 2050  CB  ASP D 332     4155   6833   4660    222    341   1587       C  
ATOM   2051  N   PRO D 333      28.709 -12.254 -82.450  1.00 31.23           N  
ANISOU 2051  N   PRO D 333     2942   5455   3469    143    192   1242       N  
ATOM   2052  CA  PRO D 333      28.072 -12.371 -83.765  1.00 30.18           C  
ANISOU 2052  CA  PRO D 333     2867   5300   3301    251    132   1104       C  
ATOM   2053  C   PRO D 333      29.020 -12.036 -84.913  1.00 33.38           C  
ANISOU 2053  C   PRO D 333     3260   5850   3575    457    157   1145       C  
ATOM   2054  O   PRO D 333      28.623 -12.120 -86.073  1.00 30.72           O  
ANISOU 2054  O   PRO D 333     2969   5508   3195    566    111   1040       O  
ATOM   2055  CB  PRO D 333      26.922 -11.362 -83.680  1.00 32.47           C  
ANISOU 2055  CB  PRO D 333     3092   5591   3653     89    111   1046       C  
ATOM   2056  CG  PRO D 333      27.436 -10.310 -82.757  1.00 30.77           C  
ANISOU 2056  CG  PRO D 333     2757   5489   3444    -29    182   1192       C  
ATOM   2057  CD  PRO D 333      28.275 -11.042 -81.733  1.00 31.19           C  
ANISOU 2057  CD  PRO D 333     2827   5509   3516    -42    222   1295       C  
ATOM   2058  N   THR D 334      30.257 -11.669 -84.589  1.00 31.87           N  
ANISOU 2058  N   THR D 334     3007   5782   3319    509    227   1296       N  
ATOM   2059  CA  THR D 334      31.259 -11.379 -85.612  1.00 35.39           C  
ANISOU 2059  CA  THR D 334     3439   6368   3638    707    256   1347       C  
ATOM   2060  C   THR D 334      32.192 -12.566 -85.837  1.00 37.60           C  
ANISOU 2060  C   THR D 334     3806   6617   3864    875    260   1369       C  
ATOM   2061  O   THR D 334      32.963 -12.587 -86.794  1.00 36.10           O  
ANISOU 2061  O   THR D 334     3631   6517   3571   1060    272   1388       O  
ATOM   2062  CB  THR D 334      32.110 -10.142 -85.250  1.00 35.59           C  
ANISOU 2062  CB  THR D 334     3338   6569   3614    677    334   1502       C  
ATOM   2063  OG1 THR D 334      32.930 -10.435 -84.112  1.00 35.05           O  
ANISOU 2063  OG1 THR D 334     3248   6504   3567    627    387   1629       O  
ATOM   2064  CG2 THR D 334      31.223  -8.944 -84.950  1.00 35.01           C  
ANISOU 2064  CG2 THR D 334     3176   6529   3596    504    334   1489       C  
ATOM   2065  N   ARG D 335      32.117 -13.547 -84.946  1.00 34.33           N  
ANISOU 2065  N   ARG D 335     3448   6076   3521    809    250   1367       N  
ATOM   2066  CA  ARG D 335      32.973 -14.724 -85.018  1.00 35.74           C  
ANISOU 2066  CA  ARG D 335     3708   6212   3659    952    254   1391       C  
ATOM   2067  C   ARG D 335      32.266 -15.832 -85.791  1.00 38.62           C  
ANISOU 2067  C   ARG D 335     4198   6438   4038   1038    177   1233       C  
ATOM   2068  O   ARG D 335      31.042 -15.808 -85.911  1.00 36.07           O  
ANISOU 2068  O   ARG D 335     3898   6022   3784    942    122   1112       O  
ATOM   2069  CB  ARG D 335      33.343 -15.196 -83.608  1.00 38.03           C  
ANISOU 2069  CB  ARG D 335     3990   6444   4016    838    289   1483       C  
ATOM   2070  N   PRO D 336      33.030 -16.804 -86.325  1.00 38.61           N  
ANISOU 2070  N   PRO D 336     4277   6422   3972   1218    173   1232       N  
ATOM   2071  CA  PRO D 336      32.376 -17.908 -87.037  1.00 42.31           C  
ANISOU 2071  CA  PRO D 336     4868   6754   4456   1300     99   1081       C  
ATOM   2072  C   PRO D 336      31.421 -18.667 -86.129  1.00 39.79           C  
ANISOU 2072  C   PRO D 336     4602   6257   4261   1143     58   1007       C  
ATOM   2073  O   PRO D 336      31.705 -18.824 -84.941  1.00 39.88           O  
ANISOU 2073  O   PRO D 336     4587   6239   4326   1033     92   1093       O  
ATOM   2074  CB  PRO D 336      33.544 -18.807 -87.465  1.00 43.39           C  
ANISOU 2074  CB  PRO D 336     5068   6912   4508   1500    117   1128       C  
ATOM   2075  CG  PRO D 336      34.755 -17.950 -87.382  1.00 43.86           C  
ANISOU 2075  CG  PRO D 336     5033   7148   4484   1555    195   1285       C  
ATOM   2076  CD  PRO D 336      34.496 -16.959 -86.294  1.00 42.55           C  
ANISOU 2076  CD  PRO D 336     4761   7023   4384   1351    233   1365       C  
ATOM   2077  N   PHE D 337      30.295 -19.107 -86.677  1.00 40.49           N  
ANISOU 2077  N   PHE D 337     4761   6229   4393   1132    -15    851       N  
ATOM   2078  CA  PHE D 337      29.358 -19.920 -85.921  1.00 42.42           C  
ANISOU 2078  CA  PHE D 337     5068   6297   4752    997    -61    768       C  
ATOM   2079  C   PHE D 337      29.869 -21.350 -85.886  1.00 43.36           C  
ANISOU 2079  C   PHE D 337     5293   6319   4862   1109    -76    754       C  
ATOM   2080  O   PHE D 337      30.818 -21.697 -86.591  1.00 44.88           O  
ANISOU 2080  O   PHE D 337     5516   6576   4958   1295    -59    789       O  
ATOM   2081  CB  PHE D 337      27.957 -19.858 -86.530  1.00 41.70           C  
ANISOU 2081  CB  PHE D 337     5013   6117   4712    943   -134    605       C  
ATOM   2082  N   SER D 338      29.237 -22.171 -85.058  1.00 45.10           N  
ANISOU 2082  N   SER D 338     5569   6385   5183    993   -107    704       N  
ATOM   2083  CA  SER D 338      29.643 -23.555 -84.888  1.00 46.38           C  
ANISOU 2083  CA  SER D 338     5831   6441   5350   1077   -122    689       C  
ATOM   2084  C   SER D 338      28.487 -24.368 -84.323  1.00 45.55           C  
ANISOU 2084  C   SER D 338     5797   6147   5362    946   -181    575       C  
ATOM   2085  O   SER D 338      27.890 -23.991 -83.314  1.00 45.79           O  
ANISOU 2085  O   SER D 338     5779   6134   5484    753   -174    591       O  
ATOM   2086  CB  SER D 338      30.862 -23.648 -83.970  1.00 45.41           C  
ANISOU 2086  CB  SER D 338     5668   6379   5205   1079    -51    851       C  
ATOM   2087  OG  SER D 338      31.622 -24.812 -84.247  1.00 47.25           O  
ANISOU 2087  OG  SER D 338     5990   6570   5391   1237    -54    855       O  
ATOM   2088  N   GLU D 339      28.169 -25.476 -84.985  1.00 43.66           N  
ANISOU 2088  N   GLU D 339     5673   5796   5120   1052   -238    459       N  
ATOM   2089  CA  GLU D 339      27.086 -26.347 -84.545  1.00 43.23           C  
ANISOU 2089  CA  GLU D 339     5696   5557   5172    946   -298    342       C  
ATOM   2090  C   GLU D 339      27.508 -27.133 -83.311  1.00 44.97           C  
ANISOU 2090  C   GLU D 339     5939   5698   5451    873   -273    415       C  
ATOM   2091  O   GLU D 339      26.674 -27.523 -82.490  1.00 44.93           O  
ANISOU 2091  O   GLU D 339     5957   5562   5552    719   -300    364       O  
ATOM   2092  CB  GLU D 339      26.675 -27.286 -85.662  1.00 44.24           C  
ANISOU 2092  CB  GLU D 339     5940   5596   5275   1090   -366    199       C  
ATOM   2093  N   ALA D 340      28.812 -27.360 -83.190  1.00 43.88           N  
ANISOU 2093  N   ALA D 340     5792   5639   5240    986   -220    534       N  
ATOM   2094  CA  ALA D 340      29.376 -28.001 -82.010  1.00 42.50           C  
ANISOU 2094  CA  ALA D 340     5627   5412   5108    925   -185    624       C  
ATOM   2095  C   ALA D 340      28.996 -27.228 -80.751  1.00 42.65           C  
ANISOU 2095  C   ALA D 340     5555   5436   5214    702   -153    693       C  
ATOM   2096  O   ALA D 340      28.785 -27.809 -79.684  1.00 40.13           O  
ANISOU 2096  O   ALA D 340     5258   5010   4979    583   -153    706       O  
ATOM   2097  CB  ALA D 340      30.891 -28.100 -82.136  1.00 42.27           C  
ANISOU 2097  CB  ALA D 340     5582   5499   4978   1080   -125    756       C  
ATOM   2098  N   SER D 341      28.885 -25.910 -80.892  1.00 40.55           N  
ANISOU 2098  N   SER D 341     5187   5292   4927    644   -126    733       N  
ATOM   2099  CA  SER D 341      28.701 -25.028 -79.747  1.00 43.61           C  
ANISOU 2099  CA  SER D 341     5475   5714   5381    446    -85    819       C  
ATOM   2100  C   SER D 341      27.248 -24.868 -79.323  1.00 34.05           C  
ANISOU 2100  C   SER D 341     4265   4388   4284    258   -134    712       C  
ATOM   2101  O   SER D 341      26.969 -24.198 -78.330  1.00 33.04           O  
ANISOU 2101  O   SER D 341     4061   4271   4223     81   -106    771       O  
ATOM   2102  CB  SER D 341      29.287 -23.648 -80.051  1.00 34.57           C  
ANISOU 2102  CB  SER D 341     4216   4759   4162    467    -31    919       C  
ATOM   2103  OG  SER D 341      29.082 -23.294 -81.405  1.00 34.08           O  
ANISOU 2103  OG  SER D 341     4165   4755   4027    594    -61    841       O  
ATOM   2104  N   MET D 342      26.327 -25.475 -80.066  1.00 23.50           N  
ANISOU 2104  N   MET D 342     2775   3121   3033      8    539    110       N  
ATOM   2105  CA  MET D 342      24.910 -25.181 -79.857  1.00 25.35           C  
ANISOU 2105  CA  MET D 342     3098   3320   3214    -46    486    107       C  
ATOM   2106  C   MET D 342      24.377 -25.543 -78.478  1.00 24.19           C  
ANISOU 2106  C   MET D 342     3004   3070   3116    -64    393     80       C  
ATOM   2107  O   MET D 342      23.650 -24.755 -77.878  1.00 19.45           O  
ANISOU 2107  O   MET D 342     2427   2437   2526   -119    344    115       O  
ATOM   2108  CB  MET D 342      24.032 -25.870 -80.906  1.00 26.33           C  
ANISOU 2108  CB  MET D 342     3300   3484   3219    -30    519     51       C  
ATOM   2109  CG  MET D 342      23.968 -25.155 -82.246  1.00 28.67           C  
ANISOU 2109  CG  MET D 342     3571   3888   3435    -55    591     98       C  
ATOM   2110  SD  MET D 342      23.158 -23.541 -82.126  1.00 53.39           S  
ANISOU 2110  SD  MET D 342     6689   7019   6580   -149    549    205       S  
ATOM   2111  CE  MET D 342      21.942 -23.845 -80.855  1.00 29.91           C  
ANISOU 2111  CE  MET D 342     3805   3927   3631   -170    451    168       C  
ATOM   2112  N   MET D 343      24.714 -26.729 -77.983  1.00 22.24           N  
ANISOU 2112  N   MET D 343     2775   2775   2901    -18    368     19       N  
ATOM   2113  CA  MET D 343      24.222 -27.150 -76.676  1.00 18.88           C  
ANISOU 2113  CA  MET D 343     2397   2263   2515    -42    276     -1       C  
ATOM   2114  C   MET D 343      24.723 -26.201 -75.594  1.00 18.59           C  
ANISOU 2114  C   MET D 343     2308   2192   2563    -89    232     60       C  
ATOM   2115  O   MET D 343      23.990 -25.851 -74.671  1.00 19.19           O  
ANISOU 2115  O   MET D 343     2425   2225   2641   -139    169     67       O  
ATOM   2116  CB  MET D 343      24.655 -28.581 -76.357  1.00 19.47           C  
ANISOU 2116  CB  MET D 343     2484   2288   2624     12    248    -65       C  
ATOM   2117  CG  MET D 343      24.090 -29.106 -75.050  1.00 22.04           C  
ANISOU 2117  CG  MET D 343     2859   2535   2981    -23    146    -77       C  
ATOM   2118  SD  MET D 343      22.291 -29.013 -75.057  1.00 23.09           S  
ANISOU 2118  SD  MET D 343     3095   2668   3010    -73    107    -87       S  
ATOM   2119  CE  MET D 343      21.895 -29.803 -73.503  1.00 24.10           C  
ANISOU 2119  CE  MET D 343     3260   2720   3178   -108     -8    -98       C  
ATOM   2120  N   GLY D 344      25.977 -25.783 -75.722  1.00 19.12           N  
ANISOU 2120  N   GLY D 344     2285   2283   2697    -74    266    104       N  
ATOM   2121  CA  GLY D 344      26.561 -24.838 -74.790  1.00 19.34           C  
ANISOU 2121  CA  GLY D 344     2262   2279   2807   -122    222    168       C  
ATOM   2122  C   GLY D 344      25.838 -23.505 -74.799  1.00 21.47           C  
ANISOU 2122  C   GLY D 344     2547   2557   3053   -181    211    213       C  
ATOM   2123  O   GLY D 344      25.615 -22.908 -73.746  1.00 17.30           O  
ANISOU 2123  O   GLY D 344     2036   1976   2562   -230    148    228       O  
ATOM   2124  N   LEU D 345      25.473 -23.036 -75.990  1.00 19.08           N  
ANISOU 2124  N   LEU D 345     2239   2321   2689   -178    272    232       N  
ATOM   2125  CA  LEU D 345      24.778 -21.762 -76.118  1.00 19.75           C  
ANISOU 2125  CA  LEU D 345     2331   2410   2763   -232    260    280       C  
ATOM   2126  C   LEU D 345      23.396 -21.852 -75.486  1.00 19.34           C  
ANISOU 2126  C   LEU D 345     2369   2309   2672   -257    211    237       C  
ATOM   2127  O   LEU D 345      22.987 -20.965 -74.734  1.00 18.51           O  
ANISOU 2127  O   LEU D 345     2273   2159   2600   -300    165    255       O  
ATOM   2128  CB  LEU D 345      24.667 -21.342 -77.589  1.00 18.11           C  
ANISOU 2128  CB  LEU D 345     2096   2290   2495   -230    330    318       C  
ATOM   2129  CG  LEU D 345      25.956 -20.921 -78.304  1.00 23.03           C  
ANISOU 2129  CG  LEU D 345     2616   2984   3152   -219    383    384       C  
ATOM   2130  CD1 LEU D 345      25.672 -20.534 -79.743  1.00 23.45           C  
ANISOU 2130  CD1 LEU D 345     2650   3133   3126   -229    448    422       C  
ATOM   2131  CD2 LEU D 345      26.618 -19.771 -77.580  1.00 25.56           C  
ANISOU 2131  CD2 LEU D 345     2874   3266   3572   -265    332    461       C  
ATOM   2132  N   LEU D 346      22.689 -22.938 -75.786  1.00 16.97           N  
ANISOU 2132  N   LEU D 346     2131   2016   2301   -229    220    179       N  
ATOM   2133  CA  LEU D 346      21.343 -23.162 -75.265  1.00 14.41           C  
ANISOU 2133  CA  LEU D 346     1887   1657   1932   -251    176    145       C  
ATOM   2134  C   LEU D 346      21.332 -23.352 -73.754  1.00 13.03           C  
ANISOU 2134  C   LEU D 346     1731   1417   1801   -271    105    122       C  
ATOM   2135  O   LEU D 346      20.430 -22.877 -73.070  1.00 14.34           O  
ANISOU 2135  O   LEU D 346     1933   1557   1958   -306     70    118       O  
ATOM   2136  CB  LEU D 346      20.702 -24.376 -75.938  1.00 15.70           C  
ANISOU 2136  CB  LEU D 346     2111   1840   2013   -219    191     96       C  
ATOM   2137  CG  LEU D 346      20.445 -24.223 -77.437  1.00 17.01           C  
ANISOU 2137  CG  LEU D 346     2278   2075   2108   -211    255    113       C  
ATOM   2138  CD1 LEU D 346      19.895 -25.503 -78.029  1.00 18.97           C  
ANISOU 2138  CD1 LEU D 346     2597   2334   2277   -180    259     55       C  
ATOM   2139  CD2 LEU D 346      19.507 -23.062 -77.697  1.00 20.82           C  
ANISOU 2139  CD2 LEU D 346     2765   2568   2576   -261    252    167       C  
ATOM   2140  N   THR D 347      22.330 -24.061 -73.241  1.00 12.84           N  
ANISOU 2140  N   THR D 347     1681   1372   1826   -251     87    107       N  
ATOM   2141  CA  THR D 347      22.429 -24.315 -71.810  1.00 13.88           C  
ANISOU 2141  CA  THR D 347     1827   1449   1997   -280     14     92       C  
ATOM   2142  C   THR D 347      22.678 -23.027 -71.034  1.00 14.19           C  
ANISOU 2142  C   THR D 347     1840   1463   2087   -328    -13    128       C  
ATOM   2143  O   THR D 347      22.039 -22.775 -70.013  1.00 16.67           O  
ANISOU 2143  O   THR D 347     2194   1747   2392   -367    -61    109       O  
ATOM   2144  CB  THR D 347      23.544 -25.325 -71.503  1.00 17.43           C  
ANISOU 2144  CB  THR D 347     2241   1878   2502   -252     -5     82       C  
ATOM   2145  OG1 THR D 347      23.180 -26.605 -72.037  1.00 16.04           O  
ANISOU 2145  OG1 THR D 347     2104   1707   2282   -208      3     35       O  
ATOM   2146  CG2 THR D 347      23.759 -25.453 -70.006  1.00 16.69           C  
ANISOU 2146  CG2 THR D 347     2154   1733   2454   -297    -86     84       C  
ATOM   2147  N   ASN D 348      23.601 -22.208 -71.528  1.00 14.23           N  
ANISOU 2147  N   ASN D 348     1779   1483   2145   -327     17    179       N  
ATOM   2148  CA  ASN D 348      23.866 -20.912 -70.908  1.00 13.49           C  
ANISOU 2148  CA  ASN D 348     1662   1357   2106   -373    -16    216       C  
ATOM   2149  C   ASN D 348      22.647 -19.987 -70.968  1.00 13.13           C  
ANISOU 2149  C   ASN D 348     1657   1305   2027   -397    -15    208       C  
ATOM   2150  O   ASN D 348      22.372 -19.256 -70.016  1.00 14.65           O  
ANISOU 2150  O   ASN D 348     1871   1454   2243   -433    -60    197       O  
ATOM   2151  CB  ASN D 348      25.074 -20.241 -71.567  1.00 17.81           C  
ANISOU 2151  CB  ASN D 348     2123   1927   2716   -369     12    287       C  
ATOM   2152  CG  ASN D 348      25.346 -18.857 -71.012  1.00 23.31           C  
ANISOU 2152  CG  ASN D 348     2799   2584   3476   -420    -32    331       C  
ATOM   2153  OD1 ASN D 348      24.811 -17.872 -71.504  1.00 18.99           O  
ANISOU 2153  OD1 ASN D 348     2250   2041   2925   -436    -21    354       O  
ATOM   2154  ND2 ASN D 348      26.161 -18.782 -69.965  1.00 28.80           N  
ANISOU 2154  ND2 ASN D 348     3479   3233   4231   -451    -91    343       N  
ATOM   2155  N   LEU D 349      21.919 -20.034 -72.082  1.00 12.47           N  
ANISOU 2155  N   LEU D 349     1584   1264   1889   -375     34    212       N  
ATOM   2156  CA  LEU D 349      20.678 -19.278 -72.234  1.00 12.17           C  
ANISOU 2156  CA  LEU D 349     1579   1220   1824   -393     36    210       C  
ATOM   2157  C   LEU D 349      19.649 -19.700 -71.190  1.00 14.63           C  
ANISOU 2157  C   LEU D 349     1958   1504   2098   -404     -1    152       C  
ATOM   2158  O   LEU D 349      19.087 -18.862 -70.477  1.00 12.95           O  
ANISOU 2158  O   LEU D 349     1761   1257   1904   -428    -26    139       O  
ATOM   2159  CB  LEU D 349      20.115 -19.462 -73.646  1.00 12.20           C  
ANISOU 2159  CB  LEU D 349     1585   1281   1771   -374     91    232       C  
ATOM   2160  CG  LEU D 349      18.733 -18.881 -73.956  1.00 16.36           C  
ANISOU 2160  CG  LEU D 349     2144   1805   2267   -391     93    239       C  
ATOM   2161  CD1 LEU D 349      18.741 -17.373 -73.803  1.00 16.65           C  
ANISOU 2161  CD1 LEU D 349     2143   1806   2379   -421     74    280       C  
ATOM   2162  CD2 LEU D 349      18.307 -19.289 -75.365  1.00 16.11           C  
ANISOU 2162  CD2 LEU D 349     2118   1835   2168   -379    141    263       C  
ATOM   2163  N   ALA D 350      19.423 -21.004 -71.095  1.00 11.70           N  
ANISOU 2163  N   ALA D 350     1622   1148   1674   -385     -6    118       N  
ATOM   2164  CA  ALA D 350      18.488 -21.547 -70.118  1.00 12.09           C  
ANISOU 2164  CA  ALA D 350     1727   1185   1680   -400    -45     74       C  
ATOM   2165  C   ALA D 350      18.932 -21.251 -68.691  1.00 12.49           C  
ANISOU 2165  C   ALA D 350     1780   1199   1768   -435    -97     54       C  
ATOM   2166  O   ALA D 350      18.099 -21.008 -67.822  1.00 12.70           O  
ANISOU 2166  O   ALA D 350     1841   1217   1768   -458   -120     24       O  
ATOM   2167  CB  ALA D 350      18.328 -23.035 -70.314  1.00 10.96           C  
ANISOU 2167  CB  ALA D 350     1617   1061   1487   -378    -54     52       C  
ATOM   2168  N   ASP D 351      20.236 -21.284 -68.444  1.00 11.76           N  
ANISOU 2168  N   ASP D 351     1648   1088   1734   -440   -114     73       N  
ATOM   2169  CA  ASP D 351      20.745 -20.942 -67.118  1.00 13.31           C  
ANISOU 2169  CA  ASP D 351     1845   1247   1965   -483   -170     62       C  
ATOM   2170  C   ASP D 351      20.285 -19.549 -66.715  1.00 13.42           C  
ANISOU 2170  C   ASP D 351     1870   1235   1996   -508   -175     51       C  
ATOM   2171  O   ASP D 351      19.818 -19.335 -65.595  1.00 12.77           O  
ANISOU 2171  O   ASP D 351     1824   1137   1891   -540   -209     10       O  
ATOM   2172  CB  ASP D 351      22.272 -21.005 -67.074  1.00 14.52           C  
ANISOU 2172  CB  ASP D 351     1942   1382   2191   -488   -188    101       C  
ATOM   2173  CG  ASP D 351      22.808 -22.428 -67.070  1.00 18.76           C  
ANISOU 2173  CG  ASP D 351     2470   1928   2730   -468   -202    100       C  
ATOM   2174  OD1 ASP D 351      22.038 -23.381 -66.832  1.00 17.32           O  
ANISOU 2174  OD1 ASP D 351     2332   1757   2492   -464   -219     66       O  
ATOM   2175  OD2 ASP D 351      24.029 -22.584 -67.299  1.00 20.13           O  
ANISOU 2175  OD2 ASP D 351     2586   2093   2968   -455   -201    137       O  
ATOM   2176  N   ARG D 352      20.400 -18.610 -67.646  1.00 12.19           N  
ANISOU 2176  N   ARG D 352     1678   1075   1879   -494   -140     88       N  
ATOM   2177  CA  ARG D 352      20.070 -17.221 -67.358  1.00 12.41           C  
ANISOU 2177  CA  ARG D 352     1707   1062   1945   -513   -152     83       C  
ATOM   2178  C   ARG D 352      18.563 -16.993 -67.320  1.00 12.27           C  
ANISOU 2178  C   ARG D 352     1730   1052   1879   -502   -131     43       C  
ATOM   2179  O   ARG D 352      18.085 -16.148 -66.563  1.00 13.04           O  
ANISOU 2179  O   ARG D 352     1849   1114   1992   -517   -149      4       O  
ATOM   2180  CB  ARG D 352      20.735 -16.289 -68.376  1.00 12.77           C  
ANISOU 2180  CB  ARG D 352     1694   1101   2059   -509   -135    150       C  
ATOM   2181  CG  ARG D 352      22.233 -16.133 -68.147  1.00 13.84           C  
ANISOU 2181  CG  ARG D 352     1782   1217   2260   -530   -168    195       C  
ATOM   2182  CD  ARG D 352      22.887 -15.251 -69.192  1.00 14.51           C  
ANISOU 2182  CD  ARG D 352     1799   1307   2407   -531   -152    275       C  
ATOM   2183  NE  ARG D 352      23.030 -15.941 -70.472  1.00 14.53           N  
ANISOU 2183  NE  ARG D 352     1765   1380   2375   -495    -89    312       N  
ATOM   2184  CZ  ARG D 352      22.436 -15.567 -71.601  1.00 15.94           C  
ANISOU 2184  CZ  ARG D 352     1927   1594   2534   -483    -47    343       C  
ATOM   2185  NH1 ARG D 352      21.649 -14.498 -71.624  1.00 13.77           N  
ANISOU 2185  NH1 ARG D 352     1663   1283   2286   -502    -64    347       N  
ATOM   2186  NH2 ARG D 352      22.632 -16.266 -72.710  1.00 15.84           N  
ANISOU 2186  NH2 ARG D 352     1889   1651   2478   -455     10    368       N  
ATOM   2187  N   GLU D 353      17.817 -17.749 -68.120  1.00 11.37           N  
ANISOU 2187  N   GLU D 353     1627    983   1710   -475    -93     51       N  
ATOM   2188  CA  GLU D 353      16.361 -17.652 -68.090  1.00 11.13           C  
ANISOU 2188  CA  GLU D 353     1629    965   1635   -466    -76     25       C  
ATOM   2189  C   GLU D 353      15.782 -18.112 -66.757  1.00 11.57           C  
ANISOU 2189  C   GLU D 353     1728   1027   1639   -483   -103    -34       C  
ATOM   2190  O   GLU D 353      14.784 -17.567 -66.287  1.00 12.66           O  
ANISOU 2190  O   GLU D 353     1884   1160   1764   -482    -95    -67       O  
ATOM   2191  CB  GLU D 353      15.729 -18.468 -69.213  1.00 10.90           C  
ANISOU 2191  CB  GLU D 353     1606    983   1552   -443    -41     54       C  
ATOM   2192  CG  GLU D 353      15.913 -17.889 -70.598  1.00 10.99           C  
ANISOU 2192  CG  GLU D 353     1578   1004   1594   -432     -6    114       C  
ATOM   2193  CD  GLU D 353      15.287 -18.776 -71.652  1.00 18.38           C  
ANISOU 2193  CD  GLU D 353     2532   1988   2462   -416     23    135       C  
ATOM   2194  OE1 GLU D 353      15.918 -19.784 -72.030  1.00 14.77           O  
ANISOU 2194  OE1 GLU D 353     2080   1558   1973   -402     30    133       O  
ATOM   2195  OE2 GLU D 353      14.148 -18.482 -72.071  1.00 18.60           O  
ANISOU 2195  OE2 GLU D 353     2572   2025   2472   -418     36    152       O  
ATOM   2196  N   LEU D 354      16.403 -19.117 -66.151  1.00 11.98           N  
ANISOU 2196  N   LEU D 354     1794   1094   1665   -500   -136    -44       N  
ATOM   2197  CA  LEU D 354      15.861 -19.684 -64.924  1.00 15.80           C  
ANISOU 2197  CA  LEU D 354     2317   1599   2090   -526   -167    -88       C  
ATOM   2198  C   LEU D 354      15.879 -18.658 -63.796  1.00 13.37           C  
ANISOU 2198  C   LEU D 354     2021   1260   1797   -554   -186   -136       C  
ATOM   2199  O   LEU D 354      14.971 -18.620 -62.964  1.00 11.57           O  
ANISOU 2199  O   LEU D 354     1822   1057   1516   -565   -186   -182       O  
ATOM   2200  CB  LEU D 354      16.633 -20.944 -64.525  1.00 14.87           C  
ANISOU 2200  CB  LEU D 354     2203   1494   1955   -546   -211    -78       C  
ATOM   2201  CG  LEU D 354      16.169 -21.659 -63.250  1.00 14.93           C  
ANISOU 2201  CG  LEU D 354     2244   1532   1897   -587   -256   -108       C  
ATOM   2202  CD1 LEU D 354      14.786 -22.232 -63.442  1.00 13.61           C  
ANISOU 2202  CD1 LEU D 354     2100   1413   1659   -574   -240   -110       C  
ATOM   2203  CD2 LEU D 354      17.142 -22.759 -62.864  1.00 15.60           C  
ANISOU 2203  CD2 LEU D 354     2310   1623   1993   -594   -303    -85       C  
ATOM   2204  N   VAL D 355      16.903 -17.811 -63.777  1.00 14.71           N  
ANISOU 2204  N   VAL D 355     2170   1380   2040   -565   -203   -127       N  
ATOM   2205  CA  VAL D 355      16.976 -16.773 -62.763  1.00 13.27           C  
ANISOU 2205  CA  VAL D 355     2007   1158   1878   -592   -227   -177       C  
ATOM   2206  C   VAL D 355      15.773 -15.837 -62.866  1.00 12.66           C  
ANISOU 2206  C   VAL D 355     1938   1070   1803   -563   -189   -217       C  
ATOM   2207  O   VAL D 355      15.137 -15.526 -61.862  1.00 14.05           O  
ANISOU 2207  O   VAL D 355     2146   1251   1940   -573   -190   -284       O  
ATOM   2208  CB  VAL D 355      18.275 -15.970 -62.874  1.00 16.31           C  
ANISOU 2208  CB  VAL D 355     2360   1486   2349   -606   -258   -146       C  
ATOM   2209  CG1 VAL D 355      18.388 -15.009 -61.709  1.00 17.66           C  
ANISOU 2209  CG1 VAL D 355     2549   1630   2530   -620   -282   -205       C  
ATOM   2210  CG2 VAL D 355      19.464 -16.912 -62.895  1.00 15.76           C  
ANISOU 2210  CG2 VAL D 355     2261   1438   2287   -615   -281    -98       C  
ATOM   2211  N   HIS D 356      15.447 -15.416 -64.083  1.00 12.07           N  
ANISOU 2211  N   HIS D 356     1830    983   1772   -527   -153   -173       N  
ATOM   2212  CA  HIS D 356      14.269 -14.581 -64.306  1.00 12.24           C  
ANISOU 2212  CA  HIS D 356     1849    989   1811   -497   -118   -196       C  
ATOM   2213  C   HIS D 356      12.958 -15.327 -64.054  1.00 13.51           C  
ANISOU 2213  C   HIS D 356     2031   1213   1888   -482    -87   -219       C  
ATOM   2214  O   HIS D 356      11.971 -14.715 -63.649  1.00 15.30           O  
ANISOU 2214  O   HIS D 356     2263   1435   2113   -463    -63   -264       O  
ATOM   2215  CB  HIS D 356      14.273 -14.015 -65.729  1.00 12.18           C  
ANISOU 2215  CB  HIS D 356     1796    959   1872   -474    -97   -125       C  
ATOM   2216  CG  HIS D 356      15.368 -13.028 -65.977  1.00 12.61           C  
ANISOU 2216  CG  HIS D 356     1820    950   2020   -489   -129    -96       C  
ATOM   2217  ND1 HIS D 356      15.212 -11.674 -65.767  1.00 19.75           N  
ANISOU 2217  ND1 HIS D 356     2717   1782   3005   -486   -148   -120       N  
ATOM   2218  CD2 HIS D 356      16.638 -13.198 -66.416  1.00 12.61           C  
ANISOU 2218  CD2 HIS D 356     1792    949   2050   -508   -150    -39       C  
ATOM   2219  CE1 HIS D 356      16.341 -11.053 -66.063  1.00 20.79           C  
ANISOU 2219  CE1 HIS D 356     2819   1869   3212   -509   -186    -73       C  
ATOM   2220  NE2 HIS D 356      17.221 -11.955 -66.459  1.00 14.37           N  
ANISOU 2220  NE2 HIS D 356     1990   1104   2368   -522   -185    -21       N  
ATOM   2221  N   MET D 357      12.947 -16.633 -64.295  1.00 11.57           N  
ANISOU 2221  N   MET D 357     1794   1025   1578   -489    -90   -185       N  
ATOM   2222  CA  MET D 357      11.745 -17.433 -64.075  1.00 10.47           C  
ANISOU 2222  CA  MET D 357     1673    948   1358   -484    -73   -191       C  
ATOM   2223  C   MET D 357      11.335 -17.419 -62.611  1.00 15.29           C  
ANISOU 2223  C   MET D 357     2311   1588   1912   -506    -83   -261       C  
ATOM   2224  O   MET D 357      10.154 -17.388 -62.282  1.00 12.78           O  
ANISOU 2224  O   MET D 357     1995   1308   1551   -493    -55   -282       O  
ATOM   2225  CB  MET D 357      11.952 -18.877 -64.532  1.00 19.00           C  
ANISOU 2225  CB  MET D 357     2762   2071   2386   -493    -91   -145       C  
ATOM   2226  CG  MET D 357      10.681 -19.722 -64.464  1.00 15.16           C  
ANISOU 2226  CG  MET D 357     2291   1646   1823   -492    -85   -133       C  
ATOM   2227  SD  MET D 357      10.980 -21.482 -64.672  1.00 12.64           S  
ANISOU 2227  SD  MET D 357     1993   1365   1445   -511   -130    -94       S  
ATOM   2228  CE  MET D 357      11.787 -21.492 -66.265  1.00 12.42           C  
ANISOU 2228  CE  MET D 357     1948   1301   1472   -481   -110    -49       C  
ATOM   2229  N   ILE D 358      12.321 -17.445 -61.729  1.00 12.92           N  
ANISOU 2229  N   ILE D 358     2027   1272   1607   -544   -124   -292       N  
ATOM   2230  CA  ILE D 358      12.041 -17.411 -60.302  1.00 15.11           C  
ANISOU 2230  CA  ILE D 358     2335   1585   1821   -577   -138   -360       C  
ATOM   2231  C   ILE D 358      11.448 -16.070 -59.877  1.00 15.14           C  
ANISOU 2231  C   ILE D 358     2343   1556   1853   -550   -103   -433       C  
ATOM   2232  O   ILE D 358      10.521 -16.026 -59.067  1.00 16.46           O  
ANISOU 2232  O   ILE D 358     2524   1775   1956   -548    -77   -487       O  
ATOM   2233  CB  ILE D 358      13.314 -17.752 -59.514  1.00 16.16           C  
ANISOU 2233  CB  ILE D 358     2487   1706   1948   -633   -199   -365       C  
ATOM   2234  CG1 ILE D 358      13.461 -19.275 -59.515  1.00 27.15           C  
ANISOU 2234  CG1 ILE D 358     3865   3159   3290   -643   -228   -305       C  
ATOM   2235  CG2 ILE D 358      13.264 -17.182 -58.094  1.00 20.98           C  
ANISOU 2235  CG2 ILE D 358     3116   2336   2520   -650   -209   -437       C  
ATOM   2236  CD1 ILE D 358      14.809 -19.780 -59.142  1.00 32.59           C  
ANISOU 2236  CD1 ILE D 358     4532   3842   4011   -653   -275   -268       C  
ATOM   2237  N   ASN D 359      11.944 -14.984 -60.456  1.00 14.16           N  
ANISOU 2237  N   ASN D 359     2204   1349   1829   -528   -102   -432       N  
ATOM   2238  CA  ASN D 359      11.357 -13.675 -60.199  1.00 14.86           C  
ANISOU 2238  CA  ASN D 359     2291   1387   1966   -494    -74   -499       C  
ATOM   2239  C   ASN D 359       9.913 -13.634 -60.697  1.00 15.30           C  
ANISOU 2239  C   ASN D 359     2321   1476   2016   -444    -15   -490       C  
ATOM   2240  O   ASN D 359       9.036 -13.064 -60.047  1.00 18.01           O  
ANISOU 2240  O   ASN D 359     2668   1828   2347   -418     20   -562       O  
ATOM   2241  CB  ASN D 359      12.193 -12.578 -60.857  1.00 18.11           C  
ANISOU 2241  CB  ASN D 359     2685   1698   2499   -485    -99   -479       C  
ATOM   2242  CG  ASN D 359      11.574 -11.204 -60.713  1.00 28.40           C  
ANISOU 2242  CG  ASN D 359     3983   2933   3876   -445    -80   -544       C  
ATOM   2243  OD1 ASN D 359      10.779 -10.778 -61.551  1.00 33.07           O  
ANISOU 2243  OD1 ASN D 359     4537   3504   4523   -402    -46   -513       O  
ATOM   2244  ND2 ASN D 359      11.920 -10.510 -59.635  1.00 32.82           N  
ANISOU 2244  ND2 ASN D 359     4582   3452   4436   -462   -106   -635       N  
ATOM   2245  N   TRP D 360       9.664 -14.269 -61.838  1.00 15.13           N  
ANISOU 2245  N   TRP D 360     2272   1475   2001   -433     -4   -402       N  
ATOM   2246  CA  TRP D 360       8.321 -14.333 -62.405  1.00 13.55           C  
ANISOU 2246  CA  TRP D 360     2044   1307   1796   -395     42   -372       C  
ATOM   2247  C   TRP D 360       7.382 -15.153 -61.535  1.00 16.33           C  
ANISOU 2247  C   TRP D 360     2410   1754   2039   -403     61   -397       C  
ATOM   2248  O   TRP D 360       6.238 -14.758 -61.289  1.00 17.17           O  
ANISOU 2248  O   TRP D 360     2498   1885   2142   -370    106   -424       O  
ATOM   2249  CB  TRP D 360       8.366 -14.926 -63.813  1.00 12.74           C  
ANISOU 2249  CB  TRP D 360     1920   1211   1710   -394     39   -270       C  
ATOM   2250  CG  TRP D 360       7.047 -15.459 -64.284  1.00 12.51           C  
ANISOU 2250  CG  TRP D 360     1875   1236   1642   -376     69   -223       C  
ATOM   2251  CD1 TRP D 360       6.014 -14.743 -64.809  1.00 13.95           C  
ANISOU 2251  CD1 TRP D 360     2022   1399   1880   -341    104   -202       C  
ATOM   2252  CD2 TRP D 360       6.615 -16.833 -64.264  1.00 12.03           C  
ANISOU 2252  CD2 TRP D 360     1832   1255   1486   -397     58   -183       C  
ATOM   2253  NE1 TRP D 360       4.966 -15.580 -65.120  1.00 14.65           N  
ANISOU 2253  NE1 TRP D 360     2104   1553   1909   -341    117   -147       N  
ATOM   2254  CE2 TRP D 360       5.309 -16.864 -64.794  1.00 16.89           C  
ANISOU 2254  CE2 TRP D 360     2422   1897   2099   -376     88   -136       C  
ATOM   2255  CE3 TRP D 360       7.206 -18.031 -63.848  1.00 14.29           C  
ANISOU 2255  CE3 TRP D 360     2148   1584   1696   -435     19   -178       C  
ATOM   2256  CZ2 TRP D 360       4.583 -18.051 -64.922  1.00 15.77           C  
ANISOU 2256  CZ2 TRP D 360     2290   1827   1876   -393     76    -83       C  
ATOM   2257  CZ3 TRP D 360       6.484 -19.210 -63.979  1.00 14.90           C  
ANISOU 2257  CZ3 TRP D 360     2235   1728   1699   -449      5   -129       C  
ATOM   2258  CH2 TRP D 360       5.185 -19.210 -64.512  1.00 14.58           C  
ANISOU 2258  CH2 TRP D 360     2173   1715   1652   -429     32    -82       C  
ATOM   2259  N   ALA D 361       7.869 -16.305 -61.084  1.00 13.36           N  
ANISOU 2259  N   ALA D 361     2060   1435   1581   -449     25   -381       N  
ATOM   2260  CA  ALA D 361       7.073 -17.214 -60.274  1.00 16.87           C  
ANISOU 2260  CA  ALA D 361     2514   1979   1917   -471     28   -386       C  
ATOM   2261  C   ALA D 361       6.600 -16.527 -59.001  1.00 20.23           C  
ANISOU 2261  C   ALA D 361     2948   2434   2304   -467     59   -484       C  
ATOM   2262  O   ALA D 361       5.455 -16.681 -58.584  1.00 15.00           O  
ANISOU 2262  O   ALA D 361     2270   1846   1585   -453     98   -494       O  
ATOM   2263  CB  ALA D 361       7.872 -18.452 -59.943  1.00 12.00           C  
ANISOU 2263  CB  ALA D 361     1922   1399   1238   -527    -32   -355       C  
ATOM   2264  N   LYS D 362       7.482 -15.742 -58.398  1.00 16.95           N  
ANISOU 2264  N   LYS D 362     2558   1962   1919   -479     42   -556       N  
ATOM   2265  CA  LYS D 362       7.143 -15.046 -57.165  1.00 16.84           C  
ANISOU 2265  CA  LYS D 362     2565   1971   1864   -477     69   -665       C  
ATOM   2266  C   LYS D 362       6.081 -13.969 -57.384  1.00 16.62           C  
ANISOU 2266  C   LYS D 362     2505   1912   1897   -404    137   -712       C  
ATOM   2267  O   LYS D 362       5.459 -13.512 -56.430  1.00 21.42           O  
ANISOU 2267  O   LYS D 362     3119   2560   2459   -387    179   -803       O  
ATOM   2268  CB  LYS D 362       8.396 -14.436 -56.538  1.00 19.08           C  
ANISOU 2268  CB  LYS D 362     2889   2188   2172   -513     23   -726       C  
ATOM   2269  CG  LYS D 362       9.314 -15.467 -55.899  1.00 23.35           C  
ANISOU 2269  CG  LYS D 362     3460   2776   2636   -593    -42   -698       C  
ATOM   2270  CD  LYS D 362      10.662 -14.868 -55.525  1.00 24.44           C  
ANISOU 2270  CD  LYS D 362     3630   2834   2823   -628    -97   -728       C  
ATOM   2271  CE  LYS D 362      10.624 -14.215 -54.148  1.00 32.67           C  
ANISOU 2271  CE  LYS D 362     4699   3900   3815   -631    -98   -820       C  
ATOM   2272  NZ  LYS D 362      11.929 -14.335 -53.425  1.00 36.52           N  
ANISOU 2272  NZ  LYS D 362     5195   4374   4307   -669   -173   -791       N  
ATOM   2273  N   ARG D 363       5.863 -13.575 -58.636  1.00 16.40           N  
ANISOU 2273  N   ARG D 363     2440   1818   1972   -361    148   -649       N  
ATOM   2274  CA  ARG D 363       4.834 -12.583 -58.946  1.00 16.64           C  
ANISOU 2274  CA  ARG D 363     2430   1810   2081   -292    205   -677       C  
ATOM   2275  C   ARG D 363       3.533 -13.185 -59.479  1.00 21.86           C  
ANISOU 2275  C   ARG D 363     3045   2543   2716   -267    246   -602       C  
ATOM   2276  O   ARG D 363       2.574 -12.458 -59.751  1.00 23.12           O  
ANISOU 2276  O   ARG D 363     3161   2679   2943   -210    294   -611       O  
ATOM   2277  CB  ARG D 363       5.362 -11.560 -59.949  1.00 22.23           C  
ANISOU 2277  CB  ARG D 363     3120   2390   2935   -266    184   -652       C  
ATOM   2278  CG  ARG D 363       6.522 -10.732 -59.433  1.00 23.44           C  
ANISOU 2278  CG  ARG D 363     3312   2459   3135   -284    140   -725       C  
ATOM   2279  CD  ARG D 363       6.943  -9.709 -60.466  1.00 28.19           C  
ANISOU 2279  CD  ARG D 363     3885   2940   3887   -261    114   -685       C  
ATOM   2280  NE  ARG D 363       5.864  -8.767 -60.755  1.00 31.58           N  
ANISOU 2280  NE  ARG D 363     4271   3322   4408   -196    157   -708       N  
ATOM   2281  CZ  ARG D 363       6.005  -7.663 -61.481  1.00 32.48           C  
ANISOU 2281  CZ  ARG D 363     4352   3322   4666   -171    133   -688       C  
ATOM   2282  NH1 ARG D 363       7.183  -7.350 -62.004  1.00 30.55           N  
ANISOU 2282  NH1 ARG D 363     4115   3010   4482   -207     71   -641       N  
ATOM   2283  NH2 ARG D 363       4.962  -6.873 -61.686  1.00 31.65           N  
ANISOU 2283  NH2 ARG D 363     4203   3174   4650   -110    170   -708       N  
ATOM   2284  N   VAL D 364       3.498 -14.502 -59.639  1.00 19.67           N  
ANISOU 2284  N   VAL D 364     2776   2347   2351   -311    221   -523       N  
ATOM   2285  CA  VAL D 364       2.250 -15.177 -59.962  1.00 19.49           C  
ANISOU 2285  CA  VAL D 364     2715   2403   2286   -300    249   -451       C  
ATOM   2286  C   VAL D 364       1.378 -15.160 -58.715  1.00 17.78           C  
ANISOU 2286  C   VAL D 364     2488   2283   1986   -289    298   -521       C  
ATOM   2287  O   VAL D 364       1.784 -15.696 -57.683  1.00 17.60           O  
ANISOU 2287  O   VAL D 364     2498   2327   1860   -336    279   -564       O  
ATOM   2288  CB  VAL D 364       2.474 -16.630 -60.416  1.00 16.36           C  
ANISOU 2288  CB  VAL D 364     2336   2061   1817   -353    196   -352       C  
ATOM   2289  CG1 VAL D 364       1.138 -17.335 -60.600  1.00 15.38           C  
ANISOU 2289  CG1 VAL D 364     2177   2023   1642   -349    215   -277       C  
ATOM   2290  CG2 VAL D 364       3.306 -16.676 -61.691  1.00 15.68           C  
ANISOU 2290  CG2 VAL D 364     2259   1893   1805   -359    158   -289       C  
ATOM   2291  N   PRO D 365       0.198 -14.522 -58.792  1.00 18.05           N  
ANISOU 2291  N   PRO D 365     2470   2326   2064   -229    363   -531       N  
ATOM   2292  CA  PRO D 365      -0.677 -14.407 -57.620  1.00 22.27           C  
ANISOU 2292  CA  PRO D 365     2982   2958   2520   -208    425   -605       C  
ATOM   2293  C   PRO D 365      -0.906 -15.745 -56.927  1.00 21.78           C  
ANISOU 2293  C   PRO D 365     2930   3039   2306   -273    404   -559       C  
ATOM   2294  O   PRO D 365      -1.268 -16.718 -57.585  1.00 26.21           O  
ANISOU 2294  O   PRO D 365     3476   3639   2843   -301    369   -440       O  
ATOM   2295  CB  PRO D 365      -1.980 -13.870 -58.215  1.00 26.75           C  
ANISOU 2295  CB  PRO D 365     3477   3517   3171   -139    486   -566       C  
ATOM   2296  CG  PRO D 365      -1.528 -13.056 -59.376  1.00 21.61           C  
ANISOU 2296  CG  PRO D 365     2820   2720   2669   -111    461   -537       C  
ATOM   2297  CD  PRO D 365      -0.359 -13.819 -59.961  1.00 19.08           C  
ANISOU 2297  CD  PRO D 365     2551   2373   2324   -177    382   -474       C  
ATOM   2298  N   GLY D 366      -0.660 -15.794 -55.622  1.00 22.83           N  
ANISOU 2298  N   GLY D 366     3091   3246   2336   -303    414   -650       N  
ATOM   2299  CA  GLY D 366      -0.876 -17.007 -54.862  1.00 23.82           C  
ANISOU 2299  CA  GLY D 366     3220   3514   2317   -373    388   -605       C  
ATOM   2300  C   GLY D 366       0.372 -17.837 -54.619  1.00 23.66           C  
ANISOU 2300  C   GLY D 366     3258   3488   2243   -458    297   -583       C  
ATOM   2301  O   GLY D 366       0.417 -18.624 -53.671  1.00 22.20           O  
ANISOU 2301  O   GLY D 366     3085   3414   1936   -525    269   -578       O  
ATOM   2302  N   PHE D 367       1.392 -17.662 -55.456  1.00 21.97           N  
ANISOU 2302  N   PHE D 367     3076   3150   2122   -457    249   -566       N  
ATOM   2303  CA  PHE D 367       2.578 -18.518 -55.390  1.00 19.26           C  
ANISOU 2303  CA  PHE D 367     2777   2793   1749   -530    162   -530       C  
ATOM   2304  C   PHE D 367       3.412 -18.313 -54.120  1.00 19.06           C  
ANISOU 2304  C   PHE D 367     2796   2790   1657   -582    141   -622       C  
ATOM   2305  O   PHE D 367       3.848 -19.282 -53.503  1.00 19.47           O  
ANISOU 2305  O   PHE D 367     2867   2908   1624   -660     80   -588       O  
ATOM   2306  CB  PHE D 367       3.462 -18.305 -56.623  1.00 15.75           C  
ANISOU 2306  CB  PHE D 367     2346   2217   1422   -510    128   -491       C  
ATOM   2307  CG  PHE D 367       4.601 -19.287 -56.731  1.00 16.77           C  
ANISOU 2307  CG  PHE D 367     2507   2331   1534   -573     44   -440       C  
ATOM   2308  CD1 PHE D 367       4.374 -20.585 -57.155  1.00 15.93           C  
ANISOU 2308  CD1 PHE D 367     2394   2270   1388   -605     -4   -341       C  
ATOM   2309  CD2 PHE D 367       5.894 -18.912 -56.418  1.00 16.30           C  
ANISOU 2309  CD2 PHE D 367     2482   2204   1506   -598      8   -488       C  
ATOM   2310  CE1 PHE D 367       5.413 -21.493 -57.259  1.00 14.12           C  
ANISOU 2310  CE1 PHE D 367     2191   2019   1157   -654    -81   -300       C  
ATOM   2311  CE2 PHE D 367       6.940 -19.814 -56.519  1.00 14.18           C  
ANISOU 2311  CE2 PHE D 367     2234   1919   1234   -651    -67   -438       C  
ATOM   2312  CZ  PHE D 367       6.697 -21.104 -56.942  1.00 13.50           C  
ANISOU 2312  CZ  PHE D 367     2139   1877   1115   -675   -109   -347       C  
ATOM   2313  N   VAL D 368       3.639 -17.064 -53.724  1.00 18.02           N  
ANISOU 2313  N   VAL D 368     2681   2599   1565   -545    182   -736       N  
ATOM   2314  CA  VAL D 368       4.464 -16.816 -52.543  1.00 21.07           C  
ANISOU 2314  CA  VAL D 368     3119   2999   1887   -600    155   -826       C  
ATOM   2315  C   VAL D 368       3.676 -17.019 -51.256  1.00 23.66           C  
ANISOU 2315  C   VAL D 368     3440   3473   2077   -626    195   -875       C  
ATOM   2316  O   VAL D 368       4.219 -16.870 -50.163  1.00 24.98           O  
ANISOU 2316  O   VAL D 368     3629   3653   2208   -652    168   -910       O  
ATOM   2317  CB  VAL D 368       5.069 -15.397 -52.539  1.00 25.83           C  
ANISOU 2317  CB  VAL D 368     3753   3477   2584   -557    172   -932       C  
ATOM   2318  CG1 VAL D 368       5.935 -15.195 -53.753  1.00 25.51           C  
ANISOU 2318  CG1 VAL D 368     3712   3303   2677   -540    128   -868       C  
ATOM   2319  CG2 VAL D 368       3.977 -14.338 -52.467  1.00 24.64           C  
ANISOU 2319  CG2 VAL D 368     3574   3321   2467   -470    265  -1018       C  
ATOM   2320  N   ASP D 369       2.396 -17.355 -51.386  1.00 21.88           N  
ANISOU 2320  N   ASP D 369     3163   3344   1808   -597    251   -839       N  
ATOM   2321  CA  ASP D 369       1.585 -17.703 -50.227  1.00 24.29           C  
ANISOU 2321  CA  ASP D 369     3440   3797   1991   -617    284   -848       C  
ATOM   2322  C   ASP D 369       1.964 -19.095 -49.746  1.00 21.02           C  
ANISOU 2322  C   ASP D 369     3016   3445   1527   -698    190   -723       C  
ATOM   2323  O   ASP D 369       1.708 -19.466 -48.605  1.00 21.61           O  
ANISOU 2323  O   ASP D 369     3073   3615   1522   -733    186   -715       O  
ATOM   2324  CB  ASP D 369       0.091 -17.653 -50.553  1.00 26.21           C  
ANISOU 2324  CB  ASP D 369     3620   4129   2209   -562    373   -835       C  
ATOM   2325  CG  ASP D 369      -0.390 -16.256 -50.895  1.00 34.11           C  
ANISOU 2325  CG  ASP D 369     4602   5041   3317   -451    462   -933       C  
ATOM   2326  OD1 ASP D 369       0.131 -15.284 -50.306  1.00 36.44           O  
ANISOU 2326  OD1 ASP D 369     4941   5281   3624   -434    484  -1068       O  
ATOM   2327  OD2 ASP D 369      -1.292 -16.136 -51.751  1.00 36.27           O  
ANISOU 2327  OD2 ASP D 369     4817   5296   3668   -386    503   -872       O  
ATOM   2328  N   LEU D 370       2.572 -19.864 -50.642  1.00 20.02           N  
ANISOU 2328  N   LEU D 370     2895   3253   1458   -724    117   -626       N  
ATOM   2329  CA  LEU D 370       2.976 -21.230 -50.338  1.00 17.75           C  
ANISOU 2329  CA  LEU D 370     2590   2992   1162   -786     29   -505       C  
ATOM   2330  C   LEU D 370       4.257 -21.253 -49.518  1.00 17.99           C  
ANISOU 2330  C   LEU D 370     2651   2974   1208   -828    -26   -521       C  
ATOM   2331  O   LEU D 370       4.999 -20.271 -49.485  1.00 20.47           O  
ANISOU 2331  O   LEU D 370     3007   3211   1559   -809    -16   -606       O  
ATOM   2332  CB  LEU D 370       3.174 -22.021 -51.633  1.00 16.62           C  
ANISOU 2332  CB  LEU D 370     2441   2784   1090   -782    -23   -404       C  
ATOM   2333  CG  LEU D 370       1.964 -22.100 -52.577  1.00 16.19           C  
ANISOU 2333  CG  LEU D 370     2359   2769   1024   -748     18   -363       C  
ATOM   2334  CD1 LEU D 370       2.365 -22.700 -53.914  1.00 15.98           C  
ANISOU 2334  CD1 LEU D 370     2344   2655   1073   -742    -36   -282       C  
ATOM   2335  CD2 LEU D 370       0.818 -22.891 -51.955  1.00 19.65           C  
ANISOU 2335  CD2 LEU D 370     2740   3331   1396   -767     21   -291       C  
ATOM   2336  N   THR D 371       4.521 -22.374 -48.860  1.00 17.02           N  
ANISOU 2336  N   THR D 371     2506   2893   1069   -885    -86   -433       N  
ATOM   2337  CA  THR D 371       5.791 -22.553 -48.168  1.00 20.04           C  
ANISOU 2337  CA  THR D 371     2912   3229   1474   -929   -143   -424       C  
ATOM   2338  C   THR D 371       6.917 -22.547 -49.197  1.00 18.64           C  
ANISOU 2338  C   THR D 371     2756   2922   1403   -905   -184   -399       C  
ATOM   2339  O   THR D 371       6.683 -22.868 -50.360  1.00 18.29           O  
ANISOU 2339  O   THR D 371     2702   2840   1408   -872   -186   -356       O  
ATOM   2340  CB  THR D 371       5.818 -23.868 -47.378  1.00 18.34           C  
ANISOU 2340  CB  THR D 371     2662   3074   1234   -994   -194   -324       C  
ATOM   2341  OG1 THR D 371       5.797 -24.966 -48.300  1.00 17.25           O  
ANISOU 2341  OG1 THR D 371     2497   2894   1164   -985   -235   -220       O  
ATOM   2342  CG2 THR D 371       4.615 -23.959 -46.442  1.00 18.35           C  
ANISOU 2342  CG2 THR D 371     2628   3213   1131  -1021   -154   -335       C  
ATOM   2343  N   LEU D 372       8.131 -22.184 -48.792  1.00 16.40           N  
ANISOU 2343  N   LEU D 372     1985   2921   1325   -692   -304   -544       N  
ATOM   2344  CA  LEU D 372       9.238 -22.204 -49.745  1.00 15.05           C  
ANISOU 2344  CA  LEU D 372     1805   2669   1244   -652   -360   -500       C  
ATOM   2345  C   LEU D 372       9.512 -23.614 -50.244  1.00 18.12           C  
ANISOU 2345  C   LEU D 372     2234   3061   1591   -670   -380   -383       C  
ATOM   2346  O   LEU D 372       9.874 -23.797 -51.404  1.00 19.47           O  
ANISOU 2346  O   LEU D 372     2401   3137   1860   -650   -390   -354       O  
ATOM   2347  CB  LEU D 372      10.526 -21.615 -49.162  1.00 19.97           C  
ANISOU 2347  CB  LEU D 372     2392   3335   1860   -625   -430   -518       C  
ATOM   2348  CG  LEU D 372      10.564 -20.118 -48.862  1.00 25.15           C  
ANISOU 2348  CG  LEU D 372     3004   3964   2589   -607   -428   -625       C  
ATOM   2349  CD1 LEU D 372      11.876 -19.775 -48.185  1.00 31.23           C  
ANISOU 2349  CD1 LEU D 372     3744   4791   3332   -592   -500   -636       C  
ATOM   2350  CD2 LEU D 372      10.381 -19.303 -50.134  1.00 31.37           C  
ANISOU 2350  CD2 LEU D 372     3781   4602   3538   -578   -409   -644       C  
ATOM   2351  N   HIS D 373       9.334 -24.608 -49.379  1.00 18.29           N  
ANISOU 2351  N   HIS D 373     2296   3187   1465   -708   -385   -304       N  
ATOM   2352  CA  HIS D 373       9.492 -25.994 -49.811  1.00 17.73           C  
ANISOU 2352  CA  HIS D 373     2272   3084   1383   -707   -394   -161       C  
ATOM   2353  C   HIS D 373       8.558 -26.332 -50.969  1.00 17.81           C  
ANISOU 2353  C   HIS D 373     2299   2959   1507   -703   -318   -164       C  
ATOM   2354  O   HIS D 373       8.964 -26.955 -51.950  1.00 16.68           O  
ANISOU 2354  O   HIS D 373     2159   2711   1467   -663   -321    -97       O  
ATOM   2355  CB  HIS D 373       9.234 -26.971 -48.665  1.00 22.66           C  
ANISOU 2355  CB  HIS D 373     2946   3805   1860   -729   -385    -49       C  
ATOM   2356  CG  HIS D 373       9.025 -28.377 -49.132  1.00 25.90           C  
ANISOU 2356  CG  HIS D 373     3401   4118   2324   -707   -350     98       C  
ATOM   2357  ND1 HIS D 373      10.063 -29.179 -49.553  1.00 33.22           N  
ANISOU 2357  ND1 HIS D 373     4325   4976   3321   -651   -405    213       N  
ATOM   2358  CD2 HIS D 373       7.896 -29.109 -49.290  1.00 30.17           C  
ANISOU 2358  CD2 HIS D 373     3980   4606   2876   -732   -264    138       C  
ATOM   2359  CE1 HIS D 373       9.586 -30.351 -49.932  1.00 33.77           C  
ANISOU 2359  CE1 HIS D 373     4429   4955   3446   -643   -357    316       C  
ATOM   2360  NE2 HIS D 373       8.273 -30.334 -49.787  1.00 34.42           N  
ANISOU 2360  NE2 HIS D 373     4539   5045   3494   -693   -270    275       N  
ATOM   2361  N   ASP D 374       7.297 -25.936 -50.838  1.00 16.31           N  
ANISOU 2361  N   ASP D 374     2115   2780   1300   -745   -252   -252       N  
ATOM   2362  CA  ASP D 374       6.319 -26.220 -51.873  1.00 14.22           C  
ANISOU 2362  CA  ASP D 374     1862   2400   1139   -743   -187   -267       C  
ATOM   2363  C   ASP D 374       6.578 -25.382 -53.125  1.00 15.95           C  
ANISOU 2363  C   ASP D 374     2045   2524   1492   -715   -208   -339       C  
ATOM   2364  O   ASP D 374       6.319 -25.841 -54.236  1.00 14.02           O  
ANISOU 2364  O   ASP D 374     1810   2175   1341   -692   -182   -311       O  
ATOM   2365  CB  ASP D 374       4.903 -25.996 -51.347  1.00 14.53           C  
ANISOU 2365  CB  ASP D 374     1909   2482   1131   -796   -113   -350       C  
ATOM   2366  CG  ASP D 374       4.444 -27.117 -50.422  1.00 20.69           C  
ANISOU 2366  CG  ASP D 374     2736   3325   1801   -827    -65   -249       C  
ATOM   2367  OD1 ASP D 374       5.080 -28.193 -50.420  1.00 21.49           O  
ANISOU 2367  OD1 ASP D 374     2869   3402   1896   -801    -86   -103       O  
ATOM   2368  OD2 ASP D 374       3.440 -26.933 -49.704  1.00 22.09           O  
ANISOU 2368  OD2 ASP D 374     2916   3573   1905   -881     -4   -313       O  
ATOM   2369  N   GLN D 375       7.106 -24.170 -52.948  1.00 15.75           N  
ANISOU 2369  N   GLN D 375     1977   2506   1503   -680   -238   -403       N  
ATOM   2370  CA  GLN D 375       7.504 -23.354 -54.094  1.00 13.09           C  
ANISOU 2370  CA  GLN D 375     1612   2057   1306   -618   -250   -421       C  
ATOM   2371  C   GLN D 375       8.627 -24.030 -54.872  1.00 12.75           C  
ANISOU 2371  C   GLN D 375     1569   1984   1290   -613   -292   -350       C  
ATOM   2372  O   GLN D 375       8.601 -24.074 -56.106  1.00 12.75           O  
ANISOU 2372  O   GLN D 375     1569   1893   1383   -586   -276   -337       O  
ATOM   2373  CB  GLN D 375       7.956 -21.959 -53.664  1.00 13.41           C  
ANISOU 2373  CB  GLN D 375     1614   2098   1384   -583   -277   -481       C  
ATOM   2374  CG  GLN D 375       6.874 -21.089 -53.064  1.00 14.00           C  
ANISOU 2374  CG  GLN D 375     1676   2181   1463   -583   -239   -555       C  
ATOM   2375  CD  GLN D 375       7.424 -19.768 -52.564  1.00 17.02           C  
ANISOU 2375  CD  GLN D 375     2021   2566   1878   -562   -272   -609       C  
ATOM   2376  OE1 GLN D 375       8.294 -19.165 -53.195  1.00 20.82           O  
ANISOU 2376  OE1 GLN D 375     2491   2986   2435   -535   -311   -591       O  
ATOM   2377  NE2 GLN D 375       6.921 -19.312 -51.425  1.00 15.10           N  
ANISOU 2377  NE2 GLN D 375     1759   2399   1579   -583   -252   -676       N  
ATOM   2378  N   VAL D 376       9.613 -24.555 -54.152  1.00 13.60           N  
ANISOU 2378  N   VAL D 376     1674   2176   1317   -634   -351   -300       N  
ATOM   2379  CA  VAL D 376      10.722 -25.246 -54.795  1.00 14.40           C  
ANISOU 2379  CA  VAL D 376     1767   2232   1473   -597   -383   -214       C  
ATOM   2380  C   VAL D 376      10.216 -26.485 -55.523  1.00 16.85           C  
ANISOU 2380  C   VAL D 376     2113   2462   1826   -577   -332   -136       C  
ATOM   2381  O   VAL D 376      10.602 -26.742 -56.662  1.00 13.92           O  
ANISOU 2381  O   VAL D 376     1730   2012   1546   -550   -323   -119       O  
ATOM   2382  CB  VAL D 376      11.818 -25.653 -53.788  1.00 19.98           C  
ANISOU 2382  CB  VAL D 376     2463   3022   2108   -581   -449   -150       C  
ATOM   2383  CG1 VAL D 376      12.905 -26.437 -54.494  1.00 16.65           C  
ANISOU 2383  CG1 VAL D 376     2024   2536   1765   -533   -475    -68       C  
ATOM   2384  CG2 VAL D 376      12.412 -24.429 -53.122  1.00 20.47           C  
ANISOU 2384  CG2 VAL D 376     2479   3162   2139   -596   -502   -241       C  
ATOM   2385  N   HIS D 377       9.337 -27.243 -54.874  1.00 13.35           N  
ANISOU 2385  N   HIS D 377     1711   2042   1320   -595   -293    -96       N  
ATOM   2386  CA  HIS D 377       8.796 -28.449 -55.497  1.00 12.47           C  
ANISOU 2386  CA  HIS D 377     1627   1849   1263   -580   -242    -29       C  
ATOM   2387  C   HIS D 377       8.060 -28.143 -56.793  1.00 13.77           C  
ANISOU 2387  C   HIS D 377     1786   1929   1517   -579   -198    -99       C  
ATOM   2388  O   HIS D 377       8.205 -28.865 -57.781  1.00 13.80           O  
ANISOU 2388  O   HIS D 377     1787   1856   1600   -551   -180    -68       O  
ATOM   2389  CB  HIS D 377       7.844 -29.184 -54.558  1.00 15.23           C  
ANISOU 2389  CB  HIS D 377     2018   2235   1534   -611   -198     18       C  
ATOM   2390  CG  HIS D 377       7.247 -30.413 -55.165  1.00 19.97           C  
ANISOU 2390  CG  HIS D 377     2640   2743   2207   -600   -143     78       C  
ATOM   2391  ND1 HIS D 377       7.949 -31.591 -55.304  1.00 25.68           N  
ANISOU 2391  ND1 HIS D 377     3365   3413   2980   -564   -160    189       N  
ATOM   2392  CD2 HIS D 377       6.033 -30.631 -55.725  1.00 22.02           C  
ANISOU 2392  CD2 HIS D 377     2910   2945   2513   -618    -75     32       C  
ATOM   2393  CE1 HIS D 377       7.182 -32.492 -55.893  1.00 27.67           C  
ANISOU 2393  CE1 HIS D 377     3628   3578   3307   -563   -101    206       C  
ATOM   2394  NE2 HIS D 377       6.013 -31.934 -56.161  1.00 23.26           N  
ANISOU 2394  NE2 HIS D 377     3075   3019   2744   -597    -48    112       N  
ATOM   2395  N   LEU D 378       7.256 -27.086 -56.788  1.00 12.80           N  
ANISOU 2395  N   LEU D 378     1657   1823   1384   -609   -184   -198       N  
ATOM   2396  CA  LEU D 378       6.510 -26.729 -57.988  1.00 12.27           C  
ANISOU 2396  CA  LEU D 378     1584   1682   1398   -606   -154   -260       C  
ATOM   2397  C   LEU D 378       7.448 -26.330 -59.117  1.00 11.80           C  
ANISOU 2397  C   LEU D 378     1499   1576   1407   -577   -184   -257       C  
ATOM   2398  O   LEU D 378       7.288 -26.779 -60.248  1.00 12.53           O  
ANISOU 2398  O   LEU D 378     1593   1606   1561   -550   -160   -245       O  
ATOM   2399  CB  LEU D 378       5.519 -25.604 -57.704  1.00 13.31           C  
ANISOU 2399  CB  LEU D 378     1703   1822   1531   -592   -134   -339       C  
ATOM   2400  CG  LEU D 378       4.333 -25.994 -56.824  1.00 13.64           C  
ANISOU 2400  CG  LEU D 378     1764   1905   1514   -641    -86   -370       C  
ATOM   2401  CD1 LEU D 378       3.434 -24.785 -56.587  1.00 14.14           C  
ANISOU 2401  CD1 LEU D 378     1800   1966   1606   -598    -69   -436       C  
ATOM   2402  CD2 LEU D 378       3.558 -27.148 -57.438  1.00 12.55           C  
ANISOU 2402  CD2 LEU D 378     1650   1707   1412   -660    -37   -348       C  
ATOM   2403  N   LEU D 379       8.434 -25.494 -58.807  1.00  9.42           N  
ANISOU 2403  N   LEU D 379     1170   1308   1100   -562   -229   -264       N  
ATOM   2404  CA  LEU D 379       9.375 -25.047 -59.827  1.00  9.40           C  
ANISOU 2404  CA  LEU D 379     1140   1265   1167   -526   -245   -254       C  
ATOM   2405  C   LEU D 379      10.264 -26.177 -60.340  1.00 13.30           C  
ANISOU 2405  C   LEU D 379     1628   1743   1683   -529   -252   -193       C  
ATOM   2406  O   LEU D 379      10.570 -26.237 -61.530  1.00 17.84           O  
ANISOU 2406  O   LEU D 379     2191   2274   2315   -516   -237   -192       O  
ATOM   2407  CB  LEU D 379      10.232 -23.904 -59.291  1.00 18.83           C  
ANISOU 2407  CB  LEU D 379     2301   2490   2365   -511   -286   -279       C  
ATOM   2408  CG  LEU D 379       9.616 -22.537 -59.581  1.00 20.35           C  
ANISOU 2408  CG  LEU D 379     2489   2635   2607   -473   -280   -317       C  
ATOM   2409  CD1 LEU D 379      10.169 -21.479 -58.636  1.00 25.21           C  
ANISOU 2409  CD1 LEU D 379     3082   3280   3217   -474   -319   -349       C  
ATOM   2410  CD2 LEU D 379       9.845 -22.159 -61.050  1.00 20.28           C  
ANISOU 2410  CD2 LEU D 379     2475   2560   2671   -446   -276   -293       C  
ATOM   2411  N   GLU D 380      10.672 -27.066 -59.442  1.00 11.35           N  
ANISOU 2411  N   GLU D 380     1388   1527   1399   -515   -267   -131       N  
ATOM   2412  CA  GLU D 380      11.443 -28.248 -59.819  1.00 11.23           C  
ANISOU 2412  CA  GLU D 380     1361   1476   1430   -478   -267    -62       C  
ATOM   2413  C   GLU D 380      10.699 -29.102 -60.843  1.00 13.66           C  
ANISOU 2413  C   GLU D 380     1684   1713   1794   -468   -210    -62       C  
ATOM   2414  O   GLU D 380      11.291 -29.650 -61.776  1.00 16.81           O  
ANISOU 2414  O   GLU D 380     2058   2070   2260   -442   -199    -54       O  
ATOM   2415  CB  GLU D 380      11.755 -29.084 -58.582  1.00 18.83           C  
ANISOU 2415  CB  GLU D 380     2335   2476   2343   -467   -297     16       C  
ATOM   2416  CG  GLU D 380      12.774 -30.167 -58.812  1.00 23.29           C  
ANISOU 2416  CG  GLU D 380     2874   3002   2974   -424   -318     87       C  
ATOM   2417  CD  GLU D 380      13.159 -30.871 -57.533  1.00 32.38           C  
ANISOU 2417  CD  GLU D 380     4036   4194   4073   -410   -366    179       C  
ATOM   2418  OE1 GLU D 380      12.295 -31.001 -56.632  1.00 36.46           O  
ANISOU 2418  OE1 GLU D 380     4596   4750   4506   -437   -352    207       O  
ATOM   2419  OE2 GLU D 380      14.330 -31.295 -57.436  1.00 36.66           O  
ANISOU 2419  OE2 GLU D 380     4540   4731   4658   -374   -417    226       O  
ATOM   2420  N   SER D 381       9.389 -29.205 -60.663  1.00 12.24           N  
ANISOU 2420  N   SER D 381     1538   1524   1590   -489   -173    -84       N  
ATOM   2421  CA ASER D 381       8.561 -30.005 -61.549  0.63 12.08           C  
ANISOU 2421  CA ASER D 381     1527   1440   1622   -481   -122    -97       C  
ATOM   2422  CA BSER D 381       8.556 -30.007 -61.546  0.37 12.50           C  
ANISOU 2422  CA BSER D 381     1580   1493   1675   -481   -121    -97       C  
ATOM   2423  C   SER D 381       8.285 -29.314 -62.878  1.00 15.19           C  
ANISOU 2423  C   SER D 381     1911   1812   2049   -483   -109   -165       C  
ATOM   2424  O   SER D 381       8.184 -29.969 -63.918  1.00 15.83           O  
ANISOU 2424  O   SER D 381     1982   1851   2182   -466    -80   -178       O  
ATOM   2425  CB ASER D 381       7.233 -30.349 -60.872  0.63 16.02           C  
ANISOU 2425  CB ASER D 381     2060   1939   2090   -507    -84   -102       C  
ATOM   2426  CB BSER D 381       7.225 -30.333 -60.865  0.37 14.97           C  
ANISOU 2426  CB BSER D 381     1926   1805   1955   -507    -84   -103       C  
ATOM   2427  OG ASER D 381       6.391 -31.059 -61.762  0.63 18.84           O  
ANISOU 2427  OG ASER D 381     2418   2233   2508   -501    -36   -130       O  
ATOM   2428  OG BSER D 381       7.436 -30.953 -59.612  0.37 15.45           O  
ANISOU 2428  OG BSER D 381     2003   1898   1969   -512    -94    -26       O  
ATOM   2429  N   ALA D 382       8.174 -27.990 -62.843  1.00 11.04           N  
ANISOU 2429  N   ALA D 382     1384   1315   1496   -505   -133   -208       N  
ATOM   2430  CA  ALA D 382       7.669 -27.246 -63.991  1.00 10.66           C  
ANISOU 2430  CA  ALA D 382     1331   1246   1473   -454   -125   -232       C  
ATOM   2431  C   ALA D 382       8.678 -26.448 -64.817  1.00 10.95           C  
ANISOU 2431  C   ALA D 382     1346   1286   1528   -441   -146   -225       C  
ATOM   2432  O   ALA D 382       8.325 -25.974 -65.892  1.00  9.95           O  
ANISOU 2432  O   ALA D 382     1223   1145   1412   -418   -143   -227       O  
ATOM   2433  CB  ALA D 382       6.573 -26.300 -63.525  1.00 15.00           C  
ANISOU 2433  CB  ALA D 382     1892   1802   2004   -433   -131   -256       C  
ATOM   2434  N   TRP D 383       9.908 -26.284 -64.338  1.00  9.99           N  
ANISOU 2434  N   TRP D 383     1200   1189   1406   -464   -169   -212       N  
ATOM   2435  CA  TRP D 383      10.801 -25.287 -64.943  1.00  9.84           C  
ANISOU 2435  CA  TRP D 383     1155   1173   1409   -457   -185   -209       C  
ATOM   2436  C   TRP D 383      11.070 -25.528 -66.438  1.00  8.61           C  
ANISOU 2436  C   TRP D 383      994   1004   1274   -455   -159   -202       C  
ATOM   2437  O   TRP D 383      11.074 -24.578 -67.218  1.00 10.36           O  
ANISOU 2437  O   TRP D 383     1216   1220   1501   -451   -161   -199       O  
ATOM   2438  CB  TRP D 383      12.133 -25.191 -64.171  1.00 12.47           C  
ANISOU 2438  CB  TRP D 383     1454   1540   1746   -480   -217   -200       C  
ATOM   2439  CG  TRP D 383      13.051 -26.366 -64.321  1.00 13.49           C  
ANISOU 2439  CG  TRP D 383     1557   1672   1896   -485   -216   -171       C  
ATOM   2440  CD1 TRP D 383      13.083 -27.490 -63.544  1.00 20.83           C  
ANISOU 2440  CD1 TRP D 383     2492   2601   2820   -459   -223   -134       C  
ATOM   2441  CD2 TRP D 383      14.083 -26.526 -65.297  1.00 11.32           C  
ANISOU 2441  CD2 TRP D 383     1243   1392   1667   -478   -198   -167       C  
ATOM   2442  NE1 TRP D 383      14.063 -28.348 -63.987  1.00 20.31           N  
ANISOU 2442  NE1 TRP D 383     2388   2519   2808   -431   -216   -111       N  
ATOM   2443  CE2 TRP D 383      14.696 -27.774 -65.065  1.00 15.88           C  
ANISOU 2443  CE2 TRP D 383     1796   1960   2277   -443   -198   -140       C  
ATOM   2444  CE3 TRP D 383      14.549 -25.738 -66.356  1.00 13.22           C  
ANISOU 2444  CE3 TRP D 383     1464   1636   1926   -501   -179   -183       C  
ATOM   2445  CZ2 TRP D 383      15.739 -28.256 -65.854  1.00 17.09           C  
ANISOU 2445  CZ2 TRP D 383     1899   2107   2487   -427   -177   -146       C  
ATOM   2446  CZ3 TRP D 383      15.592 -26.212 -67.129  1.00 15.16           C  
ANISOU 2446  CZ3 TRP D 383     1663   1885   2210   -492   -152   -182       C  
ATOM   2447  CH2 TRP D 383      16.174 -27.456 -66.878  1.00 14.87           C  
ANISOU 2447  CH2 TRP D 383     1598   1841   2212   -455   -151   -173       C  
ATOM   2448  N   LEU D 384      11.268 -26.776 -66.852  1.00  7.91           N  
ANISOU 2448  N   LEU D 384      897    909   1198   -465   -131   -205       N  
ATOM   2449  CA  LEU D 384      11.571 -27.010 -68.263  1.00  8.13           C  
ANISOU 2449  CA  LEU D 384      912    941   1237   -467    -98   -217       C  
ATOM   2450  C   LEU D 384      10.321 -26.858 -69.139  1.00 10.70           C  
ANISOU 2450  C   LEU D 384     1272   1259   1536   -449    -85   -231       C  
ATOM   2451  O   LEU D 384      10.414 -26.403 -70.278  1.00 13.60           O  
ANISOU 2451  O   LEU D 384     1637   1643   1887   -462    -73   -237       O  
ATOM   2452  CB  LEU D 384      12.207 -28.385 -68.471  1.00  9.31           C  
ANISOU 2452  CB  LEU D 384     1024   1082   1432   -458    -68   -231       C  
ATOM   2453  CG  LEU D 384      12.661 -28.677 -69.905  1.00 16.53           C  
ANISOU 2453  CG  LEU D 384     1911   2014   2357   -460    -25   -261       C  
ATOM   2454  CD1 LEU D 384      13.687 -27.621 -70.368  1.00 12.51           C  
ANISOU 2454  CD1 LEU D 384     1376   1540   1835   -488    -27   -247       C  
ATOM   2455  CD2 LEU D 384      13.208 -30.104 -70.017  1.00 10.00           C  
ANISOU 2455  CD2 LEU D 384     1040   1166   1593   -426      1   -279       C  
ATOM   2456  N   GLU D 385       9.156 -27.216 -68.600  1.00  9.47           N  
ANISOU 2456  N   GLU D 385     1143   1083   1373   -428    -89   -238       N  
ATOM   2457  CA  GLU D 385       7.889 -26.946 -69.288  1.00  8.46           C  
ANISOU 2457  CA  GLU D 385     1040    949   1226   -407    -90   -252       C  
ATOM   2458  C   GLU D 385       7.712 -25.455 -69.537  1.00  8.14           C  
ANISOU 2458  C   GLU D 385     1005    908   1178   -405   -123   -237       C  
ATOM   2459  O   GLU D 385       7.244 -25.041 -70.597  1.00 10.14           O  
ANISOU 2459  O   GLU D 385     1266   1166   1421   -408   -128   -244       O  
ATOM   2460  CB  GLU D 385       6.691 -27.433 -68.476  1.00 11.15           C  
ANISOU 2460  CB  GLU D 385     1399   1270   1567   -387    -88   -260       C  
ATOM   2461  CG  GLU D 385       6.541 -28.919 -68.328  1.00 16.94           C  
ANISOU 2461  CG  GLU D 385     2126   1985   2324   -388    -51   -277       C  
ATOM   2462  CD  GLU D 385       5.386 -29.259 -67.410  1.00 34.00           C  
ANISOU 2462  CD  GLU D 385     4304   4130   4485   -381    -44   -280       C  
ATOM   2463  OE1 GLU D 385       4.282 -29.537 -67.914  1.00 20.75           O  
ANISOU 2463  OE1 GLU D 385     2631   2445   2807   -360    -32   -301       O  
ATOM   2464  OE2 GLU D 385       5.598 -29.196 -66.178  1.00 35.31           O  
ANISOU 2464  OE2 GLU D 385     4472   4297   4647   -402    -50   -264       O  
ATOM   2465  N   ILE D 386       8.056 -24.655 -68.531  1.00  9.37           N  
ANISOU 2465  N   ILE D 386     1154   1060   1348   -404   -149   -223       N  
ATOM   2466  CA AILE D 386       7.936 -23.203 -68.613  0.32 10.46           C  
ANISOU 2466  CA AILE D 386     1284   1183   1506   -399   -179   -218       C  
ATOM   2467  CA BILE D 386       7.904 -23.212 -68.638  0.68  9.79           C  
ANISOU 2467  CA BILE D 386     1200   1099   1422   -399   -179   -218       C  
ATOM   2468  C   ILE D 386       8.873 -22.645 -69.677  1.00  9.58           C  
ANISOU 2468  C   ILE D 386     1158   1085   1398   -433   -168   -202       C  
ATOM   2469  O   ILE D 386       8.492 -21.784 -70.470  1.00 10.49           O  
ANISOU 2469  O   ILE D 386     1277   1191   1519   -444   -176   -198       O  
ATOM   2470  CB AILE D 386       8.243 -22.537 -67.258  0.32 12.41           C  
ANISOU 2470  CB AILE D 386     1519   1429   1769   -392   -201   -219       C  
ATOM   2471  CB BILE D 386       8.100 -22.529 -67.272  0.68 11.60           C  
ANISOU 2471  CB BILE D 386     1419   1324   1666   -390   -202   -220       C  
ATOM   2472  CG1AILE D 386       7.168 -22.911 -66.233  0.32 12.22           C  
ANISOU 2472  CG1AILE D 386     1516   1402   1723   -376   -206   -232       C  
ATOM   2473  CG1BILE D 386       7.022 -23.016 -66.295  0.68 12.91           C  
ANISOU 2473  CG1BILE D 386     1607   1489   1810   -375   -204   -233       C  
ATOM   2474  CG2AILE D 386       8.347 -21.021 -67.408  0.32 12.79           C  
ANISOU 2474  CG2AILE D 386     1547   1461   1852   -384   -216   -220       C  
ATOM   2475  CG2BILE D 386       8.048 -21.017 -67.414  0.68 14.57           C  
ANISOU 2475  CG2BILE D 386     1778   1683   2076   -378   -219   -220       C  
ATOM   2476  CD1AILE D 386       5.773 -22.521 -66.644  0.32 10.82           C  
ANISOU 2476  CD1AILE D 386     1365   1207   1540   -355   -216   -230       C  
ATOM   2477  CD1BILE D 386       7.385 -22.853 -64.840  0.68 11.83           C  
ANISOU 2477  CD1BILE D 386     1462   1371   1663   -386   -215   -245       C  
ATOM   2478  N   LEU D 387      10.112 -23.134 -69.692  1.00  8.95           N  
ANISOU 2478  N   LEU D 387     1061   1027   1313   -459   -149   -191       N  
ATOM   2479  CA  LEU D 387      11.049 -22.728 -70.738  1.00  8.93           C  
ANISOU 2479  CA  LEU D 387     1044   1046   1304   -502   -131   -170       C  
ATOM   2480  C   LEU D 387      10.514 -23.106 -72.109  1.00  9.05           C  
ANISOU 2480  C   LEU D 387     1079   1084   1275   -526   -109   -176       C  
ATOM   2481  O   LEU D 387      10.644 -22.342 -73.060  1.00 11.75           O  
ANISOU 2481  O   LEU D 387     1429   1442   1596   -569   -109   -148       O  
ATOM   2482  CB  LEU D 387      12.426 -23.361 -70.546  1.00 11.07           C  
ANISOU 2482  CB  LEU D 387     1278   1340   1587   -521   -110   -168       C  
ATOM   2483  CG  LEU D 387      13.274 -22.895 -69.364  1.00 12.39           C  
ANISOU 2483  CG  LEU D 387     1416   1499   1792   -515   -137   -162       C  
ATOM   2484  CD1 LEU D 387      14.631 -23.567 -69.411  1.00 15.83           C  
ANISOU 2484  CD1 LEU D 387     1806   1962   2248   -535   -118   -164       C  
ATOM   2485  CD2 LEU D 387      13.443 -21.393 -69.408  1.00 12.17           C  
ANISOU 2485  CD2 LEU D 387     1380   1451   1795   -525   -153   -149       C  
ATOM   2486  N   MET D 388       9.912 -24.287 -72.208  1.00  8.79           N  
ANISOU 2486  N   MET D 388     1055   1058   1227   -504    -91   -212       N  
ATOM   2487  CA  MET D 388       9.426 -24.766 -73.497  1.00  8.85           C  
ANISOU 2487  CA  MET D 388     1072   1099   1191   -525    -69   -240       C  
ATOM   2488  C   MET D 388       8.213 -23.995 -74.007  1.00  9.60           C  
ANISOU 2488  C   MET D 388     1200   1182   1265   -523   -107   -233       C  
ATOM   2489  O   MET D 388       8.152 -23.665 -75.191  1.00 10.59           O  
ANISOU 2489  O   MET D 388     1338   1347   1337   -572   -110   -226       O  
ATOM   2490  CB  MET D 388       9.101 -26.258 -73.424  1.00  7.89           C  
ANISOU 2490  CB  MET D 388      940    976   1081   -494    -38   -292       C  
ATOM   2491  CG  MET D 388      10.333 -27.133 -73.402  1.00  8.20           C  
ANISOU 2491  CG  MET D 388      935   1033   1149   -507      4   -313       C  
ATOM   2492  SD  MET D 388       9.921 -28.869 -73.228  1.00 39.53           S  
ANISOU 2492  SD  MET D 388     4883   4974   5163   -467     35   -371       S  
ATOM   2493  CE  MET D 388      11.477 -29.658 -73.649  1.00 16.89           C  
ANISOU 2493  CE  MET D 388     1949   2131   2338   -469     81   -396       C  
ATOM   2494  N   ILE D 389       7.248 -23.699 -73.140  1.00 11.20           N  
ANISOU 2494  N   ILE D 389     1411   1338   1506   -472   -139   -236       N  
ATOM   2495  CA  ILE D 389       6.086 -22.962 -73.616  1.00 10.87           C  
ANISOU 2495  CA  ILE D 389     1386   1280   1465   -464   -177   -240       C  
ATOM   2496  C   ILE D 389       6.499 -21.535 -73.993  1.00 13.75           C  
ANISOU 2496  C   ILE D 389     1757   1637   1832   -509   -206   -189       C  
ATOM   2497  O   ILE D 389       5.962 -20.960 -74.938  1.00 13.24           O  
ANISOU 2497  O   ILE D 389     1716   1577   1738   -540   -243   -166       O  
ATOM   2498  CB  ILE D 389       4.919 -22.957 -72.593  1.00 12.16           C  
ANISOU 2498  CB  ILE D 389     1543   1397   1679   -401   -201   -262       C  
ATOM   2499  CG1 ILE D 389       3.621 -22.526 -73.292  1.00 10.80           C  
ANISOU 2499  CG1 ILE D 389     1374   1213   1517   -387   -235   -288       C  
ATOM   2500  CG2 ILE D 389       5.225 -22.105 -71.357  1.00 12.08           C  
ANISOU 2500  CG2 ILE D 389     1512   1362   1716   -381   -210   -249       C  
ATOM   2501  CD1 ILE D 389       2.427 -22.480 -72.396  1.00 10.92           C  
ANISOU 2501  CD1 ILE D 389     1419   1193   1536   -340   -262   -262       C  
ATOM   2502  N   GLY D 390       7.482 -20.984 -73.288  1.00 11.69           N  
ANISOU 2502  N   GLY D 390     1476   1362   1603   -516   -197   -164       N  
ATOM   2503  CA  GLY D 390       8.025 -19.687 -73.649  1.00 12.82           C  
ANISOU 2503  CA  GLY D 390     1621   1489   1761   -560   -219   -106       C  
ATOM   2504  C   GLY D 390       8.628 -19.734 -75.037  1.00 12.27           C  
ANISOU 2504  C   GLY D 390     1570   1468   1625   -640   -213    -50       C  
ATOM   2505  O   GLY D 390       8.398 -18.851 -75.862  1.00 13.73           O  
ANISOU 2505  O   GLY D 390     1777   1645   1797   -676   -249     15       O  
ATOM   2506  N   LEU D 391       9.398 -20.786 -75.293  1.00 10.89           N  
ANISOU 2506  N   LEU D 391     1380   1349   1410   -652   -159    -73       N  
ATOM   2507  CA  LEU D 391      10.048 -20.972 -76.586  1.00 11.33           C  
ANISOU 2507  CA  LEU D 391     1435   1478   1392   -677   -116    -39       C  
ATOM   2508  C   LEU D 391       9.022 -21.114 -77.707  1.00 12.46           C  
ANISOU 2508  C   LEU D 391     1612   1661   1460   -668   -136    -37       C  
ATOM   2509  O   LEU D 391       9.161 -20.527 -78.783  1.00 14.15           O  
ANISOU 2509  O   LEU D 391     1845   1919   1611   -699   -138     31       O  
ATOM   2510  CB  LEU D 391      10.966 -22.197 -76.540  1.00 11.61           C  
ANISOU 2510  CB  LEU D 391     1433   1560   1417   -667    -50    -92       C  
ATOM   2511  CG  LEU D 391      11.525 -22.664 -77.880  1.00 13.47           C  
ANISOU 2511  CG  LEU D 391     1659   1887   1573   -688      7    -92       C  
ATOM   2512  CD1 LEU D 391      12.418 -21.594 -78.476  1.00 14.22           C  
ANISOU 2512  CD1 LEU D 391     1751   2006   1646   -744     26     -8       C  
ATOM   2513  CD2 LEU D 391      12.283 -23.975 -77.725  1.00 13.00           C  
ANISOU 2513  CD2 LEU D 391     1551   1856   1533   -668     66   -167       C  
ATOM   2514  N   VAL D 392       7.983 -21.891 -77.443  1.00 11.43           N  
ANISOU 2514  N   VAL D 392     1489   1518   1334   -629   -153   -108       N  
ATOM   2515  CA  VAL D 392       6.952 -22.124 -78.442  1.00 12.33           C  
ANISOU 2515  CA  VAL D 392     1628   1674   1385   -615   -179   -126       C  
ATOM   2516  C   VAL D 392       6.197 -20.824 -78.738  1.00 13.42           C  
ANISOU 2516  C   VAL D 392     1796   1773   1530   -623   -256    -54       C  
ATOM   2517  O   VAL D 392       5.878 -20.530 -79.891  1.00 17.97           O  
ANISOU 2517  O   VAL D 392     2397   2403   2029   -633   -281     -9       O  
ATOM   2518  CB  VAL D 392       5.984 -23.232 -77.982  1.00 13.41           C  
ANISOU 2518  CB  VAL D 392     1754   1791   1549   -573   -178   -226       C  
ATOM   2519  CG1 VAL D 392       4.719 -23.215 -78.793  1.00 22.27           C  
ANISOU 2519  CG1 VAL D 392     2896   2934   2630   -555   -227   -250       C  
ATOM   2520  CG2 VAL D 392       6.664 -24.592 -78.089  1.00 14.41           C  
ANISOU 2520  CG2 VAL D 392     1849   1962   1664   -564   -106   -290       C  
ATOM   2521  N   TRP D 393       5.951 -20.031 -77.698  1.00 13.76           N  
ANISOU 2521  N   TRP D 393     1835   1726   1667   -620   -296    -44       N  
ATOM   2522  CA  TRP D 393       5.276 -18.739 -77.839  1.00 12.05           C  
ANISOU 2522  CA  TRP D 393     1636   1450   1492   -625   -373     18       C  
ATOM   2523  C   TRP D 393       6.048 -17.744 -78.714  1.00 15.63           C  
ANISOU 2523  C   TRP D 393     2105   1920   1913   -669   -379    140       C  
ATOM   2524  O   TRP D 393       5.466 -17.105 -79.594  1.00 19.47           O  
ANISOU 2524  O   TRP D 393     2619   2410   2369   -673   -436    210       O  
ATOM   2525  CB  TRP D 393       5.019 -18.128 -76.456  1.00 12.36           C  
ANISOU 2525  CB  TRP D 393     1654   1393   1650   -617   -402    -16       C  
ATOM   2526  CG  TRP D 393       4.493 -16.715 -76.495  1.00 15.25           C  
ANISOU 2526  CG  TRP D 393     2022   1681   2090   -618   -475     40       C  
ATOM   2527  CD1 TRP D 393       5.157 -15.590 -76.097  1.00 18.72           C  
ANISOU 2527  CD1 TRP D 393     2444   2068   2601   -629   -476     93       C  
ATOM   2528  CD2 TRP D 393       3.210 -16.276 -76.970  1.00 16.95           C  
ANISOU 2528  CD2 TRP D 393     2250   1861   2330   -598   -557     44       C  
ATOM   2529  NE1 TRP D 393       4.370 -14.481 -76.290  1.00 19.54           N  
ANISOU 2529  NE1 TRP D 393     2549   2100   2777   -619   -551    133       N  
ATOM   2530  CE2 TRP D 393       3.172 -14.872 -76.822  1.00 20.84           C  
ANISOU 2530  CE2 TRP D 393     2732   2270   2916   -600   -607    107       C  
ATOM   2531  CE3 TRP D 393       2.094 -16.930 -77.502  1.00 22.01           C  
ANISOU 2531  CE3 TRP D 393     2901   2533   2926   -564   -585     -6       C  
ATOM   2532  CZ2 TRP D 393       2.059 -14.110 -77.189  1.00 22.74           C  
ANISOU 2532  CZ2 TRP D 393     2974   2447   3217   -579   -699    129       C  
ATOM   2533  CZ3 TRP D 393       0.986 -16.168 -77.868  1.00 18.22           C  
ANISOU 2533  CZ3 TRP D 393     2425   2001   2499   -542   -678     11       C  
ATOM   2534  CH2 TRP D 393       0.981 -14.774 -77.707  1.00 18.14           C  
ANISOU 2534  CH2 TRP D 393     2405   1897   2591   -554   -741     81       C  
ATOM   2535  N   ARG D 394       7.351 -17.601 -78.488  1.00 14.38           N  
ANISOU 2535  N   ARG D 394     1928   1772   1765   -705   -323    172       N  
ATOM   2536  CA  ARG D 394       8.102 -16.628 -79.280  1.00 17.45           C  
ANISOU 2536  CA  ARG D 394     2327   2170   2132   -755   -319    293       C  
ATOM   2537  C   ARG D 394       8.472 -17.199 -80.653  1.00 15.81           C  
ANISOU 2537  C   ARG D 394     2140   2087   1781   -778   -271    327       C  
ATOM   2538  O   ARG D 394       8.989 -16.482 -81.506  1.00 19.35           O  
ANISOU 2538  O   ARG D 394     2604   2565   2181   -826   -262    437       O  
ATOM   2539  CB  ARG D 394       9.351 -16.142 -78.532  1.00 27.07           C  
ANISOU 2539  CB  ARG D 394     3508   3348   3427   -790   -278    310       C  
ATOM   2540  CG  ARG D 394      10.376 -17.197 -78.172  1.00 23.13           C  
ANISOU 2540  CG  ARG D 394     2976   2908   2904   -791   -198    241       C  
ATOM   2541  CD  ARG D 394      11.451 -16.586 -77.270  1.00 21.18           C  
ANISOU 2541  CD  ARG D 394     2687   2608   2753   -818   -180    248       C  
ATOM   2542  NE  ARG D 394      12.461 -17.560 -76.866  1.00 15.80           N  
ANISOU 2542  NE  ARG D 394     1966   1975   2062   -813   -116    185       N  
ATOM   2543  CZ  ARG D 394      12.459 -18.195 -75.699  1.00 13.13           C  
ANISOU 2543  CZ  ARG D 394     1605   1615   1769   -774   -121    103       C  
ATOM   2544  NH1 ARG D 394      11.495 -17.967 -74.817  1.00 17.31           N  
ANISOU 2544  NH1 ARG D 394     2146   2087   2344   -714   -169     62       N  
ATOM   2545  NH2 ARG D 394      13.418 -19.061 -75.420  1.00 15.97           N  
ANISOU 2545  NH2 ARG D 394     1927   2014   2126   -767    -71     59       N  
ATOM   2546  N   SER D 395       8.182 -18.480 -80.874  1.00 20.04           N  
ANISOU 2546  N   SER D 395     2792   2717   2107  -1095   -592    744       N  
ATOM   2547  CA  SER D 395       8.407 -19.087 -82.186  1.00 20.95           C  
ANISOU 2547  CA  SER D 395     3006   2866   2089  -1113   -647    699       C  
ATOM   2548  C   SER D 395       7.149 -19.111 -83.056  1.00 26.27           C  
ANISOU 2548  C   SER D 395     3683   3558   2739  -1143   -789    741       C  
ATOM   2549  O   SER D 395       7.207 -19.533 -84.210  1.00 22.97           O  
ANISOU 2549  O   SER D 395     3357   3174   2198  -1178   -845    711       O  
ATOM   2550  CB  SER D 395       8.947 -20.516 -82.048  1.00 20.85           C  
ANISOU 2550  CB  SER D 395     3025   2832   2063  -1126   -626    595       C  
ATOM   2551  OG  SER D 395      10.135 -20.562 -81.279  1.00 20.01           O  
ANISOU 2551  OG  SER D 395     2908   2708   1986  -1100   -510    567       O  
ATOM   2552  N   MET D 396       6.024 -18.662 -82.502  1.00 22.02           N  
ANISOU 2552  N   MET D 396     3046   2998   2324  -1139   -843    809       N  
ATOM   2553  CA  MET D 396       4.734 -18.697 -83.198  1.00 25.28           C  
ANISOU 2553  CA  MET D 396     3433   3425   2745  -1168   -990    861       C  
ATOM   2554  C   MET D 396       4.781 -18.113 -84.608  1.00 26.32           C  
ANISOU 2554  C   MET D 396     3652   3607   2743  -1188  -1063    917       C  
ATOM   2555  O   MET D 396       4.258 -18.705 -85.552  1.00 29.97           O  
ANISOU 2555  O   MET D 396     4167   4100   3120  -1243  -1178    910       O  
ATOM   2556  CB  MET D 396       3.667 -17.956 -82.382  1.00 30.21           C  
ANISOU 2556  CB  MET D 396     3922   4012   3542  -1146  -1009    940       C  
ATOM   2557  CG  MET D 396       2.629 -18.861 -81.735  1.00 31.69           C  
ANISOU 2557  CG  MET D 396     4028   4174   3840  -1174  -1067    909       C  
ATOM   2558  SD  MET D 396       1.093 -17.998 -81.319  1.00 39.48           S  
ANISOU 2558  SD  MET D 396     4857   5126   5017  -1160  -1131   1011       S  
ATOM   2559  CE  MET D 396       0.371 -17.714 -82.926  1.00 35.09           C  
ANISOU 2559  CE  MET D 396     4333   4619   4380  -1182  -1311   1102       C  
ATOM   2560  N   GLU D 397       5.422 -16.959 -84.744  1.00 28.66           N  
ANISOU 2560  N   GLU D 397     3970   3910   3010  -1156   -997    972       N  
ATOM   2561  CA  GLU D 397       5.467 -16.248 -86.016  1.00 31.02           C  
ANISOU 2561  CA  GLU D 397     4350   4253   3184  -1181  -1065   1041       C  
ATOM   2562  C   GLU D 397       6.642 -16.675 -86.888  1.00 30.20           C  
ANISOU 2562  C   GLU D 397     4391   4192   2890  -1217  -1010    960       C  
ATOM   2563  O   GLU D 397       6.983 -15.993 -87.853  1.00 32.32           O  
ANISOU 2563  O   GLU D 397     4745   4499   3035  -1243  -1028   1007       O  
ATOM   2564  CB  GLU D 397       5.538 -14.742 -85.770  1.00 33.21           C  
ANISOU 2564  CB  GLU D 397     4582   4510   3527  -1132  -1022   1146       C  
ATOM   2565  CG  GLU D 397       4.344 -14.176 -85.029  1.00 34.85           C  
ANISOU 2565  CG  GLU D 397     4643   4665   3932  -1097  -1067   1230       C  
ATOM   2566  CD  GLU D 397       4.456 -12.678 -84.823  1.00 40.24           C  
ANISOU 2566  CD  GLU D 397     5289   5315   4686  -1050  -1010   1328       C  
ATOM   2567  OE1 GLU D 397       5.237 -12.030 -85.553  1.00 43.94           O  
ANISOU 2567  OE1 GLU D 397     5853   5813   5030  -1056   -987   1358       O  
ATOM   2568  OE2 GLU D 397       3.770 -12.146 -83.925  1.00 45.33           O  
ANISOU 2568  OE2 GLU D 397     5810   5900   5512  -1012   -981   1369       O  
ATOM   2569  N   HIS D 398       7.266 -17.797 -86.546  1.00 26.10           N  
ANISOU 2569  N   HIS D 398     3900   3663   2355  -1222   -938    840       N  
ATOM   2570  CA  HIS D 398       8.376 -18.316 -87.336  1.00 25.73           C  
ANISOU 2570  CA  HIS D 398     3979   3646   2152  -1254   -869    746       C  
ATOM   2571  C   HIS D 398       8.163 -19.775 -87.717  1.00 26.30           C  
ANISOU 2571  C   HIS D 398     4101   3714   2177  -1306   -910    642       C  
ATOM   2572  O   HIS D 398       8.834 -20.656 -87.182  1.00 25.69           O  
ANISOU 2572  O   HIS D 398     4022   3604   2137  -1286   -820    544       O  
ATOM   2573  CB  HIS D 398       9.687 -18.167 -86.567  1.00 28.06           C  
ANISOU 2573  CB  HIS D 398     4262   3921   2479  -1200   -704    695       C  
ATOM   2574  CG  HIS D 398      10.063 -16.746 -86.294  1.00 29.09           C  
ANISOU 2574  CG  HIS D 398     4367   4057   2628  -1162   -646    783       C  
ATOM   2575  ND1 HIS D 398       9.718 -16.099 -85.128  1.00 32.99           N  
ANISOU 2575  ND1 HIS D 398     4750   4514   3272  -1114   -618    844       N  
ATOM   2576  CD2 HIS D 398      10.756 -15.849 -87.034  1.00 26.91           C  
ANISOU 2576  CD2 HIS D 398     4168   3817   2238  -1172   -603    815       C  
ATOM   2577  CE1 HIS D 398      10.178 -14.861 -85.163  1.00 23.05           C  
ANISOU 2577  CE1 HIS D 398     3500   3263   1994  -1093   -560    910       C  
ATOM   2578  NE2 HIS D 398      10.815 -14.685 -86.306  1.00 33.28           N  
ANISOU 2578  NE2 HIS D 398     4909   4605   3132  -1126   -554    897       N  
ATOM   2579  N   PRO D 399       7.233 -20.030 -88.653  1.00 27.07           N  
ANISOU 2579  N   PRO D 399     4246   3845   2196  -1379  -1049    669       N  
ATOM   2580  CA  PRO D 399       6.918 -21.397 -89.080  1.00 27.78           C  
ANISOU 2580  CA  PRO D 399     4392   3931   2232  -1444  -1095    571       C  
ATOM   2581  C   PRO D 399       8.167 -22.184 -89.475  1.00 27.91           C  
ANISOU 2581  C   PRO D 399     4515   3939   2152  -1461   -965    432       C  
ATOM   2582  O   PRO D 399       8.999 -21.684 -90.232  1.00 28.38           O  
ANISOU 2582  O   PRO D 399     4665   4032   2086  -1482   -899    417       O  
ATOM   2583  CB  PRO D 399       5.995 -21.186 -90.285  1.00 29.76           C  
ANISOU 2583  CB  PRO D 399     4707   4238   2363  -1538  -1255    640       C  
ATOM   2584  CG  PRO D 399       5.390 -19.837 -90.066  1.00 31.72           C  
ANISOU 2584  CG  PRO D 399     4866   4494   2691  -1496  -1325    796       C  
ATOM   2585  CD  PRO D 399       6.445 -19.021 -89.382  1.00 28.39           C  
ANISOU 2585  CD  PRO D 399     4417   4051   2320  -1412  -1174    799       C  
ATOM   2586  N   GLY D 400       8.298 -23.392 -88.938  1.00 27.56           N  
ANISOU 2586  N   GLY D 400     4452   3843   2177  -1450   -923    331       N  
ATOM   2587  CA  GLY D 400       9.399 -24.270 -89.284  1.00 27.89           C  
ANISOU 2587  CA  GLY D 400     4578   3858   2159  -1461   -799    193       C  
ATOM   2588  C   GLY D 400      10.691 -24.003 -88.534  1.00 26.79           C  
ANISOU 2588  C   GLY D 400     4395   3688   2096  -1375   -645    167       C  
ATOM   2589  O   GLY D 400      11.680 -24.716 -88.718  1.00 27.04           O  
ANISOU 2589  O   GLY D 400     4474   3688   2112  -1370   -531     56       O  
ATOM   2590  N   LYS D 401      10.698 -22.976 -87.691  1.00 25.70           N  
ANISOU 2590  N   LYS D 401     4162   3555   2046  -1312   -636    267       N  
ATOM   2591  CA  LYS D 401      11.894 -22.660 -86.913  1.00 24.69           C  
ANISOU 2591  CA  LYS D 401     3987   3405   1989  -1242   -500    256       C  
ATOM   2592  C   LYS D 401      11.589 -22.416 -85.439  1.00 23.36           C  
ANISOU 2592  C   LYS D 401     3686   3201   1987  -1185   -506    323       C  
ATOM   2593  O   LYS D 401      10.444 -22.177 -85.056  1.00 23.17           O  
ANISOU 2593  O   LYS D 401     3604   3178   2023  -1193   -605    393       O  
ATOM   2594  CB  LYS D 401      12.603 -21.431 -87.479  1.00 24.81           C  
ANISOU 2594  CB  LYS D 401     4050   3473   1905  -1239   -440    301       C  
ATOM   2595  CG  LYS D 401      12.920 -21.497 -88.967  1.00 26.23           C  
ANISOU 2595  CG  LYS D 401     4371   3696   1898  -1314   -429    243       C  
ATOM   2596  CD  LYS D 401      13.582 -20.203 -89.408  1.00 26.28           C  
ANISOU 2596  CD  LYS D 401     4419   3753   1814  -1314   -373    302       C  
ATOM   2597  CE  LYS D 401      13.765 -20.123 -90.917  1.00 30.76           C  
ANISOU 2597  CE  LYS D 401     5137   4373   2178  -1409   -376    262       C  
ATOM   2598  NZ  LYS D 401      14.672 -21.182 -91.456  1.00 34.73           N  
ANISOU 2598  NZ  LYS D 401     5717   4856   2624  -1441   -257    103       N  
ATOM   2599  N   LEU D 402      12.633 -22.468 -84.617  1.00 22.53           N  
ANISOU 2599  N   LEU D 402     3536   3068   1958  -1136   -397    302       N  
ATOM   2600  CA  LEU D 402      12.497 -22.185 -83.196  1.00 21.34           C  
ANISOU 2600  CA  LEU D 402     3274   2888   1947  -1101   -388    363       C  
ATOM   2601  C   LEU D 402      13.349 -20.978 -82.826  1.00 20.68           C  
ANISOU 2601  C   LEU D 402     3167   2830   1859  -1069   -297    420       C  
ATOM   2602  O   LEU D 402      14.552 -20.954 -83.086  1.00 20.76           O  
ANISOU 2602  O   LEU D 402     3209   2850   1830  -1052   -199    379       O  
ATOM   2603  CB  LEU D 402      12.892 -23.409 -82.370  1.00 23.09           C  
ANISOU 2603  CB  LEU D 402     3453   3047   2274  -1087   -360    302       C  
ATOM   2604  CG  LEU D 402      11.951 -24.606 -82.537  1.00 21.56           C  
ANISOU 2604  CG  LEU D 402     3273   2817   2101  -1122   -452    250       C  
ATOM   2605  CD1 LEU D 402      12.391 -25.774 -81.671  1.00 21.26           C  
ANISOU 2605  CD1 LEU D 402     3194   2708   2177  -1107   -424    201       C  
ATOM   2606  CD2 LEU D 402      10.526 -24.198 -82.203  1.00 21.36           C  
ANISOU 2606  CD2 LEU D 402     3198   2807   2111  -1147   -560    324       C  
ATOM   2607  N   LEU D 403      12.711 -19.968 -82.244  1.00 20.12           N  
ANISOU 2607  N   LEU D 403     3040   2770   1835  -1064   -323    513       N  
ATOM   2608  CA  LEU D 403      13.410 -18.757 -81.839  1.00 19.52           C  
ANISOU 2608  CA  LEU D 403     2943   2714   1758  -1043   -237    571       C  
ATOM   2609  C   LEU D 403      13.871 -18.913 -80.396  1.00 18.50           C  
ANISOU 2609  C   LEU D 403     2733   2552   1745  -1034   -177    580       C  
ATOM   2610  O   LEU D 403      13.197 -18.473 -79.465  1.00 17.94           O  
ANISOU 2610  O   LEU D 403     2595   2462   1757  -1044   -192    634       O  
ATOM   2611  CB  LEU D 403      12.509 -17.526 -81.995  1.00 19.61           C  
ANISOU 2611  CB  LEU D 403     2941   2744   1767  -1046   -286    665       C  
ATOM   2612  CG  LEU D 403      13.140 -16.138 -81.830  1.00 19.23           C  
ANISOU 2612  CG  LEU D 403     2894   2716   1697  -1031   -201    728       C  
ATOM   2613  CD1 LEU D 403      12.513 -15.175 -82.810  1.00 23.39           C  
ANISOU 2613  CD1 LEU D 403     3465   3268   2154  -1037   -263    798       C  
ATOM   2614  CD2 LEU D 403      12.997 -15.596 -80.415  1.00 28.28           C  
ANISOU 2614  CD2 LEU D 403     3950   3829   2965  -1026   -151    775       C  
ATOM   2615  N   PHE D 404      15.006 -19.580 -80.215  1.00 18.41           N  
ANISOU 2615  N   PHE D 404     2724   2529   1742  -1021   -110    525       N  
ATOM   2616  CA  PHE D 404      15.570 -19.772 -78.884  1.00 17.61           C  
ANISOU 2616  CA  PHE D 404     2549   2400   1741  -1024    -63    543       C  
ATOM   2617  C   PHE D 404      15.921 -18.416 -78.289  1.00 16.97           C  
ANISOU 2617  C   PHE D 404     2443   2347   1658  -1032      5    616       C  
ATOM   2618  O   PHE D 404      15.717 -18.179 -77.102  1.00 16.31           O  
ANISOU 2618  O   PHE D 404     2299   2245   1651  -1060     16    660       O  
ATOM   2619  CB  PHE D 404      16.798 -20.682 -78.940  1.00 17.86           C  
ANISOU 2619  CB  PHE D 404     2582   2412   1791  -1004     -8    482       C  
ATOM   2620  CG  PHE D 404      16.467 -22.127 -79.183  1.00 18.41           C  
ANISOU 2620  CG  PHE D 404     2663   2432   1900  -1002    -65    410       C  
ATOM   2621  CD1 PHE D 404      16.102 -22.955 -78.135  1.00 18.05           C  
ANISOU 2621  CD1 PHE D 404     2559   2335   1965  -1019   -113    420       C  
ATOM   2622  CD2 PHE D 404      16.510 -22.655 -80.462  1.00 19.38           C  
ANISOU 2622  CD2 PHE D 404     2862   2557   1944   -993    -67    332       C  
ATOM   2623  CE1 PHE D 404      15.796 -24.285 -78.357  1.00 18.61           C  
ANISOU 2623  CE1 PHE D 404     2643   2353   2075  -1019   -163    355       C  
ATOM   2624  CE2 PHE D 404      16.199 -23.983 -80.691  1.00 19.97           C  
ANISOU 2624  CE2 PHE D 404     2953   2579   2055   -998   -110    259       C  
ATOM   2625  CZ  PHE D 404      15.845 -24.800 -79.639  1.00 19.57           C  
ANISOU 2625  CZ  PHE D 404     2840   2472   2122  -1006   -159    272       C  
ATOM   2626  N   ALA D 405      16.438 -17.534 -79.137  1.00 17.27           N  
ANISOU 2626  N   ALA D 405     2534   2427   1600  -1017     54    626       N  
ATOM   2627  CA  ALA D 405      16.705 -16.144 -78.789  1.00 16.83           C  
ANISOU 2627  CA  ALA D 405     2465   2393   1537  -1006    115    680       C  
ATOM   2628  C   ALA D 405      16.611 -15.328 -80.077  1.00 17.49           C  
ANISOU 2628  C   ALA D 405     2629   2516   1502  -1004    114    700       C  
ATOM   2629  O   ALA D 405      16.624 -15.909 -81.163  1.00 18.27           O  
ANISOU 2629  O   ALA D 405     2792   2630   1518  -1008     81    656       O  
ATOM   2630  CB  ALA D 405      18.078 -15.999 -78.131  1.00 16.39           C  
ANISOU 2630  CB  ALA D 405     2366   2336   1525   -957    198    643       C  
ATOM   2631  N   PRO D 406      16.490 -13.990 -79.973  1.00 17.97           N  
ANISOU 2631  N   PRO D 406     2667   2571   1590   -950    136    722       N  
ATOM   2632  CA  PRO D 406      16.415 -13.186 -81.198  1.00 18.70           C  
ANISOU 2632  CA  PRO D 406     2834   2694   1579   -948    125    749       C  
ATOM   2633  C   PRO D 406      17.634 -13.369 -82.094  1.00 19.18           C  
ANISOU 2633  C   PRO D 406     2963   2794   1532   -949    185    697       C  
ATOM   2634  O   PRO D 406      17.528 -13.215 -83.311  1.00 21.27           O  
ANISOU 2634  O   PRO D 406     3313   3090   1678   -974    158    700       O  
ATOM   2635  CB  PRO D 406      16.345 -11.754 -80.668  1.00 23.10           C  
ANISOU 2635  CB  PRO D 406     3344   3223   2212   -885    167    772       C  
ATOM   2636  CG  PRO D 406      15.659 -11.897 -79.356  1.00 20.05           C  
ANISOU 2636  CG  PRO D 406     2874   2791   1953   -878    160    773       C  
ATOM   2637  CD  PRO D 406      16.204 -13.178 -78.776  1.00 21.52           C  
ANISOU 2637  CD  PRO D 406     3036   2979   2161   -899    164    726       C  
ATOM   2638  N   ASN D 407      18.776 -13.688 -81.491  1.00 20.24           N  
ANISOU 2638  N   ASN D 407     3056   2925   1710   -925    264    649       N  
ATOM   2639  CA  ASN D 407      19.999 -13.937 -82.239  1.00 21.97           C  
ANISOU 2639  CA  ASN D 407     3323   3177   1847   -929    337    595       C  
ATOM   2640  C   ASN D 407      20.312 -15.426 -82.340  1.00 19.85           C  
ANISOU 2640  C   ASN D 407     3080   2915   1548   -988    356    551       C  
ATOM   2641  O   ASN D 407      21.453 -15.816 -82.578  1.00 24.64           O  
ANISOU 2641  O   ASN D 407     3693   3535   2134   -987    442    497       O  
ATOM   2642  CB  ASN D 407      21.172 -13.193 -81.597  1.00 20.09           C  
ANISOU 2642  CB  ASN D 407     3019   2931   1682   -862    416    582       C  
ATOM   2643  CG  ASN D 407      21.470 -13.680 -80.190  1.00 18.26           C  
ANISOU 2643  CG  ASN D 407     2696   2667   1575   -844    424    583       C  
ATOM   2644  OD1 ASN D 407      20.627 -14.303 -79.540  1.00 17.88           O  
ANISOU 2644  OD1 ASN D 407     2619   2593   1581   -870    368    600       O  
ATOM   2645  ND2 ASN D 407      22.674 -13.392 -79.710  1.00 21.18           N  
ANISOU 2645  ND2 ASN D 407     3020   3036   1993   -803    484    569       N  
ATOM   2646  N   LEU D 408      19.297 -16.260 -82.157  1.00 18.92           N  
ANISOU 2646  N   LEU D 408     2946   2762   1480   -993    264    543       N  
ATOM   2647  CA  LEU D 408      19.496 -17.695 -82.276  1.00 19.33           C  
ANISOU 2647  CA  LEU D 408     2989   2778   1577   -982    253    456       C  
ATOM   2648  C   LEU D 408      18.215 -18.363 -82.763  1.00 19.79           C  
ANISOU 2648  C   LEU D 408     3081   2816   1624   -996    140    436       C  
ATOM   2649  O   LEU D 408      17.478 -18.980 -81.992  1.00 19.39           O  
ANISOU 2649  O   LEU D 408     2973   2724   1669   -995     73    447       O  
ATOM   2650  CB  LEU D 408      19.954 -18.288 -80.942  1.00 18.61           C  
ANISOU 2650  CB  LEU D 408     2798   2647   1626   -967    272    466       C  
ATOM   2651  CG  LEU D 408      20.516 -19.709 -80.994  1.00 22.24           C  
ANISOU 2651  CG  LEU D 408     3235   3059   2154   -945    286    383       C  
ATOM   2652  CD1 LEU D 408      21.683 -19.760 -81.954  1.00 19.94           C  
ANISOU 2652  CD1 LEU D 408     2988   2789   1801   -931    389    311       C  
ATOM   2653  CD2 LEU D 408      20.970 -20.140 -79.618  1.00 18.46           C  
ANISOU 2653  CD2 LEU D 408     2656   2544   1814   -940    289    421       C  
ATOM   2654  N   LEU D 409      17.963 -18.207 -84.058  1.00 20.73           N  
ANISOU 2654  N   LEU D 409     3295   2966   1615  -1021    117    409       N  
ATOM   2655  CA  LEU D 409      16.810 -18.785 -84.732  1.00 23.11           C  
ANISOU 2655  CA  LEU D 409     3643   3260   1877  -1051      6    390       C  
ATOM   2656  C   LEU D 409      17.252 -20.005 -85.533  1.00 26.50           C  
ANISOU 2656  C   LEU D 409     4135   3672   2263  -1067     37    269       C  
ATOM   2657  O   LEU D 409      18.046 -19.885 -86.465  1.00 26.57           O  
ANISOU 2657  O   LEU D 409     4221   3709   2166  -1088    115    212       O  
ATOM   2658  CB  LEU D 409      16.161 -17.752 -85.654  1.00 23.32           C  
ANISOU 2658  CB  LEU D 409     3741   3334   1785  -1085    -55    456       C  
ATOM   2659  CG  LEU D 409      15.001 -18.227 -86.532  1.00 25.40           C  
ANISOU 2659  CG  LEU D 409     4062   3605   1983  -1132   -182    450       C  
ATOM   2660  CD1 LEU D 409      13.748 -18.483 -85.705  1.00 25.04           C  
ANISOU 2660  CD1 LEU D 409     3929   3524   2060  -1119   -288    503       C  
ATOM   2661  CD2 LEU D 409      14.737 -17.225 -87.647  1.00 28.66           C  
ANISOU 2661  CD2 LEU D 409     4564   4071   2253  -1178   -226    512       C  
ATOM   2662  N   LEU D 410      16.743 -21.177 -85.172  1.00 22.42           N  
ANISOU 2662  N   LEU D 410     3586   3103   1828  -1065    -15    223       N  
ATOM   2663  CA  LEU D 410      17.221 -22.418 -85.770  1.00 24.20           C  
ANISOU 2663  CA  LEU D 410     3860   3292   2044  -1075     31    100       C  
ATOM   2664  C   LEU D 410      16.132 -23.134 -86.552  1.00 24.23           C  
ANISOU 2664  C   LEU D 410     3936   3291   1980  -1131    -70     59       C  
ATOM   2665  O   LEU D 410      14.985 -23.186 -86.114  1.00 23.86           O  
ANISOU 2665  O   LEU D 410     3852   3238   1977  -1140   -185    117       O  
ATOM   2666  CB  LEU D 410      17.757 -23.347 -84.688  1.00 25.45           C  
ANISOU 2666  CB  LEU D 410     3925   3380   2367  -1026     69     72       C  
ATOM   2667  CG  LEU D 410      18.770 -22.718 -83.738  1.00 26.32           C  
ANISOU 2667  CG  LEU D 410     3949   3494   2557   -982    148    127       C  
ATOM   2668  CD1 LEU D 410      19.100 -23.732 -82.678  1.00 28.87           C  
ANISOU 2668  CD1 LEU D 410     4182   3744   3042   -949    150    115       C  
ATOM   2669  CD2 LEU D 410      20.015 -22.265 -84.488  1.00 30.34           C  
ANISOU 2669  CD2 LEU D 410     4500   4036   2991   -976    274     81       C  
ATOM   2670  N   ASP D 411      16.487 -23.690 -87.705  1.00 26.47           N  
ANISOU 2670  N   ASP D 411     4324   3577   2157  -1177    -22    -46       N  
ATOM   2671  CA  ASP D 411      15.538 -24.510 -88.443  1.00 28.63           C  
ANISOU 2671  CA  ASP D 411     4673   3843   2362  -1245   -109    -98       C  
ATOM   2672  C   ASP D 411      15.693 -25.965 -88.027  1.00 28.96           C  
ANISOU 2672  C   ASP D 411     4686   3797   2520  -1224    -79   -196       C  
ATOM   2673  O   ASP D 411      16.502 -26.287 -87.158  1.00 27.20           O  
ANISOU 2673  O   ASP D 411     4379   3522   2435  -1156     -4   -207       O  
ATOM   2674  CB  ASP D 411      15.706 -24.343 -89.962  1.00 33.96           C  
ANISOU 2674  CB  ASP D 411     5496   4569   2840  -1333    -81   -160       C  
ATOM   2675  CG  ASP D 411      17.088 -24.741 -90.470  1.00 36.35           C  
ANISOU 2675  CG  ASP D 411     5845   4848   3117  -1331     93   -286       C  
ATOM   2676  OD1 ASP D 411      17.804 -25.522 -89.809  1.00 37.02           O  
ANISOU 2676  OD1 ASP D 411     5859   4861   3347  -1266    180   -349       O  
ATOM   2677  OD2 ASP D 411      17.463 -24.258 -91.560  1.00 39.45           O  
ANISOU 2677  OD2 ASP D 411     6348   5294   3348  -1399    145   -320       O  
ATOM   2678  N   ARG D 412      14.920 -26.836 -88.661  1.00 34.55           N  
ANISOU 2678  N   ARG D 412     5466   4489   3172  -1290   -144   -259       N  
ATOM   2679  CA  ARG D 412      14.887 -28.248 -88.308  1.00 35.83           C  
ANISOU 2679  CA  ARG D 412     5611   4561   3443  -1280   -131   -348       C  
ATOM   2680  C   ARG D 412      16.243 -28.933 -88.484  1.00 38.53           C  
ANISOU 2680  C   ARG D 412     5961   4836   3841  -1244     35   -467       C  
ATOM   2681  O   ARG D 412      16.666 -29.710 -87.631  1.00 37.70           O  
ANISOU 2681  O   ARG D 412     5775   4648   3903  -1181     70   -489       O  
ATOM   2682  CB  ARG D 412      13.827 -28.956 -89.148  1.00 36.75           C  
ANISOU 2682  CB  ARG D 412     5825   4682   3456  -1376   -223   -401       C  
ATOM   2683  CG  ARG D 412      13.557 -30.391 -88.752  1.00 38.89           C  
ANISOU 2683  CG  ARG D 412     6081   4859   3836  -1375   -232   -481       C  
ATOM   2684  CD  ARG D 412      12.502 -31.013 -89.654  1.00 38.68           C  
ANISOU 2684  CD  ARG D 412     6161   4848   3688  -1486   -324   -533       C  
ATOM   2685  NE  ARG D 412      12.820 -30.833 -91.070  1.00 47.45           N  
ANISOU 2685  NE  ARG D 412     7414   6006   4607  -1577   -267   -610       N  
ATOM   2686  CZ  ARG D 412      12.282 -29.899 -91.850  1.00 46.48           C  
ANISOU 2686  CZ  ARG D 412     7357   5983   4320  -1651   -350   -540       C  
ATOM   2687  NH1 ARG D 412      11.393 -29.047 -91.354  1.00 48.29           N  
ANISOU 2687  NH1 ARG D 412     7510   6268   4571  -1631   -489   -392       N  
ATOM   2688  NH2 ARG D 412      12.641 -29.814 -93.122  1.00 45.70           N  
ANISOU 2688  NH2 ARG D 412     7399   5924   4040  -1748   -291   -617       N  
ATOM   2689  N   ASN D 413      16.921 -28.643 -89.590  1.00 36.31           N  
ANISOU 2689  N   ASN D 413     5778   4590   3429  -1288    136   -542       N  
ATOM   2690  CA  ASN D 413      18.226 -29.241 -89.855  1.00 36.64           C  
ANISOU 2690  CA  ASN D 413     5825   4567   3529  -1257    310   -664       C  
ATOM   2691  C   ASN D 413      19.278 -28.850 -88.818  1.00 37.23           C  
ANISOU 2691  C   ASN D 413     5765   4619   3762  -1151    383   -607       C  
ATOM   2692  O   ASN D 413      20.083 -29.682 -88.400  1.00 38.94           O  
ANISOU 2692  O   ASN D 413     5917   4746   4134  -1092    472   -669       O  
ATOM   2693  CB  ASN D 413      18.710 -28.865 -91.258  1.00 38.26           C  
ANISOU 2693  CB  ASN D 413     6166   4826   3545  -1341    409   -753       C  
ATOM   2694  CG  ASN D 413      17.902 -29.535 -92.352  1.00 42.54           C  
ANISOU 2694  CG  ASN D 413     6854   5373   3938  -1463    367   -843       C  
ATOM   2695  OD1 ASN D 413      17.247 -30.553 -92.123  1.00 44.39           O  
ANISOU 2695  OD1 ASN D 413     7085   5544   4237  -1473    308   -881       O  
ATOM   2696  ND2 ASN D 413      17.949 -28.970 -93.553  1.00 43.75           N  
ANISOU 2696  ND2 ASN D 413     7140   5602   3882  -1567    395   -876       N  
ATOM   2697  N   GLN D 414      19.266 -27.588 -88.399  1.00 36.09           N  
ANISOU 2697  N   GLN D 414     5577   4553   3584  -1130    343   -484       N  
ATOM   2698  CA  GLN D 414      20.190 -27.133 -87.366  1.00 36.22           C  
ANISOU 2698  CA  GLN D 414     5469   4558   3734  -1047    398   -417       C  
ATOM   2699  C   GLN D 414      19.841 -27.763 -86.023  1.00 33.58           C  
ANISOU 2699  C   GLN D 414     5021   4157   3580   -995    319   -355       C  
ATOM   2700  O   GLN D 414      20.712 -27.963 -85.178  1.00 37.42           O  
ANISOU 2700  O   GLN D 414     5405   4598   4214   -932    372   -334       O  
ATOM   2701  CB  GLN D 414      20.188 -25.604 -87.263  1.00 35.65           C  
ANISOU 2701  CB  GLN D 414     5391   4583   3571  -1051    376   -304       C  
ATOM   2702  CG  GLN D 414      20.803 -24.917 -88.471  1.00 36.29           C  
ANISOU 2702  CG  GLN D 414     5575   4727   3488  -1099    472   -355       C  
ATOM   2703  CD  GLN D 414      20.468 -23.440 -88.556  1.00 35.20           C  
ANISOU 2703  CD  GLN D 414     5459   4680   3234  -1122    418   -239       C  
ATOM   2704  OE1 GLN D 414      19.446 -22.989 -88.040  1.00 29.78           O  
ANISOU 2704  OE1 GLN D 414     4744   4014   2556  -1122    291   -135       O  
ATOM   2705  NE2 GLN D 414      21.340 -22.677 -89.203  1.00 37.91           N  
ANISOU 2705  NE2 GLN D 414     5852   5074   3478  -1142    521   -258       N  
ATOM   2706  N   GLY D 415      18.567 -28.091 -85.838  1.00 31.72           N  
ANISOU 2706  N   GLY D 415     4803   3918   3330  -1029    189   -325       N  
ATOM   2707  CA  GLY D 415      18.126 -28.769 -84.632  1.00 32.99           C  
ANISOU 2707  CA  GLY D 415     4874   4016   3646   -999    111   -276       C  
ATOM   2708  C   GLY D 415      18.789 -30.122 -84.449  1.00 37.28           C  
ANISOU 2708  C   GLY D 415     5388   4446   4332   -963    175   -364       C  
ATOM   2709  O   GLY D 415      18.992 -30.574 -83.324  1.00 37.13           O  
ANISOU 2709  O   GLY D 415     5271   4368   4470   -921    148   -313       O  
ATOM   2710  N   LYS D 416      19.131 -30.769 -85.560  1.00 37.28           N  
ANISOU 2710  N   LYS D 416     5473   4411   4279   -986    261   -497       N  
ATOM   2711  CA  LYS D 416      19.799 -32.067 -85.524  1.00 38.37           C  
ANISOU 2711  CA  LYS D 416     5588   4428   4564   -949    342   -596       C  
ATOM   2712  C   LYS D 416      21.180 -31.978 -84.885  1.00 39.35           C  
ANISOU 2712  C   LYS D 416     5596   4511   4843   -867    441   -571       C  
ATOM   2713  O   LYS D 416      21.726 -32.982 -84.431  1.00 40.19           O  
ANISOU 2713  O   LYS D 416     5636   4506   5127   -817    477   -602       O  
ATOM   2714  CB  LYS D 416      19.929 -32.644 -86.934  1.00 40.34           C  
ANISOU 2714  CB  LYS D 416     5963   4652   4710  -1004    441   -756       C  
ATOM   2715  CG  LYS D 416      18.628 -32.742 -87.705  1.00 38.20           C  
ANISOU 2715  CG  LYS D 416     5816   4428   4268  -1103    343   -784       C  
ATOM   2716  CD  LYS D 416      18.893 -33.224 -89.121  1.00 41.01           C  
ANISOU 2716  CD  LYS D 416     6309   4769   4504  -1176    457   -945       C  
ATOM   2717  CE  LYS D 416      17.614 -33.345 -89.925  1.00 40.20           C  
ANISOU 2717  CE  LYS D 416     6335   4719   4222  -1292    350   -968       C  
ATOM   2718  NZ  LYS D 416      17.910 -33.263 -91.381  1.00 42.96           N  
ANISOU 2718  NZ  LYS D 416     6832   5104   4386  -1389    453  -1089       N  
ATOM   2719  N   GLU D 419      22.058 -32.026 -79.446  1.00 30.53           N  
ANISOU 2719  N   GLU D 419     4018   3295   4290   -742    187   -104       N  
ATOM   2720  CA  GLU D 419      21.913 -33.282 -78.723  1.00 29.29           C  
ANISOU 2720  CA  GLU D 419     3813   3021   4294   -733    121    -91       C  
ATOM   2721  C   GLU D 419      20.605 -33.288 -77.936  1.00 28.87           C  
ANISOU 2721  C   GLU D 419     3778   2990   4201   -796    -17    -20       C  
ATOM   2722  O   GLU D 419      20.251 -32.298 -77.291  1.00 31.39           O  
ANISOU 2722  O   GLU D 419     4078   3395   4453   -833    -65     75       O  
ATOM   2723  CB  GLU D 419      23.105 -33.508 -77.785  1.00 28.04           C  
ANISOU 2723  CB  GLU D 419     3525   2807   4321   -687    135     -8       C  
ATOM   2724  CG  GLU D 419      23.342 -32.378 -76.799  1.00 30.45           C  
ANISOU 2724  CG  GLU D 419     3768   3205   4596   -716     94    130       C  
ATOM   2725  CD  GLU D 419      24.430 -32.696 -75.793  1.00 30.15           C  
ANISOU 2725  CD  GLU D 419     3602   3112   4742   -690     79    228       C  
ATOM   2726  OE1 GLU D 419      24.109 -33.302 -74.750  1.00 28.50           O  
ANISOU 2726  OE1 GLU D 419     3352   2849   4627   -722    -28    311       O  
ATOM   2727  OE2 GLU D 419      25.601 -32.338 -76.042  1.00 33.44           O  
ANISOU 2727  OE2 GLU D 419     3957   3541   5206   -645    171    227       O  
ATOM   2728  N   GLY D 420      19.875 -34.394 -78.016  1.00 30.17           N  
ANISOU 2728  N   GLY D 420     3982   3074   4406   -813    -71    -72       N  
ATOM   2729  CA  GLY D 420      18.632 -34.535 -77.280  1.00 30.32           C  
ANISOU 2729  CA  GLY D 420     4014   3105   4402   -877   -197    -15       C  
ATOM   2730  C   GLY D 420      17.394 -34.085 -78.035  1.00 28.56           C  
ANISOU 2730  C   GLY D 420     3884   2959   4009   -927   -233    -61       C  
ATOM   2731  O   GLY D 420      16.276 -34.298 -77.569  1.00 23.59           O  
ANISOU 2731  O   GLY D 420     3267   2334   3364   -981   -330    -32       O  
ATOM   2732  N   MET D 421      17.583 -33.484 -79.208  1.00 28.09           N  
ANISOU 2732  N   MET D 421     3887   2960   3826   -916   -158   -129       N  
ATOM   2733  CA  MET D 421      16.481 -32.822 -79.905  1.00 24.38           C  
ANISOU 2733  CA  MET D 421     3494   2579   3191   -967   -203   -142       C  
ATOM   2734  C   MET D 421      16.020 -33.554 -81.162  1.00 27.48           C  
ANISOU 2734  C   MET D 421     3993   2946   3502   -995   -191   -267       C  
ATOM   2735  O   MET D 421      15.303 -32.978 -81.978  1.00 26.71           O  
ANISOU 2735  O   MET D 421     3967   2926   3255  -1039   -218   -283       O  
ATOM   2736  CB  MET D 421      16.879 -31.387 -80.274  1.00 28.02           C  
ANISOU 2736  CB  MET D 421     3959   3145   3542   -956   -150   -102       C  
ATOM   2737  CG  MET D 421      16.987 -30.454 -79.074  1.00 22.59           C  
ANISOU 2737  CG  MET D 421     3186   2504   2895   -956   -177     25       C  
ATOM   2738  SD  MET D 421      16.635 -28.707 -79.367  1.00 27.24           S  
ANISOU 2738  SD  MET D 421     3795   3218   3337   -974   -170     90       S  
ATOM   2739  CE  MET D 421      14.845 -28.729 -79.291  1.00 23.30           C  
ANISOU 2739  CE  MET D 421     3320   2740   2793  -1034   -298    113       C  
ATOM   2740  N   VAL D 422      16.425 -34.814 -81.313  1.00 28.66           N  
ANISOU 2740  N   VAL D 422     4154   2984   3751   -977   -151   -351       N  
ATOM   2741  CA  VAL D 422      16.052 -35.607 -82.488  1.00 29.68           C  
ANISOU 2741  CA  VAL D 422     4394   3078   3807  -1016   -124   -483       C  
ATOM   2742  C   VAL D 422      14.535 -35.679 -82.680  1.00 29.21           C  
ANISOU 2742  C   VAL D 422     4394   3064   3642  -1097   -247   -476       C  
ATOM   2743  O   VAL D 422      14.047 -35.560 -83.804  1.00 34.60           O  
ANISOU 2743  O   VAL D 422     5176   3796   4176  -1153   -247   -543       O  
ATOM   2744  CB  VAL D 422      16.635 -37.042 -82.413  1.00 32.21           C  
ANISOU 2744  CB  VAL D 422     4706   3247   4285   -984    -66   -568       C  
ATOM   2745  CG1 VAL D 422      16.020 -37.945 -83.478  1.00 33.35           C  
ANISOU 2745  CG1 VAL D 422     4972   3349   4352  -1046    -53   -704       C  
ATOM   2746  CG2 VAL D 422      18.138 -36.994 -82.601  1.00 33.97           C  
ANISOU 2746  CG2 VAL D 422     4881   3425   4601   -909     76   -604       C  
ATOM   2747  N   GLU D 423      13.792 -35.851 -81.588  1.00 28.24           N  
ANISOU 2747  N   GLU D 423     4209   2929   3593  -1111   -354   -392       N  
ATOM   2748  CA  GLU D 423      12.331 -35.860 -81.655  1.00 26.12           C  
ANISOU 2748  CA  GLU D 423     3974   2707   3243  -1186   -473   -374       C  
ATOM   2749  C   GLU D 423      11.722 -34.560 -81.133  1.00 24.89           C  
ANISOU 2749  C   GLU D 423     3762   2658   3038  -1196   -539   -257       C  
ATOM   2750  O   GLU D 423      10.685 -34.114 -81.623  1.00 24.94           O  
ANISOU 2750  O   GLU D 423     3801   2735   2939  -1247   -612   -242       O  
ATOM   2751  CB  GLU D 423      11.746 -37.024 -80.857  1.00 28.11           C  
ANISOU 2751  CB  GLU D 423     4204   2869   3608  -1212   -545   -376       C  
ATOM   2752  CG  GLU D 423      12.345 -38.378 -81.155  1.00 30.20           C  
ANISOU 2752  CG  GLU D 423     4509   3003   3962  -1195   -482   -480       C  
ATOM   2753  CD  GLU D 423      12.263 -39.294 -79.954  1.00 37.07           C  
ANISOU 2753  CD  GLU D 423     5318   3773   4995  -1190   -537   -435       C  
ATOM   2754  OE1 GLU D 423      11.156 -39.812 -79.673  1.00 36.84           O  
ANISOU 2754  OE1 GLU D 423     5308   3734   4956  -1255   -633   -431       O  
ATOM   2755  OE2 GLU D 423      13.300 -39.478 -79.275  1.00 40.38           O  
ANISOU 2755  OE2 GLU D 423     5666   4124   5552  -1127   -490   -397       O  
ATOM   2756  N   ILE D 424      12.366 -33.960 -80.135  1.00 20.92           N  
ANISOU 2756  N   ILE D 424     3239   2186   2524   -827    431   -245       N  
ATOM   2757  CA  ILE D 424      11.778 -32.834 -79.413  1.00 16.08           C  
ANISOU 2757  CA  ILE D 424     2714   1560   1838   -804    368    -84       C  
ATOM   2758  C   ILE D 424      11.602 -31.592 -80.293  1.00 14.89           C  
ANISOU 2758  C   ILE D 424     2574   1613   1471   -751    294    -16       C  
ATOM   2759  O   ILE D 424      10.603 -30.880 -80.168  1.00 18.04           O  
ANISOU 2759  O   ILE D 424     2982   2062   1809   -731    240     17       O  
ATOM   2760  CB  ILE D 424      12.621 -32.483 -78.166  1.00 18.89           C  
ANISOU 2760  CB  ILE D 424     3034   1872   2271   -652    305     82       C  
ATOM   2761  CG1 ILE D 424      12.569 -33.630 -77.154  1.00 21.09           C  
ANISOU 2761  CG1 ILE D 424     3209   2074   2730   -603    308     64       C  
ATOM   2762  CG2 ILE D 424      12.117 -31.215 -77.503  1.00 19.27           C  
ANISOU 2762  CG2 ILE D 424     3080   1971   2270   -572    226    177       C  
ATOM   2763  CD1 ILE D 424      13.569 -33.496 -76.028  1.00 22.65           C  
ANISOU 2763  CD1 ILE D 424     3346   2270   2990   -509    251    180       C  
ATOM   2764  N   PHE D 425      12.553 -31.342 -81.188  1.00 15.90           N  
ANISOU 2764  N   PHE D 425     2691   1856   1493   -726    297     11       N  
ATOM   2765  CA  PHE D 425      12.475 -30.170 -82.059  1.00 19.83           C  
ANISOU 2765  CA  PHE D 425     3190   2552   1792   -671    237    108       C  
ATOM   2766  C   PHE D 425      11.161 -30.146 -82.845  1.00 19.77           C  
ANISOU 2766  C   PHE D 425     3101   2733   1676   -654    189    -19       C  
ATOM   2767  O   PHE D 425      10.467 -29.131 -82.876  1.00 16.81           O  
ANISOU 2767  O   PHE D 425     2742   2429   1217   -617    123     87       O  
ATOM   2768  CB  PHE D 425      13.662 -30.133 -83.024  1.00 20.49           C  
ANISOU 2768  CB  PHE D 425     3253   2754   1779   -652    267    129       C  
ATOM   2769  CG  PHE D 425      13.955 -28.765 -83.571  1.00 20.38           C  
ANISOU 2769  CG  PHE D 425     3254   2867   1623   -583    216    318       C  
ATOM   2770  CD1 PHE D 425      13.194 -28.234 -84.597  1.00 22.22           C  
ANISOU 2770  CD1 PHE D 425     3419   3328   1696   -530    164    307       C  
ATOM   2771  CD2 PHE D 425      14.994 -28.010 -83.055  1.00 21.69           C  
ANISOU 2771  CD2 PHE D 425     3394   2900   1947   -489    200    454       C  
ATOM   2772  CE1 PHE D 425      13.464 -26.978 -85.099  1.00 25.99           C  
ANISOU 2772  CE1 PHE D 425     3855   3849   2172   -400    126    460       C  
ATOM   2773  CE2 PHE D 425      15.270 -26.751 -83.555  1.00 22.01           C  
ANISOU 2773  CE2 PHE D 425     3374   3010   1979   -362    174    571       C  
ATOM   2774  CZ  PHE D 425      14.501 -26.236 -84.579  1.00 24.30           C  
ANISOU 2774  CZ  PHE D 425     3647   3475   2111   -323    146    583       C  
ATOM   2775  N   ASP D 426      10.825 -31.273 -83.467  1.00 17.26           N  
ANISOU 2775  N   ASP D 426     2686   2492   1379   -682    221   -254       N  
ATOM   2776  CA  ASP D 426       9.584 -31.394 -84.230  1.00 19.99           C  
ANISOU 2776  CA  ASP D 426     2938   3027   1632   -671    171   -411       C  
ATOM   2777  C   ASP D 426       8.348 -31.281 -83.336  1.00 17.84           C  
ANISOU 2777  C   ASP D 426     2678   2635   1466   -685    141   -411       C  
ATOM   2778  O   ASP D 426       7.315 -30.750 -83.755  1.00 18.41           O  
ANISOU 2778  O   ASP D 426     2706   2848   1441   -656     71   -426       O  
ATOM   2779  CB  ASP D 426       9.556 -32.722 -84.993  1.00 23.88           C  
ANISOU 2779  CB  ASP D 426     3311   3601   2160   -707    221   -697       C  
ATOM   2780  CG  ASP D 426      10.513 -32.740 -86.172  1.00 28.03           C  
ANISOU 2780  CG  ASP D 426     3796   4334   2522   -685    241   -736       C  
ATOM   2781  OD1 ASP D 426      10.839 -31.656 -86.700  1.00 26.45           O  
ANISOU 2781  OD1 ASP D 426     3633   4291   2127   -632    197   -557       O  
ATOM   2782  OD2 ASP D 426      10.939 -33.844 -86.579  1.00 29.89           O  
ANISOU 2782  OD2 ASP D 426     3953   4571   2832   -721    309   -947       O  
ATOM   2783  N   MET D 427       8.456 -31.780 -82.108  1.00 17.78           N  
ANISOU 2783  N   MET D 427     2724   2376   1658   -728    195   -388       N  
ATOM   2784  CA  MET D 427       7.351 -31.697 -81.163  1.00 17.26           C  
ANISOU 2784  CA  MET D 427     2673   2188   1697   -744    183   -379       C  
ATOM   2785  C   MET D 427       7.067 -30.232 -80.834  1.00 16.53           C  
ANISOU 2785  C   MET D 427     2654   2119   1508   -698    115   -175       C  
ATOM   2786  O   MET D 427       5.910 -29.801 -80.802  1.00 17.92           O  
ANISOU 2786  O   MET D 427     2800   2341   1668   -684     68   -192       O  
ATOM   2787  CB  MET D 427       7.661 -32.487 -79.888  1.00 16.47           C  
ANISOU 2787  CB  MET D 427     2617   1831   1809   -795    262   -359       C  
ATOM   2788  CG  MET D 427       7.665 -34.004 -80.061  1.00 18.07           C  
ANISOU 2788  CG  MET D 427     2723   1965   2176   -844    338   -566       C  
ATOM   2789  SD  MET D 427       8.254 -34.875 -78.599  1.00 20.79           S  
ANISOU 2789  SD  MET D 427     3081   2069   2748   -822    406   -442       S  
ATOM   2790  CE  MET D 427       6.748 -34.931 -77.651  1.00 30.85           C  
ANISOU 2790  CE  MET D 427     4316   3303   4104   -784    385   -421       C  
ATOM   2791  N   LEU D 428       8.133 -29.473 -80.600  1.00 14.64           N  
ANISOU 2791  N   LEU D 428     2500   1838   1224   -676    112     10       N  
ATOM   2792  CA  LEU D 428       8.020 -28.050 -80.303  1.00 14.07           C  
ANISOU 2792  CA  LEU D 428     2487   1769   1091   -633     56    203       C  
ATOM   2793  C   LEU D 428       7.428 -27.280 -81.484  1.00 15.11           C  
ANISOU 2793  C   LEU D 428     2551   2129   1060   -577    -17    224       C  
ATOM   2794  O   LEU D 428       6.582 -26.401 -81.300  1.00 15.77           O  
ANISOU 2794  O   LEU D 428     2631   2226   1136   -548    -70    300       O  
ATOM   2795  CB  LEU D 428       9.389 -27.483 -79.921  1.00 13.27           C  
ANISOU 2795  CB  LEU D 428     2426   1583   1034   -591     65    346       C  
ATOM   2796  CG  LEU D 428       9.926 -27.923 -78.553  1.00 13.22           C  
ANISOU 2796  CG  LEU D 428     2393   1408   1223   -555     91    314       C  
ATOM   2797  CD1 LEU D 428      11.404 -27.610 -78.431  1.00 11.76           C  
ANISOU 2797  CD1 LEU D 428     2138   1223   1106   -466     90    363       C  
ATOM   2798  CD2 LEU D 428       9.150 -27.265 -77.417  1.00 15.34           C  
ANISOU 2798  CD2 LEU D 428     2615   1632   1582   -493     65    321       C  
ATOM   2799  N   LEU D 429       7.875 -27.624 -82.690  1.00 15.48           N  
ANISOU 2799  N   LEU D 429     2538   2365    979   -561    -19    159       N  
ATOM   2800  CA  LEU D 429       7.369 -27.001 -83.910  1.00 16.78           C  
ANISOU 2800  CA  LEU D 429     2626   2789    959   -505    -89    182       C  
ATOM   2801  C   LEU D 429       5.879 -27.248 -84.060  1.00 17.50           C  
ANISOU 2801  C   LEU D 429     2635   2957   1056   -506   -139     40       C  
ATOM   2802  O   LEU D 429       5.128 -26.350 -84.442  1.00 18.07           O  
ANISOU 2802  O   LEU D 429     2671   3148   1048   -457   -213    132       O  
ATOM   2803  CB  LEU D 429       8.100 -27.527 -85.148  1.00 20.65           C  
ANISOU 2803  CB  LEU D 429     3057   3489   1300   -496    -69     98       C  
ATOM   2804  CG  LEU D 429       9.534 -27.042 -85.366  1.00 22.10           C  
ANISOU 2804  CG  LEU D 429     3280   3632   1485   -451    -29    255       C  
ATOM   2805  CD1 LEU D 429      10.143 -27.727 -86.586  1.00 20.47           C  
ANISOU 2805  CD1 LEU D 429     3004   3624   1151   -445      2    131       C  
ATOM   2806  CD2 LEU D 429       9.597 -25.522 -85.504  1.00 19.40           C  
ANISOU 2806  CD2 LEU D 429     2936   3243   1194   -332    -67    464       C  
ATOM   2807  N   ALA D 430       5.460 -28.474 -83.764  1.00 17.44           N  
ANISOU 2807  N   ALA D 430     2589   2875   1164   -562    -96   -179       N  
ATOM   2808  CA  ALA D 430       4.052 -28.841 -83.859  1.00 20.52           C  
ANISOU 2808  CA  ALA D 430     2889   3316   1590   -572   -134   -340       C  
ATOM   2809  C   ALA D 430       3.218 -28.052 -82.859  1.00 17.31           C  
ANISOU 2809  C   ALA D 430     2529   2764   1285   -564   -158   -221       C  
ATOM   2810  O   ALA D 430       2.065 -27.729 -83.126  1.00 18.85           O  
ANISOU 2810  O   ALA D 430     2652   3050   1459   -541   -221   -259       O  
ATOM   2811  CB  ALA D 430       3.877 -30.333 -83.639  1.00 21.06           C  
ANISOU 2811  CB  ALA D 430     2903   3291   1808   -639    -65   -587       C  
ATOM   2812  N   THR D 431       3.809 -27.727 -81.714  1.00 16.76           N  
ANISOU 2812  N   THR D 431     2569   2476   1323   -581   -109    -84       N  
ATOM   2813  CA  THR D 431       3.090 -26.983 -80.685  1.00 23.06           C  
ANISOU 2813  CA  THR D 431     3410   3133   2218   -578   -120     11       C  
ATOM   2814  C   THR D 431       2.894 -25.527 -81.116  1.00 15.06           C  
ANISOU 2814  C   THR D 431     2393   2221   1111   -509   -198    191       C  
ATOM   2815  O   THR D 431       1.810 -24.964 -80.961  1.00 16.15           O  
ANISOU 2815  O   THR D 431     2489   2363   1284   -488   -242    204       O  
ATOM   2816  CB  THR D 431       3.824 -27.039 -79.335  1.00 18.65           C  
ANISOU 2816  CB  THR D 431     2964   2339   1782   -615    -49     96       C  
ATOM   2817  OG1 THR D 431       4.059 -28.407 -78.978  1.00 17.87           O  
ANISOU 2817  OG1 THR D 431     2860   2146   1785   -674     26    -41       O  
ATOM   2818  CG2 THR D 431       2.991 -26.378 -78.244  1.00 12.84           C  
ANISOU 2818  CG2 THR D 431     2261   1474   1142   -618    -49    154       C  
ATOM   2819  N   SER D 432       3.941 -24.921 -81.662  1.00 16.93           N  
ANISOU 2819  N   SER D 432     2660   2528   1244   -473   -211    338       N  
ATOM   2820  CA  SER D 432       3.833 -23.553 -82.148  1.00 16.18           C  
ANISOU 2820  CA  SER D 432     2545   2525   1077   -405   -277    531       C  
ATOM   2821  C   SER D 432       2.853 -23.496 -83.315  1.00 17.76           C  
ANISOU 2821  C   SER D 432     2625   2972   1152   -361   -357    479       C  
ATOM   2822  O   SER D 432       2.080 -22.548 -83.439  1.00 23.66           O  
ANISOU 2822  O   SER D 432     3326   3758   1905   -313   -419    587       O  
ATOM   2823  CB  SER D 432       5.206 -23.012 -82.553  1.00 24.09           C  
ANISOU 2823  CB  SER D 432     3554   3513   2087   -333   -236    641       C  
ATOM   2824  OG  SER D 432       5.620 -23.540 -83.799  1.00 36.80           O  
ANISOU 2824  OG  SER D 432     5116   5324   3542   -317   -244    589       O  
ATOM   2825  N   SER D 433       2.875 -24.529 -84.152  1.00 18.28           N  
ANISOU 2825  N   SER D 433     2631   3204   1112   -379   -355    304       N  
ATOM   2826  CA  SER D 433       1.908 -24.665 -85.236  1.00 22.12           C  
ANISOU 2826  CA  SER D 433     2991   3945   1469   -346   -435    206       C  
ATOM   2827  C   SER D 433       0.481 -24.646 -84.695  1.00 23.21           C  
ANISOU 2827  C   SER D 433     3078   4009   1731   -354   -470    121       C  
ATOM   2828  O   SER D 433      -0.396 -23.977 -85.243  1.00 28.25           O  
ANISOU 2828  O   SER D 433     3633   4791   2311   -301   -557    180       O  
ATOM   2829  CB  SER D 433       2.159 -25.958 -86.019  1.00 22.76           C  
ANISOU 2829  CB  SER D 433     3011   4180   1456   -381   -412    -32       C  
ATOM   2830  OG  SER D 433       1.163 -26.173 -87.003  1.00 34.18           O  
ANISOU 2830  OG  SER D 433     4325   5881   2780   -355   -494   -166       O  
ATOM   2831  N   ARG D 434       0.258 -25.379 -83.611  1.00 19.12           N  
ANISOU 2831  N   ARG D 434     2604   3268   1392   -420   -400     -6       N  
ATOM   2832  CA  ARG D 434      -1.068 -25.473 -83.008  1.00 22.41           C  
ANISOU 2832  CA  ARG D 434     2973   3595   1945   -437   -412   -101       C  
ATOM   2833  C   ARG D 434      -1.488 -24.144 -82.384  1.00 18.67           C  
ANISOU 2833  C   ARG D 434     2530   3018   1544   -396   -440     94       C  
ATOM   2834  O   ARG D 434      -2.642 -23.733 -82.516  1.00 19.42           O  
ANISOU 2834  O   ARG D 434     2543   3162   1673   -368   -500     82       O  
ATOM   2835  CB  ARG D 434      -1.097 -26.582 -81.962  1.00 20.92           C  
ANISOU 2835  CB  ARG D 434     2826   3191   1931   -516   -312   -255       C  
ATOM   2836  CG  ARG D 434      -2.409 -26.703 -81.196  1.00 21.55           C  
ANISOU 2836  CG  ARG D 434     2864   3153   2171   -540   -301   -342       C  
ATOM   2837  CD  ARG D 434      -3.504 -27.338 -82.040  1.00 24.47           C  
ANISOU 2837  CD  ARG D 434     3086   3685   2526   -541   -358   -547       C  
ATOM   2838  NE  ARG D 434      -4.746 -27.507 -81.289  1.00 23.01           N  
ANISOU 2838  NE  ARG D 434     2854   3374   2514   -568   -337   -635       N  
ATOM   2839  CZ  ARG D 434      -5.962 -27.419 -81.820  1.00 26.92           C  
ANISOU 2839  CZ  ARG D 434     3224   3990   3017   -546   -412   -732       C  
ATOM   2840  NH1 ARG D 434      -6.111 -27.162 -83.113  1.00 27.66           N  
ANISOU 2840  NH1 ARG D 434     3224   4349   2936   -494   -522   -750       N  
ATOM   2841  NH2 ARG D 434      -7.033 -27.592 -81.055  1.00 27.58           N  
ANISOU 2841  NH2 ARG D 434     3266   3936   3276   -575   -377   -808       N  
ATOM   2842  N   PHE D 435      -0.554 -23.480 -81.705  1.00 17.96           N  
ANISOU 2842  N   PHE D 435     2549   2781   1495   -394   -397    262       N  
ATOM   2843  CA  PHE D 435      -0.800 -22.140 -81.179  1.00 17.67           C  
ANISOU 2843  CA  PHE D 435     2532   2644   1537   -354   -420    444       C  
ATOM   2844  C   PHE D 435      -1.249 -21.194 -82.294  1.00 22.63           C  
ANISOU 2844  C   PHE D 435     3062   3472   2065   -272   -521    579       C  
ATOM   2845  O   PHE D 435      -2.143 -20.371 -82.104  1.00 19.50           O  
ANISOU 2845  O   PHE D 435     2612   3042   1757   -237   -563    647       O  
ATOM   2846  CB  PHE D 435       0.453 -21.580 -80.494  1.00 18.36           C  
ANISOU 2846  CB  PHE D 435     2734   2579   1663   -361   -367    593       C  
ATOM   2847  CG  PHE D 435       0.655 -22.067 -79.083  1.00 21.73           C  
ANISOU 2847  CG  PHE D 435     3254   2783   2221   -427   -281    518       C  
ATOM   2848  CD1 PHE D 435      -0.239 -22.944 -78.497  1.00 19.45           C  
ANISOU 2848  CD1 PHE D 435     2946   2430   2016   -475   -243    348       C  
ATOM   2849  CD2 PHE D 435       1.731 -21.618 -78.337  1.00 24.30           C  
ANISOU 2849  CD2 PHE D 435     3676   2970   2587   -439   -238    627       C  
ATOM   2850  CE1 PHE D 435      -0.054 -23.384 -77.196  1.00 26.13           C  
ANISOU 2850  CE1 PHE D 435     3872   3091   2967   -532   -159    306       C  
ATOM   2851  CE2 PHE D 435       1.924 -22.049 -77.035  1.00 23.03           C  
ANISOU 2851  CE2 PHE D 435     3586   2637   2528   -489   -165    562       C  
ATOM   2852  CZ  PHE D 435       1.031 -22.932 -76.467  1.00 22.46           C  
ANISOU 2852  CZ  PHE D 435     3506   2511   2517   -540   -125    419       C  
ATOM   2853  N   ARG D 436      -0.624 -21.328 -83.459  1.00 21.71           N  
ANISOU 2853  N   ARG D 436     2914   3570   1765   -241   -556    621       N  
ATOM   2854  CA  ARG D 436      -0.970 -20.500 -84.607  1.00 24.46           C  
ANISOU 2854  CA  ARG D 436     3163   4146   1985   -159   -652    771       C  
ATOM   2855  C   ARG D 436      -2.355 -20.830 -85.141  1.00 22.91           C  
ANISOU 2855  C   ARG D 436     2839   4107   1757   -144   -732    636       C  
ATOM   2856  O   ARG D 436      -3.147 -19.932 -85.426  1.00 34.27           O  
ANISOU 2856  O   ARG D 436     4196   5608   3218    -83   -808    762       O  
ATOM   2857  CB  ARG D 436       0.073 -20.655 -85.712  1.00 28.16           C  
ANISOU 2857  CB  ARG D 436     3633   4753   2313   -122   -624    789       C  
ATOM   2858  CG  ARG D 436       0.256 -19.410 -86.559  1.00 32.33           C  
ANISOU 2858  CG  ARG D 436     4119   5308   2856    -30   -632    965       C  
ATOM   2859  CD  ARG D 436       1.315 -19.632 -87.621  1.00 31.63           C  
ANISOU 2859  CD  ARG D 436     4037   5327   2654    -11   -590    960       C  
ATOM   2860  NE  ARG D 436       2.555 -20.111 -87.028  1.00 38.38           N  
ANISOU 2860  NE  ARG D 436     4996   6032   3555    -53   -504    918       N  
ATOM   2861  CZ  ARG D 436       3.082 -21.311 -87.249  1.00 35.19           C  
ANISOU 2861  CZ  ARG D 436     4609   5707   3054    -99   -475    771       C  
ATOM   2862  NH1 ARG D 436       2.478 -22.167 -88.058  1.00 35.35           N  
ANISOU 2862  NH1 ARG D 436     4548   5954   2931   -111   -519    621       N  
ATOM   2863  NH2 ARG D 436       4.214 -21.655 -86.652  1.00 28.32           N  
ANISOU 2863  NH2 ARG D 436     3829   4684   2249   -131   -398    757       N  
ATOM   2864  N   MET D 437      -2.644 -22.122 -85.273  1.00 23.56           N  
ANISOU 2864  N   MET D 437     2896   4250   1808   -198   -716    377       N  
ATOM   2865  CA  MET D 437      -3.952 -22.584 -85.722  1.00 28.34           C  
ANISOU 2865  CA  MET D 437     3373   4992   2403   -195   -787    205       C  
ATOM   2866  C   MET D 437      -5.052 -22.008 -84.829  1.00 26.52           C  
ANISOU 2866  C   MET D 437     3121   4578   2378   -192   -795    230       C  
ATOM   2867  O   MET D 437      -6.135 -21.657 -85.300  1.00 28.28           O  
ANISOU 2867  O   MET D 437     3225   4922   2597   -149   -885    229       O  
ATOM   2868  CB  MET D 437      -4.003 -24.115 -85.716  1.00 27.48           C  
ANISOU 2868  CB  MET D 437     3248   4890   2305   -270   -738    -97       C  
ATOM   2869  CG  MET D 437      -5.362 -24.715 -86.036  1.00 30.61           C  
ANISOU 2869  CG  MET D 437     3506   5388   2736   -281   -799   -314       C  
ATOM   2870  SD  MET D 437      -5.809 -24.573 -87.770  1.00 48.32           S  
ANISOU 2870  SD  MET D 437     5588   8065   4706   -209   -948   -339       S  
ATOM   2871  CE  MET D 437      -4.785 -25.858 -88.481  1.00 34.00           C  
ANISOU 2871  CE  MET D 437     3792   6340   2785   -251   -869   -543       C  
ATOM   2872  N   MET D 438      -4.750 -21.891 -83.539  1.00 23.07           N  
ANISOU 2872  N   MET D 438     2452   3973   2340   -136   -719     91       N  
ATOM   2873  CA  MET D 438      -5.730 -21.455 -82.551  1.00 23.62           C  
ANISOU 2873  CA  MET D 438     2471   3973   2529    -89   -749     76       C  
ATOM   2874  C   MET D 438      -5.749 -19.946 -82.359  1.00 23.08           C  
ANISOU 2874  C   MET D 438     2456   3799   2514     28   -758    259       C  
ATOM   2875  O   MET D 438      -6.632 -19.419 -81.681  1.00 24.92           O  
ANISOU 2875  O   MET D 438     2637   3992   2841     88   -792    254       O  
ATOM   2876  CB  MET D 438      -5.449 -22.118 -81.208  1.00 21.17           C  
ANISOU 2876  CB  MET D 438     2173   3500   2371   -195   -677    -30       C  
ATOM   2877  CG  MET D 438      -5.676 -23.611 -81.177  1.00 24.70           C  
ANISOU 2877  CG  MET D 438     2563   4012   2810   -304   -656   -215       C  
ATOM   2878  SD  MET D 438      -5.520 -24.168 -79.484  1.00 22.85           S  
ANISOU 2878  SD  MET D 438     2358   3578   2747   -394   -576   -289       S  
ATOM   2879  CE  MET D 438      -6.991 -23.428 -78.781  1.00 28.33           C  
ANISOU 2879  CE  MET D 438     2965   4290   3509   -330   -626   -304       C  
ATOM   2880  N   ASN D 439      -4.770 -19.265 -82.948  1.00 20.44           N  
ANISOU 2880  N   ASN D 439     2223   3413   2130     54   -716    409       N  
ATOM   2881  CA  ASN D 439      -4.571 -17.835 -82.732  1.00 21.01           C  
ANISOU 2881  CA  ASN D 439     2364   3337   2280    146   -689    585       C  
ATOM   2882  C   ASN D 439      -4.463 -17.517 -81.239  1.00 22.80           C  
ANISOU 2882  C   ASN D 439     2590   3362   2710    108   -632    536       C  
ATOM   2883  O   ASN D 439      -5.209 -16.691 -80.710  1.00 21.35           O  
ANISOU 2883  O   ASN D 439     2371   3115   2626    189   -657    574       O  
ATOM   2884  CB  ASN D 439      -5.701 -17.017 -83.372  1.00 25.25           C  
ANISOU 2884  CB  ASN D 439     2859   3982   2754    308   -787    694       C  
ATOM   2885  CG  ASN D 439      -5.378 -15.535 -83.432  1.00 30.81           C  
ANISOU 2885  CG  ASN D 439     3655   4527   3523    412   -744    906       C  
ATOM   2886  OD1 ASN D 439      -4.209 -15.152 -83.470  1.00 32.77           O  
ANISOU 2886  OD1 ASN D 439     4008   4641   3799    358   -640    988       O  
ATOM   2887  ND2 ASN D 439      -6.409 -14.693 -83.419  1.00 32.31           N  
ANISOU 2887  ND2 ASN D 439     3801   4721   3753    559   -816    985       N  
ATOM   2888  N   LEU D 440      -3.537 -18.188 -80.562  1.00 19.03           N  
ANISOU 2888  N   LEU D 440     2144   2797   2289    -11   -558    445       N  
ATOM   2889  CA  LEU D 440      -3.357 -17.996 -79.127  1.00 18.35           C  
ANISOU 2889  CA  LEU D 440     2052   2552   2369    -53   -505    387       C  
ATOM   2890  C   LEU D 440      -2.999 -16.550 -78.810  1.00 20.62           C  
ANISOU 2890  C   LEU D 440     2386   2683   2767      8   -451    507       C  
ATOM   2891  O   LEU D 440      -2.142 -15.956 -79.461  1.00 20.04           O  
ANISOU 2891  O   LEU D 440     2390   2558   2665     19   -396    617       O  
ATOM   2892  CB  LEU D 440      -2.274 -18.932 -78.591  1.00 18.02           C  
ANISOU 2892  CB  LEU D 440     2045   2457   2344   -169   -440    290       C  
ATOM   2893  CG  LEU D 440      -1.980 -18.815 -77.096  1.00 17.33           C  
ANISOU 2893  CG  LEU D 440     1953   2235   2397   -211   -389    227       C  
ATOM   2894  CD1 LEU D 440      -3.139 -19.369 -76.290  1.00 16.72           C  
ANISOU 2894  CD1 LEU D 440     1800   2195   2357   -224   -429    127       C  
ATOM   2895  CD2 LEU D 440      -0.687 -19.532 -76.743  1.00 15.81           C  
ANISOU 2895  CD2 LEU D 440     1807   1993   2206   -293   -329    167       C  
ATOM   2896  N   GLN D 441      -3.663 -15.987 -77.808  1.00 16.93           N  
ANISOU 2896  N   GLN D 441     1865   2135   2433     39   -454    476       N  
ATOM   2897  CA  GLN D 441      -3.422 -14.603 -77.418  1.00 17.46           C  
ANISOU 2897  CA  GLN D 441     1958   2041   2636     94   -394    565       C  
ATOM   2898  C   GLN D 441      -2.459 -14.498 -76.237  1.00 20.00           C  
ANISOU 2898  C   GLN D 441     2291   2230   3079      5   -299    481       C  
ATOM   2899  O   GLN D 441      -2.331 -15.430 -75.439  1.00 18.54           O  
ANISOU 2899  O   GLN D 441     2076   2077   2890    -75   -300    354       O  
ATOM   2900  CB  GLN D 441      -4.745 -13.917 -77.085  1.00 21.20           C  
ANISOU 2900  CB  GLN D 441     2351   2510   3194    195   -455    572       C  
ATOM   2901  CG  GLN D 441      -5.740 -13.978 -78.230  1.00 24.52           C  
ANISOU 2901  CG  GLN D 441     2743   3086   3488    304   -564    644       C  
ATOM   2902  CD  GLN D 441      -5.343 -13.067 -79.377  1.00 27.12           C  
ANISOU 2902  CD  GLN D 441     3163   3384   3759    402   -549    849       C  
ATOM   2903  OE1 GLN D 441      -5.286 -11.845 -79.226  1.00 30.56           O  
ANISOU 2903  OE1 GLN D 441     3630   3664   4318    478   -501    958       O  
ATOM   2904  NE2 GLN D 441      -5.040 -13.660 -80.526  1.00 26.03           N  
ANISOU 2904  NE2 GLN D 441     3068   3388   3434    395   -579    900       N  
ATOM   2905  N   GLY D 442      -1.777 -13.360 -76.139  1.00 21.06           N  
ANISOU 2905  N   GLY D 442     2466   2216   3319     22   -211    551       N  
ATOM   2906  CA  GLY D 442      -0.811 -13.135 -75.079  1.00 20.77           C  
ANISOU 2906  CA  GLY D 442     2425   2071   3397    -57   -117    458       C  
ATOM   2907  C   GLY D 442      -1.414 -13.312 -73.699  1.00 18.14           C  
ANISOU 2907  C   GLY D 442     2002   1739   3152    -81   -135    324       C  
ATOM   2908  O   GLY D 442      -0.791 -13.891 -72.810  1.00 16.66           O  
ANISOU 2908  O   GLY D 442     1800   1561   2970   -159   -106    211       O  
ATOM   2909  N   GLU D 443      -2.639 -12.824 -73.527  1.00 20.00           N  
ANISOU 2909  N   GLU D 443     2176   1975   3449     -9   -185    335       N  
ATOM   2910  CA  GLU D 443      -3.337 -12.940 -72.252  1.00 18.81           C  
ANISOU 2910  CA  GLU D 443     1933   1836   3377    -35   -197    203       C  
ATOM   2911  C   GLU D 443      -3.632 -14.398 -71.909  1.00 16.71           C  
ANISOU 2911  C   GLU D 443     1652   1703   2996   -105   -250    109       C  
ATOM   2912  O   GLU D 443      -3.562 -14.800 -70.745  1.00 17.01           O  
ANISOU 2912  O   GLU D 443     1654   1749   3061   -170   -225     -2       O  
ATOM   2913  CB  GLU D 443      -4.632 -12.126 -72.274  1.00 19.56           C  
ANISOU 2913  CB  GLU D 443     1956   1912   3562     63   -243    228       C  
ATOM   2914  CG  GLU D 443      -4.401 -10.629 -72.337  1.00 23.26           C  
ANISOU 2914  CG  GLU D 443     2432   2213   4191    131   -172    306       C  
ATOM   2915  CD  GLU D 443      -4.139 -10.123 -73.743  1.00 29.99           C  
ANISOU 2915  CD  GLU D 443     3379   3026   4991    215   -172    496       C  
ATOM   2916  OE1 GLU D 443      -4.219 -10.920 -74.709  1.00 33.83           O  
ANISOU 2916  OE1 GLU D 443     3911   3641   5304    227   -242    559       O  
ATOM   2917  OE2 GLU D 443      -3.803  -8.923 -73.879  1.00 35.36           O  
ANISOU 2917  OE2 GLU D 443     4089   3543   5803    264    -91    581       O  
ATOM   2918  N   GLU D 444      -3.957 -15.188 -72.928  1.00 15.06           N  
ANISOU 2918  N   GLU D 444     1470   1597   2657    -91   -314    153       N  
ATOM   2919  CA  GLU D 444      -4.187 -16.614 -72.735  1.00 14.28           C  
ANISOU 2919  CA  GLU D 444     1363   1601   2460   -163   -346     66       C  
ATOM   2920  C   GLU D 444      -2.879 -17.325 -72.407  1.00 13.88           C  
ANISOU 2920  C   GLU D 444     1377   1526   2371   -241   -293     35       C  
ATOM   2921  O   GLU D 444      -2.840 -18.185 -71.524  1.00 14.88           O  
ANISOU 2921  O   GLU D 444     1496   1672   2485   -303   -281    -50       O  
ATOM   2922  CB  GLU D 444      -4.826 -17.238 -73.975  1.00 16.42           C  
ANISOU 2922  CB  GLU D 444     1632   1996   2611   -132   -421     98       C  
ATOM   2923  CG  GLU D 444      -6.228 -16.736 -74.284  1.00 17.51           C  
ANISOU 2923  CG  GLU D 444     1687   2199   2768    -46   -493    103       C  
ATOM   2924  CD  GLU D 444      -6.732 -17.215 -75.638  1.00 18.86           C  
ANISOU 2924  CD  GLU D 444     1847   2515   2802      0   -571    137       C  
ATOM   2925  OE1 GLU D 444      -5.930 -17.233 -76.599  1.00 21.41           O  
ANISOU 2925  OE1 GLU D 444     2243   2854   3037     11   -564    228       O  
ATOM   2926  OE2 GLU D 444      -7.922 -17.583 -75.728  1.00 20.05           O  
ANISOU 2926  OE2 GLU D 444     1909   2780   2931     20   -634     58       O  
ATOM   2927  N   PHE D 445      -1.814 -16.957 -73.116  1.00 13.78           N  
ANISOU 2927  N   PHE D 445     1427   1470   2340   -232   -259    107       N  
ATOM   2928  CA  PHE D 445      -0.495 -17.551 -72.906  1.00 12.63           C  
ANISOU 2928  CA  PHE D 445     1330   1305   2163   -293   -213     69       C  
ATOM   2929  C   PHE D 445      -0.023 -17.407 -71.453  1.00 12.02           C  
ANISOU 2929  C   PHE D 445     1224   1177   2165   -327   -166    -19       C  
ATOM   2930  O   PHE D 445       0.417 -18.378 -70.843  1.00 13.58           O  
ANISOU 2930  O   PHE D 445     1435   1405   2319   -370   -165    -82       O  
ATOM   2931  CB  PHE D 445       0.523 -16.924 -73.868  1.00 14.09           C  
ANISOU 2931  CB  PHE D 445     1573   1445   2335   -281   -167    149       C  
ATOM   2932  CG  PHE D 445       1.962 -17.128 -73.462  1.00 12.51           C  
ANISOU 2932  CG  PHE D 445     1399   1205   2149   -335   -104     89       C  
ATOM   2933  CD1 PHE D 445       2.564 -18.372 -73.569  1.00 13.48           C  
ANISOU 2933  CD1 PHE D 445     1547   1387   2189   -378   -121     34       C  
ATOM   2934  CD2 PHE D 445       2.718 -16.068 -72.979  1.00 15.49           C  
ANISOU 2934  CD2 PHE D 445     1768   1487   2632   -340    -24     73       C  
ATOM   2935  CE1 PHE D 445       3.891 -18.558 -73.195  1.00 16.40           C  
ANISOU 2935  CE1 PHE D 445     1928   1731   2572   -412    -73    -31       C  
ATOM   2936  CE2 PHE D 445       4.042 -16.249 -72.604  1.00 16.93           C  
ANISOU 2936  CE2 PHE D 445     1954   1653   2824   -386     30     -7       C  
ATOM   2937  CZ  PHE D 445       4.630 -17.497 -72.710  1.00 18.07           C  
ANISOU 2937  CZ  PHE D 445     2120   1868   2876   -416     -1    -57       C  
ATOM   2938  N   VAL D 446      -0.120 -16.206 -70.887  1.00 13.81           N  
ANISOU 2938  N   VAL D 446     1410   1331   2507   -303   -125    -25       N  
ATOM   2939  CA  VAL D 446       0.356 -16.005 -69.517  1.00 14.31           C  
ANISOU 2939  CA  VAL D 446     1429   1371   2635   -337    -80   -126       C  
ATOM   2940  C   VAL D 446      -0.487 -16.797 -68.511  1.00 12.47           C  
ANISOU 2940  C   VAL D 446     1167   1216   2356   -356   -113   -193       C  
ATOM   2941  O   VAL D 446       0.025 -17.238 -67.480  1.00 14.04           O  
ANISOU 2941  O   VAL D 446     1389   1468   2477   -360    -87   -244       O  
ATOM   2942  CB  VAL D 446       0.376 -14.510 -69.116  1.00 15.17           C  
ANISOU 2942  CB  VAL D 446     1485   1385   2894   -314    -16   -143       C  
ATOM   2943  CG1 VAL D 446       1.377 -13.735 -69.975  1.00 19.32           C  
ANISOU 2943  CG1 VAL D 446     2057   1822   3462   -306     51    -81       C  
ATOM   2944  CG2 VAL D 446      -1.014 -13.905 -69.198  1.00 15.83           C  
ANISOU 2944  CG2 VAL D 446     1520   1451   3044   -262    -50   -110       C  
ATOM   2945  N   CYS D 447      -1.768 -16.993 -68.815  1.00 13.85           N  
ANISOU 2945  N   CYS D 447     1310   1420   2532   -347   -163   -177       N  
ATOM   2946  CA  CYS D 447      -2.613 -17.840 -67.976  1.00 14.43           C  
ANISOU 2946  CA  CYS D 447     1376   1571   2536   -372   -173   -234       C  
ATOM   2947  C   CYS D 447      -2.129 -19.284 -68.007  1.00 13.06           C  
ANISOU 2947  C   CYS D 447     1279   1444   2240   -409   -176   -229       C  
ATOM   2948  O   CYS D 447      -1.994 -19.923 -66.963  1.00 12.91           O  
ANISOU 2948  O   CYS D 447     1291   1458   2155   -426   -150   -254       O  
ATOM   2949  CB  CYS D 447      -4.078 -17.782 -68.415  1.00 15.81           C  
ANISOU 2949  CB  CYS D 447     1480   1774   2752   -364   -226   -243       C  
ATOM   2950  SG  CYS D 447      -4.942 -16.259 -67.999  1.00 17.08           S  
ANISOU 2950  SG  CYS D 447     1538   1888   3063   -311   -221   -271       S  
ATOM   2951  N   LEU D 448      -1.873 -19.793 -69.208  1.00 13.39           N  
ANISOU 2951  N   LEU D 448     1342   1480   2266   -421   -213   -193       N  
ATOM   2952  CA  LEU D 448      -1.426 -21.171 -69.372  1.00 10.21           C  
ANISOU 2952  CA  LEU D 448     1004   1105   1769   -453   -211   -198       C  
ATOM   2953  C   LEU D 448      -0.110 -21.415 -68.646  1.00 11.07           C  
ANISOU 2953  C   LEU D 448     1164   1197   1845   -446   -175   -204       C  
ATOM   2954  O   LEU D 448       0.068 -22.441 -67.994  1.00 12.30           O  
ANISOU 2954  O   LEU D 448     1360   1365   1948   -464   -166   -217       O  
ATOM   2955  CB  LEU D 448      -1.272 -21.513 -70.852  1.00 12.56           C  
ANISOU 2955  CB  LEU D 448     1321   1422   2029   -451   -246   -161       C  
ATOM   2956  CG  LEU D 448      -2.548 -21.542 -71.692  1.00 15.90           C  
ANISOU 2956  CG  LEU D 448     1700   1912   2429   -440   -292   -157       C  
ATOM   2957  CD1 LEU D 448      -2.216 -21.816 -73.162  1.00 15.60           C  
ANISOU 2957  CD1 LEU D 448     1688   1925   2317   -427   -319   -118       C  
ATOM   2958  CD2 LEU D 448      -3.530 -22.573 -71.131  1.00 17.38           C  
ANISOU 2958  CD2 LEU D 448     1862   2135   2607   -496   -287   -234       C  
ATOM   2959  N   LYS D 449       0.806 -20.460 -68.757  1.00 11.19           N  
ANISOU 2959  N   LYS D 449     1168   1178   1905   -422   -156   -199       N  
ATOM   2960  CA  LYS D 449       2.117 -20.602 -68.142  1.00 12.52           C  
ANISOU 2960  CA  LYS D 449     1360   1347   2049   -410   -131   -227       C  
ATOM   2961  C   LYS D 449       1.996 -20.668 -66.614  1.00  9.91           C  
ANISOU 2961  C   LYS D 449     1011   1051   1703   -403   -118   -268       C  
ATOM   2962  O   LYS D 449       2.696 -21.443 -65.963  1.00 13.97           O  
ANISOU 2962  O   LYS D 449     1544   1584   2179   -402   -123   -293       O  
ATOM   2963  CB  LYS D 449       3.036 -19.453 -68.572  1.00 15.71           C  
ANISOU 2963  CB  LYS D 449     1745   1712   2513   -394    -96   -232       C  
ATOM   2964  CG  LYS D 449       4.476 -19.633 -68.141  1.00 21.74           C  
ANISOU 2964  CG  LYS D 449     2516   2492   3252   -381    -74   -282       C  
ATOM   2965  CD  LYS D 449       5.437 -18.746 -68.920  1.00 21.14           C  
ANISOU 2965  CD  LYS D 449     2433   2374   3223   -384    -27   -289       C  
ATOM   2966  CE  LYS D 449       5.017 -17.293 -68.898  1.00 22.64           C  
ANISOU 2966  CE  LYS D 449     2585   2510   3508   -377     20   -279       C  
ATOM   2967  NZ  LYS D 449       6.172 -16.413 -69.163  1.00 13.65           N  
ANISOU 2967  NZ  LYS D 449     1434   1335   2417   -380     92   -314       N  
ATOM   2968  N   SER D 450       1.095 -19.866 -66.048  1.00 11.31           N  
ANISOU 2968  N   SER D 450     1141   1237   1917   -398   -104   -281       N  
ATOM   2969  CA  SER D 450       0.830 -19.915 -64.613  1.00 12.39           C  
ANISOU 2969  CA  SER D 450     1253   1420   2035   -402    -89   -325       C  
ATOM   2970  C   SER D 450       0.204 -21.230 -64.194  1.00 10.40           C  
ANISOU 2970  C   SER D 450     1037   1189   1724   -441   -104   -313       C  
ATOM   2971  O   SER D 450       0.491 -21.743 -63.112  1.00 11.97           O  
ANISOU 2971  O   SER D 450     1236   1422   1888   -458    -95   -347       O  
ATOM   2972  CB  SER D 450      -0.080 -18.769 -64.187  1.00 21.54           C  
ANISOU 2972  CB  SER D 450     2351   2579   3252   -389    -66   -351       C  
ATOM   2973  OG  SER D 450       0.655 -17.571 -64.126  1.00 27.58           O  
ANISOU 2973  OG  SER D 450     3078   3317   4084   -358    -31   -386       O  
ATOM   2974  N   ILE D 451      -0.674 -21.759 -65.039  1.00 10.90           N  
ANISOU 2974  N   ILE D 451     1125   1237   1781   -463   -120   -278       N  
ATOM   2975  CA  ILE D 451      -1.293 -23.047 -64.772  1.00  9.99           C  
ANISOU 2975  CA  ILE D 451     1048   1121   1626   -508   -116   -272       C  
ATOM   2976  C   ILE D 451      -0.229 -24.143 -64.707  1.00  9.91           C  
ANISOU 2976  C   ILE D 451     1098   1082   1586   -520   -115   -268       C  
ATOM   2977  O   ILE D 451      -0.263 -24.981 -63.813  1.00 11.15           O  
ANISOU 2977  O   ILE D 451     1296   1240   1700   -547    -87   -267       O  
ATOM   2978  CB  ILE D 451      -2.359 -23.391 -65.835  1.00 10.15           C  
ANISOU 2978  CB  ILE D 451     1066   1139   1650   -525   -132   -258       C  
ATOM   2979  CG1 ILE D 451      -3.582 -22.488 -65.660  1.00 12.48           C  
ANISOU 2979  CG1 ILE D 451     1295   1467   1978   -519   -131   -282       C  
ATOM   2980  CG2 ILE D 451      -2.769 -24.856 -65.740  1.00 10.43           C  
ANISOU 2980  CG2 ILE D 451     1149   1156   1659   -569   -110   -260       C  
ATOM   2981  CD1 ILE D 451      -4.559 -22.552 -66.810  1.00 11.56           C  
ANISOU 2981  CD1 ILE D 451     1146   1370   1875   -526   -159   -290       C  
ATOM   2982  N   ILE D 452       0.734 -24.116 -65.628  1.00 10.24           N  
ANISOU 2982  N   ILE D 452     1158   1100   1635   -491   -137   -256       N  
ATOM   2983  CA  ILE D 452       1.831 -25.085 -65.602  1.00 10.27           C  
ANISOU 2983  CA  ILE D 452     1220   1078   1603   -471   -142   -248       C  
ATOM   2984  C   ILE D 452       2.593 -25.021 -64.276  1.00 10.49           C  
ANISOU 2984  C   ILE D 452     1250   1148   1589   -427   -139   -260       C  
ATOM   2985  O   ILE D 452       2.870 -26.045 -63.654  1.00 12.33           O  
ANISOU 2985  O   ILE D 452     1546   1375   1763   -403   -134   -225       O  
ATOM   2986  CB  ILE D 452       2.818 -24.858 -66.765  1.00 11.24           C  
ANISOU 2986  CB  ILE D 452     1342   1185   1745   -447   -163   -253       C  
ATOM   2987  CG1 ILE D 452       2.156 -25.185 -68.104  1.00 12.46           C  
ANISOU 2987  CG1 ILE D 452     1508   1330   1898   -477   -168   -232       C  
ATOM   2988  CG2 ILE D 452       4.066 -25.713 -66.595  1.00 11.81           C  
ANISOU 2988  CG2 ILE D 452     1459   1245   1782   -402   -172   -257       C  
ATOM   2989  CD1 ILE D 452       2.991 -24.760 -69.292  1.00 12.76           C  
ANISOU 2989  CD1 ILE D 452     1541   1372   1936   -461   -177   -230       C  
ATOM   2990  N   LEU D 453       2.924 -23.810 -63.845  1.00 10.09           N  
ANISOU 2990  N   LEU D 453     1125   1142   1567   -412   -139   -311       N  
ATOM   2991  CA  LEU D 453       3.645 -23.614 -62.590  1.00 10.45           C  
ANISOU 2991  CA  LEU D 453     1145   1261   1563   -370   -140   -350       C  
ATOM   2992  C   LEU D 453       2.908 -24.220 -61.395  1.00 13.77           C  
ANISOU 2992  C   LEU D 453     1597   1725   1909   -384   -122   -321       C  
ATOM   2993  O   LEU D 453       3.507 -24.899 -60.564  1.00 12.49           O  
ANISOU 2993  O   LEU D 453     1477   1608   1658   -333   -132   -296       O  
ATOM   2994  CB  LEU D 453       3.884 -22.123 -62.350  1.00 10.44           C  
ANISOU 2994  CB  LEU D 453     1040   1296   1630   -375   -124   -436       C  
ATOM   2995  CG  LEU D 453       4.529 -21.772 -61.010  1.00 11.72           C  
ANISOU 2995  CG  LEU D 453     1143   1566   1743   -341   -121   -513       C  
ATOM   2996  CD1 LEU D 453       5.955 -22.310 -60.916  1.00 12.47           C  
ANISOU 2996  CD1 LEU D 453     1254   1704   1778   -270   -154   -532       C  
ATOM   2997  CD2 LEU D 453       4.497 -20.277 -60.785  1.00 12.64           C  
ANISOU 2997  CD2 LEU D 453     1167   1696   1939   -348    -78   -589       C  
ATOM   2998  N   LEU D 454       1.602 -23.990 -61.329  1.00 11.07           N  
ANISOU 2998  N   LEU D 454     1235   1372   1597   -449    -93   -323       N  
ATOM   2999  CA  LEU D 454       0.826 -24.405 -60.168  1.00 11.69           C  
ANISOU 2999  CA  LEU D 454     1334   1499   1609   -481    -57   -311       C  
ATOM   3000  C   LEU D 454       0.388 -25.870 -60.227  1.00 13.31           C  
ANISOU 3000  C   LEU D 454     1652   1642   1764   -504    -29   -225       C  
ATOM   3001  O   LEU D 454       0.253 -26.527 -59.195  1.00 15.06           O  
ANISOU 3001  O   LEU D 454     1930   1894   1896   -504      3   -180       O  
ATOM   3002  CB  LEU D 454      -0.391 -23.491 -60.015  1.00 12.93           C  
ANISOU 3002  CB  LEU D 454     1405   1677   1832   -546    -30   -374       C  
ATOM   3003  CG  LEU D 454      -0.021 -22.055 -59.614  1.00 12.94           C  
ANISOU 3003  CG  LEU D 454     1292   1734   1890   -529    -35   -468       C  
ATOM   3004  CD1 LEU D 454      -1.227 -21.135 -59.700  1.00 20.15           C  
ANISOU 3004  CD1 LEU D 454     2160   2630   2868   -524    -13   -477       C  
ATOM   3005  CD2 LEU D 454       0.593 -22.020 -58.222  1.00 16.88           C  
ANISOU 3005  CD2 LEU D 454     1769   2351   2292   -503    -26   -508       C  
ATOM   3006  N   ASN D 455       0.189 -26.388 -61.434  1.00 11.71           N  
ANISOU 3006  N   ASN D 455     1481   1352   1616   -524    -34   -204       N  
ATOM   3007  CA  ASN D 455      -0.375 -27.723 -61.598  1.00 14.47           C  
ANISOU 3007  CA  ASN D 455     1920   1626   1951   -566     11   -150       C  
ATOM   3008  C   ASN D 455       0.640 -28.858 -61.713  1.00 14.86           C  
ANISOU 3008  C   ASN D 455     2068   1612   1968   -503      4    -81       C  
ATOM   3009  O   ASN D 455       0.350 -29.990 -61.337  1.00 15.21           O  
ANISOU 3009  O   ASN D 455     2204   1591   1985   -520     59    -19       O  
ATOM   3010  CB  ASN D 455      -1.276 -27.752 -62.831  1.00 12.52           C  
ANISOU 3010  CB  ASN D 455     1638   1335   1782   -629     16   -190       C  
ATOM   3011  CG  ASN D 455      -1.972 -29.084 -63.008  1.00 12.82           C  
ANISOU 3011  CG  ASN D 455     1747   1297   1826   -694     81   -170       C  
ATOM   3012  OD1 ASN D 455      -2.806 -29.476 -62.190  1.00 16.74           O  
ANISOU 3012  OD1 ASN D 455     2269   1791   2300   -754    149   -165       O  
ATOM   3013  ND2 ASN D 455      -1.622 -29.794 -64.071  1.00 14.63           N  
ANISOU 3013  ND2 ASN D 455     2005   1463   2091   -689     73   -170       N  
ATOM   3014  N   SER D 456       1.820 -28.568 -62.246  1.00 15.16           N  
ANISOU 3014  N   SER D 456     2086   1658   2018   -432    -54    -96       N  
ATOM   3015  CA  SER D 456       2.727 -29.641 -62.641  1.00 14.21           C  
ANISOU 3015  CA  SER D 456     2039   1466   1893   -374    -65    -53       C  
ATOM   3016  C   SER D 456       3.186 -30.501 -61.466  1.00 17.83           C  
ANISOU 3016  C   SER D 456     2587   1919   2269   -303    -52     31       C  
ATOM   3017  O   SER D 456       3.287 -31.722 -61.589  1.00 19.84           O  
ANISOU 3017  O   SER D 456     2934   2070   2533   -285    -21     95       O  
ATOM   3018  CB  SER D 456       3.933 -29.064 -63.373  1.00 20.05           C  
ANISOU 3018  CB  SER D 456     2725   2233   2659   -317   -125   -105       C  
ATOM   3019  OG  SER D 456       3.554 -28.647 -64.677  1.00 22.68           O  
ANISOU 3019  OG  SER D 456     3012   2545   3059   -375   -128   -150       O  
ATOM   3020  N   GLY D 457       3.434 -29.878 -60.320  1.00 17.90           N  
ANISOU 3020  N   GLY D 457     2567   2039   2195   -260    -71     33       N  
ATOM   3021  CA  GLY D 457       3.923 -30.619 -59.172  1.00 16.74           C  
ANISOU 3021  CA  GLY D 457     2503   1918   1940   -172    -71    124       C  
ATOM   3022  C   GLY D 457       2.931 -30.801 -58.037  1.00 16.58           C  
ANISOU 3022  C   GLY D 457     2532   1931   1838   -223     -3    184       C  
ATOM   3023  O   GLY D 457       3.286 -31.337 -56.990  1.00 19.66           O  
ANISOU 3023  O   GLY D 457     2995   2363   2114   -147      0    275       O  
ATOM   3024  N   VAL D 458       1.688 -30.373 -58.243  1.00 19.22           N  
ANISOU 3024  N   VAL D 458     2825   2254   2225   -348     51    135       N  
ATOM   3025  CA  VAL D 458       0.702 -30.353 -57.162  1.00 21.04           C  
ANISOU 3025  CA  VAL D 458     3075   2537   2382   -415    121    159       C  
ATOM   3026  C   VAL D 458       0.263 -31.754 -56.719  1.00 25.76           C  
ANISOU 3026  C   VAL D 458     3825   3027   2937   -435    213    287       C  
ATOM   3027  O   VAL D 458      -0.239 -31.928 -55.608  1.00 25.42           O  
ANISOU 3027  O   VAL D 458     3830   3036   2791   -462    275    343       O  
ATOM   3028  CB  VAL D 458      -0.550 -29.534 -57.563  1.00 20.11           C  
ANISOU 3028  CB  VAL D 458     2859   2434   2349   -540    155     53       C  
ATOM   3029  CG1 VAL D 458      -1.410 -30.314 -58.544  1.00 20.22           C  
ANISOU 3029  CG1 VAL D 458     2911   2312   2458   -627    212     52       C  
ATOM   3030  CG2 VAL D 458      -1.361 -29.147 -56.328  1.00 19.54           C  
ANISOU 3030  CG2 VAL D 458     2763   2465   2196   -600    211     36       C  
ATOM   3031  N   TYR D 459       0.467 -32.753 -57.575  1.00 22.29           N  
ANISOU 3031  N   TYR D 459     3460   2433   2577   -425    232    331       N  
ATOM   3032  CA  TYR D 459       0.056 -34.115 -57.247  1.00 23.27           C  
ANISOU 3032  CA  TYR D 459     3732   2417   2692   -450    339    449       C  
ATOM   3033  C   TYR D 459       1.216 -34.944 -56.705  1.00 25.11           C  
ANISOU 3033  C   TYR D 459     4080   2613   2848   -295    309    589       C  
ATOM   3034  O   TYR D 459       1.042 -36.119 -56.401  1.00 24.83           O  
ANISOU 3034  O   TYR D 459     4185   2439   2809   -289    399    713       O  
ATOM   3035  CB  TYR D 459      -0.558 -34.817 -58.473  1.00 21.90           C  
ANISOU 3035  CB  TYR D 459     3568   2084   2670   -546    402    397       C  
ATOM   3036  CG  TYR D 459      -1.563 -33.974 -59.228  1.00 27.10           C  
ANISOU 3036  CG  TYR D 459     4094   2795   3406   -667    401    250       C  
ATOM   3037  CD1 TYR D 459      -2.838 -33.750 -58.720  1.00 30.39           C  
ANISOU 3037  CD1 TYR D 459     4486   3248   3813   -787    483    207       C  
ATOM   3038  CD2 TYR D 459      -1.236 -33.400 -60.449  1.00 28.07           C  
ANISOU 3038  CD2 TYR D 459     4119   2939   3609   -655    318    154       C  
ATOM   3039  CE1 TYR D 459      -3.758 -32.971 -59.407  1.00 29.58           C  
ANISOU 3039  CE1 TYR D 459     4254   3201   3784   -877    470     69       C  
ATOM   3040  CE2 TYR D 459      -2.147 -32.622 -61.144  1.00 27.29           C  
ANISOU 3040  CE2 TYR D 459     3904   2894   3570   -742    308     37       C  
ATOM   3041  CZ  TYR D 459      -3.406 -32.410 -60.619  1.00 30.74           C  
ANISOU 3041  CZ  TYR D 459     4310   3367   4002   -845    378     -6       C  
ATOM   3042  OH  TYR D 459      -4.309 -31.633 -61.313  1.00 31.94           O  
ANISOU 3042  OH  TYR D 459     4340   3580   4217   -912    356   -125       O  
ATOM   3043  N   THR D 460       2.390 -34.333 -56.564  1.00 25.70           N  
ANISOU 3043  N   THR D 460     4092   2807   2865   -165    188    567       N  
ATOM   3044  CA  THR D 460       3.575 -35.074 -56.133  1.00 22.71           C  
ANISOU 3044  CA  THR D 460     3800   2412   2417      5    137    680       C  
ATOM   3045  C   THR D 460       4.269 -34.480 -54.904  1.00 26.80           C  
ANISOU 3045  C   THR D 460     4288   3140   2757    123     60    707       C  
ATOM   3046  O   THR D 460       5.484 -34.617 -54.749  1.00 26.32           O  
ANISOU 3046  O   THR D 460     4221   3134   2645    282    -33    729       O  
ATOM   3047  CB  THR D 460       4.616 -35.165 -57.265  1.00 27.46           C  
ANISOU 3047  CB  THR D 460     4351   2958   3125     80     55    611       C  
ATOM   3048  OG1 THR D 460       4.822 -33.863 -57.823  1.00 24.50           O  
ANISOU 3048  OG1 THR D 460     3818   2705   2784     42    -17    454       O  
ATOM   3049  CG2 THR D 460       4.142 -36.117 -58.363  1.00 26.20           C  
ANISOU 3049  CG2 THR D 460     4248   2587   3121     -1    133    608       C  
ATOM   3050  N   PHE D 461       3.508 -33.832 -54.026  1.00 27.15           N  
ANISOU 3050  N   PHE D 461     4298   3313   2705     48     99    690       N  
ATOM   3051  CA  PHE D 461       4.086 -33.276 -52.804  1.00 26.95           C  
ANISOU 3051  CA  PHE D 461     4232   3511   2497    148     35    699       C  
ATOM   3052  C   PHE D 461       4.567 -34.361 -51.847  1.00 30.32           C  
ANISOU 3052  C   PHE D 461     4815   3937   2770    292     42    899       C  
ATOM   3053  O   PHE D 461       5.403 -34.099 -50.981  1.00 30.25           O  
ANISOU 3053  O   PHE D 461     4774   4119   2601    431    -44    914       O  
ATOM   3054  CB  PHE D 461       3.081 -32.363 -52.093  1.00 25.25           C  
ANISOU 3054  CB  PHE D 461     3940   3434   2221     20     88    621       C  
ATOM   3055  CG  PHE D 461       2.979 -30.992 -52.698  1.00 26.41           C  
ANISOU 3055  CG  PHE D 461     3904   3655   2476    -56     43    420       C  
ATOM   3056  CD1 PHE D 461       4.093 -30.173 -52.771  1.00 26.33           C  
ANISOU 3056  CD1 PHE D 461     3772   3773   2460     37    -62    311       C  
ATOM   3057  CD2 PHE D 461       1.777 -30.526 -53.203  1.00 28.50           C  
ANISOU 3057  CD2 PHE D 461     4117   3857   2854   -216    112    338       C  
ATOM   3058  CE1 PHE D 461       4.011 -28.911 -53.332  1.00 24.76           C  
ANISOU 3058  CE1 PHE D 461     3418   3616   2373    -34    -85    139       C  
ATOM   3059  CE2 PHE D 461       1.688 -29.264 -53.764  1.00 27.36           C  
ANISOU 3059  CE2 PHE D 461     3817   3766   2815   -268     72    174       C  
ATOM   3060  CZ  PHE D 461       2.807 -28.456 -53.830  1.00 25.34           C  
ANISOU 3060  CZ  PHE D 461     3456   3615   2559   -180    -20     83       C  
ATOM   3061  N   LEU D 462       4.042 -35.573 -52.021  1.00 29.72           N  
ANISOU 3061  N   LEU D 462     4903   3645   2744    261    146   1046       N  
ATOM   3062  CA  LEU D 462       4.364 -36.708 -51.156  1.00 33.36           C  
ANISOU 3062  CA  LEU D 462     5544   4057   3076    393    178   1271       C  
ATOM   3063  C   LEU D 462       4.242 -36.342 -49.679  1.00 34.95           C  
ANISOU 3063  C   LEU D 462     5759   4488   3032    433    178   1341       C  
ATOM   3064  O   LEU D 462       5.119 -36.658 -48.875  1.00 38.91           O  
ANISOU 3064  O   LEU D 462     6313   5105   3365    621    103   1458       O  
ATOM   3065  CB  LEU D 462       5.771 -37.236 -51.454  1.00 34.98           C  
ANISOU 3065  CB  LEU D 462     5768   4231   3294    605     62   1319       C  
ATOM   3066  CG  LEU D 462       5.996 -37.855 -52.835  1.00 35.92           C  
ANISOU 3066  CG  LEU D 462     5897   4111   3638    587     73   1275       C  
ATOM   3067  CD1 LEU D 462       7.464 -38.193 -53.018  1.00 36.69           C  
ANISOU 3067  CD1 LEU D 462     5981   4227   3735    803    -57   1289       C  
ATOM   3068  CD2 LEU D 462       5.131 -39.095 -53.014  1.00 37.55           C  
ANISOU 3068  CD2 LEU D 462     6279   4047   3940    503    235   1416       C  
ATOM   3069  N   SER D 463       3.154 -35.663 -49.333  1.00 35.53           N  
ANISOU 3069  N   SER D 463     5775   4642   3081    260    257   1258       N  
ATOM   3070  CA  SER D 463       2.910 -35.265 -47.952  1.00 37.39           C  
ANISOU 3070  CA  SER D 463     6009   5110   3086    266    273   1298       C  
ATOM   3071  C   SER D 463       1.422 -35.196 -47.649  1.00 32.63           C  
ANISOU 3071  C   SER D 463     5436   4470   2492     52    433   1283       C  
ATOM   3072  O   SER D 463       0.612 -34.825 -48.505  1.00 39.35           O  
ANISOU 3072  O   SER D 463     6209   5215   3526   -110    483   1144       O  
ATOM   3073  CB  SER D 463       3.563 -33.914 -47.651  1.00 35.28           C  
ANISOU 3073  CB  SER D 463     5533   5124   2749    314    140   1105       C  
ATOM   3074  OG  SER D 463       3.388 -33.555 -46.289  1.00 37.91           O  
ANISOU 3074  OG  SER D 463     5852   5706   2846    327    152   1128       O  
ATOM   3075  N   SER D 464       1.077 -35.553 -46.419  1.00 38.96           N  
ANISOU 3075  N   SER D 464     6346   5373   3084     57    510   1425       N  
ATOM   3076  CA  SER D 464      -0.306 -35.561 -45.981  1.00 39.46           C  
ANISOU 3076  CA  SER D 464     6446   5418   3131   -147    676   1417       C  
ATOM   3077  C   SER D 464      -0.465 -34.767 -44.690  1.00 40.30           C  
ANISOU 3077  C   SER D 464     6475   5834   3003   -160    667   1370       C  
ATOM   3078  O   SER D 464      -1.491 -34.868 -44.015  1.00 42.30           O  
ANISOU 3078  O   SER D 464     6768   6119   3185   -303    804   1392       O  
ATOM   3079  CB  SER D 464      -0.795 -36.994 -45.781  1.00 39.57           C  
ANISOU 3079  CB  SER D 464     6621   5218   3197   -182    799   1609       C  
ATOM   3080  OG  SER D 464       0.004 -37.673 -44.826  1.00 45.48           O  
ANISOU 3080  OG  SER D 464     7451   6041   3790    -26    733   1787       O  
ATOM   3081  N   THR D 465       0.558 -33.987 -44.347  1.00 39.43           N  
ANISOU 3081  N   THR D 465     6232   5961   2787    -17    509   1285       N  
ATOM   3082  CA  THR D 465       0.503 -33.110 -43.181  1.00 35.48           C  
ANISOU 3082  CA  THR D 465     5618   5785   2077    -28    486   1192       C  
ATOM   3083  C   THR D 465      -0.648 -32.123 -43.345  1.00 33.27           C  
ANISOU 3083  C   THR D 465     5183   5538   1921   -251    561    966       C  
ATOM   3084  O   THR D 465      -1.095 -31.870 -44.465  1.00 32.51           O  
ANISOU 3084  O   THR D 465     5022   5257   2072   -351    573    851       O  
ATOM   3085  CB  THR D 465       1.822 -32.339 -42.981  1.00 33.81           C  
ANISOU 3085  CB  THR D 465     5248   5787   1810    141    298   1063       C  
ATOM   3086  OG1 THR D 465       2.049 -31.472 -44.100  1.00 31.17           O  
ANISOU 3086  OG1 THR D 465     4744   5408   1693    104    228    860       O  
ATOM   3087  CG2 THR D 465       2.989 -33.308 -42.858  1.00 35.77           C  
ANISOU 3087  CG2 THR D 465     5616   5959   2015    347    198   1230       C  
ATOM   3088  N   LEU D 466      -1.132 -31.576 -42.234  1.00 29.68           N  
ANISOU 3088  N   LEU D 466     4242   5043   1991   -515    275    305       N  
ATOM   3089  CA  LEU D 466      -2.229 -30.615 -42.284  1.00 32.20           C  
ANISOU 3089  CA  LEU D 466     4514   5378   2341   -559    376    139       C  
ATOM   3090  C   LEU D 466      -1.867 -29.418 -43.157  1.00 28.00           C  
ANISOU 3090  C   LEU D 466     3922   4783   1932   -500    358    -10       C  
ATOM   3091  O   LEU D 466      -2.691 -28.937 -43.935  1.00 26.44           O  
ANISOU 3091  O   LEU D 466     3687   4497   1860   -486    414   -105       O  
ATOM   3092  CB  LEU D 466      -2.604 -30.141 -40.882  1.00 31.62           C  
ANISOU 3092  CB  LEU D 466     4433   5460   2120   -640    426     76       C  
ATOM   3093  CG  LEU D 466      -3.748 -29.124 -40.870  1.00 32.18           C  
ANISOU 3093  CG  LEU D 466     4443   5533   2250   -678    528   -105       C  
ATOM   3094  CD1 LEU D 466      -4.952 -29.665 -41.626  1.00 32.32           C  
ANISOU 3094  CD1 LEU D 466     4464   5462   2355   -693    607    -95       C  
ATOM   3095  CD2 LEU D 466      -4.129 -28.743 -39.453  1.00 34.77           C  
ANISOU 3095  CD2 LEU D 466     4755   5978   2480   -746    567   -161       C  
ATOM   3096  N   LYS D 467      -0.629 -28.949 -43.028  1.00 29.79           N  
ANISOU 3096  N   LYS D 467     4140   5056   2124   -467    279    -26       N  
ATOM   3097  CA  LYS D 467      -0.141 -27.845 -43.844  1.00 27.30           C  
ANISOU 3097  CA  LYS D 467     3775   4676   1921   -414    258   -155       C  
ATOM   3098  C   LYS D 467      -0.230 -28.192 -45.325  1.00 25.80           C  
ANISOU 3098  C   LYS D 467     3583   4306   1914   -343    239   -121       C  
ATOM   3099  O   LYS D 467      -0.662 -27.375 -46.135  1.00 25.32           O  
ANISOU 3099  O   LYS D 467     3484   4166   1971   -320    272   -230       O  
ATOM   3100  CB  LYS D 467       1.299 -27.490 -43.469  1.00 30.71           C  
ANISOU 3100  CB  LYS D 467     4200   5185   2283   -393    170   -159       C  
ATOM   3101  CG  LYS D 467       1.456 -26.088 -42.905  1.00 34.61           C  
ANISOU 3101  CG  LYS D 467     4645   5780   2726   -429    202   -334       C  
ATOM   3102  CD  LYS D 467       1.213 -25.041 -43.982  1.00 31.70           C  
ANISOU 3102  CD  LYS D 467     4231   5287   2526   -389    235   -467       C  
ATOM   3103  CE  LYS D 467       1.009 -23.658 -43.379  1.00 32.58           C  
ANISOU 3103  CE  LYS D 467     4287   5449   2642   -426    288   -637       C  
ATOM   3104  NZ  LYS D 467       0.764 -22.623 -44.423  1.00 37.33           N  
ANISOU 3104  NZ  LYS D 467     4851   5930   3404   -388    319   -756       N  
ATOM   3105  N   SER D 468       0.165 -29.415 -45.663  1.00 24.91           N  
ANISOU 3105  N   SER D 468     3510   4130   1824   -310    186     29       N  
ATOM   3106  CA  SER D 468       0.176 -29.856 -47.052  1.00 25.30           C  
ANISOU 3106  CA  SER D 468     3556   4019   2037   -249    166     63       C  
ATOM   3107  C   SER D 468      -1.229 -29.953 -47.640  1.00 23.91           C  
ANISOU 3107  C   SER D 468     3368   3767   1950   -265    248     29       C  
ATOM   3108  O   SER D 468      -1.423 -29.660 -48.817  1.00 22.67           O  
ANISOU 3108  O   SER D 468     3186   3502   1928   -223    249    -20       O  
ATOM   3109  CB  SER D 468       0.894 -31.200 -47.179  1.00 26.72           C  
ANISOU 3109  CB  SER D 468     3776   4152   2225   -215     97    227       C  
ATOM   3110  OG  SER D 468       2.304 -31.024 -47.110  1.00 33.03           O  
ANISOU 3110  OG  SER D 468     4568   4980   3001   -174      7    239       O  
ATOM   3111  N   LEU D 469      -2.205 -30.363 -46.833  1.00 25.63           N  
ANISOU 3111  N   LEU D 469     3602   4047   2090   -329    317     52       N  
ATOM   3112  CA  LEU D 469      -3.597 -30.370 -47.283  1.00 22.30           C  
ANISOU 3112  CA  LEU D 469     3157   3570   1746   -351    401      0       C  
ATOM   3113  C   LEU D 469      -4.063 -28.955 -47.598  1.00 22.51           C  
ANISOU 3113  C   LEU D 469     3125   3596   1832   -343    438   -169       C  
ATOM   3114  O   LEU D 469      -4.740 -28.715 -48.599  1.00 22.45           O  
ANISOU 3114  O   LEU D 469     3086   3493   1953   -313    460   -221       O  
ATOM   3115  CB  LEU D 469      -4.514 -30.998 -46.231  1.00 26.15           C  
ANISOU 3115  CB  LEU D 469     3671   4140   2126   -432    475     44       C  
ATOM   3116  CG  LEU D 469      -4.497 -32.518 -46.077  1.00 29.34           C  
ANISOU 3116  CG  LEU D 469     4133   4510   2507   -447    465    216       C  
ATOM   3117  CD1 LEU D 469      -5.412 -32.931 -44.942  1.00 30.81           C  
ANISOU 3117  CD1 LEU D 469     4344   4793   2570   -541    548    243       C  
ATOM   3118  CD2 LEU D 469      -4.925 -33.181 -47.378  1.00 29.51           C  
ANISOU 3118  CD2 LEU D 469     4144   4378   2692   -405    470    243       C  
ATOM   3119  N   GLU D 470      -3.689 -28.022 -46.731  1.00 20.23           N  
ANISOU 3119  N   GLU D 470     2821   3415   1451   -370    442   -254       N  
ATOM   3120  CA  GLU D 470      -4.044 -26.621 -46.900  1.00 19.97           C  
ANISOU 3120  CA  GLU D 470     2731   3381   1476   -365    479   -418       C  
ATOM   3121  C   GLU D 470      -3.351 -26.016 -48.125  1.00 20.09           C  
ANISOU 3121  C   GLU D 470     2729   3283   1621   -289    420   -449       C  
ATOM   3122  O   GLU D 470      -3.953 -25.238 -48.867  1.00 19.26           O  
ANISOU 3122  O   GLU D 470     2584   3104   1631   -262    447   -539       O  
ATOM   3123  CB  GLU D 470      -3.695 -25.846 -45.630  1.00 21.80           C  
ANISOU 3123  CB  GLU D 470     2950   3759   1573   -419    499   -502       C  
ATOM   3124  CG  GLU D 470      -4.565 -26.244 -44.438  1.00 22.30           C  
ANISOU 3124  CG  GLU D 470     3022   3943   1507   -507    575   -500       C  
ATOM   3125  CD  GLU D 470      -4.067 -25.689 -43.116  1.00 27.43           C  
ANISOU 3125  CD  GLU D 470     3667   4753   2003   -566    581   -558       C  
ATOM   3126  OE1 GLU D 470      -2.922 -25.193 -43.067  1.00 28.88           O  
ANISOU 3126  OE1 GLU D 470     3847   4958   2170   -536    513   -574       O  
ATOM   3127  OE2 GLU D 470      -4.822 -25.747 -42.121  1.00 29.18           O  
ANISOU 3127  OE2 GLU D 470     3877   5043   2166   -629    635   -575       O  
ATOM   3128  N   GLU D 471      -2.090 -26.384 -48.338  1.00 17.37           N  
ANISOU 3128  N   GLU D 471     2414   2926   1259   -255    339   -371       N  
ATOM   3129  CA  GLU D 471      -1.346 -25.902 -49.499  1.00 16.31           C  
ANISOU 3129  CA  GLU D 471     2269   2691   1239   -192    285   -393       C  
ATOM   3130  C   GLU D 471      -2.000 -26.353 -50.805  1.00 18.02           C  
ANISOU 3130  C   GLU D 471     2481   2777   1589   -154    290   -358       C  
ATOM   3131  O   GLU D 471      -2.148 -25.567 -51.741  1.00 17.57           O  
ANISOU 3131  O   GLU D 471     2397   2642   1637   -119    289   -426       O  
ATOM   3132  CB  GLU D 471       0.104 -26.385 -49.449  1.00 23.52           C  
ANISOU 3132  CB  GLU D 471     3208   3620   2107   -167    201   -314       C  
ATOM   3133  CG  GLU D 471       0.919 -25.815 -48.299  1.00 26.21           C  
ANISOU 3133  CG  GLU D 471     3545   4093   2323   -198    182   -360       C  
ATOM   3134  CD  GLU D 471       1.548 -24.480 -48.640  1.00 28.12           C  
ANISOU 3134  CD  GLU D 471     3751   4318   2616   -180    172   -486       C  
ATOM   3135  OE1 GLU D 471       2.568 -24.455 -49.361  1.00 16.83           O  
ANISOU 3135  OE1 GLU D 471     2322   2830   1241   -138    112   -468       O  
ATOM   3136  OE2 GLU D 471       1.018 -23.446 -48.188  1.00 23.29           O  
ANISOU 3136  OE2 GLU D 471     3107   3748   1996   -212    230   -608       O  
ATOM   3137  N   LYS D 472      -2.394 -27.620 -50.862  1.00 17.25           N  
ANISOU 3137  N   LYS D 472     2410   2659   1485   -163    295   -252       N  
ATOM   3138  CA  LYS D 472      -3.018 -28.161 -52.064  1.00 17.92           C  
ANISOU 3138  CA  LYS D 472     2488   2633   1688   -134    301   -222       C  
ATOM   3139  C   LYS D 472      -4.367 -27.497 -52.339  1.00 17.33           C  
ANISOU 3139  C   LYS D 472     2369   2538   1677   -144    366   -317       C  
ATOM   3140  O   LYS D 472      -4.701 -27.211 -53.491  1.00 18.10           O  
ANISOU 3140  O   LYS D 472     2443   2548   1885   -106    357   -345       O  
ATOM   3141  CB  LYS D 472      -3.187 -29.674 -51.947  1.00 21.09           C  
ANISOU 3141  CB  LYS D 472     2924   3019   2072   -151    303    -96       C  
ATOM   3142  CG  LYS D 472      -1.876 -30.444 -51.933  1.00 23.76           C  
ANISOU 3142  CG  LYS D 472     3297   3346   2386   -126    229      7       C  
ATOM   3143  CD  LYS D 472      -2.112 -31.946 -51.854  1.00 31.24           C  
ANISOU 3143  CD  LYS D 472     4276   4257   3335   -139    236    133       C  
ATOM   3144  CE  LYS D 472      -1.146 -32.608 -50.880  1.00 32.09           C  
ANISOU 3144  CE  LYS D 472     4425   4426   3343   -145    186    239       C  
ATOM   3145  NZ  LYS D 472      -1.241 -34.099 -50.935  1.00 35.92           N  
ANISOU 3145  NZ  LYS D 472     4944   4849   3856   -148    185    372       N  
ATOM   3146  N   ASP D 473      -5.141 -27.253 -51.284  1.00 17.96           N  
ANISOU 3146  N   ASP D 473     2436   2703   1685   -195    430   -367       N  
ATOM   3147  CA  ASP D 473      -6.402 -26.536 -51.429  1.00 18.45           C  
ANISOU 3147  CA  ASP D 473     2445   2754   1810   -202    493   -474       C  
ATOM   3148  C   ASP D 473      -6.187 -25.134 -51.986  1.00 17.27           C  
ANISOU 3148  C   ASP D 473     2259   2560   1742   -159    475   -578       C  
ATOM   3149  O   ASP D 473      -6.911 -24.697 -52.879  1.00 18.34           O  
ANISOU 3149  O   ASP D 473     2357   2621   1989   -124    482   -624       O  
ATOM   3150  CB  ASP D 473      -7.134 -26.437 -50.095  1.00 22.27           C  
ANISOU 3150  CB  ASP D 473     2917   3350   2195   -272    570   -526       C  
ATOM   3151  CG  ASP D 473      -8.385 -25.596 -50.193  1.00 30.63           C  
ANISOU 3151  CG  ASP D 473     3909   4398   3331   -277    636   -655       C  
ATOM   3152  OD1 ASP D 473      -9.344 -26.030 -50.862  1.00 32.91           O  
ANISOU 3152  OD1 ASP D 473     4173   4629   3701   -267    659   -649       O  
ATOM   3153  OD2 ASP D 473      -8.386 -24.479 -49.642  1.00 37.65           O  
ANISOU 3153  OD2 ASP D 473     4764   5333   4207   -287    661   -768       O  
ATOM   3154  N   HIS D 474      -5.198 -24.429 -51.440  1.00 17.00           N  
ANISOU 3154  N   HIS D 474     2234   2573   1651   -161    450   -614       N  
ATOM   3155  CA  HIS D 474      -4.855 -23.096 -51.915  1.00 17.92           C  
ANISOU 3155  CA  HIS D 474     2322   2642   1843   -126    435   -709       C  
ATOM   3156  C   HIS D 474      -4.501 -23.099 -53.398  1.00 17.80           C  
ANISOU 3156  C   HIS D 474     2316   2508   1939    -66    378   -664       C  
ATOM   3157  O   HIS D 474      -4.996 -22.276 -54.160  1.00 16.81           O  
ANISOU 3157  O   HIS D 474     2159   2310   1919    -32    382   -721       O  
ATOM   3158  CB  HIS D 474      -3.689 -22.522 -51.108  1.00 18.39           C  
ANISOU 3158  CB  HIS D 474     2394   2776   1818   -144    414   -745       C  
ATOM   3159  CG  HIS D 474      -3.235 -21.173 -51.575  1.00 22.36           C  
ANISOU 3159  CG  HIS D 474     2872   3223   2402   -114    402   -840       C  
ATOM   3160  ND1 HIS D 474      -4.008 -20.039 -51.449  1.00 29.12           N  
ANISOU 3160  ND1 HIS D 474     3679   4060   3327   -114    456   -963       N  
ATOM   3161  CD2 HIS D 474      -2.086 -20.780 -52.173  1.00 29.50           C  
ANISOU 3161  CD2 HIS D 474     3793   4078   3336    -84    347   -831       C  
ATOM   3162  CE1 HIS D 474      -3.350 -19.003 -51.940  1.00 28.01           C  
ANISOU 3162  CE1 HIS D 474     3530   3856   3256    -86    434  -1019       C  
ATOM   3163  NE2 HIS D 474      -2.182 -19.426 -52.388  1.00 33.70           N  
ANISOU 3163  NE2 HIS D 474     4292   4562   3951    -70    370   -941       N  
ATOM   3164  N   ILE D 475      -3.641 -24.031 -53.793  1.00 13.90           N  
ANISOU 3164  N   ILE D 475     1863   1997   1422    -55    324   -561       N  
ATOM   3165  CA  ILE D 475      -3.197 -24.134 -55.179  1.00 13.93           C  
ANISOU 3165  CA  ILE D 475     1876   1901   1515     -9    273   -519       C  
ATOM   3166  C   ILE D 475      -4.379 -24.354 -56.124  1.00 16.40           C  
ANISOU 3166  C   ILE D 475     2165   2147   1921     10    290   -514       C  
ATOM   3167  O   ILE D 475      -4.460 -23.739 -57.184  1.00 16.07           O  
ANISOU 3167  O   ILE D 475     2109   2031   1967     47    267   -536       O  
ATOM   3168  CB  ILE D 475      -2.172 -25.271 -55.348  1.00 17.61           C  
ANISOU 3168  CB  ILE D 475     2382   2365   1942     -6    222   -414       C  
ATOM   3169  CG1 ILE D 475      -0.873 -24.930 -54.605  1.00 17.35           C  
ANISOU 3169  CG1 ILE D 475     2365   2394   1833    -14    188   -425       C  
ATOM   3170  CG2 ILE D 475      -1.890 -25.538 -56.820  1.00 16.20           C  
ANISOU 3170  CG2 ILE D 475     2208   2090   1857     30    181   -376       C  
ATOM   3171  CD1 ILE D 475       0.151 -26.047 -54.619  1.00 16.23           C  
ANISOU 3171  CD1 ILE D 475     2254   2257   1654     -7    134   -325       C  
ATOM   3172  N   HIS D 476      -5.315 -25.209 -55.728  1.00 14.62           N  
ANISOU 3172  N   HIS D 476     1932   1952   1672    -17    331   -487       N  
ATOM   3173  CA  HIS D 476      -6.462 -25.486 -56.583  1.00 15.72           C  
ANISOU 3173  CA  HIS D 476     2039   2038   1896     -3    349   -490       C  
ATOM   3174  C   HIS D 476      -7.442 -24.309 -56.632  1.00 16.58           C  
ANISOU 3174  C   HIS D 476     2094   2135   2070     14    380   -594       C  
ATOM   3175  O   HIS D 476      -8.094 -24.088 -57.654  1.00 16.46           O  
ANISOU 3175  O   HIS D 476     2049   2059   2148     48    366   -606       O  
ATOM   3176  CB  HIS D 476      -7.159 -26.764 -56.124  1.00 18.03           C  
ANISOU 3176  CB  HIS D 476     2337   2364   2149    -43    390   -436       C  
ATOM   3177  CG  HIS D 476      -6.426 -28.012 -56.515  1.00 22.16           C  
ANISOU 3177  CG  HIS D 476     2901   2859   2660    -44    354   -328       C  
ATOM   3178  ND1 HIS D 476      -6.228 -28.377 -57.829  1.00 24.30           N  
ANISOU 3178  ND1 HIS D 476     3170   3053   3009    -13    314   -296       N  
ATOM   3179  CD2 HIS D 476      -5.821 -28.965 -55.766  1.00 24.31           C  
ANISOU 3179  CD2 HIS D 476     3216   3167   2854    -72    351   -247       C  
ATOM   3180  CE1 HIS D 476      -5.546 -29.508 -57.874  1.00 22.32           C  
ANISOU 3180  CE1 HIS D 476     2953   2788   2739    -22    294   -210       C  
ATOM   3181  NE2 HIS D 476      -5.287 -29.886 -56.635  1.00 24.45           N  
ANISOU 3181  NE2 HIS D 476     3251   3120   2919    -53    313   -174       N  
ATOM   3182  N   ARG D 477      -7.534 -23.541 -55.549  1.00 16.69           N  
ANISOU 3182  N   ARG D 477     2092   2208   2041     -9    421   -672       N  
ATOM   3183  CA  ARG D 477      -8.345 -22.329 -55.582  1.00 15.99           C  
ANISOU 3183  CA  ARG D 477     1948   2097   2032     12    450   -780       C  
ATOM   3184  C   ARG D 477      -7.747 -21.297 -56.538  1.00 16.34           C  
ANISOU 3184  C   ARG D 477     1994   2055   2160     65    397   -795       C  
ATOM   3185  O   ARG D 477      -8.478 -20.633 -57.271  1.00 20.37           O  
ANISOU 3185  O   ARG D 477     2464   2501   2773    106    390   -832       O  
ATOM   3186  CB  ARG D 477      -8.513 -21.736 -54.179  1.00 18.20           C  
ANISOU 3186  CB  ARG D 477     2206   2462   2248    -32    512   -874       C  
ATOM   3187  CG  ARG D 477      -9.409 -22.569 -53.274  1.00 24.24           C  
ANISOU 3187  CG  ARG D 477     2958   3310   2943    -90    578   -876       C  
ATOM   3188  CD  ARG D 477      -9.672 -21.876 -51.950  1.00 28.83           C  
ANISOU 3188  CD  ARG D 477     3509   3982   3463   -140    646   -986       C  
ATOM   3189  NE  ARG D 477     -10.584 -22.645 -51.105  1.00 33.12           N  
ANISOU 3189  NE  ARG D 477     4040   4608   3936   -204    717   -993       N  
ATOM   3190  CZ  ARG D 477     -11.913 -22.550 -51.143  1.00 36.77           C  
ANISOU 3190  CZ  ARG D 477     4440   5065   4466   -211    774  -1065       C  
ATOM   3191  NH1 ARG D 477     -12.505 -21.713 -51.989  1.00 40.66           N  
ANISOU 3191  NH1 ARG D 477     4875   5473   5103   -150    761  -1133       N  
ATOM   3192  NH2 ARG D 477     -12.654 -23.291 -50.328  1.00 40.83           N  
ANISOU 3192  NH2 ARG D 477     4948   5659   4905   -281    845  -1069       N  
ATOM   3193  N   VAL D 478      -6.424 -21.166 -56.549  1.00 16.97           N  
ANISOU 3193  N   VAL D 478     2118   2133   2196     65    358   -764       N  
ATOM   3194  CA  VAL D 478      -5.784 -20.245 -57.490  1.00 17.13           C  
ANISOU 3194  CA  VAL D 478     2148   2070   2291    106    313   -771       C  
ATOM   3195  C   VAL D 478      -5.955 -20.746 -58.926  1.00 17.31           C  
ANISOU 3195  C   VAL D 478     2181   2022   2376    139    265   -694       C  
ATOM   3196  O   VAL D 478      -6.221 -19.960 -59.841  1.00 17.03           O  
ANISOU 3196  O   VAL D 478     2131   1913   2429    178    241   -707       O  
ATOM   3197  CB  VAL D 478      -4.282 -20.052 -57.189  1.00 18.50           C  
ANISOU 3197  CB  VAL D 478     2362   2263   2402     90    286   -761       C  
ATOM   3198  CG1 VAL D 478      -3.664 -19.082 -58.179  1.00 18.38           C  
ANISOU 3198  CG1 VAL D 478     2358   2159   2467    124    249   -771       C  
ATOM   3199  CG2 VAL D 478      -4.084 -19.538 -55.768  1.00 21.70           C  
ANISOU 3199  CG2 VAL D 478     2755   2754   2738     52    331   -844       C  
ATOM   3200  N   LEU D 479      -5.806 -22.054 -59.121  1.00 15.93           N  
ANISOU 3200  N   LEU D 479     2029   1870   2155    122    252   -615       N  
ATOM   3201  CA  LEU D 479      -6.003 -22.637 -60.442  1.00 12.96           C  
ANISOU 3201  CA  LEU D 479     1656   1440   1829    144    213   -554       C  
ATOM   3202  C   LEU D 479      -7.420 -22.384 -60.941  1.00 13.27           C  
ANISOU 3202  C   LEU D 479     1642   1453   1945    168    226   -585       C  
ATOM   3203  O   LEU D 479      -7.626 -22.115 -62.122  1.00 15.98           O  
ANISOU 3203  O   LEU D 479     1978   1742   2352    201    186   -565       O  
ATOM   3204  CB  LEU D 479      -5.708 -24.137 -60.429  1.00 12.52           C  
ANISOU 3204  CB  LEU D 479     1626   1412   1721    117    209   -477       C  
ATOM   3205  CG  LEU D 479      -4.218 -24.465 -60.453  1.00 12.14           C  
ANISOU 3205  CG  LEU D 479     1623   1364   1626    109    172   -431       C  
ATOM   3206  CD1 LEU D 479      -3.957 -25.935 -60.124  1.00 12.12           C  
ANISOU 3206  CD1 LEU D 479     1640   1389   1575     84    175   -359       C  
ATOM   3207  CD2 LEU D 479      -3.641 -24.087 -61.816  1.00 16.06           C  
ANISOU 3207  CD2 LEU D 479     2131   1794   2178    134    124   -415       C  
ATOM   3208  N   ASP D 480      -8.389 -22.463 -60.033  1.00 15.56           N  
ANISOU 3208  N   ASP D 480     1895   1791   2226    150    281   -636       N  
ATOM   3209  CA  ASP D 480      -9.780 -22.183 -60.370  1.00 17.42           C  
ANISOU 3209  CA  ASP D 480     2068   2010   2539    174    298   -682       C  
ATOM   3210  C   ASP D 480      -9.957 -20.737 -60.818  1.00 17.77           C  
ANISOU 3210  C   ASP D 480     2086   1993   2674    224    274   -734       C  
ATOM   3211  O   ASP D 480     -10.703 -20.456 -61.753  1.00 15.58           O  
ANISOU 3211  O   ASP D 480     1773   1670   2478    266    243   -731       O  
ATOM   3212  CB  ASP D 480     -10.700 -22.468 -59.184  1.00 15.82           C  
ANISOU 3212  CB  ASP D 480     1828   1876   2306    136    371   -741       C  
ATOM   3213  CG  ASP D 480     -10.926 -23.946 -58.960  1.00 18.04           C  
ANISOU 3213  CG  ASP D 480     2125   2202   2527     91    398   -684       C  
ATOM   3214  OD1 ASP D 480     -10.623 -24.748 -59.866  1.00 17.59           O  
ANISOU 3214  OD1 ASP D 480     2090   2114   2477     97    359   -610       O  
ATOM   3215  OD2 ASP D 480     -11.428 -24.308 -57.878  1.00 19.49           O  
ANISOU 3215  OD2 ASP D 480     2296   2450   2658     45    461   -714       O  
ATOM   3216  N   LYS D 481      -9.277 -19.821 -60.136  1.00 18.39           N  
ANISOU 3216  N   LYS D 481     2179   2068   2741    221    288   -782       N  
ATOM   3217  CA  LYS D 481      -9.335 -18.414 -60.500  1.00 17.44           C  
ANISOU 3217  CA  LYS D 481     2041   1880   2706    262    267   -817       C  
ATOM   3218  C   LYS D 481      -8.775 -18.173 -61.899  1.00 14.28           C  
ANISOU 3218  C   LYS D 481     1677   1407   2342    294    196   -738       C  
ATOM   3219  O   LYS D 481      -9.304 -17.357 -62.650  1.00 17.51           O  
ANISOU 3219  O   LYS D 481     2065   1764   2823    331    162   -719       O  
ATOM   3220  CB  LYS D 481      -8.583 -17.566 -59.475  1.00 17.35           C  
ANISOU 3220  CB  LYS D 481     2044   1891   2657    234    294   -866       C  
ATOM   3221  CG  LYS D 481      -8.576 -16.083 -59.797  1.00 20.25           C  
ANISOU 3221  CG  LYS D 481     2400   2192   3101    261    271   -873       C  
ATOM   3222  CD  LYS D 481      -9.987 -15.523 -59.833  1.00 26.67           C  
ANISOU 3222  CD  LYS D 481     3146   2986   4001    288    281   -910       C  
ATOM   3223  CE  LYS D 481     -10.589 -15.443 -58.438  1.00 27.74           C  
ANISOU 3223  CE  LYS D 481     3234   3192   4115    250    349  -1003       C  
ATOM   3224  NZ  LYS D 481     -11.734 -14.496 -58.369  1.00 32.39           N  
ANISOU 3224  NZ  LYS D 481     3754   3749   4803    273    357  -1054       N  
ATOM   3225  N   ILE D 482      -7.708 -18.884 -62.250  1.00 15.42           N  
ANISOU 3225  N   ILE D 482     1875   1556   2429    275    173   -685       N  
ATOM   3226  CA  ILE D 482      -7.128 -18.746 -63.580  1.00 13.44           C  
ANISOU 3226  CA  ILE D 482     1659   1246   2202    295    113   -616       C  
ATOM   3227  C   ILE D 482      -8.054 -19.337 -64.652  1.00 17.19           C  
ANISOU 3227  C   ILE D 482     2107   1713   2711    316     79   -570       C  
ATOM   3228  O   ILE D 482      -8.126 -18.825 -65.772  1.00 16.82           O  
ANISOU 3228  O   ILE D 482     2065   1612   2714    347     30   -533       O  
ATOM   3229  CB  ILE D 482      -5.738 -19.407 -63.658  1.00 14.01           C  
ANISOU 3229  CB  ILE D 482     1789   1339   2195    258     98   -567       C  
ATOM   3230  CG1 ILE D 482      -4.795 -18.771 -62.636  1.00 17.03           C  
ANISOU 3230  CG1 ILE D 482     2192   1737   2541    237    124   -619       C  
ATOM   3231  CG2 ILE D 482      -5.155 -19.250 -65.050  1.00 14.94           C  
ANISOU 3231  CG2 ILE D 482     1940   1402   2334    268     44   -507       C  
ATOM   3232  CD1 ILE D 482      -3.446 -19.460 -62.536  1.00 19.65           C  
ANISOU 3232  CD1 ILE D 482     2569   2101   2796    204    109   -581       C  
ATOM   3233  N   THR D 483      -8.761 -20.411 -64.310  1.00 15.47           N  
ANISOU 3233  N   THR D 483     1862   1552   2465    296    106   -571       N  
ATOM   3234  CA  THR D 483      -9.793 -20.943 -65.195  1.00 14.19           C  
ANISOU 3234  CA  THR D 483     1659   1393   2340    313     83   -548       C  
ATOM   3235  C   THR D 483     -10.868 -19.896 -65.452  1.00 14.57           C  
ANISOU 3235  C   THR D 483     1649   1402   2484    367     68   -591       C  
ATOM   3236  O   THR D 483     -11.216 -19.622 -66.600  1.00 15.80           O  
ANISOU 3236  O   THR D 483     1792   1524   2686    401     11   -553       O  
ATOM   3237  CB  THR D 483     -10.455 -22.200 -64.618  1.00 16.14           C  
ANISOU 3237  CB  THR D 483     1879   1703   2549    276    129   -558       C  
ATOM   3238  OG1 THR D 483      -9.467 -23.220 -64.453  1.00 14.64           O  
ANISOU 3238  OG1 THR D 483     1742   1538   2285    234    135   -508       O  
ATOM   3239  CG2 THR D 483     -11.554 -22.699 -65.556  1.00 18.64           C  
ANISOU 3239  CG2 THR D 483     2145   2027   2912    292    106   -549       C  
ATOM   3240  N   ASP D 484     -11.381 -19.313 -64.372  1.00 15.70           N  
ANISOU 3240  N   ASP D 484     1755   1555   2653    371    117   -667       N  
ATOM   3241  CA  ASP D 484     -12.338 -18.209 -64.457  1.00 14.62           C  
ANISOU 3241  CA  ASP D 484     1568   1393   2594    408    103   -693       C  
ATOM   3242  C   ASP D 484     -11.824 -17.085 -65.348  1.00 17.77           C  
ANISOU 3242  C   ASP D 484     2001   1720   3029    440     45   -638       C  
ATOM   3243  O   ASP D 484     -12.575 -16.484 -66.116  1.00 18.62           O  
ANISOU 3243  O   ASP D 484     2077   1794   3205    483      2   -617       O  
ATOM   3244  CB  ASP D 484     -12.635 -17.642 -63.066  1.00 15.15           C  
ANISOU 3244  CB  ASP D 484     1607   1488   2661    386    167   -775       C  
ATOM   3245  CG  ASP D 484     -13.379 -18.616 -62.172  1.00 24.61           C  
ANISOU 3245  CG  ASP D 484     2764   2760   3827    350    231   -833       C  
ATOM   3246  OD1 ASP D 484     -13.901 -19.633 -62.676  1.00 26.85           O  
ANISOU 3246  OD1 ASP D 484     3026   3066   4108    349    228   -816       O  
ATOM   3247  OD2 ASP D 484     -13.437 -18.356 -60.948  1.00 22.79           O  
ANISOU 3247  OD2 ASP D 484     2522   2570   3569    317    290   -898       O  
ATOM   3248  N   THR D 485     -10.533 -16.803 -65.220  1.00 15.81           N  
ANISOU 3248  N   THR D 485     1818   1452   2735    417     48   -615       N  
ATOM   3249  CA  THR D 485      -9.898 -15.723 -65.955  1.00 15.87           C  
ANISOU 3249  CA  THR D 485     1867   1395   2769    435      8   -566       C  
ATOM   3250  C   THR D 485      -9.789 -16.043 -67.448  1.00 18.66           C  
ANISOU 3250  C   THR D 485     2244   1721   3126    453    -58   -484       C  
ATOM   3251  O   THR D 485     -10.037 -15.179 -68.291  1.00 18.63           O  
ANISOU 3251  O   THR D 485     2241   1665   3171    487   -102   -441       O  
ATOM   3252  CB  THR D 485      -8.509 -15.421 -65.370  1.00 18.79           C  
ANISOU 3252  CB  THR D 485     2294   1761   3083    396     35   -574       C  
ATOM   3253  OG1 THR D 485      -8.656 -14.905 -64.040  1.00 18.99           O  
ANISOU 3253  OG1 THR D 485     2293   1811   3112    381     90   -654       O  
ATOM   3254  CG2 THR D 485      -7.790 -14.398 -66.207  1.00 21.86           C  
ANISOU 3254  CG2 THR D 485     2729   2083   3494    405      2   -522       C  
ATOM   3255  N   LEU D 486      -9.430 -17.283 -67.776  1.00 17.22           N  
ANISOU 3255  N   LEU D 486     2078   1574   2890    429    -66   -463       N  
ATOM   3256  CA  LEU D 486      -9.402 -17.709 -69.174  1.00 16.04           C  
ANISOU 3256  CA  LEU D 486     1942   1411   2741    440   -128   -397       C  
ATOM   3257  C   LEU D 486     -10.777 -17.607 -69.818  1.00 16.57           C  
ANISOU 3257  C   LEU D 486     1945   1480   2871    488   -169   -390       C  
ATOM   3258  O   LEU D 486     -10.912 -17.099 -70.933  1.00 19.02           O  
ANISOU 3258  O   LEU D 486     2263   1758   3207    516   -232   -330       O  
ATOM   3259  CB  LEU D 486      -8.877 -19.140 -69.303  1.00 17.79           C  
ANISOU 3259  CB  LEU D 486     2185   1691   2884    390   -118   -379       C  
ATOM   3260  CG  LEU D 486      -7.361 -19.289 -69.392  1.00 21.62           C  
ANISOU 3260  CG  LEU D 486     2739   2168   3306    348   -114   -351       C  
ATOM   3261  CD1 LEU D 486      -6.948 -20.744 -69.197  1.00 21.54           C  
ANISOU 3261  CD1 LEU D 486     2737   2219   3227    300    -90   -343       C  
ATOM   3262  CD2 LEU D 486      -6.869 -18.751 -70.737  1.00 18.69           C  
ANISOU 3262  CD2 LEU D 486     2407   1756   2938    350   -170   -287       C  
ATOM   3263  N   ILE D 487     -11.792 -18.095 -69.111  1.00 16.30           N  
ANISOU 3263  N   ILE D 487     1845   1490   2858    494   -134   -451       N  
ATOM   3264  CA  ILE D 487     -13.163 -18.034 -69.597  1.00 19.55           C  
ANISOU 3264  CA  ILE D 487     2182   1915   3331    536   -167   -460       C  
ATOM   3265  C   ILE D 487     -13.596 -16.587 -69.794  1.00 17.50           C  
ANISOU 3265  C   ILE D 487     1910   1600   3137    581   -197   -444       C  
ATOM   3266  O   ILE D 487     -14.272 -16.263 -70.770  1.00 18.89           O  
ANISOU 3266  O   ILE D 487     2057   1764   3355    624   -262   -402       O  
ATOM   3267  CB  ILE D 487     -14.137 -18.750 -68.630  1.00 20.83           C  
ANISOU 3267  CB  ILE D 487     2275   2136   3502    523   -107   -542       C  
ATOM   3268  CG1 ILE D 487     -13.928 -20.264 -68.704  1.00 19.68           C  
ANISOU 3268  CG1 ILE D 487     2141   2054   3284    469    -82   -532       C  
ATOM   3269  CG2 ILE D 487     -15.590 -18.407 -68.956  1.00 21.84           C  
ANISOU 3269  CG2 ILE D 487     2320   2276   3704    566   -135   -566       C  
ATOM   3270  CD1 ILE D 487     -14.478 -20.900 -69.969  1.00 18.81           C  
ANISOU 3270  CD1 ILE D 487     2000   1977   3168    473   -138   -491       C  
ATOM   3271  N   HIS D 488     -13.179 -15.715 -68.879  1.00 19.11           N  
ANISOU 3271  N   HIS D 488     2137   1774   3352    571   -152   -477       N  
ATOM   3272  CA  HIS D 488     -13.523 -14.297 -68.962  1.00 18.34           C  
ANISOU 3272  CA  HIS D 488     2028   1614   3325    610   -169   -469       C  
ATOM   3273  C   HIS D 488     -12.914 -13.635 -70.198  1.00 17.81           C  
ANISOU 3273  C   HIS D 488     2017   1487   3261    630   -233   -372       C  
ATOM   3274  O   HIS D 488     -13.578 -12.859 -70.886  1.00 20.99           O  
ANISOU 3274  O   HIS D 488     2398   1851   3726    678   -283   -333       O  
ATOM   3275  CB  HIS D 488     -13.074 -13.558 -67.698  1.00 21.07           C  
ANISOU 3275  CB  HIS D 488     2386   1944   3676    586   -103   -532       C  
ATOM   3276  CG  HIS D 488     -13.374 -12.094 -67.727  1.00 24.75           C  
ANISOU 3276  CG  HIS D 488     2840   2339   4225    623   -113   -533       C  
ATOM   3277  ND1 HIS D 488     -14.659 -11.600 -67.682  1.00 28.59           N  
ANISOU 3277  ND1 HIS D 488     3252   2813   4797    667   -126   -566       N  
ATOM   3278  CD2 HIS D 488     -12.558 -11.017 -67.817  1.00 27.87           C  
ANISOU 3278  CD2 HIS D 488     3285   2667   4635    623   -111   -507       C  
ATOM   3279  CE1 HIS D 488     -14.622 -10.280 -67.733  1.00 29.27           C  
ANISOU 3279  CE1 HIS D 488     3344   2824   4952    695   -133   -557       C  
ATOM   3280  NE2 HIS D 488     -13.359  -9.902 -67.817  1.00 32.33           N  
ANISOU 3280  NE2 HIS D 488     3809   3178   5299    668   -122   -521       N  
ATOM   3281  N   LEU D 489     -11.648 -13.941 -70.470  1.00 17.60           N  
ANISOU 3281  N   LEU D 489     2064   1456   3167    590   -231   -334       N  
ATOM   3282  CA  LEU D 489     -10.972 -13.436 -71.661  1.00 18.84           C  
ANISOU 3282  CA  LEU D 489     2282   1565   3314    594   -285   -242       C  
ATOM   3283  C   LEU D 489     -11.721 -13.837 -72.926  1.00 18.25           C  
ANISOU 3283  C   LEU D 489     2180   1507   3247    627   -366   -178       C  
ATOM   3284  O   LEU D 489     -11.826 -13.061 -73.874  1.00 20.45           O  
ANISOU 3284  O   LEU D 489     2477   1743   3549    656   -422   -103       O  
ATOM   3285  CB  LEU D 489      -9.534 -13.954 -71.727  1.00 18.11           C  
ANISOU 3285  CB  LEU D 489     2261   1479   3141    536   -265   -226       C  
ATOM   3286  CG  LEU D 489      -8.527 -13.372 -70.738  1.00 20.14           C  
ANISOU 3286  CG  LEU D 489     2557   1716   3380    501   -200   -269       C  
ATOM   3287  CD1 LEU D 489      -7.220 -14.162 -70.782  1.00 19.83           C  
ANISOU 3287  CD1 LEU D 489     2574   1704   3258    444   -185   -262       C  
ATOM   3288  CD2 LEU D 489      -8.287 -11.891 -71.026  1.00 23.29           C  
ANISOU 3288  CD2 LEU D 489     2986   2035   3828    519   -206   -237       C  
ATOM   3289  N   MET D 490     -12.241 -15.059 -72.929  1.00 16.71           N  
ANISOU 3289  N   MET D 490     1940   1380   3030    621   -372   -209       N  
ATOM   3290  CA  MET D 490     -12.962 -15.582 -74.080  1.00 18.60           C  
ANISOU 3290  CA  MET D 490     2143   1656   3268    648   -449   -161       C  
ATOM   3291  C   MET D 490     -14.333 -14.922 -74.231  1.00 20.07           C  
ANISOU 3291  C   MET D 490     2256   1840   3530    708   -484   -165       C  
ATOM   3292  O   MET D 490     -14.787 -14.664 -75.349  1.00 20.39           O  
ANISOU 3292  O   MET D 490     2286   1885   3577    741   -564    -94       O  
ATOM   3293  CB  MET D 490     -13.100 -17.100 -73.959  1.00 17.32           C  
ANISOU 3293  CB  MET D 490     1949   1576   3055    612   -429   -205       C  
ATOM   3294  CG  MET D 490     -11.756 -17.820 -74.041  1.00 17.32           C  
ANISOU 3294  CG  MET D 490     2027   1601   2954    535   -395   -184       C  
ATOM   3295  SD  MET D 490     -11.836 -19.589 -73.710  1.00 18.49           S  
ANISOU 3295  SD  MET D 490     2149   1847   3031    471   -341   -232       S  
ATOM   3296  CE  MET D 490     -10.106 -19.962 -73.412  1.00 16.97           C  
ANISOU 3296  CE  MET D 490     2046   1642   2760    404   -297   -218       C  
ATOM   3297  N   ALA D 491     -14.982 -14.644 -73.105  1.00 19.37           N  
ANISOU 3297  N   ALA D 491     2117   1749   3492    720   -425   -248       N  
ATOM   3298  CA  ALA D 491     -16.265 -13.953 -73.108  1.00 20.96           C  
ANISOU 3298  CA  ALA D 491     2247   1941   3777    775   -450   -265       C  
ATOM   3299  C   ALA D 491     -16.093 -12.512 -73.578  1.00 22.25           C  
ANISOU 3299  C   ALA D 491     2447   2020   3988    813   -485   -197       C  
ATOM   3300  O   ALA D 491     -16.905 -12.001 -74.351  1.00 24.76           O  
ANISOU 3300  O   ALA D 491     2731   2327   4351    866   -551   -149       O  
ATOM   3301  CB  ALA D 491     -16.893 -13.996 -71.727  1.00 27.21           C  
ANISOU 3301  CB  ALA D 491     2981   2750   4608    766   -372   -377       C  
ATOM   3302  N   LYS D 492     -15.027 -11.866 -73.109  1.00 21.91           N  
ANISOU 3302  N   LYS D 492     2472   1919   3933    785   -439   -194       N  
ATOM   3303  CA  LYS D 492     -14.651 -10.532 -73.580  1.00 26.69           C  
ANISOU 3303  CA  LYS D 492     3126   2439   4578    811   -463   -126       C  
ATOM   3304  C   LYS D 492     -14.535 -10.492 -75.099  1.00 25.43           C  
ANISOU 3304  C   LYS D 492     3003   2275   4385    828   -551     -5       C  
ATOM   3305  O   LYS D 492     -14.952  -9.530 -75.742  1.00 29.78           O  
ANISOU 3305  O   LYS D 492     3554   2775   4985    876   -600     60       O  
ATOM   3306  CB  LYS D 492     -13.320 -10.096 -72.968  1.00 29.35           C  
ANISOU 3306  CB  LYS D 492     3536   2731   4883    763   -399   -141       C  
ATOM   3307  CG  LYS D 492     -13.397  -9.204 -71.743  1.00 29.49           C  
ANISOU 3307  CG  LYS D 492     3533   2707   4964    765   -332   -224       C  
ATOM   3308  CD  LYS D 492     -11.990  -8.994 -71.206  1.00 27.31           C  
ANISOU 3308  CD  LYS D 492     3329   2411   4638    709   -275   -241       C  
ATOM   3309  CE  LYS D 492     -11.860  -7.733 -70.381  1.00 31.02           C  
ANISOU 3309  CE  LYS D 492     3797   2816   5175    715   -226   -293       C  
ATOM   3310  NZ  LYS D 492     -10.424  -7.487 -70.059  1.00 35.27           N  
ANISOU 3310  NZ  LYS D 492     4406   3335   5659    660   -181   -299       N  
ATOM   3311  N   ALA D 493     -13.959 -11.550 -75.663  1.00 23.27           N  
ANISOU 3311  N   ALA D 493     2760   2057   4025    786   -573     25       N  
ATOM   3312  CA  ALA D 493     -13.706 -11.612 -77.098  1.00 25.95           C  
ANISOU 3312  CA  ALA D 493     3141   2407   4311    784   -655    137       C  
ATOM   3313  C   ALA D 493     -14.962 -11.948 -77.903  1.00 27.83           C  
ANISOU 3313  C   ALA D 493     3307   2707   4558    831   -736    168       C  
ATOM   3314  O   ALA D 493     -14.947 -11.902 -79.133  1.00 30.75           O  
ANISOU 3314  O   ALA D 493     3702   3100   4881    834   -814    266       O  
ATOM   3315  CB  ALA D 493     -12.611 -12.619 -77.386  1.00 23.78           C  
ANISOU 3315  CB  ALA D 493     2922   2171   3941    717   -649    149       C  
ATOM   3316  N   GLY D 494     -16.042 -12.291 -77.209  1.00 23.68           N  
ANISOU 3316  N   GLY D 494     2692   2219   4088    860   -716     81       N  
ATOM   3317  CA  GLY D 494     -17.318 -12.516 -77.862  1.00 23.13           C  
ANISOU 3317  CA  GLY D 494     2541   2209   4039    907   -786     95       C  
ATOM   3318  C   GLY D 494     -17.606 -13.960 -78.225  1.00 23.03           C  
ANISOU 3318  C   GLY D 494     2483   2306   3963    878   -809     64       C  
ATOM   3319  O   GLY D 494     -18.510 -14.235 -79.011  1.00 26.22           O  
ANISOU 3319  O   GLY D 494     2826   2777   4358    905   -878     87       O  
ATOM   3320  N   LEU D 495     -16.845 -14.887 -77.655  1.00 22.87           N  
ANISOU 3320  N   LEU D 495     2487   2306   3897    822   -751     10       N  
ATOM   3321  CA  LEU D 495     -17.074 -16.301 -77.918  1.00 20.38           C  
ANISOU 3321  CA  LEU D 495     2124   2089   3531    790   -762    -30       C  
ATOM   3322  C   LEU D 495     -18.362 -16.761 -77.252  1.00 20.56           C  
ANISOU 3322  C   LEU D 495     2041   2162   3610    811   -729   -130       C  
ATOM   3323  O   LEU D 495     -18.702 -16.298 -76.165  1.00 22.73           O  
ANISOU 3323  O   LEU D 495     2295   2393   3947    825   -664   -195       O  
ATOM   3324  CB  LEU D 495     -15.896 -17.149 -77.428  1.00 20.54           C  
ANISOU 3324  CB  LEU D 495     2204   2115   3487    719   -694    -61       C  
ATOM   3325  CG  LEU D 495     -14.724 -17.380 -78.389  1.00 23.64           C  
ANISOU 3325  CG  LEU D 495     2689   2526   3767    653   -714     20       C  
ATOM   3326  CD1 LEU D 495     -14.072 -16.075 -78.838  1.00 26.06           C  
ANISOU 3326  CD1 LEU D 495     3069   2738   4093    681   -759    113       C  
ATOM   3327  CD2 LEU D 495     -13.697 -18.316 -77.757  1.00 22.15           C  
ANISOU 3327  CD2 LEU D 495     2548   2357   3511    572   -623    -29       C  
ATOM   3328  N   THR D 496     -19.081 -17.665 -77.909  1.00 21.45           N  
ANISOU 3328  N   THR D 496     2083   2371   3694    805   -772   -147       N  
ATOM   3329  CA  THR D 496     -20.256 -18.281 -77.303  1.00 23.24           C  
ANISOU 3329  CA  THR D 496     2210   2656   3965    808   -730   -250       C  
ATOM   3330  C   THR D 496     -19.814 -19.157 -76.135  1.00 24.42           C  
ANISOU 3330  C   THR D 496     2363   2807   4107    756   -624   -339       C  
ATOM   3331  O   THR D 496     -18.639 -19.502 -76.029  1.00 22.24           O  
ANISOU 3331  O   THR D 496     2170   2515   3767    705   -589   -313       O  
ATOM   3332  CB  THR D 496     -21.054 -19.129 -78.318  1.00 25.33           C  
ANISOU 3332  CB  THR D 496     2399   3034   4191    799   -792   -255       C  
ATOM   3333  OG1 THR D 496     -20.307 -20.300 -78.667  1.00 23.61           O  
ANISOU 3333  OG1 THR D 496     2209   2878   3885    724   -772   -261       O  
ATOM   3334  CG2 THR D 496     -21.348 -18.323 -79.580  1.00 27.17           C  
ANISOU 3334  CG2 THR D 496     2638   3278   4406    843   -903   -149       C  
ATOM   3335  N   LEU D 497     -20.749 -19.506 -75.256  1.00 25.71           N  
ANISOU 3335  N   LEU D 497     2424   3080   4263    182   -589   -118       N  
ATOM   3336  CA  LEU D 497     -20.427 -20.366 -74.121  1.00 27.15           C  
ANISOU 3336  CA  LEU D 497     2612   3308   4395    118   -470   -175       C  
ATOM   3337  C   LEU D 497     -19.873 -21.708 -74.581  1.00 23.69           C  
ANISOU 3337  C   LEU D 497     2244   2913   3842     24   -492   -154       C  
ATOM   3338  O   LEU D 497     -18.944 -22.237 -73.975  1.00 23.14           O  
ANISOU 3338  O   LEU D 497     2254   2851   3688    -26   -418   -173       O  
ATOM   3339  CB  LEU D 497     -21.650 -20.580 -73.228  1.00 23.87           C  
ANISOU 3339  CB  LEU D 497     2048   2938   4083    127   -406   -232       C  
ATOM   3340  CG  LEU D 497     -21.916 -19.461 -72.224  1.00 24.84           C  
ANISOU 3340  CG  LEU D 497     2120   3020   4299    197   -315   -287       C  
ATOM   3341  CD1 LEU D 497     -23.246 -19.676 -71.520  1.00 28.81           C  
ANISOU 3341  CD1 LEU D 497     2462   3568   4915    205   -258   -344       C  
ATOM   3342  CD2 LEU D 497     -20.779 -19.402 -71.220  1.00 26.32           C  
ANISOU 3342  CD2 LEU D 497     2413   3191   4397    159   -204   -324       C  
ATOM   3343  N   GLN D 498     -20.434 -22.251 -75.656  1.00 24.04           N  
ANISOU 3343  N   GLN D 498     2264   2987   3885     -2   -594   -112       N  
ATOM   3344  CA  GLN D 498     -19.928 -23.503 -76.213  1.00 22.41           C  
ANISOU 3344  CA  GLN D 498     2132   2812   3573    -93   -614    -94       C  
ATOM   3345  C   GLN D 498     -18.497 -23.332 -76.719  1.00 20.32           C  
ANISOU 3345  C   GLN D 498     2017   2500   3205   -109   -621    -66       C  
ATOM   3346  O   GLN D 498     -17.640 -24.177 -76.460  1.00 21.28           O  
ANISOU 3346  O   GLN D 498     2212   2630   3243   -167   -567    -77       O  
ATOM   3347  CB  GLN D 498     -20.837 -24.010 -77.338  1.00 23.79           C  
ANISOU 3347  CB  GLN D 498     2252   3023   3762   -123   -728    -56       C  
ATOM   3348  CG  GLN D 498     -20.283 -25.229 -78.071  1.00 23.14           C  
ANISOU 3348  CG  GLN D 498     2261   2963   3567   -219   -751    -38       C  
ATOM   3349  CD  GLN D 498     -21.185 -25.705 -79.197  1.00 26.84           C  
ANISOU 3349  CD  GLN D 498     2684   3471   4042   -261   -864     -3       C  
ATOM   3350  OE1 GLN D 498     -21.852 -24.909 -79.857  1.00 33.11           O  
ANISOU 3350  OE1 GLN D 498     3425   4258   4896   -212   -964     34       O  
ATOM   3351  NE2 GLN D 498     -21.202 -27.009 -79.426  1.00 26.19           N  
ANISOU 3351  NE2 GLN D 498     2627   3429   3896   -355   -853    -13       N  
ATOM   3352  N   GLN D 499     -18.236 -22.233 -77.425  1.00 18.32           N  
ANISOU 3352  N   GLN D 499     1808   2192   2961    -57   -685    -29       N  
ATOM   3353  CA  GLN D 499     -16.885 -21.950 -77.904  1.00 18.08           C  
ANISOU 3353  CA  GLN D 499     1917   2114   2839    -74   -685     -8       C  
ATOM   3354  C   GLN D 499     -15.911 -21.724 -76.753  1.00 17.57           C  
ANISOU 3354  C   GLN D 499     1896   2033   2747    -67   -572    -50       C  
ATOM   3355  O   GLN D 499     -14.735 -22.082 -76.856  1.00 19.19           O  
ANISOU 3355  O   GLN D 499     2199   2228   2865   -109   -543    -49       O  
ATOM   3356  CB  GLN D 499     -16.867 -20.732 -78.832  1.00 20.02           C  
ANISOU 3356  CB  GLN D 499     2204   2301   3103    -21   -773     40       C  
ATOM   3357  CG  GLN D 499     -17.559 -20.940 -80.169  1.00 21.72           C  
ANISOU 3357  CG  GLN D 499     2411   2528   3312    -43   -904     96       C  
ATOM   3358  CD  GLN D 499     -17.754 -19.640 -80.925  1.00 25.25           C  
ANISOU 3358  CD  GLN D 499     2884   2914   3798     21   -996    149       C  
ATOM   3359  OE1 GLN D 499     -17.888 -18.566 -80.328  1.00 25.05           O  
ANISOU 3359  OE1 GLN D 499     2827   2842   3850    103   -967    139       O  
ATOM   3360  NE2 GLN D 499     -17.749 -19.726 -82.247  1.00 30.92           N  
ANISOU 3360  NE2 GLN D 499     3667   3624   4456    -20  -1106    207       N  
ATOM   3361  N   GLN D 500     -16.398 -21.127 -75.665  1.00 15.11           N  
ANISOU 3361  N   GLN D 500     1511   1720   2512    -17   -508    -89       N  
ATOM   3362  CA  GLN D 500     -15.571 -20.904 -74.481  1.00 16.01           C  
ANISOU 3362  CA  GLN D 500     1661   1825   2597    -20   -402   -132       C  
ATOM   3363  C   GLN D 500     -15.092 -22.228 -73.884  1.00 14.80           C  
ANISOU 3363  C   GLN D 500     1528   1721   2375    -93   -343   -151       C  
ATOM   3364  O   GLN D 500     -13.898 -22.405 -73.632  1.00 17.44           O  
ANISOU 3364  O   GLN D 500     1946   2045   2634   -121   -305   -153       O  
ATOM   3365  CB  GLN D 500     -16.334 -20.098 -73.422  1.00 20.18           C  
ANISOU 3365  CB  GLN D 500     2101   2345   3220     36   -337   -177       C  
ATOM   3366  CG  GLN D 500     -16.582 -18.640 -73.787  1.00 23.03           C  
ANISOU 3366  CG  GLN D 500     2457   2639   3655    118   -373   -164       C  
ATOM   3367  CD  GLN D 500     -17.541 -17.958 -72.831  1.00 21.66           C  
ANISOU 3367  CD  GLN D 500     2178   2457   3595    176   -308   -214       C  
ATOM   3368  OE1 GLN D 500     -17.520 -18.220 -71.628  1.00 23.27           O  
ANISOU 3368  OE1 GLN D 500     2357   2690   3794    148   -204   -271       O  
ATOM   3369  NE2 GLN D 500     -18.390 -17.081 -73.360  1.00 19.52           N  
ANISOU 3369  NE2 GLN D 500     1843   2144   3429    254   -368   -194       N  
ATOM   3370  N   HIS D 501     -16.025 -23.155 -73.671  1.00 15.68           N  
ANISOU 3370  N   HIS D 501     1562   1883   2514   -123   -339   -163       N  
ATOM   3371  CA  HIS D 501     -15.700 -24.456 -73.089  1.00 17.05           C  
ANISOU 3371  CA  HIS D 501     1755   2096   2629   -192   -285   -177       C  
ATOM   3372  C   HIS D 501     -14.756 -25.230 -73.995  0.96 13.46           C  
ANISOU 3372  C   HIS D 501     1395   1632   2089   -239   -325   -142       C  
ATOM   3373  O   HIS D 501     -13.797 -25.846 -73.526  0.83 12.79           O  
ANISOU 3373  O   HIS D 501     1371   1547   1941   -273   -276   -146       O  
ATOM   3374  CB  HIS D 501     -16.955 -25.296 -72.850  1.00 22.10           C  
ANISOU 3374  CB  HIS D 501     2296   2787   3314   -223   -279   -194       C  
ATOM   3375  CG  HIS D 501     -18.035 -24.585 -72.097  1.00 29.98           C  
ANISOU 3375  CG  HIS D 501     3184   3798   4410   -179   -241   -234       C  
ATOM   3376  ND1 HIS D 501     -19.374 -24.818 -72.329  1.00 32.83           N  
ANISOU 3376  ND1 HIS D 501     3430   4195   4849   -177   -271   -243       N  
ATOM   3377  CD2 HIS D 501     -17.981 -23.641 -71.128  1.00 32.76           C  
ANISOU 3377  CD2 HIS D 501     3519   4130   4800   -137   -170   -272       C  
ATOM   3378  CE1 HIS D 501     -20.098 -24.056 -71.529  1.00 29.97           C  
ANISOU 3378  CE1 HIS D 501     2980   3832   4575   -132   -217   -286       C  
ATOM   3379  NE2 HIS D 501     -19.278 -23.329 -70.794  1.00 32.16           N  
ANISOU 3379  NE2 HIS D 501     3318   4074   4828   -108   -153   -306       N  
ATOM   3380  N   GLN D 502     -15.045 -25.202 -75.295  1.00 15.36           N  
ANISOU 3380  N   GLN D 502     1645   1861   2328   -241   -413   -108       N  
ATOM   3381  CA  GLN D 502     -14.239 -25.922 -76.271  1.00 13.72           C  
ANISOU 3381  CA  GLN D 502     1528   1641   2042   -292   -446    -82       C  
ATOM   3382  C   GLN D 502     -12.810 -25.381 -76.321  1.00 14.07           C  
ANISOU 3382  C   GLN D 502     1669   1643   2032   -281   -422    -77       C  
ATOM   3383  O   GLN D 502     -11.853 -26.157 -76.327  1.00 14.74           O  
ANISOU 3383  O   GLN D 502     1817   1725   2058   -322   -389    -79       O  
ATOM   3384  CB  GLN D 502     -14.884 -25.857 -77.657  1.00 14.69           C  
ANISOU 3384  CB  GLN D 502     1648   1763   2170   -303   -549    -47       C  
ATOM   3385  CG  GLN D 502     -16.095 -26.767 -77.808  1.00 17.29           C  
ANISOU 3385  CG  GLN D 502     1897   2144   2531   -343   -577    -50       C  
ATOM   3386  CD  GLN D 502     -16.728 -26.686 -79.185  1.00 17.30           C  
ANISOU 3386  CD  GLN D 502     1895   2148   2529   -362   -689    -12       C  
ATOM   3387  OE1 GLN D 502     -16.234 -25.988 -80.075  1.00 19.70           O  
ANISOU 3387  OE1 GLN D 502     2270   2414   2802   -350   -747     21       O  
ATOM   3388  NE2 GLN D 502     -17.833 -27.403 -79.366  1.00 22.56           N  
ANISOU 3388  NE2 GLN D 502     2483   2864   3224   -400   -723    -14       N  
ATOM   3389  N   ARG D 503     -12.664 -24.059 -76.343  1.00 13.06           N  
ANISOU 3389  N   ARG D 503     1552   1481   1930   -227   -435    -74       N  
ATOM   3390  CA  ARG D 503     -11.336 -23.450 -76.406  1.00 12.52           C  
ANISOU 3390  CA  ARG D 503     1573   1374   1811   -223   -411    -74       C  
ATOM   3391  C   ARG D 503     -10.545 -23.687 -75.128  1.00 12.10           C  
ANISOU 3391  C   ARG D 503     1526   1336   1737   -230   -323   -105       C  
ATOM   3392  O   ARG D 503      -9.342 -23.937 -75.172  1.00 13.91           O  
ANISOU 3392  O   ARG D 503     1822   1554   1909   -255   -298   -105       O  
ATOM   3393  CB  ARG D 503     -11.434 -21.952 -76.678  1.00 14.65           C  
ANISOU 3393  CB  ARG D 503     1854   1597   2115   -166   -442    -63       C  
ATOM   3394  CG  ARG D 503     -10.086 -21.308 -76.951  1.00 15.50           C  
ANISOU 3394  CG  ARG D 503     2062   1664   2164   -173   -424    -62       C  
ATOM   3395  CD  ARG D 503     -10.255 -19.867 -77.409  1.00 13.72           C  
ANISOU 3395  CD  ARG D 503     1862   1383   1968   -124   -464    -44       C  
ATOM   3396  NE  ARG D 503      -8.974 -19.196 -77.608  1.00 18.06           N  
ANISOU 3396  NE  ARG D 503     2509   1893   2461   -138   -439    -49       N  
ATOM   3397  CZ  ARG D 503      -8.237 -19.300 -78.710  1.00 19.41           C  
ANISOU 3397  CZ  ARG D 503     2766   2042   2565   -182   -472    -27       C  
ATOM   3398  NH1 ARG D 503      -8.644 -20.061 -79.720  1.00 17.97           N  
ANISOU 3398  NH1 ARG D 503     2593   1873   2360   -218   -533      1       N  
ATOM   3399  NH2 ARG D 503      -7.090 -18.641 -78.802  1.00 21.20           N  
ANISOU 3399  NH2 ARG D 503     3073   2236   2747   -198   -439    -38       N  
ATOM   3400  N   LEU D 504     -11.224 -23.592 -73.990  1.00 13.65           N  
ANISOU 3400  N   LEU D 504     1651   1556   1978   -211   -276   -131       N  
ATOM   3401  CA  LEU D 504     -10.594 -23.876 -72.709  1.00 13.88           C  
ANISOU 3401  CA  LEU D 504     1688   1607   1981   -228   -199   -157       C  
ATOM   3402  C   LEU D 504      -9.989 -25.274 -72.731  1.00 10.83           C  
ANISOU 3402  C   LEU D 504     1333   1240   1541   -281   -188   -145       C  
ATOM   3403  O   LEU D 504      -8.833 -25.468 -72.360  1.00 11.74           O  
ANISOU 3403  O   LEU D 504     1499   1352   1610   -296   -158   -145       O  
ATOM   3404  CB  LEU D 504     -11.606 -23.752 -71.570  1.00 15.69           C  
ANISOU 3404  CB  LEU D 504     1836   1864   2263   -216   -149   -190       C  
ATOM   3405  CG  LEU D 504     -11.089 -24.203 -70.204  1.00 14.00           C  
ANISOU 3405  CG  LEU D 504     1632   1678   2010   -249    -74   -213       C  
ATOM   3406  CD1 LEU D 504      -9.911 -23.333 -69.770  1.00 17.87           C  
ANISOU 3406  CD1 LEU D 504     2182   2146   2461   -240    -45   -222       C  
ATOM   3407  CD2 LEU D 504     -12.210 -24.196 -69.162  1.00 15.15           C  
ANISOU 3407  CD2 LEU D 504     1700   1853   2203   -252    -19   -250       C  
ATOM   3408  N   ALA D 505     -10.784 -26.240 -73.179  1.00 11.34           N  
ANISOU 3408  N   ALA D 505     1366   1324   1617   -308   -214   -135       N  
ATOM   3409  CA  ALA D 505     -10.338 -27.623 -73.264  1.00 11.54           C  
ANISOU 3409  CA  ALA D 505     1424   1359   1601   -358   -201   -123       C  
ATOM   3410  C   ALA D 505      -9.161 -27.759 -74.223  1.00 10.60           C  
ANISOU 3410  C   ALA D 505     1384   1206   1436   -370   -222   -107       C  
ATOM   3411  O   ALA D 505      -8.166 -28.397 -73.893  1.00 12.10           O  
ANISOU 3411  O   ALA D 505     1614   1392   1593   -387   -189   -104       O  
ATOM   3412  CB  ALA D 505     -11.486 -28.528 -73.693  1.00 11.70           C  
ANISOU 3412  CB  ALA D 505     1400   1402   1643   -390   -226   -119       C  
ATOM   3413  N   GLN D 506      -9.268 -27.143 -75.398  1.00 10.65           N  
ANISOU 3413  N   GLN D 506     1415   1190   1443   -362   -277    -95       N  
ATOM   3414  CA  GLN D 506      -8.203 -27.226 -76.398  1.00 11.29           C  
ANISOU 3414  CA  GLN D 506     1574   1237   1476   -383   -290    -86       C  
ATOM   3415  C   GLN D 506      -6.876 -26.715 -75.840  1.00 10.99           C  
ANISOU 3415  C   GLN D 506     1574   1185   1415   -367   -247    -97       C  
ATOM   3416  O   GLN D 506      -5.818 -27.292 -76.092  1.00 14.15           O  
ANISOU 3416  O   GLN D 506     2020   1573   1784   -391   -224    -98       O  
ATOM   3417  CB  GLN D 506      -8.565 -26.433 -77.656  1.00 13.75           C  
ANISOU 3417  CB  GLN D 506     1914   1526   1785   -380   -358    -69       C  
ATOM   3418  CG  GLN D 506      -9.706 -27.011 -78.479  1.00 14.30           C  
ANISOU 3418  CG  GLN D 506     1958   1611   1864   -410   -416    -54       C  
ATOM   3419  CD  GLN D 506     -10.427 -25.951 -79.300  1.00 22.42           C  
ANISOU 3419  CD  GLN D 506     2981   2626   2912   -385   -495    -30       C  
ATOM   3420  OE1 GLN D 506     -10.048 -24.773 -79.293  1.00 23.35           O  
ANISOU 3420  OE1 GLN D 506     3123   2713   3035   -345   -501    -25       O  
ATOM   3421  NE2 GLN D 506     -11.464 -26.369 -80.025  1.00 20.44           N  
ANISOU 3421  NE2 GLN D 506     2700   2395   2672   -412   -558    -12       N  
ATOM   3422  N   LEU D 507      -6.944 -25.634 -75.070  1.00 11.10           N  
ANISOU 3422  N   LEU D 507     1566   1202   1449   -330   -232   -108       N  
ATOM   3423  CA  LEU D 507      -5.749 -25.041 -74.485  1.00 10.09           C  
ANISOU 3423  CA  LEU D 507     1470   1067   1297   -321   -194   -121       C  
ATOM   3424  C   LEU D 507      -5.131 -25.942 -73.423  1.00 12.26           C  
ANISOU 3424  C   LEU D 507     1733   1370   1558   -337   -148   -125       C  
ATOM   3425  O   LEU D 507      -3.917 -26.140 -73.391  1.00 12.96           O  
ANISOU 3425  O   LEU D 507     1854   1452   1618   -348   -130   -126       O  
ATOM   3426  CB  LEU D 507      -6.076 -23.672 -73.881  1.00 11.25           C  
ANISOU 3426  CB  LEU D 507     1598   1207   1468   -283   -184   -136       C  
ATOM   3427  CG  LEU D 507      -6.377 -22.565 -74.889  1.00 16.84           C  
ANISOU 3427  CG  LEU D 507     2335   1874   2189   -260   -230   -126       C  
ATOM   3428  CD1 LEU D 507      -6.704 -21.261 -74.176  1.00 17.64           C  
ANISOU 3428  CD1 LEU D 507     2417   1959   2325   -218   -210   -145       C  
ATOM   3429  CD2 LEU D 507      -5.201 -22.382 -75.834  1.00 22.17           C  
ANISOU 3429  CD2 LEU D 507     3090   2519   2814   -286   -239   -121       C  
ATOM   3430  N   LEU D 508      -5.969 -26.486 -72.549  1.00 10.23           N  
ANISOU 3430  N   LEU D 508     1426   1141   1319   -340   -131   -126       N  
ATOM   3431  CA  LEU D 508      -5.473 -27.330 -71.470  1.00  9.17           C  
ANISOU 3431  CA  LEU D 508     1287   1032   1167   -358    -95   -121       C  
ATOM   3432  C   LEU D 508      -4.920 -28.658 -71.973  1.00 11.31           C  
ANISOU 3432  C   LEU D 508     1583   1289   1423   -383    -98   -102       C  
ATOM   3433  O   LEU D 508      -4.027 -29.228 -71.358  1.00 12.90           O  
ANISOU 3433  O   LEU D 508     1798   1496   1609   -389    -78    -91       O  
ATOM   3434  CB  LEU D 508      -6.573 -27.585 -70.442  1.00 12.38           C  
ANISOU 3434  CB  LEU D 508     1642   1469   1591   -365    -71   -129       C  
ATOM   3435  CG  LEU D 508      -7.088 -26.324 -69.754  1.00 13.26           C  
ANISOU 3435  CG  LEU D 508     1725   1590   1722   -342    -49   -157       C  
ATOM   3436  CD1 LEU D 508      -8.143 -26.686 -68.730  1.00 11.43           C  
ANISOU 3436  CD1 LEU D 508     1443   1391   1508   -359    -13   -172       C  
ATOM   3437  CD2 LEU D 508      -5.940 -25.563 -69.107  1.00 16.70           C  
ANISOU 3437  CD2 LEU D 508     2194   2026   2124   -339    -26   -167       C  
ATOM   3438  N   LEU D 509      -5.452 -29.154 -73.086  1.00 11.90           N  
ANISOU 3438  N   LEU D 509     1667   1346   1507   -397   -125    -97       N  
ATOM   3439  CA  LEU D 509      -4.988 -30.429 -73.616  1.00 10.90           C  
ANISOU 3439  CA  LEU D 509     1570   1199   1371   -424   -119    -86       C  
ATOM   3440  C   LEU D 509      -3.600 -30.291 -74.233  1.00 11.13           C  
ANISOU 3440  C   LEU D 509     1644   1200   1384   -421   -112    -90       C  
ATOM   3441  O   LEU D 509      -2.842 -31.259 -74.282  1.00 15.01           O  
ANISOU 3441  O   LEU D 509     2154   1673   1876   -431    -90    -84       O  
ATOM   3442  CB  LEU D 509      -5.978 -30.990 -74.640  1.00 14.14           C  
ANISOU 3442  CB  LEU D 509     1982   1602   1789   -453   -147    -85       C  
ATOM   3443  CG  LEU D 509      -7.201 -31.636 -73.987  1.00 18.10           C  
ANISOU 3443  CG  LEU D 509     2437   2132   2309   -471   -141    -82       C  
ATOM   3444  CD1 LEU D 509      -8.166 -32.168 -75.027  1.00 23.02           C  
ANISOU 3444  CD1 LEU D 509     3056   2752   2937   -507   -173    -83       C  
ATOM   3445  CD2 LEU D 509      -6.782 -32.737 -73.027  1.00 17.41           C  
ANISOU 3445  CD2 LEU D 509     2357   2044   2215   -485   -100    -70       C  
ATOM   3446  N   ILE D 510      -3.266 -29.088 -74.694  1.00 11.28           N  
ANISOU 3446  N   ILE D 510     1681   1212   1394   -408   -125   -102       N  
ATOM   3447  CA  ILE D 510      -1.926 -28.824 -75.209  1.00 10.22           C  
ANISOU 3447  CA  ILE D 510     1585   1056   1243   -411   -110   -113       C  
ATOM   3448  C   ILE D 510      -0.900 -28.924 -74.082  1.00 14.54           C  
ANISOU 3448  C   ILE D 510     2112   1621   1791   -395    -82   -111       C  
ATOM   3449  O   ILE D 510       0.241 -29.323 -74.305  1.00 12.36           O  
ANISOU 3449  O   ILE D 510     1850   1331   1517   -399    -63   -115       O  
ATOM   3450  CB  ILE D 510      -1.827 -27.432 -75.887  1.00 18.08           C  
ANISOU 3450  CB  ILE D 510     2610   2037   2222   -406   -130   -126       C  
ATOM   3451  CG1 ILE D 510      -2.697 -27.382 -77.139  1.00 21.71           C  
ANISOU 3451  CG1 ILE D 510     3098   2477   2674   -427   -170   -120       C  
ATOM   3452  CG2 ILE D 510      -0.378 -27.110 -76.266  1.00 24.42           C  
ANISOU 3452  CG2 ILE D 510     3448   2824   3006   -416   -103   -143       C  
ATOM   3453  CD1 ILE D 510      -2.892 -25.993 -77.701  1.00 25.18           C  
ANISOU 3453  CD1 ILE D 510     3566   2899   3101   -417   -201   -120       C  
ATOM   3454  N   LEU D 511      -1.316 -28.582 -72.866  1.00 11.56           N  
ANISOU 3454  N   LEU D 511     1701   1276   1414   -381    -80   -104       N  
ATOM   3455  CA  LEU D 511      -0.416 -28.662 -71.721  1.00 12.95           C  
ANISOU 3455  CA  LEU D 511     1862   1476   1581   -375    -63    -97       C  
ATOM   3456  C   LEU D 511       0.075 -30.088 -71.488  1.00 15.19           C  
ANISOU 3456  C   LEU D 511     2142   1752   1879   -378    -56    -72       C  
ATOM   3457  O   LEU D 511       1.181 -30.302 -71.008  1.00 18.24           O  
ANISOU 3457  O   LEU D 511     2520   2144   2267   -371    -51    -62       O  
ATOM   3458  CB  LEU D 511      -1.091 -28.121 -70.458  1.00 16.23           C  
ANISOU 3458  CB  LEU D 511     2252   1928   1987   -373    -57    -97       C  
ATOM   3459  CG  LEU D 511      -1.453 -26.635 -70.518  1.00 17.99           C  
ANISOU 3459  CG  LEU D 511     2477   2152   2205   -363    -56   -124       C  
ATOM   3460  CD1 LEU D 511      -1.902 -26.128 -69.157  1.00 20.14           C  
ANISOU 3460  CD1 LEU D 511     2728   2458   2467   -366    -34   -133       C  
ATOM   3461  CD2 LEU D 511      -0.280 -25.822 -71.025  1.00 20.83           C  
ANISOU 3461  CD2 LEU D 511     2866   2498   2550   -362    -54   -139       C  
ATOM   3462  N   SER D 512      -0.726 -31.079 -71.845  1.00 12.75           N  
ANISOU 3462  N   SER D 512     1836   1424   1583   -390    -57    -61       N  
ATOM   3463  CA  SER D 512      -0.265 -32.443 -71.675  1.00 12.03           C  
ANISOU 3463  CA  SER D 512     1749   1312   1509   -391    -46    -37       C  
ATOM   3464  C   SER D 512       0.872 -32.763 -72.650  1.00 12.64           C  
ANISOU 3464  C   SER D 512     1845   1351   1606   -386    -32    -50       C  
ATOM   3465  O   SER D 512       1.791 -33.519 -72.323  1.00 14.82           O  
ANISOU 3465  O   SER D 512     2113   1612   1907   -370    -22    -33       O  
ATOM   3466  CB  SER D 512      -1.415 -33.422 -71.856  1.00 23.15           C  
ANISOU 3466  CB  SER D 512     3164   2707   2925   -414    -43    -28       C  
ATOM   3467  OG  SER D 512      -0.939 -34.741 -71.723  1.00 39.19           O  
ANISOU 3467  OG  SER D 512     5209   4706   4977   -415    -29     -4       O  
ATOM   3468  N   HIS D 513       0.807 -32.179 -73.844  1.00 12.01           N  
ANISOU 3468  N   HIS D 513     1790   1254   1518   -399    -31    -79       N  
ATOM   3469  CA  HIS D 513       1.865 -32.353 -74.832  1.00 12.35           C  
ANISOU 3469  CA  HIS D 513     1856   1263   1575   -405     -7   -102       C  
ATOM   3470  C   HIS D 513       3.147 -31.658 -74.381  1.00 12.11           C  
ANISOU 3470  C   HIS D 513     1803   1251   1548   -386      0   -110       C  
ATOM   3471  O   HIS D 513       4.246 -32.157 -74.609  1.00 12.39           O  
ANISOU 3471  O   HIS D 513     1829   1265   1614   -377     25   -118       O  
ATOM   3472  CB  HIS D 513       1.438 -31.818 -76.199  1.00 14.34           C  
ANISOU 3472  CB  HIS D 513     2151   1495   1802   -437    -10   -130       C  
ATOM   3473  CG  HIS D 513       2.470 -32.015 -77.265  0.58 13.53           C  
ANISOU 3473  CG  HIS D 513     2063   1372   1707   -435     24   -154       C  
ATOM   3474  ND1 HIS D 513       3.078 -30.967 -77.920  0.48 16.07           N  
ANISOU 3474  ND1 HIS D 513     2393   1706   2005   -432     30   -172       N  
ATOM   3475  CD2 HIS D 513       3.024 -33.145 -77.770  1.00 22.03           C  
ANISOU 3475  CD2 HIS D 513     3144   2415   2811   -437     61   -163       C  
ATOM   3476  CE1 HIS D 513       3.950 -31.440 -78.795  1.00 22.68           C  
ANISOU 3476  CE1 HIS D 513     3240   2525   2853   -436     68   -193       C  
ATOM   3477  NE2 HIS D 513       3.933 -32.760 -78.723  0.72 23.13           N  
ANISOU 3477  NE2 HIS D 513     3293   2552   2944   -438     88   -190       N  
ATOM   3478  N   ILE D 514       2.995 -30.504 -73.741  1.00  9.90           N  
ANISOU 3478  N   ILE D 514     1512   1009   1241   -381    -18   -111       N  
ATOM   3479  CA  ILE D 514       4.138 -29.754 -73.234  1.00  9.91           C  
ANISOU 3479  CA  ILE D 514     1492   1035   1238   -373    -14   -121       C  
ATOM   3480  C   ILE D 514       4.822 -30.526 -72.105  1.00  9.50           C  
ANISOU 3480  C   ILE D 514     1398   1004   1209   -351    -21    -89       C  
ATOM   3481  O   ILE D 514       6.047 -30.529 -71.999  1.00 15.74           O  
ANISOU 3481  O   ILE D 514     2162   1800   2019   -342    -15    -94       O  
ATOM   3482  CB  ILE D 514       3.711 -28.351 -72.761  1.00 15.36           C  
ANISOU 3482  CB  ILE D 514     2188   1757   1893   -378    -27   -131       C  
ATOM   3483  CG1 ILE D 514       3.381 -27.480 -73.975  1.00 18.10           C  
ANISOU 3483  CG1 ILE D 514     2579   2076   2221   -395    -25   -158       C  
ATOM   3484  CG2 ILE D 514       4.806 -27.691 -71.944  1.00 20.75           C  
ANISOU 3484  CG2 ILE D 514     2845   2474   2564   -377    -25   -138       C  
ATOM   3485  CD1 ILE D 514       2.779 -26.143 -73.625  1.00 19.96           C  
ANISOU 3485  CD1 ILE D 514     2826   2326   2433   -393    -37   -167       C  
ATOM   3486  N   ARG D 515       4.028 -31.201 -71.277  1.00 11.09           N  
ANISOU 3486  N   ARG D 515     1592   1213   1407   -346    -37    -54       N  
ATOM   3487  CA  ARG D 515       4.582 -32.078 -70.255  1.00 10.19           C  
ANISOU 3487  CA  ARG D 515     1451   1110   1311   -329    -51    -13       C  
ATOM   3488  C   ARG D 515       5.380 -33.211 -70.891  1.00 11.37           C  
ANISOU 3488  C   ARG D 515     1593   1210   1516   -308    -35     -7       C  
ATOM   3489  O   ARG D 515       6.489 -33.513 -70.458  1.00 14.13           O  
ANISOU 3489  O   ARG D 515     1907   1565   1897   -285    -44     10       O  
ATOM   3490  CB  ARG D 515       3.473 -32.647 -69.363  1.00 11.97           C  
ANISOU 3490  CB  ARG D 515     1685   1346   1517   -338    -64     21       C  
ATOM   3491  CG  ARG D 515       3.957 -33.712 -68.389  1.00 16.62           C  
ANISOU 3491  CG  ARG D 515     2261   1933   2120   -324    -83     73       C  
ATOM   3492  CD  ARG D 515       5.083 -33.164 -67.512  1.00 24.48           C  
ANISOU 3492  CD  ARG D 515     3226   2973   3104   -317   -111     88       C  
ATOM   3493  NE  ARG D 515       4.639 -32.852 -66.159  1.00 25.46           N  
ANISOU 3493  NE  ARG D 515     3354   3145   3173   -343   -133    114       N  
ATOM   3494  CZ  ARG D 515       5.442 -32.465 -65.171  1.00 29.70           C  
ANISOU 3494  CZ  ARG D 515     3872   3728   3683   -351   -164    135       C  
ATOM   3495  NH1 ARG D 515       4.936 -32.212 -63.973  1.00 33.18           N  
ANISOU 3495  NH1 ARG D 515     4330   4212   4065   -387   -176    153       N  
ATOM   3496  NH2 ARG D 515       6.747 -32.311 -65.374  1.00 31.20           N  
ANISOU 3496  NH2 ARG D 515     4025   3926   3902   -331   -181    134       N  
ATOM   3497  N   HIS D 516       4.816 -33.823 -71.925  1.00 11.07           N  
ANISOU 3497  N   HIS D 516     1586   1126   1494   -318    -10    -24       N  
ATOM   3498  CA  HIS D 516       5.495 -34.894 -72.650  1.00 11.80           C  
ANISOU 3498  CA  HIS D 516     1679   1161   1642   -304     21    -30       C  
ATOM   3499  C   HIS D 516       6.870 -34.434 -73.134  1.00 13.60           C  
ANISOU 3499  C   HIS D 516     1879   1388   1900   -292     42    -62       C  
ATOM   3500  O   HIS D 516       7.877 -35.109 -72.912  1.00 14.37           O  
ANISOU 3500  O   HIS D 516     1939   1468   2055   -260     48    -49       O  
ATOM   3501  CB  HIS D 516       4.633 -35.351 -73.826  1.00 10.87           C  
ANISOU 3501  CB  HIS D 516     1611   1001   1520   -334     49    -56       C  
ATOM   3502  CG  HIS D 516       5.131 -36.583 -74.513  1.00 18.03           C  
ANISOU 3502  CG  HIS D 516     2528   1840   2480   -327     90    -65       C  
ATOM   3503  ND1 HIS D 516       5.817 -37.585 -73.859  1.00 22.15           N  
ANISOU 3503  ND1 HIS D 516     3023   2334   3060   -287     92    -31       N  
ATOM   3504  CD2 HIS D 516       4.992 -37.003 -75.793  1.00 27.79           C  
ANISOU 3504  CD2 HIS D 516     3806   3029   3724   -358    133   -105       C  
ATOM   3505  CE1 HIS D 516       6.103 -38.552 -74.712  1.00 25.71           C  
ANISOU 3505  CE1 HIS D 516     3494   2716   3558   -288    141    -53       C  
ATOM   3506  NE2 HIS D 516       5.607 -38.226 -75.893  1.00 30.70           N  
ANISOU 3506  NE2 HIS D 516     4170   3337   4157   -336    170   -102       N  
ATOM   3507  N   MET D 517       6.911 -33.269 -73.772  1.00 10.69           N  
ANISOU 3507  N   MET D 517     1527   1039   1495   -319     51   -103       N  
ATOM   3508  CA  MET D 517       8.169 -32.738 -74.282  1.00 12.16           C  
ANISOU 3508  CA  MET D 517     1691   1227   1701   -321     78   -141       C  
ATOM   3509  C   MET D 517       9.182 -32.486 -73.173  1.00 10.78           C  
ANISOU 3509  C   MET D 517     1451   1097   1546   -294     51   -119       C  
ATOM   3510  O   MET D 517      10.375 -32.749 -73.347  1.00 11.85           O  
ANISOU 3510  O   MET D 517     1541   1225   1735   -277     71   -134       O  
ATOM   3511  CB  MET D 517       7.934 -31.451 -75.060  1.00 10.94           C  
ANISOU 3511  CB  MET D 517     1578   1085   1494   -362     88   -182       C  
ATOM   3512  CG  MET D 517       7.096 -31.645 -76.306  1.00 15.00           C  
ANISOU 3512  CG  MET D 517     2156   1556   1986   -395    109   -205       C  
ATOM   3513  SD  MET D 517       7.065 -30.152 -77.304  1.00 15.07           S  
ANISOU 3513  SD  MET D 517     2214   1575   1935   -435    114   -242       S  
ATOM   3514  CE  MET D 517       6.004 -29.089 -76.325  1.00 18.05           C  
ANISOU 3514  CE  MET D 517     2597   1992   2270   -430     60   -215       C  
ATOM   3515  N   SER D 518       8.711 -31.968 -72.043  1.00 12.18           N  
ANISOU 3515  N   SER D 518     1624   1325   1681   -295      7    -87       N  
ATOM   3516  CA  SER D 518       9.591 -31.710 -70.912  1.00 18.07           C  
ANISOU 3516  CA  SER D 518     2315   2120   2429   -282    -28    -61       C  
ATOM   3517  C   SER D 518      10.213 -33.003 -70.396  1.00 11.23           C  
ANISOU 3517  C   SER D 518     1405   1235   1628   -239    -48    -15       C  
ATOM   3518  O   SER D 518      11.408 -33.054 -70.119  1.00 12.74           O  
ANISOU 3518  O   SER D 518     1535   1444   1862   -218    -60    -11       O  
ATOM   3519  CB  SER D 518       8.835 -31.005 -69.789  1.00 10.44           C  
ANISOU 3519  CB  SER D 518     1364   1205   1397   -301    -65    -38       C  
ATOM   3520  OG  SER D 518       9.627 -30.934 -68.611  1.00 12.74           O  
ANISOU 3520  OG  SER D 518     1611   1547   1684   -296   -105     -5       O  
ATOM   3521  N   ASN D 519       9.400 -34.047 -70.274  1.00 11.01           N  
ANISOU 3521  N   ASN D 519     1405   1168   1610   -225    -51     20       N  
ATOM   3522  CA  ASN D 519       9.904 -35.341 -69.833  1.00 12.08           C  
ANISOU 3522  CA  ASN D 519     1511   1268   1811   -181    -69     69       C  
ATOM   3523  C   ASN D 519      11.013 -35.863 -70.728  1.00 12.48           C  
ANISOU 3523  C   ASN D 519     1521   1272   1950   -150    -28     38       C  
ATOM   3524  O   ASN D 519      12.026 -36.363 -70.246  1.00 22.29           O  
ANISOU 3524  O   ASN D 519     2702   2513   3256   -107    -52     69       O  
ATOM   3525  CB  ASN D 519       8.770 -36.358 -69.760  1.00 24.31           C  
ANISOU 3525  CB  ASN D 519     3111   2772   3354   -183    -65    101       C  
ATOM   3526  CG  ASN D 519       7.987 -36.245 -68.479  1.00 22.99           C  
ANISOU 3526  CG  ASN D 519     2964   2649   3124   -201   -111    151       C  
ATOM   3527  OD1 ASN D 519       8.562 -35.982 -67.419  1.00 33.48           O  
ANISOU 3527  OD1 ASN D 519     4261   4024   4436   -196   -159    188       O  
ATOM   3528  ND2 ASN D 519       6.676 -36.443 -68.560  1.00 15.83           N  
ANISOU 3528  ND2 ASN D 519     2107   1730   2179   -230    -97    150       N  
ATOM   3529  N   LYS D 520      10.829 -35.725 -72.034  1.00 11.96           N  
ANISOU 3529  N   LYS D 520     1488   1169   1888   -173     34    -23       N  
ATOM   3530  CA  LYS D 520      11.833 -36.185 -72.985  1.00 16.99           C  
ANISOU 3530  CA  LYS D 520     2093   1757   2604   -154     90    -66       C  
ATOM   3531  C   LYS D 520      13.091 -35.324 -72.881  1.00 14.94           C  
ANISOU 3531  C   LYS D 520     1765   1547   2365   -152     88    -94       C  
ATOM   3532  O   LYS D 520      14.211 -35.824 -72.997  1.00 17.20           O  
ANISOU 3532  O   LYS D 520     1983   1814   2740   -115    106   -103       O  
ATOM   3533  CB  LYS D 520      11.268 -36.165 -74.408  1.00 16.32           C  
ANISOU 3533  CB  LYS D 520     2076   1626   2500   -198    157   -127       C  
ATOM   3534  CG  LYS D 520      10.061 -37.085 -74.598  1.00 18.40           C  
ANISOU 3534  CG  LYS D 520     2402   1841   2748   -207    163   -106       C  
ATOM   3535  CD  LYS D 520       9.671 -37.246 -76.065  1.00 26.23           C  
ANISOU 3535  CD  LYS D 520     3456   2783   3728   -254    228   -166       C  
ATOM   3536  CE  LYS D 520      10.642 -38.154 -76.812  1.00 31.78           C  
ANISOU 3536  CE  LYS D 520     4138   3416   4520   -235    299   -205       C  
ATOM   3537  NZ  LYS D 520      10.545 -39.579 -76.386  1.00 33.69           N  
ANISOU 3537  NZ  LYS D 520     4376   3596   4830   -190    303   -164       N  
ATOM   3538  N   GLY D 521      12.897 -34.031 -72.642  1.00 15.53           N  
ANISOU 3538  N   GLY D 521     1855   1685   2362   -193     67   -109       N  
ATOM   3539  CA  GLY D 521      14.004 -33.113 -72.442  1.00 13.45           C  
ANISOU 3539  CA  GLY D 521     1532   1476   2103   -204     61   -136       C  
ATOM   3540  C   GLY D 521      14.756 -33.395 -71.154  1.00 16.39           C  
ANISOU 3540  C   GLY D 521     1825   1893   2509   -165     -6    -78       C  
ATOM   3541  O   GLY D 521      15.988 -33.375 -71.135  1.00 16.22           O  
ANISOU 3541  O   GLY D 521     1722   1889   2550   -147     -4    -93       O  
ATOM   3542  N   MET D 522      14.015 -33.658 -70.078  1.00 14.29           N  
ANISOU 3542  N   MET D 522     1582   1646   2201   -157    -67    -12       N  
ATOM   3543  CA  MET D 522      14.624 -33.971 -68.787  1.00 19.74           C  
ANISOU 3543  CA  MET D 522     2212   2379   2908   -129   -143     54       C  
ATOM   3544  C   MET D 522      15.395 -35.278 -68.869  1.00 23.17           C  
ANISOU 3544  C   MET D 522     2587   2760   3458    -61   -147     87       C  
ATOM   3545  O   MET D 522      16.437 -35.431 -68.235  1.00 24.93           O  
ANISOU 3545  O   MET D 522     2726   3014   3732    -30   -197    119       O  
ATOM   3546  CB  MET D 522      13.567 -34.047 -67.675  1.00 20.77           C  
ANISOU 3546  CB  MET D 522     2397   2535   2962   -146   -196    115       C  
ATOM   3547  CG  MET D 522      12.954 -32.709 -67.285  1.00 24.68           C  
ANISOU 3547  CG  MET D 522     2934   3090   3353   -206   -200     90       C  
ATOM   3548  SD  MET D 522      14.146 -31.542 -66.595  1.00 18.65           S  
ANISOU 3548  SD  MET D 522     2108   2417   2562   -238   -238     75       S  
ATOM   3549  CE  MET D 522      14.778 -32.487 -65.219  1.00 24.01           C  
ANISOU 3549  CE  MET D 522     2731   3126   3266   -205   -332    170       C  
ATOM   3550  N   GLU D 523      14.877 -36.216 -69.656  1.00 17.62           N  
ANISOU 3550  N   GLU D 523     1924   1973   2797    -40    -96     77       N  
ATOM   3551  CA  GLU D 523      15.557 -37.489 -69.867  1.00 21.25           C  
ANISOU 3551  CA  GLU D 523     2335   2363   3376     27    -84     99       C  
ATOM   3552  C   GLU D 523      16.958 -37.271 -70.429  1.00 19.36           C  
ANISOU 3552  C   GLU D 523     2000   2130   3226     49    -49     47       C  
ATOM   3553  O   GLU D 523      17.918 -37.910 -69.992  1.00 20.18           O  
ANISOU 3553  O   GLU D 523     2017   2224   3427    110    -84     84       O  
ATOM   3554  CB  GLU D 523      14.753 -38.398 -70.807  1.00 22.34           C  
ANISOU 3554  CB  GLU D 523     2544   2408   3536     30    -15     76       C  
ATOM   3555  CG  GLU D 523      13.576 -39.118 -70.161  1.00 28.19           C  
ANISOU 3555  CG  GLU D 523     3357   3123   4231     28    -50    141       C  
ATOM   3556  CD  GLU D 523      12.573 -39.611 -71.193  1.00 30.95           C  
ANISOU 3556  CD  GLU D 523     3789   3405   4567      0     21    100       C  
ATOM   3557  OE1 GLU D 523      13.008 -39.999 -72.297  1.00 31.01           O  
ANISOU 3557  OE1 GLU D 523     3790   3352   4639      8     94     43       O  
ATOM   3558  OE2 GLU D 523      11.355 -39.591 -70.916  1.00 37.38           O  
ANISOU 3558  OE2 GLU D 523     4671   4228   5303    -37      6    121       O  
ATOM   3559  N   HIS D 524      17.080 -36.364 -71.393  1.00 17.18           N  
ANISOU 3559  N   HIS D 524     1739   1870   2920     -1     17    -38       N  
ATOM   3560  CA  HIS D 524      18.389 -36.078 -71.963  1.00 18.24           C  
ANISOU 3560  CA  HIS D 524     1784   2014   3131      6     62    -98       C  
ATOM   3561  C   HIS D 524      19.311 -35.373 -70.981  1.00 19.88           C  
ANISOU 3561  C   HIS D 524     1902   2314   3339      7    -12    -72       C  
ATOM   3562  O   HIS D 524      20.494 -35.704 -70.890  1.00 19.66           O  
ANISOU 3562  O   HIS D 524     1763   2292   3415     51    -18    -74       O  
ATOM   3563  CB  HIS D 524      18.283 -35.231 -73.227  1.00 20.77           C  
ANISOU 3563  CB  HIS D 524     2156   2330   3407    -62    151   -194       C  
ATOM   3564  CG  HIS D 524      19.612 -34.959 -73.851  1.00 22.32           C  
ANISOU 3564  CG  HIS D 524     2266   2535   3681    -65    210   -263       C  
ATOM   3565  ND1 HIS D 524      20.378 -35.950 -74.425  1.00 24.39           N  
ANISOU 3565  ND1 HIS D 524     2464   2731   4072    -15    270   -292       N  
ATOM   3566  CD2 HIS D 524      20.337 -33.819 -73.950  1.00 18.62           C  
ANISOU 3566  CD2 HIS D 524     1758   2132   3184   -114    222   -313       C  
ATOM   3567  CE1 HIS D 524      21.509 -35.431 -74.867  1.00 22.55           C  
ANISOU 3567  CE1 HIS D 524     2152   2527   3890    -33    319   -359       C  
ATOM   3568  NE2 HIS D 524      21.508 -34.138 -74.592  1.00 23.84           N  
ANISOU 3568  NE2 HIS D 524     2331   2771   3955    -96    289   -372       N  
ATOM   3569  N   LEU D 525      18.776 -34.392 -70.261  1.00 16.72           N  
ANISOU 3569  N   LEU D 525     1544   1985   2823    -44    -64    -52       N  
ATOM   3570  CA  LEU D 525      19.586 -33.625 -69.323  1.00 14.66           C  
ANISOU 3570  CA  LEU D 525     1211   1818   2542    -62   -132    -34       C  
ATOM   3571  C   LEU D 525      20.211 -34.536 -68.271  1.00 17.29           C  
ANISOU 3571  C   LEU D 525     1460   2162   2948      4   -222     53       C  
ATOM   3572  O   LEU D 525      21.397 -34.412 -67.957  1.00 20.07           O  
ANISOU 3572  O   LEU D 525     1702   2562   3364     22   -257     55       O  
ATOM   3573  CB  LEU D 525      18.752 -32.526 -68.661  1.00 16.03           C  
ANISOU 3573  CB  LEU D 525     1461   2053   2576   -128   -167    -24       C  
ATOM   3574  CG  LEU D 525      18.363 -31.362 -69.579  1.00 15.44           C  
ANISOU 3574  CG  LEU D 525     1454   1982   2432   -195    -94   -106       C  
ATOM   3575  CD1 LEU D 525      17.555 -30.320 -68.821  1.00 14.16           C  
ANISOU 3575  CD1 LEU D 525     1360   1874   2148   -250   -129    -94       C  
ATOM   3576  CD2 LEU D 525      19.614 -30.740 -70.183  1.00 15.56           C  
ANISOU 3576  CD2 LEU D 525     1397   2025   2491   -219    -49   -176       C  
ATOM   3577  N   TYR D 526      19.420 -35.464 -67.742  1.00 20.75           N  
ANISOU 3577  N   TYR D 526     1950   2555   3379     39   -262    127       N  
ATOM   3578  CA  TYR D 526      19.937 -36.432 -66.781  1.00 21.77           C  
ANISOU 3578  CA  TYR D 526     2016   2680   3577    105   -351    221       C  
ATOM   3579  C   TYR D 526      20.966 -37.364 -67.414  1.00 19.82           C  
ANISOU 3579  C   TYR D 526     1670   2368   3494    185   -319    208       C  
ATOM   3580  O   TYR D 526      21.927 -37.768 -66.757  1.00 20.03           O  
ANISOU 3580  O   TYR D 526     1593   2416   3601    238   -393    262       O  
ATOM   3581  CB  TYR D 526      18.801 -37.254 -66.163  1.00 19.36           C  
ANISOU 3581  CB  TYR D 526     1803   2328   3223    117   -389    298       C  
ATOM   3582  CG  TYR D 526      18.051 -36.525 -65.071  1.00 19.48           C  
ANISOU 3582  CG  TYR D 526     1885   2420   3098     52   -452    338       C  
ATOM   3583  CD1 TYR D 526      18.709 -36.095 -63.925  1.00 25.62           C  
ANISOU 3583  CD1 TYR D 526     2610   3285   3841     34   -548    390       C  
ATOM   3584  CD2 TYR D 526      16.688 -36.283 -65.175  1.00 20.87           C  
ANISOU 3584  CD2 TYR D 526     2172   2581   3178      4   -414    323       C  
ATOM   3585  CE1 TYR D 526      18.034 -35.430 -62.917  1.00 24.88           C  
ANISOU 3585  CE1 TYR D 526     2581   3257   3614    -35   -596    419       C  
ATOM   3586  CE2 TYR D 526      16.001 -35.620 -64.168  1.00 20.61           C  
ANISOU 3586  CE2 TYR D 526     2194   2612   3023    -56   -460    352       C  
ATOM   3587  CZ  TYR D 526      16.681 -35.197 -63.042  1.00 23.68           C  
ANISOU 3587  CZ  TYR D 526     2538   3084   3375    -77   -547    397       C  
ATOM   3588  OH  TYR D 526      16.003 -34.535 -62.040  1.00 33.64           O  
ANISOU 3588  OH  TYR D 526     3862   4408   4512   -146   -582    418       O  
ATOM   3589  N   SER D 527      20.771 -37.698 -68.687  1.00 18.96           N  
ANISOU 3589  N   SER D 527     1591   2180   3435    193   -208    135       N  
ATOM   3590  CA  SER D 527      21.678 -38.613 -69.376  1.00 22.88           C  
ANISOU 3590  CA  SER D 527     2001   2602   4091    266   -155    109       C  
ATOM   3591  C   SER D 527      23.071 -38.011 -69.543  1.00 23.63           C  
ANISOU 3591  C   SER D 527     1960   2756   4261    269   -147     58       C  
ATOM   3592  O   SER D 527      24.054 -38.733 -69.720  1.00 21.20           O  
ANISOU 3592  O   SER D 527     1543   2410   4103    342   -136     56       O  
ATOM   3593  CB  SER D 527      21.113 -38.997 -70.745  1.00 25.49           C  
ANISOU 3593  CB  SER D 527     2407   2839   4438    251    -28     30       C  
ATOM   3594  OG  SER D 527      21.369 -37.986 -71.704  1.00 28.31           O  
ANISOU 3594  OG  SER D 527     2767   3228   4760    184     55    -73       O  
ATOM   3595  N   MET D 528      23.155 -36.687 -69.487  1.00 20.67           N  
ANISOU 3595  N   MET D 528     1593   2474   3788    189   -149     13       N  
ATOM   3596  CA  MET D 528      24.428 -36.008 -69.693  1.00 20.55           C  
ANISOU 3596  CA  MET D 528     1457   2522   3829    173   -133    -46       C  
ATOM   3597  C   MET D 528      25.412 -36.238 -68.553  1.00 22.47           C  
ANISOU 3597  C   MET D 528     1568   2828   4142    224   -252     31       C  
ATOM   3598  O   MET D 528      26.619 -36.136 -68.753  1.00 25.00           O  
ANISOU 3598  O   MET D 528     1754   3178   4567    244   -241     -8       O  
ATOM   3599  CB  MET D 528      24.210 -34.507 -69.886  1.00 21.35           C  
ANISOU 3599  CB  MET D 528     1614   2701   3799     68   -106   -110       C  
ATOM   3600  CG  MET D 528      23.379 -34.157 -71.104  1.00 23.97           C  
ANISOU 3600  CG  MET D 528     2064   2976   4066     14      6   -188       C  
ATOM   3601  SD  MET D 528      22.997 -32.402 -71.205  1.00 20.52           S  
ANISOU 3601  SD  MET D 528     1708   2618   3470   -102     22   -244       S  
ATOM   3602  CE  MET D 528      24.634 -31.694 -71.387  1.00 23.35           C  
ANISOU 3602  CE  MET D 528     1927   3047   3897   -131     48   -314       C  
ATOM   3603  N   LYS D 529      24.892 -36.543 -67.365  1.00 22.74           N  
ANISOU 3603  N   LYS D 529     2023   2781   3838    750   -184    266       N  
ATOM   3604  CA  LYS D 529      25.718 -36.722 -66.172  1.00 24.42           C  
ANISOU 3604  CA  LYS D 529     1952   3192   4134    803   -376    245       C  
ATOM   3605  C   LYS D 529      26.577 -35.477 -65.936  1.00 25.41           C  
ANISOU 3605  C   LYS D 529     1916   3458   4281    650   -255     47       C  
ATOM   3606  O   LYS D 529      27.756 -35.571 -65.590  1.00 27.47           O  
ANISOU 3606  O   LYS D 529     1900   3836   4701    674   -295    -66       O  
ATOM   3607  CB  LYS D 529      26.587 -37.980 -66.294  1.00 27.06           C  
ANISOU 3607  CB  LYS D 529     2092   3495   4695    981   -476    233       C  
ATOM   3608  CG  LYS D 529      25.849 -39.275 -65.960  1.00 30.75           C  
ANISOU 3608  CG  LYS D 529     2680   3892   5111   1125   -702    452       C  
ATOM   3609  CD  LYS D 529      26.414 -40.456 -66.748  1.00 33.46           C  
ANISOU 3609  CD  LYS D 529     3019   4108   5586   1252   -656    398       C  
ATOM   3610  CE  LYS D 529      26.679 -41.676 -65.868  1.00 36.33           C  
ANISOU 3610  CE  LYS D 529     3380   4568   5856   1324   -849    482       C  
ATOM   3611  NZ  LYS D 529      27.555 -41.389 -64.696  1.00 40.54           N  
ANISOU 3611  NZ  LYS D 529     3670   5307   6427   1300   -980    453       N  
ATOM   3612  N  ASER D 530      25.975 -34.317 -66.174  0.45 24.06           N  
ANISOU 3612  N  ASER D 530     1923   3259   3959    492   -111      9       N  
ATOM   3613  N  BSER D 530      25.965 -34.306 -66.104  0.55 24.06           N  
ANISOU 3613  N  BSER D 530     1919   3268   3955    492   -121     13       N  
ATOM   3614  CA ASER D 530      26.604 -33.040 -65.881  0.45 25.20           C  
ANISOU 3614  CA ASER D 530     1963   3522   4089    326    -13   -159       C  
ATOM   3615  CA BSER D 530      26.652 -33.029 -65.912  0.55 24.88           C  
ANISOU 3615  CA BSER D 530     1917   3482   4055    324     -6   -167       C  
ATOM   3616  C  ASER D 530      26.084 -32.567 -64.537  0.45 25.74           C  
ANISOU 3616  C  ASER D 530     2028   3746   4007    286   -189    -86       C  
ATOM   3617  C  BSER D 530      26.124 -32.310 -64.667  0.55 25.02           C  
ANISOU 3617  C  BSER D 530     1951   3645   3911    251   -143   -119       C  
ATOM   3618  O  ASER D 530      24.880 -32.603 -64.286  0.45 22.78           O  
ANISOU 3618  O  ASER D 530     1850   3326   3479    302   -252     56       O  
ATOM   3619  O  BSER D 530      24.964 -31.895 -64.634  0.55 23.32           O  
ANISOU 3619  O  BSER D 530     1960   3363   3539    213   -130    -32       O  
ATOM   3620  CB ASER D 530      26.310 -32.012 -66.976  0.45 24.45           C  
ANISOU 3620  CB ASER D 530     2071   3285   3933    165    243   -255       C  
ATOM   3621  CB BSER D 530      26.484 -32.140 -67.148  0.55 24.27           C  
ANISOU 3621  CB BSER D 530     2027   3252   3944    175    265   -272       C  
ATOM   3622  OG ASER D 530      27.100 -30.843 -66.813  0.45 25.00           O  
ANISOU 3622  OG ASER D 530     2026   3457   4017     -1    344   -433       O  
ATOM   3623  OG BSER D 530      27.200 -32.652 -68.262  0.55 26.41           O  
ANISOU 3623  OG BSER D 530     2248   3428   4358    199    424   -369       O  
ATOM   3624  N   LYS D 531      26.998 -32.143 -63.673  1.00 29.09           N  
ANISOU 3624  N   LYS D 531     2223   4358   4472    226   -265   -186       N  
ATOM   3625  CA  LYS D 531      26.641 -31.735 -62.309  1.00 31.47           C  
ANISOU 3625  CA  LYS D 531     2502   4831   4623    172   -439   -136       C  
ATOM   3626  C   LYS D 531      25.467 -30.770 -62.147  1.00 32.92           C  
ANISOU 3626  C   LYS D 531     2925   4975   4608     70   -368   -120       C  
ATOM   3627  O   LYS D 531      24.549 -31.042 -61.374  1.00 32.07           O  
ANISOU 3627  O   LYS D 531     2903   4923   4357    105   -506     14       O  
ATOM   3628  CB  LYS D 531      27.864 -31.123 -61.621  1.00 33.72           C  
ANISOU 3628  CB  LYS D 531     2534   5304   4976     69   -476   -286       C  
ATOM   3629  CG  LYS D 531      27.647 -30.861 -60.140  1.00 35.84           C  
ANISOU 3629  CG  LYS D 531     2756   5769   5091      8   -680   -236       C  
ATOM   3630  CD  LYS D 531      27.912 -32.118 -59.323  1.00 37.39           C  
ANISOU 3630  CD  LYS D 531     2796   6073   5337    136   -960    -83       C  
ATOM   3631  CE  LYS D 531      27.835 -31.849 -57.828  1.00 38.44           C  
ANISOU 3631  CE  LYS D 531     2873   6426   5306     39  -1168    -41       C  
ATOM   3632  NZ  LYS D 531      28.086 -33.092 -57.043  1.00 41.66           N  
ANISOU 3632  NZ  LYS D 531     3261   6789   5778    140  -1415    112       N  
ATOM   3633  N   ASN D 532      25.486 -29.660 -62.877  1.00 32.71           N  
ANISOU 3633  N   ASN D 532     3001   4850   4577    -60   -157   -256       N  
ATOM   3634  CA  ASN D 532      24.474 -28.623 -62.687  1.00 33.50           C  
ANISOU 3634  CA  ASN D 532     3303   4903   4524   -156    -96   -268       C  
ATOM   3635  C   ASN D 532      23.636 -28.318 -63.928  1.00 32.52           C  
ANISOU 3635  C   ASN D 532     3431   4534   4390   -173     72   -236       C  
ATOM   3636  O   ASN D 532      23.239 -27.171 -64.143  1.00 33.60           O  
ANISOU 3636  O   ASN D 532     3702   4589   4475   -292    181   -317       O  
ATOM   3637  CB  ASN D 532      25.140 -27.331 -62.204  1.00 33.81           C  
ANISOU 3637  CB  ASN D 532     3259   5043   4544   -327    -39   -457       C  
ATOM   3638  CG  ASN D 532      25.668 -27.443 -60.792  1.00 35.99           C  
ANISOU 3638  CG  ASN D 532     3337   5566   4771   -342   -227   -472       C  
ATOM   3639  OD1 ASN D 532      24.903 -27.404 -59.826  1.00 39.32           O  
ANISOU 3639  OD1 ASN D 532     3816   6081   5043   -339   -341   -407       O  
ATOM   3640  ND2 ASN D 532      26.982 -27.583 -60.661  1.00 38.56           N  
ANISOU 3640  ND2 ASN D 532     3425   6006   5222   -371   -261   -558       N  
ATOM   3641  N   VAL D 533      23.359 -29.338 -64.735  1.00 24.65           N  
ANISOU 3641  N   VAL D 533     2508   3413   3447    -61     80   -116       N  
ATOM   3642  CA  VAL D 533      22.564 -29.139 -65.942  1.00 24.89           C  
ANISOU 3642  CA  VAL D 533     2787   3210   3461    -88    221    -67       C  
ATOM   3643  C   VAL D 533      21.095 -29.419 -65.622  1.00 22.98           C  
ANISOU 3643  C   VAL D 533     2719   2916   3096    -12    122    113       C  
ATOM   3644  O   VAL D 533      20.198 -29.102 -66.401  1.00 20.56           O  
ANISOU 3644  O   VAL D 533     2630   2427   2756    -42    202    174       O  
ATOM   3645  CB  VAL D 533      23.048 -30.033 -67.102  1.00 24.49           C  
ANISOU 3645  CB  VAL D 533     2745   3038   3523    -33    308    -51       C  
ATOM   3646  CG1 VAL D 533      22.579 -31.473 -66.912  1.00 23.34           C  
ANISOU 3646  CG1 VAL D 533     2603   2886   3378    150    152    132       C  
ATOM   3647  CG2 VAL D 533      22.604 -29.459 -68.447  1.00 25.24           C  
ANISOU 3647  CG2 VAL D 533     3081   2907   3603   -146    494    -65       C  
ATOM   3648  N   VAL D 534      20.860 -30.025 -64.465  1.00 20.49           N  
ANISOU 3648  N   VAL D 534     2302   2769   2714     75    -60    202       N  
ATOM   3649  CA  VAL D 534      19.530 -30.056 -63.876  1.00 20.48           C  
ANISOU 3649  CA  VAL D 534     2423   2783   2575    111   -149    335       C  
ATOM   3650  C   VAL D 534      19.643 -29.290 -62.570  1.00 22.14           C  
ANISOU 3650  C   VAL D 534     2521   3196   2695     39   -210    234       C  
ATOM   3651  O   VAL D 534      20.466 -29.640 -61.724  1.00 25.34           O  
ANISOU 3651  O   VAL D 534     2737   3787   3104     45   -325    203       O  
ATOM   3652  CB  VAL D 534      19.020 -31.489 -63.616  1.00 24.34           C  
ANISOU 3652  CB  VAL D 534     2919   3302   3026    251   -317    546       C  
ATOM   3653  CG1 VAL D 534      17.700 -31.453 -62.840  1.00 23.08           C  
ANISOU 3653  CG1 VAL D 534     2852   3209   2709    263   -407    667       C  
ATOM   3654  CG2 VAL D 534      18.880 -32.271 -64.925  1.00 20.44           C  
ANISOU 3654  CG2 VAL D 534     2556   2596   2615    317   -256    639       C  
ATOM   3655  N   PRO D 535      18.841 -28.228 -62.402  1.00 19.99           N  
ANISOU 3655  N   PRO D 535     2364   2883   2350    -33   -137    175       N  
ATOM   3656  CA  PRO D 535      18.995 -27.431 -61.184  1.00 20.98           C  
ANISOU 3656  CA  PRO D 535     2392   3194   2386   -114   -174     46       C  
ATOM   3657  C   PRO D 535      18.583 -28.214 -59.951  1.00 22.29           C  
ANISOU 3657  C   PRO D 535     2480   3574   2416    -61   -353    159       C  
ATOM   3658  O   PRO D 535      17.499 -28.800 -59.912  1.00 20.51           O  
ANISOU 3658  O   PRO D 535     2351   3324   2116     12   -405    316       O  
ATOM   3659  CB  PRO D 535      18.066 -26.240 -61.425  1.00 22.35           C  
ANISOU 3659  CB  PRO D 535     2728   3230   2533   -175    -53    -30       C  
ATOM   3660  CG  PRO D 535      17.007 -26.783 -62.304  1.00 22.33           C  
ANISOU 3660  CG  PRO D 535     2894   3045   2547    -88    -37    144       C  
ATOM   3661  CD  PRO D 535      17.706 -27.766 -63.217  1.00 22.24           C  
ANISOU 3661  CD  PRO D 535     2865   2955   2629    -36    -40    229       C  
ATOM   3662  N   SER D 536      19.460 -28.233 -58.955  1.00 25.61           N  
ANISOU 3662  N   SER D 536     2725   4205   2799   -114   -455     87       N  
ATOM   3663  CA  SER D 536      19.202 -28.970 -57.730  1.00 25.50           C  
ANISOU 3663  CA  SER D 536     2635   4411   2642    -98   -645    196       C  
ATOM   3664  C   SER D 536      18.091 -28.313 -56.927  1.00 24.59           C  
ANISOU 3664  C   SER D 536     2607   4383   2355   -156   -617    160       C  
ATOM   3665  O   SER D 536      17.765 -27.144 -57.138  1.00 21.93           O  
ANISOU 3665  O   SER D 536     2348   3955   2027   -215   -465      8       O  
ATOM   3666  CB  SER D 536      20.471 -29.064 -56.883  1.00 26.11           C  
ANISOU 3666  CB  SER D 536     2507   4687   2727   -164   -771    125       C  
ATOM   3667  OG  SER D 536      20.848 -27.788 -56.395  1.00 28.14           O  
ANISOU 3667  OG  SER D 536     2732   5017   2942   -304   -686    -85       O  
ATOM   3668  N   TYR D 537      17.506 -29.079 -56.015  1.00 26.51           N  
ANISOU 3668  N   TYR D 537     2834   4795   2444   -143   -765    296       N  
ATOM   3669  CA  TYR D 537      16.578 -28.535 -55.036  1.00 27.03           C  
ANISOU 3669  CA  TYR D 537     2944   4998   2329   -216   -742    240       C  
ATOM   3670  C   TYR D 537      17.218 -27.360 -54.296  1.00 25.54           C  
ANISOU 3670  C   TYR D 537     2684   4933   2088   -355   -689      2       C  
ATOM   3671  O   TYR D 537      16.597 -26.314 -54.104  1.00 24.14           O  
ANISOU 3671  O   TYR D 537     2577   4732   1864   -407   -554   -150       O  
ATOM   3672  CB  TYR D 537      16.150 -29.626 -54.045  1.00 28.37           C  
ANISOU 3672  CB  TYR D 537     3154   5124   2503   -189   -806    361       C  
ATOM   3673  CG  TYR D 537      15.174 -29.158 -52.986  1.00 28.95           C  
ANISOU 3673  CG  TYR D 537     3261   5310   2429   -263   -752    304       C  
ATOM   3674  CD1 TYR D 537      15.617 -28.464 -51.866  1.00 30.63           C  
ANISOU 3674  CD1 TYR D 537     3398   5726   2513   -393   -765    168       C  
ATOM   3675  CD2 TYR D 537      13.814 -29.419 -53.096  1.00 30.58           C  
ANISOU 3675  CD2 TYR D 537     3568   5416   2636   -210   -684    373       C  
ATOM   3676  CE1 TYR D 537      14.739 -28.029 -50.896  1.00 32.76           C  
ANISOU 3676  CE1 TYR D 537     3692   6110   2645   -467   -703    101       C  
ATOM   3677  CE2 TYR D 537      12.921 -28.987 -52.122  1.00 31.69           C  
ANISOU 3677  CE2 TYR D 537     3709   5686   2645   -280   -631    312       C  
ATOM   3678  CZ  TYR D 537      13.392 -28.292 -51.026  1.00 31.70           C  
ANISOU 3678  CZ  TYR D 537     3635   5901   2507   -407   -636    174       C  
ATOM   3679  OH  TYR D 537      12.520 -27.858 -50.053  1.00 35.85           O  
ANISOU 3679  OH  TYR D 537     4159   6563   2898   -483   -570     95       O  
ATOM   3680  N   ASP D 538      18.467 -27.540 -53.885  1.00 28.01           N  
ANISOU 3680  N   ASP D 538     2853   5364   2424   -414   -799    -33       N  
ATOM   3681  CA  ASP D 538      19.158 -26.529 -53.096  1.00 28.87           C  
ANISOU 3681  CA  ASP D 538     2890   5607   2474   -565   -777   -243       C  
ATOM   3682  C   ASP D 538      19.446 -25.247 -53.872  1.00 26.33           C  
ANISOU 3682  C   ASP D 538     2621   5096   2285   -602   -579   -447       C  
ATOM   3683  O   ASP D 538      19.406 -24.155 -53.306  1.00 28.01           O  
ANISOU 3683  O   ASP D 538     2858   5360   2424   -715   -501   -639       O  
ATOM   3684  CB  ASP D 538      20.459 -27.102 -52.533  1.00 30.48           C  
ANISOU 3684  CB  ASP D 538     2940   5917   2725   -601   -935   -201       C  
ATOM   3685  CG  ASP D 538      20.209 -28.124 -51.442  1.00 36.96           C  
ANISOU 3685  CG  ASP D 538     3804   6745   3493   -568  -1044    -31       C  
ATOM   3686  OD1 ASP D 538      19.112 -28.080 -50.844  1.00 40.33           O  
ANISOU 3686  OD1 ASP D 538     4335   7194   3794   -583   -992     -8       O  
ATOM   3687  OD2 ASP D 538      21.106 -28.951 -51.165  1.00 40.48           O  
ANISOU 3687  OD2 ASP D 538     4177   7170   4034   -535  -1179     58       O  
ATOM   3688  N   LEU D 539      19.735 -25.375 -55.162  1.00 25.53           N  
ANISOU 3688  N   LEU D 539     2552   4777   2373   -521   -499   -407       N  
ATOM   3689  CA  LEU D 539      19.953 -24.196 -55.991  1.00 24.44           C  
ANISOU 3689  CA  LEU D 539     2488   4443   2355   -573   -320   -575       C  
ATOM   3690  C   LEU D 539      18.645 -23.427 -56.157  1.00 23.27           C  
ANISOU 3690  C   LEU D 539     2512   4159   2171   -555   -196   -626       C  
ATOM   3691  O   LEU D 539      18.617 -22.202 -56.024  1.00 24.00           O  
ANISOU 3691  O   LEU D 539     2656   4196   2268   -644    -94   -817       O  
ATOM   3692  CB  LEU D 539      20.529 -24.576 -57.356  1.00 24.39           C  
ANISOU 3692  CB  LEU D 539     2485   4245   2537   -510   -261   -513       C  
ATOM   3693  CG  LEU D 539      20.546 -23.429 -58.367  1.00 25.02           C  
ANISOU 3693  CG  LEU D 539     2686   4093   2727   -573    -78   -646       C  
ATOM   3694  CD1 LEU D 539      21.468 -22.304 -57.903  1.00 27.50           C  
ANISOU 3694  CD1 LEU D 539     2928   4479   3042   -735    -40   -863       C  
ATOM   3695  CD2 LEU D 539      20.934 -23.921 -59.749  1.00 21.91           C  
ANISOU 3695  CD2 LEU D 539     2323   3517   2486   -521    -10   -566       C  
ATOM   3696  N   LEU D 540      17.566 -24.152 -56.442  1.00 21.90           N  
ANISOU 3696  N   LEU D 540     2421   3927   1974   -438   -212   -455       N  
ATOM   3697  CA  LEU D 540      16.244 -23.543 -56.553  1.00 21.26           C  
ANISOU 3697  CA  LEU D 540     2477   3730   1872   -403   -113   -483       C  
ATOM   3698  C   LEU D 540      15.817 -22.874 -55.246  1.00 22.71           C  
ANISOU 3698  C   LEU D 540     2631   4099   1897   -483   -104   -638       C  
ATOM   3699  O   LEU D 540      15.264 -21.775 -55.258  1.00 23.08           O  
ANISOU 3699  O   LEU D 540     2758   4038   1975   -507     15   -797       O  
ATOM   3700  CB  LEU D 540      15.202 -24.583 -56.975  1.00 19.73           C  
ANISOU 3700  CB  LEU D 540     2351   3482   1665   -275   -158   -252       C  
ATOM   3701  CG  LEU D 540      15.377 -25.167 -58.379  1.00 18.27           C  
ANISOU 3701  CG  LEU D 540     2238   3074   1630   -196   -140   -109       C  
ATOM   3702  CD1 LEU D 540      14.378 -26.279 -58.637  1.00 16.97           C  
ANISOU 3702  CD1 LEU D 540     2137   2885   1427    -84   -211    126       C  
ATOM   3703  CD2 LEU D 540      15.220 -24.077 -59.414  1.00 17.85           C  
ANISOU 3703  CD2 LEU D 540     2313   2753   1716   -226      7   -211       C  
ATOM   3704  N   LEU D 541      16.081 -23.535 -54.124  1.00 23.70           N  
ANISOU 3704  N   LEU D 541     2649   4499   1856   -530   -233   -595       N  
ATOM   3705  CA  LEU D 541      15.750 -22.971 -52.819  1.00 25.33           C  
ANISOU 3705  CA  LEU D 541     2831   4914   1880   -633   -225   -748       C  
ATOM   3706  C   LEU D 541      16.544 -21.694 -52.548  1.00 26.80           C  
ANISOU 3706  C   LEU D 541     3005   5086   2094   -761   -150  -1007       C  
ATOM   3707  O   LEU D 541      15.989 -20.699 -52.081  1.00 27.75           O  
ANISOU 3707  O   LEU D 541     3180   5198   2165   -810    -43  -1199       O  
ATOM   3708  CB  LEU D 541      16.006 -23.984 -51.703  1.00 26.30           C  
ANISOU 3708  CB  LEU D 541     2851   5336   1807   -691   -405   -630       C  
ATOM   3709  CG  LEU D 541      15.773 -23.408 -50.302  1.00 28.76           C  
ANISOU 3709  CG  LEU D 541     3144   5847   1937   -821   -382   -782       C  
ATOM   3710  CD1 LEU D 541      14.305 -23.085 -50.102  1.00 28.11           C  
ANISOU 3710  CD1 LEU D 541     3142   5745   1795   -775   -256   -826       C  
ATOM   3711  CD2 LEU D 541      16.273 -24.344 -49.215  1.00 32.44           C  
ANISOU 3711  CD2 LEU D 541     3533   6453   2341   -866   -527   -619       C  
ATOM   3712  N   GLU D 542      17.840 -21.726 -52.850  1.00 27.15           N  
ANISOU 3712  N   GLU D 542     2970   5122   2222   -815   -204  -1017       N  
ATOM   3713  CA  GLU D 542      18.695 -20.561 -52.651  1.00 29.77           C  
ANISOU 3713  CA  GLU D 542     3286   5441   2584   -953   -147  -1245       C  
ATOM   3714  C   GLU D 542      18.177 -19.367 -53.444  1.00 28.17           C  
ANISOU 3714  C   GLU D 542     3226   4962   2516   -937     25  -1390       C  
ATOM   3715  O   GLU D 542      18.145 -18.245 -52.942  1.00 29.54           O  
ANISOU 3715  O   GLU D 542     3442   5127   2654  -1034     97  -1609       O  
ATOM   3716  CB  GLU D 542      20.142 -20.874 -53.047  1.00 38.74           C  
ANISOU 3716  CB  GLU D 542     4301   6594   3823   -999   -225  -1209       C  
ATOM   3717  CG  GLU D 542      21.057 -19.651 -53.108  1.00 35.58           C  
ANISOU 3717  CG  GLU D 542     3893   6140   3486  -1146   -154  -1428       C  
ATOM   3718  CD  GLU D 542      21.515 -19.195 -51.740  1.00 36.69           C  
ANISOU 3718  CD  GLU D 542     3966   6521   3453  -1307   -227  -1575       C  
ATOM   3719  OE1 GLU D 542      21.636 -20.052 -50.837  1.00 41.01           O  
ANISOU 3719  OE1 GLU D 542     4416   7308   3858  -1326   -379  -1472       O  
ATOM   3720  OE2 GLU D 542      21.747 -17.978 -51.552  1.00 36.58           O  
ANISOU 3720  OE2 GLU D 542     4007   6453   3437  -1429   -144  -1792       O  
ATOM   3721  N   MET D 543      17.751 -19.616 -54.678  1.00 26.42           N  
ANISOU 3721  N   MET D 543     3086   4505   2447   -822     79  -1263       N  
ATOM   3722  CA  MET D 543      17.269 -18.545 -55.540  1.00 26.06           C  
ANISOU 3722  CA  MET D 543     3184   4171   2545   -812    212  -1365       C  
ATOM   3723  C   MET D 543      15.881 -18.044 -55.138  1.00 26.21           C  
ANISOU 3723  C   MET D 543     3290   4141   2529   -749    282  -1436       C  
ATOM   3724  O   MET D 543      15.595 -16.853 -55.248  1.00 27.01           O  
ANISOU 3724  O   MET D 543     3479   4075   2708   -783    373  -1615       O  
ATOM   3725  CB  MET D 543      17.255 -19.003 -56.999  1.00 24.30           C  
ANISOU 3725  CB  MET D 543     3032   3718   2483   -730    237  -1195       C  
ATOM   3726  CG  MET D 543      18.542 -18.737 -57.768  1.00 24.57           C  
ANISOU 3726  CG  MET D 543     3040   3668   2626   -827    260  -1235       C  
ATOM   3727  SD  MET D 543      18.409 -19.167 -59.513  1.00 51.30           S  
ANISOU 3727  SD  MET D 543     6541   6773   6175   -759    317  -1063       S  
ATOM   3728  CE  MET D 543      18.188 -20.936 -59.394  1.00 21.52           C  
ANISOU 3728  CE  MET D 543     2679   3159   2340   -611    205   -817       C  
ATOM   3729  N   LEU D 544      15.016 -18.940 -54.674  1.00 25.64           N  
ANISOU 3729  N   LEU D 544     3185   4208   2348   -659    236  -1301       N  
ATOM   3730  CA  LEU D 544      13.671 -18.528 -54.276  1.00 25.96           C  
ANISOU 3730  CA  LEU D 544     3279   4226   2360   -595    312  -1372       C  
ATOM   3731  C   LEU D 544      13.660 -17.715 -52.984  1.00 28.17           C  
ANISOU 3731  C   LEU D 544     3522   4681   2500   -701    357  -1626       C  
ATOM   3732  O   LEU D 544      12.777 -16.886 -52.768  1.00 29.00           O  
ANISOU 3732  O   LEU D 544     3680   4699   2641   -670    462  -1785       O  
ATOM   3733  CB  LEU D 544      12.754 -19.743 -54.127  1.00 24.88           C  
ANISOU 3733  CB  LEU D 544     3112   4210   2131   -491    252  -1151       C  
ATOM   3734  CG  LEU D 544      12.171 -20.263 -55.443  1.00 22.85           C  
ANISOU 3734  CG  LEU D 544     2940   3713   2030   -362    251   -938       C  
ATOM   3735  CD1 LEU D 544      11.738 -21.713 -55.330  1.00 21.76           C  
ANISOU 3735  CD1 LEU D 544     2760   3722   1786   -291    146   -684       C  
ATOM   3736  CD2 LEU D 544      11.005 -19.388 -55.873  1.00 22.87           C  
ANISOU 3736  CD2 LEU D 544     3036   3490   2164   -289    357  -1016       C  
ATOM   3737  N   ASP D 545      14.650 -17.953 -52.133  1.00 29.27           N  
ANISOU 3737  N   ASP D 545     3570   5063   2489   -828    276  -1669       N  
ATOM   3738  CA  ASP D 545      14.722 -17.280 -50.846  1.00 31.52           C  
ANISOU 3738  CA  ASP D 545     3824   5526   2626   -946    303  -1876       C  
ATOM   3739  C   ASP D 545      15.746 -16.153 -50.893  1.00 32.78           C  
ANISOU 3739  C   ASP D 545     4004   5566   2884  -1054    331  -2039       C  
ATOM   3740  O   ASP D 545      16.153 -15.633 -49.857  1.00 35.61           O  
ANISOU 3740  O   ASP D 545     4327   6047   3157  -1159    326  -2145       O  
ATOM   3741  CB  ASP D 545      15.076 -18.287 -49.751  1.00 32.23           C  
ANISOU 3741  CB  ASP D 545     3803   5935   2509  -1016    172  -1746       C  
ATOM   3742  CG  ASP D 545      14.584 -17.861 -48.384  1.00 34.39           C  
ANISOU 3742  CG  ASP D 545     4057   6353   2655  -1084    219  -1849       C  
ATOM   3743  OD1 ASP D 545      13.736 -16.947 -48.312  1.00 35.12           O  
ANISOU 3743  OD1 ASP D 545     4209   6321   2813  -1042    354  -2006       O  
ATOM   3744  OD2 ASP D 545      15.028 -18.464 -47.389  1.00 35.48           O  
ANISOU 3744  OD2 ASP D 545     4121   6720   2641  -1178    117  -1766       O  
ATOM   3745  N   ALA D 546      16.148 -15.782 -52.108  1.00 33.01           N  
ANISOU 3745  N   ALA D 546     4099   5351   3093  -1038    360  -2044       N  
ATOM   3746  CA  ALA D 546      17.231 -14.821 -52.321  1.00 37.36           C  
ANISOU 3746  CA  ALA D 546     4666   5786   3744  -1150    372  -2152       C  
ATOM   3747  C   ALA D 546      16.795 -13.362 -52.166  1.00 40.82           C  
ANISOU 3747  C   ALA D 546     5201   6021   4287  -1148    469  -2311       C  
ATOM   3748  O   ALA D 546      17.639 -12.466 -52.138  1.00 41.84           O  
ANISOU 3748  O   ALA D 546     5350   6081   4469  -1249    473  -2402       O  
ATOM   3749  CB  ALA D 546      17.860 -15.034 -53.695  1.00 36.92           C  
ANISOU 3749  CB  ALA D 546     4640   5552   3836  -1152    365  -2072       C  
ATOM   3750  N   HIS D 547      15.492 -13.110 -52.080  1.00 42.53           N  
ANISOU 3750  N   HIS D 547     5474   6144   4540  -1031    539  -2341       N  
ATOM   3751  CA  HIS D 547      15.047 -11.812 -51.582  1.00 46.56           C  
ANISOU 3751  CA  HIS D 547     6045   6535   5112  -1029    610  -2508       C  
ATOM   3752  C   HIS D 547      14.664 -11.920 -50.114  1.00 49.29           C  
ANISOU 3752  C   HIS D 547     6319   7140   5269  -1066    628  -2600       C  
ATOM   3753  O   HIS D 547      14.912 -11.001 -49.333  1.00 52.49           O  
ANISOU 3753  O   HIS D 547     6739   7563   5644  -1145    658  -2754       O  
ATOM   3754  CB  HIS D 547      13.866 -11.249 -52.367  1.00 45.65           C  
ANISOU 3754  CB  HIS D 547     6028   6130   5186   -882    674  -2508       C  
ATOM   3755  CG  HIS D 547      13.543  -9.832 -51.999  1.00 48.99           C  
ANISOU 3755  CG  HIS D 547     6517   6398   5700   -876    726  -2677       C  
ATOM   3756  ND1 HIS D 547      12.929  -9.498 -50.810  1.00 50.05           N  
ANISOU 3756  ND1 HIS D 547     6610   6666   5739   -871    784  -2824       N  
ATOM   3757  CD2 HIS D 547      13.760  -8.663 -52.649  1.00 48.27           C  
ANISOU 3757  CD2 HIS D 547     6531   6033   5778   -880    720  -2718       C  
ATOM   3758  CE1 HIS D 547      12.781  -8.187 -50.744  1.00 50.93           C  
ANISOU 3758  CE1 HIS D 547     6799   6587   5966   -862    818  -2964       C  
ATOM   3759  NE2 HIS D 547      13.275  -7.657 -51.849  1.00 51.50           N  
ANISOU 3759  NE2 HIS D 547     6963   6408   6196   -866    770  -2896       N  
TER    3760      HIS D 547                                                      
ATOM   3761  N   SER C 309       6.984  13.364 -85.400  1.00 47.15           N  
ANISOU 3761  N   SER C 309     6187   6294   5436   1068  -1068    504       N  
ATOM   3762  CA  SER C 309       5.563  13.094 -85.424  1.00 47.84           C  
ANISOU 3762  CA  SER C 309     6070   6489   5620   1121  -1320    424       C  
ATOM   3763  C   SER C 309       4.902  13.306 -84.063  1.00 44.99           C  
ANISOU 3763  C   SER C 309     5453   6067   5575   1043  -1250    374       C  
ATOM   3764  O   SER C 309       3.805  13.845 -83.965  1.00 48.39           O  
ANISOU 3764  O   SER C 309     5729   6523   6134   1152  -1366    403       O  
ATOM   3765  CB  SER C 309       5.352  11.643 -85.866  1.00 48.13           C  
ANISOU 3765  CB  SER C 309     6069   6652   5566   1027  -1506    241       C  
ATOM   3766  OG  SER C 309       6.388  11.225 -86.731  1.00 48.34           O  
ANISOU 3766  OG  SER C 309     6346   6696   5324   1029  -1460    250       O  
ATOM   3767  N   LEU C 310       5.605  12.885 -83.019  1.00 39.83           N  
ANISOU 3767  N   LEU C 310     4765   5334   5036    865  -1054    302       N  
ATOM   3768  CA  LEU C 310       4.988  12.529 -81.750  1.00 37.89           C  
ANISOU 3768  CA  LEU C 310     4281   5069   5046    751  -1010    198       C  
ATOM   3769  C   LEU C 310       4.596  13.676 -80.831  1.00 36.01           C  
ANISOU 3769  C   LEU C 310     3947   4732   5005    814   -881    274       C  
ATOM   3770  O   LEU C 310       5.235  14.729 -80.803  1.00 37.23           O  
ANISOU 3770  O   LEU C 310     4238   4776   5133    881   -738    391       O  
ATOM   3771  CB  LEU C 310       5.933  11.602 -80.984  1.00 35.08           C  
ANISOU 3771  CB  LEU C 310     3951   4671   4708    555   -854     98       C  
ATOM   3772  CG  LEU C 310       6.378  10.310 -81.678  1.00 35.93           C  
ANISOU 3772  CG  LEU C 310     4141   4855   4657    468   -947     -4       C  
ATOM   3773  CD1 LEU C 310       7.194   9.434 -80.722  1.00 32.87           C  
ANISOU 3773  CD1 LEU C 310     3746   4412   4332    288   -785    -96       C  
ATOM   3774  CD2 LEU C 310       5.194   9.536 -82.243  1.00 37.76           C  
ANISOU 3774  CD2 LEU C 310     4231   5207   4910    480  -1208   -108       C  
ATOM   3775  N   THR C 311       3.543  13.438 -80.059  1.00 34.95           N  
ANISOU 3775  N   THR C 311     3570   4627   5081    787   -921    198       N  
ATOM   3776  CA  THR C 311       3.187  14.310 -78.952  1.00 34.08           C  
ANISOU 3776  CA  THR C 311     3355   4423   5173    820   -767    230       C  
ATOM   3777  C   THR C 311       4.095  13.977 -77.772  1.00 30.73           C  
ANISOU 3777  C   THR C 311     2969   3913   4795    658   -544    163       C  
ATOM   3778  O   THR C 311       4.760  12.938 -77.774  1.00 27.89           O  
ANISOU 3778  O   THR C 311     2664   3584   4350    522   -533     86       O  
ATOM   3779  CB  THR C 311       1.720  14.142 -78.536  1.00 33.01           C  
ANISOU 3779  CB  THR C 311     2936   4355   5251    856   -867    175       C  
ATOM   3780  OG1 THR C 311       1.532  12.853 -77.938  1.00 32.11           O  
ANISOU 3780  OG1 THR C 311     2686   4291   5223    680   -858     38       O  
ATOM   3781  CG2 THR C 311       0.797  14.277 -79.745  1.00 37.47           C  
ANISOU 3781  CG2 THR C 311     3438   5031   5768   1009  -1138    214       C  
ATOM   3782  N   ALA C 312       4.118  14.850 -76.767  1.00 28.90           N  
ANISOU 3782  N   ALA C 312     2714   3573   4692    685   -375    186       N  
ATOM   3783  CA  ALA C 312       4.923  14.620 -75.568  1.00 26.75           C  
ANISOU 3783  CA  ALA C 312     2478   3227   4458    554   -182    116       C  
ATOM   3784  C   ALA C 312       4.531  13.311 -74.891  1.00 26.04           C  
ANISOU 3784  C   ALA C 312     2246   3213   4435    422   -184      0       C  
ATOM   3785  O   ALA C 312       5.384  12.487 -74.579  1.00 24.51           O  
ANISOU 3785  O   ALA C 312     2129   3018   4168    293   -123    -60       O  
ATOM   3786  CB  ALA C 312       4.782  15.782 -74.595  1.00 26.91           C  
ANISOU 3786  CB  ALA C 312     2481   3130   4613    626    -28    138       C  
ATOM   3787  N   ASP C 313       3.232  13.122 -74.679  1.00 27.36           N  
ANISOU 3787  N   ASP C 313     2200   3439   4754    457   -248    -25       N  
ATOM   3788  CA  ASP C 313       2.729  11.887 -74.087  1.00 27.13           C  
ANISOU 3788  CA  ASP C 313     2018   3469   4820    331   -239   -121       C  
ATOM   3789  C   ASP C 313       3.138  10.658 -74.897  1.00 26.74           C  
ANISOU 3789  C   ASP C 313     2022   3486   4651    221   -369   -177       C  
ATOM   3790  O   ASP C 313       3.517   9.628 -74.335  1.00 25.63           O  
ANISOU 3790  O   ASP C 313     1885   3340   4511     85   -296   -247       O  
ATOM   3791  CB  ASP C 313       1.210  11.933 -73.958  1.00 30.82           C  
ANISOU 3791  CB  ASP C 313     2223   3992   5494    394   -305   -130       C  
ATOM   3792  CG  ASP C 313       0.751  12.702 -72.735  1.00 32.54           C  
ANISOU 3792  CG  ASP C 313     2355   4144   5864    457   -113   -116       C  
ATOM   3793  OD1 ASP C 313       1.606  13.119 -71.923  1.00 31.51           O  
ANISOU 3793  OD1 ASP C 313     2374   3926   5672    439     61   -116       O  
ATOM   3794  OD2 ASP C 313      -0.475  12.871 -72.578  1.00 34.54           O  
ANISOU 3794  OD2 ASP C 313     2386   4435   6304    526   -137   -113       O  
ATOM   3795  N   GLN C 314       3.060  10.771 -76.219  1.00 27.84           N  
ANISOU 3795  N   GLN C 314     2216   3685   4677    294   -560   -146       N  
ATOM   3796  CA  GLN C 314       3.461   9.678 -77.097  1.00 28.62           C  
ANISOU 3796  CA  GLN C 314     2391   3845   4638    211   -692   -210       C  
ATOM   3797  C   GLN C 314       4.966   9.419 -77.054  1.00 25.79           C  
ANISOU 3797  C   GLN C 314     2258   3431   4111    136   -570   -207       C  
ATOM   3798  O   GLN C 314       5.397   8.277 -77.199  1.00 25.16           O  
ANISOU 3798  O   GLN C 314     2218   3372   3971     24   -592   -286       O  
ATOM   3799  CB  GLN C 314       3.023   9.956 -78.538  1.00 35.10           C  
ANISOU 3799  CB  GLN C 314     3243   4750   5345    336   -930   -176       C  
ATOM   3800  CG  GLN C 314       1.522   9.840 -78.767  1.00 38.24           C  
ANISOU 3800  CG  GLN C 314     3388   5233   5910    388  -1117   -217       C  
ATOM   3801  CD  GLN C 314       1.085  10.414 -80.102  1.00 37.54           C  
ANISOU 3801  CD  GLN C 314     3344   5226   5694    561  -1354   -160       C  
ATOM   3802  OE1 GLN C 314       1.876  11.032 -80.817  1.00 34.05           O  
ANISOU 3802  OE1 GLN C 314     3134   4765   5037    655  -1346    -65       O  
ATOM   3803  NE2 GLN C 314      -0.182  10.208 -80.447  1.00 38.76           N  
ANISOU 3803  NE2 GLN C 314     3271   5472   5982    608  -1565   -214       N  
ATOM   3804  N   MET C 315       5.761  10.472 -76.866  1.00 25.02           N  
ANISOU 3804  N   MET C 315     2297   3255   3955    198   -442   -121       N  
ATOM   3805  CA  MET C 315       7.211  10.322 -76.773  1.00 23.37           C  
ANISOU 3805  CA  MET C 315     2271   2989   3619    129   -319   -119       C  
ATOM   3806  C   MET C 315       7.564   9.543 -75.508  1.00 21.83           C  
ANISOU 3806  C   MET C 315     2029   2762   3504     -2   -186   -201       C  
ATOM   3807  O   MET C 315       8.376   8.619 -75.546  1.00 20.84           O  
ANISOU 3807  O   MET C 315     1983   2640   3295    -95   -163   -252       O  
ATOM   3808  CB  MET C 315       7.906  11.688 -76.784  1.00 23.23           C  
ANISOU 3808  CB  MET C 315     2378   2877   3570    214   -208    -16       C  
ATOM   3809  CG  MET C 315       9.408  11.637 -76.514  1.00 21.69           C  
ANISOU 3809  CG  MET C 315     2330   2612   3297    134    -64    -22       C  
ATOM   3810  SD  MET C 315      10.366  10.775 -77.779  1.00 27.85           S  
ANISOU 3810  SD  MET C 315     3269   3447   3865     99   -121    -23       S  
ATOM   3811  CE  MET C 315      10.402  12.028 -79.057  1.00 28.05           C  
ANISOU 3811  CE  MET C 315     3429   3450   3779    258   -152    131       C  
ATOM   3812  N   VAL C 316       6.929   9.910 -74.397  1.00 23.02           N  
ANISOU 3812  N   VAL C 316     2058   2881   3807      7    -95   -210       N  
ATOM   3813  CA  VAL C 316       7.139   9.235 -73.118  1.00 22.22           C  
ANISOU 3813  CA  VAL C 316     1921   2754   3769    -92     39   -273       C  
ATOM   3814  C   VAL C 316       6.731   7.770 -73.189  1.00 24.52           C  
ANISOU 3814  C   VAL C 316     2129   3097   4090   -197    -22   -343       C  
ATOM   3815  O   VAL C 316       7.468   6.893 -72.738  1.00 20.76           O  
ANISOU 3815  O   VAL C 316     1720   2602   3567   -289     47   -385       O  
ATOM   3816  CB  VAL C 316       6.353   9.917 -71.976  1.00 22.47           C  
ANISOU 3816  CB  VAL C 316     1837   2751   3949    -40    151   -266       C  
ATOM   3817  CG1 VAL C 316       6.435   9.095 -70.693  1.00 23.00           C  
ANISOU 3817  CG1 VAL C 316     1874   2806   4059   -128    287   -323       C  
ATOM   3818  CG2 VAL C 316       6.878  11.309 -71.736  1.00 21.58           C  
ANISOU 3818  CG2 VAL C 316     1822   2558   3820     48    231   -220       C  
ATOM   3819  N   SER C 317       5.555   7.516 -73.756  1.00 23.42           N  
ANISOU 3819  N   SER C 317     1840   3018   4043   -181   -156   -357       N  
ATOM   3820  CA  SER C 317       5.053   6.154 -73.911  1.00 24.38           C  
ANISOU 3820  CA  SER C 317     1862   3173   4229   -290   -229   -436       C  
ATOM   3821  C   SER C 317       6.022   5.304 -74.720  1.00 24.42           C  
ANISOU 3821  C   SER C 317     2025   3185   4069   -352   -299   -480       C  
ATOM   3822  O   SER C 317       6.313   4.167 -74.356  1.00 21.83           O  
ANISOU 3822  O   SER C 317     1708   2830   3756   -461   -253   -538       O  
ATOM   3823  CB  SER C 317       3.672   6.157 -74.570  1.00 29.24           C  
ANISOU 3823  CB  SER C 317     2280   3855   4974   -253   -401   -457       C  
ATOM   3824  OG  SER C 317       2.697   6.643 -73.670  1.00 34.99           O  
ANISOU 3824  OG  SER C 317     2824   4573   5896   -217   -306   -431       O  
ATOM   3825  N   ALA C 318       6.537   5.874 -75.805  1.00 22.72           N  
ANISOU 3825  N   ALA C 318     1941   2997   3694   -272   -394   -444       N  
ATOM   3826  CA  ALA C 318       7.491   5.175 -76.657  1.00 22.53           C  
ANISOU 3826  CA  ALA C 318     2082   2983   3496   -307   -446   -481       C  
ATOM   3827  C   ALA C 318       8.768   4.808 -75.899  1.00 21.77           C  
ANISOU 3827  C   ALA C 318     2103   2821   3346   -375   -274   -484       C  
ATOM   3828  O   ALA C 318       9.278   3.694 -76.028  1.00 24.26           O  
ANISOU 3828  O   ALA C 318     2476   3126   3614   -454   -275   -549       O  
ATOM   3829  CB  ALA C 318       7.824   6.018 -77.869  1.00 22.78           C  
ANISOU 3829  CB  ALA C 318     2245   3051   3358   -188   -536   -416       C  
ATOM   3830  N   LEU C 319       9.278   5.745 -75.107  1.00 20.20           N  
ANISOU 3830  N   LEU C 319     1937   2574   3162   -337   -136   -422       N  
ATOM   3831  CA  LEU C 319      10.507   5.516 -74.358  1.00 19.44           C  
ANISOU 3831  CA  LEU C 319     1940   2425   3021   -387      4   -430       C  
ATOM   3832  C   LEU C 319      10.318   4.508 -73.229  1.00 19.10           C  
ANISOU 3832  C   LEU C 319     1830   2359   3069   -473     82   -481       C  
ATOM   3833  O   LEU C 319      11.180   3.660 -72.998  1.00 23.25           O  
ANISOU 3833  O   LEU C 319     2433   2861   3539   -530    131   -514       O  
ATOM   3834  CB  LEU C 319      11.043   6.833 -73.802  1.00 18.12           C  
ANISOU 3834  CB  LEU C 319     1816   2208   2861   -326    110   -370       C  
ATOM   3835  CG  LEU C 319      11.506   7.807 -74.886  1.00 20.75           C  
ANISOU 3835  CG  LEU C 319     2249   2534   3101   -247     76   -299       C  
ATOM   3836  CD1 LEU C 319      12.074   9.072 -74.267  1.00 18.38           C  
ANISOU 3836  CD1 LEU C 319     1985   2155   2844   -207    192   -252       C  
ATOM   3837  CD2 LEU C 319      12.530   7.143 -75.789  1.00 18.33           C  
ANISOU 3837  CD2 LEU C 319     2070   2244   2652   -275     61   -310       C  
ATOM   3838  N   LEU C 320       9.192   4.604 -72.528  1.00 20.45           N  
ANISOU 3838  N   LEU C 320     1857   2533   3380   -474    107   -479       N  
ATOM   3839  CA  LEU C 320       8.885   3.657 -71.462  1.00 24.79           C  
ANISOU 3839  CA  LEU C 320     2344   3055   4021   -549    203   -507       C  
ATOM   3840  C   LEU C 320       8.740   2.252 -72.031  1.00 23.81           C  
ANISOU 3840  C   LEU C 320     2207   2929   3912   -642    127   -567       C  
ATOM   3841  O   LEU C 320       9.177   1.282 -71.416  1.00 24.16           O  
ANISOU 3841  O   LEU C 320     2294   2928   3958   -706    210   -586       O  
ATOM   3842  CB  LEU C 320       7.609   4.059 -70.713  1.00 23.42           C  
ANISOU 3842  CB  LEU C 320     2004   2885   4008   -526    260   -486       C  
ATOM   3843  CG  LEU C 320       7.680   5.333 -69.870  1.00 23.92           C  
ANISOU 3843  CG  LEU C 320     2084   2931   4075   -436    368   -444       C  
ATOM   3844  CD1 LEU C 320       6.299   5.710 -69.347  1.00 26.75           C  
ANISOU 3844  CD1 LEU C 320     2264   3300   4599   -398    416   -426       C  
ATOM   3845  CD2 LEU C 320       8.660   5.160 -68.720  1.00 20.86           C  
ANISOU 3845  CD2 LEU C 320     1814   2503   3609   -449    506   -451       C  
ATOM   3846  N   ASP C 321       8.133   2.154 -73.211  1.00 24.33           N  
ANISOU 3846  N   ASP C 321     2221   3039   3984   -640    -37   -601       N  
ATOM   3847  CA  ASP C 321       7.957   0.864 -73.875  1.00 24.65           C  
ANISOU 3847  CA  ASP C 321     2254   3071   4040   -727   -136   -685       C  
ATOM   3848  C   ASP C 321       9.289   0.270 -74.326  1.00 22.07           C  
ANISOU 3848  C   ASP C 321     2115   2722   3549   -741   -126   -712       C  
ATOM   3849  O   ASP C 321       9.419  -0.947 -74.447  1.00 28.09           O  
ANISOU 3849  O   ASP C 321     2902   3441   4330   -820   -138   -779       O  
ATOM   3850  CB  ASP C 321       7.024   0.986 -75.089  1.00 24.33           C  
ANISOU 3850  CB  ASP C 321     2127   3098   4022   -703   -346   -732       C  
ATOM   3851  CG  ASP C 321       5.570   1.225 -74.701  1.00 34.24           C  
ANISOU 3851  CG  ASP C 321     3147   4372   5491   -711   -374   -730       C  
ATOM   3852  OD1 ASP C 321       5.251   1.211 -73.489  1.00 37.49           O  
ANISOU 3852  OD1 ASP C 321     3471   4740   6035   -742   -209   -691       O  
ATOM   3853  OD2 ASP C 321       4.732   1.406 -75.615  1.00 36.79           O  
ANISOU 3853  OD2 ASP C 321     3371   4758   5848   -679   -563   -769       O  
ATOM   3854  N   ALA C 322      10.271   1.129 -74.578  1.00 20.91           N  
ANISOU 3854  N   ALA C 322     2093   2593   3258   -663    -95   -661       N  
ATOM   3855  CA  ALA C 322      11.542   0.692 -75.152  1.00 20.34           C  
ANISOU 3855  CA  ALA C 322     2184   2508   3034   -660    -83   -682       C  
ATOM   3856  C   ALA C 322      12.530   0.232 -74.090  1.00 21.62           C  
ANISOU 3856  C   ALA C 322     2403   2613   3197   -691     66   -671       C  
ATOM   3857  O   ALA C 322      13.605  -0.269 -74.419  1.00 22.29           O  
ANISOU 3857  O   ALA C 322     2602   2681   3186   -691     91   -692       O  
ATOM   3858  CB  ALA C 322      12.160   1.809 -75.985  1.00 22.07           C  
ANISOU 3858  CB  ALA C 322     2502   2767   3117   -566   -104   -625       C  
ATOM   3859  N   GLU C 323      12.165   0.398 -72.823  1.00 19.58           N  
ANISOU 3859  N   GLU C 323     2069   2329   3040   -704    163   -638       N  
ATOM   3860  CA  GLU C 323      13.086   0.128 -71.720  1.00 18.83           C  
ANISOU 3860  CA  GLU C 323     2036   2193   2924   -706    290   -619       C  
ATOM   3861  C   GLU C 323      13.631  -1.291 -71.761  1.00 16.98           C  
ANISOU 3861  C   GLU C 323     1868   1911   2672   -758    305   -661       C  
ATOM   3862  O   GLU C 323      12.872  -2.245 -71.919  1.00 17.91           O  
ANISOU 3862  O   GLU C 323     1938   1996   2873   -824    274   -699       O  
ATOM   3863  CB  GLU C 323      12.404   0.382 -70.376  1.00 17.97           C  
ANISOU 3863  CB  GLU C 323     1847   2070   2912   -703    389   -583       C  
ATOM   3864  CG  GLU C 323      12.502   1.816 -69.901  1.00 20.26           C  
ANISOU 3864  CG  GLU C 323     2130   2382   3187   -630    427   -545       C  
ATOM   3865  CD  GLU C 323      13.935   2.244 -69.641  1.00 21.75           C  
ANISOU 3865  CD  GLU C 323     2427   2562   3275   -594    464   -546       C  
ATOM   3866  OE1 GLU C 323      14.576   2.792 -70.563  1.00 19.52           O  
ANISOU 3866  OE1 GLU C 323     2192   2291   2934   -573    415   -543       O  
ATOM   3867  OE2 GLU C 323      14.423   2.026 -68.511  1.00 22.77           O  
ANISOU 3867  OE2 GLU C 323     2592   2673   3385   -583    543   -547       O  
ATOM   3868  N   PRO C 324      14.960  -1.427 -71.633  1.00 15.50           N  
ANISOU 3868  N   PRO C 324     1785   1712   2393   -727    352   -659       N  
ATOM   3869  CA  PRO C 324      15.583  -2.748 -71.585  1.00 17.55           C  
ANISOU 3869  CA  PRO C 324     2115   1917   2636   -755    379   -692       C  
ATOM   3870  C   PRO C 324      15.350  -3.387 -70.223  1.00 15.64           C  
ANISOU 3870  C   PRO C 324     1857   1627   2457   -762    474   -650       C  
ATOM   3871  O   PRO C 324      15.047  -2.683 -69.257  1.00 15.68           O  
ANISOU 3871  O   PRO C 324     1820   1647   2489   -744    536   -611       O  
ATOM   3872  CB  PRO C 324      17.062  -2.440 -71.818  1.00 19.69           C  
ANISOU 3872  CB  PRO C 324     2474   2205   2802   -697    403   -689       C  
ATOM   3873  CG  PRO C 324      17.237  -1.119 -71.162  1.00 20.17           C  
ANISOU 3873  CG  PRO C 324     2499   2302   2862   -655    437   -644       C  
ATOM   3874  CD  PRO C 324      15.948  -0.355 -71.419  1.00 17.05           C  
ANISOU 3874  CD  PRO C 324     2023   1935   2522   -665    390   -627       C  
ATOM   3875  N   PRO C 325      15.473  -4.715 -70.145  1.00 16.12           N  
ANISOU 3875  N   PRO C 325     1963   1626   2536   -780    493   -656       N  
ATOM   3876  CA  PRO C 325      15.285  -5.399 -68.867  1.00 18.16           C  
ANISOU 3876  CA  PRO C 325     2229   1823   2847   -785    602   -606       C  
ATOM   3877  C   PRO C 325      16.461  -5.202 -67.930  1.00 18.67           C  
ANISOU 3877  C   PRO C 325     2374   1886   2831   -725    675   -580       C  
ATOM   3878  O   PRO C 325      17.552  -4.843 -68.371  1.00 16.58           O  
ANISOU 3878  O   PRO C 325     2154   1660   2484   -678    631   -606       O  
ATOM   3879  CB  PRO C 325      15.172  -6.863 -69.273  1.00 18.76           C  
ANISOU 3879  CB  PRO C 325     2341   1819   2968   -820    590   -625       C  
ATOM   3880  CG  PRO C 325      15.970  -6.959 -70.524  1.00 17.69           C  
ANISOU 3880  CG  PRO C 325     2265   1706   2751   -802    500   -690       C  
ATOM   3881  CD  PRO C 325      15.753  -5.655 -71.243  1.00 20.27           C  
ANISOU 3881  CD  PRO C 325     2544   2122   3036   -795    425   -711       C  
ATOM   3882  N   ILE C 326      16.233  -5.440 -66.645  1.00 15.50           N  
ANISOU 3882  N   ILE C 326     1990   1460   2440   -698    773   -516       N  
ATOM   3883  CA  ILE C 326      17.316  -5.491 -65.682  1.00 15.22           C  
ANISOU 3883  CA  ILE C 326     2044   1437   2302   -604    811   -482       C  
ATOM   3884  C   ILE C 326      17.899  -6.901 -65.692  1.00 15.76           C  
ANISOU 3884  C   ILE C 326     2198   1418   2372   -595    839   -468       C  
ATOM   3885  O   ILE C 326      17.191  -7.874 -65.428  1.00 20.23           O  
ANISOU 3885  O   ILE C 326     2777   1892   3019   -641    914   -429       O  
ATOM   3886  CB  ILE C 326      16.829  -5.109 -64.273  1.00 19.41           C  
ANISOU 3886  CB  ILE C 326     2583   1986   2804   -554    904   -418       C  
ATOM   3887  CG1 ILE C 326      16.387  -3.643 -64.252  1.00 23.19           C  
ANISOU 3887  CG1 ILE C 326     2987   2542   3280   -546    876   -443       C  
ATOM   3888  CG2 ILE C 326      17.919  -5.352 -63.244  1.00 21.79           C  
ANISOU 3888  CG2 ILE C 326     2994   2301   2985   -444    923   -387       C  
ATOM   3889  CD1 ILE C 326      15.574  -3.262 -63.033  1.00 26.91           C  
ANISOU 3889  CD1 ILE C 326     3453   3026   3745   -507    984   -392       C  
ATOM   3890  N   LEU C 327      19.178  -7.018 -66.035  1.00 14.62           N  
ANISOU 3890  N   LEU C 327     2105   1292   2159   -537    787   -501       N  
ATOM   3891  CA  LEU C 327      19.827  -8.322 -66.117  1.00 15.22           C  
ANISOU 3891  CA  LEU C 327     2263   1280   2238   -509    810   -493       C  
ATOM   3892  C   LEU C 327      20.467  -8.740 -64.799  1.00 17.23           C  
ANISOU 3892  C   LEU C 327     2600   1524   2423   -399    863   -417       C  
ATOM   3893  O   LEU C 327      20.698  -7.917 -63.909  1.00 15.47           O  
ANISOU 3893  O   LEU C 327     2375   1382   2121   -333    854   -395       O  
ATOM   3894  CB  LEU C 327      20.885  -8.328 -67.223  1.00 14.77           C  
ANISOU 3894  CB  LEU C 327     2214   1245   2151   -489    741   -565       C  
ATOM   3895  CG  LEU C 327      20.396  -7.921 -68.613  1.00 14.51           C  
ANISOU 3895  CG  LEU C 327     2133   1235   2145   -570    681   -638       C  
ATOM   3896  CD1 LEU C 327      21.485  -8.149 -69.645  1.00 14.44           C  
ANISOU 3896  CD1 LEU C 327     2162   1233   2092   -534    651   -698       C  
ATOM   3897  CD2 LEU C 327      19.134  -8.689 -68.983  1.00 15.37           C  
ANISOU 3897  CD2 LEU C 327     2228   1261   2351   -668    688   -655       C  
ATOM   3898  N   TYR C 328      20.757 -10.030 -64.686  1.00 17.92           N  
ANISOU 3898  N   TYR C 328     2769   1505   2533   -371    910   -381       N  
ATOM   3899  CA  TYR C 328      21.409 -10.560 -63.497  1.00 17.35           C  
ANISOU 3899  CA  TYR C 328     2795   1416   2383   -244    952   -296       C  
ATOM   3900  C   TYR C 328      22.878 -10.864 -63.741  1.00 17.30           C  
ANISOU 3900  C   TYR C 328     2818   1428   2329   -141    883   -329       C  
ATOM   3901  O   TYR C 328      23.288 -11.139 -64.870  1.00 17.03           O  
ANISOU 3901  O   TYR C 328     2759   1367   2345   -176    850   -401       O  
ATOM   3902  CB  TYR C 328      20.705 -11.826 -63.016  1.00 18.76           C  
ANISOU 3902  CB  TYR C 328     3055   1443   2628   -262   1077   -203       C  
ATOM   3903  CG  TYR C 328      19.396 -11.557 -62.318  1.00 19.26           C  
ANISOU 3903  CG  TYR C 328     3095   1496   2728   -322   1180   -135       C  
ATOM   3904  CD1 TYR C 328      18.272 -11.173 -63.034  1.00 26.93           C  
ANISOU 3904  CD1 TYR C 328     3952   2463   3819   -465   1181   -188       C  
ATOM   3905  CD2 TYR C 328      19.292 -11.666 -60.939  1.00 20.99           C  
ANISOU 3905  CD2 TYR C 328     3404   1715   2855   -224   1277    -18       C  
ATOM   3906  CE1 TYR C 328      17.075 -10.920 -62.398  1.00 30.58           C  
ANISOU 3906  CE1 TYR C 328     4368   2916   4336   -515   1287   -127       C  
ATOM   3907  CE2 TYR C 328      18.102 -11.418 -60.294  1.00 23.88           C  
ANISOU 3907  CE2 TYR C 328     3748   2072   3255   -270   1399     49       C  
ATOM   3908  CZ  TYR C 328      16.996 -11.043 -61.029  1.00 27.93           C  
ANISOU 3908  CZ  TYR C 328     4123   2575   3915   -420   1408     -7       C  
ATOM   3909  OH  TYR C 328      15.802 -10.791 -60.398  1.00 36.56           O  
ANISOU 3909  OH  TYR C 328     5169   3658   5063   -462   1540     59       O  
ATOM   3910  N   SER C 329      23.665 -10.811 -62.672  1.00 18.19           N  
ANISOU 3910  N   SER C 329     2981   1591   2341     -4    861   -279       N  
ATOM   3911  CA  SER C 329      25.042 -11.272 -62.720  1.00 18.75           C  
ANISOU 3911  CA  SER C 329     3071   1669   2383    115    800   -294       C  
ATOM   3912  C   SER C 329      25.064 -12.781 -62.949  1.00 19.25           C  
ANISOU 3912  C   SER C 329     3230   1576   2508    138    876   -243       C  
ATOM   3913  O   SER C 329      24.193 -13.495 -62.452  1.00 20.12           O  
ANISOU 3913  O   SER C 329     3423   1579   2644    114    978   -155       O  
ATOM   3914  CB  SER C 329      25.776 -10.918 -61.429  1.00 21.89           C  
ANISOU 3914  CB  SER C 329     3503   2159   2655    266    738   -255       C  
ATOM   3915  OG  SER C 329      27.158 -11.199 -61.549  1.00 23.83           O  
ANISOU 3915  OG  SER C 329     3724   2434   2896    379    655   -287       O  
ATOM   3916  N   GLU C 330      26.041 -13.253 -63.720  1.00 19.36           N  
ANISOU 3916  N   GLU C 330     3230   1566   2560    184    841   -298       N  
ATOM   3917  CA  GLU C 330      26.215 -14.682 -63.960  1.00 22.55           C  
ANISOU 3917  CA  GLU C 330     3731   1810   3027    225    908   -263       C  
ATOM   3918  C   GLU C 330      27.173 -15.292 -62.961  1.00 25.74           C  
ANISOU 3918  C   GLU C 330     4210   2203   3365    418    893   -174       C  
ATOM   3919  O   GLU C 330      28.373 -15.350 -63.221  1.00 26.66           O  
ANISOU 3919  O   GLU C 330     4283   2365   3480    523    827   -217       O  
ATOM   3920  CB  GLU C 330      26.752 -14.964 -65.367  1.00 26.83           C  
ANISOU 3920  CB  GLU C 330     4234   2319   3641    191    892   -375       C  
ATOM   3921  CG  GLU C 330      25.711 -15.348 -66.397  1.00 29.90           C  
ANISOU 3921  CG  GLU C 330     4638   2605   4117     33    939   -439       C  
ATOM   3922  CD  GLU C 330      26.333 -15.723 -67.735  1.00 28.09           C  
ANISOU 3922  CD  GLU C 330     4407   2342   3922     32    928   -552       C  
ATOM   3923  OE1 GLU C 330      26.305 -16.923 -68.083  1.00 37.98           O  
ANISOU 3923  OE1 GLU C 330     5751   3435   5244     41    983   -569       O  
ATOM   3924  OE2 GLU C 330      26.846 -14.837 -68.441  1.00 33.72           O  
ANISOU 3924  OE2 GLU C 330     5037   3178   4596     25    878   -624       O  
ATOM   3925  N   TYR C 331      26.658 -15.744 -61.824  1.00 26.48           N  
ANISOU 3925  N   TYR C 331     4415   2241   3405    476    958    -46       N  
ATOM   3926  CA  TYR C 331      27.461 -16.536 -60.900  1.00 30.86           C  
ANISOU 3926  CA  TYR C 331     5077   2758   3889    676    953     61       C  
ATOM   3927  C   TYR C 331      26.559 -17.496 -60.141  1.00 29.46           C  
ANISOU 3927  C   TYR C 331     5057   2419   3716    685   1102    214       C  
ATOM   3928  O   TYR C 331      25.377 -17.220 -59.953  1.00 31.88           O  
ANISOU 3928  O   TYR C 331     5368   2703   4042    558   1189    244       O  
ATOM   3929  CB  TYR C 331      28.230 -15.642 -59.918  1.00 28.22           C  
ANISOU 3929  CB  TYR C 331     4709   2610   3404    815    822     65       C  
ATOM   3930  CG  TYR C 331      27.359 -14.898 -58.922  1.00 29.91           C  
ANISOU 3930  CG  TYR C 331     4964   2899   3501    792    845    120       C  
ATOM   3931  CD1 TYR C 331      26.978 -15.492 -57.722  1.00 29.77           C  
ANISOU 3931  CD1 TYR C 331     5111   2827   3373    906    927    275       C  
ATOM   3932  CD2 TYR C 331      26.914 -13.608 -59.180  1.00 28.67           C  
ANISOU 3932  CD2 TYR C 331     4693   2861   3341    668    801     22       C  
ATOM   3933  CE1 TYR C 331      26.181 -14.824 -56.808  1.00 31.50           C  
ANISOU 3933  CE1 TYR C 331     5379   3117   3473    898    970    324       C  
ATOM   3934  CE2 TYR C 331      26.114 -12.929 -58.269  1.00 24.81           C  
ANISOU 3934  CE2 TYR C 331     4245   2435   2748    658    833     64       C  
ATOM   3935  CZ  TYR C 331      25.752 -13.544 -57.083  1.00 30.09           C  
ANISOU 3935  CZ  TYR C 331     5077   3056   3299    774    921    211       C  
ATOM   3936  OH  TYR C 331      24.957 -12.890 -56.165  1.00 32.03           O  
ANISOU 3936  OH  TYR C 331     5375   3365   3428    779    976    254       O  
ATOM   3937  N   ASP C 332      27.117 -18.615 -59.694  1.00 33.34           N  
ANISOU 3937  N   ASP C 332     5675   2793   4200    839   1142    318       N  
ATOM   3938  CA  ASP C 332      26.360 -19.566 -58.889  1.00 35.69           C  
ANISOU 3938  CA  ASP C 332     6140   2920   4502    868   1304    491       C  
ATOM   3939  C   ASP C 332      26.253 -19.068 -57.451  1.00 32.72           C  
ANISOU 3939  C   ASP C 332     5848   2660   3923    998   1301    615       C  
ATOM   3940  O   ASP C 332      27.257 -18.979 -56.744  1.00 32.00           O  
ANISOU 3940  O   ASP C 332     5801   2674   3685   1205   1187    651       O  
ATOM   3941  CB  ASP C 332      27.008 -20.951 -58.932  1.00 46.01           C  
ANISOU 3941  CB  ASP C 332     7567   4040   5873   1002   1356    570       C  
ATOM   3942  N   PRO C 333      25.027 -18.741 -57.012  1.00 34.07           N  
ANISOU 3942  N   PRO C 333     6042   2817   4085    886   1424    673       N  
ATOM   3943  CA  PRO C 333      24.835 -18.148 -55.684  1.00 32.77           C  
ANISOU 3943  CA  PRO C 333     5965   2777   3711   1004   1434    773       C  
ATOM   3944  C   PRO C 333      25.038 -19.142 -54.544  1.00 35.53           C  
ANISOU 3944  C   PRO C 333     6537   3027   3936   1212   1534    985       C  
ATOM   3945  O   PRO C 333      25.055 -18.732 -53.386  1.00 38.66           O  
ANISOU 3945  O   PRO C 333     7040   3536   4114   1357   1526   1072       O  
ATOM   3946  CB  PRO C 333      23.386 -17.653 -55.732  1.00 34.70           C  
ANISOU 3946  CB  PRO C 333     6155   3001   4028    809   1574    773       C  
ATOM   3947  CG  PRO C 333      22.716 -18.570 -56.692  1.00 31.64           C  
ANISOU 3947  CG  PRO C 333     5733   2399   3889    634   1695    765       C  
ATOM   3948  CD  PRO C 333      23.752 -18.911 -57.732  1.00 33.45           C  
ANISOU 3948  CD  PRO C 333     5902   2609   4197    649   1558    642       C  
ATOM   3949  N   THR C 334      25.193 -20.422 -54.866  1.00 34.79           N  
ANISOU 3949  N   THR C 334     6527   2720   3970   1237   1627   1067       N  
ATOM   3950  CA  THR C 334      25.456 -21.430 -53.844  1.00 37.58           C  
ANISOU 3950  CA  THR C 334     7094   2968   4215   1447   1721   1277       C  
ATOM   3951  C   THR C 334      26.955 -21.640 -53.646  1.00 39.27           C  
ANISOU 3951  C   THR C 334     7349   3258   4313   1699   1530   1276       C  
ATOM   3952  O   THR C 334      27.378 -22.362 -52.744  1.00 40.51           O  
ANISOU 3952  O   THR C 334     7634   3414   4345   1887   1539   1405       O  
ATOM   3953  CB  THR C 334      24.806 -22.784 -54.194  1.00 39.57           C  
ANISOU 3953  CB  THR C 334     7341   3014   4681   1313   1893   1317       C  
ATOM   3954  OG1 THR C 334      25.448 -23.339 -55.348  1.00 38.36           O  
ANISOU 3954  OG1 THR C 334     7116   2761   4698   1269   1818   1206       O  
ATOM   3955  CG2 THR C 334      23.314 -22.617 -54.465  1.00 39.07           C  
ANISOU 3955  CG2 THR C 334     7177   2895   4772   1057   2047   1284       C  
ATOM   3956  N   ARG C 335      27.753 -21.004 -54.496  1.00 37.19           N  
ANISOU 3956  N   ARG C 335     6896   3129   4105   1658   1336   1075       N  
ATOM   3957  CA  ARG C 335      29.203 -21.163 -54.466  1.00 41.14           C  
ANISOU 3957  CA  ARG C 335     7369   3713   4548   1870   1147   1039       C  
ATOM   3958  C   ARG C 335      29.853 -20.014 -53.705  1.00 39.93           C  
ANISOU 3958  C   ARG C 335     7157   3833   4182   1996    934    970       C  
ATOM   3959  O   ARG C 335      29.291 -18.922 -53.644  1.00 39.49           O  
ANISOU 3959  O   ARG C 335     7021   3906   4077   1865    911    881       O  
ATOM   3960  CB  ARG C 335      29.753 -21.241 -55.895  1.00 40.02           C  
ANISOU 3960  CB  ARG C 335     7051   3537   4617   1757   1085    864       C  
ATOM   3961  N   PRO C 336      31.038 -20.260 -53.114  1.00 41.14           N  
ANISOU 3961  N   PRO C 336     7346   4068   4216   2255    771   1005       N  
ATOM   3962  CA  PRO C 336      31.809 -19.203 -52.441  1.00 43.41           C  
ANISOU 3962  CA  PRO C 336     7554   4614   4325   2380    528    907       C  
ATOM   3963  C   PRO C 336      31.972 -17.953 -53.300  1.00 41.85           C  
ANISOU 3963  C   PRO C 336     7101   4560   4239   2182    412    673       C  
ATOM   3964  O   PRO C 336      32.022 -18.038 -54.530  1.00 41.06           O  
ANISOU 3964  O   PRO C 336     6861   4386   4353   2022    458    576       O  
ATOM   3965  CB  PRO C 336      33.176 -19.856 -52.179  1.00 46.87           C  
ANISOU 3965  CB  PRO C 336     7996   5079   4734   2649    364    941       C  
ATOM   3966  CG  PRO C 336      32.957 -21.315 -52.289  1.00 48.42           C  
ANISOU 3966  CG  PRO C 336     8363   5022   5012   2720    552   1123       C  
ATOM   3967  CD  PRO C 336      31.726 -21.565 -53.093  1.00 45.77           C  
ANISOU 3967  CD  PRO C 336     8039   4500   4853   2445    797   1128       C  
ATOM   3968  N   PHE C 337      32.040 -16.796 -52.653  1.00 45.32           N  
ANISOU 3968  N   PHE C 337     7495   5195   4529   2198    271    585       N  
ATOM   3969  CA  PHE C 337      32.121 -15.540 -53.381  1.00 46.43           C  
ANISOU 3969  CA  PHE C 337     7411   5456   4775   2010    178    379       C  
ATOM   3970  C   PHE C 337      33.483 -14.896 -53.191  1.00 47.49           C  
ANISOU 3970  C   PHE C 337     7385   5769   4890   2133    -89    240       C  
ATOM   3971  O   PHE C 337      33.886 -14.594 -52.067  1.00 48.54           O  
ANISOU 3971  O   PHE C 337     7588   6032   4824   2313   -246    244       O  
ATOM   3972  CB  PHE C 337      31.022 -14.588 -52.926  1.00 42.71           C  
ANISOU 3972  CB  PHE C 337     6985   5046   4198   1887    243    358       C  
ATOM   3973  CG  PHE C 337      30.853 -13.396 -53.816  1.00 42.45           C  
ANISOU 3973  CG  PHE C 337     6744   5084   4303   1666    204    176       C  
ATOM   3974  CD2 PHE C 337      31.066 -12.114 -53.350  1.00 41.09           C  
ANISOU 3974  CD2 PHE C 337     6493   5076   4042   1662     54     44       C  
ATOM   3975  CE2 PHE C 337      30.903 -11.040 -54.197  1.00 40.03           C  
ANISOU 3975  CE2 PHE C 337     6179   4983   4047   1463     36   -105       C  
ATOM   3976  CZ  PHE C 337      30.525 -11.256 -55.510  1.00 38.32           C  
ANISOU 3976  CZ  PHE C 337     5869   4660   4032   1281    160   -120       C  
ATOM   3977  N   SER C 338      34.184 -14.684 -54.299  1.00 48.49           N  
ANISOU 3977  N   SER C 338     7295   5902   5228   2037   -138    111       N  
ATOM   3978  CA  SER C 338      35.519 -14.106 -54.266  1.00 49.35           C  
ANISOU 3978  CA  SER C 338     7205   6163   5383   2130   -372    -28       C  
ATOM   3979  C   SER C 338      35.478 -12.670 -54.765  1.00 45.99           C  
ANISOU 3979  C   SER C 338     6586   5841   5048   1930   -432   -210       C  
ATOM   3980  O   SER C 338      34.716 -12.340 -55.677  1.00 46.55           O  
ANISOU 3980  O   SER C 338     6618   5842   5228   1715   -283   -239       O  
ATOM   3981  CB  SER C 338      36.486 -14.937 -55.115  1.00 50.63           C  
ANISOU 3981  CB  SER C 338     7251   6253   5731   2193   -368    -32       C  
ATOM   3982  OG  SER C 338      36.166 -16.321 -55.038  1.00 50.16           O  
ANISOU 3982  OG  SER C 338     7386   6024   5648   2298   -224    143       O  
ATOM   3983  N   GLU C 339      36.287 -11.814 -54.155  1.00 46.93           N  
ANISOU 3983  N   GLU C 339     7142   5169   5519    451  -1350   1172       N  
ATOM   3984  CA  GLU C 339      36.396 -10.437 -54.608  1.00 45.63           C  
ANISOU 3984  CA  GLU C 339     6804   5133   5399    352  -1363   1071       C  
ATOM   3985  C   GLU C 339      37.174 -10.387 -55.922  1.00 44.45           C  
ANISOU 3985  C   GLU C 339     6371   5037   5482    439  -1327   1047       C  
ATOM   3986  O   GLU C 339      36.968  -9.494 -56.746  1.00 44.84           O  
ANISOU 3986  O   GLU C 339     6286   5155   5598    364  -1240    945       O  
ATOM   3987  CB  GLU C 339      37.072  -9.575 -53.542  1.00 46.70           C  
ANISOU 3987  CB  GLU C 339     6954   5359   5431    295  -1594   1102       C  
ATOM   3988  N   ALA C 340      38.054 -11.368 -56.106  1.00 44.20           N  
ANISOU 3988  N   ALA C 340     6262   4965   5568    605  -1383   1147       N  
ATOM   3989  CA  ALA C 340      38.902 -11.459 -57.293  1.00 42.54           C  
ANISOU 3989  CA  ALA C 340     5790   4795   5577    717  -1334   1143       C  
ATOM   3990  C   ALA C 340      38.098 -11.409 -58.592  1.00 44.31           C  
ANISOU 3990  C   ALA C 340     5991   4984   5860    679  -1091   1021       C  
ATOM   3991  O   ALA C 340      38.487 -10.740 -59.554  1.00 43.27           O  
ANISOU 3991  O   ALA C 340     5657   4932   5850    673  -1036    963       O  
ATOM   3992  CB  ALA C 340      39.736 -12.736 -57.238  1.00 42.65           C  
ANISOU 3992  CB  ALA C 340     5784   4732   5689    925  -1386   1270       C  
ATOM   3993  N   SER C 341      36.959 -12.094 -58.606  1.00 43.83           N  
ANISOU 3993  N   SER C 341     6142   4805   5707    642   -952    986       N  
ATOM   3994  CA  SER C 341      36.188 -12.262 -59.835  1.00 44.34           C  
ANISOU 3994  CA  SER C 341     6204   4818   5825    615   -745    882       C  
ATOM   3995  C   SER C 341      35.207 -11.132 -60.125  1.00 31.22           C  
ANISOU 3995  C   SER C 341     4537   3224   4101    443   -667    762       C  
ATOM   3996  O   SER C 341      34.361 -11.266 -61.008  1.00 24.28           O  
ANISOU 3996  O   SER C 341     3688   2299   3238    398   -515    678       O  
ATOM   3997  CB  SER C 341      35.415 -13.580 -59.793  1.00 37.80           C  
ANISOU 3997  CB  SER C 341     5595   3821   4947    643   -638    901       C  
ATOM   3998  OG  SER C 341      34.966 -13.873 -58.477  1.00 41.42           O  
ANISOU 3998  OG  SER C 341     6253   4233   5254    590   -709    969       O  
ATOM   3999  N   MET C 342      35.309 -10.025 -59.398  1.00 24.78           N  
ANISOU 3999  N   MET C 342     3692   2509   3212    351   -777    753       N  
ATOM   4000  CA  MET C 342      34.329  -8.952 -59.545  1.00 27.15           C  
ANISOU 4000  CA  MET C 342     4012   2859   3443    204   -702    647       C  
ATOM   4001  C   MET C 342      34.333  -8.321 -60.934  1.00 24.58           C  
ANISOU 4001  C   MET C 342     3522   2584   3233    191   -602    558       C  
ATOM   4002  O   MET C 342      33.275  -8.126 -61.535  1.00 21.99           O  
ANISOU 4002  O   MET C 342     3235   2235   2884    120   -473    473       O  
ATOM   4003  CB  MET C 342      34.557  -7.864 -58.501  1.00 27.85           C  
ANISOU 4003  CB  MET C 342     4122   3031   3428    118   -843    653       C  
ATOM   4004  CG  MET C 342      33.464  -6.822 -58.511  1.00 30.60           C  
ANISOU 4004  CG  MET C 342     4527   3409   3691    -14   -752    550       C  
ATOM   4005  SD  MET C 342      31.848  -7.561 -58.197  1.00 60.88           S  
ANISOU 4005  SD  MET C 342     8570   7143   7419    -68   -581    527       S  
ATOM   4006  CE  MET C 342      32.193  -8.534 -56.741  1.00 30.71           C  
ANISOU 4006  CE  MET C 342     4948   3251   3469    -22   -690    654       C  
ATOM   4007  N   MET C 343      35.518  -7.995 -61.439  1.00 22.92           N  
ANISOU 4007  N   MET C 343     3123   2442   3145    259   -662    583       N  
ATOM   4008  CA  MET C 343      35.628  -7.391 -62.761  1.00 21.55           C  
ANISOU 4008  CA  MET C 343     2805   2313   3072    251   -560    510       C  
ATOM   4009  C   MET C 343      35.064  -8.317 -63.833  1.00 19.69           C  
ANISOU 4009  C   MET C 343     2625   1982   2873    308   -398    467       C  
ATOM   4010  O   MET C 343      34.397  -7.866 -64.764  1.00 20.20           O  
ANISOU 4010  O   MET C 343     2685   2051   2939    251   -293    379       O  
ATOM   4011  CB  MET C 343      37.082  -7.040 -63.079  1.00 21.46           C  
ANISOU 4011  CB  MET C 343     2573   2384   3198    322   -635    563       C  
ATOM   4012  CG  MET C 343      37.252  -6.308 -64.400  1.00 22.90           C  
ANISOU 4012  CG  MET C 343     2616   2613   3470    304   -521    496       C  
ATOM   4013  SD  MET C 343      36.283  -4.788 -64.423  1.00 23.77           S  
ANISOU 4013  SD  MET C 343     2778   2774   3481    125   -507    392       S  
ATOM   4014  CE  MET C 343      36.778  -4.073 -65.986  1.00 23.19           C  
ANISOU 4014  CE  MET C 343     2539   2747   3524    131   -387    347       C  
ATOM   4015  N   GLY C 344      35.331  -9.612 -63.690  1.00 20.15           N  
ANISOU 4015  N   GLY C 344     2754   1945   2955    421   -389    532       N  
ATOM   4016  CA  GLY C 344      34.822 -10.606 -64.616  1.00 20.41           C  
ANISOU 4016  CA  GLY C 344     2880   1863   3011    471   -249    492       C  
ATOM   4017  C   GLY C 344      33.306 -10.649 -64.620  1.00 24.12           C  
ANISOU 4017  C   GLY C 344     3503   2280   3383    338   -177    419       C  
ATOM   4018  O   GLY C 344      32.684 -10.728 -65.681  1.00 18.09           O  
ANISOU 4018  O   GLY C 344     2761   1480   2632    307    -72    338       O  
ATOM   4019  N   LEU C 345      32.709 -10.594 -63.432  1.00 19.01           N  
ANISOU 4019  N   LEU C 345     2960   1629   2633    259   -234    449       N  
ATOM   4020  CA  LEU C 345      31.254 -10.611 -63.315  1.00 20.58           C  
ANISOU 4020  CA  LEU C 345     3277   1789   2752    131   -156    393       C  
ATOM   4021  C   LEU C 345      30.647  -9.372 -63.960  1.00 19.14           C  
ANISOU 4021  C   LEU C 345     3001   1699   2570     36   -116    297       C  
ATOM   4022  O   LEU C 345      29.677  -9.461 -64.715  1.00 18.90           O  
ANISOU 4022  O   LEU C 345     2997   1638   2547    -27    -30    229       O  
ATOM   4023  CB  LEU C 345      30.826 -10.696 -61.846  1.00 21.26           C  
ANISOU 4023  CB  LEU C 345     3492   1864   2722     73   -207    453       C  
ATOM   4024  CG  LEU C 345      31.103 -11.986 -61.071  1.00 25.82           C  
ANISOU 4024  CG  LEU C 345     4218   2327   3266    144   -237    554       C  
ATOM   4025  CD1 LEU C 345      30.600 -11.871 -59.639  1.00 25.86           C  
ANISOU 4025  CD1 LEU C 345     4365   2331   3130     70   -274    607       C  
ATOM   4026  CD2 LEU C 345      30.467 -13.183 -61.761  1.00 25.88           C  
ANISOU 4026  CD2 LEU C 345     4329   2194   3310    144   -125    536       C  
ATOM   4027  N   LEU C 346      31.230  -8.218 -63.648  1.00 16.70           N  
ANISOU 4027  N   LEU C 346     2591   1498   2257     24   -192    298       N  
ATOM   4028  CA  LEU C 346      30.749  -6.934 -64.149  1.00 15.46           C  
ANISOU 4028  CA  LEU C 346     2358   1420   2095    -55   -164    218       C  
ATOM   4029  C   LEU C 346      30.926  -6.787 -65.656  1.00 15.37           C  
ANISOU 4029  C   LEU C 346     2256   1416   2169    -24    -96    161       C  
ATOM   4030  O   LEU C 346      30.082  -6.207 -66.334  1.00 13.91           O  
ANISOU 4030  O   LEU C 346     2063   1248   1974    -88    -40     89       O  
ATOM   4031  CB  LEU C 346      31.463  -5.786 -63.432  1.00 17.92           C  
ANISOU 4031  CB  LEU C 346     2604   1823   2380    -79   -270    236       C  
ATOM   4032  CG  LEU C 346      31.124  -5.631 -61.947  1.00 18.18           C  
ANISOU 4032  CG  LEU C 346     2761   1856   2290   -132   -333    271       C  
ATOM   4033  CD1 LEU C 346      31.904  -4.500 -61.323  1.00 20.36           C  
ANISOU 4033  CD1 LEU C 346     2990   2210   2535   -163   -456    280       C  
ATOM   4034  CD2 LEU C 346      29.638  -5.396 -61.774  1.00 23.93           C  
ANISOU 4034  CD2 LEU C 346     3581   2565   2945   -217   -228    215       C  
ATOM   4035  N   THR C 347      32.033  -7.304 -66.174  1.00 14.80           N  
ANISOU 4035  N   THR C 347     2119   1328   2176     83    -99    198       N  
ATOM   4036  CA  THR C 347      32.301  -7.239 -67.602  1.00 14.52           C  
ANISOU 4036  CA  THR C 347     2022   1289   2205    126    -16    150       C  
ATOM   4037  C   THR C 347      31.311  -8.097 -68.379  1.00 16.86           C  
ANISOU 4037  C   THR C 347     2440   1486   2478    109     71     93       C  
ATOM   4038  O   THR C 347      30.783  -7.674 -69.410  1.00 15.84           O  
ANISOU 4038  O   THR C 347     2311   1365   2344     69    124     22       O  
ATOM   4039  CB  THR C 347      33.735  -7.686 -67.922  1.00 18.18           C  
ANISOU 4039  CB  THR C 347     2388   1754   2766    261    -15    210       C  
ATOM   4040  OG1 THR C 347      34.666  -6.779 -67.312  1.00 18.30           O  
ANISOU 4040  OG1 THR C 347     2262   1873   2819    254   -111    260       O  
ATOM   4041  CG2 THR C 347      33.962  -7.710 -69.421  1.00 17.43           C  
ANISOU 4041  CG2 THR C 347     2264   1639   2718    312    103    158       C  
ATOM   4042  N   ASN C 348      31.056  -9.303 -67.878  1.00 15.19           N  
ANISOU 4042  N   ASN C 348     2346   1176   2250    132     74    129       N  
ATOM   4043  CA  ASN C 348      30.070 -10.181 -68.504  1.00 15.25           C  
ANISOU 4043  CA  ASN C 348     2483   1075   2235     89    141     78       C  
ATOM   4044  C   ASN C 348      28.661  -9.593 -68.439  1.00 16.62           C  
ANISOU 4044  C   ASN C 348     2671   1284   2361    -57    143     21       C  
ATOM   4045  O   ASN C 348      27.883  -9.738 -69.382  1.00 15.77           O  
ANISOU 4045  O   ASN C 348     2602   1141   2250   -111    181    -46       O  
ATOM   4046  CB  ASN C 348      30.087 -11.568 -67.855  1.00 18.01           C  
ANISOU 4046  CB  ASN C 348     2967   1300   2577    130    142    137       C  
ATOM   4047  CG  ASN C 348      29.003 -12.477 -68.399  1.00 24.04           C  
ANISOU 4047  CG  ASN C 348     3875   1941   3318     53    199     85       C  
ATOM   4048  OD1 ASN C 348      27.894 -12.496 -67.884  1.00 20.90           O  
ANISOU 4048  OD1 ASN C 348     3521   1536   2882    -72    196     77       O  
ATOM   4049  ND2 ASN C 348      29.314 -13.214 -69.460  1.00 28.58           N  
ANISOU 4049  ND2 ASN C 348     4524   2418   3918    123    254     48       N  
ATOM   4050  N   LEU C 349      28.340  -8.929 -67.330  1.00 13.42           N  
ANISOU 4050  N   LEU C 349     2237    947   1915   -115    102     50       N  
ATOM   4051  CA  LEU C 349      27.059  -8.239 -67.178  1.00 12.71           C  
ANISOU 4051  CA  LEU C 349     2135    904   1792   -231    119      5       C  
ATOM   4052  C   LEU C 349      26.889  -7.134 -68.225  1.00 16.46           C  
ANISOU 4052  C   LEU C 349     2517   1451   2285   -247    124    -64       C  
ATOM   4053  O   LEU C 349      25.867  -7.063 -68.922  1.00 12.70           O  
ANISOU 4053  O   LEU C 349     2044    969   1814   -312    148   -118       O  
ATOM   4054  CB  LEU C 349      26.937  -7.659 -65.770  1.00 12.75           C  
ANISOU 4054  CB  LEU C 349     2145    963   1739   -265     89     49       C  
ATOM   4055  CG  LEU C 349      25.712  -6.800 -65.470  1.00 14.46           C  
ANISOU 4055  CG  LEU C 349     2338   1235   1923   -359    126     10       C  
ATOM   4056  CD1 LEU C 349      24.431  -7.606 -65.624  1.00 17.21           C  
ANISOU 4056  CD1 LEU C 349     2731   1522   2287   -442    191     -4       C  
ATOM   4057  CD2 LEU C 349      25.828  -6.205 -64.067  1.00 16.72           C  
ANISOU 4057  CD2 LEU C 349     2661   1562   2130   -370    104     50       C  
ATOM   4058  N   ALA C 350      27.905  -6.287 -68.342  1.00 12.53           N  
ANISOU 4058  N   ALA C 350     1937   1020   1802   -191     95    -55       N  
ATOM   4059  CA  ALA C 350      27.898  -5.206 -69.318  1.00 11.81           C  
ANISOU 4059  CA  ALA C 350     1775    989   1723   -200    104   -108       C  
ATOM   4060  C   ALA C 350      27.847  -5.748 -70.744  1.00 13.18           C  
ANISOU 4060  C   ALA C 350     1983   1108   1915   -173    149   -153       C  
ATOM   4061  O   ALA C 350      27.185  -5.170 -71.603  1.00 11.89           O  
ANISOU 4061  O   ALA C 350     1814    965   1738   -212    156   -206       O  
ATOM   4062  CB  ALA C 350      29.112  -4.320 -69.131  1.00 11.78           C  
ANISOU 4062  CB  ALA C 350     1682   1053   1740   -157     69    -78       C  
ATOM   4063  N   ASP C 351      28.537  -6.859 -70.992  1.00 12.46           N  
ANISOU 4063  N   ASP C 351     1947    941   1848    -99    176   -130       N  
ATOM   4064  CA  ASP C 351      28.506  -7.479 -72.315  1.00 12.83           C  
ANISOU 4064  CA  ASP C 351     2069    914   1891    -68    228   -180       C  
ATOM   4065  C   ASP C 351      27.069  -7.787 -72.718  1.00 16.45           C  
ANISOU 4065  C   ASP C 351     2605   1330   2315   -173    213   -237       C  
ATOM   4066  O   ASP C 351      26.649  -7.480 -73.835  1.00 14.38           O  
ANISOU 4066  O   ASP C 351     2369   1067   2027   -198    215   -295       O  
ATOM   4067  CB  ASP C 351      29.332  -8.762 -72.355  1.00 13.95           C  
ANISOU 4067  CB  ASP C 351     2284    956   2060     34    270   -147       C  
ATOM   4068  CG  ASP C 351      30.829  -8.506 -72.327  1.00 20.90           C  
ANISOU 4068  CG  ASP C 351     3062   1881   2997    155    295    -93       C  
ATOM   4069  OD1 ASP C 351      31.256  -7.345 -72.501  1.00 19.94           O  
ANISOU 4069  OD1 ASP C 351     2825   1860   2892    146    288    -91       O  
ATOM   4070  OD2 ASP C 351      31.576  -9.493 -72.127  1.00 18.92           O  
ANISOU 4070  OD2 ASP C 351     2844   1560   2785    260    322    -46       O  
ATOM   4071  N   ARG C 352      26.312  -8.370 -71.794  1.00 12.94           N  
ANISOU 4071  N   ARG C 352     2194    852   1870   -240    194   -214       N  
ATOM   4072  CA  ARG C 352      24.939  -8.766 -72.080  1.00 13.17           C  
ANISOU 4072  CA  ARG C 352     2271    842   1891   -354    177   -256       C  
ATOM   4073  C   ARG C 352      23.994  -7.569 -72.121  1.00 12.43           C  
ANISOU 4073  C   ARG C 352     2073    852   1798   -426    146   -282       C  
ATOM   4074  O   ARG C 352      23.018  -7.567 -72.879  1.00 12.84           O  
ANISOU 4074  O   ARG C 352     2106    927   1847   -476    104   -315       O  
ATOM   4075  CB  ARG C 352      24.452  -9.797 -71.055  1.00 13.89           C  
ANISOU 4075  CB  ARG C 352     2425    862   1990   -408    186   -211       C  
ATOM   4076  CG  ARG C 352      25.026 -11.188 -71.296  1.00 14.96           C  
ANISOU 4076  CG  ARG C 352     2684    878   2123   -347    206   -196       C  
ATOM   4077  CD  ARG C 352      24.637 -12.197 -70.223  1.00 15.81           C  
ANISOU 4077  CD  ARG C 352     2855    920   2231   -389    214   -137       C  
ATOM   4078  NE  ARG C 352      25.312 -11.949 -68.951  1.00 15.67           N  
ANISOU 4078  NE  ARG C 352     2843    902   2207   -343    225    -62       N  
ATOM   4079  CZ  ARG C 352      24.695 -11.618 -67.822  1.00 15.55           C  
ANISOU 4079  CZ  ARG C 352     2798    939   2172   -415    227    -21       C  
ATOM   4080  NH1 ARG C 352      23.373 -11.499 -67.790  1.00 15.57           N  
ANISOU 4080  NH1 ARG C 352     2754    981   2182   -534    240    -45       N  
ATOM   4081  NH2 ARG C 352      25.405 -11.414 -66.722  1.00 15.62           N  
ANISOU 4081  NH2 ARG C 352     2803    981   2150   -352    209     50       N  
ATOM   4082  N   GLU C 353      24.278  -6.551 -71.316  1.00 11.95           N  
ANISOU 4082  N   GLU C 353     1924    881   1736   -403    145   -251       N  
ATOM   4083  CA  GLU C 353      23.469  -5.338 -71.335  1.00 11.38           C  
ANISOU 4083  CA  GLU C 353     1763    896   1664   -445    128   -273       C  
ATOM   4084  C   GLU C 353      23.589  -4.592 -72.657  1.00 12.68           C  
ANISOU 4084  C   GLU C 353     1912   1087   1817   -418    105   -320       C  
ATOM   4085  O   GLU C 353      22.636  -3.956 -73.097  1.00 13.73           O  
ANISOU 4085  O   GLU C 353     2001   1261   1955   -459     74   -348       O  
ATOM   4086  CB  GLU C 353      23.859  -4.394 -70.204  1.00 10.92           C  
ANISOU 4086  CB  GLU C 353     1651    906   1591   -421    135   -237       C  
ATOM   4087  CG  GLU C 353      23.490  -4.867 -68.817  1.00 11.35           C  
ANISOU 4087  CG  GLU C 353     1732    947   1631   -457    161   -191       C  
ATOM   4088  CD  GLU C 353      23.925  -3.868 -67.766  1.00 18.49           C  
ANISOU 4088  CD  GLU C 353     2618   1912   2497   -434    156   -166       C  
ATOM   4089  OE1 GLU C 353      25.107  -3.897 -67.367  1.00 13.62           O  
ANISOU 4089  OE1 GLU C 353     2019   1293   1861   -383    124   -133       O  
ATOM   4090  OE2 GLU C 353      23.091  -3.031 -67.371  1.00 16.58           O  
ANISOU 4090  OE2 GLU C 353     2341   1715   2242   -464    182   -182       O  
ATOM   4091  N   LEU C 354      24.763  -4.658 -73.278  1.00 11.92           N  
ANISOU 4091  N   LEU C 354     1851    971   1708   -344    125   -320       N  
ATOM   4092  CA  LEU C 354      24.994  -3.920 -74.513  1.00 16.22           C  
ANISOU 4092  CA  LEU C 354     2401   1536   2226   -315    123   -355       C  
ATOM   4093  C   LEU C 354      24.092  -4.429 -75.632  1.00 13.35           C  
ANISOU 4093  C   LEU C 354     2112   1128   1833   -358     84   -405       C  
ATOM   4094  O   LEU C 354      23.582  -3.650 -76.435  1.00 12.94           O  
ANISOU 4094  O   LEU C 354     2047   1115   1754   -366     43   -426       O  
ATOM   4095  CB  LEU C 354      26.463  -4.008 -74.929  1.00 15.56           C  
ANISOU 4095  CB  LEU C 354     2333   1436   2141   -226    178   -336       C  
ATOM   4096  CG  LEU C 354      26.845  -3.219 -76.188  1.00 16.42           C  
ANISOU 4096  CG  LEU C 354     2461   1563   2215   -195    204   -362       C  
ATOM   4097  CD1 LEU C 354      26.640  -1.736 -75.954  1.00 14.02           C  
ANISOU 4097  CD1 LEU C 354     2076   1338   1911   -221    176   -352       C  
ATOM   4098  CD2 LEU C 354      28.278  -3.499 -76.603  1.00 17.08           C  
ANISOU 4098  CD2 LEU C 354     2551   1626   2313   -105    289   -337       C  
ATOM   4099  N   VAL C 355      23.887  -5.741 -75.672  1.00 14.08           N  
ANISOU 4099  N   VAL C 355     2272   1151   1925   -372     79   -405       N  
ATOM   4100  CA  VAL C 355      23.014  -6.328 -76.672  1.00 13.19           C  
ANISOU 4100  CA  VAL C 355     2211   1014   1788   -410     18   -438       C  
ATOM   4101  C   VAL C 355      21.601  -5.754 -76.562  1.00 13.51           C  
ANISOU 4101  C   VAL C 355     2154   1117   1860   -486    -59   -441       C  
ATOM   4102  O   VAL C 355      20.997  -5.387 -77.567  1.00 14.19           O  
ANISOU 4102  O   VAL C 355     2246   1222   1924   -503   -122   -473       O  
ATOM   4103  CB  VAL C 355      22.970  -7.856 -76.541  1.00 18.46           C  
ANISOU 4103  CB  VAL C 355     2962   1591   2461   -426     27   -436       C  
ATOM   4104  CG1 VAL C 355      22.196  -8.455 -77.693  1.00 17.73           C  
ANISOU 4104  CG1 VAL C 355     2935   1466   2336   -469    -35   -480       C  
ATOM   4105  CG2 VAL C 355      24.384  -8.409 -76.515  1.00 16.54           C  
ANISOU 4105  CG2 VAL C 355     2803   1280   2203   -329    113   -424       C  
ATOM   4106  N   HIS C 356      21.087  -5.653 -75.339  1.00 12.53           N  
ANISOU 4106  N   HIS C 356     1946   1025   1789   -529    -46   -405       N  
ATOM   4107  CA  HIS C 356      19.775  -5.049 -75.119  1.00 12.68           C  
ANISOU 4107  CA  HIS C 356     1857   1106   1855   -592    -93   -401       C  
ATOM   4108  C   HIS C 356      19.779  -3.544 -75.372  1.00 12.44           C  
ANISOU 4108  C   HIS C 356     1768   1146   1812   -557   -103   -411       C  
ATOM   4109  O   HIS C 356      18.767  -2.986 -75.789  1.00 13.13           O  
ANISOU 4109  O   HIS C 356     1790   1274   1925   -592   -166   -424       O  
ATOM   4110  CB  HIS C 356      19.278  -5.333 -73.700  1.00 12.78           C  
ANISOU 4110  CB  HIS C 356     1807   1133   1917   -641    -42   -357       C  
ATOM   4111  CG  HIS C 356      18.970  -6.776 -73.454  1.00 13.72           C  
ANISOU 4111  CG  HIS C 356     1977   1179   2057   -696    -40   -342       C  
ATOM   4112  ND1 HIS C 356      17.726  -7.320 -73.693  1.00 20.15           N  
ANISOU 4112  ND1 HIS C 356     2743   1985   2929   -785    -92   -343       N  
ATOM   4113  CD2 HIS C 356      19.747  -7.783 -73.000  1.00 13.90           C  
ANISOU 4113  CD2 HIS C 356     2096   1127   2059   -677      6   -324       C  
ATOM   4114  CE1 HIS C 356      17.754  -8.609 -73.396  1.00 21.51           C  
ANISOU 4114  CE1 HIS C 356     2986   2077   3108   -822    -72   -329       C  
ATOM   4115  NE2 HIS C 356      18.964  -8.916 -72.971  1.00 15.94           N  
ANISOU 4115  NE2 HIS C 356     2376   1329   2352   -753    -12   -316       N  
ATOM   4116  N   MET C 357      20.909  -2.892 -75.128  1.00 13.02           N  
ANISOU 4116  N   MET C 357     1861   1231   1854   -492    -47   -405       N  
ATOM   4117  CA  MET C 357      21.003  -1.457 -75.366  1.00 12.45           C  
ANISOU 4117  CA  MET C 357     1749   1211   1770   -459    -49   -417       C  
ATOM   4118  C   MET C 357      20.782  -1.122 -76.837  1.00 15.84           C  
ANISOU 4118  C   MET C 357     2233   1631   2153   -450   -115   -450       C  
ATOM   4119  O   MET C 357      20.178  -0.105 -77.166  1.00 15.72           O  
ANISOU 4119  O   MET C 357     2172   1661   2140   -436   -159   -449       O  
ATOM   4120  CB  MET C 357      22.356  -0.914 -74.922  1.00 20.47           C  
ANISOU 4120  CB  MET C 357     2778   2234   2764   -397     12   -394       C  
ATOM   4121  CG  MET C 357      22.424   0.604 -74.938  1.00 18.21           C  
ANISOU 4121  CG  MET C 357     2453   1999   2468   -362     11   -388       C  
ATOM   4122  SD  MET C 357      24.101   1.201 -74.732  1.00 11.72           S  
ANISOU 4122  SD  MET C 357     1646   1180   1626   -316     63   -362       S  
ATOM   4123  CE  MET C 357      24.500   0.564 -73.111  1.00 13.99           C  
ANISOU 4123  CE  MET C 357     1904   1470   1940   -330     85   -329       C  
ATOM   4124  N   ILE C 358      21.274  -1.981 -77.721  1.00 12.07           N  
ANISOU 4124  N   ILE C 358     1860   1097   1627   -434   -121   -465       N  
ATOM   4125  CA  ILE C 358      21.102  -1.763 -79.152  1.00 13.96           C  
ANISOU 4125  CA  ILE C 358     2180   1325   1800   -421   -178   -495       C  
ATOM   4126  C   ILE C 358      19.633  -1.891 -79.542  1.00 16.73           C  
ANISOU 4126  C   ILE C 358     2483   1697   2176   -488   -291   -513       C  
ATOM   4127  O   ILE C 358      19.129  -1.105 -80.344  1.00 18.12           O  
ANISOU 4127  O   ILE C 358     2671   1899   2315   -484   -367   -521       O  
ATOM   4128  CB  ILE C 358      21.982  -2.731 -79.961  1.00 16.96           C  
ANISOU 4128  CB  ILE C 358     2688   1640   2118   -384   -132   -510       C  
ATOM   4129  CG1 ILE C 358      23.369  -2.112 -80.128  1.00 24.89           C  
ANISOU 4129  CG1 ILE C 358     3734   2639   3084   -311    -33   -496       C  
ATOM   4130  CG2 ILE C 358      21.382  -3.014 -81.335  1.00 21.42           C  
ANISOU 4130  CG2 ILE C 358     3345   2184   2611   -402   -208   -543       C  
ATOM   4131  CD1 ILE C 358      24.486  -3.018 -79.726  1.00 32.61           C  
ANISOU 4131  CD1 ILE C 358     4745   3567   4078   -270     63   -486       C  
ATOM   4132  N   ASN C 359      18.939  -2.858 -78.950  1.00 14.39           N  
ANISOU 4132  N   ASN C 359     2131   1390   1947   -551   -306   -511       N  
ATOM   4133  CA  ASN C 359      17.507  -3.002 -79.189  1.00 14.56           C  
ANISOU 4133  CA  ASN C 359     2071   1446   2015   -632   -402   -521       C  
ATOM   4134  C   ASN C 359      16.759  -1.765 -78.700  1.00 15.41           C  
ANISOU 4134  C   ASN C 359     2045   1631   2180   -638   -438   -495       C  
ATOM   4135  O   ASN C 359      15.833  -1.288 -79.356  1.00 18.14           O  
ANISOU 4135  O   ASN C 359     2335   2018   2538   -652   -549   -491       O  
ATOM   4136  CB  ASN C 359      16.970  -4.264 -78.504  1.00 17.88           C  
ANISOU 4136  CB  ASN C 359     2449   1833   2510   -703   -387   -516       C  
ATOM   4137  CG  ASN C 359      15.453  -4.366 -78.553  1.00 29.29           C  
ANISOU 4137  CG  ASN C 359     3770   3332   4026   -801   -465   -517       C  
ATOM   4138  OD1 ASN C 359      14.748  -3.819 -77.697  1.00 35.79           O  
ANISOU 4138  OD1 ASN C 359     4450   4225   4925   -836   -445   -483       O  
ATOM   4139  ND2 ASN C 359      14.941  -5.078 -79.553  1.00 31.48           N  
ANISOU 4139  ND2 ASN C 359     4106   3585   4272   -852   -552   -547       N  
ATOM   4140  N   TRP C 360      17.183  -1.236 -77.556  1.00 14.92           N  
ANISOU 4140  N   TRP C 360     1923   1586   2160   -605   -350   -469       N  
ATOM   4141  CA  TRP C 360      16.574  -0.040 -76.986  1.00 14.08           C  
ANISOU 4141  CA  TRP C 360     1681   1556   2111   -554   -333   -436       C  
ATOM   4142  C   TRP C 360      16.813   1.180 -77.868  1.00 18.11           C  
ANISOU 4142  C   TRP C 360     2235   2083   2562   -470   -379   -437       C  
ATOM   4143  O   TRP C 360      15.894   1.956 -78.138  1.00 17.74           O  
ANISOU 4143  O   TRP C 360     2101   2083   2556   -441   -446   -420       O  
ATOM   4144  CB  TRP C 360      17.124   0.215 -75.582  1.00 13.42           C  
ANISOU 4144  CB  TRP C 360     1569   1486   2046   -520   -202   -411       C  
ATOM   4145  CG  TRP C 360      16.928   1.620 -75.107  1.00 13.60           C  
ANISOU 4145  CG  TRP C 360     1526   1558   2084   -441   -164   -390       C  
ATOM   4146  CD1 TRP C 360      15.788   2.161 -74.589  1.00 17.39           C  
ANISOU 4146  CD1 TRP C 360     1872   2091   2643   -425   -150   -369       C  
ATOM   4147  CD2 TRP C 360      17.902   2.676 -75.128  1.00 14.07           C  
ANISOU 4147  CD2 TRP C 360     1657   1609   2081   -367   -128   -389       C  
ATOM   4148  NE1 TRP C 360      15.994   3.486 -74.277  1.00 16.56           N  
ANISOU 4148  NE1 TRP C 360     1774   2000   2519   -334   -105   -360       N  
ATOM   4149  CE2 TRP C 360      17.279   3.825 -74.598  1.00 14.54           C  
ANISOU 4149  CE2 TRP C 360     1645   1703   2175   -308    -98   -373       C  
ATOM   4150  CE3 TRP C 360      19.237   2.757 -75.539  1.00 13.36           C  
ANISOU 4150  CE3 TRP C 360     1677   1481   1917   -346   -110   -397       C  
ATOM   4151  CZ2 TRP C 360      17.949   5.043 -74.470  1.00 13.04           C  
ANISOU 4151  CZ2 TRP C 360     1515   1499   1939   -243    -64   -370       C  
ATOM   4152  CZ3 TRP C 360      19.900   3.969 -75.411  1.00 14.30           C  
ANISOU 4152  CZ3 TRP C 360     1829   1600   2004   -292    -76   -387       C  
ATOM   4153  CH2 TRP C 360      19.255   5.096 -74.878  1.00 13.58           C  
ANISOU 4153  CH2 TRP C 360     1688   1531   1938   -247    -59   -377       C  
ATOM   4154  N   ALA C 361      18.059   1.343 -78.304  1.00 13.55           N  
ANISOU 4154  N   ALA C 361     1790   1464   1896   -428   -335   -448       N  
ATOM   4155  CA  ALA C 361      18.449   2.476 -79.133  1.00 18.90           C  
ANISOU 4155  CA  ALA C 361     2535   2141   2506   -358   -355   -441       C  
ATOM   4156  C   ALA C 361      17.603   2.547 -80.393  1.00 21.92           C  
ANISOU 4156  C   ALA C 361     2953   2524   2852   -367   -496   -451       C  
ATOM   4157  O   ALA C 361      17.167   3.621 -80.803  1.00 14.56           O  
ANISOU 4157  O   ALA C 361     2004   1616   1912   -310   -550   -428       O  
ATOM   4158  CB  ALA C 361      19.917   2.382 -79.492  1.00 15.28           C  
ANISOU 4158  CB  ALA C 361     2204   1635   1967   -332   -275   -449       C  
ATOM   4159  N   LYS C 362      17.356   1.391 -80.994  1.00 17.84           N  
ANISOU 4159  N   LYS C 362     2498   1972   2309   -441   -567   -485       N  
ATOM   4160  CA  LYS C 362      16.583   1.334 -82.226  1.00 16.39           C  
ANISOU 4160  CA  LYS C 362     2373   1781   2073   -467   -728   -500       C  
ATOM   4161  C   LYS C 362      15.118   1.725 -82.019  1.00 20.08           C  
ANISOU 4161  C   LYS C 362     2655   2322   2652   -483   -846   -470       C  
ATOM   4162  O   LYS C 362      14.421   2.030 -82.981  1.00 21.03           O  
ANISOU 4162  O   LYS C 362     2792   2457   2740   -479   -997   -463       O  
ATOM   4163  CB  LYS C 362      16.677  -0.065 -82.839  1.00 19.90           C  
ANISOU 4163  CB  LYS C 362     2911   2187   2462   -523   -717   -526       C  
ATOM   4164  CG  LYS C 362      18.060  -0.406 -83.382  1.00 23.46           C  
ANISOU 4164  CG  LYS C 362     3535   2573   2805   -474   -604   -543       C  
ATOM   4165  CD  LYS C 362      18.162  -1.873 -83.781  1.00 24.71           C  
ANISOU 4165  CD  LYS C 362     3774   2678   2935   -515   -587   -572       C  
ATOM   4166  CE  LYS C 362      17.638  -2.118 -85.189  1.00 33.66           C  
ANISOU 4166  CE  LYS C 362     5031   3788   3970   -536   -701   -588       C  
ATOM   4167  NZ  LYS C 362      17.432  -3.569 -85.472  1.00 36.87           N  
ANISOU 4167  NZ  LYS C 362     5503   4138   4367   -597   -714   -621       N  
ATOM   4168  N   ARG C 363      14.659   1.727 -80.770  1.00 17.57           N  
ANISOU 4168  N   ARG C 363     2160   2053   2463   -492   -771   -446       N  
ATOM   4169  CA  ARG C 363      13.281   2.115 -80.468  1.00 17.38           C  
ANISOU 4169  CA  ARG C 363     1930   2106   2569   -492   -847   -410       C  
ATOM   4170  C   ARG C 363      13.158   3.547 -79.950  1.00 21.69           C  
ANISOU 4170  C   ARG C 363     2392   2695   3155   -365   -779   -368       C  
ATOM   4171  O   ARG C 363      12.053   4.035 -79.713  1.00 23.77           O  
ANISOU 4171  O   ARG C 363     2480   3021   3530   -330   -822   -331       O  
ATOM   4172  CB  ARG C 363      12.662   1.147 -79.456  1.00 21.63           C  
ANISOU 4172  CB  ARG C 363     2322   2666   3229   -590   -795   -405       C  
ATOM   4173  CG  ARG C 363      12.511  -0.272 -79.975  1.00 22.34           C  
ANISOU 4173  CG  ARG C 363     2496   2723   3271   -707   -836   -430       C  
ATOM   4174  CD  ARG C 363      11.844  -1.176 -78.947  1.00 28.59           C  
ANISOU 4174  CD  ARG C 363     3159   3539   4164   -798   -757   -410       C  
ATOM   4175  NE  ARG C 363      10.486  -0.736 -78.627  1.00 31.77           N  
ANISOU 4175  NE  ARG C 363     3330   4035   4706   -805   -799   -362       N  
ATOM   4176  CZ  ARG C 363       9.653  -1.401 -77.832  1.00 32.50           C  
ANISOU 4176  CZ  ARG C 363     3286   4168   4895   -887   -736   -333       C  
ATOM   4177  NH1 ARG C 363      10.037  -2.542 -77.275  1.00 31.77           N  
ANISOU 4177  NH1 ARG C 363     3282   4022   4769   -974   -644   -348       N  
ATOM   4178  NH2 ARG C 363       8.437  -0.924 -77.594  1.00 33.47           N  
ANISOU 4178  NH2 ARG C 363     3188   4384   5146   -875   -757   -284       N  
ATOM   4179  N   VAL C 364      14.287   4.218 -79.762  1.00 18.29           N  
ANISOU 4179  N   VAL C 364     2083   2225   2641   -296   -670   -371       N  
ATOM   4180  CA  VAL C 364      14.255   5.634 -79.425  1.00 18.29           C  
ANISOU 4180  CA  VAL C 364     2056   2239   2656   -181   -618   -339       C  
ATOM   4181  C   VAL C 364      13.816   6.391 -80.667  1.00 21.32           C  
ANISOU 4181  C   VAL C 364     2487   2620   2993   -118   -761   -316       C  
ATOM   4182  O   VAL C 364      14.488   6.313 -81.696  1.00 20.45           O  
ANISOU 4182  O   VAL C 364     2549   2463   2759   -130   -812   -331       O  
ATOM   4183  CB  VAL C 364      15.631   6.155 -78.960  1.00 16.52           C  
ANISOU 4183  CB  VAL C 364     1958   1965   2353   -148   -482   -348       C  
ATOM   4184  CG1 VAL C 364      15.610   7.674 -78.822  1.00 15.28           C  
ANISOU 4184  CG1 VAL C 364     1816   1797   2194    -40   -449   -319       C  
ATOM   4185  CG2 VAL C 364      16.051   5.482 -77.663  1.00 16.32           C  
ANISOU 4185  CG2 VAL C 364     1891   1944   2367   -198   -359   -362       C  
ATOM   4186  N   PRO C 365      12.676   7.101 -80.591  1.00 20.93           N  
ANISOU 4186  N   PRO C 365     2290   2620   3041    -44   -824   -275       N  
ATOM   4187  CA  PRO C 365      12.151   7.792 -81.774  1.00 22.34           C  
ANISOU 4187  CA  PRO C 365     2509   2800   3182     24   -988   -241       C  
ATOM   4188  C   PRO C 365      13.191   8.676 -82.463  1.00 21.17           C  
ANISOU 4188  C   PRO C 365     2586   2575   2883     86   -960   -236       C  
ATOM   4189  O   PRO C 365      13.853   9.490 -81.818  1.00 23.64           O  
ANISOU 4189  O   PRO C 365     2946   2852   3185    143   -821   -230       O  
ATOM   4190  CB  PRO C 365      11.008   8.635 -81.205  1.00 26.16           C  
ANISOU 4190  CB  PRO C 365     2789   3338   3811    133   -990   -190       C  
ATOM   4191  CG  PRO C 365      10.529   7.847 -80.034  1.00 21.42           C  
ANISOU 4191  CG  PRO C 365     2004   2792   3341     65   -890   -202       C  
ATOM   4192  CD  PRO C 365      11.778   7.246 -79.430  1.00 19.68           C  
ANISOU 4192  CD  PRO C 365     1922   2521   3036    -14   -746   -251       C  
ATOM   4193  N   GLY C 366      13.350   8.482 -83.765  1.00 24.81           N  
ANISOU 4193  N   GLY C 366     3198   3006   3222     63  -1089   -238       N  
ATOM   4194  CA  GLY C 366      14.275   9.286 -84.536  1.00 24.92           C  
ANISOU 4194  CA  GLY C 366     3433   2946   3088    114  -1058   -224       C  
ATOM   4195  C   GLY C 366      15.610   8.620 -84.791  1.00 25.05           C  
ANISOU 4195  C   GLY C 366     3618   2910   2988     37   -950   -268       C  
ATOM   4196  O   GLY C 366      16.309   8.977 -85.741  1.00 24.90           O  
ANISOU 4196  O   GLY C 366     3798   2834   2830     53   -945   -258       O  
ATOM   4197  N   PHE C 367      15.971   7.646 -83.958  1.00 21.43           N  
ANISOU 4197  N   PHE C 367     3085   2469   2588    -40   -857   -310       N  
ATOM   4198  CA  PHE C 367      17.310   7.064 -84.023  1.00 17.96           C  
ANISOU 4198  CA  PHE C 367     2775   1982   2066    -90   -731   -344       C  
ATOM   4199  C   PHE C 367      17.568   6.251 -85.295  1.00 18.26           C  
ANISOU 4199  C   PHE C 367     2991   1979   1970   -136   -800   -375       C  
ATOM   4200  O   PHE C 367      18.621   6.389 -85.913  1.00 22.30           O  
ANISOU 4200  O   PHE C 367     3670   2437   2367   -124   -712   -376       O  
ATOM   4201  CB  PHE C 367      17.575   6.188 -82.795  1.00 15.59           C  
ANISOU 4201  CB  PHE C 367     2356   1706   1862   -148   -629   -373       C  
ATOM   4202  CG  PHE C 367      18.997   5.704 -82.694  1.00 16.19           C  
ANISOU 4202  CG  PHE C 367     2530   1740   1881   -175   -494   -395       C  
ATOM   4203  CD1 PHE C 367      20.002   6.555 -82.275  1.00 17.27           C  
ANISOU 4203  CD1 PHE C 367     2692   1860   2011   -142   -373   -372       C  
ATOM   4204  CD2 PHE C 367      19.326   4.399 -83.010  1.00 17.04           C  
ANISOU 4204  CD2 PHE C 367     2701   1820   1952   -234   -489   -434       C  
ATOM   4205  CE1 PHE C 367      21.311   6.117 -82.178  1.00 14.07           C  
ANISOU 4205  CE1 PHE C 367     2342   1428   1577   -164   -256   -382       C  
ATOM   4206  CE2 PHE C 367      20.636   3.953 -82.912  1.00 15.28           C  
ANISOU 4206  CE2 PHE C 367     2550   1562   1695   -238   -357   -446       C  
ATOM   4207  CZ  PHE C 367      21.625   4.814 -82.497  1.00 13.44           C  
ANISOU 4207  CZ  PHE C 367     2309   1329   1469   -201   -244   -416       C  
ATOM   4208  N   VAL C 368      16.621   5.407 -85.692  1.00 19.34           N  
ANISOU 4208  N   VAL C 368     3099   2134   2117   -193   -952   -399       N  
ATOM   4209  CA  VAL C 368      16.840   4.566 -86.869  1.00 21.02           C  
ANISOU 4209  CA  VAL C 368     3505   2294   2189   -242  -1015   -436       C  
ATOM   4210  C   VAL C 368      16.598   5.333 -88.166  1.00 25.01           C  
ANISOU 4210  C   VAL C 368     4163   2776   2563   -189  -1120   -399       C  
ATOM   4211  O   VAL C 368      16.742   4.781 -89.255  1.00 28.61           O  
ANISOU 4211  O   VAL C 368     4770   3192   2908   -209  -1132   -404       O  
ATOM   4212  CB  VAL C 368      15.951   3.305 -86.860  1.00 25.05           C  
ANISOU 4212  CB  VAL C 368     3919   2832   2768   -331  -1095   -457       C  
ATOM   4213  CG1 VAL C 368      16.269   2.449 -85.655  1.00 26.92           C  
ANISOU 4213  CG1 VAL C 368     4041   3076   3112   -383   -973   -485       C  
ATOM   4214  CG2 VAL C 368      14.475   3.680 -86.895  1.00 24.12           C  
ANISOU 4214  CG2 VAL C 368     3642   2780   2742   -337  -1287   -425       C  
ATOM   4215  N   ASP C 369      16.226   6.604 -88.047  1.00 23.38           N  
ANISOU 4215  N   ASP C 369     3912   2590   2380   -109  -1175   -349       N  
ATOM   4216  CA  ASP C 369      16.130   7.480 -89.208  1.00 25.03           C  
ANISOU 4216  CA  ASP C 369     4300   2763   2447    -44  -1271   -306       C  
ATOM   4217  C   ASP C 369      17.525   7.853 -89.680  1.00 22.76           C  
ANISOU 4217  C   ASP C 369     4227   2401   2020    -22  -1089   -301       C  
ATOM   4218  O   ASP C 369      17.723   8.272 -90.821  1.00 22.59           O  
ANISOU 4218  O   ASP C 369     4390   2329   1863     11  -1099   -265       O  
ATOM   4219  CB  ASP C 369      15.340   8.747 -88.884  1.00 26.33           C  
ANISOU 4219  CB  ASP C 369     4334   2964   2707     55  -1342   -235       C  
ATOM   4220  CG  ASP C 369      13.906   8.460 -88.494  1.00 32.46           C  
ANISOU 4220  CG  ASP C 369     4874   3822   3636     46  -1516   -226       C  
ATOM   4221  OD1 ASP C 369      13.292   7.557 -89.101  1.00 35.38           O  
ANISOU 4221  OD1 ASP C 369     5244   4210   3988    -30  -1650   -248       O  
ATOM   4222  OD2 ASP C 369      13.402   9.139 -87.574  1.00 34.13           O  
ANISOU 4222  OD2 ASP C 369     4889   4079   4001    115  -1477   -190       O  
ATOM   4223  N   LEU C 370      18.488   7.708 -88.776  1.00 20.21           N  
ANISOU 4223  N   LEU C 370     3829   2078   1771    -38   -887   -317       N  
ATOM   4224  CA  LEU C 370      19.874   8.052 -89.055  1.00 18.51           C  
ANISOU 4224  CA  LEU C 370     3759   1807   1467    -26   -694   -305       C  
ATOM   4225  C   LEU C 370      20.535   6.976 -89.901  1.00 19.08           C  
ANISOU 4225  C   LEU C 370     3971   1839   1438    -63   -620   -336       C  
ATOM   4226  O   LEU C 370      20.056   5.845 -89.958  1.00 19.40           O  
ANISOU 4226  O   LEU C 370     3963   1896   1512   -108   -684   -372       O  
ATOM   4227  CB  LEU C 370      20.642   8.236 -87.744  1.00 18.49           C  
ANISOU 4227  CB  LEU C 370     3591   1828   1605    -34   -526   -303       C  
ATOM   4228  CG  LEU C 370      20.150   9.360 -86.827  1.00 16.38           C  
ANISOU 4228  CG  LEU C 370     3178   1590   1457     11   -541   -262       C  
ATOM   4229  CD1 LEU C 370      20.871   9.282 -85.495  1.00 14.96           C  
ANISOU 4229  CD1 LEU C 370     2855   1432   1396    -18   -399   -275       C  
ATOM   4230  CD2 LEU C 370      20.345  10.730 -87.472  1.00 20.47           C  
ANISOU 4230  CD2 LEU C 370     3833   2053   1893     70   -530   -200       C  
ATOM   4231  N   THR C 371      21.638   7.323 -90.553  1.00 19.23           N  
ANISOU 4231  N   THR C 371     4138   1806   1361    -41   -463   -307       N  
ATOM   4232  CA  THR C 371      22.438   6.317 -91.236  1.00 20.07           C  
ANISOU 4232  CA  THR C 371     4338   1877   1410    -58   -343   -323       C  
ATOM   4233  C   THR C 371      22.989   5.323 -90.224  1.00 19.98           C  
ANISOU 4233  C   THR C 371     4179   1896   1517    -87   -241   -366       C  
ATOM   4234  O   THR C 371      23.149   5.641 -89.048  1.00 17.63           O  
ANISOU 4234  O   THR C 371     3733   1636   1331    -94   -205   -371       O  
ATOM   4235  CB  THR C 371      23.607   6.938 -92.012  1.00 20.42           C  
ANISOU 4235  CB  THR C 371     4540   1864   1356    -28   -166   -277       C  
ATOM   4236  OG1 THR C 371      24.553   7.484 -91.083  1.00 19.65           O  
ANISOU 4236  OG1 THR C 371     4342   1785   1340    -30     -9   -263       O  
ATOM   4237  CG2 THR C 371      23.110   8.029 -92.954  1.00 21.69           C  
ANISOU 4237  CG2 THR C 371     4857   1981   1401      5   -258   -225       C  
ATOM   4238  N   LEU C 372      23.277   4.117 -90.692  1.00 18.27           N  
ANISOU 4238  N   LEU C 372     4018   1653   1271    -99   -198   -393       N  
ATOM   4239  CA  LEU C 372      23.821   3.078 -89.838  1.00 17.41           C  
ANISOU 4239  CA  LEU C 372     3794   1559   1262   -114   -106   -426       C  
ATOM   4240  C   LEU C 372      25.172   3.510 -89.259  1.00 19.30           C  
ANISOU 4240  C   LEU C 372     3977   1803   1553    -85     89   -402       C  
ATOM   4241  O   LEU C 372      25.462   3.248 -88.093  1.00 19.92           O  
ANISOU 4241  O   LEU C 372     3903   1914   1752    -96    130   -416       O  
ATOM   4242  CB  LEU C 372      23.935   1.774 -90.629  1.00 21.35           C  
ANISOU 4242  CB  LEU C 372     4409   2007   1695   -119    -90   -455       C  
ATOM   4243  CG  LEU C 372      24.503   0.543 -89.937  1.00 24.08           C  
ANISOU 4243  CG  LEU C 372     4679   2346   2123   -120      1   -486       C  
ATOM   4244  CD1 LEU C 372      23.666   0.169 -88.731  1.00 26.25           C  
ANISOU 4244  CD1 LEU C 372     4775   2670   2528   -170   -105   -511       C  
ATOM   4245  CD2 LEU C 372      24.572  -0.618 -90.920  1.00 27.14           C  
ANISOU 4245  CD2 LEU C 372     5231   2663   2418   -118     12   -512       C  
ATOM   4246  N   HIS C 373      25.980   4.197 -90.064  1.00 21.16           N  
ANISOU 4246  N   HIS C 373     4333   2003   1703    -55    208   -362       N  
ATOM   4247  CA  HIS C 373      27.254   4.737 -89.580  1.00 17.42           C  
ANISOU 4247  CA  HIS C 373     3796   1536   1286    -41    397   -331       C  
ATOM   4248  C   HIS C 373      27.069   5.729 -88.434  1.00 18.60           C  
ANISOU 4248  C   HIS C 373     3812   1726   1527    -67    363   -325       C  
ATOM   4249  O   HIS C 373      27.805   5.693 -87.448  1.00 17.00           O  
ANISOU 4249  O   HIS C 373     3463   1554   1444    -78    453   -320       O  
ATOM   4250  CB  HIS C 373      28.027   5.427 -90.705  1.00 23.93           C  
ANISOU 4250  CB  HIS C 373     4774   2312   2007    -18    528   -280       C  
ATOM   4251  CG  HIS C 373      29.127   6.313 -90.207  1.00 28.14           C  
ANISOU 4251  CG  HIS C 373     5225   2860   2606    -27    697   -237       C  
ATOM   4252  ND1 HIS C 373      30.302   5.814 -89.686  1.00 35.73           N  
ANISOU 4252  ND1 HIS C 373     6062   3843   3671    -16    865   -231       N  
ATOM   4253  CD2 HIS C 373      29.215   7.661 -90.110  1.00 30.59           C  
ANISOU 4253  CD2 HIS C 373     5549   3168   2904    -52    719   -192       C  
ATOM   4254  CE1 HIS C 373      31.075   6.817 -89.309  1.00 32.06           C  
ANISOU 4254  CE1 HIS C 373     5521   3398   3263    -46    981   -181       C  
ATOM   4255  NE2 HIS C 373      30.438   7.949 -89.552  1.00 33.98           N  
ANISOU 4255  NE2 HIS C 373     5857   3623   3433    -74    900   -157       N  
ATOM   4256  N   ASP C 374      26.104   6.630 -88.577  1.00 18.27           N  
ANISOU 4256  N   ASP C 374     3813   1684   1443    -73    226   -314       N  
ATOM   4257  CA  ASP C 374      25.861   7.630 -87.545  1.00 15.34           C  
ANISOU 4257  CA  ASP C 374     3290   1352   1188    -87    185   -283       C  
ATOM   4258  C   ASP C 374      25.270   6.992 -86.291  1.00 14.21           C  
ANISOU 4258  C   ASP C 374     2958   1263   1180   -107    102   -319       C  
ATOM   4259  O   ASP C 374      25.565   7.430 -85.180  1.00 14.68           O  
ANISOU 4259  O   ASP C 374     2869   1355   1355   -124    134   -301       O  
ATOM   4260  CB  ASP C 374      24.948   8.740 -88.065  1.00 15.92           C  
ANISOU 4260  CB  ASP C 374     3451   1405   1192    -64     62   -250       C  
ATOM   4261  CG  ASP C 374      25.669   9.691 -88.998  1.00 20.58           C  
ANISOU 4261  CG  ASP C 374     4209   1938   1673    -53    168   -192       C  
ATOM   4262  OD1 ASP C 374      26.918   9.666 -89.030  1.00 20.99           O  
ANISOU 4262  OD1 ASP C 374     4257   1979   1739    -74    351   -172       O  
ATOM   4263  OD2 ASP C 374      24.993  10.481 -89.692  1.00 20.66           O  
ANISOU 4263  OD2 ASP C 374     4349   1913   1588    -22     72   -160       O  
ATOM   4264  N   GLN C 375      24.451   5.954 -86.465  1.00 15.86           N  
ANISOU 4264  N   GLN C 375     3187   1472   1366   -116     -2   -369       N  
ATOM   4265  CA  GLN C 375      23.951   5.201 -85.319  1.00 13.87           C  
ANISOU 4265  CA  GLN C 375     2771   1262   1236   -144    -55   -398       C  
ATOM   4266  C   GLN C 375      25.099   4.568 -84.541  1.00 13.22           C  
ANISOU 4266  C   GLN C 375     2604   1186   1232   -150     82   -398       C  
ATOM   4267  O   GLN C 375      25.138   4.627 -83.307  1.00 13.42           O  
ANISOU 4267  O   GLN C 375     2477   1252   1369   -166     86   -389       O  
ATOM   4268  CB  GLN C 375      22.972   4.108 -85.749  1.00 14.50           C  
ANISOU 4268  CB  GLN C 375     2893   1334   1284   -171   -179   -443       C  
ATOM   4269  CG  GLN C 375      21.714   4.597 -86.434  1.00 15.41           C  
ANISOU 4269  CG  GLN C 375     3057   1455   1344   -171   -354   -440       C  
ATOM   4270  CD  GLN C 375      20.826   3.449 -86.870  1.00 16.26           C  
ANISOU 4270  CD  GLN C 375     3163   1567   1447   -213   -469   -467       C  
ATOM   4271  OE1 GLN C 375      20.766   2.409 -86.211  1.00 20.11           O  
ANISOU 4271  OE1 GLN C 375     3564   2065   2014   -253   -448   -493       O  
ATOM   4272  NE2 GLN C 375      20.128   3.630 -87.982  1.00 17.60           N  
ANISOU 4272  NE2 GLN C 375     3439   1724   1523   -210   -594   -458       N  
ATOM   4273  N   VAL C 376      26.034   3.961 -85.265  1.00 15.33           N  
ANISOU 4273  N   VAL C 376     2977   1412   1435   -128    196   -407       N  
ATOM   4274  CA  VAL C 376      27.186   3.334 -84.633  1.00 14.02           C  
ANISOU 4274  CA  VAL C 376     2724   1253   1350   -113    326   -397       C  
ATOM   4275  C   VAL C 376      28.024   4.378 -83.901  1.00 15.40           C  
ANISOU 4275  C   VAL C 376     2768   1470   1614   -124    395   -341       C  
ATOM   4276  O   VAL C 376      28.444   4.159 -82.766  1.00 13.50           O  
ANISOU 4276  O   VAL C 376     2383   1265   1482   -136    407   -328       O  
ATOM   4277  CB  VAL C 376      28.072   2.590 -85.652  1.00 19.60           C  
ANISOU 4277  CB  VAL C 376     3563   1906   1977    -67    458   -406       C  
ATOM   4278  CG1 VAL C 376      29.306   2.052 -84.964  1.00 15.82           C  
ANISOU 4278  CG1 VAL C 376     2968   1439   1604    -34    595   -385       C  
ATOM   4279  CG2 VAL C 376      27.300   1.454 -86.309  1.00 22.38           C  
ANISOU 4279  CG2 VAL C 376     4004   2232   2268    -67    364   -437       C  
ATOM   4280  N   HIS C 377      28.255   5.515 -84.548  1.00 13.58           N  
ANISOU 4280  N   HIS C 377     2604   1229   1329   -126    432   -306       N  
ATOM   4281  CA  HIS C 377      29.014   6.589 -83.923  1.00 13.10           C  
ANISOU 4281  CA  HIS C 377     2438   1192   1346   -158    487   -255       C  
ATOM   4282  C   HIS C 377      28.388   7.075 -82.622  1.00 13.44           C  
ANISOU 4282  C   HIS C 377     2360   1271   1475   -190    380   -259       C  
ATOM   4283  O   HIS C 377      29.093   7.337 -81.646  1.00 14.04           O  
ANISOU 4283  O   HIS C 377     2317   1376   1643   -222    408   -236       O  
ATOM   4284  CB  HIS C 377      29.165   7.779 -84.862  1.00 15.65           C  
ANISOU 4284  CB  HIS C 377     2882   1478   1585   -165    531   -215       C  
ATOM   4285  CG  HIS C 377      29.945   8.905 -84.260  1.00 19.12           C  
ANISOU 4285  CG  HIS C 377     3232   1927   2106   -217    584   -164       C  
ATOM   4286  ND1 HIS C 377      31.317   8.872 -84.130  1.00 25.72           N  
ANISOU 4286  ND1 HIS C 377     3976   2782   3017   -246    719   -124       N  
ATOM   4287  CD2 HIS C 377      29.540  10.068 -83.699  1.00 22.75           C  
ANISOU 4287  CD2 HIS C 377     3675   2376   2591   -251    515   -148       C  
ATOM   4288  CE1 HIS C 377      31.726   9.987 -83.548  1.00 27.80           C  
ANISOU 4288  CE1 HIS C 377     4174   3044   3343   -313    718    -86       C  
ATOM   4289  NE2 HIS C 377      30.669  10.729 -83.275  1.00 23.05           N  
ANISOU 4289  NE2 HIS C 377     3634   2418   2706   -315    599   -104       N  
ATOM   4290  N   LEU C 378      27.067   7.211 -82.611  1.00 11.14           N  
ANISOU 4290  N   LEU C 378     2102    978   1152   -180    259   -285       N  
ATOM   4291  CA  LEU C 378      26.387   7.700 -81.420  1.00 10.85           C  
ANISOU 4291  CA  LEU C 378     1965    970   1188   -195    183   -289       C  
ATOM   4292  C   LEU C 378      26.488   6.697 -80.279  1.00 13.96           C  
ANISOU 4292  C   LEU C 378     2244   1399   1662   -212    177   -309       C  
ATOM   4293  O   LEU C 378      26.750   7.074 -79.141  1.00 15.14           O  
ANISOU 4293  O   LEU C 378     2309   1570   1874   -237    178   -298       O  
ATOM   4294  CB  LEU C 378      24.924   8.015 -81.717  1.00 11.68           C  
ANISOU 4294  CB  LEU C 378     2107   1072   1259   -167     66   -305       C  
ATOM   4295  CG  LEU C 378      24.690   9.249 -82.585  1.00 12.46           C  
ANISOU 4295  CG  LEU C 378     2318   1130   1287   -139     47   -273       C  
ATOM   4296  CD1 LEU C 378      23.202   9.436 -82.818  1.00 14.93           C  
ANISOU 4296  CD1 LEU C 378     2634   1450   1587    -97    -86   -281       C  
ATOM   4297  CD2 LEU C 378      25.306  10.480 -81.944  1.00 11.93           C  
ANISOU 4297  CD2 LEU C 378     2231   1041   1259   -159    103   -241       C  
ATOM   4298  N   LEU C 379      26.289   5.419 -80.587  1.00  9.62           N  
ANISOU 4298  N   LEU C 379     1712    845   1098   -200    170   -337       N  
ATOM   4299  CA  LEU C 379      26.392   4.380 -79.569  1.00 10.18           C  
ANISOU 4299  CA  LEU C 379     1698    935   1235   -212    169   -348       C  
ATOM   4300  C   LEU C 379      27.818   4.209 -79.064  1.00 13.14           C  
ANISOU 4300  C   LEU C 379     2008   1321   1665   -210    253   -316       C  
ATOM   4301  O   LEU C 379      28.030   3.981 -77.876  1.00 16.79           O  
ANISOU 4301  O   LEU C 379     2382   1808   2188   -227    236   -304       O  
ATOM   4302  CB  LEU C 379      25.864   3.051 -80.104  1.00 17.29           C  
ANISOU 4302  CB  LEU C 379     2658   1806   2104   -206    142   -385       C  
ATOM   4303  CG  LEU C 379      24.371   2.864 -79.860  1.00 20.00           C  
ANISOU 4303  CG  LEU C 379     2979   2162   2458   -235     33   -410       C  
ATOM   4304  CD1 LEU C 379      23.835   1.745 -80.727  1.00 27.27           C  
ANISOU 4304  CD1 LEU C 379     3994   3041   3328   -250    -14   -450       C  
ATOM   4305  CD2 LEU C 379      24.108   2.591 -78.378  1.00 19.83           C  
ANISOU 4305  CD2 LEU C 379     2844   2172   2519   -260     27   -401       C  
ATOM   4306  N   GLU C 380      28.790   4.318 -79.966  1.00 11.36           N  
ANISOU 4306  N   GLU C 380     1823   1079   1416   -189    344   -296       N  
ATOM   4307  CA  GLU C 380      30.197   4.247 -79.583  1.00 10.96           C  
ANISOU 4307  CA  GLU C 380     1677   1048   1437   -185    427   -254       C  
ATOM   4308  C   GLU C 380      30.542   5.309 -78.555  1.00 15.67           C  
ANISOU 4308  C   GLU C 380     2180   1680   2094   -242    389   -223       C  
ATOM   4309  O   GLU C 380      31.303   5.072 -77.616  1.00 16.59           O  
ANISOU 4309  O   GLU C 380     2189   1828   2287   -256    382   -197       O  
ATOM   4310  CB  GLU C 380      31.102   4.423 -80.797  1.00 20.39           C  
ANISOU 4310  CB  GLU C 380     2925   2222   2599   -158    554   -230       C  
ATOM   4311  CG  GLU C 380      32.515   3.941 -80.562  1.00 21.76           C  
ANISOU 4311  CG  GLU C 380     2983   2419   2866   -131    655   -186       C  
ATOM   4312  CD  GLU C 380      33.355   3.973 -81.818  1.00 30.93           C  
ANISOU 4312  CD  GLU C 380     4199   3557   3995    -91    814   -162       C  
ATOM   4313  OE1 GLU C 380      33.043   4.774 -82.731  1.00 34.46           O  
ANISOU 4313  OE1 GLU C 380     4765   3977   4351   -112    842   -164       O  
ATOM   4314  OE2 GLU C 380      34.339   3.207 -81.889  1.00 37.69           O  
ANISOU 4314  OE2 GLU C 380     4984   4420   4916    -32    920   -136       O  
ATOM   4315  N   SER C 381      29.969   6.489 -78.745  1.00 12.83           N  
ANISOU 4315  N   SER C 381     1875   1307   1693   -272    356   -228       N  
ATOM   4316  CA ASER C 381      30.233   7.615 -77.866  0.70 12.09           C  
ANISOU 4316  CA ASER C 381     1735   1222   1637   -331    321   -209       C  
ATOM   4317  CA BSER C 381      30.245   7.612 -77.867  0.30 12.72           C  
ANISOU 4317  CA BSER C 381     1814   1302   1717   -331    322   -208       C  
ATOM   4318  C   SER C 381      29.502   7.495 -76.538  1.00 13.40           C  
ANISOU 4318  C   SER C 381     1868   1405   1820   -343    234   -234       C  
ATOM   4319  O   SER C 381      30.005   7.937 -75.499  1.00 14.99           O  
ANISOU 4319  O   SER C 381     2019   1619   2058   -391    202   -221       O  
ATOM   4320  CB ASER C 381      29.837   8.928 -78.547  0.70 15.14           C  
ANISOU 4320  CB ASER C 381     2218   1566   1967   -347    325   -203       C  
ATOM   4321  CB BSER C 381      29.867   8.924 -78.556  0.30 14.31           C  
ANISOU 4321  CB BSER C 381     2113   1461   1864   -347    327   -202       C  
ATOM   4322  OG ASER C 381      30.111  10.040 -77.712  0.70 18.33           O  
ANISOU 4322  OG ASER C 381     2605   1958   2402   -409    295   -191       O  
ATOM   4323  OG BSER C 381      30.536   9.057 -79.797  0.30 14.31           O  
ANISOU 4323  OG BSER C 381     2165   1440   1831   -341    423   -173       O  
ATOM   4324  N   ALA C 382      28.316   6.894 -76.575  1.00 10.46           N  
ANISOU 4324  N   ALA C 382     1529   1029   1416   -306    196   -268       N  
ATOM   4325  CA  ALA C 382      27.405   6.956 -75.438  1.00  9.60           C  
ANISOU 4325  CA  ALA C 382     1404    932   1313   -313    138   -289       C  
ATOM   4326  C   ALA C 382      27.238   5.690 -74.601  1.00 11.31           C  
ANISOU 4326  C   ALA C 382     1574   1169   1555   -309    122   -295       C  
ATOM   4327  O   ALA C 382      26.672   5.765 -73.517  1.00 10.62           O  
ANISOU 4327  O   ALA C 382     1477   1091   1469   -322     94   -304       O  
ATOM   4328  CB  ALA C 382      26.030   7.396 -75.927  1.00 11.70           C  
ANISOU 4328  CB  ALA C 382     1718   1182   1543   -281    107   -313       C  
ATOM   4329  N   TRP C 383      27.705   4.540 -75.079  1.00 10.80           N  
ANISOU 4329  N   TRP C 383     1498   1101   1503   -287    149   -289       N  
ATOM   4330  CA  TRP C 383      27.282   3.277 -74.464  1.00 10.08           C  
ANISOU 4330  CA  TRP C 383     1395   1009   1427   -280    132   -296       C  
ATOM   4331  C   TRP C 383      27.643   3.161 -72.975  1.00  8.94           C  
ANISOU 4331  C   TRP C 383     1209    883   1305   -302    106   -272       C  
ATOM   4332  O   TRP C 383      26.834   2.680 -72.194  1.00  9.95           O  
ANISOU 4332  O   TRP C 383     1347   1010   1425   -313     89   -280       O  
ATOM   4333  CB  TRP C 383      27.839   2.063 -75.238  1.00 12.87           C  
ANISOU 4333  CB  TRP C 383     1769   1334   1786   -243    173   -294       C  
ATOM   4334  CG  TRP C 383      29.315   1.853 -75.115  1.00 14.21           C  
ANISOU 4334  CG  TRP C 383     1883   1513   2001   -216    217   -252       C  
ATOM   4335  CD1 TRP C 383      30.286   2.387 -75.909  1.00 20.43           C  
ANISOU 4335  CD1 TRP C 383     2652   2308   2803   -201    278   -231       C  
ATOM   4336  CD2 TRP C 383      29.992   1.059 -74.133  1.00 11.62           C  
ANISOU 4336  CD2 TRP C 383     1501   1193   1722   -199    203   -217       C  
ATOM   4337  NE1 TRP C 383      31.529   1.976 -75.481  1.00 19.35           N  
ANISOU 4337  NE1 TRP C 383     2424   2191   2736   -176    305   -184       N  
ATOM   4338  CE2 TRP C 383      31.373   1.156 -74.390  1.00 16.94           C  
ANISOU 4338  CE2 TRP C 383     2100   1886   2451   -168    248   -174       C  
ATOM   4339  CE3 TRP C 383      29.563   0.268 -73.059  1.00 14.13           C  
ANISOU 4339  CE3 TRP C 383     1827   1501   2042   -205    158   -209       C  
ATOM   4340  CZ2 TRP C 383      32.330   0.508 -73.609  1.00 15.46           C  
ANISOU 4340  CZ2 TRP C 383     1832   1714   2329   -134    230   -123       C  
ATOM   4341  CZ3 TRP C 383      30.515  -0.386 -72.292  1.00 12.82           C  
ANISOU 4341  CZ3 TRP C 383     1611   1339   1920   -172    143   -159       C  
ATOM   4342  CH2 TRP C 383      31.880  -0.263 -72.572  1.00 13.59           C  
ANISOU 4342  CH2 TRP C 383     1622   1462   2081   -133    169   -116       C  
ATOM   4343  N   LEU C 384      28.825   3.617 -72.568  1.00  8.59           N  
ANISOU 4343  N   LEU C 384     1121    856   1284   -315     99   -240       N  
ATOM   4344  CA  LEU C 384      29.195   3.477 -71.159  1.00  8.78           C  
ANISOU 4344  CA  LEU C 384     1126    897   1314   -339     49   -215       C  
ATOM   4345  C   LEU C 384      28.433   4.483 -70.284  1.00  8.63           C  
ANISOU 4345  C   LEU C 384     1157    877   1246   -378     21   -240       C  
ATOM   4346  O   LEU C 384      28.071   4.168 -69.154  1.00 12.92           O  
ANISOU 4346  O   LEU C 384     1732   1420   1758   -389     -2   -237       O  
ATOM   4347  CB  LEU C 384      30.699   3.638 -70.956  1.00  9.41           C  
ANISOU 4347  CB  LEU C 384     1130   1002   1444   -350     25   -169       C  
ATOM   4348  CG  LEU C 384      31.158   3.381 -69.515  1.00 14.01           C  
ANISOU 4348  CG  LEU C 384     1700   1601   2022   -373    -57   -137       C  
ATOM   4349  CD1 LEU C 384      30.760   1.957 -69.055  1.00 11.57           C  
ANISOU 4349  CD1 LEU C 384     1420   1273   1703   -325    -55   -122       C  
ATOM   4350  CD2 LEU C 384      32.655   3.634 -69.377  1.00 10.76           C  
ANISOU 4350  CD2 LEU C 384     1184   1225   1680   -393   -104    -85       C  
ATOM   4351  N   GLU C 385      28.180   5.681 -70.814  1.00  8.75           N  
ANISOU 4351  N   GLU C 385     1198    881   1246   -391     34   -262       N  
ATOM   4352  CA  GLU C 385      27.291   6.635 -70.139  1.00  8.75           C  
ANISOU 4352  CA  GLU C 385     1261    864   1200   -403     29   -292       C  
ATOM   4353  C   GLU C 385      25.915   6.030 -69.892  1.00  8.55           C  
ANISOU 4353  C   GLU C 385     1245    841   1163   -371     58   -311       C  
ATOM   4354  O   GLU C 385      25.323   6.215 -68.829  1.00 11.87           O  
ANISOU 4354  O   GLU C 385     1705   1256   1548   -375     70   -322       O  
ATOM   4355  CB  GLU C 385      27.099   7.907 -70.960  1.00 10.31           C  
ANISOU 4355  CB  GLU C 385     1493   1033   1390   -401     46   -308       C  
ATOM   4356  CG  GLU C 385      28.305   8.782 -71.151  1.00 15.48           C  
ANISOU 4356  CG  GLU C 385     2150   1674   2057   -454     29   -289       C  
ATOM   4357  CD  GLU C 385      27.993   9.934 -72.082  1.00 30.65           C  
ANISOU 4357  CD  GLU C 385     4128   3553   3964   -446     57   -298       C  
ATOM   4358  OE1 GLU C 385      27.703  11.047 -71.588  1.00 18.81           O  
ANISOU 4358  OE1 GLU C 385     2707   2007   2432   -462     47   -317       O  
ATOM   4359  OE2 GLU C 385      27.989   9.688 -73.311  1.00 27.92           O  
ANISOU 4359  OE2 GLU C 385     3769   3212   3629   -416     90   -285       O  
ATOM   4360  N   ILE C 386      25.392   5.332 -70.898  1.00  8.82           N  
ANISOU 4360  N   ILE C 386     1247    879   1224   -344     74   -316       N  
ATOM   4361  CA  ILE C 386      24.065   4.736 -70.801  1.00  9.14           C  
ANISOU 4361  CA  ILE C 386     1272    926   1275   -331     92   -329       C  
ATOM   4362  C   ILE C 386      24.044   3.637 -69.743  1.00  9.01           C  
ANISOU 4362  C   ILE C 386     1257    911   1255   -353    103   -311       C  
ATOM   4363  O   ILE C 386      23.107   3.558 -68.953  1.00 11.24           O  
ANISOU 4363  O   ILE C 386     1543   1198   1529   -359    137   -314       O  
ATOM   4364  CB  ILE C 386      23.600   4.179 -72.161  1.00 12.48           C  
ANISOU 4364  CB  ILE C 386     1675   1346   1721   -317     80   -340       C  
ATOM   4365  CG1 ILE C 386      23.454   5.326 -73.161  1.00 16.04           C  
ANISOU 4365  CG1 ILE C 386     2146   1791   2159   -290     66   -351       C  
ATOM   4366  CG2 ILE C 386      22.284   3.405 -72.017  1.00 14.39           C  
ANISOU 4366  CG2 ILE C 386     1879   1597   1991   -330     82   -349       C  
ATOM   4367  CD1 ILE C 386      22.413   6.338 -72.773  1.00 25.98           C  
ANISOU 4367  CD1 ILE C 386     3396   3053   3420   -262     71   -360       C  
ATOM   4368  N   LEU C 387      25.077   2.799 -69.726  1.00 10.35           N  
ANISOU 4368  N   LEU C 387     1427   1074   1432   -357     84   -286       N  
ATOM   4369  CA  LEU C 387      25.204   1.794 -68.674  1.00 10.56           C  
ANISOU 4369  CA  LEU C 387     1476   1090   1446   -370     84   -257       C  
ATOM   4370  C   LEU C 387      25.266   2.453 -67.303  1.00 10.50           C  
ANISOU 4370  C   LEU C 387     1518   1089   1381   -389     77   -249       C  
ATOM   4371  O   LEU C 387      24.645   1.981 -66.355  1.00 12.26           O  
ANISOU 4371  O   LEU C 387     1783   1305   1572   -403    108   -237       O  
ATOM   4372  CB  LEU C 387      26.446   0.920 -68.871  1.00 11.11           C  
ANISOU 4372  CB  LEU C 387     1534   1147   1540   -349     57   -222       C  
ATOM   4373  CG  LEU C 387      26.439  -0.095 -70.018  1.00 11.30           C  
ANISOU 4373  CG  LEU C 387     1553   1140   1601   -323     79   -230       C  
ATOM   4374  CD1 LEU C 387      27.712  -0.925 -69.981  1.00 15.84           C  
ANISOU 4374  CD1 LEU C 387     2118   1697   2203   -279     70   -189       C  
ATOM   4375  CD2 LEU C 387      25.214  -0.982 -69.954  1.00 12.93           C  
ANISOU 4375  CD2 LEU C 387     1788   1317   1809   -352    100   -243       C  
ATOM   4376  N   MET C 388      26.005   3.553 -67.205  1.00  9.38           N  
ANISOU 4376  N   MET C 388     1388    956   1221   -398     40   -256       N  
ATOM   4377  CA  MET C 388      26.185   4.224 -65.920  1.00  9.76           C  
ANISOU 4377  CA  MET C 388     1514    997   1196   -425     17   -256       C  
ATOM   4378  C   MET C 388      24.908   4.895 -65.408  1.00  9.96           C  
ANISOU 4378  C   MET C 388     1597   1010   1177   -415     89   -291       C  
ATOM   4379  O   MET C 388      24.602   4.806 -64.220  1.00 11.83           O  
ANISOU 4379  O   MET C 388     1918   1235   1342   -425    114   -287       O  
ATOM   4380  CB  MET C 388      27.312   5.247 -66.014  1.00  9.95           C  
ANISOU 4380  CB  MET C 388     1538   1022   1219   -456    -50   -258       C  
ATOM   4381  CG  MET C 388      28.695   4.616 -66.045  1.00 10.24           C  
ANISOU 4381  CG  MET C 388     1512   1081   1299   -467   -125   -209       C  
ATOM   4382  SD  MET C 388      29.997   5.845 -66.190  1.00 12.23           S  
ANISOU 4382  SD  MET C 388     1730   1341   1575   -529   -202   -203       S  
ATOM   4383  CE  MET C 388      31.457   4.874 -65.809  1.00 11.56           C  
ANISOU 4383  CE  MET C 388     1548   1296   1549   -528   -297   -130       C  
ATOM   4384  N   ILE C 389      24.160   5.570 -66.278  1.00 11.58           N  
ANISOU 4384  N   ILE C 389     1764   1215   1420   -386    129   -320       N  
ATOM   4385  CA  ILE C 389      22.934   6.204 -65.809  1.00 10.62           C  
ANISOU 4385  CA  ILE C 389     1675   1084   1277   -355    208   -346       C  
ATOM   4386  C   ILE C 389      21.896   5.142 -65.434  1.00 10.90           C  
ANISOU 4386  C   ILE C 389     1670   1137   1333   -352    278   -329       C  
ATOM   4387  O   ILE C 389      21.108   5.346 -64.515  1.00 13.02           O  
ANISOU 4387  O   ILE C 389     1984   1400   1564   -339    361   -333       O  
ATOM   4388  CB  ILE C 389      22.347   7.208 -66.840  1.00 11.05           C  
ANISOU 4388  CB  ILE C 389     1691   1132   1375   -309    223   -371       C  
ATOM   4389  CG1 ILE C 389      21.274   8.076 -66.164  1.00 11.23           C  
ANISOU 4389  CG1 ILE C 389     1760   1134   1372   -258    309   -396       C  
ATOM   4390  CG2 ILE C 389      21.818   6.503 -68.091  1.00 12.78           C  
ANISOU 4390  CG2 ILE C 389     1803   1381   1673   -295    210   -362       C  
ATOM   4391  CD1 ILE C 389      20.704   9.159 -67.043  1.00 11.35           C  
ANISOU 4391  CD1 ILE C 389     1753   1132   1426   -194    317   -412       C  
ATOM   4392  N   GLY C 390      21.922   4.000 -66.117  1.00 11.75           N  
ANISOU 4392  N   GLY C 390     1707   1259   1499   -370    253   -308       N  
ATOM   4393  CA  GLY C 390      21.061   2.890 -65.756  1.00 13.22           C  
ANISOU 4393  CA  GLY C 390     1863   1450   1710   -393    309   -285       C  
ATOM   4394  C   GLY C 390      21.393   2.400 -64.360  1.00 11.47           C  
ANISOU 4394  C   GLY C 390     1743   1209   1408   -417    337   -255       C  
ATOM   4395  O   GLY C 390      20.504   2.198 -63.530  1.00 12.71           O  
ANISOU 4395  O   GLY C 390     1923   1363   1541   -426    431   -243       O  
ATOM   4396  N   LEU C 391      22.687   2.226 -64.107  1.00 11.64           N  
ANISOU 4396  N   LEU C 391     1821   1216   1384   -426    254   -238       N  
ATOM   4397  CA  LEU C 391      23.180   1.777 -62.807  1.00 12.12           C  
ANISOU 4397  CA  LEU C 391     1994   1256   1354   -445    242   -202       C  
ATOM   4398  C   LEU C 391      22.800   2.747 -61.695  1.00 12.84           C  
ANISOU 4398  C   LEU C 391     2198   1338   1343   -443    296   -223       C  
ATOM   4399  O   LEU C 391      22.368   2.343 -60.611  1.00 15.49           O  
ANISOU 4399  O   LEU C 391     2631   1655   1601   -456    362   -200       O  
ATOM   4400  CB  LEU C 391      24.701   1.605 -62.855  1.00 11.98           C  
ANISOU 4400  CB  LEU C 391     1986   1237   1327   -446    118   -176       C  
ATOM   4401  CG  LEU C 391      25.392   1.337 -61.518  1.00 13.49           C  
ANISOU 4401  CG  LEU C 391     2299   1412   1416   -462     60   -135       C  
ATOM   4402  CD1 LEU C 391      24.932   0.015 -60.939  1.00 13.40           C  
ANISOU 4402  CD1 LEU C 391     2340   1370   1381   -466    109    -84       C  
ATOM   4403  CD2 LEU C 391      26.895   1.335 -61.701  1.00 13.93           C  
ANISOU 4403  CD2 LEU C 391     2316   1481   1496   -459    -77   -107       C  
ATOM   4404  N   VAL C 392      22.965   4.033 -61.974  1.00 12.11           N  
ANISOU 4404  N   VAL C 392     2113   1246   1243   -427    276   -268       N  
ATOM   4405  CA  VAL C 392      22.627   5.058 -61.000  1.00 12.94           C  
ANISOU 4405  CA  VAL C 392     2349   1323   1245   -416    331   -300       C  
ATOM   4406  C   VAL C 392      21.129   5.034 -60.699  1.00 13.54           C  
ANISOU 4406  C   VAL C 392     2411   1402   1332   -380    496   -307       C  
ATOM   4407  O   VAL C 392      20.728   5.124 -59.543  1.00 16.78           O  
ANISOU 4407  O   VAL C 392     2950   1788   1639   -376    585   -306       O  
ATOM   4408  CB  VAL C 392      23.057   6.453 -61.489  1.00 14.62           C  
ANISOU 4408  CB  VAL C 392     2578   1518   1460   -407    281   -348       C  
ATOM   4409  CG1 VAL C 392      22.458   7.532 -60.625  1.00 21.81           C  
ANISOU 4409  CG1 VAL C 392     3632   2382   2273   -379    367   -392       C  
ATOM   4410  CG2 VAL C 392      24.570   6.561 -61.470  1.00 16.73           C  
ANISOU 4410  CG2 VAL C 392     2869   1782   1705   -461    129   -335       C  
ATOM   4411  N   TRP C 393      20.315   4.871 -61.741  1.00 14.26           N  
ANISOU 4411  N   TRP C 393     2343   1525   1549   -355    536   -309       N  
ATOM   4412  CA  TRP C 393      18.857   4.810 -61.610  1.00 14.58           C  
ANISOU 4412  CA  TRP C 393     2312   1584   1643   -323    683   -305       C  
ATOM   4413  C   TRP C 393      18.399   3.645 -60.726  1.00 15.39           C  
ANISOU 4413  C   TRP C 393     2444   1686   1717   -366    771   -258       C  
ATOM   4414  O   TRP C 393      17.570   3.817 -59.828  1.00 18.48           O  
ANISOU 4414  O   TRP C 393     2888   2071   2064   -346    920   -252       O  
ATOM   4415  CB  TRP C 393      18.197   4.707 -62.996  1.00 14.02           C  
ANISOU 4415  CB  TRP C 393     2054   1554   1721   -306    659   -307       C  
ATOM   4416  CG  TRP C 393      16.718   4.432 -62.937  1.00 17.34           C  
ANISOU 4416  CG  TRP C 393     2352   2008   2229   -290    785   -289       C  
ATOM   4417  CD1 TRP C 393      16.090   3.257 -63.247  1.00 20.16           C  
ANISOU 4417  CD1 TRP C 393     2593   2392   2675   -350    799   -253       C  
ATOM   4418  CD2 TRP C 393      15.685   5.339 -62.534  1.00 17.93           C  
ANISOU 4418  CD2 TRP C 393     2399   2090   2322   -213    918   -301       C  
ATOM   4419  NE1 TRP C 393      14.735   3.376 -63.058  1.00 19.84           N  
ANISOU 4419  NE1 TRP C 393     2432   2387   2718   -326    927   -237       N  
ATOM   4420  CE2 TRP C 393      14.459   4.647 -62.624  1.00 20.60           C  
ANISOU 4420  CE2 TRP C 393     2574   2476   2777   -230   1009   -264       C  
ATOM   4421  CE3 TRP C 393      15.675   6.671 -62.115  1.00 19.54           C  
ANISOU 4421  CE3 TRP C 393     2703   2259   2462   -128    973   -339       C  
ATOM   4422  CZ2 TRP C 393      13.238   5.241 -62.296  1.00 22.58           C  
ANISOU 4422  CZ2 TRP C 393     2733   2753   3093   -155   1161   -257       C  
ATOM   4423  CZ3 TRP C 393      14.465   7.258 -61.783  1.00 20.50           C  
ANISOU 4423  CZ3 TRP C 393     2763   2393   2634    -42   1130   -339       C  
ATOM   4424  CH2 TRP C 393      13.265   6.546 -61.880  1.00 22.37           C  
ANISOU 4424  CH2 TRP C 393     2811   2691   3000    -50   1226   -295       C  
ATOM   4425  N   ARG C 394      18.935   2.454 -60.967  1.00 14.05           N  
ANISOU 4425  N   ARG C 394     2255   1514   1569   -422    695   -220       N  
ATOM   4426  CA  ARG C 394      18.478   1.308 -60.190  1.00 14.91           C  
ANISOU 4426  CA  ARG C 394     2403   1608   1654   -470    780   -167       C  
ATOM   4427  C   ARG C 394      19.136   1.254 -58.806  1.00 22.92           C  
ANISOU 4427  C   ARG C 394     3629   2581   2499   -478    786   -144       C  
ATOM   4428  O   ARG C 394      18.757   0.433 -57.974  1.00 20.92           O  
ANISOU 4428  O   ARG C 394     3452   2305   2194   -513    875    -95       O  
ATOM   4429  CB  ARG C 394      18.700  -0.001 -60.961  1.00 24.43           C  
ANISOU 4429  CB  ARG C 394     3531   2806   2946   -522    706   -135       C  
ATOM   4430  CG  ARG C 394      20.136  -0.430 -61.181  1.00 19.31           C  
ANISOU 4430  CG  ARG C 394     2943   2131   2260   -522    558   -123       C  
ATOM   4431  CD  ARG C 394      20.166  -1.635 -62.126  1.00 19.54           C  
ANISOU 4431  CD  ARG C 394     2895   2143   2388   -555    512   -104       C  
ATOM   4432  NE  ARG C 394      21.518  -2.011 -62.527  1.00 14.82           N  
ANISOU 4432  NE  ARG C 394     2327   1523   1780   -531    388    -94       N  
ATOM   4433  CZ  ARG C 394      22.057  -1.708 -63.703  1.00 11.81           C  
ANISOU 4433  CZ  ARG C 394     1867   1158   1461   -503    312   -127       C  
ATOM   4434  NH1 ARG C 394      21.360  -1.023 -64.600  1.00 14.31           N  
ANISOU 4434  NH1 ARG C 394     2088   1510   1841   -499    329   -172       N  
ATOM   4435  NH2 ARG C 394      23.293  -2.094 -63.980  1.00 16.40           N  
ANISOU 4435  NH2 ARG C 394     2466   1722   2042   -474    225   -109       N  
ATOM   4436  N   SER C 395      20.093   2.144 -58.554  1.00 22.33           N  
ANISOU 4436  N   SER C 395     3657   2493   2335   -455    688   -177       N  
ATOM   4437  CA  SER C 395      20.699   2.249 -57.226  1.00 19.44           C  
ANISOU 4437  CA  SER C 395     3508   2088   1791   -467    668   -163       C  
ATOM   4438  C   SER C 395      20.096   3.362 -56.369  1.00 19.67           C  
ANISOU 4438  C   SER C 395     3673   2093   1708   -432    792   -208       C  
ATOM   4439  O   SER C 395      20.522   3.564 -55.231  1.00 20.84           O  
ANISOU 4439  O   SER C 395     4035   2200   1683   -444    780   -206       O  
ATOM   4440  CB  SER C 395      22.213   2.472 -57.327  1.00 16.02           C  
ANISOU 4440  CB  SER C 395     3120   1650   1319   -482    464   -165       C  
ATOM   4441  OG  SER C 395      22.838   1.498 -58.138  1.00 15.88           O  
ANISOU 4441  OG  SER C 395     2981   1647   1404   -493    365   -126       O  
ATOM   4442  N   MET C 396      19.114   4.079 -56.908  1.00 17.36           N  
ANISOU 4442  N   MET C 396     3268   1820   1507   -382    908   -246       N  
ATOM   4443  CA  MET C 396      18.553   5.248 -56.227  1.00 23.94           C  
ANISOU 4443  CA  MET C 396     4227   2621   2250   -323   1036   -296       C  
ATOM   4444  C   MET C 396      18.049   4.961 -54.821  1.00 26.03           C  
ANISOU 4444  C   MET C 396     4630   2848   2411   -316   1146   -259       C  
ATOM   4445  O   MET C 396      18.226   5.772 -53.911  1.00 29.11           O  
ANISOU 4445  O   MET C 396     5185   3185   2692   -288   1136   -282       O  
ATOM   4446  CB  MET C 396      17.418   5.852 -57.052  1.00 28.28           C  
ANISOU 4446  CB  MET C 396     4592   3203   2951   -251   1152   -320       C  
ATOM   4447  CG  MET C 396      17.042   7.266 -56.629  1.00 34.40           C  
ANISOU 4447  CG  MET C 396     5446   3934   3692   -164   1200   -361       C  
ATOM   4448  SD  MET C 396      16.133   8.115 -57.923  1.00 43.77           S  
ANISOU 4448  SD  MET C 396     6420   5155   5057    -70   1252   -390       S  
ATOM   4449  CE  MET C 396      17.092   7.526 -59.301  1.00 28.97           C  
ANISOU 4449  CE  MET C 396     4417   3319   3270   -144   1054   -388       C  
ATOM   4450  N   GLU C 397      17.428   3.804 -54.644  1.00 29.73           N  
ANISOU 4450  N   GLU C 397     5035   3338   2923   -347   1242   -200       N  
ATOM   4451  CA  GLU C 397      16.831   3.464 -53.364  1.00 30.61           C  
ANISOU 4451  CA  GLU C 397     5261   3414   2954   -339   1361   -162       C  
ATOM   4452  C   GLU C 397      17.751   2.584 -52.534  1.00 28.71           C  
ANISOU 4452  C   GLU C 397     5203   3134   2573   -400   1259   -117       C  
ATOM   4453  O   GLU C 397      17.308   1.919 -51.601  1.00 34.47           O  
ANISOU 4453  O   GLU C 397     6015   3837   3247   -411   1349    -71       O  
ATOM   4454  CB  GLU C 397      15.490   2.769 -53.576  1.00 33.61           C  
ANISOU 4454  CB  GLU C 397     5454   3837   3477   -339   1529   -119       C  
ATOM   4455  CG  GLU C 397      14.504   3.604 -54.364  1.00 34.13           C  
ANISOU 4455  CG  GLU C 397     5321   3950   3696   -269   1616   -151       C  
ATOM   4456  CD  GLU C 397      13.113   3.014 -54.353  1.00 37.64           C  
ANISOU 4456  CD  GLU C 397     5583   4441   4278   -269   1772   -102       C  
ATOM   4457  OE1 GLU C 397      12.492   2.932 -55.433  1.00 43.97           O  
ANISOU 4457  OE1 GLU C 397     6146   5305   5255   -270   1772    -98       O  
ATOM   4458  OE2 GLU C 397      12.638   2.638 -53.260  1.00 44.10           O  
ANISOU 4458  OE2 GLU C 397     6493   5234   5028   -274   1888    -66       O  
ATOM   4459  N   HIS C 398      19.033   2.578 -52.879  1.00 26.86           N  
ANISOU 4459  N   HIS C 398     5024   2897   2285   -435   1065   -125       N  
ATOM   4460  CA  HIS C 398      20.017   1.858 -52.086  1.00 25.24           C  
ANISOU 4460  CA  HIS C 398     4986   2655   1947   -477    931    -76       C  
ATOM   4461  C   HIS C 398      21.188   2.767 -51.730  1.00 23.76           C  
ANISOU 4461  C   HIS C 398     4932   2443   1654   -481    743   -115       C  
ATOM   4462  O   HIS C 398      22.276   2.631 -52.289  1.00 27.84           O  
ANISOU 4462  O   HIS C 398     5418   2983   2178   -513    560   -108       O  
ATOM   4463  CB  HIS C 398      20.500   0.618 -52.837  1.00 26.42           C  
ANISOU 4463  CB  HIS C 398     5048   2829   2160   -526    854    -14       C  
ATOM   4464  CG  HIS C 398      19.400  -0.337 -53.176  1.00 30.27           C  
ANISOU 4464  CG  HIS C 398     5399   3330   2774   -545   1014     29       C  
ATOM   4465  ND1 HIS C 398      18.734  -0.304 -54.383  1.00 32.63           N  
ANISOU 4465  ND1 HIS C 398     5477   3675   3245   -552   1082      9       N  
ATOM   4466  CD2 HIS C 398      18.841  -1.345 -52.465  1.00 31.14           C  
ANISOU 4466  CD2 HIS C 398     5553   3409   2871   -566   1106     90       C  
ATOM   4467  CE1 HIS C 398      17.812  -1.250 -54.399  1.00 27.42           C  
ANISOU 4467  CE1 HIS C 398     4722   3015   2682   -584   1195     55       C  
ATOM   4468  NE2 HIS C 398      17.859  -1.899 -53.250  1.00 33.90           N  
ANISOU 4468  NE2 HIS C 398     5701   3787   3391   -594   1217    104       N  
ATOM   4469  N   PRO C 399      20.959   3.700 -50.791  1.00 27.64           N  
ANISOU 4469  N   PRO C 399     5564   2884   2055   -452    785   -152       N  
ATOM   4470  CA  PRO C 399      21.973   4.663 -50.349  1.00 26.81           C  
ANISOU 4470  CA  PRO C 399     5586   2742   1860   -470    613   -187       C  
ATOM   4471  C   PRO C 399      23.285   3.991 -49.952  1.00 26.30           C  
ANISOU 4471  C   PRO C 399     5601   2675   1716   -525    391   -138       C  
ATOM   4472  O   PRO C 399      23.278   3.025 -49.186  1.00 27.55           O  
ANISOU 4472  O   PRO C 399     5858   2813   1797   -533    398    -81       O  
ATOM   4473  CB  PRO C 399      21.313   5.336 -49.139  1.00 31.38           C  
ANISOU 4473  CB  PRO C 399     6344   3251   2330   -434    737   -210       C  
ATOM   4474  CG  PRO C 399      19.851   5.178 -49.373  1.00 33.46           C  
ANISOU 4474  CG  PRO C 399     6496   3533   2682   -376    985   -209       C  
ATOM   4475  CD  PRO C 399      19.697   3.850 -50.046  1.00 30.04           C  
ANISOU 4475  CD  PRO C 399     5913   3159   2341   -406   1005   -154       C  
ATOM   4476  N   GLY C 400      24.391   4.498 -50.490  1.00 25.51           N  
ANISOU 4476  N   GLY C 400     5444   2597   1650   -559    194   -156       N  
ATOM   4477  CA  GLY C 400      25.715   4.007 -50.159  1.00 26.13           C  
ANISOU 4477  CA  GLY C 400     5560   2684   1683   -604    -40   -106       C  
ATOM   4478  C   GLY C 400      26.123   2.754 -50.908  1.00 26.17           C  
ANISOU 4478  C   GLY C 400     5441   2743   1760   -607   -108    -42       C  
ATOM   4479  O   GLY C 400      27.226   2.236 -50.712  1.00 28.23           O  
ANISOU 4479  O   GLY C 400     5703   3017   2008   -626   -306     14       O  
ATOM   4480  N   LYS C 401      25.236   2.250 -51.760  1.00 22.72           N  
ANISOU 4480  N   LYS C 401     4893   2333   1408   -584     54    -41       N  
ATOM   4481  CA  LYS C 401      25.539   1.043 -52.526  1.00 21.76           C  
ANISOU 4481  CA  LYS C 401     4647   2245   1376   -581      9     26       C  
ATOM   4482  C   LYS C 401      25.175   1.160 -54.001  1.00 23.24           C  
ANISOU 4482  C   LYS C 401     4569   2476   1784   -559     73    -12       C  
ATOM   4483  O   LYS C 401      24.379   2.011 -54.398  1.00 21.86           O  
ANISOU 4483  O   LYS C 401     4348   2309   1649   -548    196    -79       O  
ATOM   4484  CB  LYS C 401      24.821  -0.163 -51.926  1.00 23.69           C  
ANISOU 4484  CB  LYS C 401     4985   2453   1562   -574    141    100       C  
ATOM   4485  CG  LYS C 401      25.151  -0.388 -50.462  1.00 24.84           C  
ANISOU 4485  CG  LYS C 401     5325   2547   1567   -571     77    135       C  
ATOM   4486  CD  LYS C 401      24.486  -1.633 -49.916  1.00 27.60           C  
ANISOU 4486  CD  LYS C 401     5739   2855   1892   -562    203    206       C  
ATOM   4487  CE  LYS C 401      24.751  -1.786 -48.425  1.00 29.84           C  
ANISOU 4487  CE  LYS C 401     6236   3085   2017   -559    151    233       C  
ATOM   4488  NZ  LYS C 401      23.997  -2.928 -47.845  1.00 36.54           N  
ANISOU 4488  NZ  LYS C 401     7158   3889   2839   -554    297    295       N  
ATOM   4489  N   LEU C 402      25.758   0.284 -54.808  1.00 18.23           N  
ANISOU 4489  N   LEU C 402     3775   1865   1288   -543    -10     35       N  
ATOM   4490  CA  LEU C 402      25.467   0.268 -56.232  1.00 16.72           C  
ANISOU 4490  CA  LEU C 402     3360   1707   1286   -524     39      4       C  
ATOM   4491  C   LEU C 402      24.855  -1.073 -56.613  1.00 16.50           C  
ANISOU 4491  C   LEU C 402     3269   1661   1340   -514    131     52       C  
ATOM   4492  O   LEU C 402      25.455  -2.122 -56.390  1.00 18.39           O  
ANISOU 4492  O   LEU C 402     3540   1873   1574   -503     58    122       O  
ATOM   4493  CB  LEU C 402      26.734   0.540 -57.040  1.00 17.63           C  
ANISOU 4493  CB  LEU C 402     3341   1858   1501   -517   -127      1       C  
ATOM   4494  CG  LEU C 402      27.278   1.970 -56.945  1.00 17.39           C  
ANISOU 4494  CG  LEU C 402     3336   1842   1428   -548   -212    -56       C  
ATOM   4495  CD1 LEU C 402      28.539   2.123 -57.773  1.00 16.40           C  
ANISOU 4495  CD1 LEU C 402     3054   1756   1422   -551   -358    -43       C  
ATOM   4496  CD2 LEU C 402      26.238   2.984 -57.394  1.00 15.57           C  
ANISOU 4496  CD2 LEU C 402     3090   1608   1217   -544    -72   -134       C  
ATOM   4497  N   LEU C 403      23.653  -1.029 -57.178  1.00 16.29           N  
ANISOU 4497  N   LEU C 403     3156   1643   1392   -521    285     19       N  
ATOM   4498  CA  LEU C 403      22.959  -2.244 -57.590  1.00 18.92           C  
ANISOU 4498  CA  LEU C 403     3426   1952   1811   -537    371     57       C  
ATOM   4499  C   LEU C 403      23.332  -2.560 -59.031  1.00 15.07           C  
ANISOU 4499  C   LEU C 403     2767   1480   1477   -519    304     37       C  
ATOM   4500  O   LEU C 403      22.622  -2.196 -59.964  1.00 14.36           O  
ANISOU 4500  O   LEU C 403     2553   1420   1485   -525    359    -11       O  
ATOM   4501  CB  LEU C 403      21.443  -2.085 -57.432  1.00 17.51           C  
ANISOU 4501  CB  LEU C 403     3225   1779   1648   -564    563     38       C  
ATOM   4502  CG  LEU C 403      20.509  -3.297 -57.570  1.00 17.19           C  
ANISOU 4502  CG  LEU C 403     3143   1708   1681   -614    675     83       C  
ATOM   4503  CD1 LEU C 403      19.251  -3.052 -56.774  1.00 26.81           C  
ANISOU 4503  CD1 LEU C 403     4401   2931   2856   -641    870     90       C  
ATOM   4504  CD2 LEU C 403      20.126  -3.586 -59.008  1.00 25.44           C  
ANISOU 4504  CD2 LEU C 403     3996   2773   2898   -628    657     51       C  
ATOM   4505  N   PHE C 404      24.471  -3.218 -59.210  1.00 14.84           N  
ANISOU 4505  N   PHE C 404     2740   1433   1466   -490    183     78       N  
ATOM   4506  CA  PHE C 404      24.914  -3.597 -60.548  1.00 13.96           C  
ANISOU 4506  CA  PHE C 404     2495   1326   1485   -462    137     62       C  
ATOM   4507  C   PHE C 404      23.914  -4.569 -61.148  1.00 16.07           C  
ANISOU 4507  C   PHE C 404     2728   1552   1827   -495    232     62       C  
ATOM   4508  O   PHE C 404      23.604  -4.503 -62.339  1.00 15.23           O  
ANISOU 4508  O   PHE C 404     2513   1459   1815   -498    242     16       O  
ATOM   4509  CB  PHE C 404      26.312  -4.204 -60.507  1.00 14.30           C  
ANISOU 4509  CB  PHE C 404     2546   1350   1537   -408     11    116       C  
ATOM   4510  CG  PHE C 404      27.393  -3.193 -60.255  1.00 14.32           C  
ANISOU 4510  CG  PHE C 404     2525   1405   1511   -391   -108    111       C  
ATOM   4511  CD1 PHE C 404      27.922  -2.451 -61.298  1.00 14.34           C  
ANISOU 4511  CD1 PHE C 404     2395   1453   1601   -376   -142     67       C  
ATOM   4512  CD2 PHE C 404      27.864  -2.967 -58.971  1.00 20.26           C  
ANISOU 4512  CD2 PHE C 404     3400   2157   2142   -401   -190    150       C  
ATOM   4513  CE1 PHE C 404      28.914  -1.516 -61.071  1.00 15.49           C  
ANISOU 4513  CE1 PHE C 404     2510   1643   1733   -382   -250     65       C  
ATOM   4514  CE2 PHE C 404      28.852  -2.025 -58.735  1.00 19.86           C  
ANISOU 4514  CE2 PHE C 404     3326   2151   2069   -407   -319    142       C  
ATOM   4515  CZ  PHE C 404      29.377  -1.302 -59.785  1.00 16.61           C  
ANISOU 4515  CZ  PHE C 404     2763   1784   1764   -403   -347    101       C  
ATOM   4516  N   ALA C 405      23.414  -5.460 -60.297  1.00 14.82           N  
ANISOU 4516  N   ALA C 405     2677   1338   1617   -530    295    116       N  
ATOM   4517  CA  ALA C 405      22.368  -6.415 -60.637  1.00 15.20           C  
ANISOU 4517  CA  ALA C 405     2710   1337   1728   -591    391    126       C  
ATOM   4518  C   ALA C 405      21.606  -6.725 -59.350  1.00 16.61           C  
ANISOU 4518  C   ALA C 405     3009   1485   1816   -644    501    179       C  
ATOM   4519  O   ALA C 405      22.106  -6.434 -58.260  1.00 17.03           O  
ANISOU 4519  O   ALA C 405     3188   1538   1743   -617    479    214       O  
ATOM   4520  CB  ALA C 405      22.966  -7.679 -61.252  1.00 15.66           C  
ANISOU 4520  CB  ALA C 405     2792   1315   1841   -570    337    155       C  
ATOM   4521  N   PRO C 406      20.389  -7.292 -59.460  1.00 19.45           N  
ANISOU 4521  N   PRO C 406     3334   1820   2235   -726    622    186       N  
ATOM   4522  CA  PRO C 406      19.641  -7.608 -58.239  1.00 18.56           C  
ANISOU 4522  CA  PRO C 406     3335   1678   2039   -781    757    245       C  
ATOM   4523  C   PRO C 406      20.386  -8.588 -57.339  1.00 19.80           C  
ANISOU 4523  C   PRO C 406     3688   1746   2088   -764    718    330       C  
ATOM   4524  O   PRO C 406      20.182  -8.584 -56.125  1.00 24.46           O  
ANISOU 4524  O   PRO C 406     4401   2334   2561   -762    778    370       O  
ATOM   4525  CB  PRO C 406      18.348  -8.232 -58.773  1.00 20.38           C  
ANISOU 4525  CB  PRO C 406     3432   1912   2398   -857    842    233       C  
ATOM   4526  CG  PRO C 406      18.171  -7.607 -60.111  1.00 17.91           C  
ANISOU 4526  CG  PRO C 406     2949   1653   2205   -858    790    160       C  
ATOM   4527  CD  PRO C 406      19.565  -7.493 -60.666  1.00 21.15           C  
ANISOU 4527  CD  PRO C 406     3398   2046   2592   -780    643    140       C  
ATOM   4528  N   ASN C 407      21.244  -9.411 -57.935  1.00 19.06           N  
ANISOU 4528  N   ASN C 407     3611   1591   2040   -728    606    350       N  
ATOM   4529  CA  ASN C 407      22.066 -10.348 -57.184  1.00 21.08           C  
ANISOU 4529  CA  ASN C 407     4038   1762   2209   -683    542    435       C  
ATOM   4530  C   ASN C 407      23.519  -9.885 -57.091  1.00 19.60           C  
ANISOU 4530  C   ASN C 407     3870   1605   1973   -574    374    444       C  
ATOM   4531  O   ASN C 407      24.422 -10.680 -56.834  1.00 21.55           O  
ANISOU 4531  O   ASN C 407     4210   1784   2193   -510    282    512       O  
ATOM   4532  CB  ASN C 407      21.985 -11.742 -57.814  1.00 20.54           C  
ANISOU 4532  CB  ASN C 407     3961   1608   2237   -691    534    450       C  
ATOM   4533  CG  ASN C 407      22.549 -11.779 -59.223  1.00 19.38           C  
ANISOU 4533  CG  ASN C 407     3716   1445   2204   -655    455    398       C  
ATOM   4534  OD1 ASN C 407      22.640 -10.752 -59.892  1.00 18.15           O  
ANISOU 4534  OD1 ASN C 407     3429   1377   2091   -638    425    329       O  
ATOM   4535  ND2 ASN C 407      22.922 -12.971 -59.683  1.00 22.27           N  
ANISOU 4535  ND2 ASN C 407     4125   1719   2619   -620    419    418       N  
ATOM   4536  N   LEU C 408      23.743  -8.590 -57.295  1.00 18.91           N  
ANISOU 4536  N   LEU C 408     3681   1620   1884   -551    331    376       N  
ATOM   4537  CA  LEU C 408      25.082  -8.038 -57.154  1.00 18.69           C  
ANISOU 4537  CA  LEU C 408     3646   1634   1820   -469    168    382       C  
ATOM   4538  C   LEU C 408      25.013  -6.586 -56.680  1.00 18.38           C  
ANISOU 4538  C   LEU C 408     3603   1680   1702   -485    159    329       C  
ATOM   4539  O   LEU C 408      25.196  -5.647 -57.456  1.00 17.28           O  
ANISOU 4539  O   LEU C 408     3326   1607   1632   -474    126    258       O  
ATOM   4540  CB  LEU C 408      25.848  -8.147 -58.474  1.00 17.69           C  
ANISOU 4540  CB  LEU C 408     3363   1523   1835   -409     88    348       C  
ATOM   4541  CG  LEU C 408      27.354  -7.900 -58.387  1.00 20.10           C  
ANISOU 4541  CG  LEU C 408     3635   1862   2141   -321    -78    379       C  
ATOM   4542  CD1 LEU C 408      27.986  -8.873 -57.412  1.00 22.08           C  
ANISOU 4542  CD1 LEU C 408     4034   2042   2315   -270   -155    487       C  
ATOM   4543  CD2 LEU C 408      27.979  -8.045 -59.761  1.00 19.87           C  
ANISOU 4543  CD2 LEU C 408     3449   1843   2257   -261   -106    345       C  
ATOM   4544  N   LEU C 409      24.724  -6.428 -55.393  1.00 18.68           N  
ANISOU 4544  N   LEU C 409     3816   1701   1581   -511    197    364       N  
ATOM   4545  CA  LEU C 409      24.655  -5.130 -54.735  1.00 22.45           C  
ANISOU 4545  CA  LEU C 409     4353   2231   1946   -524    196    316       C  
ATOM   4546  C   LEU C 409      25.936  -4.913 -53.933  1.00 23.84           C  
ANISOU 4546  C   LEU C 409     4643   2409   2004   -490      2    357       C  
ATOM   4547  O   LEU C 409      26.199  -5.641 -52.979  1.00 25.65           O  
ANISOU 4547  O   LEU C 409     5048   2585   2114   -482    -40    440       O  
ATOM   4548  CB  LEU C 409      23.429  -5.066 -53.819  1.00 21.94           C  
ANISOU 4548  CB  LEU C 409     4426   2140   1769   -575    387    323       C  
ATOM   4549  CG  LEU C 409      23.164  -3.803 -52.998  1.00 24.12           C  
ANISOU 4549  CG  LEU C 409     4818   2446   1901   -582    434    271       C  
ATOM   4550  CD1 LEU C 409      22.799  -2.620 -53.882  1.00 24.37           C  
ANISOU 4550  CD1 LEU C 409     4679   2540   2039   -573    469    172       C  
ATOM   4551  CD2 LEU C 409      22.073  -4.076 -51.972  1.00 28.01           C  
ANISOU 4551  CD2 LEU C 409     5434   2902   2305   -604    623    290       C  
ATOM   4552  N   LEU C 410      26.733  -3.922 -54.319  1.00 20.50           N  
ANISOU 4552  N   LEU C 410     4125   2047   1616   -477   -126    306       N  
ATOM   4553  CA  LEU C 410      28.037  -3.717 -53.691  1.00 23.80           C  
ANISOU 4553  CA  LEU C 410     4606   2479   1957   -457   -342    348       C  
ATOM   4554  C   LEU C 410      28.099  -2.392 -52.936  1.00 22.01           C  
ANISOU 4554  C   LEU C 410     4499   2276   1587   -504   -390    290       C  
ATOM   4555  O   LEU C 410      27.530  -1.398 -53.381  1.00 23.95           O  
ANISOU 4555  O   LEU C 410     4687   2547   1864   -530   -296    203       O  
ATOM   4556  CB  LEU C 410      29.143  -3.763 -54.746  1.00 24.11           C  
ANISOU 4556  CB  LEU C 410     4427   2564   2170   -410   -475    352       C  
ATOM   4557  CG  LEU C 410      29.150  -5.005 -55.643  1.00 27.78           C  
ANISOU 4557  CG  LEU C 410     4781   2994   2781   -352   -424    393       C  
ATOM   4558  CD1 LEU C 410      30.183  -4.855 -56.746  1.00 29.92           C  
ANISOU 4558  CD1 LEU C 410     4838   3315   3217   -301   -516    382       C  
ATOM   4559  CD2 LEU C 410      29.382  -6.273 -54.829  1.00 30.08           C  
ANISOU 4559  CD2 LEU C 410     5220   3211   2999   -311   -466    501       C  
ATOM   4560  N   ASP C 411      28.784  -2.374 -51.795  1.00 26.10           N  
ANISOU 4560  N   ASP C 411     5201   2777   1940   -515   -542    339       N  
ATOM   4561  CA  ASP C 411      29.002  -1.117 -51.085  1.00 28.49           C  
ANISOU 4561  CA  ASP C 411     5616   3088   2121   -564   -614    274       C  
ATOM   4562  C   ASP C 411      30.397  -0.579 -51.383  1.00 31.71           C  
ANISOU 4562  C   ASP C 411     5896   3549   2605   -579   -859    276       C  
ATOM   4563  O   ASP C 411      31.107  -1.115 -52.233  1.00 30.98           O  
ANISOU 4563  O   ASP C 411     5609   3495   2667   -541   -946    323       O  
ATOM   4564  CB  ASP C 411      28.794  -1.274 -49.571  1.00 32.70           C  
ANISOU 4564  CB  ASP C 411     6362   3561   2500   -566   -594    289       C  
ATOM   4565  CG  ASP C 411      29.772  -2.246 -48.922  1.00 35.53           C  
ANISOU 4565  CG  ASP C 411     6763   3907   2829   -533   -777    388       C  
ATOM   4566  OD1 ASP C 411      30.705  -2.741 -49.587  1.00 38.03           O  
ANISOU 4566  OD1 ASP C 411     6928   4262   3258   -499   -931    448       O  
ATOM   4567  OD2 ASP C 411      29.605  -2.506 -47.711  1.00 39.67           O  
ANISOU 4567  OD2 ASP C 411     7473   4381   3220   -533   -764    408       O  
ATOM   4568  N   ARG C 412      30.787   0.468 -50.664  1.00 33.75           N  
ANISOU 4568  N   ARG C 412     6219   3800   2804   -626   -939    224       N  
ATOM   4569  CA  ARG C 412      32.026   1.185 -50.951  1.00 37.91           C  
ANISOU 4569  CA  ARG C 412     6604   4376   3425   -664  -1141    216       C  
ATOM   4570  C   ARG C 412      33.285   0.325 -50.881  1.00 36.41           C  
ANISOU 4570  C   ARG C 412     6301   4225   3309   -629  -1353    318       C  
ATOM   4571  O   ARG C 412      34.087   0.324 -51.812  1.00 37.82           O  
ANISOU 4571  O   ARG C 412     6255   4464   3649   -620  -1450    341       O  
ATOM   4572  CB  ARG C 412      32.173   2.369 -49.999  1.00 37.93           C  
ANISOU 4572  CB  ARG C 412     6741   4339   3330   -725  -1180    157       C  
ATOM   4573  CG  ARG C 412      31.397   3.593 -50.427  1.00 35.39           C  
ANISOU 4573  CG  ARG C 412     6434   3997   3017   -753  -1027     57       C  
ATOM   4574  CD  ARG C 412      32.008   4.826 -49.806  1.00 37.37           C  
ANISOU 4574  CD  ARG C 412     6752   4219   3228   -819  -1132     18       C  
ATOM   4575  NE  ARG C 412      33.410   4.948 -50.192  1.00 37.74           N  
ANISOU 4575  NE  ARG C 412     6618   4327   3396   -861  -1345     56       N  
ATOM   4576  CZ  ARG C 412      34.136   6.050 -50.046  1.00 40.91           C  
ANISOU 4576  CZ  ARG C 412     7003   4723   3820   -934  -1449     27       C  
ATOM   4577  NH1 ARG C 412      33.594   7.141 -49.521  1.00 44.17           N  
ANISOU 4577  NH1 ARG C 412     7588   5063   4130   -966  -1368    -41       N  
ATOM   4578  NH2 ARG C 412      35.407   6.061 -50.429  1.00 40.95           N  
ANISOU 4578  NH2 ARG C 412     6814   4792   3953   -971  -1626     72       N  
ATOM   4579  N   ASN C 413      33.466  -0.393 -49.777  1.00 39.58           N  
ANISOU 4579  N   ASN C 413     6846   4590   3603   -601  -1416    380       N  
ATOM   4580  CA  ASN C 413      34.640  -1.244 -49.621  1.00 39.13           C  
ANISOU 4580  CA  ASN C 413     6683   4567   3619   -548  -1612    483       C  
ATOM   4581  C   ASN C 413      34.685  -2.342 -50.681  1.00 38.44           C  
ANISOU 4581  C   ASN C 413     6436   4499   3671   -457  -1578    556       C  
ATOM   4582  O   ASN C 413      35.752  -2.665 -51.205  1.00 42.23           O  
ANISOU 4582  O   ASN C 413     6707   5032   4306   -408  -1717    617       O  
ATOM   4583  CB  ASN C 413      34.682  -1.844 -48.216  1.00 40.95           C  
ANISOU 4583  CB  ASN C 413     7126   4744   3689   -529  -1666    534       C  
ATOM   4584  CG  ASN C 413      34.915  -0.793 -47.146  1.00 45.89           C  
ANISOU 4584  CG  ASN C 413     7900   5347   4187   -613  -1749    478       C  
ATOM   4585  OD1 ASN C 413      35.886  -0.037 -47.207  1.00 50.22           O  
ANISOU 4585  OD1 ASN C 413     8334   5941   4807   -664  -1912    465       O  
ATOM   4586  ND2 ASN C 413      34.027  -0.741 -46.157  1.00 49.51           N  
ANISOU 4586  ND2 ASN C 413     8619   5729   4463   -628  -1628    447       N  
ATOM   4587  N   GLU C 419      38.509  -3.249 -59.836  1.00 29.88           N  
ANISOU 4587  N   GLU C 419     3565   3719   4067    -59  -1242    600       N  
ATOM   4588  CA  GLU C 419      39.546  -2.512 -60.546  1.00 28.68           C  
ANISOU 4588  CA  GLU C 419     3169   3652   4076    -82  -1275    610       C  
ATOM   4589  C   GLU C 419      38.961  -1.349 -61.357  1.00 27.75           C  
ANISOU 4589  C   GLU C 419     3049   3543   3949   -190  -1148    503       C  
ATOM   4590  O   GLU C 419      37.896  -1.466 -61.972  1.00 28.18           O  
ANISOU 4590  O   GLU C 419     3207   3545   3956   -180   -977    431       O  
ATOM   4591  CB  GLU C 419      40.351  -3.462 -61.449  1.00 27.84           C  
ANISOU 4591  CB  GLU C 419     2868   3554   4154     75  -1196    677       C  
ATOM   4592  CG  GLU C 419      39.659  -3.877 -62.736  1.00 29.52           C  
ANISOU 4592  CG  GLU C 419     3104   3710   4402    137   -952    611       C  
ATOM   4593  CD  GLU C 419      40.514  -4.792 -63.598  1.00 31.00           C  
ANISOU 4593  CD  GLU C 419     3126   3893   4758    301   -864    673       C  
ATOM   4594  OE1 GLU C 419      40.868  -4.392 -64.727  1.00 31.10           O  
ANISOU 4594  OE1 GLU C 419     3000   3939   4878    310   -738    645       O  
ATOM   4595  OE2 GLU C 419      40.827  -5.913 -63.148  1.00 33.17           O  
ANISOU 4595  OE2 GLU C 419     3426   4125   5054    428   -911    751       O  
ATOM   4596  N   GLY C 420      39.656  -0.215 -61.325  1.00 29.25           N  
ANISOU 4596  N   GLY C 420     3128   3797   4188   -298  -1247    497       N  
ATOM   4597  CA  GLY C 420      39.251   0.962 -62.074  1.00 30.48           C  
ANISOU 4597  CA  GLY C 420     3282   3956   4344   -399  -1144    410       C  
ATOM   4598  C   GLY C 420      38.216   1.842 -61.392  1.00 27.66           C  
ANISOU 4598  C   GLY C 420     3152   3552   3805   -510  -1157    324       C  
ATOM   4599  O   GLY C 420      37.818   2.870 -61.940  1.00 25.55           O  
ANISOU 4599  O   GLY C 420     2906   3274   3526   -587  -1078    253       O  
ATOM   4600  N   MET C 421      37.793   1.457 -60.190  1.00 25.08           N  
ANISOU 4600  N   MET C 421     3005   3193   3331   -511  -1247    335       N  
ATOM   4601  CA  MET C 421      36.667   2.121 -59.536  1.00 23.52           C  
ANISOU 4601  CA  MET C 421     3044   2940   2952   -585  -1212    254       C  
ATOM   4602  C   MET C 421      37.053   2.928 -58.299  1.00 25.70           C  
ANISOU 4602  C   MET C 421     3444   3216   3104   -699  -1408    250       C  
ATOM   4603  O   MET C 421      36.181   3.287 -57.510  1.00 28.82           O  
ANISOU 4603  O   MET C 421     4070   3557   3323   -739  -1386    195       O  
ATOM   4604  CB  MET C 421      35.604   1.088 -59.140  1.00 25.04           C  
ANISOU 4604  CB  MET C 421     3397   3076   3042   -507  -1111    255       C  
ATOM   4605  CG  MET C 421      34.940   0.393 -60.321  1.00 19.21           C  
ANISOU 4605  CG  MET C 421     2593   2316   2391   -422   -915    234       C  
ATOM   4606  SD  MET C 421      33.218  -0.096 -60.073  1.00 28.26           S  
ANISOU 4606  SD  MET C 421     3936   3390   3411   -407   -749    184       S  
ATOM   4607  CE  MET C 421      32.398   1.485 -60.300  1.00 23.68           C  
ANISOU 4607  CE  MET C 421     3414   2809   2775   -497   -674     78       C  
ATOM   4608  N   VAL C 422      38.343   3.216 -58.132  1.00 28.72           N  
ANISOU 4608  N   VAL C 422     3680   3654   3581   -736  -1556    302       N  
ATOM   4609  CA  VAL C 422      38.833   3.886 -56.920  1.00 30.50           C  
ANISOU 4609  CA  VAL C 422     4020   3866   3701   -807  -1680    297       C  
ATOM   4610  C   VAL C 422      38.175   5.254 -56.712  1.00 30.14           C  
ANISOU 4610  C   VAL C 422     4144   3763   3545   -898  -1601    195       C  
ATOM   4611  O   VAL C 422      37.950   5.676 -55.580  1.00 37.15           O  
ANISOU 4611  O   VAL C 422     5234   4603   4279   -939  -1653    169       O  
ATOM   4612  CB  VAL C 422      40.383   4.054 -56.941  1.00 31.52           C  
ANISOU 4612  CB  VAL C 422     3929   4068   3981   -829  -1812    362       C  
ATOM   4613  CG1 VAL C 422      40.825   4.899 -58.125  1.00 33.26           C  
ANISOU 4613  CG1 VAL C 422     3964   4321   4353   -877  -1719    334       C  
ATOM   4614  CG2 VAL C 422      40.897   4.650 -55.622  1.00 34.87           C  
ANISOU 4614  CG2 VAL C 422     4482   4475   4292   -910  -1970    359       C  
ATOM   4615  N   GLU C 423      37.851   5.933 -57.807  1.00 31.92           N  
ANISOU 4615  N   GLU C 423     4295   3986   3848   -916  -1467    141       N  
ATOM   4616  CA  GLU C 423      37.190   7.232 -57.733  1.00 28.28           C  
ANISOU 4616  CA  GLU C 423     3984   3464   3298   -974  -1375     53       C  
ATOM   4617  C   GLU C 423      35.769   7.165 -58.300  1.00 21.88           C  
ANISOU 4617  C   GLU C 423     3267   2609   2436   -923  -1194     -9       C  
ATOM   4618  O   GLU C 423      34.874   7.869 -57.837  1.00 22.23           O  
ANISOU 4618  O   GLU C 423     3495   2592   2359   -929  -1113    -72       O  
ATOM   4619  CB  GLU C 423      37.997   8.300 -58.481  1.00 29.19           C  
ANISOU 4619  CB  GLU C 423     3959   3599   3533  -1040  -1369     41       C  
ATOM   4620  CG  GLU C 423      39.462   8.391 -58.078  1.00 31.05           C  
ANISOU 4620  CG  GLU C 423     4059   3888   3850  -1099  -1538    103       C  
ATOM   4621  CD  GLU C 423      40.155   9.615 -58.661  1.00 37.71           C  
ANISOU 4621  CD  GLU C 423     4811   4734   4782  -1188  -1524     81       C  
ATOM   4622  OE1 GLU C 423      39.633  10.187 -59.643  1.00 41.16           O  
ANISOU 4622  OE1 GLU C 423     5240   5145   5253  -1183  -1376     35       O  
ATOM   4623  OE2 GLU C 423      41.224  10.008 -58.140  1.00 40.10           O  
ANISOU 4623  OE2 GLU C 423     5054   5062   5120  -1265  -1665    112       O  
ATOM   4624  N   ILE C 424      35.568   6.312 -59.299  1.00 22.28           N  
ANISOU 4624  N   ILE C 424     3186   2692   2588   -869  -1129     12       N  
ATOM   4625  CA  ILE C 424      34.295   6.244 -60.011  1.00 18.28           C  
ANISOU 4625  CA  ILE C 424     2736   2149   2062   -829   -961    -47       C  
ATOM   4626  C   ILE C 424      33.135   5.766 -59.131  1.00 18.07           C  
ANISOU 4626  C   ILE C 424     2912   2076   1879   -790   -898    -73       C  
ATOM   4627  O   ILE C 424      32.013   6.268 -59.255  1.00 18.25           O  
ANISOU 4627  O   ILE C 424     3038   2055   1842   -775   -760   -138       O  
ATOM   4628  CB  ILE C 424      34.423   5.336 -61.254  1.00 18.82           C  
ANISOU 4628  CB  ILE C 424     2610   2257   2283   -743   -867     -8       C  
ATOM   4629  CG1 ILE C 424      35.388   5.964 -62.267  1.00 23.30           C  
ANISOU 4629  CG1 ILE C 424     2995   2861   2996   -788   -879      7       C  
ATOM   4630  CG2 ILE C 424      33.073   5.096 -61.901  1.00 20.18           C  
ANISOU 4630  CG2 ILE C 424     2836   2397   2436   -674   -680    -57       C  
ATOM   4631  CD1 ILE C 424      35.800   5.036 -63.388  1.00 22.98           C  
ANISOU 4631  CD1 ILE C 424     2770   2862   3101   -694   -792     56       C  
ATOM   4632  N   PHE C 425      33.403   4.813 -58.242  1.00 20.59           N  
ANISOU 4632  N   PHE C 425     3283   2405   2137   -763   -985    -13       N  
ATOM   4633  CA  PHE C 425      32.366   4.298 -57.348  1.00 20.37           C  
ANISOU 4633  CA  PHE C 425     3451   2331   1957   -726   -906    -22       C  
ATOM   4634  C   PHE C 425      31.700   5.431 -56.569  1.00 18.34           C  
ANISOU 4634  C   PHE C 425     3403   2017   1547   -776   -863    -96       C  
ATOM   4635  O   PHE C 425      30.475   5.526 -56.526  1.00 17.73           O  
ANISOU 4635  O   PHE C 425     3430   1903   1404   -744   -699   -145       O  
ATOM   4636  CB  PHE C 425      32.944   3.267 -56.375  1.00 23.86           C  
ANISOU 4636  CB  PHE C 425     3952   2781   2334   -704  -1040     63       C  
ATOM   4637  CG  PHE C 425      31.927   2.293 -55.850  1.00 20.54           C  
ANISOU 4637  CG  PHE C 425     3667   2320   1818   -642   -915     83       C  
ATOM   4638  CD1 PHE C 425      31.072   2.650 -54.819  1.00 26.22           C  
ANISOU 4638  CD1 PHE C 425     4629   2988   2348   -670   -851     45       C  
ATOM   4639  CD2 PHE C 425      31.826   1.022 -56.387  1.00 21.66           C  
ANISOU 4639  CD2 PHE C 425     3704   2466   2059   -561   -849    141       C  
ATOM   4640  CE1 PHE C 425      30.136   1.755 -54.335  1.00 25.05           C  
ANISOU 4640  CE1 PHE C 425     4596   2803   2120   -625   -717     72       C  
ATOM   4641  CE2 PHE C 425      30.892   0.123 -55.909  1.00 24.25           C  
ANISOU 4641  CE2 PHE C 425     4158   2748   2307   -524   -732    164       C  
ATOM   4642  CZ  PHE C 425      30.045   0.495 -54.882  1.00 24.04           C  
ANISOU 4642  CZ  PHE C 425     4353   2680   2101   -560   -663    134       C  
ATOM   4643  N   ASP C 426      32.516   6.289 -55.965  1.00 20.26           N  
ANISOU 4643  N   ASP C 426     3671   2254   1773   -826   -971    -92       N  
ATOM   4644  CA  ASP C 426      32.001   7.414 -55.196  1.00 22.50           C  
ANISOU 4644  CA  ASP C 426     4131   2474   1943   -846   -909   -146       C  
ATOM   4645  C   ASP C 426      31.279   8.423 -56.087  1.00 19.51           C  
ANISOU 4645  C   ASP C 426     3717   2073   1622   -829   -761   -213       C  
ATOM   4646  O   ASP C 426      30.303   9.042 -55.664  1.00 19.69           O  
ANISOU 4646  O   ASP C 426     3882   2040   1557   -800   -637   -260       O  
ATOM   4647  CB  ASP C 426      33.130   8.110 -54.431  1.00 26.74           C  
ANISOU 4647  CB  ASP C 426     4702   3003   2455   -919  -1076   -128       C  
ATOM   4648  CG  ASP C 426      33.619   7.296 -53.251  1.00 28.68           C  
ANISOU 4648  CG  ASP C 426     5047   3247   2603   -925  -1212    -70       C  
ATOM   4649  OD1 ASP C 426      32.858   6.431 -52.772  1.00 24.74           O  
ANISOU 4649  OD1 ASP C 426     4664   2728   2009   -873  -1140    -56       O  
ATOM   4650  OD2 ASP C 426      34.752   7.538 -52.779  1.00 31.16           O  
ANISOU 4650  OD2 ASP C 426     5329   3578   2934   -983  -1387    -36       O  
ATOM   4651  N   MET C 427      31.759   8.589 -57.316  1.00 19.50           N  
ANISOU 4651  N   MET C 427     3524   2114   1771   -837   -769   -210       N  
ATOM   4652  CA  MET C 427      31.112   9.504 -58.249  1.00 18.53           C  
ANISOU 4652  CA  MET C 427     3365   1969   1706   -811   -639   -261       C  
ATOM   4653  C   MET C 427      29.717   8.991 -58.590  1.00 17.36           C  
ANISOU 4653  C   MET C 427     3245   1809   1541   -736   -476   -291       C  
ATOM   4654  O   MET C 427      28.758   9.765 -58.663  1.00 17.20           O  
ANISOU 4654  O   MET C 427     3294   1749   1494   -695   -354   -336       O  
ATOM   4655  CB  MET C 427      31.939   9.678 -59.527  1.00 17.89           C  
ANISOU 4655  CB  MET C 427     3080   1932   1784   -834   -671   -243       C  
ATOM   4656  CG  MET C 427      33.285  10.367 -59.342  1.00 19.22           C  
ANISOU 4656  CG  MET C 427     3194   2113   1994   -915   -805   -217       C  
ATOM   4657  SD  MET C 427      34.261  10.362 -60.856  1.00 21.14           S  
ANISOU 4657  SD  MET C 427     3187   2415   2431   -936   -809   -183       S  
ATOM   4658  CE  MET C 427      33.556  11.780 -61.674  1.00 32.55           C  
ANISOU 4658  CE  MET C 427     4689   3798   3880   -925   -677   -243       C  
ATOM   4659  N   LEU C 428      29.608   7.681 -58.793  1.00 15.91           N  
ANISOU 4659  N   LEU C 428     3006   1658   1380   -719   -477   -262       N  
ATOM   4660  CA  LEU C 428      28.326   7.065 -59.109  1.00 15.01           C  
ANISOU 4660  CA  LEU C 428     2904   1537   1264   -660   -322   -285       C  
ATOM   4661  C   LEU C 428      27.346   7.198 -57.943  1.00 15.86           C  
ANISOU 4661  C   LEU C 428     3205   1599   1223   -636   -223   -309       C  
ATOM   4662  O   LEU C 428      26.175   7.516 -58.148  1.00 15.55           O  
ANISOU 4662  O   LEU C 428     3183   1540   1186   -584    -66   -348       O  
ATOM   4663  CB  LEU C 428      28.521   5.596 -59.484  1.00 14.46           C  
ANISOU 4663  CB  LEU C 428     2701   1515   1279   -619   -327   -216       C  
ATOM   4664  CG  LEU C 428      29.181   5.365 -60.844  1.00 13.56           C  
ANISOU 4664  CG  LEU C 428     2384   1443   1326   -605   -352   -194       C  
ATOM   4665  CD1 LEU C 428      29.659   3.935 -60.967  1.00 13.52           C  
ANISOU 4665  CD1 LEU C 428     2290   1466   1381   -565   -385   -124       C  
ATOM   4666  CD2 LEU C 428      28.234   5.701 -61.984  1.00 12.47           C  
ANISOU 4666  CD2 LEU C 428     2176   1302   1261   -564   -222   -235       C  
ATOM   4667  N   LEU C 429      27.833   6.961 -56.726  1.00 16.86           N  
ANISOU 4667  N   LEU C 429     3463   1711   1231   -665   -309   -276       N  
ATOM   4668  CA  LEU C 429      27.008   7.111 -55.527  1.00 17.99           C  
ANISOU 4668  CA  LEU C 429     3796   1805   1233   -639   -207   -286       C  
ATOM   4669  C   LEU C 429      26.492   8.534 -55.371  1.00 18.50           C  
ANISOU 4669  C   LEU C 429     3928   1821   1282   -615   -124   -338       C  
ATOM   4670  O   LEU C 429      25.345   8.751 -54.976  1.00 20.40           O  
ANISOU 4670  O   LEU C 429     4249   2027   1474   -559     41   -362       O  
ATOM   4671  CB  LEU C 429      27.782   6.726 -54.264  1.00 20.66           C  
ANISOU 4671  CB  LEU C 429     4271   2127   1451   -677   -340   -238       C  
ATOM   4672  CG  LEU C 429      28.132   5.257 -54.036  1.00 22.18           C  
ANISOU 4672  CG  LEU C 429     4463   2350   1615   -679   -411   -169       C  
ATOM   4673  CD1 LEU C 429      29.032   5.129 -52.812  1.00 21.91           C  
ANISOU 4673  CD1 LEU C 429     4553   2294   1478   -713   -574   -120       C  
ATOM   4674  CD2 LEU C 429      26.874   4.411 -53.883  1.00 21.53           C  
ANISOU 4674  CD2 LEU C 429     4443   2256   1482   -633   -217   -160       C  
ATOM   4675  N   ALA C 430      27.357   9.500 -55.657  1.00 18.28           N  
ANISOU 4675  N   ALA C 430     3863   1786   1296   -657   -235   -349       N  
ATOM   4676  CA  ALA C 430      26.991  10.908 -55.567  1.00 18.91           C  
ANISOU 4676  CA  ALA C 430     4018   1808   1357   -640   -175   -394       C  
ATOM   4677  C   ALA C 430      25.877  11.232 -56.557  1.00 17.81           C  
ANISOU 4677  C   ALA C 430     3789   1671   1305   -562    -17   -427       C  
ATOM   4678  O   ALA C 430      24.997  12.042 -56.273  1.00 21.73           O  
ANISOU 4678  O   ALA C 430     4374   2117   1766   -505    102   -459       O  
ATOM   4679  CB  ALA C 430      28.205  11.790 -55.818  1.00 22.08           C  
ANISOU 4679  CB  ALA C 430     4382   2205   1800   -714   -324   -391       C  
ATOM   4680  N   THR C 431      25.908  10.580 -57.712  1.00 17.52           N  
ANISOU 4680  N   THR C 431     3579   1691   1385   -554    -19   -416       N  
ATOM   4681  CA  THR C 431      24.902  10.817 -58.736  1.00 20.43           C  
ANISOU 4681  CA  THR C 431     3851   2065   1845   -484    107   -443       C  
ATOM   4682  C   THR C 431      23.561  10.240 -58.301  1.00 15.99           C  
ANISOU 4682  C   THR C 431     3325   1500   1248   -417    274   -452       C  
ATOM   4683  O   THR C 431      22.517  10.853 -58.499  1.00 16.42           O  
ANISOU 4683  O   THR C 431     3373   1534   1331   -341    402   -478       O  
ATOM   4684  CB  THR C 431      25.319  10.209 -60.081  1.00 20.08           C  
ANISOU 4684  CB  THR C 431     3623   2074   1931   -499     57   -427       C  
ATOM   4685  OG1 THR C 431      26.641  10.649 -60.409  1.00 20.22           O  
ANISOU 4685  OG1 THR C 431     3592   2103   1988   -563    -83   -407       O  
ATOM   4686  CG2 THR C 431      24.354  10.628 -61.191  1.00 15.59           C  
ANISOU 4686  CG2 THR C 431     2968   1503   1454   -430    160   -453       C  
ATOM   4687  N   SER C 432      23.599   9.057 -57.700  1.00 19.11           N  
ANISOU 4687  N   SER C 432     3753   1919   1588   -444    277   -424       N  
ATOM   4688  CA  SER C 432      22.377   8.410 -57.247  1.00 18.25           C  
ANISOU 4688  CA  SER C 432     3667   1815   1453   -394    451   -419       C  
ATOM   4689  C   SER C 432      21.752   9.241 -56.135  1.00 18.91           C  
ANISOU 4689  C   SER C 432     3899   1841   1443   -348    550   -431       C  
ATOM   4690  O   SER C 432      20.534   9.420 -56.079  1.00 22.85           O  
ANISOU 4690  O   SER C 432     4370   2337   1974   -272    721   -439       O  
ATOM   4691  CB  SER C 432      22.669   6.982 -56.776  1.00 25.31           C  
ANISOU 4691  CB  SER C 432     4591   2735   2291   -441    426   -373       C  
ATOM   4692  OG  SER C 432      21.550   6.133 -56.975  1.00 31.19           O  
ANISOU 4692  OG  SER C 432     5223   3514   3115   -404    576   -340       O  
ATOM   4693  N   SER C 433      22.605   9.771 -55.265  1.00 18.83           N  
ANISOU 4693  N   SER C 433     4040   1787   1329   -393    438   -429       N  
ATOM   4694  CA  SER C 433      22.164  10.627 -54.174  1.00 22.71           C  
ANISOU 4694  CA  SER C 433     4706   2207   1717   -359    514   -447       C  
ATOM   4695  C   SER C 433      21.517  11.903 -54.711  1.00 23.80           C  
ANISOU 4695  C   SER C 433     4815   2312   1917   -287    596   -488       C  
ATOM   4696  O   SER C 433      20.532  12.390 -54.155  1.00 27.46           O  
ANISOU 4696  O   SER C 433     5352   2734   2349   -212    747   -502       O  
ATOM   4697  CB  SER C 433      23.344  10.967 -53.264  1.00 26.71           C  
ANISOU 4697  CB  SER C 433     5372   2668   2106   -438    348   -440       C  
ATOM   4698  OG  SER C 433      23.818   9.799 -52.614  1.00 37.88           O  
ANISOU 4698  OG  SER C 433     6836   4105   3451   -485    279   -395       O  
ATOM   4699  N   ARG C 434      22.074  12.433 -55.797  1.00 20.40           N  
ANISOU 4699  N   ARG C 434     4278   1896   1577   -306    499   -501       N  
ATOM   4700  CA  ARG C 434      21.542  13.648 -56.418  1.00 22.92           C  
ANISOU 4700  CA  ARG C 434     4573   2177   1956   -237    557   -532       C  
ATOM   4701  C   ARG C 434      20.182  13.368 -57.046  1.00 20.16           C  
ANISOU 4701  C   ARG C 434     4088   1864   1707   -133    721   -534       C  
ATOM   4702  O   ARG C 434      19.263  14.177 -56.931  1.00 21.16           O  
ANISOU 4702  O   ARG C 434     4243   1952   1847    -39    840   -550       O  
ATOM   4703  CB  ARG C 434      22.518  14.197 -57.461  1.00 24.31           C  
ANISOU 4703  CB  ARG C 434     4669   2362   2206   -291    414   -535       C  
ATOM   4704  CG  ARG C 434      22.027  15.420 -58.249  1.00 23.97           C  
ANISOU 4704  CG  ARG C 434     4605   2275   2228   -222    462   -559       C  
ATOM   4705  CD  ARG C 434      21.910  16.675 -57.391  1.00 27.50           C  
ANISOU 4705  CD  ARG C 434     5244   2625   2579   -202    496   -584       C  
ATOM   4706  NE  ARG C 434      21.429  17.824 -58.157  1.00 23.09           N  
ANISOU 4706  NE  ARG C 434     4677   2018   2080   -129    542   -602       N  
ATOM   4707  CZ  ARG C 434      20.706  18.818 -57.649  1.00 29.00           C  
ANISOU 4707  CZ  ARG C 434     5555   2684   2780    -49    645   -624       C  
ATOM   4708  NH1 ARG C 434      20.373  18.813 -56.367  1.00 29.79           N  
ANISOU 4708  NH1 ARG C 434     5807   2743   2769    -33    720   -635       N  
ATOM   4709  NH2 ARG C 434      20.319  19.825 -58.420  1.00 28.08           N  
ANISOU 4709  NH2 ARG C 434     5427   2520   2720     21    675   -634       N  
ATOM   4710  N   PHE C 435      20.059  12.217 -57.707  1.00 19.04           N  
ANISOU 4710  N   PHE C 435     3797   1795   1643   -148    724   -514       N  
ATOM   4711  CA  PHE C 435      18.777  11.766 -58.242  1.00 19.80           C  
ANISOU 4711  CA  PHE C 435     3743   1936   1844    -66    874   -508       C  
ATOM   4712  C   PHE C 435      17.720  11.686 -57.140  1.00 23.37           C  
ANISOU 4712  C   PHE C 435     4255   2376   2249     -5   1046   -494       C  
ATOM   4713  O   PHE C 435      16.577  12.105 -57.324  1.00 21.28           O  
ANISOU 4713  O   PHE C 435     3907   2118   2061     96   1179   -494       O  
ATOM   4714  CB  PHE C 435      18.918  10.399 -58.914  1.00 18.76           C  
ANISOU 4714  CB  PHE C 435     3473   1876   1780   -120    849   -488       C  
ATOM   4715  CG  PHE C 435      19.470  10.446 -60.314  1.00 23.23           C  
ANISOU 4715  CG  PHE C 435     3921   2462   2443   -143    738   -502       C  
ATOM   4716  CD1 PHE C 435      19.898  11.635 -60.878  1.00 22.15           C  
ANISOU 4716  CD1 PHE C 435     3807   2284   2325   -126    658   -520       C  
ATOM   4717  CD2 PHE C 435      19.533   9.290 -61.075  1.00 24.76           C  
ANISOU 4717  CD2 PHE C 435     3941   2727   2739   -182    684   -459       C  
ATOM   4718  CE1 PHE C 435      20.397  11.666 -62.168  1.00 25.79           C  
ANISOU 4718  CE1 PHE C 435     4166   2760   2872   -149    564   -522       C  
ATOM   4719  CE2 PHE C 435      20.027   9.311 -62.367  1.00 23.17           C  
ANISOU 4719  CE2 PHE C 435     3621   2551   2633   -198    571   -451       C  
ATOM   4720  CZ  PHE C 435      20.460  10.500 -62.912  1.00 22.78           C  
ANISOU 4720  CZ  PHE C 435     3619   2454   2581   -181    518   -482       C  
ATOM   4721  N   ARG C 436      18.118  11.134 -55.999  1.00 22.77           N  
ANISOU 4721  N   ARG C 436     4320   2281   2050    -63   1039   -476       N  
ATOM   4722  CA  ARG C 436      17.239  11.020 -54.842  1.00 27.59           C  
ANISOU 4722  CA  ARG C 436     5017   2869   2598    -18   1199   -460       C  
ATOM   4723  C   ARG C 436      16.846  12.389 -54.310  1.00 25.69           C  
ANISOU 4723  C   ARG C 436     4903   2551   2307     59   1265   -491       C  
ATOM   4724  O   ARG C 436      15.675  12.642 -54.027  1.00 36.37           O  
ANISOU 4724  O   ARG C 436     6219   3901   3697    154   1438   -485       O  
ATOM   4725  CB  ARG C 436      17.916  10.194 -53.746  1.00 32.13           C  
ANISOU 4725  CB  ARG C 436     5749   3424   3034   -102   1148   -433       C  
ATOM   4726  CG  ARG C 436      16.960   9.550 -52.756  1.00 35.93           C  
ANISOU 4726  CG  ARG C 436     6272   3903   3476    -73   1325   -398       C  
ATOM   4727  CD  ARG C 436      17.739   8.813 -51.679  1.00 35.87           C  
ANISOU 4727  CD  ARG C 436     6449   3864   3318   -153   1249   -371       C  
ATOM   4728  NE  ARG C 436      18.686   7.879 -52.273  1.00 40.85           N  
ANISOU 4728  NE  ARG C 436     7013   4541   3967   -236   1093   -347       N  
ATOM   4729  CZ  ARG C 436      20.009   7.970 -52.168  1.00 34.76           C  
ANISOU 4729  CZ  ARG C 436     6336   3750   3120   -304    890   -352       C  
ATOM   4730  NH1 ARG C 436      20.560   8.955 -51.474  1.00 34.57           N  
ANISOU 4730  NH1 ARG C 436     6480   3661   2995   -314    812   -380       N  
ATOM   4731  NH2 ARG C 436      20.784   7.070 -52.760  1.00 26.06           N  
ANISOU 4731  NH2 ARG C 436     5156   2697   2051   -364    764   -324       N  
ATOM   4732  N  AMET C 437      17.854  13.242 -54.153  0.59 26.31           N  
ANISOU 4732  N  AMET C 437     5127   2567   2303     13   1127   -520       N  
ATOM   4733  N  BMET C 437      17.816  13.292 -54.186  0.41 26.11           N  
ANISOU 4733  N  BMET C 437     5099   2541   2282     18   1131   -521       N  
ATOM   4734  CA AMET C 437      17.670  14.636 -53.784  0.59 28.12           C  
ANISOU 4734  CA AMET C 437     5494   2709   2482     71   1163   -553       C  
ATOM   4735  CA BMET C 437      17.532  14.640 -53.693  0.41 27.87           C  
ANISOU 4735  CA BMET C 437     5467   2674   2447     82   1186   -553       C  
ATOM   4736  C  AMET C 437      16.549  15.258 -54.612  0.59 29.34           C  
ANISOU 4736  C  AMET C 437     5502   2877   2767    197   1284   -561       C  
ATOM   4737  C  BMET C 437      16.662  15.452 -54.655  0.41 28.38           C  
ANISOU 4737  C  BMET C 437     5398   2744   2641    195   1266   -566       C  
ATOM   4738  O  AMET C 437      15.618  15.859 -54.077  0.59 30.25           O  
ANISOU 4738  O  AMET C 437     5672   2951   2870    296   1436   -567       O  
ATOM   4739  O  BMET C 437      16.034  16.434 -54.255  0.41 30.57           O  
ANISOU 4739  O  BMET C 437     5768   2956   2893    283   1370   -584       O  
ATOM   4740  CB AMET C 437      18.987  15.397 -53.983  0.59 28.20           C  
ANISOU 4740  CB AMET C 437     5602   2671   2441    -16    969   -576       C  
ATOM   4741  CB BMET C 437      18.830  15.396 -53.410  0.41 26.49           C  
ANISOU 4741  CB BMET C 437     5462   2432   2172     -9   1010   -576       C  
ATOM   4742  CG AMET C 437      19.012  16.812 -53.441  0.59 28.89           C  
ANISOU 4742  CG AMET C 437     5880   2650   2445     13    985   -609       C  
ATOM   4743  CG BMET C 437      19.229  15.409 -51.945  0.41 33.37           C  
ANISOU 4743  CG BMET C 437     6575   3233   2870    -59    997   -577       C  
ATOM   4744  SD AMET C 437      20.547  17.220 -52.571  0.59 48.02           S  
ANISOU 4744  SD AMET C 437     8526   5003   4715   -130    788   -620       S  
ATOM   4745  SD BMET C 437      19.335  17.086 -51.283  0.41 33.82           S  
ANISOU 4745  SD BMET C 437     6878   3154   2817    -36   1005   -622       S  
ATOM   4746  CE AMET C 437      21.758  17.230 -53.892  0.59 25.84           C  
ANISOU 4746  CE AMET C 437     5548   2254   2017   -225    585   -610       C  
ATOM   4747  CE BMET C 437      17.843  17.836 -51.935  0.41 34.74           C  
ANISOU 4747  CE BMET C 437     6885   3263   3052    133   1213   -636       C  
ATOM   4748  N   MET C 438      16.627  15.049 -55.921  1.00 26.06           N  
ANISOU 4748  N   MET C 438     4898   2523   2481    198   1216   -556       N  
ATOM   4749  CA  MET C 438      15.733  15.685 -56.884  1.00 28.75           C  
ANISOU 4749  CA  MET C 438     5095   2876   2953    313   1283   -560       C  
ATOM   4750  C   MET C 438      14.411  14.946 -57.062  1.00 26.05           C  
ANISOU 4750  C   MET C 438     4554   2614   2729    395   1438   -527       C  
ATOM   4751  O   MET C 438      13.503  15.449 -57.723  1.00 26.67           O  
ANISOU 4751  O   MET C 438     4499   2711   2924    506   1505   -520       O  
ATOM   4752  CB  MET C 438      16.426  15.790 -58.235  1.00 27.37           C  
ANISOU 4752  CB  MET C 438     4816   2723   2859    274   1134   -566       C  
ATOM   4753  CG  MET C 438      17.637  16.691 -58.248  1.00 29.97           C  
ANISOU 4753  CG  MET C 438     5297   2980   3109    197    987   -589       C  
ATOM   4754  SD  MET C 438      18.181  16.873 -59.939  1.00 25.93           S  
ANISOU 4754  SD  MET C 438     4643   2493   2714    176    856   -586       S  
ATOM   4755  CE  MET C 438      16.801  17.801 -60.599  1.00 26.97           C  
ANISOU 4755  CE  MET C 438     4701   2600   2948    351    976   -586       C  
ATOM   4756  N   ASN C 439      14.316  13.757 -56.472  1.00 21.21           N  
ANISOU 4756  N   ASN C 439     3267   2248   2545    598    825   -106       N  
ATOM   4757  CA  ASN C 439      13.188  12.855 -56.690  1.00 22.16           C  
ANISOU 4757  CA  ASN C 439     3291   2442   2687    427    986    -54       C  
ATOM   4758  C   ASN C 439      12.949  12.627 -58.184  1.00 22.21           C  
ANISOU 4758  C   ASN C 439     3123   2481   2834    281    917    -62       C  
ATOM   4759  O   ASN C 439      11.855  12.865 -58.703  1.00 21.38           O  
ANISOU 4759  O   ASN C 439     2819   2491   2811    215    966    -70       O  
ATOM   4760  CB  ASN C 439      11.919  13.390 -56.021  1.00 26.86           C  
ANISOU 4760  CB  ASN C 439     3771   3179   3257    471   1136    -54       C  
ATOM   4761  CG  ASN C 439      10.802  12.367 -56.002  1.00 29.93           C  
ANISOU 4761  CG  ASN C 439     4077   3633   3663    290   1328      6       C  
ATOM   4762  OD1 ASN C 439      11.056  11.159 -55.991  1.00 33.57           O  
ANISOU 4762  OD1 ASN C 439     4655   4002   4099    162   1375     65       O  
ATOM   4763  ND2 ASN C 439       9.558  12.838 -56.011  1.00 36.14           N  
ANISOU 4763  ND2 ASN C 439     4655   4572   4503    277   1431    -12       N  
ATOM   4764  N   LEU C 440      13.992  12.175 -58.872  1.00 17.45           N  
ANISOU 4764  N   LEU C 440     2596   1778   2255    244    796    -69       N  
ATOM   4765  CA  LEU C 440      13.903  11.894 -60.300  1.00 17.49           C  
ANISOU 4765  CA  LEU C 440     2472   1805   2370    122    721    -78       C  
ATOM   4766  C   LEU C 440      12.816  10.875 -60.607  1.00 19.80           C  
ANISOU 4766  C   LEU C 440     2676   2140   2708    -52    836    -42       C  
ATOM   4767  O   LEU C 440      12.723   9.832 -59.960  1.00 22.35           O  
ANISOU 4767  O   LEU C 440     3115   2404   2972   -126    937      6       O  
ATOM   4768  CB  LEU C 440      15.246  11.393 -60.829  1.00 16.59           C  
ANISOU 4768  CB  LEU C 440     2477   1577   2250    116    599    -93       C  
ATOM   4769  CG  LEU C 440      15.318  11.125 -62.332  1.00 17.53           C  
ANISOU 4769  CG  LEU C 440     2486   1716   2459     14    513   -109       C  
ATOM   4770  CD1 LEU C 440      15.249  12.431 -63.091  1.00 20.10           C  
ANISOU 4770  CD1 LEU C 440     2671   2115   2851     76    421   -138       C  
ATOM   4771  CD2 LEU C 440      16.589  10.364 -62.680  1.00 17.79           C  
ANISOU 4771  CD2 LEU C 440     2651   1643   2467      5    427   -126       C  
ATOM   4772  N   GLN C 441      11.994  11.185 -61.601  1.00 16.62           N  
ANISOU 4772  N   GLN C 441     2071   1830   2415   -117    809    -65       N  
ATOM   4773  CA  GLN C 441      10.909  10.297 -61.994  1.00 17.83           C  
ANISOU 4773  CA  GLN C 441     2108   2024   2643   -283    895    -43       C  
ATOM   4774  C   GLN C 441      11.324   9.395 -63.153  1.00 18.08           C  
ANISOU 4774  C   GLN C 441     2155   1987   2729   -395    792    -49       C  
ATOM   4775  O   GLN C 441      12.205   9.747 -63.938  1.00 19.11           O  
ANISOU 4775  O   GLN C 441     2314   2087   2860   -339    654    -81       O  
ATOM   4776  CB  GLN C 441       9.669  11.109 -62.375  1.00 21.85           C  
ANISOU 4776  CB  GLN C 441     2380   2674   3249   -280    915    -82       C  
ATOM   4777  CG  GLN C 441       9.107  11.965 -61.245  1.00 25.00           C  
ANISOU 4777  CG  GLN C 441     2741   3161   3597   -165   1023    -89       C  
ATOM   4778  CD  GLN C 441       8.548  11.129 -60.108  1.00 27.26           C  
ANISOU 4778  CD  GLN C 441     3083   3453   3822   -237   1230    -28       C  
ATOM   4779  OE1 GLN C 441       7.488  10.512 -60.232  1.00 30.14           O  
ANISOU 4779  OE1 GLN C 441     3309   3877   4266   -378   1340    -11       O  
ATOM   4780  NE2 GLN C 441       9.267  11.100 -58.992  1.00 27.39           N  
ANISOU 4780  NE2 GLN C 441     3307   3403   3698   -142   1281      5       N  
ATOM   4781  N   GLY C 442      10.686   8.231 -63.255  1.00 19.83           N  
ANISOU 4781  N   GLY C 442     2358   2183   2993   -551    862    -18       N  
ATOM   4782  CA  GLY C 442      10.988   7.283 -64.314  1.00 21.21           C  
ANISOU 4782  CA  GLY C 442     2553   2288   3217   -653    760    -30       C  
ATOM   4783  C   GLY C 442      10.841   7.877 -65.701  1.00 19.47           C  
ANISOU 4783  C   GLY C 442     2184   2132   3082   -637    624    -90       C  
ATOM   4784  O   GLY C 442      11.643   7.612 -66.596  1.00 17.83           O  
ANISOU 4784  O   GLY C 442     2037   1875   2865   -628    501   -116       O  
ATOM   4785  N   GLU C 443       9.812   8.696 -65.875  1.00 20.63           N  
ANISOU 4785  N   GLU C 443     2143   2392   3304   -623    645   -116       N  
ATOM   4786  CA  GLU C 443       9.566   9.367 -67.146  1.00 20.73           C  
ANISOU 4786  CA  GLU C 443     2025   2464   3389   -594    511   -173       C  
ATOM   4787  C   GLU C 443      10.673  10.350 -67.506  1.00 15.82           C  
ANISOU 4787  C   GLU C 443     1481   1832   2699   -458    402   -187       C  
ATOM   4788  O   GLU C 443      11.046  10.478 -68.674  1.00 19.31           O  
ANISOU 4788  O   GLU C 443     1915   2269   3154   -450    279   -214       O  
ATOM   4789  CB  GLU C 443       8.218  10.085 -67.106  1.00 19.14           C  
ANISOU 4789  CB  GLU C 443     1612   2381   3280   -590    553   -207       C  
ATOM   4790  CG  GLU C 443       7.038   9.145 -66.957  1.00 24.69           C  
ANISOU 4790  CG  GLU C 443     2190   3105   4085   -743    652   -201       C  
ATOM   4791  CD  GLU C 443       6.782   8.710 -65.523  1.00 30.19           C  
ANISOU 4791  CD  GLU C 443     2938   3799   4733   -787    850   -138       C  
ATOM   4792  OE1 GLU C 443       7.471   9.187 -64.592  1.00 33.18           O  
ANISOU 4792  OE1 GLU C 443     3450   4164   4992   -678    904   -108       O  
ATOM   4793  OE2 GLU C 443       5.891   7.859 -65.328  1.00 35.17           O  
ANISOU 4793  OE2 GLU C 443     3515   4442   5407   -901    913   -107       O  
ATOM   4794  N   GLU C 444      11.193  11.044 -66.500  1.00 15.26           N  
ANISOU 4794  N   GLU C 444     1489   1755   2556   -351    448   -168       N  
ATOM   4795  CA  GLU C 444      12.319  11.944 -66.705  1.00 16.50           C  
ANISOU 4795  CA  GLU C 444     1723   1884   2661   -233    349   -176       C  
ATOM   4796  C   GLU C 444      13.575  11.148 -67.032  1.00 15.73           C  
ANISOU 4796  C   GLU C 444     1773   1691   2511   -254    299   -168       C  
ATOM   4797  O   GLU C 444      14.338  11.519 -67.921  1.00 13.75           O  
ANISOU 4797  O   GLU C 444     1535   1433   2255   -221    197   -183       O  
ATOM   4798  CB  GLU C 444      12.553  12.817 -65.471  1.00 17.50           C  
ANISOU 4798  CB  GLU C 444     1902   2014   2732   -110    398   -167       C  
ATOM   4799  CG  GLU C 444      11.409  13.774 -65.151  1.00 17.55           C  
ANISOU 4799  CG  GLU C 444     1764   2125   2782    -54    431   -191       C  
ATOM   4800  CD  GLU C 444      11.553  14.423 -63.784  1.00 19.25           C  
ANISOU 4800  CD  GLU C 444     2047   2342   2927     71    495   -187       C  
ATOM   4801  OE1 GLU C 444      11.942  13.716 -62.826  1.00 19.66           O  
ANISOU 4801  OE1 GLU C 444     2232   2335   2903     65    587   -154       O  
ATOM   4802  OE2 GLU C 444      11.279  15.636 -63.676  1.00 20.22           O  
ANISOU 4802  OE2 GLU C 444     2103   2517   3064    184    442   -219       O  
ATOM   4803  N   PHE C 445      13.773  10.044 -66.318  1.00 13.37           N  
ANISOU 4803  N   PHE C 445     1586   1322   2172   -309    371   -146       N  
ATOM   4804  CA  PHE C 445      14.942   9.191 -66.522  1.00 12.75           C  
ANISOU 4804  CA  PHE C 445     1653   1147   2043   -318    318   -152       C  
ATOM   4805  C   PHE C 445      15.064   8.704 -67.972  1.00 12.49           C  
ANISOU 4805  C   PHE C 445     1575   1122   2047   -379    221   -182       C  
ATOM   4806  O   PHE C 445      16.133   8.800 -68.574  1.00 13.25           O  
ANISOU 4806  O   PHE C 445     1725   1197   2111   -330    141   -206       O  
ATOM   4807  CB  PHE C 445      14.893   7.998 -65.557  1.00 14.15           C  
ANISOU 4807  CB  PHE C 445     1961   1240   2175   -380    404   -122       C  
ATOM   4808  CG  PHE C 445      15.771   6.844 -65.964  1.00 14.86           C  
ANISOU 4808  CG  PHE C 445     2181   1232   2234   -417    334   -141       C  
ATOM   4809  CD1 PHE C 445      17.149   6.931 -65.851  1.00 14.68           C  
ANISOU 4809  CD1 PHE C 445     2278   1148   2152   -320    263   -172       C  
ATOM   4810  CD2 PHE C 445      15.219   5.662 -66.440  1.00 16.27           C  
ANISOU 4810  CD2 PHE C 445     2358   1375   2450   -546    331   -137       C  
ATOM   4811  CE1 PHE C 445      17.962   5.868 -66.223  1.00 15.37           C  
ANISOU 4811  CE1 PHE C 445     2463   1170   2206   -330    184   -201       C  
ATOM   4812  CE2 PHE C 445      16.029   4.596 -66.812  1.00 17.04           C  
ANISOU 4812  CE2 PHE C 445     2581   1377   2514   -566    251   -165       C  
ATOM   4813  CZ  PHE C 445      17.405   4.704 -66.706  1.00 19.55           C  
ANISOU 4813  CZ  PHE C 445     2990   1679   2758   -436    169   -194       C  
ATOM   4814  N   VAL C 446      13.980   8.185 -68.539  1.00 13.66           N  
ANISOU 4814  N   VAL C 446     1623   1304   2264   -481    228   -187       N  
ATOM   4815  CA  VAL C 446      14.060   7.666 -69.904  1.00 13.58           C  
ANISOU 4815  CA  VAL C 446     1586   1295   2279   -526    124   -224       C  
ATOM   4816  C   VAL C 446      14.312   8.798 -70.907  1.00 12.84           C  
ANISOU 4816  C   VAL C 446     1422   1273   2185   -449     38   -244       C  
ATOM   4817  O   VAL C 446      14.971   8.589 -71.928  1.00 13.91           O  
ANISOU 4817  O   VAL C 446     1593   1404   2290   -435    -45   -269       O  
ATOM   4818  CB  VAL C 446      12.791   6.868 -70.301  1.00 15.26           C  
ANISOU 4818  CB  VAL C 446     1700   1517   2582   -650    130   -233       C  
ATOM   4819  CG1 VAL C 446      12.657   5.622 -69.430  1.00 17.36           C  
ANISOU 4819  CG1 VAL C 446     2060   1690   2844   -747    206   -201       C  
ATOM   4820  CG2 VAL C 446      11.543   7.738 -70.224  1.00 15.55           C  
ANISOU 4820  CG2 VAL C 446     1560   1649   2699   -655    169   -235       C  
ATOM   4821  N   CYS C 447      13.814   9.995 -70.607  1.00 14.43           N  
ANISOU 4821  N   CYS C 447     1535   1536   2410   -393     58   -232       N  
ATOM   4822  CA  CYS C 447      14.129  11.167 -71.422  1.00 12.49           C  
ANISOU 4822  CA  CYS C 447     1251   1338   2155   -317    -25   -238       C  
ATOM   4823  C   CYS C 447      15.620  11.475 -71.391  1.00 10.92           C  
ANISOU 4823  C   CYS C 447     1162   1100   1889   -250    -49   -225       C  
ATOM   4824  O   CYS C 447      16.234  11.679 -72.434  1.00 12.66           O  
ANISOU 4824  O   CYS C 447     1396   1334   2082   -234   -116   -231       O  
ATOM   4825  CB  CYS C 447      13.342  12.393 -70.959  1.00 15.28           C  
ANISOU 4825  CB  CYS C 447     1506   1751   2548   -259    -11   -232       C  
ATOM   4826  SG  CYS C 447      11.613  12.406 -71.472  1.00 17.74           S  
ANISOU 4826  SG  CYS C 447     1642   2139   2960   -314    -29   -271       S  
ATOM   4827  N   LEU C 448      16.192  11.509 -70.190  1.00 12.35           N  
ANISOU 4827  N   LEU C 448     1419   1231   2042   -208      9   -211       N  
ATOM   4828  CA  LEU C 448      17.612  11.801 -70.022  1.00 10.42           C  
ANISOU 4828  CA  LEU C 448     1264    940   1754   -140    -18   -211       C  
ATOM   4829  C   LEU C 448      18.490  10.783 -70.741  1.00 10.92           C  
ANISOU 4829  C   LEU C 448     1395    972   1781   -171    -52   -239       C  
ATOM   4830  O   LEU C 448      19.495  11.145 -71.352  1.00 13.02           O  
ANISOU 4830  O   LEU C 448     1675   1246   2027   -134    -95   -247       O  
ATOM   4831  CB  LEU C 448      17.984  11.838 -68.539  1.00 12.24           C  
ANISOU 4831  CB  LEU C 448     1579   1109   1962    -83     36   -205       C  
ATOM   4832  CG  LEU C 448      17.402  12.973 -67.694  1.00 17.67           C  
ANISOU 4832  CG  LEU C 448     2221   1824   2668    -13     60   -187       C  
ATOM   4833  CD1 LEU C 448      17.881  12.864 -66.250  1.00 15.88           C  
ANISOU 4833  CD1 LEU C 448     2109   1527   2397     57    106   -188       C  
ATOM   4834  CD2 LEU C 448      17.761  14.332 -68.282  1.00 17.32           C  
ANISOU 4834  CD2 LEU C 448     2121   1808   2651     47    -21   -180       C  
ATOM   4835  N   LYS C 449      18.109   9.513 -70.663  1.00 11.96           N  
ANISOU 4835  N   LYS C 449     1568   1070   1908   -239    -32   -256       N  
ATOM   4836  CA  LYS C 449      18.888   8.452 -71.292  1.00 13.62           C  
ANISOU 4836  CA  LYS C 449     1851   1243   2079   -257    -78   -297       C  
ATOM   4837  C   LYS C 449      18.878   8.601 -72.815  1.00 10.86           C  
ANISOU 4837  C   LYS C 449     1441    963   1723   -266   -143   -314       C  
ATOM   4838  O   LYS C 449      19.896   8.384 -73.469  1.00 13.72           O  
ANISOU 4838  O   LYS C 449     1843   1331   2040   -232   -179   -345       O  
ATOM   4839  CB  LYS C 449      18.364   7.070 -70.871  1.00 15.33           C  
ANISOU 4839  CB  LYS C 449     2133   1392   2299   -334    -58   -307       C  
ATOM   4840  CG  LYS C 449      19.295   5.923 -71.253  1.00 21.65           C  
ANISOU 4840  CG  LYS C 449     3042   2151   3031   -323   -112   -345       C  
ATOM   4841  CD  LYS C 449      18.985   4.628 -70.507  1.00 20.32           C  
ANISOU 4841  CD  LYS C 449     2921   1916   2886   -351   -103   -338       C  
ATOM   4842  CE  LYS C 449      17.504   4.300 -70.479  1.00 20.21           C  
ANISOU 4842  CE  LYS C 449     2872   1881   2926   -479    -73   -305       C  
ATOM   4843  NZ  LYS C 449      17.292   2.839 -70.263  1.00 15.27           N  
ANISOU 4843  NZ  LYS C 449     2303   1189   2310   -524    -91   -302       N  
ATOM   4844  N   SER C 450      17.732   8.987 -73.375  1.00 11.86           N  
ANISOU 4844  N   SER C 450     1472   1144   1891   -303   -158   -300       N  
ATOM   4845  CA  SER C 450      17.643   9.239 -74.809  1.00 11.61           C  
ANISOU 4845  CA  SER C 450     1399   1174   1840   -297   -229   -314       C  
ATOM   4846  C   SER C 450      18.471  10.444 -75.224  1.00 10.67           C  
ANISOU 4846  C   SER C 450     1273   1097   1685   -231   -237   -285       C  
ATOM   4847  O   SER C 450      19.039  10.465 -76.318  1.00 11.70           O  
ANISOU 4847  O   SER C 450     1421   1265   1760   -213   -274   -294       O  
ATOM   4848  CB  SER C 450      16.193   9.446 -75.240  1.00 18.96           C  
ANISOU 4848  CB  SER C 450     2229   2143   2831   -339   -260   -316       C  
ATOM   4849  OG  SER C 450      15.524   8.204 -75.317  1.00 28.81           O  
ANISOU 4849  OG  SER C 450     3476   3355   4116   -414   -277   -351       O  
ATOM   4850  N   ILE C 451      18.524  11.450 -74.358  1.00  9.80           N  
ANISOU 4850  N   ILE C 451     1141    979   1605   -197   -204   -247       N  
ATOM   4851  CA  ILE C 451      19.298  12.649 -74.645  1.00  9.43           C  
ANISOU 4851  CA  ILE C 451     1088    952   1542   -146   -218   -211       C  
ATOM   4852  C   ILE C 451      20.777  12.278 -74.730  1.00  9.10           C  
ANISOU 4852  C   ILE C 451     1106    890   1460   -124   -203   -229       C  
ATOM   4853  O   ILE C 451      21.483  12.739 -75.624  1.00 12.80           O  
ANISOU 4853  O   ILE C 451     1571   1399   1894   -112   -215   -212       O  
ATOM   4854  CB  ILE C 451      19.067  13.744 -73.579  1.00  9.18           C  
ANISOU 4854  CB  ILE C 451     1030    899   1560   -104   -203   -179       C  
ATOM   4855  CG1 ILE C 451      17.702  14.401 -73.795  1.00 13.27           C  
ANISOU 4855  CG1 ILE C 451     1468   1459   2115   -107   -235   -168       C  
ATOM   4856  CG2 ILE C 451      20.165  14.802 -73.636  1.00  9.53           C  
ANISOU 4856  CG2 ILE C 451     1088    931   1603    -59   -221   -145       C  
ATOM   4857  CD1 ILE C 451      17.260  15.270 -72.647  1.00 14.82           C  
ANISOU 4857  CD1 ILE C 451     1634   1641   2355    -56   -218   -156       C  
ATOM   4858  N   ILE C 452      21.231  11.415 -73.822  1.00  9.71           N  
ANISOU 4858  N   ILE C 452     1242    909   1540   -117   -176   -266       N  
ATOM   4859  CA  ILE C 452      22.624  10.965 -73.831  1.00  9.79           C  
ANISOU 4859  CA  ILE C 452     1301    897   1521    -84   -174   -305       C  
ATOM   4860  C   ILE C 452      22.966  10.267 -75.145  1.00 10.50           C  
ANISOU 4860  C   ILE C 452     1397   1041   1550    -97   -196   -340       C  
ATOM   4861  O   ILE C 452      24.001  10.531 -75.755  1.00 12.47           O  
ANISOU 4861  O   ILE C 452     1636   1332   1771    -70   -188   -348       O  
ATOM   4862  CB  ILE C 452      22.923  10.012 -72.654  1.00 11.97           C  
ANISOU 4862  CB  ILE C 452     1661   1092   1796    -66   -160   -345       C  
ATOM   4863  CG1 ILE C 452      22.831  10.755 -71.319  1.00 11.90           C  
ANISOU 4863  CG1 ILE C 452     1661   1055   1806    -28   -127   -300       C  
ATOM   4864  CG2 ILE C 452      24.297   9.369 -72.806  1.00 13.96           C  
ANISOU 4864  CG2 ILE C 452     1950   1363   1991    -27   -155   -371       C  
ATOM   4865  CD1 ILE C 452      22.951   9.839 -70.110  1.00 17.22           C  
ANISOU 4865  CD1 ILE C 452     2423   1697   2422    -17    -81   -292       C  
ATOM   4866  N   LEU C 453      22.088   9.368 -75.576  1.00 10.43           N  
ANISOU 4866  N   LEU C 453     1403   1035   1523   -136   -223   -364       N  
ATOM   4867  CA  LEU C 453      22.286   8.642 -76.827  1.00  9.77           C  
ANISOU 4867  CA  LEU C 453     1338    999   1374   -134   -261   -408       C  
ATOM   4868  C   LEU C 453      22.430   9.577 -78.028  1.00 12.26           C  
ANISOU 4868  C   LEU C 453     1612   1402   1643   -120   -262   -369       C  
ATOM   4869  O   LEU C 453      23.315   9.399 -78.864  1.00 13.35           O  
ANISOU 4869  O   LEU C 453     1765   1594   1712    -88   -255   -393       O  
ATOM   4870  CB  LEU C 453      21.124   7.673 -77.060  1.00 10.29           C  
ANISOU 4870  CB  LEU C 453     1418   1040   1453   -185   -310   -436       C  
ATOM   4871  CG  LEU C 453      21.125   6.960 -78.414  1.00 11.45           C  
ANISOU 4871  CG  LEU C 453     1588   1230   1531   -172   -374   -488       C  
ATOM   4872  CD1 LEU C 453      22.293   5.983 -78.509  1.00 12.13           C  
ANISOU 4872  CD1 LEU C 453     1746   1301   1560   -124   -388   -562       C  
ATOM   4873  CD2 LEU C 453      19.797   6.266 -78.649  1.00 12.35           C  
ANISOU 4873  CD2 LEU C 453     1691   1313   1688   -229   -438   -507       C  
ATOM   4874  N   LEU C 454      21.569  10.586 -78.094  1.00 11.45           N  
ANISOU 4874  N   LEU C 454     1462   1316   1573   -138   -270   -308       N  
ATOM   4875  CA  LEU C 454      21.540  11.470 -79.251  1.00 10.53           C  
ANISOU 4875  CA  LEU C 454     1330   1267   1404   -127   -286   -262       C  
ATOM   4876  C   LEU C 454      22.580  12.592 -79.188  1.00 10.35           C  
ANISOU 4876  C   LEU C 454     1292   1259   1380   -111   -237   -203       C  
ATOM   4877  O   LEU C 454      23.056  13.056 -80.222  1.00 14.77           O  
ANISOU 4877  O   LEU C 454     1862   1878   1870   -105   -223   -168       O  
ATOM   4878  CB  LEU C 454      20.139  12.063 -79.415  1.00 10.78           C  
ANISOU 4878  CB  LEU C 454     1324   1300   1472   -145   -339   -233       C  
ATOM   4879  CG  LEU C 454      19.078  11.029 -79.818  1.00 11.56           C  
ANISOU 4879  CG  LEU C 454     1421   1393   1578   -168   -401   -292       C  
ATOM   4880  CD1 LEU C 454      17.688  11.615 -79.697  1.00 18.17           C  
ANISOU 4880  CD1 LEU C 454     2192   2227   2485   -185   -448   -279       C  
ATOM   4881  CD2 LEU C 454      19.319  10.518 -81.230  1.00 17.01           C  
ANISOU 4881  CD2 LEU C 454     2164   2133   2167   -141   -449   -326       C  
ATOM   4882  N   ASN C 455      22.944  13.014 -77.981  1.00 10.89           N  
ANISOU 4882  N   ASN C 455     1341   1272   1525   -106   -211   -190       N  
ATOM   4883  CA  ASN C 455      23.812  14.179 -77.813  1.00 13.10           C  
ANISOU 4883  CA  ASN C 455     1595   1546   1834    -98   -184   -133       C  
ATOM   4884  C   ASN C 455      25.299  13.867 -77.708  1.00 13.57           C  
ANISOU 4884  C   ASN C 455     1650   1612   1894    -82   -135   -167       C  
ATOM   4885  O   ASN C 455      26.138  14.684 -78.074  1.00 14.97           O  
ANISOU 4885  O   ASN C 455     1797   1812   2079    -92   -103   -120       O  
ATOM   4886  CB  ASN C 455      23.393  14.965 -76.568  1.00 14.03           C  
ANISOU 4886  CB  ASN C 455     1694   1596   2042    -85   -202   -108       C  
ATOM   4887  CG  ASN C 455      24.168  16.255 -76.407  1.00 14.17           C  
ANISOU 4887  CG  ASN C 455     1687   1590   2107    -79   -202    -48       C  
ATOM   4888  OD1 ASN C 455      24.040  17.175 -77.215  1.00 17.41           O  
ANISOU 4888  OD1 ASN C 455     2093   2026   2497    -99   -219     20       O  
ATOM   4889  ND2 ASN C 455      24.990  16.323 -75.366  1.00 15.33           N  
ANISOU 4889  ND2 ASN C 455     1828   1678   2318    -51   -193    -74       N  
ATOM   4890  N   SER C 456      25.631  12.695 -77.187  1.00 13.55           N  
ANISOU 4890  N   SER C 456     1675   1582   1890    -59   -134   -250       N  
ATOM   4891  CA  SER C 456      27.010  12.432 -76.798  1.00 14.47           C  
ANISOU 4891  CA  SER C 456     1780   1687   2032    -27   -107   -302       C  
ATOM   4892  C   SER C 456      27.990  12.456 -77.970  1.00 17.96           C  
ANISOU 4892  C   SER C 456     2186   2223   2416    -28    -57   -306       C  
ATOM   4893  O   SER C 456      29.109  12.946 -77.831  1.00 18.48           O  
ANISOU 4893  O   SER C 456     2197   2297   2530    -23    -19   -306       O  
ATOM   4894  CB  SER C 456      27.094  11.097 -76.074  1.00 20.71           C  
ANISOU 4894  CB  SER C 456     2629   2422   2818      6   -134   -396       C  
ATOM   4895  OG  SER C 456      26.512  11.209 -74.784  1.00 22.40           O  
ANISOU 4895  OG  SER C 456     2876   2545   3090     12   -155   -386       O  
ATOM   4896  N   GLY C 457      27.569  11.947 -79.124  1.00 15.77           N  
ANISOU 4896  N   GLY C 457     1936   2019   2037    -33    -55   -312       N  
ATOM   4897  CA  GLY C 457      28.453  11.889 -80.275  1.00 18.32           C  
ANISOU 4897  CA  GLY C 457     2236   2446   2278    -22      5   -319       C  
ATOM   4898  C   GLY C 457      28.126  12.858 -81.399  1.00 17.63           C  
ANISOU 4898  C   GLY C 457     2151   2425   2122    -59     38   -215       C  
ATOM   4899  O   GLY C 457      28.754  12.814 -82.455  1.00 18.84           O  
ANISOU 4899  O   GLY C 457     2301   2675   2184    -51    101   -209       O  
ATOM   4900  N   VAL C 458      27.161  13.745 -81.171  1.00 17.95           N  
ANISOU 4900  N   VAL C 458     2205   2415   2201    -92     -5   -135       N  
ATOM   4901  CA  VAL C 458      26.636  14.593 -82.244  1.00 22.03           C  
ANISOU 4901  CA  VAL C 458     2755   2975   2642   -117     -6    -42       C  
ATOM   4902  C   VAL C 458      27.607  15.698 -82.674  1.00 24.17           C  
ANISOU 4902  C   VAL C 458     2993   3278   2911   -159     73     52       C  
ATOM   4903  O   VAL C 458      27.451  16.285 -83.747  1.00 26.45           O  
ANISOU 4903  O   VAL C 458     3328   3616   3105   -178     94    131       O  
ATOM   4904  CB  VAL C 458      25.287  15.236 -81.837  1.00 20.78           C  
ANISOU 4904  CB  VAL C 458     2614   2748   2533   -129    -93      2       C  
ATOM   4905  CG1 VAL C 458      25.510  16.373 -80.856  1.00 19.02           C  
ANISOU 4905  CG1 VAL C 458     2350   2452   2426   -153    -97     61       C  
ATOM   4906  CG2 VAL C 458      24.528  15.728 -83.065  1.00 22.14           C  
ANISOU 4906  CG2 VAL C 458     2848   2961   2605   -130   -130     61       C  
ATOM   4907  N   TYR C 459      28.611  16.004 -81.849  1.00 22.02           N  
ANISOU 4907  N   TYR C 459     2648   2973   2746   -174    114     42       N  
ATOM   4908  CA  TYR C 459      29.626  17.048 -82.157  1.00 18.12           C  
ANISOU 4908  CA  TYR C 459     2104   2499   2281   -231    191    131       C  
ATOM   4909  C   TYR C 459      30.907  16.387 -82.697  1.00 23.73           C  
ANISOU 4909  C   TYR C 459     2754   3311   2953   -225    302     80       C  
ATOM   4910  O   TYR C 459      31.833  17.096 -82.989  1.00 27.90           O  
ANISOU 4910  O   TYR C 459     3217   3868   3515   -281    387    145       O  
ATOM   4911  CB  TYR C 459      29.880  17.928 -80.917  1.00 20.45           C  
ANISOU 4911  CB  TYR C 459     2345   2684   2741   -255    150    159       C  
ATOM   4912  CG  TYR C 459      28.627  18.403 -80.198  1.00 27.22           C  
ANISOU 4912  CG  TYR C 459     3251   3449   3642   -240     41    185       C  
ATOM   4913  CD1 TYR C 459      27.811  19.382 -80.747  1.00 28.85           C  
ANISOU 4913  CD1 TYR C 459     3511   3639   3811   -269     -1    287       C  
ATOM   4914  CD2 TYR C 459      28.219  17.843 -78.993  1.00 25.03           C  
ANISOU 4914  CD2 TYR C 459     2971   3104   3435   -190    -19    104       C  
ATOM   4915  CE1 TYR C 459      26.639  19.792 -80.128  1.00 30.23           C  
ANISOU 4915  CE1 TYR C 459     3716   3741   4028   -242   -103    294       C  
ATOM   4916  CE2 TYR C 459      27.054  18.231 -78.370  1.00 26.92           C  
ANISOU 4916  CE2 TYR C 459     3242   3278   3709   -171   -101    121       C  
ATOM   4917  CZ  TYR C 459      26.248  19.200 -78.943  1.00 33.01           C  
ANISOU 4917  CZ  TYR C 459     4047   4043   4452   -193   -145    210       C  
ATOM   4918  OH  TYR C 459      25.096  19.607 -78.336  1.00 36.30           O  
ANISOU 4918  OH  TYR C 459     4479   4404   4908   -161   -229    210       O  
ATOM   4919  N   THR C 460      30.933  15.061 -82.870  1.00 24.65           N  
ANISOU 4919  N   THR C 460     2886   3481   3000   -158    299    -37       N  
ATOM   4920  CA  THR C 460      32.176  14.361 -83.305  1.00 20.56           C  
ANISOU 4920  CA  THR C 460     2302   3065   2446   -130    393   -112       C  
ATOM   4921  C   THR C 460      31.982  13.479 -84.546  1.00 24.65           C  
ANISOU 4921  C   THR C 460     2884   3700   2783    -75    423   -158       C  
ATOM   4922  O   THR C 460      32.727  12.521 -84.704  1.00 24.69           O  
ANISOU 4922  O   THR C 460     2858   3773   2752    -11    451   -274       O  
ATOM   4923  CB  THR C 460      32.804  13.544 -82.177  1.00 24.37           C  
ANISOU 4923  CB  THR C 460     2732   3495   3034    -74    350   -249       C  
ATOM   4924  OG1 THR C 460      31.777  12.709 -81.670  1.00 23.85           O  
ANISOU 4924  OG1 THR C 460     2753   3357   2953    -28    241   -313       O  
ATOM   4925  CG2 THR C 460      33.323  14.402 -81.050  1.00 23.28           C  
ANISOU 4925  CG2 THR C 460     2515   3260   3071   -113    335   -222       C  
ATOM   4926  N   PHE C 461      31.087  13.880 -85.442  1.00 30.00           N  
ATOM   4927  CA  PHE C 461      30.864  13.144 -86.713  1.00 30.00           C  
ATOM   4928  C   PHE C 461      32.078  13.281 -87.648  1.00 30.00           C  
ATOM   4929  O   PHE C 461      32.275  12.389 -88.455  1.00 30.00           O  
ATOM   4930  CB  PHE C 461      29.557  13.600 -87.368  1.00 30.00           C  
ATOM   4931  CG  PHE C 461      28.331  12.974 -86.752  1.00 30.00           C  
ATOM   4932  CD1 PHE C 461      28.252  11.613 -86.560  1.00 30.00           C  
ATOM   4933  CD2 PHE C 461      27.291  13.754 -86.311  1.00 30.00           C  
ATOM   4934  CE1 PHE C 461      27.152  11.033 -85.965  1.00 30.00           C  
ATOM   4935  CE2 PHE C 461      26.181  13.173 -85.729  1.00 30.00           C  
ATOM   4936  CZ  PHE C 461      26.121  11.818 -85.550  1.00 30.00           C  
ATOM   4937  N   LEU C 462      32.830  14.371 -87.524  1.00 28.88           N  
ANISOU 4937  N   LEU C 462     3467   4511   2997   -106    676      0       N  
ATOM   4938  CA  LEU C 462      34.034  14.610 -88.354  1.00 30.22           C  
ANISOU 4938  CA  LEU C 462     3572   4820   3091   -130    851     39       C  
ATOM   4939  C   LEU C 462      33.625  14.477 -89.821  1.00 34.25           C  
ANISOU 4939  C   LEU C 462     4209   5443   3363    -89    905     87       C  
ATOM   4940  O   LEU C 462      34.300  13.767 -90.573  1.00 35.15           O  
ANISOU 4940  O   LEU C 462     4306   5700   3348    -23   1003     19       O  
ATOM   4941  CB  LEU C 462      35.174  13.654 -87.982  1.00 30.70           C  
ANISOU 4941  CB  LEU C 462     3506   4957   3202    -69    907   -115       C  
ATOM   4942  CG  LEU C 462      35.595  13.626 -86.517  1.00 32.11           C  
ANISOU 4942  CG  LEU C 462     3572   5024   3605    -87    843   -185       C  
ATOM   4943  CD1 LEU C 462      36.721  12.632 -86.311  1.00 32.97           C  
ANISOU 4943  CD1 LEU C 462     3559   5220   3746    -14    896   -344       C  
ATOM   4944  CD2 LEU C 462      36.034  14.998 -86.068  1.00 33.19           C  
ANISOU 4944  CD2 LEU C 462     3637   5087   3888   -211    884    -48       C  
ATOM   4945  N   SER C 463      32.533  15.141 -90.174  1.00 35.76           N  
ANISOU 4945  N   SER C 463     4530   5566   3492   -115    829    196       N  
ATOM   4946  CA  SER C 463      32.063  15.135 -91.550  1.00 35.25           C  
ANISOU 4946  CA  SER C 463     4614   5583   3198    -68    851    247       C  
ATOM   4947  C   SER C 463      31.102  16.289 -91.783  1.00 33.04           C  
ANISOU 4947  C   SER C 463     4451   5204   2898   -129    780    398       C  
ATOM   4948  O   SER C 463      30.279  16.614 -90.924  1.00 36.19           O  
ANISOU 4948  O   SER C 463     4849   5468   3433   -154    644    403       O  
ATOM   4949  CB  SER C 463      31.386  13.803 -91.887  1.00 35.27           C  
ANISOU 4949  CB  SER C 463     4697   5610   3096     65    734     98       C  
ATOM   4950  OG  SER C 463      30.792  13.837 -93.174  1.00 34.80           O  
ANISOU 4950  OG  SER C 463     4798   5606   2817    125    719    142       O  
ATOM   4951  N   SER C 464      31.222  16.920 -92.943  1.00 35.63           N  
ANISOU 4951  N   SER C 464     4886   5601   3049   -148    873    520       N  
ATOM   4952  CA  SER C 464      30.273  17.946 -93.335  1.00 37.57           C  
ANISOU 4952  CA  SER C 464     5279   5754   3243   -183    786    654       C  
ATOM   4953  C   SER C 464      29.835  17.711 -94.770  1.00 37.15           C  
ANISOU 4953  C   SER C 464     5412   5783   2921    -93    787    674       C  
ATOM   4954  O   SER C 464      29.682  18.647 -95.552  1.00 40.59           O  
ANISOU 4954  O   SER C 464     5983   6208   3232   -131    820    822       O  
ATOM   4955  CB  SER C 464      30.865  19.346 -93.163  1.00 38.56           C  
ANISOU 4955  CB  SER C 464     5373   5830   3449   -326    882    829       C  
ATOM   4956  OG  SER C 464      30.777  19.770 -91.816  1.00 41.06           O  
ANISOU 4956  OG  SER C 464     5575   6018   4010   -387    798    817       O  
ATOM   4957  N   THR C 465      29.655  16.438 -95.109  1.00 38.16           N  
ANISOU 4957  N   THR C 465     5558   5984   2957     32    741    522       N  
ATOM   4958  CA  THR C 465      28.917  16.068 -96.303  1.00 30.70           C  
ANISOU 4958  CA  THR C 465     4802   5079   1784    149    664    500       C  
ATOM   4959  C   THR C 465      27.500  16.600 -96.129  1.00 29.81           C  
ANISOU 4959  C   THR C 465     4788   4815   1723    151    456    530       C  
ATOM   4960  O   THR C 465      27.062  16.837 -95.000  1.00 31.06           O  
ANISOU 4960  O   THR C 465     4847   4859   2096     92    364    514       O  
ATOM   4961  CB  THR C 465      28.891  14.543 -96.517  1.00 31.12           C  
ANISOU 4961  CB  THR C 465     4845   5208   1771    286    609    309       C  
ATOM   4962  OG1 THR C 465      28.211  13.922 -95.420  1.00 28.35           O  
ANISOU 4962  OG1 THR C 465     4406   4745   1621    290    447    192       O  
ATOM   4963  CG2 THR C 465      30.303  13.986 -96.604  1.00 31.38           C  
ANISOU 4963  CG2 THR C 465     4759   5380   1785    291    797    252       C  
ATOM   4964  N   LEU C 466      26.787  16.793 -97.234  1.00 31.68           N  
ANISOU 4964  N   LEU C 466     5221   5052   1764    229    378    566       N  
ATOM   4965  CA  LEU C 466      25.415  17.281 -97.168  1.00 32.61           C  
ANISOU 4965  CA  LEU C 466     5433   5033   1926    249    165    576       C  
ATOM   4966  C   LEU C 466      24.567  16.382 -96.270  1.00 29.07           C  
ANISOU 4966  C   LEU C 466     4875   4511   1659    286     -2    414       C  
ATOM   4967  O   LEU C 466      23.769  16.864 -95.467  1.00 26.03           O  
ANISOU 4967  O   LEU C 466     4438   4009   1441    241   -121    420       O  
ATOM   4968  CB  LEU C 466      24.802  17.364 -98.564  1.00 32.69           C  
ANISOU 4968  CB  LEU C 466     5618   5049   1752    330     80    584       C  
ATOM   4969  CG  LEU C 466      23.350  17.844 -98.605  1.00 34.02           C  
ANISOU 4969  CG  LEU C 466     5867   5081   1977    369   -151    573       C  
ATOM   4970  CD1 LEU C 466      23.178  19.148 -97.829  1.00 31.92           C  
ANISOU 4970  CD1 LEU C 466     5598   4710   1822    269   -169    705       C  
ATOM   4971  CD2 LEU C 466      22.873  17.994-100.041  1.00 34.84           C  
ANISOU 4971  CD2 LEU C 466     6121   5189   1928    445   -218    581       C  
ATOM   4972  N   LYS C 467      24.768  15.074 -96.403  1.00 28.13           N  
ANISOU 4972  N   LYS C 467     4721   4464   1504    368     -7    271       N  
ATOM   4973  CA  LYS C 467      24.071  14.096 -95.582  1.00 27.46           C  
ANISOU 4973  CA  LYS C 467     4538   4312   1583    393   -148    122       C  
ATOM   4974  C   LYS C 467      24.321  14.333 -94.098  1.00 27.21           C  
ANISOU 4974  C   LYS C 467     4330   4213   1794    282   -108    133       C  
ATOM   4975  O   LYS C 467      23.399  14.258 -93.290  1.00 25.58           O  
ANISOU 4975  O   LYS C 467     4066   3906   1748    261   -235     87       O  
ATOM   4976  CB  LYS C 467      24.500  12.678 -95.962  1.00 30.58           C  
ANISOU 4976  CB  LYS C 467     4930   4795   1894    492   -141    -22       C  
ATOM   4977  CG  LYS C 467      23.699  11.585 -95.275  1.00 28.23           C  
ANISOU 4977  CG  LYS C 467     4564   4416   1746    518   -304   -172       C  
ATOM   4978  CD  LYS C 467      22.278  11.525 -95.808  1.00 31.60           C  
ANISOU 4978  CD  LYS C 467     5078   4756   2172    572   -508   -213       C  
ATOM   4979  CE  LYS C 467      21.366  10.747 -94.871  1.00 29.30           C  
ANISOU 4979  CE  LYS C 467     4689   4364   2082    549   -655   -324       C  
ATOM   4980  NZ  LYS C 467      19.990  10.658 -95.435  1.00 34.25           N  
ANISOU 4980  NZ  LYS C 467     5350   4900   2765    583   -830   -365       N  
ATOM   4981  N   SER C 468      25.571  14.627 -93.751  1.00 24.50           N  
ANISOU 4981  N   SER C 468     3902   3929   1477    215     69    191       N  
ATOM   4982  CA  SER C 468      25.944  14.858 -92.359  1.00 23.74           C  
ANISOU 4982  CA  SER C 468     3651   3770   1601    124    105    196       C  
ATOM   4983  C   SER C 468      25.254  16.084 -91.776  1.00 22.27           C  
ANISOU 4983  C   SER C 468     3462   3468   1532     50     37    298       C  
ATOM   4984  O   SER C 468      24.810  16.062 -90.630  1.00 20.77           O  
ANISOU 4984  O   SER C 468     3180   3192   1520     18    -32    259       O  
ATOM   4985  CB  SER C 468      27.459  15.000 -92.227  1.00 26.26           C  
ANISOU 4985  CB  SER C 468     3879   4176   1923     74    299    233       C  
ATOM   4986  OG  SER C 468      28.094  13.738 -92.358  1.00 33.62           O  
ANISOU 4986  OG  SER C 468     4769   5198   2807    148    341    100       O  
ATOM   4987  N   LEU C 469      25.169  17.152 -92.563  1.00 25.28           N  
ANISOU 4987  N   LEU C 469     3954   3846   1804     30     53    428       N  
ATOM   4988  CA  LEU C 469      24.475  18.358 -92.123  1.00 22.61           C  
ANISOU 4988  CA  LEU C 469     3635   3393   1561    -23    -36    520       C  
ATOM   4989  C   LEU C 469      23.018  18.042 -91.813  1.00 22.11           C  
ANISOU 4989  C   LEU C 469     3580   3251   1570     35   -231    427       C  
ATOM   4990  O   LEU C 469      22.467  18.502 -90.811  1.00 22.23           O  
ANISOU 4990  O   LEU C 469     3519   3177   1751      0   -303    424       O  
ATOM   4991  CB  LEU C 469      24.575  19.457 -93.181  1.00 28.43           C  
ANISOU 4991  CB  LEU C 469     4527   4133   2140    -42     -5    672       C  
ATOM   4992  CG  LEU C 469      25.947  20.129 -93.281  1.00 30.03           C  
ANISOU 4992  CG  LEU C 469     4700   4386   2325   -141    192    800       C  
ATOM   4993  CD1 LEU C 469      26.004  21.063 -94.470  1.00 31.64           C  
ANISOU 4993  CD1 LEU C 469     5087   4597   2338   -158    230    955       C  
ATOM   4994  CD2 LEU C 469      26.267  20.878 -91.993  1.00 29.77           C  
ANISOU 4994  CD2 LEU C 469     4533   4259   2520   -240    196    843       C  
ATOM   4995  N   GLU C 470      22.412  17.228 -92.672  1.00 21.73           N  
ANISOU 4995  N   GLU C 470     3616   3239   1401    127   -314    343       N  
ATOM   4996  CA  GLU C 470      21.021  16.825 -92.519  1.00 21.21           C  
ANISOU 4996  CA  GLU C 470     3548   3107   1406    182   -501    242       C  
ATOM   4997  C   GLU C 470      20.833  15.915 -91.300  1.00 19.57           C  
ANISOU 4997  C   GLU C 470     3184   2871   1383    156   -515    132       C  
ATOM   4998  O   GLU C 470      19.844  16.033 -90.573  1.00 18.77           O  
ANISOU 4998  O   GLU C 470     3015   2693   1422    144   -620     93       O  
ATOM   4999  CB  GLU C 470      20.543  16.139 -93.800  1.00 22.55           C  
ANISOU 4999  CB  GLU C 470     3851   3319   1398    291   -590    175       C  
ATOM   5000  CG  GLU C 470      20.601  17.062 -95.020  1.00 24.36           C  
ANISOU 5000  CG  GLU C 470     4267   3565   1425    328   -591    287       C  
ATOM   5001  CD  GLU C 470      20.243  16.362 -96.318  1.00 30.00           C  
ANISOU 5001  CD  GLU C 470     5133   4327   1939    455   -675    217       C  
ATOM   5002  OE1 GLU C 470      20.380  15.124 -96.379  1.00 31.00           O  
ANISOU 5002  OE1 GLU C 470     5208   4502   2069    500   -675     95       O  
ATOM   5003  OE2 GLU C 470      19.833  17.052 -97.278  1.00 30.75           O  
ANISOU 5003  OE2 GLU C 470     5341   4395   1949    486   -722    273       O  
ATOM   5004  N   GLU C 471      21.791  15.022 -91.067  1.00 19.05           N  
ANISOU 5004  N   GLU C 471     3061   2864   1311    149   -406     83       N  
ATOM   5005  CA  GLU C 471      21.720  14.123 -89.920  1.00 17.66           C  
ANISOU 5005  CA  GLU C 471     2764   2653   1293    125   -415    -14       C  
ATOM   5006  C   GLU C 471      21.794  14.904 -88.608  1.00 16.44           C  
ANISOU 5006  C   GLU C 471     2508   2431   1308     47   -380     41       C  
ATOM   5007  O   GLU C 471      21.049  14.628 -87.667  1.00 15.47           O  
ANISOU 5007  O   GLU C 471     2312   2244   1323     30   -444    -12       O  
ATOM   5008  CB  GLU C 471      22.839  13.082 -89.979  1.00 21.44           C  
ANISOU 5008  CB  GLU C 471     3221   3206   1719    146   -316    -79       C  
ATOM   5009  CG  GLU C 471      22.717  12.114 -91.148  1.00 25.86           C  
ANISOU 5009  CG  GLU C 471     3878   3829   2121    242   -371   -164       C  
ATOM   5010  CD  GLU C 471      21.929  10.864 -90.799  1.00 26.06           C  
ANISOU 5010  CD  GLU C 471     3877   3798   2228    269   -500   -297       C  
ATOM   5011  OE1 GLU C 471      22.441  10.012 -90.048  1.00 18.99           O  
ANISOU 5011  OE1 GLU C 471     2916   2892   1407    255   -466   -366       O  
ATOM   5012  OE2 GLU C 471      20.783  10.737 -91.273  1.00 26.61           O  
ANISOU 5012  OE2 GLU C 471     3993   3825   2292    304   -643   -335       O  
ATOM   5013  N   LYS C 472      22.690  15.887 -88.556  1.00 16.82           N  
ANISOU 5013  N   LYS C 472     2554   2492   1345      2   -278    148       N  
ATOM   5014  CA  LYS C 472      22.856  16.706 -87.359  1.00 16.01           C  
ANISOU 5014  CA  LYS C 472     2367   2319   1396    -60   -256    200       C  
ATOM   5015  C   LYS C 472      21.611  17.544 -87.074  1.00 15.64           C  
ANISOU 5015  C   LYS C 472     2330   2193   1418    -57   -382    226       C  
ATOM   5016  O   LYS C 472      21.195  17.674 -85.923  1.00 19.11           O  
ANISOU 5016  O   LYS C 472     2688   2573   2000    -74   -413    199       O  
ATOM   5017  CB  LYS C 472      24.078  17.612 -87.495  1.00 22.45           C  
ANISOU 5017  CB  LYS C 472     3181   3159   2191   -114   -134    310       C  
ATOM   5018  CG  LYS C 472      25.405  16.886 -87.374  1.00 20.04           C  
ANISOU 5018  CG  LYS C 472     2812   2924   1877   -124     -3    269       C  
ATOM   5019  CD  LYS C 472      26.576  17.829 -87.598  1.00 27.60           C  
ANISOU 5019  CD  LYS C 472     3751   3910   2827   -190    122    381       C  
ATOM   5020  CE  LYS C 472      27.734  17.107 -88.273  1.00 29.26           C  
ANISOU 5020  CE  LYS C 472     3940   4243   2934   -175    259    347       C  
ATOM   5021  NZ  LYS C 472      28.859  18.022 -88.622  1.00 33.01           N  
ANISOU 5021  NZ  LYS C 472     4386   4758   3397   -252    399    464       N  
ATOM   5022  N   ASP C 473      21.021  18.113 -88.125  1.00 17.28           N  
ANISOU 5022  N   ASP C 473     2644   2402   1518    -25   -456    272       N  
ATOM   5023  CA  ASP C 473      19.765  18.839 -87.984  1.00 17.31           C  
ANISOU 5023  CA  ASP C 473     2661   2336   1579     -1   -598    274       C  
ATOM   5024  C   ASP C 473      18.669  17.943 -87.419  1.00 16.60           C  
ANISOU 5024  C   ASP C 473     2487   2229   1592     27   -687    148       C  
ATOM   5025  O   ASP C 473      17.947  18.341 -86.507  1.00 16.75           O  
ANISOU 5025  O   ASP C 473     2427   2195   1741     20   -741    129       O  
ATOM   5026  CB  ASP C 473      19.310  19.419 -89.322  1.00 21.10           C  
ANISOU 5026  CB  ASP C 473     3291   2820   1907     47   -682    325       C  
ATOM   5027  CG  ASP C 473      17.991  20.162 -89.212  1.00 29.92           C  
ANISOU 5027  CG  ASP C 473     4418   3862   3087     87   -851    308       C  
ATOM   5028  OD1 ASP C 473      17.988  21.307 -88.714  1.00 33.45           O  
ANISOU 5028  OD1 ASP C 473     4864   4248   3599     63   -873    382       O  
ATOM   5029  OD2 ASP C 473      16.953  19.590 -89.604  1.00 34.24           O  
ANISOU 5029  OD2 ASP C 473     4970   4410   3630    148   -970    211       O  
ATOM   5030  N   HIS C 474      18.546  16.737 -87.968  1.00 17.24           N  
ANISOU 5030  N   HIS C 474     2583   2353   1613     58   -700     63       N  
ATOM   5031  CA  HIS C 474      17.554  15.784 -87.491  1.00 16.80           C  
ANISOU 5031  CA  HIS C 474     2447   2274   1660     66   -778    -51       C  
ATOM   5032  C   HIS C 474      17.743  15.462 -86.011  1.00 17.60           C  
ANISOU 5032  C   HIS C 474     2429   2347   1911     11   -705    -73       C  
ATOM   5033  O   HIS C 474      16.786  15.484 -85.238  1.00 16.94           O  
ANISOU 5033  O   HIS C 474     2262   2224   1951     -1   -757   -113       O  
ATOM   5034  CB  HIS C 474      17.607  14.491 -88.307  1.00 17.45           C  
ANISOU 5034  CB  HIS C 474     2578   2399   1656    104   -803   -136       C  
ATOM   5035  CG  HIS C 474      16.642  13.445 -87.840  1.00 21.12           C  
ANISOU 5035  CG  HIS C 474     2960   2827   2237     95   -885   -247       C  
ATOM   5036  ND1 HIS C 474      15.276  13.585 -87.960  1.00 28.48           N  
ANISOU 5036  ND1 HIS C 474     3854   3722   3246    113  -1022   -298       N  
ATOM   5037  CD2 HIS C 474      16.846  12.246 -87.244  1.00 26.92           C  
ANISOU 5037  CD2 HIS C 474     3643   3552   3034     64   -850   -316       C  
ATOM   5038  CE1 HIS C 474      14.680  12.514 -87.466  1.00 26.91           C  
ANISOU 5038  CE1 HIS C 474     3572   3495   3157     82  -1056   -388       C  
ATOM   5039  NE2 HIS C 474      15.610  11.685 -87.028  1.00 31.31           N  
ANISOU 5039  NE2 HIS C 474     4131   4063   3702     50   -956   -395       N  
ATOM   5040  N   ILE C 475      18.979  15.156 -85.629  1.00 14.44           N  
ANISOU 5040  N   ILE C 475     2023   1968   1495    -17   -585    -52       N  
ATOM   5041  CA  ILE C 475      19.293  14.822 -84.244  1.00 14.58           C  
ANISOU 5041  CA  ILE C 475     1955   1951   1634    -56   -520    -74       C  
ATOM   5042  C   ILE C 475      18.891  15.947 -83.294  1.00 15.06           C  
ANISOU 5042  C   ILE C 475     1962   1960   1799    -71   -532    -25       C  
ATOM   5043  O   ILE C 475      18.304  15.703 -82.243  1.00 15.32           O  
ANISOU 5043  O   ILE C 475     1924   1958   1939    -84   -537    -65       O  
ATOM   5044  CB  ILE C 475      20.790  14.511 -84.072  1.00 16.32           C  
ANISOU 5044  CB  ILE C 475     2183   2200   1818    -69   -404    -61       C  
ATOM   5045  CG1 ILE C 475      21.137  13.192 -84.773  1.00 16.34           C  
ANISOU 5045  CG1 ILE C 475     2226   2249   1732    -40   -399   -140       C  
ATOM   5046  CG2 ILE C 475      21.155  14.432 -82.598  1.00 14.52           C  
ANISOU 5046  CG2 ILE C 475     1887   1920   1711    -96   -353    -73       C  
ATOM   5047  CD1 ILE C 475      22.619  12.947 -84.921  1.00 14.28           C  
ANISOU 5047  CD1 ILE C 475     1974   2042   1411    -33   -292   -137       C  
ATOM   5048  N   HIS C 476      19.183  17.185 -83.676  1.00 13.87           N  
ANISOU 5048  N   HIS C 476     1853   1804   1612    -66   -539     63       N  
ATOM   5049  CA  HIS C 476      18.849  18.328 -82.828  1.00 15.57           C  
ANISOU 5049  CA  HIS C 476     2030   1964   1922    -66   -570    106       C  
ATOM   5050  C   HIS C 476      17.340  18.589 -82.782  1.00 16.67           C  
ANISOU 5050  C   HIS C 476     2135   2085   2113    -31   -687     61       C  
ATOM   5051  O   HIS C 476      16.816  19.043 -81.764  1.00 16.16           O  
ANISOU 5051  O   HIS C 476     2002   1988   2151    -21   -706     47       O  
ATOM   5052  CB  HIS C 476      19.606  19.570 -83.296  1.00 20.20           C  
ANISOU 5052  CB  HIS C 476     2680   2534   2460    -79   -558    217       C  
ATOM   5053  CG  HIS C 476      21.051  19.568 -82.899  1.00 22.29           C  
ANISOU 5053  CG  HIS C 476     2929   2802   2739   -120   -442    257       C  
ATOM   5054  ND1 HIS C 476      21.459  19.602 -81.583  1.00 23.79           N  
ANISOU 5054  ND1 HIS C 476     3048   2948   3043   -128   -408    237       N  
ATOM   5055  CD2 HIS C 476      22.183  19.514 -83.640  1.00 25.69           C  
ANISOU 5055  CD2 HIS C 476     3398   3279   3086   -150   -354    307       C  
ATOM   5056  CE1 HIS C 476      22.779  19.581 -81.530  1.00 25.23           C  
ANISOU 5056  CE1 HIS C 476     3221   3140   3225   -161   -318    266       C  
ATOM   5057  NE2 HIS C 476      23.242  19.527 -82.766  1.00 24.82           N  
ANISOU 5057  NE2 HIS C 476     3224   3148   3058   -179   -276    309       N  
ATOM   5058  N   ARG C 477      16.645  18.294 -83.875  1.00 15.96           N  
ANISOU 5058  N   ARG C 477     2090   2020   1954     -4   -769     29       N  
ATOM   5059  CA  ARG C 477      15.191  18.388 -83.887  1.00 16.20           C  
ANISOU 5059  CA  ARG C 477     2068   2039   2048     32   -888    -37       C  
ATOM   5060  C   ARG C 477      14.562  17.380 -82.918  1.00 16.86           C  
ANISOU 5060  C   ARG C 477     2032   2127   2249      4   -857   -124       C  
ATOM   5061  O   ARG C 477      13.616  17.701 -82.196  1.00 18.85           O  
ANISOU 5061  O   ARG C 477     2192   2367   2605     15   -894   -162       O  
ATOM   5062  CB  ARG C 477      14.663  18.192 -85.311  1.00 20.24           C  
ANISOU 5062  CB  ARG C 477     2662   2569   2460     75   -995    -64       C  
ATOM   5063  CG  ARG C 477      15.024  19.330 -86.257  1.00 24.61           C  
ANISOU 5063  CG  ARG C 477     3350   3108   2893    108  -1041     29       C  
ATOM   5064  CD  ARG C 477      13.846  20.272 -86.431  1.00 35.09           C  
ANISOU 5064  CD  ARG C 477     4680   4394   4259    169  -1200      8       C  
ATOM   5065  NE  ARG C 477      12.603  19.522 -86.577  1.00 37.40           N  
ANISOU 5065  NE  ARG C 477     4893   4698   4620    202  -1300   -117       N  
ATOM   5066  CZ  ARG C 477      11.523  19.702 -85.821  1.00 33.75           C  
ANISOU 5066  CZ  ARG C 477     4301   4222   4301    211  -1307   -184       C  
ATOM   5067  NH1 ARG C 477      11.528  20.619 -84.857  1.00 40.29           N  
ANISOU 5067  NH1 ARG C 477     5080   5028   5200    211  -1275   -151       N  
ATOM   5068  NH2 ARG C 477      10.444  18.963 -86.025  1.00 38.83           N  
ANISOU 5068  NH2 ARG C 477     4867   4875   5012    221  -1341   -284       N  
ATOM   5069  N   VAL C 478      15.097  16.165 -82.892  1.00 16.66           N  
ANISOU 5069  N   VAL C 478     2011   2116   2202    -33   -787   -155       N  
ATOM   5070  CA  VAL C 478      14.616  15.154 -81.960  1.00 16.06           C  
ANISOU 5070  CA  VAL C 478     1846   2030   2228    -75   -747   -221       C  
ATOM   5071  C   VAL C 478      14.971  15.544 -80.523  1.00 16.37           C  
ANISOU 5071  C   VAL C 478     1836   2044   2339    -92   -656   -189       C  
ATOM   5072  O   VAL C 478      14.170  15.365 -79.602  1.00 16.38           O  
ANISOU 5072  O   VAL C 478     1750   2037   2437   -108   -640   -225       O  
ATOM   5073  CB  VAL C 478      15.198  13.761 -82.281  1.00 17.22           C  
ANISOU 5073  CB  VAL C 478     2034   2183   2327   -104   -711   -261       C  
ATOM   5074  CG1 VAL C 478      14.703  12.734 -81.287  1.00 20.96           C  
ANISOU 5074  CG1 VAL C 478     2434   2627   2904   -159   -673   -314       C  
ATOM   5075  CG2 VAL C 478      14.820  13.343 -83.702  1.00 19.42           C  
ANISOU 5075  CG2 VAL C 478     2370   2484   2527    -70   -814   -303       C  
ATOM   5076  N   LEU C 479      16.174  16.081 -80.330  1.00 13.78           N  
ANISOU 5076  N   LEU C 479     1564   1706   1966    -85   -596   -125       N  
ATOM   5077  CA  LEU C 479      16.590  16.531 -79.007  1.00 12.06           C  
ANISOU 5077  CA  LEU C 479     1316   1454   1811    -84   -531   -100       C  
ATOM   5078  C   LEU C 479      15.669  17.636 -78.500  1.00 13.90           C  
ANISOU 5078  C   LEU C 479     1493   1677   2111    -44   -588    -94       C  
ATOM   5079  O   LEU C 479      15.353  17.691 -77.313  1.00 15.97           O  
ANISOU 5079  O   LEU C 479     1700   1924   2442    -34   -548   -113       O  
ATOM   5080  CB  LEU C 479      18.039  17.015 -79.025  1.00 11.65           C  
ANISOU 5080  CB  LEU C 479     1324   1389   1715    -83   -479    -38       C  
ATOM   5081  CG  LEU C 479      19.086  15.905 -78.978  1.00 11.29           C  
ANISOU 5081  CG  LEU C 479     1308   1348   1632   -107   -403    -64       C  
ATOM   5082  CD1 LEU C 479      20.479  16.444 -79.296  1.00 13.18           C  
ANISOU 5082  CD1 LEU C 479     1586   1593   1830   -108   -358     -8       C  
ATOM   5083  CD2 LEU C 479      19.053  15.226 -77.613  1.00 14.18           C  
ANISOU 5083  CD2 LEU C 479     1647   1674   2067   -114   -353   -106       C  
ATOM   5084  N   ASP C 480      15.233  18.506 -79.408  1.00 14.12           N  
ANISOU 5084  N   ASP C 480     1545   1711   2108    -11   -684    -73       N  
ATOM   5085  CA  ASP C 480      14.299  19.569 -79.055  1.00 18.36           C  
ANISOU 5085  CA  ASP C 480     2033   2237   2704     43   -766    -82       C  
ATOM   5086  C   ASP C 480      12.966  18.997 -78.602  1.00 16.56           C  
ANISOU 5086  C   ASP C 480     1689   2042   2561     44   -778   -170       C  
ATOM   5087  O   ASP C 480      12.342  19.514 -77.678  1.00 15.69           O  
ANISOU 5087  O   ASP C 480     1504   1936   2523     82   -778   -196       O  
ATOM   5088  CB  ASP C 480      14.077  20.516 -80.231  1.00 19.03           C  
ANISOU 5088  CB  ASP C 480     2189   2313   2729     81   -885    -47       C  
ATOM   5089  CG  ASP C 480      15.247  21.442 -80.456  1.00 21.07           C  
ANISOU 5089  CG  ASP C 480     2545   2529   2931     76   -874     54       C  
ATOM   5090  OD1 ASP C 480      16.108  21.537 -79.560  1.00 17.65           O  
ANISOU 5090  OD1 ASP C 480     2101   2071   2533     58   -795     84       O  
ATOM   5091  OD2 ASP C 480      15.303  22.087 -81.521  1.00 21.88           O  
ANISOU 5091  OD2 ASP C 480     2737   2618   2957     89   -948    105       O  
ATOM   5092  N   LYS C 481      12.529  17.931 -79.263  1.00 17.22           N  
ANISOU 5092  N   LYS C 481     1754   2150   2638      5   -788   -219       N  
ATOM   5093  CA  LYS C 481      11.268  17.302 -78.909  1.00 16.59           C  
ANISOU 5093  CA  LYS C 481     1550   2098   2656    -14   -796   -300       C  
ATOM   5094  C   LYS C 481      11.341  16.666 -77.520  1.00 16.33           C  
ANISOU 5094  C   LYS C 481     1461   2064   2681    -59   -663   -305       C  
ATOM   5095  O   LYS C 481      10.364  16.679 -76.771  1.00 17.00           O  
ANISOU 5095  O   LYS C 481     1436   2175   2850    -58   -634   -347       O  
ATOM   5096  CB  LYS C 481      10.878  16.261 -79.957  1.00 17.94           C  
ANISOU 5096  CB  LYS C 481     1731   2277   2807    -50   -842   -347       C  
ATOM   5097  CG  LYS C 481       9.596  15.530 -79.617  1.00 21.96           C  
ANISOU 5097  CG  LYS C 481     2129   2805   3411    -86   -814   -412       C  
ATOM   5098  CD  LYS C 481       8.443  16.512 -79.478  1.00 28.59           C  
ANISOU 5098  CD  LYS C 481     2897   3667   4299    -25   -854   -440       C  
ATOM   5099  CE  LYS C 481       7.313  15.912 -78.667  1.00 31.16           C  
ANISOU 5099  CE  LYS C 481     3084   4021   4733    -70   -786   -492       C  
ATOM   5100  NZ  LYS C 481       6.984  14.540 -79.123  1.00 34.83           N  
ANISOU 5100  NZ  LYS C 481     3528   4475   5229   -147   -785   -525       N  
ATOM   5101  N   ILE C 482      12.499  16.112 -77.175  1.00 15.21           N  
ANISOU 5101  N   ILE C 482     1401   1892   2487    -92   -576   -263       N  
ATOM   5102  CA  ILE C 482      12.673  15.541 -75.848  1.00 13.92           C  
ANISOU 5102  CA  ILE C 482     1219   1712   2358   -123   -459   -261       C  
ATOM   5103  C   ILE C 482      12.701  16.644 -74.784  1.00 13.85           C  
ANISOU 5103  C   ILE C 482     1192   1700   2371    -55   -433   -239       C  
ATOM   5104  O   ILE C 482      12.194  16.455 -73.676  1.00 14.84           O  
ANISOU 5104  O   ILE C 482     1262   1836   2542    -56   -357   -257       O  
ATOM   5105  CB  ILE C 482      13.952  14.687 -75.761  1.00 16.76           C  
ANISOU 5105  CB  ILE C 482     1682   2033   2655   -157   -396   -236       C  
ATOM   5106  CG1 ILE C 482      13.901  13.563 -76.794  1.00 17.36           C  
ANISOU 5106  CG1 ILE C 482     1781   2111   2704   -208   -433   -270       C  
ATOM   5107  CG2 ILE C 482      14.095  14.088 -74.376  1.00 18.58           C  
ANISOU 5107  CG2 ILE C 482     1917   2231   2910   -180   -289   -235       C  
ATOM   5108  CD1 ILE C 482      15.164  12.742 -76.855  1.00 21.02           C  
ANISOU 5108  CD1 ILE C 482     2344   2543   3099   -225   -390   -261       C  
ATOM   5109  N   THR C 483      13.285  17.793 -75.121  1.00 14.04           N  
ANISOU 5109  N   THR C 483     1269   1706   2360      4   -498   -199       N  
ATOM   5110  CA  THR C 483      13.239  18.952 -74.231  1.00 13.07           C  
ANISOU 5110  CA  THR C 483     1132   1570   2264     82   -512   -187       C  
ATOM   5111  C   THR C 483      11.794  19.357 -73.967  1.00 13.89           C  
ANISOU 5111  C   THR C 483     1118   1726   2435    124   -548   -247       C  
ATOM   5112  O   THR C 483      11.390  19.548 -72.820  1.00 15.85           O  
ANISOU 5112  O   THR C 483     1314   1991   2718    164   -490   -270       O  
ATOM   5113  CB  THR C 483      13.994  20.160 -74.812  1.00 16.88           C  
ANISOU 5113  CB  THR C 483     1690   2012   2710    126   -601   -131       C  
ATOM   5114  OG1 THR C 483      15.375  19.827 -74.978  1.00 16.45           O  
ANISOU 5114  OG1 THR C 483     1721   1920   2607     87   -553    -81       O  
ATOM   5115  CG2 THR C 483      13.874  21.362 -73.879  1.00 21.86           C  
ANISOU 5115  CG2 THR C 483     2317   2618   3372    211   -632   -129       C  
ATOM   5116  N   ASP C 484      11.024  19.476 -75.045  1.00 14.88           N  
ANISOU 5116  N   ASP C 484     1212   1877   2564    120   -636   -275       N  
ATOM   5117  CA  ASP C 484       9.596  19.770 -74.959  1.00 15.19           C  
ANISOU 5117  CA  ASP C 484     1162   1966   2645    152   -651   -336       C  
ATOM   5118  C   ASP C 484       8.871  18.763 -74.074  1.00 18.20           C  
ANISOU 5118  C   ASP C 484     1419   2394   3100     99   -543   -383       C  
ATOM   5119  O   ASP C 484       7.968  19.113 -73.310  1.00 18.71           O  
ANISOU 5119  O   ASP C 484     1397   2506   3206    138   -504   -422       O  
ATOM   5120  CB  ASP C 484       8.961  19.757 -76.351  1.00 16.08           C  
ANISOU 5120  CB  ASP C 484     1286   2084   2739    145   -748   -360       C  
ATOM   5121  CG  ASP C 484       9.469  20.873 -77.243  1.00 25.92           C  
ANISOU 5121  CG  ASP C 484     2652   3285   3910    197   -849   -313       C  
ATOM   5122  OD1 ASP C 484      10.127  21.805 -76.735  1.00 25.53           O  
ANISOU 5122  OD1 ASP C 484     2666   3200   3835    237   -847   -266       O  
ATOM   5123  OD2 ASP C 484       9.200  20.817 -78.466  1.00 28.23           O  
ANISOU 5123  OD2 ASP C 484     2985   3572   4168    196   -931   -322       O  
ATOM   5124  N   THR C 485       9.274  17.506 -74.200  1.00 17.27           N  
ANISOU 5124  N   THR C 485     1303   2263   2996      6   -488   -377       N  
ATOM   5125  CA  THR C 485       8.657  16.413 -73.470  1.00 17.26           C  
ANISOU 5125  CA  THR C 485     1210   2288   3061    -75   -373   -405       C  
ATOM   5126  C   THR C 485       8.978  16.491 -71.977  1.00 17.57           C  
ANISOU 5126  C   THR C 485     1270   2325   3081    -52   -241   -376       C  
ATOM   5127  O   THR C 485       8.109  16.261 -71.136  1.00 18.63           O  
ANISOU 5127  O   THR C 485     1301   2509   3270    -67   -147   -404       O  
ATOM   5128  CB  THR C 485       9.113  15.058 -74.036  1.00 18.93           C  
ANISOU 5128  CB  THR C 485     1481   2457   3253   -179   -353   -392       C  
ATOM   5129  OG1 THR C 485       8.643  14.922 -75.383  1.00 18.46           O  
ANISOU 5129  OG1 THR C 485     1424   2404   3188   -185   -465   -421       O  
ATOM   5130  CG2 THR C 485       8.550  13.928 -73.217  1.00 21.97           C  
ANISOU 5130  CG2 THR C 485     1802   2847   3699   -276   -230   -402       C  
ATOM   5131  N   LEU C 486      10.229  16.815 -71.651  1.00 16.74           N  
ANISOU 5131  N   LEU C 486     1301   2162   2897    -11   -233   -321       N  
ATOM   5132  CA  LEU C 486      10.626  16.995 -70.255  1.00 16.57           C  
ANISOU 5132  CA  LEU C 486     1327   2125   2845     37   -135   -299       C  
ATOM   5133  C   LEU C 486       9.865  18.137 -69.602  1.00 16.37           C  
ANISOU 5133  C   LEU C 486     1217   2153   2848    145   -151   -335       C  
ATOM   5134  O   LEU C 486       9.375  18.006 -68.479  1.00 17.95           O  
ANISOU 5134  O   LEU C 486     1376   2391   3053    167    -41   -349       O  
ATOM   5135  CB  LEU C 486      12.130  17.248 -70.139  1.00 17.10           C  
ANISOU 5135  CB  LEU C 486     1543   2113   2841     72   -157   -249       C  
ATOM   5136  CG  LEU C 486      13.018  16.010 -70.029  1.00 19.98           C  
ANISOU 5136  CG  LEU C 486     2008   2422   3163     -3    -90   -223       C  
ATOM   5137  CD1 LEU C 486      14.471  16.395 -70.202  1.00 19.89           C  
ANISOU 5137  CD1 LEU C 486     2108   2346   3103     36   -138   -191       C  
ATOM   5138  CD2 LEU C 486      12.801  15.315 -68.685  1.00 20.09           C  
ANISOU 5138  CD2 LEU C 486     2045   2425   3163    -16     39   -221       C  
ATOM   5139  N   ILE C 487       9.777  19.256 -70.312  1.00 16.59           N  
ANISOU 5139  N   ILE C 487     1232   2184   2889    218   -290   -350       N  
ATOM   5140  CA  ILE C 487       9.054  20.424 -69.824  1.00 19.84           C  
ANISOU 5140  CA  ILE C 487     1592   2637   3310    329   -334   -389       C  
ATOM   5141  C   ILE C 487       7.589  20.078 -69.604  1.00 16.41           C  
ANISOU 5141  C   ILE C 487     1006   2296   2931    307   -270   -451       C  
ATOM   5142  O   ILE C 487       6.978  20.506 -68.624  1.00 20.34           O  
ANISOU 5142  O   ILE C 487     1453   2849   3427    376   -210   -480       O  
ATOM   5143  CB  ILE C 487       9.176  21.611 -70.805  1.00 22.87           C  
ANISOU 5143  CB  ILE C 487     2065   2981   3644    370   -479   -368       C  
ATOM   5144  CG1 ILE C 487      10.583  22.210 -70.730  1.00 19.88           C  
ANISOU 5144  CG1 ILE C 487     1835   2514   3206    392   -516   -301       C  
ATOM   5145  CG2 ILE C 487       8.147  22.692 -70.493  1.00 22.44           C  
ANISOU 5145  CG2 ILE C 487     1976   2967   3585    453   -520   -413       C  
ATOM   5146  CD1 ILE C 487      10.907  22.829 -69.391  1.00 21.24           C  
ANISOU 5146  CD1 ILE C 487     2057   2668   3345    469   -475   -296       C  
ATOM   5147  N   HIS C 488       7.040  19.272 -70.504  1.00 17.70           N  
ANISOU 5147  N   HIS C 488     1107   2477   3139    209   -281   -468       N  
ATOM   5148  CA  HIS C 488       5.633  18.898 -70.425  1.00 18.65           C  
ANISOU 5148  CA  HIS C 488     1087   2677   3323    172   -231   -522       C  
ATOM   5149  C   HIS C 488       5.355  17.996 -69.222  1.00 19.24           C  
ANISOU 5149  C   HIS C 488     1081   2797   3430    111    -42   -519       C  
ATOM   5150  O   HIS C 488       4.334  18.150 -68.555  1.00 20.58           O  
ANISOU 5150  O   HIS C 488     1144   3047   3627    134     33   -553       O  
ATOM   5151  CB  HIS C 488       5.193  18.213 -71.716  1.00 22.75           C  
ANISOU 5151  CB  HIS C 488     1585   3182   3876     85   -302   -537       C  
ATOM   5152  CG  HIS C 488       3.757  17.797 -71.710  1.00 24.34           C  
ANISOU 5152  CG  HIS C 488     1641   3450   4156     43   -265   -592       C  
ATOM   5153  ND1 HIS C 488       3.362  16.482 -71.582  1.00 30.02           N  
ANISOU 5153  ND1 HIS C 488     2294   4180   4934    -84   -168   -587       N  
ATOM   5154  CD2 HIS C 488       2.622  18.528 -71.778  1.00 24.30           C  
ANISOU 5154  CD2 HIS C 488     1546   3499   4186    109   -314   -654       C  
ATOM   5155  CE1 HIS C 488       2.043  16.421 -71.595  1.00 30.81           C  
ANISOU 5155  CE1 HIS C 488     2259   4341   5107    -98   -158   -638       C  
ATOM   5156  NE2 HIS C 488       1.568  17.648 -71.715  1.00 30.90           N  
ANISOU 5156  NE2 HIS C 488     2248   4384   5109     22   -245   -686       N  
ATOM   5157  N   LEU C 489       6.259  17.057 -68.948  1.00 17.91           N  
ANISOU 5157  N   LEU C 489      974   2575   3255     32     42   -475       N  
ATOM   5158  CA  LEU C 489       6.135  16.210 -67.764  1.00 20.45           C  
ANISOU 5158  CA  LEU C 489     1299   2911   3561    -31    234   -443       C  
ATOM   5159  C   LEU C 489       6.111  17.058 -66.500  1.00 18.76           C  
ANISOU 5159  C   LEU C 489     1098   2740   3289    100    307   -449       C  
ATOM   5160  O   LEU C 489       5.345  16.794 -65.574  1.00 20.05           O  
ANISOU 5160  O   LEU C 489     1175   2978   3465     88    458   -460       O  
ATOM   5161  CB  LEU C 489       7.279  15.196 -67.686  1.00 17.42           C  
ANISOU 5161  CB  LEU C 489     1093   2423   3103   -114    278   -368       C  
ATOM   5162  CG  LEU C 489       7.284  14.038 -68.686  1.00 18.88           C  
ANISOU 5162  CG  LEU C 489     1278   2563   3333   -253    241   -361       C  
ATOM   5163  CD1 LEU C 489       8.635  13.330 -68.677  1.00 20.43           C  
ANISOU 5163  CD1 LEU C 489     1670   2653   3438   -284    243   -303       C  
ATOM   5164  CD2 LEU C 489       6.156  13.068 -68.357  1.00 23.62           C  
ANISOU 5164  CD2 LEU C 489     1746   3206   4024   -379    361   -373       C  
ATOM   5165  N   MET C 490       6.953  18.084 -66.477  1.00 17.93           N  
ANISOU 5165  N   MET C 490     1103   2587   3121    225    198   -441       N  
ATOM   5166  CA  MET C 490       7.044  18.979 -65.333  1.00 19.63           C  
ANISOU 5166  CA  MET C 490     1355   2826   3279    372    229   -455       C  
ATOM   5167  C   MET C 490       5.788  19.841 -65.194  1.00 20.30           C  
ANISOU 5167  C   MET C 490     1297   3017   3400    456    204   -523       C  
ATOM   5168  O   MET C 490       5.331  20.112 -64.079  1.00 23.07           O  
ANISOU 5168  O   MET C 490     1626   3431   3708    534    306   -538       O  
ATOM   5169  CB  MET C 490       8.288  19.857 -65.459  1.00 18.63           C  
ANISOU 5169  CB  MET C 490     1385   2600   3095    469     91   -427       C  
ATOM   5170  CG  MET C 490       9.589  19.073 -65.356  1.00 17.29           C  
ANISOU 5170  CG  MET C 490     1385   2323   2861    402    124   -355       C  
ATOM   5171  SD  MET C 490      11.041  20.055 -65.737  1.00 18.76           S  
ANISOU 5171  SD  MET C 490     1714   2398   3016    484    -42   -325       S  
ATOM   5172  CE  MET C 490      12.269  18.765 -65.948  1.00 18.36           C  
ANISOU 5172  CE  MET C 490     1797   2257   2922    366     11   -265       C  
ATOM   5173  N   ALA C 491       5.231  20.262 -66.327  1.00 19.21           N  
ANISOU 5173  N   ALA C 491     1110   2885   3306    437     64   -547       N  
ATOM   5174  CA  ALA C 491       4.004  21.056 -66.336  1.00 20.93           C  
ANISOU 5174  CA  ALA C 491     1231   3177   3544    501     20   -603       C  
ATOM   5175  C   ALA C 491       2.823  20.215 -65.862  1.00 24.75           C  
ANISOU 5175  C   ALA C 491     1550   3766   4088    425    179   -628       C  
ATOM   5176  O   ALA C 491       1.985  20.682 -65.089  1.00 24.90           O  
ANISOU 5176  O   ALA C 491     1491   3868   4102    499    243   -663       O  
ATOM   5177  CB  ALA C 491       3.739  21.618 -67.729  1.00 24.88           C  
ANISOU 5177  CB  ALA C 491     1745   3640   4070    494   -162   -626       C  
ATOM   5178  N   LYS C 492       2.772  18.969 -66.327  1.00 22.43           N  
ANISOU 5178  N   LYS C 492     1214   3460   3848    272    243   -604       N  
ATOM   5179  CA  LYS C 492       1.764  18.010 -65.880  1.00 24.83           C  
ANISOU 5179  CA  LYS C 492     1386   3839   4207    163    402   -602       C  
ATOM   5180  C   LYS C 492       1.775  17.862 -64.362  1.00 24.85           C  
ANISOU 5180  C   LYS C 492     1397   3900   4145    197    603   -571       C  
ATOM   5181  O   LYS C 492       0.728  17.717 -63.734  1.00 30.09           O  
ANISOU 5181  O   LYS C 492     1942   4661   4830    185    723   -580       O  
ATOM   5182  CB  LYS C 492       2.001  16.643 -66.528  1.00 26.34           C  
ANISOU 5182  CB  LYS C 492     1593   3969   4446    -14    428   -560       C  
ATOM   5183  CG  LYS C 492       1.044  16.278 -67.648  1.00 32.64           C  
ANISOU 5183  CG  LYS C 492     2289   4775   5338    -90    331   -599       C  
ATOM   5184  CD  LYS C 492       1.553  15.062 -68.417  1.00 26.89           C  
ANISOU 5184  CD  LYS C 492     1627   3957   4632   -233    308   -558       C  
ATOM   5185  CE  LYS C 492       0.613  13.870 -68.269  1.00 31.56           C  
ANISOU 5185  CE  LYS C 492     2118   4572   5300   -380    409   -541       C  
ATOM   5186  NZ  LYS C 492       1.218  12.614 -68.805  1.00 36.03           N  
ANISOU 5186  NZ  LYS C 492     2781   5038   5871   -512    395   -492       N  
ATOM   5187  N   ALA C 493       2.972  17.902 -63.782  1.00 23.96           N  
ANISOU 5187  N   ALA C 493     1433   3724   3949    247    639   -534       N  
ATOM   5188  CA  ALA C 493       3.143  17.696 -62.347  1.00 26.33           C  
ANISOU 5188  CA  ALA C 493     1791   4056   4157    289    829   -501       C  
ATOM   5189  C   ALA C 493       2.849  18.955 -61.542  1.00 26.67           C  
ANISOU 5189  C   ALA C 493     1837   4162   4135    486    808   -542       C  
ATOM   5190  O   ALA C 493       2.811  18.912 -60.315  1.00 27.83           O  
ANISOU 5190  O   ALA C 493     2030   4351   4191    550    962   -521       O  
ATOM   5191  CB  ALA C 493       4.546  17.205 -62.050  1.00 24.33           C  
ANISOU 5191  CB  ALA C 493     1722   3685   3838    273    867   -453       C  
ATOM   5192  N   GLY C 494       2.667  20.076 -62.231  1.00 25.40           N  
ANISOU 5192  N   GLY C 494     1654   3988   4007    581    613   -593       N  
ATOM   5193  CA  GLY C 494       2.230  21.296 -61.579  1.00 24.54           C  
ANISOU 5193  CA  GLY C 494     1548   3920   3857    746    571   -637       C  
ATOM   5194  C   GLY C 494       3.323  22.271 -61.189  1.00 23.55           C  
ANISOU 5194  C   GLY C 494     1609   3694   3644    883    452   -628       C  
ATOM   5195  O   GLY C 494       3.074  23.215 -60.440  1.00 26.82           O  
ANISOU 5195  O   GLY C 494     2057   4124   4010   1011    427   -660       O  
ATOM   5196  N   LEU C 495       4.533  22.054 -61.692  1.00 24.27           N  
ANISOU 5196  N   LEU C 495     1825   3676   3719    848    369   -585       N  
ATOM   5197  CA  LEU C 495       5.627  22.979 -61.420  1.00 22.11           C  
ANISOU 5197  CA  LEU C 495     1736   3288   3374    948    236   -562       C  
ATOM   5198  C   LEU C 495       5.355  24.315 -62.103  1.00 21.77           C  
ANISOU 5198  C   LEU C 495     1703   3219   3348    995     37   -590       C  
ATOM   5199  O   LEU C 495       4.756  24.357 -63.177  1.00 21.25           O  
ANISOU 5199  O   LEU C 495     1546   3178   3348    937    -37   -615       O  
ATOM   5200  CB  LEU C 495       6.968  22.414 -61.901  1.00 21.42           C  
ANISOU 5200  CB  LEU C 495     1770   3090   3278    885    193   -506       C  
ATOM   5201  CG  LEU C 495       7.433  21.015 -61.483  1.00 27.02           C  
ANISOU 5201  CG  LEU C 495     2498   3799   3970    816    363   -486       C  
ATOM   5202  CD1 LEU C 495       8.939  20.883 -61.681  1.00 21.95           C  
ANISOU 5202  CD1 LEU C 495     2029   3015   3295    812    276   -440       C  
ATOM   5203  CD2 LEU C 495       7.051  20.690 -60.056  1.00 29.61           C  
ANISOU 5203  CD2 LEU C 495     2845   4190   4213    877    553   -491       C  
ATOM   5204  N   THR C 496       5.795  25.405 -61.482  1.00 23.87           N  
ANISOU 5204  N   THR C 496     2093   3427   3549   1090    -52   -590       N  
ATOM   5205  CA  THR C 496       5.711  26.714 -62.119  1.00 26.30           C  
ANISOU 5205  CA  THR C 496     2444   3691   3855   1116   -237   -613       C  
ATOM   5206  C   THR C 496       6.669  26.743 -63.305  1.00 25.58           C  
ANISOU 5206  C   THR C 496     2444   3499   3778   1021   -345   -554       C  
ATOM   5207  O   THR C 496       7.527  25.872 -63.426  1.00 21.12           O  
ANISOU 5207  O   THR C 496     1921   2889   3213    958   -292   -498       O  
ATOM   5208  CB  THR C 496       6.063  27.862 -61.150  1.00 26.19           C  
ANISOU 5208  CB  THR C 496     2550   3636   3766   1213   -305   -626       C  
ATOM   5209  OG1 THR C 496       7.407  27.699 -60.685  1.00 23.12           O  
ANISOU 5209  OG1 THR C 496     2308   3148   3328   1187   -302   -559       O  
ATOM   5210  CG2 THR C 496       5.124  27.868 -59.951  1.00 29.24           C  
ANISOU 5210  CG2 THR C 496     2856   4129   4123   1320   -195   -688       C  
ATOM   5211  N   LEU C 497       6.522  27.737 -64.176  1.00 23.78           N  
ANISOU 5211  N   LEU C 497     2874   2623   3539     99     78   -516       N  
ATOM   5212  CA  LEU C 497       7.431  27.894 -65.305  1.00 24.30           C  
ANISOU 5212  CA  LEU C 497     2994   2644   3597     95     32   -469       C  
ATOM   5213  C   LEU C 497       8.870  28.033 -64.831  1.00 22.32           C  
ANISOU 5213  C   LEU C 497     2811   2363   3307     51     47   -475       C  
ATOM   5214  O   LEU C 497       9.782  27.454 -65.418  1.00 24.51           O  
ANISOU 5214  O   LEU C 497     3123   2639   3552     15     22   -441       O  
ATOM   5215  CB  LEU C 497       7.038  29.104 -66.153  1.00 25.82           C  
ANISOU 5215  CB  LEU C 497     3190   2779   3842    161      5   -455       C  
ATOM   5216  CG  LEU C 497       5.867  28.867 -67.102  1.00 24.56           C  
ANISOU 5216  CG  LEU C 497     2972   2642   3717    198    -35   -424       C  
ATOM   5217  CD1 LEU C 497       5.489  30.152 -67.817  1.00 28.67           C  
ANISOU 5217  CD1 LEU C 497     3499   3100   4294    265    -62   -411       C  
ATOM   5218  CD2 LEU C 497       6.242  27.781 -68.100  1.00 25.57           C  
ANISOU 5218  CD2 LEU C 497     3115   2796   3805    156    -79   -374       C  
ATOM   5219  N   GLN C 498       9.066  28.791 -63.758  1.00 21.46           N  
ANISOU 5219  N   GLN C 498     2721   2231   3202     54     89   -521       N  
ATOM   5220  CA  GLN C 498      10.403  28.987 -63.211  1.00 22.56           C  
ANISOU 5220  CA  GLN C 498     2923   2343   3307      9    102   -527       C  
ATOM   5221  C   GLN C 498      10.978  27.669 -62.700  1.00 18.89           C  
ANISOU 5221  C   GLN C 498     2458   1929   2789    -59    107   -521       C  
ATOM   5222  O   GLN C 498      12.139  27.357 -62.958  1.00 20.96           O  
ANISOU 5222  O   GLN C 498     2762   2179   3023    -96     90   -494       O  
ATOM   5223  CB  GLN C 498      10.386  30.032 -62.092  1.00 24.38           C  
ANISOU 5223  CB  GLN C 498     3175   2540   3550     22    146   -581       C  
ATOM   5224  CG  GLN C 498      11.737  30.225 -61.414  1.00 22.45           C  
ANISOU 5224  CG  GLN C 498     2993   2269   3266    -31    158   -589       C  
ATOM   5225  CD  GLN C 498      11.684  31.229 -60.277  1.00 27.29           C  
ANISOU 5225  CD  GLN C 498     3633   2849   3886    -22    201   -645       C  
ATOM   5226  OE1 GLN C 498      10.645  31.416 -59.646  1.00 33.25           O  
ANISOU 5226  OE1 GLN C 498     4351   3622   4658      8    236   -688       O  
ATOM   5227  NE2 GLN C 498      12.807  31.884 -60.013  1.00 25.84           N  
ANISOU 5227  NE2 GLN C 498     3515   2617   3687    -51    198   -645       N  
ATOM   5228  N   GLN C 499      10.160  26.895 -61.991  1.00 19.09           N  
ANISOU 5228  N   GLN C 499     2436   2012   2803    -73    130   -544       N  
ATOM   5229  CA  GLN C 499      10.590  25.591 -61.494  1.00 18.02           C  
ANISOU 5229  CA  GLN C 499     2300   1925   2620   -137    130   -536       C  
ATOM   5230  C   GLN C 499      10.873  24.629 -62.642  1.00 15.97           C  
ANISOU 5230  C   GLN C 499     2040   1679   2347   -150     84   -485       C  
ATOM   5231  O   GLN C 499      11.786  23.807 -62.548  1.00 18.83           O  
ANISOU 5231  O   GLN C 499     2428   2052   2673   -198     73   -467       O  
ATOM   5232  CB  GLN C 499       9.548  24.979 -60.554  1.00 19.47           C  
ANISOU 5232  CB  GLN C 499     2433   2170   2794   -152    162   -568       C  
ATOM   5233  CG  GLN C 499       9.387  25.707 -59.231  1.00 20.54           C  
ANISOU 5233  CG  GLN C 499     2576   2302   2927   -155    215   -624       C  
ATOM   5234  CD  GLN C 499       8.175  25.234 -58.454  1.00 23.36           C  
ANISOU 5234  CD  GLN C 499     2873   2720   3281   -160    251   -656       C  
ATOM   5235  OE1 GLN C 499       7.176  24.809 -59.036  1.00 22.98           O  
ANISOU 5235  OE1 GLN C 499     2768   2707   3256   -136    237   -641       O  
ATOM   5236  NE2 GLN C 499       8.259  25.301 -57.132  1.00 31.25           N  
ANISOU 5236  NE2 GLN C 499     3886   3736   4250   -196    297   -699       N  
ATOM   5237  N   GLN C 500      10.092  24.727 -63.717  1.00 14.29           N  
ANISOU 5237  N   GLN C 500     1799   1465   2165   -107     56   -462       N  
ATOM   5238  CA  GLN C 500      10.319  23.904 -64.903  1.00 15.89           C  
ANISOU 5238  CA  GLN C 500     2007   1675   2353   -117     12   -415       C  
ATOM   5239  C   GLN C 500      11.697  24.163 -65.506  1.00 15.34           C  
ANISOU 5239  C   GLN C 500     1998   1563   2269   -129     -4   -388       C  
ATOM   5240  O   GLN C 500      12.452  23.225 -65.760  1.00 20.61           O  
ANISOU 5240  O   GLN C 500     2684   2243   2903   -166    -19   -366       O  
ATOM   5241  CB  GLN C 500       9.244  24.149 -65.969  1.00 22.55           C  
ANISOU 5241  CB  GLN C 500     2815   2519   3232    -69    -19   -393       C  
ATOM   5242  CG  GLN C 500       7.844  23.685 -65.598  1.00 24.19           C  
ANISOU 5242  CG  GLN C 500     2955   2780   3456    -60    -11   -409       C  
ATOM   5243  CD  GLN C 500       6.792  24.160 -66.585  1.00 22.51           C  
ANISOU 5243  CD  GLN C 500     2704   2561   3288     -7    -42   -388       C  
ATOM   5244  OE1 GLN C 500       7.042  24.239 -67.787  1.00 23.98           O  
ANISOU 5244  OE1 GLN C 500     2915   2720   3475      6    -85   -349       O  
ATOM   5245  NE2 GLN C 500       5.606  24.478 -66.078  1.00 22.49           N  
ANISOU 5245  NE2 GLN C 500     2640   2585   3321     25    -22   -414       N  
ATOM   5246  N   HIS C 501      12.015  25.435 -65.737  1.00 15.00           N  
ANISOU 5246  N   HIS C 501     1982   1466   2251    -98     -2   -390       N  
ATOM   5247  CA  HIS C 501      13.304  25.808 -66.316  1.00 18.89           C  
ANISOU 5247  CA  HIS C 501     2528   1918   2731   -111    -15   -364       C  
ATOM   5248  C   HIS C 501      14.452  25.356 -65.427  0.93 15.04           C  
ANISOU 5248  C   HIS C 501     2067   1438   2209   -164      4   -374       C  
ATOM   5249  O   HIS C 501      15.446  24.807 -65.909  0.86 14.56           O  
ANISOU 5249  O   HIS C 501     2031   1378   2125   -191    -10   -345       O  
ATOM   5250  CB  HIS C 501      13.423  27.319 -66.522  1.00 22.43           C  
ANISOU 5250  CB  HIS C 501     3004   2306   3212    -74    -14   -368       C  
ATOM   5251  CG  HIS C 501      12.281  27.938 -67.266  1.00 29.42           C  
ANISOU 5251  CG  HIS C 501     3864   3176   4139    -17    -34   -361       C  
ATOM   5252  ND1 HIS C 501      12.077  29.301 -67.297  1.00 32.85           N  
ANISOU 5252  ND1 HIS C 501     4314   3555   4611     25    -33   -371       N  
ATOM   5253  CD2 HIS C 501      11.279  27.392 -67.993  1.00 34.32           C  
ANISOU 5253  CD2 HIS C 501     4443   3825   4770      4    -60   -342       C  
ATOM   5254  CE1 HIS C 501      11.006  29.569 -68.022  1.00 31.27           C  
ANISOU 5254  CE1 HIS C 501     4083   3352   4447     73    -58   -358       C  
ATOM   5255  NE2 HIS C 501      10.497  28.429 -68.449  1.00 34.30           N  
ANISOU 5255  NE2 HIS C 501     4430   3789   4815     60    -75   -340       N  
ATOM   5256  N   GLN C 502      14.312  25.615 -64.128  1.00 14.46           N  
ANISOU 5256  N   GLN C 502     1988   1371   2134   -178     37   -414       N  
ATOM   5257  CA  GLN C 502      15.358  25.302 -63.165  1.00 13.87           C  
ANISOU 5257  CA  GLN C 502     1940   1302   2028   -230     53   -424       C  
ATOM   5258  C   GLN C 502      15.617  23.801 -63.114  1.00 15.00           C  
ANISOU 5258  C   GLN C 502     2069   1490   2138   -270     40   -406       C  
ATOM   5259  O   GLN C 502      16.769  23.370 -63.129  1.00 14.89           O  
ANISOU 5259  O   GLN C 502     2080   1473   2104   -304     31   -387       O  
ATOM   5260  CB  GLN C 502      14.990  25.823 -61.774  1.00 18.30           C  
ANISOU 5260  CB  GLN C 502     2499   1865   2588   -239     90   -473       C  
ATOM   5261  CG  GLN C 502      15.108  27.334 -61.622  1.00 14.66           C  
ANISOU 5261  CG  GLN C 502     2070   1348   2154   -210    104   -493       C  
ATOM   5262  CD  GLN C 502      14.710  27.809 -60.238  1.00 17.28           C  
ANISOU 5262  CD  GLN C 502     2404   1682   2481   -219    145   -547       C  
ATOM   5263  OE1 GLN C 502      14.374  27.007 -59.366  1.00 22.03           O  
ANISOU 5263  OE1 GLN C 502     2983   2330   3056   -251    164   -567       O  
ATOM   5264  NE2 GLN C 502      14.749  29.120 -60.030  1.00 21.30           N  
ANISOU 5264  NE2 GLN C 502     2944   2138   3012   -193    159   -571       N  
ATOM   5265  N   ARG C 503      14.548  23.008 -63.069  1.00 14.08           N  
ANISOU 5265  N   ARG C 503     1912   1417   2020   -267     38   -413       N  
ATOM   5266  CA  ARG C 503      14.685  21.551 -63.014  1.00 13.29           C  
ANISOU 5266  CA  ARG C 503     1803   1357   1890   -305     23   -397       C  
ATOM   5267  C   ARG C 503      15.275  20.995 -64.306  1.00 13.58           C  
ANISOU 5267  C   ARG C 503     1855   1384   1920   -299     -9   -355       C  
ATOM   5268  O   ARG C 503      16.099  20.077 -64.281  1.00 13.56           O  
ANISOU 5268  O   ARG C 503     1867   1390   1893   -332    -20   -339       O  
ATOM   5269  CB  ARG C 503      13.338  20.888 -62.736  1.00 13.50           C  
ANISOU 5269  CB  ARG C 503     1782   1431   1915   -304     27   -410       C  
ATOM   5270  CG  ARG C 503      13.439  19.398 -62.451  1.00 14.95           C  
ANISOU 5270  CG  ARG C 503     1960   1654   2065   -352     12   -398       C  
ATOM   5271  CD  ARG C 503      12.093  18.830 -62.036  1.00 14.86           C  
ANISOU 5271  CD  ARG C 503     1902   1691   2051   -359     19   -413       C  
ATOM   5272  NE  ARG C 503      12.140  17.385 -61.850  1.00 16.42           N  
ANISOU 5272  NE  ARG C 503     2098   1923   2216   -406     -1   -398       N  
ATOM   5273  CZ  ARG C 503      12.590  16.794 -60.749  1.00 17.91           C  
ANISOU 5273  CZ  ARG C 503     2300   2129   2375   -457      9   -408       C  
ATOM   5274  NH1 ARG C 503      13.035  17.528 -59.737  1.00 20.48           N  
ANISOU 5274  NH1 ARG C 503     2641   2443   2696   -470     39   -434       N  
ATOM   5275  NH2 ARG C 503      12.590  15.468 -60.658  1.00 21.99           N  
ANISOU 5275  NH2 ARG C 503     2819   2671   2865   -497    -15   -391       N  
ATOM   5276  N   LEU C 504      14.842  21.540 -65.438  1.00 13.90           N  
ANISOU 5276  N   LEU C 504     1894   1405   1983   -257    -25   -339       N  
ATOM   5277  CA  LEU C 504      15.403  21.141 -66.720  1.00 12.93           C  
ANISOU 5277  CA  LEU C 504     1791   1270   1850   -252    -52   -302       C  
ATOM   5278  C   LEU C 504      16.918  21.328 -66.695  1.00 12.68           C  
ANISOU 5278  C   LEU C 504     1797   1212   1807   -273    -46   -289       C  
ATOM   5279  O   LEU C 504      17.669  20.433 -67.079  1.00 13.01           O  
ANISOU 5279  O   LEU C 504     1852   1263   1828   -293    -56   -270       O  
ATOM   5280  CB  LEU C 504      14.782  21.945 -67.858  1.00 14.21           C  
ANISOU 5280  CB  LEU C 504     1953   1409   2038   -207    -70   -285       C  
ATOM   5281  CG  LEU C 504      15.395  21.703 -69.241  1.00 14.40           C  
ANISOU 5281  CG  LEU C 504     2007   1417   2047   -203    -95   -248       C  
ATOM   5282  CD1 LEU C 504      15.228  20.253 -69.680  1.00 15.43           C  
ANISOU 5282  CD1 LEU C 504     2131   1581   2149   -222   -114   -234       C  
ATOM   5283  CD2 LEU C 504      14.798  22.644 -70.274  1.00 13.68           C  
ANISOU 5283  CD2 LEU C 504     1919   1298   1979   -162   -115   -230       C  
ATOM   5284  N   ALA C 505      17.357  22.492 -66.223  1.00 13.93           N  
ANISOU 5284  N   ALA C 505     1973   1340   1981   -269    -29   -302       N  
ATOM   5285  CA  ALA C 505      18.778  22.795 -66.136  1.00 13.62           C  
ANISOU 5285  CA  ALA C 505     1966   1277   1933   -293    -23   -289       C  
ATOM   5286  C   ALA C 505      19.482  21.846 -65.171  1.00 12.82           C  
ANISOU 5286  C   ALA C 505     1862   1201   1809   -338    -18   -295       C  
ATOM   5287  O   ALA C 505      20.550  21.330 -65.478  1.00 10.99           O  
ANISOU 5287  O   ALA C 505     1643    969   1566   -357    -25   -272       O  
ATOM   5288  CB  ALA C 505      18.991  24.250 -65.715  1.00 12.48           C  
ANISOU 5288  CB  ALA C 505     1842   1092   1808   -284     -9   -304       C  
ATOM   5289  N   GLN C 506      18.876  21.600 -64.013  1.00 12.32           N  
ANISOU 5289  N   GLN C 506     1781   1159   1739   -356     -5   -324       N  
ATOM   5290  CA  GLN C 506      19.494  20.716 -63.024  1.00 12.39           C  
ANISOU 5290  CA  GLN C 506     1791   1191   1725   -403     -4   -328       C  
ATOM   5291  C   GLN C 506      19.694  19.311 -63.595  1.00 11.82           C  
ANISOU 5291  C   GLN C 506     1712   1142   1637   -412    -26   -304       C  
ATOM   5292  O   GLN C 506      20.721  18.673 -63.360  1.00 13.43           O  
ANISOU 5292  O   GLN C 506     1925   1347   1829   -440    -34   -289       O  
ATOM   5293  CB  GLN C 506      18.651  20.630 -61.749  1.00 14.37           C  
ANISOU 5293  CB  GLN C 506     2027   1467   1967   -423     13   -363       C  
ATOM   5294  CG  GLN C 506      18.532  21.927 -60.966  1.00 12.67           C  
ANISOU 5294  CG  GLN C 506     1824   1228   1761   -420     39   -394       C  
ATOM   5295  CD  GLN C 506      17.270  21.990 -60.114  1.00 22.90           C  
ANISOU 5295  CD  GLN C 506     3096   2551   3056   -417     63   -432       C  
ATOM   5296  OE1 GLN C 506      16.531  21.009 -59.997  1.00 25.05           O  
ANISOU 5296  OE1 GLN C 506     3340   2863   3316   -427     59   -433       O  
ATOM   5297  NE2 GLN C 506      17.031  23.145 -59.501  1.00 20.73           N  
ANISOU 5297  NE2 GLN C 506     2833   2252   2791   -406     90   -465       N  
ATOM   5298  N   LEU C 507      18.709  18.834 -64.347  1.00 11.54           N  
ANISOU 5298  N   LEU C 507     1659   1122   1603   -388    -38   -299       N  
ATOM   5299  CA  LEU C 507      18.796  17.509 -64.944  1.00 11.31           C  
ANISOU 5299  CA  LEU C 507     1630   1111   1558   -396    -60   -280       C  
ATOM   5300  C   LEU C 507      19.892  17.425 -66.002  1.00 11.15           C  
ANISOU 5300  C   LEU C 507     1632   1069   1537   -384    -67   -252       C  
ATOM   5301  O   LEU C 507      20.652  16.459 -66.048  1.00 11.61           O  
ANISOU 5301  O   LEU C 507     1698   1132   1583   -401    -77   -239       O  
ATOM   5302  CB  LEU C 507      17.452  17.103 -65.562  1.00 12.77           C  
ANISOU 5302  CB  LEU C 507     1793   1315   1742   -376    -73   -280       C  
ATOM   5303  CG  LEU C 507      16.335  16.824 -64.560  1.00 17.11           C  
ANISOU 5303  CG  LEU C 507     2314   1899   2288   -394    -66   -304       C  
ATOM   5304  CD1 LEU C 507      15.076  16.385 -65.276  1.00 17.60           C  
ANISOU 5304  CD1 LEU C 507     2351   1983   2352   -377    -84   -299       C  
ATOM   5305  CD2 LEU C 507      16.768  15.756 -63.568  1.00 22.47           C  
ANISOU 5305  CD2 LEU C 507     2997   2599   2942   -442    -70   -307       C  
ATOM   5306  N   LEU C 508      19.973  18.434 -66.861  1.00 10.78           N  
ANISOU 5306  N   LEU C 508     1595    996   1503   -355    -63   -242       N  
ATOM   5307  CA  LEU C 508      20.949  18.399 -67.941  1.00 10.69           C  
ANISOU 5307  CA  LEU C 508     1605    969   1488   -345    -66   -216       C  
ATOM   5308  C   LEU C 508      22.375  18.603 -67.439  1.00 10.61           C  
ANISOU 5308  C   LEU C 508     1604    947   1480   -368    -54   -209       C  
ATOM   5309  O   LEU C 508      23.323  18.108 -68.044  1.00 11.55           O  
ANISOU 5309  O   LEU C 508     1731   1063   1592   -369    -54   -189       O  
ATOM   5310  CB  LEU C 508      20.609  19.447 -68.999  1.00 11.74           C  
ANISOU 5310  CB  LEU C 508     1750   1078   1632   -313    -67   -205       C  
ATOM   5311  CG  LEU C 508      19.228  19.264 -69.630  1.00 11.04           C  
ANISOU 5311  CG  LEU C 508     1650   1000   1544   -289    -86   -206       C  
ATOM   5312  CD1 LEU C 508      18.951  20.360 -70.644  1.00 11.29           C  
ANISOU 5312  CD1 LEU C 508     1696   1005   1589   -258    -92   -191       C  
ATOM   5313  CD2 LEU C 508      19.121  17.884 -70.269  1.00 16.15           C  
ANISOU 5313  CD2 LEU C 508     2300   1668   2167   -295   -103   -195       C  
ATOM   5314  N   LEU C 509      22.530  19.322 -66.331  1.00 11.39           N  
ANISOU 5314  N   LEU C 509     1701   1038   1588   -387    -43   -225       N  
ATOM   5315  CA  LEU C 509      23.861  19.551 -65.779  1.00 11.36           C  
ANISOU 5315  CA  LEU C 509     1704   1025   1587   -415    -37   -215       C  
ATOM   5316  C   LEU C 509      24.444  18.278 -65.176  1.00 11.37           C  
ANISOU 5316  C   LEU C 509     1695   1047   1577   -442    -47   -211       C  
ATOM   5317  O   LEU C 509      25.661  18.112 -65.124  1.00 14.86           O  
ANISOU 5317  O   LEU C 509     2137   1485   2022   -457    -47   -193       O  
ATOM   5318  CB  LEU C 509      23.831  20.662 -64.731  1.00 14.83           C  
ANISOU 5318  CB  LEU C 509     2151   1449   2034   -432    -25   -235       C  
ATOM   5319  CG  LEU C 509      23.772  22.065 -65.335  1.00 16.84           C  
ANISOU 5319  CG  LEU C 509     2424   1671   2305   -410    -17   -232       C  
ATOM   5320  CD1 LEU C 509      23.905  23.112 -64.253  1.00 19.36           C  
ANISOU 5320  CD1 LEU C 509     2757   1969   2630   -430     -7   -253       C  
ATOM   5321  CD2 LEU C 509      24.859  22.231 -66.382  1.00 16.30           C  
ANISOU 5321  CD2 LEU C 509     2366   1588   2237   -407    -18   -199       C  
ATOM   5322  N   ILE C 510      23.575  17.378 -64.723  1.00 10.54           N  
ANISOU 5322  N   ILE C 510     1580    964   1460   -449    -57   -224       N  
ATOM   5323  CA  ILE C 510      24.031  16.094 -64.195  1.00 10.41           C  
ANISOU 5323  CA  ILE C 510     1558    964   1433   -474    -72   -218       C  
ATOM   5324  C   ILE C 510      24.633  15.254 -65.324  1.00 14.06           C  
ANISOU 5324  C   ILE C 510     2023   1423   1894   -453    -80   -196       C  
ATOM   5325  O   ILE C 510      25.539  14.454 -65.101  1.00 13.47           O  
ANISOU 5325  O   ILE C 510     1947   1350   1822   -466    -89   -183       O  
ATOM   5326  CB  ILE C 510      22.884  15.318 -63.495  1.00 17.69           C  
ANISOU 5326  CB  ILE C 510     2471   1910   2339   -491    -83   -236       C  
ATOM   5327  CG1 ILE C 510      22.431  16.064 -62.237  1.00 21.51           C  
ANISOU 5327  CG1 ILE C 510     2952   2401   2820   -516    -70   -260       C  
ATOM   5328  CG2 ILE C 510      23.319  13.900 -63.117  1.00 22.22           C  
ANISOU 5328  CG2 ILE C 510     3045   2496   2902   -515   -105   -224       C  
ATOM   5329  CD1 ILE C 510      21.093  15.622 -61.701  1.00 27.32           C  
ANISOU 5329  CD1 ILE C 510     3675   3164   3542   -527    -70   -281       C  
ATOM   5330  N   LEU C 511      24.142  15.462 -66.543  1.00 14.25           N  
ANISOU 5330  N   LEU C 511     2056   1442   1917   -420    -76   -192       N  
ATOM   5331  CA  LEU C 511      24.658  14.732 -67.696  1.00 14.88           C  
ANISOU 5331  CA  LEU C 511     2145   1518   1991   -399    -78   -175       C  
ATOM   5332  C   LEU C 511      26.148  15.004 -67.931  1.00 13.60           C  
ANISOU 5332  C   LEU C 511     1982   1345   1841   -400    -64   -157       C  
ATOM   5333  O   LEU C 511      26.867  14.131 -68.410  1.00 13.96           O  
ANISOU 5333  O   LEU C 511     2028   1392   1885   -391    -64   -147       O  
ATOM   5334  CB  LEU C 511      23.851  15.067 -68.954  1.00 19.56           C  
ANISOU 5334  CB  LEU C 511     2750   2106   2575   -369    -77   -173       C  
ATOM   5335  CG  LEU C 511      22.378  14.641 -68.910  1.00 20.64           C  
ANISOU 5335  CG  LEU C 511     2883   2257   2702   -367    -95   -186       C  
ATOM   5336  CD1 LEU C 511      21.712  14.785 -70.273  1.00 20.13           C  
ANISOU 5336  CD1 LEU C 511     2833   2188   2628   -339   -102   -178       C  
ATOM   5337  CD2 LEU C 511      22.236  13.222 -68.393  1.00 20.38           C  
ANISOU 5337  CD2 LEU C 511     2848   2240   2657   -386   -113   -191       C  
ATOM   5338  N   SER C 512      26.628  16.196 -67.584  1.00 12.54           N  
ANISOU 5338  N   SER C 512     1845   1200   1719   -410    -51   -154       N  
ATOM   5339  CA  SER C 512      28.062  16.461 -67.689  1.00 12.93           C  
ANISOU 5339  CA  SER C 512     1887   1244   1781   -418    -39   -134       C  
ATOM   5340  C   SER C 512      28.862  15.596 -66.727  1.00 12.61           C  
ANISOU 5340  C   SER C 512     1829   1213   1749   -442    -52   -129       C  
ATOM   5341  O   SER C 512      29.949  15.127 -67.065  1.00 16.05           O  
ANISOU 5341  O   SER C 512     2252   1650   2195   -437    -47   -112       O  
ATOM   5342  CB  SER C 512      28.375  17.933 -67.431  1.00 24.48           C  
ANISOU 5342  CB  SER C 512     3354   2691   3254   -432    -28   -130       C  
ATOM   5343  OG  SER C 512      28.245  18.688 -68.618  1.00 33.06           O  
ANISOU 5343  OG  SER C 512     4458   3766   4339   -409    -16   -120       O  
ATOM   5344  N   HIS C 513      28.331  15.394 -65.525  1.00 12.51           N  
ANISOU 5344  N   HIS C 513     1815   1206   1732   -469    -68   -144       N  
ATOM   5345  CA  HIS C 513      29.004  14.549 -64.549  1.00 13.22           C  
ANISOU 5345  CA  HIS C 513     1891   1303   1827   -496    -87   -136       C  
ATOM   5346  C   HIS C 513      29.027  13.097 -65.026  1.00 12.32           C  
ANISOU 5346  C   HIS C 513     1777   1194   1711   -477   -100   -132       C  
ATOM   5347  O   HIS C 513      30.003  12.382 -64.818  1.00 12.06           O  
ANISOU 5347  O   HIS C 513     1730   1160   1692   -481   -110   -117       O  
ATOM   5348  CB  HIS C 513      28.329  14.645 -63.180  1.00 14.06           C  
ANISOU 5348  CB  HIS C 513     2002   1417   1922   -533   -101   -154       C  
ATOM   5349  CG  HIS C 513      29.006  13.828 -62.122  0.59 14.78           C  
ANISOU 5349  CG  HIS C 513     2085   1515   2017   -567   -126   -143       C  
ATOM   5350  ND1 HIS C 513      28.426  12.714 -61.554  0.49 17.88           N  
ANISOU 5350  ND1 HIS C 513     2481   1917   2395   -582   -148   -149       N  
ATOM   5351  CD2 HIS C 513      30.226  13.950 -61.546  1.00 23.03           C  
ANISOU 5351  CD2 HIS C 513     3118   2556   3077   -592   -136   -123       C  
ATOM   5352  CE1 HIS C 513      29.252  12.196 -60.662  1.00 22.19           C  
ANISOU 5352  CE1 HIS C 513     3020   2463   2947   -614   -173   -133       C  
ATOM   5353  NE2 HIS C 513      30.352  12.926 -60.640  0.52 19.75           N  
ANISOU 5353  NE2 HIS C 513     2700   2147   2657   -619   -166   -117       N  
ATOM   5354  N   ILE C 514      27.946  12.668 -65.671  1.00 10.82           N  
ANISOU 5354  N   ILE C 514     1601   1007   1504   -457   -101   -145       N  
ATOM   5355  CA  ILE C 514      27.863  11.304 -66.187  1.00 11.48           C  
ANISOU 5355  CA  ILE C 514     1692   1090   1580   -440   -115   -143       C  
ATOM   5356  C   ILE C 514      28.867  11.095 -67.330  1.00 10.54           C  
ANISOU 5356  C   ILE C 514     1572    962   1471   -407    -97   -130       C  
ATOM   5357  O   ILE C 514      29.471  10.030 -67.444  1.00 13.81           O  
ANISOU 5357  O   ILE C 514     1983   1370   1892   -396   -105   -124       O  
ATOM   5358  CB  ILE C 514      26.431  10.979 -66.643  1.00 14.13           C  
ANISOU 5358  CB  ILE C 514     2044   1431   1894   -431   -123   -158       C  
ATOM   5359  CG1 ILE C 514      25.511  10.875 -65.418  1.00 15.42           C  
ANISOU 5359  CG1 ILE C 514     2204   1609   2047   -466   -140   -171       C  
ATOM   5360  CG2 ILE C 514      26.386   9.680 -67.428  1.00 22.39           C  
ANISOU 5360  CG2 ILE C 514     3107   2472   2930   -411   -135   -157       C  
ATOM   5361  CD1 ILE C 514      24.058  10.646 -65.760  1.00 20.45           C  
ANISOU 5361  CD1 ILE C 514     2848   2258   2666   -462   -147   -185       C  
ATOM   5362  N   ARG C 515      29.062  12.122 -68.157  1.00 10.79           N  
ANISOU 5362  N   ARG C 515     1605    991   1503   -391    -71   -125       N  
ATOM   5363  CA  ARG C 515      30.098  12.078 -69.187  1.00 10.97           C  
ANISOU 5363  CA  ARG C 515     1625   1010   1533   -366    -46   -112       C  
ATOM   5364  C   ARG C 515      31.478  11.948 -68.551  1.00 11.32           C  
ANISOU 5364  C   ARG C 515     1639   1057   1606   -377    -45    -96       C  
ATOM   5365  O   ARG C 515      32.305  11.156 -69.000  1.00 11.85           O  
ANISOU 5365  O   ARG C 515     1696   1123   1685   -356    -37    -89       O  
ATOM   5366  CB  ARG C 515      30.034  13.327 -70.080  1.00 12.59           C  
ANISOU 5366  CB  ARG C 515     1839   1213   1731   -357    -21   -107       C  
ATOM   5367  CG  ARG C 515      31.241  13.500 -71.001  1.00 15.75           C  
ANISOU 5367  CG  ARG C 515     2232   1615   2138   -341      9    -90       C  
ATOM   5368  CD  ARG C 515      31.448  12.277 -71.896  1.00 27.50           C  
ANISOU 5368  CD  ARG C 515     3731   3104   3616   -310     18    -96       C  
ATOM   5369  NE  ARG C 515      30.728  12.368 -73.164  1.00 28.88           N  
ANISOU 5369  NE  ARG C 515     3939   3274   3759   -291     29   -102       N  
ATOM   5370  CZ  ARG C 515      30.768  11.442 -74.119  1.00 33.31           C  
ANISOU 5370  CZ  ARG C 515     4522   3834   4302   -265     39   -110       C  
ATOM   5371  NH1 ARG C 515      30.091  11.624 -75.242  1.00 33.06           N  
ANISOU 5371  NH1 ARG C 515     4525   3799   4238   -254     45   -113       N  
ATOM   5372  NH2 ARG C 515      31.471  10.327 -73.956  1.00 32.49           N  
ANISOU 5372  NH2 ARG C 515     4407   3727   4211   -251     41   -115       N  
ATOM   5373  N   HIS C 516      31.715  12.721 -67.499  1.00 11.58           N  
ANISOU 5373  N   HIS C 516     1658   1092   1651   -411    -54    -90       N  
ATOM   5374  CA  HIS C 516      32.988  12.684 -66.790  1.00 12.34           C  
ANISOU 5374  CA  HIS C 516     1723   1192   1775   -429    -60    -70       C  
ATOM   5375  C   HIS C 516      33.274  11.271 -66.286  1.00 13.79           C  
ANISOU 5375  C   HIS C 516     1898   1374   1970   -425    -86    -68       C  
ATOM   5376  O   HIS C 516      34.370  10.745 -66.483  1.00 14.02           O  
ANISOU 5376  O   HIS C 516     1901   1403   2023   -410    -82    -53       O  
ATOM   5377  CB  HIS C 516      32.971  13.687 -65.632  1.00 11.53           C  
ANISOU 5377  CB  HIS C 516     1617   1089   1674   -473    -72    -68       C  
ATOM   5378  CG  HIS C 516      34.282  13.853 -64.931  1.00 22.14           C  
ANISOU 5378  CG  HIS C 516     2931   2437   3045   -499    -81    -45       C  
ATOM   5379  ND1 HIS C 516      35.501  13.676 -65.559  1.00 24.00           N  
ANISOU 5379  ND1 HIS C 516     3136   2678   3304   -481    -65    -23       N  
ATOM   5380  CD2 HIS C 516      34.572  14.228 -63.663  1.00 28.87           C  
ANISOU 5380  CD2 HIS C 516     3777   3290   3903   -544   -104    -38       C  
ATOM   5381  CE1 HIS C 516      36.474  13.911 -64.700  1.00 23.39           C  
ANISOU 5381  CE1 HIS C 516     3031   2605   3250   -514    -82     -2       C  
ATOM   5382  NE2 HIS C 516      35.938  14.252 -63.539  1.00 28.82           N  
ANISOU 5382  NE2 HIS C 516     3737   3289   3925   -554   -108    -10       N  
ATOM   5383  N   MET C 517      32.273  10.646 -65.674  1.00 10.94           N  
ANISOU 5383  N   MET C 517     1555   1010   1591   -439   -112    -82       N  
ATOM   5384  CA  MET C 517      32.437   9.294 -65.145  1.00 11.01           C  
ANISOU 5384  CA  MET C 517     1562   1013   1607   -440   -143    -79       C  
ATOM   5385  C   MET C 517      32.713   8.283 -66.243  1.00 11.23           C  
ANISOU 5385  C   MET C 517     1596   1030   1639   -394   -133    -81       C  
ATOM   5386  O   MET C 517      33.525   7.378 -66.063  1.00 11.75           O  
ANISOU 5386  O   MET C 517     1648   1088   1730   -382   -147    -70       O  
ATOM   5387  CB  MET C 517      31.204   8.863 -64.354  1.00 11.97           C  
ANISOU 5387  CB  MET C 517     1708   1137   1704   -468   -171    -93       C  
ATOM   5388  CG  MET C 517      30.919   9.735 -63.148  1.00 14.55           C  
ANISOU 5388  CG  MET C 517     2032   1473   2023   -515   -179    -96       C  
ATOM   5389  SD  MET C 517      29.657   8.999 -62.112  1.00 16.42           S  
ANISOU 5389  SD  MET C 517     2290   1718   2231   -552   -211   -110       S  
ATOM   5390  CE  MET C 517      28.193   9.273 -63.110  1.00 17.96           C  
ANISOU 5390  CE  MET C 517     2503   1919   2401   -526   -189   -135       C  
ATOM   5391  N   SER C 518      32.029   8.429 -67.374  1.00 13.17           N  
ANISOU 5391  N   SER C 518     1866   1276   1863   -368   -110    -96       N  
ATOM   5392  CA  SER C 518      32.235   7.528 -68.498  1.00 15.73           C  
ANISOU 5392  CA  SER C 518     2204   1589   2184   -326    -96   -103       C  
ATOM   5393  C   SER C 518      33.658   7.652 -69.017  1.00 10.93           C  
ANISOU 5393  C   SER C 518     1566    983   1604   -301    -66    -89       C  
ATOM   5394  O   SER C 518      34.306   6.654 -69.317  1.00 12.77           O  
ANISOU 5394  O   SER C 518     1794   1206   1854   -271    -65    -89       O  
ATOM   5395  CB  SER C 518      31.242   7.814 -69.620  1.00 10.52           C  
ANISOU 5395  CB  SER C 518     1577    930   1490   -311    -78   -118       C  
ATOM   5396  OG  SER C 518      31.619   7.146 -70.815  1.00 12.35           O  
ANISOU 5396  OG  SER C 518     1826   1153   1715   -272    -57   -125       O  
ATOM   5397  N   ASN C 519      34.145   8.885 -69.115  1.00 13.71           N  
ANISOU 5397  N   ASN C 519     1897   1349   1962   -312    -42    -77       N  
ATOM   5398  CA  ASN C 519      35.507   9.116 -69.571  1.00 12.51           C  
ANISOU 5398  CA  ASN C 519     1710   1206   1838   -295    -11    -61       C  
ATOM   5399  C   ASN C 519      36.532   8.406 -68.701  1.00 12.75           C  
ANISOU 5399  C   ASN C 519     1701   1233   1909   -296    -33    -44       C  
ATOM   5400  O   ASN C 519      37.455   7.779 -69.211  1.00 18.74           O  
ANISOU 5400  O   ASN C 519     2438   1992   2692   -261    -15    -40       O  
ATOM   5401  CB  ASN C 519      35.798  10.610 -69.618  1.00 14.92           C  
ANISOU 5401  CB  ASN C 519     2002   1525   2143   -319     10    -47       C  
ATOM   5402  CG  ASN C 519      35.326  11.239 -70.903  1.00 22.46           C  
ANISOU 5402  CG  ASN C 519     2984   2482   3067   -303     44    -55       C  
ATOM   5403  OD1 ASN C 519      35.349  10.600 -71.956  1.00 34.86           O  
ANISOU 5403  OD1 ASN C 519     4571   4050   4624   -269     66    -66       O  
ATOM   5404  ND2 ASN C 519      34.868  12.483 -70.826  1.00 15.07           N  
ANISOU 5404  ND2 ASN C 519     2060   1547   2119   -328     46    -52       N  
ATOM   5405  N   LYS C 520      36.352   8.487 -67.389  1.00 13.72           N  
ANISOU 5405  N   LYS C 520     1818   1355   2039   -336    -73    -36       N  
ATOM   5406  CA  LYS C 520      37.249   7.818 -66.458  1.00 15.84           C  
ANISOU 5406  CA  LYS C 520     2053   1619   2344   -344   -105    -16       C  
ATOM   5407  C   LYS C 520      37.123   6.301 -66.575  1.00 17.39           C  
ANISOU 5407  C   LYS C 520     2265   1795   2548   -311   -125    -25       C  
ATOM   5408  O   LYS C 520      38.114   5.576 -66.473  1.00 19.04           O  
ANISOU 5408  O   LYS C 520     2442   1996   2795   -288   -133    -12       O  
ATOM   5409  CB  LYS C 520      36.958   8.266 -65.026  1.00 14.83           C  
ANISOU 5409  CB  LYS C 520     1927   1495   2214   -400   -145     -6       C  
ATOM   5410  CG  LYS C 520      37.122   9.764 -64.804  1.00 18.86           C  
ANISOU 5410  CG  LYS C 520     2427   2020   2718   -435   -129      2       C  
ATOM   5411  CD  LYS C 520      38.430  10.274 -65.387  1.00 27.66           C  
ANISOU 5411  CD  LYS C 520     3499   3147   3864   -421    -99     24       C  
ATOM   5412  CE  LYS C 520      39.611   9.927 -64.491  1.00 29.06           C  
ANISOU 5412  CE  LYS C 520     3631   3329   4083   -438   -130     54       C  
ATOM   5413  NZ  LYS C 520      40.913  10.273 -65.143  1.00 30.05           N  
ANISOU 5413  NZ  LYS C 520     3704   3471   4242   -420    -98     76       N  
ATOM   5414  N   GLY C 521      35.900   5.824 -66.783  1.00 16.35           N  
ANISOU 5414  N   GLY C 521     2179   1651   2380   -310   -136    -47       N  
ATOM   5415  CA  GLY C 521      35.672   4.405 -66.975  1.00 14.67           C  
ANISOU 5415  CA  GLY C 521     1991   1415   2169   -283   -157    -58       C  
ATOM   5416  C   GLY C 521      36.299   3.914 -68.267  1.00 17.37           C  
ANISOU 5416  C   GLY C 521     2330   1748   2521   -225   -117    -69       C  
ATOM   5417  O   GLY C 521      36.893   2.836 -68.306  1.00 16.76           O  
ANISOU 5417  O   GLY C 521     2247   1650   2471   -192   -128    -68       O  
ATOM   5418  N   MET C 522      36.168   4.708 -69.327  1.00 15.95           N  
ANISOU 5418  N   MET C 522     2159   1583   2319   -212    -70    -79       N  
ATOM   5419  CA  MET C 522      36.737   4.353 -70.624  1.00 19.22           C  
ANISOU 5419  CA  MET C 522     2575   1994   2735   -161    -25    -92       C  
ATOM   5420  C   MET C 522      38.255   4.321 -70.549  1.00 20.47           C  
ANISOU 5420  C   MET C 522     2674   2161   2943   -137     -5    -74       C  
ATOM   5421  O   MET C 522      38.889   3.460 -71.157  1.00 18.20           O  
ANISOU 5421  O   MET C 522     2381   1861   2675    -89     16    -84       O  
ATOM   5422  CB  MET C 522      36.288   5.332 -71.716  1.00 21.11           C  
ANISOU 5422  CB  MET C 522     2835   2249   2935   -161     18   -102       C  
ATOM   5423  CG  MET C 522      34.839   5.177 -72.178  1.00 21.65           C  
ANISOU 5423  CG  MET C 522     2962   2309   2956   -169      5   -123       C  
ATOM   5424  SD  MET C 522      34.374   3.557 -72.834  1.00 20.02           S  
ANISOU 5424  SD  MET C 522     2807   2070   2730   -133     -7   -149       S  
ATOM   5425  CE  MET C 522      35.620   3.329 -74.090  1.00 25.91           C  
ANISOU 5425  CE  MET C 522     3540   2816   3487    -79     55   -159       C  
ATOM   5426  N   GLU C 523      38.835   5.260 -69.804  1.00 17.98           N  
ANISOU 5426  N   GLU C 523     2316   1867   2651   -171    -10    -48       N  
ATOM   5427  CA  GLU C 523      40.282   5.282 -69.603  1.00 19.88           C  
ANISOU 5427  CA  GLU C 523     2491   2119   2942   -157      2    -24       C  
ATOM   5428  C   GLU C 523      40.777   3.962 -69.026  1.00 20.41           C  
ANISOU 5428  C   GLU C 523     2543   2163   3051   -130    -34    -20       C  
ATOM   5429  O   GLU C 523      41.811   3.441 -69.452  1.00 21.68           O  
ANISOU 5429  O   GLU C 523     2665   2322   3250    -85    -11    -17       O  
ATOM   5430  CB  GLU C 523      40.705   6.436 -68.684  1.00 22.19           C  
ANISOU 5430  CB  GLU C 523     2747   2435   3250   -209    -14      5       C  
ATOM   5431  CG  GLU C 523      40.482   7.828 -69.260  1.00 26.88           C  
ANISOU 5431  CG  GLU C 523     3348   3050   3814   -233     23      6       C  
ATOM   5432  CD  GLU C 523      40.505   8.910 -68.192  1.00 29.21           C  
ANISOU 5432  CD  GLU C 523     3630   3356   4112   -292     -5     27       C  
ATOM   5433  OE1 GLU C 523      41.112   8.673 -67.128  1.00 30.09           O  
ANISOU 5433  OE1 GLU C 523     3709   3468   4257   -313    -42     49       O  
ATOM   5434  OE2 GLU C 523      39.909   9.988 -68.411  1.00 37.84           O  
ANISOU 5434  OE2 GLU C 523     4749   4456   5175   -317      9     23       O  
ATOM   5435  N   HIS C 524      40.041   3.417 -68.064  1.00 16.91           N  
ANISOU 5435  N   HIS C 524     2129   1698   2598   -157    -91    -18       N  
ATOM   5436  CA  HIS C 524      40.449   2.152 -67.473  1.00 16.42           C  
ANISOU 5436  CA  HIS C 524     2059   1608   2574   -136   -134    -11       C  
ATOM   5437  C   HIS C 524      40.302   0.995 -68.445  1.00 18.14           C  
ANISOU 5437  C   HIS C 524     2310   1795   2787    -77   -116    -40       C  
ATOM   5438  O   HIS C 524      41.205   0.166 -68.549  1.00 19.93           O  
ANISOU 5438  O   HIS C 524     2508   2004   3059    -31   -115    -36       O  
ATOM   5439  CB  HIS C 524      39.664   1.830 -66.211  1.00 18.54           C  
ANISOU 5439  CB  HIS C 524     2355   1861   2828   -186   -200     -1       C  
ATOM   5440  CG  HIS C 524      40.139   0.583 -65.541  1.00 23.29           C  
ANISOU 5440  CG  HIS C 524     2950   2432   3469   -170   -250     13       C  
ATOM   5441  ND1 HIS C 524      39.399  -0.581 -65.527  1.00 24.56           N  
ANISOU 5441  ND1 HIS C 524     3162   2556   3613   -160   -282     -2       N  
ATOM   5442  CD2 HIS C 524      41.301   0.299 -64.910  1.00 22.46           C  
ANISOU 5442  CD2 HIS C 524     2790   2322   3420   -161   -276     44       C  
ATOM   5443  CE1 HIS C 524      40.076  -1.519 -64.892  1.00 23.41           C  
ANISOU 5443  CE1 HIS C 524     2999   2383   3512   -145   -327     18       C  
ATOM   5444  NE2 HIS C 524      41.233  -1.014 -64.507  1.00 26.19           N  
ANISOU 5444  NE2 HIS C 524     3285   2754   3911   -144   -325     46       N  
ATOM   5445  N   LEU C 525      39.171   0.932 -69.145  1.00 16.77           N  
ANISOU 5445  N   LEU C 525     2197   1615   2561    -78   -102    -68       N  
ATOM   5446  CA  LEU C 525      38.937  -0.153 -70.095  1.00 15.05           C  
ANISOU 5446  CA  LEU C 525     2022   1365   2330    -28    -87    -98       C  
ATOM   5447  C   LEU C 525      40.039  -0.228 -71.145  1.00 17.10           C  
ANISOU 5447  C   LEU C 525     2250   1632   2616     31    -25   -109       C  
ATOM   5448  O   LEU C 525      40.527  -1.312 -71.460  1.00 17.65           O  
ANISOU 5448  O   LEU C 525     2323   1671   2711     83    -22   -122       O  
ATOM   5449  CB  LEU C 525      37.572  -0.006 -70.771  1.00 15.37           C  
ANISOU 5449  CB  LEU C 525     2129   1405   2307    -45    -79   -124       C  
ATOM   5450  CG  LEU C 525      36.357  -0.167 -69.855  1.00 15.96           C  
ANISOU 5450  CG  LEU C 525     2240   1471   2354    -98   -137   -119       C  
ATOM   5451  CD1 LEU C 525      35.064   0.065 -70.615  1.00 16.42           C  
ANISOU 5451  CD1 LEU C 525     2352   1533   2353   -112   -126   -142       C  
ATOM   5452  CD2 LEU C 525      36.366  -1.553 -69.240  1.00 16.13           C  
ANISOU 5452  CD2 LEU C 525     2281   1452   2395    -89   -189   -118       C  
ATOM   5453  N   TYR C 526      40.440   0.923 -71.674  1.00 16.80           N  
ANISOU 5453  N   TYR C 526     2181   1633   2570     24     25   -103       N  
ATOM   5454  CA  TYR C 526      41.535   0.964 -72.636  1.00 19.58           C  
ANISOU 5454  CA  TYR C 526     2496   2000   2945     73     89   -110       C  
ATOM   5455  C   TYR C 526      42.860   0.538 -72.005  1.00 21.10           C  
ANISOU 5455  C   TYR C 526     2615   2192   3211    101     79    -87       C  
ATOM   5456  O   TYR C 526      43.685  -0.101 -72.658  1.00 22.90           O  
ANISOU 5456  O   TYR C 526     2820   2413   3469    161    117   -101       O  
ATOM   5457  CB  TYR C 526      41.670   2.359 -73.248  1.00 19.62           C  
ANISOU 5457  CB  TYR C 526     2483   2047   2924     49    139   -102       C  
ATOM   5458  CG  TYR C 526      40.667   2.640 -74.343  1.00 20.80           C  
ANISOU 5458  CG  TYR C 526     2699   2197   3007     45    168   -129       C  
ATOM   5459  CD1 TYR C 526      40.646   1.865 -75.495  1.00 23.20           C  
ANISOU 5459  CD1 TYR C 526     3041   2484   3288     92    207   -163       C  
ATOM   5460  CD2 TYR C 526      39.760   3.686 -74.239  1.00 23.08           C  
ANISOU 5460  CD2 TYR C 526     3013   2501   3256     -6    156   -122       C  
ATOM   5461  CE1 TYR C 526      39.742   2.114 -76.507  1.00 24.63           C  
ANISOU 5461  CE1 TYR C 526     3286   2666   3406     84    229   -185       C  
ATOM   5462  CE2 TYR C 526      38.850   3.945 -75.252  1.00 21.11           C  
ANISOU 5462  CE2 TYR C 526     2821   2251   2948     -9    177   -142       C  
ATOM   5463  CZ  TYR C 526      38.847   3.151 -76.383  1.00 24.98           C  
ANISOU 5463  CZ  TYR C 526     3350   2727   3415     34    212   -172       C  
ATOM   5464  OH  TYR C 526      37.953   3.390 -77.402  1.00 29.57           O  
ANISOU 5464  OH  TYR C 526     3992   3307   3936     26    229   -190       O  
ATOM   5465  N   SER C 527      43.057   0.878 -70.735  1.00 20.04           N  
ANISOU 5465  N   SER C 527     2445   2064   3106     58     27    -52       N  
ATOM   5466  CA  SER C 527      44.299   0.535 -70.044  1.00 24.14           C  
ANISOU 5466  CA  SER C 527     2891   2585   3697     77      7    -23       C  
ATOM   5467  C   SER C 527      44.468  -0.976 -69.887  1.00 25.03           C  
ANISOU 5467  C   SER C 527     3017   2650   3844    129    -25    -34       C  
ATOM   5468  O   SER C 527      45.579  -1.472 -69.695  1.00 20.64           O  
ANISOU 5468  O   SER C 527     2400   2088   3352    170    -27    -19       O  
ATOM   5469  CB  SER C 527      44.350   1.205 -68.668  1.00 24.03           C  
ANISOU 5469  CB  SER C 527     2848   2585   3697     12    -50     17       C  
ATOM   5470  OG  SER C 527      43.569   0.500 -67.715  1.00 27.73           O  
ANISOU 5470  OG  SER C 527     3360   3020   4155    -15   -120     20       O  
ATOM   5471  N   MET C 528      43.357  -1.700 -69.967  1.00 20.61           N  
ANISOU 5471  N   MET C 528     2535   2054   3244    127    -52    -59       N  
ATOM   5472  CA  MET C 528      43.361  -3.141 -69.751  1.00 20.26           C  
ANISOU 5472  CA  MET C 528     2517   1956   3226    167    -92    -69       C  
ATOM   5473  C   MET C 528      44.056  -3.884 -70.881  1.00 22.79           C  
ANISOU 5473  C   MET C 528     2831   2258   3569    250    -35   -100       C  
ATOM   5474  O   MET C 528      44.620  -4.956 -70.667  1.00 25.06           O  
ANISOU 5474  O   MET C 528     3107   2506   3907    299    -59   -100       O  
ATOM   5475  CB  MET C 528      41.934  -3.659 -69.591  1.00 18.69           C  
ANISOU 5475  CB  MET C 528     2405   1725   2970    134   -134    -86       C  
ATOM   5476  CG  MET C 528      41.226  -3.115 -68.375  1.00 21.83           C  
ANISOU 5476  CG  MET C 528     2810   2136   3347     56   -191    -59       C  
ATOM   5477  SD  MET C 528      39.545  -3.731 -68.251  1.00 21.04           S  
ANISOU 5477  SD  MET C 528     2804   2006   3182     18   -234    -79       S  
ATOM   5478  CE  MET C 528      39.820  -5.482 -67.978  1.00 21.95           C  
ANISOU 5478  CE  MET C 528     2948   2055   3336     61   -286    -82       C  
ATOM   5479  N   LYS C 529      44.010  -3.305 -72.078  1.00 24.29           N  
ANISOU 5479  N   LYS C 529     3024   3184   3023   1301    259    368       N  
ATOM   5480  CA  LYS C 529      44.586  -3.915 -73.274  1.00 25.99           C  
ANISOU 5480  CA  LYS C 529     3225   3365   3285   1467    370    204       C  
ATOM   5481  C   LYS C 529      44.007  -5.313 -73.498  1.00 26.97           C  
ANISOU 5481  C   LYS C 529     3483   3314   3449   1519    255    125       C  
ATOM   5482  O   LYS C 529      44.721  -6.263 -73.828  1.00 28.78           O  
ANISOU 5482  O   LYS C 529     3677   3434   3824   1660    249     32       O  
ATOM   5483  CB  LYS C 529      46.114  -3.952 -73.177  1.00 28.05           C  
ANISOU 5483  CB  LYS C 529     3293   3620   3744   1592    424    181       C  
ATOM   5484  CG  LYS C 529      46.735  -2.560 -73.211  1.00 30.70           C  
ANISOU 5484  CG  LYS C 529     3494   4134   4037   1555    576    227       C  
ATOM   5485  CD  LYS C 529      48.105  -2.530 -72.554  1.00 32.86           C  
ANISOU 5485  CD  LYS C 529     3558   4383   4543   1627    548    262       C  
ATOM   5486  CE  LYS C 529      49.041  -1.582 -73.290  1.00 35.15           C  
ANISOU 5486  CE  LYS C 529     3701   4809   4845   1682    787    196       C  
ATOM   5487  NZ  LYS C 529      48.720  -1.489 -74.745  1.00 37.63           N  
ANISOU 5487  NZ  LYS C 529     4122   5175   5000   1731    998     51       N  
ATOM   5488  N   SER C 530      42.696  -5.408 -73.284  1.00 25.84           N  
ANISOU 5488  N   SER C 530     3487   3143   3190   1398    166    162       N  
ATOM   5489  CA ASER C 530      41.929  -6.622 -73.545  0.62 27.39           C  
ANISOU 5489  CA ASER C 530     3827   3183   3397   1420     64     86       C  
ATOM   5490  CA BSER C 530      41.944  -6.626 -73.550  0.38 26.52           C  
ANISOU 5490  CA BSER C 530     3715   3072   3288   1422     65     85       C  
ATOM   5491  C   SER C 530      41.143  -6.431 -74.833  1.00 27.25           C  
ANISOU 5491  C   SER C 530     3924   3218   3211   1428    162    -34       C  
ATOM   5492  O   SER C 530      40.320  -5.520 -74.925  1.00 24.86           O  
ANISOU 5492  O   SER C 530     3664   3018   2763   1313    191      7       O  
ATOM   5493  CB ASER C 530      40.988  -6.933 -72.378  0.62 27.84           C  
ANISOU 5493  CB ASER C 530     3972   3144   3463   1272   -107    201       C  
ATOM   5494  CB BSER C 530      41.022  -6.966 -72.377  0.38 26.12           C  
ANISOU 5494  CB BSER C 530     3752   2922   3250   1277   -108    199       C  
ATOM   5495  OG ASER C 530      40.250  -8.129 -72.594  0.62 26.30           O  
ANISOU 5495  OG ASER C 530     3912   2790   3292   1289   -203    125       O  
ATOM   5496  OG BSER C 530      41.762  -7.298 -71.211  0.38 28.05           O  
ANISOU 5496  OG BSER C 530     3931   3084   3643   1278   -224    303       O  
ATOM   5497  N   LYS C 531      41.399  -7.292 -75.817  1.00 28.44           N  
ANISOU 5497  N   LYS C 531     4131   3290   3386   1562    205   -182       N  
ATOM   5498  CA  LYS C 531      40.878  -7.130 -77.178  1.00 33.43           C  
ANISOU 5498  CA  LYS C 531     4886   3964   3852   1593    307   -311       C  
ATOM   5499  C   LYS C 531      39.423  -6.683 -77.305  1.00 34.02           C  
ANISOU 5499  C   LYS C 531     5086   4069   3770   1457    240   -290       C  
ATOM   5500  O   LYS C 531      39.120  -5.816 -78.124  1.00 36.21           O  
ANISOU 5500  O   LYS C 531     5415   4457   3885   1436    336   -327       O  
ATOM   5501  CB  LYS C 531      41.056  -8.430 -77.968  1.00 32.85           C  
ANISOU 5501  CB  LYS C 531     4900   3744   3839   1727    302   -463       C  
ATOM   5502  CG  LYS C 531      40.623  -8.298 -79.425  1.00 34.79           C  
ANISOU 5502  CG  LYS C 531     5297   4019   3903   1766    408   -605       C  
ATOM   5503  CD  LYS C 531      41.819  -8.201 -80.359  1.00 36.65           C  
ANISOU 5503  CD  LYS C 531     5494   4289   4143   1904    617   -718       C  
ATOM   5504  N   ASN C 532      38.525  -7.248 -76.503  1.00 33.01           N  
ANISOU 5504  N   ASN C 532     5008   3836   3698   1362     78   -233       N  
ATOM   5505  CA  ASN C 532      37.102  -6.950 -76.676  1.00 35.51           C  
ANISOU 5505  CA  ASN C 532     5432   4155   3905   1239     11   -236       C  
ATOM   5506  C   ASN C 532      36.386  -6.376 -75.443  1.00 34.03           C  
ANISOU 5506  C   ASN C 532     5203   3987   3742   1064    -64    -89       C  
ATOM   5507  O   ASN C 532      35.184  -6.584 -75.265  1.00 34.95           O  
ANISOU 5507  O   ASN C 532     5396   4031   3853    960   -157    -93       O  
ATOM   5508  CB  ASN C 532      36.373  -8.214 -77.144  1.00 33.88           C  
ANISOU 5508  CB  ASN C 532     5361   3782   3730   1274    -95   -350       C  
ATOM   5509  CG  ASN C 532      36.684  -8.564 -78.589  1.00 36.85           C  
ANISOU 5509  CG  ASN C 532     5830   4149   4020   1412    -14   -512       C  
ATOM   5510  OD1 ASN C 532      36.482  -7.750 -79.493  1.00 42.11           O  
ANISOU 5510  OD1 ASN C 532     6552   4918   4529   1411     66   -560       O  
ATOM   5511  ND2 ASN C 532      37.174  -9.780 -78.814  1.00 40.36           N  
ANISOU 5511  ND2 ASN C 532     6309   4462   4565   1528    -35   -598       N  
ATOM   5512  N   VAL C 533      37.113  -5.635 -74.610  1.00 26.06           N  
ANISOU 5512  N   VAL C 533     4072   3068   2763   1027    -18     33       N  
ATOM   5513  CA  VAL C 533      36.516  -5.022 -73.426  1.00 23.65           C  
ANISOU 5513  CA  VAL C 533     3737   2781   2467    856    -68    174       C  
ATOM   5514  C   VAL C 533      36.018  -3.611 -73.764  1.00 24.78           C  
ANISOU 5514  C   VAL C 533     3856   3087   2474    770     20    204       C  
ATOM   5515  O   VAL C 533      35.292  -2.985 -72.990  1.00 22.54           O  
ANISOU 5515  O   VAL C 533     3559   2824   2180    618     -3    298       O  
ATOM   5516  CB  VAL C 533      37.515  -4.981 -72.254  1.00 24.64           C  
ANISOU 5516  CB  VAL C 533     3764   2902   2695    848    -88    298       C  
ATOM   5517  CG1 VAL C 533      38.541  -3.874 -72.459  1.00 25.84           C  
ANISOU 5517  CG1 VAL C 533     3786   3227   2803    895     43    335       C  
ATOM   5518  CG2 VAL C 533      36.783  -4.832 -70.923  1.00 25.46           C  
ANISOU 5518  CG2 VAL C 533     3901   2947   2827    667   -172    428       C  
ATOM   5519  N   VAL C 534      36.422  -3.111 -74.925  1.00 22.26           N  
ANISOU 5519  N   VAL C 534     3537   2873   2049    866    129    121       N  
ATOM   5520  CA  VAL C 534      35.783  -1.941 -75.516  1.00 22.72           C  
ANISOU 5520  CA  VAL C 534     3617   3055   1962    802    190    118       C  
ATOM   5521  C   VAL C 534      35.181  -2.393 -76.838  1.00 23.28           C  
ANISOU 5521  C   VAL C 534     3826   3074   1946    873    165    -32       C  
ATOM   5522  O   VAL C 534      35.902  -2.890 -77.703  1.00 25.99           O  
ANISOU 5522  O   VAL C 534     4212   3402   2263   1011    227   -133       O  
ATOM   5523  CB  VAL C 534      36.767  -0.775 -75.757  1.00 25.15           C  
ANISOU 5523  CB  VAL C 534     3832   3536   2189    836    346    160       C  
ATOM   5524  CG1 VAL C 534      36.070   0.360 -76.511  1.00 24.64           C  
ANISOU 5524  CG1 VAL C 534     3820   3581   1961    781    399    144       C  
ATOM   5525  CG2 VAL C 534      37.365  -0.283 -74.442  1.00 21.22           C  
ANISOU 5525  CG2 VAL C 534     3200   3087   1774    761    356    310       C  
ATOM   5526  N   PRO C 535      33.856  -2.242 -77.001  1.00 20.65           N  
ANISOU 5526  N   PRO C 535     3565   2702   1578    777     74    -54       N  
ATOM   5527  CA  PRO C 535      33.236  -2.753 -78.228  1.00 22.50           C  
ANISOU 5527  CA  PRO C 535     3944   2866   1737    842     16   -199       C  
ATOM   5528  C   PRO C 535      33.712  -1.998 -79.460  1.00 24.01           C  
ANISOU 5528  C   PRO C 535     4202   3169   1750    927    130   -264       C  
ATOM   5529  O   PRO C 535      33.686  -0.767 -79.489  1.00 23.46           O  
ANISOU 5529  O   PRO C 535     4096   3230   1589    871    197   -201       O  
ATOM   5530  CB  PRO C 535      31.741  -2.535 -77.984  1.00 23.68           C  
ANISOU 5530  CB  PRO C 535     4120   2961   1915    705   -108   -190       C  
ATOM   5531  CG  PRO C 535      31.689  -1.370 -77.059  1.00 23.59           C  
ANISOU 5531  CG  PRO C 535     3991   3062   1912    581    -52    -50       C  
ATOM   5532  CD  PRO C 535      32.890  -1.524 -76.156  1.00 20.82           C  
ANISOU 5532  CD  PRO C 535     3540   2743   1628    609     26     44       C  
ATOM   5533  N   SER C 536      34.157  -2.743 -80.464  1.00 23.95           N  
ANISOU 5533  N   SER C 536     4305   3104   1692   1058    159   -392       N  
ATOM   5534  CA  SER C 536      34.667  -2.147 -81.688  1.00 27.46           C  
ANISOU 5534  CA  SER C 536     4829   3625   1979   1125    280   -459       C  
ATOM   5535  C   SER C 536      33.542  -1.521 -82.501  1.00 28.73           C  
ANISOU 5535  C   SER C 536     5045   3778   2092   1016    180   -468       C  
ATOM   5536  O   SER C 536      32.371  -1.852 -82.314  1.00 24.31           O  
ANISOU 5536  O   SER C 536     4554   3139   1545    972     24   -496       O  
ATOM   5537  CB  SER C 536      35.394  -3.197 -82.529  1.00 30.86           C  
ANISOU 5537  CB  SER C 536     5350   3969   2408   1264    337   -588       C  
ATOM   5538  OG  SER C 536      34.471  -4.112 -83.100  1.00 30.88           O  
ANISOU 5538  OG  SER C 536     5508   3833   2393   1281    194   -696       O  
ATOM   5539  N   TYR C 537      33.909  -0.608 -83.395  1.00 28.92           N  
ANISOU 5539  N   TYR C 537     5037   3873   2078    970    263   -452       N  
ATOM   5540  CA  TYR C 537      32.978  -0.081 -84.384  1.00 27.43           C  
ANISOU 5540  CA  TYR C 537     4923   3664   1835    900    177   -479       C  
ATOM   5541  C   TYR C 537      32.309  -1.233 -85.127  1.00 27.67           C  
ANISOU 5541  C   TYR C 537     5134   3558   1823    970     55   -600       C  
ATOM   5542  O   TYR C 537      31.096  -1.236 -85.334  1.00 26.75           O  
ANISOU 5542  O   TYR C 537     5076   3378   1710    921   -100   -622       O  
ATOM   5543  CB  TYR C 537      33.707   0.844 -85.369  1.00 29.19           C  
ANISOU 5543  CB  TYR C 537     5125   3959   2007    866    297   -472       C  
ATOM   5544  CG  TYR C 537      32.815   1.463 -86.426  1.00 32.37           C  
ANISOU 5544  CG  TYR C 537     5614   4343   2344    805    211   -494       C  
ATOM   5545  CD1 TYR C 537      32.428   0.739 -87.547  1.00 33.78           C  
ANISOU 5545  CD1 TYR C 537     5976   4423   2437    865    144   -593       C  
ATOM   5546  CD2 TYR C 537      32.369   2.774 -86.310  1.00 31.06           C  
ANISOU 5546  CD2 TYR C 537     5347   4250   2205    689    193   -418       C  
ATOM   5547  CE1 TYR C 537      31.613   1.289 -88.513  1.00 34.63           C  
ANISOU 5547  CE1 TYR C 537     6175   4503   2481    822     54   -609       C  
ATOM   5548  CE2 TYR C 537      31.550   3.340 -87.280  1.00 31.11           C  
ANISOU 5548  CE2 TYR C 537     5437   4233   2153    652    109   -439       C  
ATOM   5549  CZ  TYR C 537      31.175   2.588 -88.377  1.00 31.63           C  
ANISOU 5549  CZ  TYR C 537     5695   4197   2127    722     37   -532       C  
ATOM   5550  OH  TYR C 537      30.363   3.129 -89.352  1.00 36.51           O  
ANISOU 5550  OH  TYR C 537     6411   4778   2682    695    -59   -549       O  
ATOM   5551  N   ASP C 538      33.110  -2.216 -85.518  1.00 31.25           N  
ANISOU 5551  N   ASP C 538     5661   3956   2256   1081    124   -682       N  
ATOM   5552  CA  ASP C 538      32.615  -3.320 -86.326  1.00 30.50           C  
ANISOU 5552  CA  ASP C 538     5730   3728   2131   1139     23   -801       C  
ATOM   5553  C   ASP C 538      31.628  -4.201 -85.564  1.00 28.86           C  
ANISOU 5553  C   ASP C 538     5551   3408   2006   1138   -154   -836       C  
ATOM   5554  O   ASP C 538      30.661  -4.702 -86.143  1.00 30.49           O  
ANISOU 5554  O   ASP C 538     5859   3512   2214   1121   -304   -903       O  
ATOM   5555  CB  ASP C 538      33.786  -4.156 -86.845  1.00 33.27           C  
ANISOU 5555  CB  ASP C 538     6128   4045   2468   1250    160   -882       C  
ATOM   5556  CG  ASP C 538      34.594  -3.421 -87.898  1.00 40.66           C  
ANISOU 5556  CG  ASP C 538     7076   5054   3320   1232    314   -882       C  
ATOM   5557  OD1 ASP C 538      34.082  -2.412 -88.434  1.00 41.45           O  
ANISOU 5557  OD1 ASP C 538     7190   5202   3356   1143    280   -838       O  
ATOM   5558  OD2 ASP C 538      35.720  -3.865 -88.215  1.00 42.50           O  
ANISOU 5558  OD2 ASP C 538     7303   5282   3562   1302    466   -936       O  
ATOM   5559  N   LEU C 539      31.870  -4.387 -84.269  1.00 27.08           N  
ANISOU 5559  N   LEU C 539     5236   3193   1860   1148   -141   -793       N  
ATOM   5560  CA  LEU C 539      30.946  -5.143 -83.431  1.00 27.12           C  
ANISOU 5560  CA  LEU C 539     5263   3077   1963   1118   -306   -824       C  
ATOM   5561  C   LEU C 539      29.630  -4.394 -83.273  1.00 25.60           C  
ANISOU 5561  C   LEU C 539     5040   2891   1794    982   -441   -780       C  
ATOM   5562  O   LEU C 539      28.560  -4.978 -83.424  1.00 26.09           O  
ANISOU 5562  O   LEU C 539     5154   2829   1929    940   -605   -845       O  
ATOM   5563  CB  LEU C 539      31.551  -5.433 -82.056  1.00 28.01           C  
ANISOU 5563  CB  LEU C 539     5200   3201   2244   1092   -252   -715       C  
ATOM   5564  CG  LEU C 539      30.571  -6.107 -81.090  1.00 26.42           C  
ANISOU 5564  CG  LEU C 539     4941   2874   2221    986   -400   -681       C  
ATOM   5565  CD1 LEU C 539      30.170  -7.492 -81.579  1.00 26.72           C  
ANISOU 5565  CD1 LEU C 539     5099   2739   2315   1045   -510   -811       C  
ATOM   5566  CD2 LEU C 539      31.151  -6.186 -79.698  1.00 25.16           C  
ANISOU 5566  CD2 LEU C 539     4627   2732   2201    938   -347   -549       C  
ATOM   5567  N   LEU C 540      29.710  -3.104 -82.962  1.00 24.26           N  
ANISOU 5567  N   LEU C 540     4764   2860   1593    907   -366   -668       N  
ATOM   5568  CA  LEU C 540      28.515  -2.273 -82.870  1.00 23.37           C  
ANISOU 5568  CA  LEU C 540     4602   2757   1522    782   -473   -626       C  
ATOM   5569  C   LEU C 540      27.745  -2.254 -84.192  1.00 24.67           C  
ANISOU 5569  C   LEU C 540     4859   2859   1657    783   -578   -697       C  
ATOM   5570  O   LEU C 540      26.514  -2.309 -84.211  1.00 24.73           O  
ANISOU 5570  O   LEU C 540     4871   2780   1745    717   -739   -728       O  
ATOM   5571  CB  LEU C 540      28.890  -0.849 -82.458  1.00 21.89           C  
ANISOU 5571  CB  LEU C 540     4272   2729   1317    708   -348   -493       C  
ATOM   5572  CG  LEU C 540      29.509  -0.718 -81.067  1.00 20.53           C  
ANISOU 5572  CG  LEU C 540     3993   2626   1183    681   -258   -392       C  
ATOM   5573  CD1 LEU C 540      29.946   0.712 -80.789  1.00 19.22           C  
ANISOU 5573  CD1 LEU C 540     3660   2613   1030    596   -128   -265       C  
ATOM   5574  CD2 LEU C 540      28.502  -1.174 -80.036  1.00 19.88           C  
ANISOU 5574  CD2 LEU C 540     3851   2438   1265    570   -378   -367       C  
ATOM   5575  N   LEU C 541      28.486  -2.184 -85.293  1.00 25.86           N  
ANISOU 5575  N   LEU C 541     5083   3043   1699    853   -485   -722       N  
ATOM   5576  CA  LEU C 541      27.902  -2.180 -86.626  1.00 27.45           C  
ANISOU 5576  CA  LEU C 541     5404   3184   1842    862   -573   -783       C  
ATOM   5577  C   LEU C 541      27.140  -3.480 -86.886  1.00 28.61           C  
ANISOU 5577  C   LEU C 541     5653   3173   2046    894   -737   -888       C  
ATOM   5578  O   LEU C 541      26.008  -3.465 -87.372  1.00 29.21           O  
ANISOU 5578  O   LEU C 541     5766   3170   2161    853   -898   -920       O  
ATOM   5579  CB  LEU C 541      28.992  -1.986 -87.680  1.00 29.00           C  
ANISOU 5579  CB  LEU C 541     5674   3435   1909    923   -421   -796       C  
ATOM   5580  CG  LEU C 541      28.520  -1.877 -89.129  1.00 32.54           C  
ANISOU 5580  CG  LEU C 541     6272   3825   2265    928   -494   -849       C  
ATOM   5581  CD1 LEU C 541      27.690  -0.636 -89.255  1.00 30.12           C  
ANISOU 5581  CD1 LEU C 541     5915   3559   1971    842   -565   -786       C  
ATOM   5582  CD2 LEU C 541      29.690  -1.832 -90.095  1.00 35.00           C  
ANISOU 5582  CD2 LEU C 541     6667   4176   2456    980   -326   -875       C  
ATOM   5583  N   GLU C 542      27.770  -4.601 -86.541  1.00 29.09           N  
ANISOU 5583  N   GLU C 542     5742   3180   2130    966   -697   -941       N  
ATOM   5584  CA  GLU C 542      27.166  -5.920 -86.709  1.00 31.69           C  
ANISOU 5584  CA  GLU C 542     6148   3356   2537    992   -835  -1039       C  
ATOM   5585  C   GLU C 542      25.860  -6.042 -85.930  1.00 29.50           C  
ANISOU 5585  C   GLU C 542     5791   2996   2423    892  -1006  -1037       C  
ATOM   5586  O   GLU C 542      24.876  -6.588 -86.432  1.00 30.56           O  
ANISOU 5586  O   GLU C 542     5966   3022   2624    869  -1158  -1096       O  
ATOM   5587  CB  GLU C 542      28.143  -7.013 -86.264  1.00 39.49           C  
ANISOU 5587  CB  GLU C 542     7151   4302   3553   1082   -746  -1084       C  
ATOM   5588  CG  GLU C 542      27.567  -8.427 -86.287  1.00 37.33           C  
ANISOU 5588  CG  GLU C 542     6930   3866   3388   1097   -876  -1174       C  
ATOM   5589  CD  GLU C 542      27.664  -9.070 -87.654  1.00 38.43           C  
ANISOU 5589  CD  GLU C 542     7213   3952   3437   1161   -886  -1259       C  
ATOM   5590  OE1 GLU C 542      28.597  -8.719 -88.411  1.00 41.62           O  
ANISOU 5590  OE1 GLU C 542     7679   4430   3706   1221   -742  -1261       O  
ATOM   5591  OE2 GLU C 542      26.806  -9.920 -87.986  1.00 38.67           O  
ANISOU 5591  OE2 GLU C 542     7293   3864   3536   1144  -1031  -1323       O  
ATOM   5592  N   MET C 543      25.851  -5.524 -84.705  1.00 27.77           N  
ANISOU 5592  N   MET C 543     5451   2823   2275    824   -973   -966       N  
ATOM   5593  CA  MET C 543      24.678  -5.631 -83.847  1.00 27.05           C  
ANISOU 5593  CA  MET C 543     5268   2643   2365    708  -1105   -962       C  
ATOM   5594  C   MET C 543      23.541  -4.714 -84.296  1.00 26.95           C  
ANISOU 5594  C   MET C 543     5208   2643   2388    628  -1208   -943       C  
ATOM   5595  O   MET C 543      22.372  -5.087 -84.209  1.00 27.38           O  
ANISOU 5595  O   MET C 543     5214   2588   2601    559  -1347   -980       O  
ATOM   5596  CB  MET C 543      25.046  -5.332 -82.388  1.00 25.35           C  
ANISOU 5596  CB  MET C 543     4958   2463   2210    646  -1030   -891       C  
ATOM   5597  CG  MET C 543      25.513  -6.555 -81.596  1.00 27.18           C  
ANISOU 5597  CG  MET C 543     5165   2601   2562    664   -992   -888       C  
ATOM   5598  SD  MET C 543      25.870  -6.247 -79.852  1.00 50.19           S  
ANISOU 5598  SD  MET C 543     7886   5568   5617    548   -869   -712       S  
ATOM   5599  CE  MET C 543      27.307  -5.191 -79.983  1.00 23.05           C  
ANISOU 5599  CE  MET C 543     4414   2344   2000    629   -685   -617       C  
ATOM   5600  N   LEU C 544      23.877  -3.521 -84.779  1.00 26.50           N  
ANISOU 5600  N   LEU C 544     5152   2712   2205    636  -1133   -881       N  
ATOM   5601  CA  LEU C 544      22.847  -2.559 -85.161  1.00 26.41           C  
ANISOU 5601  CA  LEU C 544     5092   2706   2236    567  -1227   -857       C  
ATOM   5602  C   LEU C 544      22.106  -2.931 -86.444  1.00 29.42           C  
ANISOU 5602  C   LEU C 544     5581   2991   2607    606  -1371   -930       C  
ATOM   5603  O   LEU C 544      20.962  -2.525 -86.642  1.00 28.60           O  
ANISOU 5603  O   LEU C 544     5429   2832   2605    551  -1503   -936       O  
ATOM   5604  CB  LEU C 544      23.449  -1.160 -85.310  1.00 25.44           C  
ANISOU 5604  CB  LEU C 544     4935   2739   1993    558  -1094   -765       C  
ATOM   5605  CG  LEU C 544      23.581  -0.390 -83.997  1.00 24.34           C  
ANISOU 5605  CG  LEU C 544     4647   2690   1910    470  -1009   -672       C  
ATOM   5606  CD1 LEU C 544      24.645   0.682 -84.099  1.00 24.97           C  
ANISOU 5606  CD1 LEU C 544     4688   2938   1861    486   -822   -578       C  
ATOM   5607  CD2 LEU C 544      22.239   0.206 -83.595  1.00 23.58           C  
ANISOU 5607  CD2 LEU C 544     4445   2542   1970    358  -1131   -662       C  
ATOM   5608  N   ASP C 545      22.745  -3.710 -87.307  1.00 29.75           N  
ANISOU 5608  N   ASP C 545     5765   3005   2533    702  -1345   -987       N  
ATOM   5609  CA  ASP C 545      22.185  -3.972 -88.627  1.00 31.70           C  
ANISOU 5609  CA  ASP C 545     6145   3172   2730    742  -1468  -1047       C  
ATOM   5610  C   ASP C 545      21.424  -5.291 -88.697  1.00 32.94           C  
ANISOU 5610  C   ASP C 545     6323   3183   3009    747  -1616  -1133       C  
ATOM   5611  O   ASP C 545      21.854  -6.229 -89.366  1.00 34.36           O  
ANISOU 5611  O   ASP C 545     6630   3313   3112    820  -1611  -1197       O  
ATOM   5612  CB  ASP C 545      23.297  -3.949 -89.675  1.00 32.80           C  
ANISOU 5612  CB  ASP C 545     6440   3364   2661    829  -1343  -1057       C  
ATOM   5613  CG  ASP C 545      22.774  -3.675 -91.072  1.00 34.62           C  
ANISOU 5613  CG  ASP C 545     6817   3538   2800    850  -1449  -1086       C  
ATOM   5614  OD1 ASP C 545      21.583  -3.328 -91.211  1.00 34.88           O  
ANISOU 5614  OD1 ASP C 545     6819   3507   2929    804  -1618  -1087       O  
ATOM   5615  OD2 ASP C 545      23.568  -3.784 -92.026  1.00 35.90           O  
ANISOU 5615  OD2 ASP C 545     7125   3715   2800    910  -1359  -1109       O  
ATOM   5616  N   ALA C 546      20.287  -5.350 -88.008  1.00 42.50           N  
ANISOU 5616  N   ALA C 546     7399   4327   4423    663  -1734  -1134       N  
ATOM   5617  CA  ALA C 546      19.431  -6.533 -88.025  1.00 44.74           C  
ANISOU 5617  CA  ALA C 546     7668   4476   4857    648  -1867  -1208       C  
ATOM   5618  C   ALA C 546      17.983  -6.165 -87.706  1.00 45.50           C  
ANISOU 5618  C   ALA C 546     7617   4510   5161    556  -2003  -1202       C  
ATOM   5619  O   ALA C 546      17.060  -6.531 -88.434  1.00 48.77           O  
ANISOU 5619  O   ALA C 546     8061   4831   5639    565  -2158  -1254       O  
ATOM   5620  CB  ALA C 546      19.944  -7.575 -87.044  1.00 40.50           C  
ANISOU 5620  CB  ALA C 546     7081   3908   4398    640  -1786  -1225       C  
TER    5621      ALA C 546                                                      
ATOM   5622  N   SER A 309      42.919   1.211  -8.300  1.00 46.23           N  
ANISOU 5622  N   SER A 309     7040   5027   5498    425   -214  -1425       N  
ATOM   5623  CA  SER A 309      43.365   2.598  -8.390  1.00 45.66           C  
ANISOU 5623  CA  SER A 309     7113   4748   5488    412   -393  -1530       C  
ATOM   5624  C   SER A 309      44.073   2.866  -9.714  1.00 41.97           C  
ANISOU 5624  C   SER A 309     6480   4223   5245    285   -578  -1398       C  
ATOM   5625  O   SER A 309      44.485   3.993  -9.990  1.00 45.64           O  
ANISOU 5625  O   SER A 309     7029   4512   5801    251   -742  -1449       O  
ATOM   5626  CB  SER A 309      44.294   2.940  -7.224  1.00 45.69           C  
ANISOU 5626  CB  SER A 309     7398   4690   5271    344   -548  -1637       C  
ATOM   5627  OG  SER A 309      45.479   2.161  -7.281  1.00 44.95           O  
ANISOU 5627  OG  SER A 309     7250   4690   5138    171   -709  -1505       O  
ATOM   5628  N   LEU A 310      44.216   1.823 -10.527  1.00 40.39           N  
ANISOU 5628  N   LEU A 310     6054   4166   5126    215   -548  -1228       N  
ATOM   5629  CA  LEU A 310      44.889   1.946 -11.816  1.00 37.91           C  
ANISOU 5629  CA  LEU A 310     5580   3823   5002     98   -693  -1090       C  
ATOM   5630  C   LEU A 310      44.094   2.785 -12.805  1.00 36.65           C  
ANISOU 5630  C   LEU A 310     5332   3549   5046    173   -669  -1093       C  
ATOM   5631  O   LEU A 310      42.881   2.618 -12.944  1.00 37.86           O  
ANISOU 5631  O   LEU A 310     5404   3734   5249    305   -491  -1113       O  
ATOM   5632  CB  LEU A 310      45.151   0.568 -12.428  1.00 34.51           C  
ANISOU 5632  CB  LEU A 310     4948   3571   4591     27   -644   -922       C  
ATOM   5633  CG  LEU A 310      46.232  -0.313 -11.803  1.00 35.52           C  
ANISOU 5633  CG  LEU A 310     5112   3807   4578    -82   -723   -863       C  
ATOM   5634  CD1 LEU A 310      46.508  -1.509 -12.706  1.00 32.36           C  
ANISOU 5634  CD1 LEU A 310     4497   3545   4251   -144   -690   -693       C  
ATOM   5635  CD2 LEU A 310      47.502   0.486 -11.563  1.00 37.64           C  
ANISOU 5635  CD2 LEU A 310     5497   3965   4839   -204   -962   -880       C  
ATOM   5636  N   THR A 311      44.787   3.689 -13.490  1.00 32.90           N  
ANISOU 5636  N   THR A 311     4865   2938   4697     84   -855  -1059       N  
ATOM   5637  CA  THR A 311      44.203   4.387 -14.627  1.00 33.43           C  
ANISOU 5637  CA  THR A 311     4827   2905   4971    123   -865  -1016       C  
ATOM   5638  C   THR A 311      44.034   3.406 -15.783  1.00 29.48           C  
ANISOU 5638  C   THR A 311     4091   2546   4563     84   -800   -845       C  
ATOM   5639  O   THR A 311      44.575   2.297 -15.749  1.00 28.18           O  
ANISOU 5639  O   THR A 311     3855   2534   4318      9   -777   -759       O  
ATOM   5640  CB  THR A 311      45.069   5.572 -15.087  1.00 32.57           C  
ANISOU 5640  CB  THR A 311     4790   2615   4970     17  -1090  -1003       C  
ATOM   5641  OG1 THR A 311      46.290   5.084 -15.656  1.00 31.15           O  
ANISOU 5641  OG1 THR A 311     4513   2514   4808   -158  -1211   -849       O  
ATOM   5642  CG2 THR A 311      45.381   6.505 -13.918  1.00 37.15           C  
ANISOU 5642  CG2 THR A 311     5627   3041   5445     33  -1190  -1175       C  
ATOM   5643  N   ALA A 312      43.286   3.816 -16.803  1.00 29.20           N  
ANISOU 5643  N   ALA A 312     3948   2450   4696    135   -780   -797       N  
ATOM   5644  CA  ALA A 312      43.077   2.978 -17.978  1.00 27.34           C  
ANISOU 5644  CA  ALA A 312     3515   2328   4546     97   -738   -642       C  
ATOM   5645  C   ALA A 312      44.404   2.687 -18.665  1.00 26.18           C  
ANISOU 5645  C   ALA A 312     3321   2226   4401    -70   -868   -510       C  
ATOM   5646  O   ALA A 312      44.678   1.555 -19.047  1.00 24.70           O  
ANISOU 5646  O   ALA A 312     3025   2186   4175   -120   -818   -410       O  
ATOM   5647  CB  ALA A 312      42.112   3.640 -18.947  1.00 27.60           C  
ANISOU 5647  CB  ALA A 312     3467   2263   4758    172   -735   -613       C  
ATOM   5648  N   ASP A 313      45.233   3.714 -18.807  1.00 27.04           N  
ANISOU 5648  N   ASP A 313     3509   2201   4562   -155  -1033   -507       N  
ATOM   5649  CA  ASP A 313      46.541   3.536 -19.420  1.00 26.28           C  
ANISOU 5649  CA  ASP A 313     3357   2145   4484   -315  -1150   -374       C  
ATOM   5650  C   ASP A 313      47.423   2.594 -18.603  1.00 26.00           C  
ANISOU 5650  C   ASP A 313     3333   2239   4307   -378  -1146   -367       C  
ATOM   5651  O   ASP A 313      48.143   1.762 -19.161  1.00 26.54           O  
ANISOU 5651  O   ASP A 313     3286   2426   4372   -459  -1144   -241       O  
ATOM   5652  CB  ASP A 313      47.231   4.882 -19.599  1.00 27.71           C  
ANISOU 5652  CB  ASP A 313     3625   2147   4757   -401  -1333   -371       C  
ATOM   5653  CG  ASP A 313      46.644   5.683 -20.741  1.00 29.83           C  
ANISOU 5653  CG  ASP A 313     3847   2302   5184   -380  -1364   -312       C  
ATOM   5654  OD1 ASP A 313      45.955   5.089 -21.601  1.00 31.56           O  
ANISOU 5654  OD1 ASP A 313     3944   2605   5442   -333  -1265   -237       O  
ATOM   5655  OD2 ASP A 313      46.882   6.905 -20.789  1.00 37.01           O  
ANISOU 5655  OD2 ASP A 313     4849   3031   6180   -416  -1500   -335       O  
ATOM   5656  N   GLN A 314      47.363   2.725 -17.281  1.00 27.00           N  
ANISOU 5656  N   GLN A 314     3606   2340   4313   -334  -1145   -502       N  
ATOM   5657  CA  GLN A 314      48.126   1.847 -16.401  1.00 27.89           C  
ANISOU 5657  CA  GLN A 314     3748   2569   4281   -387  -1154   -499       C  
ATOM   5658  C   GLN A 314      47.618   0.412 -16.485  1.00 25.31           C  
ANISOU 5658  C   GLN A 314     3305   2420   3891   -333   -985   -446       C  
ATOM   5659  O   GLN A 314      48.404  -0.529 -16.403  1.00 24.51           O  
ANISOU 5659  O   GLN A 314     3144   2435   3734   -402   -997   -363       O  
ATOM   5660  CB  GLN A 314      48.071   2.337 -14.951  1.00 35.08           C  
ANISOU 5660  CB  GLN A 314     4871   3405   5052   -346  -1190   -663       C  
ATOM   5661  CG  GLN A 314      48.934   3.554 -14.658  1.00 37.93           C  
ANISOU 5661  CG  GLN A 314     5370   3596   5447   -440  -1405   -708       C  
ATOM   5662  CD  GLN A 314      48.670   4.131 -13.280  1.00 36.40           C  
ANISOU 5662  CD  GLN A 314     5422   3305   5104   -374  -1431   -898       C  
ATOM   5663  OE1 GLN A 314      47.636   3.857 -12.667  1.00 34.22           O  
ANISOU 5663  OE1 GLN A 314     5210   3067   4725   -231  -1260  -1005       O  
ATOM   5664  NE2 GLN A 314      49.610   4.926 -12.782  1.00 39.01           N  
ANISOU 5664  NE2 GLN A 314     5895   3508   5419   -480  -1644   -938       N  
ATOM   5665  N   MET A 315      46.306   0.249 -16.649  1.00 25.07           N  
ANISOU 5665  N   MET A 315     3239   2405   3882   -211   -835   -487       N  
ATOM   5666  CA  MET A 315      45.717  -1.081 -16.776  1.00 23.94           C  
ANISOU 5666  CA  MET A 315     2985   2415   3698   -166   -683   -432       C  
ATOM   5667  C   MET A 315      46.226  -1.763 -18.045  1.00 22.19           C  
ANISOU 5667  C   MET A 315     2607   2265   3558   -244   -705   -277       C  
ATOM   5668  O   MET A 315      46.629  -2.925 -18.009  1.00 21.24           O  
ANISOU 5668  O   MET A 315     2426   2268   3376   -276   -665   -208       O  
ATOM   5669  CB  MET A 315      44.186  -1.005 -16.787  1.00 24.12           C  
ANISOU 5669  CB  MET A 315     2978   2425   3763    -28   -533   -493       C  
ATOM   5670  CG  MET A 315      43.493  -2.337 -17.064  1.00 22.92           C  
ANISOU 5670  CG  MET A 315     2694   2414   3600      4   -392   -419       C  
ATOM   5671  SD  MET A 315      43.759  -3.615 -15.815  1.00 29.29           S  
ANISOU 5671  SD  MET A 315     3549   3365   4213     -4   -306   -427       S  
ATOM   5672  CE  MET A 315      42.456  -3.221 -14.652  1.00 27.92           C  
ANISOU 5672  CE  MET A 315     3468   3172   3969    143   -143   -567       C  
ATOM   5673  N   VAL A 316      46.221  -1.032 -19.158  1.00 22.05           N  
ANISOU 5673  N   VAL A 316     2538   2166   3673   -271   -768   -223       N  
ATOM   5674  CA  VAL A 316      46.706  -1.558 -20.432  1.00 23.76           C  
ANISOU 5674  CA  VAL A 316     2631   2443   3953   -341   -783    -80       C  
ATOM   5675  C   VAL A 316      48.183  -1.921 -20.358  1.00 24.35           C  
ANISOU 5675  C   VAL A 316     2687   2575   3990   -452   -863     -4       C  
ATOM   5676  O   VAL A 316      48.591  -2.983 -20.830  1.00 22.51           O  
ANISOU 5676  O   VAL A 316     2364   2453   3736   -477   -815     86       O  
ATOM   5677  CB  VAL A 316      46.495  -0.552 -21.585  1.00 24.43           C  
ANISOU 5677  CB  VAL A 316     2692   2418   4174   -358   -851    -32       C  
ATOM   5678  CG1 VAL A 316      47.179  -1.038 -22.858  1.00 23.76           C  
ANISOU 5678  CG1 VAL A 316     2507   2398   4125   -440   -867    116       C  
ATOM   5679  CG2 VAL A 316      45.024  -0.350 -21.838  1.00 22.73           C  
ANISOU 5679  CG2 VAL A 316     2457   2159   4021   -247   -776    -79       C  
ATOM   5680  N   SER A 317      48.977  -1.038 -19.760  1.00 23.97           N  
ANISOU 5680  N   SER A 317     2724   2443   3943   -515   -989    -39       N  
ATOM   5681  CA  SER A 317      50.408  -1.280 -19.592  1.00 24.88           C  
ANISOU 5681  CA  SER A 317     2809   2603   4044   -626  -1085     40       C  
ATOM   5682  C   SER A 317      50.645  -2.561 -18.806  1.00 24.83           C  
ANISOU 5682  C   SER A 317     2788   2726   3919   -607  -1024     40       C  
ATOM   5683  O   SER A 317      51.480  -3.382 -19.180  1.00 22.30           O  
ANISOU 5683  O   SER A 317     2367   2500   3606   -655  -1020    147       O  
ATOM   5684  CB  SER A 317      51.081  -0.103 -18.885  1.00 30.41           C  
ANISOU 5684  CB  SER A 317     3622   3175   4759   -697  -1251    -14       C  
ATOM   5685  OG  SER A 317      50.915   1.092 -19.622  1.00 38.90           O  
ANISOU 5685  OG  SER A 317     4711   4115   5953   -722  -1320     -3       O  
ATOM   5686  N   ALA A 318      49.893  -2.729 -17.724  1.00 22.38           N  
ANISOU 5686  N   ALA A 318     2583   2420   3501   -530   -968    -76       N  
ATOM   5687  CA  ALA A 318      50.011  -3.916 -16.885  1.00 22.90           C  
ANISOU 5687  CA  ALA A 318     2657   2601   3443   -511   -910    -76       C  
ATOM   5688  C   ALA A 318      49.693  -5.199 -17.653  1.00 23.70           C  
ANISOU 5688  C   ALA A 318     2627   2817   3560   -478   -786     14       C  
ATOM   5689  O   ALA A 318      50.395  -6.203 -17.517  1.00 24.13           O  
ANISOU 5689  O   ALA A 318     2630   2962   3577   -508   -786     85       O  
ATOM   5690  CB  ALA A 318      49.105  -3.792 -15.678  1.00 23.59           C  
ANISOU 5690  CB  ALA A 318     2886   2671   3407   -427   -846   -212       C  
ATOM   5691  N   LEU A 319      48.634  -5.163 -18.456  1.00 19.79           N  
ANISOU 5691  N   LEU A 319     2086   2308   3127   -417   -693      9       N  
ATOM   5692  CA  LEU A 319      48.202  -6.343 -19.197  1.00 18.81           C  
ANISOU 5692  CA  LEU A 319     1860   2272   3015   -387   -589     81       C  
ATOM   5693  C   LEU A 319      49.157  -6.688 -20.335  1.00 21.98           C  
ANISOU 5693  C   LEU A 319     2163   2707   3481   -450   -625    201       C  
ATOM   5694  O   LEU A 319      49.428  -7.863 -20.587  1.00 25.03           O  
ANISOU 5694  O   LEU A 319     2490   3179   3841   -446   -573    264       O  
ATOM   5695  CB  LEU A 319      46.788  -6.142 -19.742  1.00 18.33           C  
ANISOU 5695  CB  LEU A 319     1776   2178   3012   -312   -505     48       C  
ATOM   5696  CG  LEU A 319      45.710  -6.041 -18.661  1.00 19.10           C  
ANISOU 5696  CG  LEU A 319     1941   2268   3050   -229   -421    -57       C  
ATOM   5697  CD1 LEU A 319      44.335  -5.862 -19.284  1.00 19.03           C  
ANISOU 5697  CD1 LEU A 319     1873   2226   3131   -156   -344    -69       C  
ATOM   5698  CD2 LEU A 319      45.743  -7.260 -17.750  1.00 19.46           C  
ANISOU 5698  CD2 LEU A 319     2001   2418   2977   -220   -350    -49       C  
ATOM   5699  N   LEU A 320      49.665  -5.667 -21.020  1.00 22.39           N  
ANISOU 5699  N   LEU A 320     2204   2689   3616   -504   -706    234       N  
ATOM   5700  CA  LEU A 320      50.637  -5.888 -22.084  1.00 24.93           C  
ANISOU 5700  CA  LEU A 320     2433   3045   3993   -564   -724    353       C  
ATOM   5701  C   LEU A 320      51.920  -6.467 -21.510  1.00 23.91           C  
ANISOU 5701  C   LEU A 320     2266   2983   3835   -613   -767    407       C  
ATOM   5702  O   LEU A 320      52.545  -7.330 -22.121  1.00 26.16           O  
ANISOU 5702  O   LEU A 320     2465   3344   4131   -618   -721    496       O  
ATOM   5703  CB  LEU A 320      50.933  -4.593 -22.843  1.00 24.68           C  
ANISOU 5703  CB  LEU A 320     2400   2920   4056   -623   -804    390       C  
ATOM   5704  CG  LEU A 320      49.803  -4.076 -23.731  1.00 24.54           C  
ANISOU 5704  CG  LEU A 320     2396   2838   4089   -580   -774    376       C  
ATOM   5705  CD1 LEU A 320      50.140  -2.704 -24.294  1.00 27.84           C  
ANISOU 5705  CD1 LEU A 320     2832   3147   4599   -645   -873    412       C  
ATOM   5706  CD2 LEU A 320      49.524  -5.065 -24.852  1.00 20.09           C  
ANISOU 5706  CD2 LEU A 320     1769   2351   3513   -554   -683    448       C  
ATOM   5707  N   ASP A 321      52.305  -5.992 -20.329  1.00 25.33           N  
ANISOU 5707  N   ASP A 321     2516   3128   3979   -645   -860    351       N  
ATOM   5708  CA  ASP A 321      53.501  -6.493 -19.662  1.00 26.89           C  
ANISOU 5708  CA  ASP A 321     2681   3381   4155   -696   -930    404       C  
ATOM   5709  C   ASP A 321      53.332  -7.932 -19.190  1.00 24.32           C  
ANISOU 5709  C   ASP A 321     2343   3154   3745   -638   -847    410       C  
ATOM   5710  O   ASP A 321      54.310  -8.668 -19.069  1.00 29.71           O  
ANISOU 5710  O   ASP A 321     2953   3900   4436   -661   -873    489       O  
ATOM   5711  CB  ASP A 321      53.872  -5.609 -18.468  1.00 27.30           C  
ANISOU 5711  CB  ASP A 321     2840   3360   4172   -749  -1073    333       C  
ATOM   5712  CG  ASP A 321      54.738  -4.423 -18.863  1.00 33.56           C  
ANISOU 5712  CG  ASP A 321     3606   4069   5076   -852  -1207    384       C  
ATOM   5713  OD1 ASP A 321      54.597  -3.929 -20.004  1.00 37.79           O  
ANISOU 5713  OD1 ASP A 321     4101   4574   5683   -843  -1148    429       O  
ATOM   5714  OD2 ASP A 321      55.566  -3.989 -18.033  1.00 38.71           O  
ANISOU 5714  OD2 ASP A 321     4311   4685   5712   -911  -1333    378       O  
ATOM   5715  N   ALA A 322      52.093  -8.331 -18.920  1.00 20.39           N  
ANISOU 5715  N   ALA A 322     1906   2664   3178   -562   -751    334       N  
ATOM   5716  CA  ALA A 322      51.826  -9.652 -18.363  1.00 22.24           C  
ANISOU 5716  CA  ALA A 322     2144   2977   3329   -515   -678    340       C  
ATOM   5717  C   ALA A 322      51.761 -10.740 -19.429  1.00 22.60           C  
ANISOU 5717  C   ALA A 322     2094   3078   3414   -481   -585    417       C  
ATOM   5718  O   ALA A 322      51.661 -11.922 -19.097  1.00 21.96           O  
ANISOU 5718  O   ALA A 322     2007   3054   3283   -448   -535    439       O  
ATOM   5719  CB  ALA A 322      50.526  -9.634 -17.565  1.00 22.94           C  
ANISOU 5719  CB  ALA A 322     2332   3054   3330   -455   -607    239       C  
ATOM   5720  N   GLU A 323      51.816 -10.343 -20.698  1.00 20.68           N  
ANISOU 5720  N   GLU A 323     1793   2813   3254   -491   -567    457       N  
ATOM   5721  CA  GLU A 323      51.572 -11.278 -21.797  1.00 19.13           C  
ANISOU 5721  CA  GLU A 323     1541   2653   3076   -453   -477    509       C  
ATOM   5722  C   GLU A 323      52.538 -12.453 -21.763  1.00 16.30           C  
ANISOU 5722  C   GLU A 323     1124   2361   2709   -441   -460    582       C  
ATOM   5723  O   GLU A 323      53.743 -12.260 -21.613  1.00 17.78           O  
ANISOU 5723  O   GLU A 323     1291   2554   2912   -465   -503    623       O  
ATOM   5724  CB  GLU A 323      51.664 -10.565 -23.148  1.00 21.54           C  
ANISOU 5724  CB  GLU A 323     1819   2921   3445   -470   -468    546       C  
ATOM   5725  CG  GLU A 323      50.361  -9.926 -23.575  1.00 22.97           C  
ANISOU 5725  CG  GLU A 323     2037   3043   3647   -453   -456    493       C  
ATOM   5726  CD  GLU A 323      49.292 -10.956 -23.884  1.00 21.44           C  
ANISOU 5726  CD  GLU A 323     1852   2872   3422   -396   -376    477       C  
ATOM   5727  OE1 GLU A 323      48.437 -11.206 -23.010  1.00 18.05           O  
ANISOU 5727  OE1 GLU A 323     1455   2443   2959   -364   -352    418       O  
ATOM   5728  OE2 GLU A 323      49.308 -11.517 -24.999  1.00 23.54           O  
ANISOU 5728  OE2 GLU A 323     2098   3151   3694   -386   -339    526       O  
ATOM   5729  N   PRO A 324      52.000 -13.677 -21.883  1.00 15.89           N  
ANISOU 5729  N   PRO A 324     1079   2338   2619   -388   -385    584       N  
ATOM   5730  CA  PRO A 324      52.825 -14.885 -21.930  1.00 16.29           C  
ANISOU 5730  CA  PRO A 324     1096   2431   2662   -355   -358    643       C  
ATOM   5731  C   PRO A 324      53.509 -14.993 -23.284  1.00 15.87           C  
ANISOU 5731  C   PRO A 324     1024   2370   2636   -328   -299    683       C  
ATOM   5732  O   PRO A 324      53.079 -14.348 -24.243  1.00 17.49           O  
ANISOU 5732  O   PRO A 324     1246   2546   2854   -335   -276    671       O  
ATOM   5733  CB  PRO A 324      51.810 -16.009 -21.722  1.00 18.55           C  
ANISOU 5733  CB  PRO A 324     1417   2726   2903   -314   -302    623       C  
ATOM   5734  CG  PRO A 324      50.578 -15.481 -22.341  1.00 19.28           C  
ANISOU 5734  CG  PRO A 324     1545   2779   3003   -312   -268    572       C  
ATOM   5735  CD  PRO A 324      50.572 -13.990 -22.068  1.00 17.62           C  
ANISOU 5735  CD  PRO A 324     1345   2537   2811   -353   -323    533       C  
ATOM   5736  N   PRO A 325      54.574 -15.794 -23.370  1.00 16.26           N  
ANISOU 5736  N   PRO A 325     1030   2448   2699   -296   -279    739       N  
ATOM   5737  CA  PRO A 325      55.248 -15.923 -24.662  1.00 17.35           C  
ANISOU 5737  CA  PRO A 325     1134   2592   2864   -265   -209    786       C  
ATOM   5738  C   PRO A 325      54.500 -16.852 -25.610  1.00 16.00           C  
ANISOU 5738  C   PRO A 325      983   2422   2673   -215   -131    781       C  
ATOM   5739  O   PRO A 325      53.654 -17.633 -25.176  1.00 17.21           O  
ANISOU 5739  O   PRO A 325     1165   2570   2803   -198   -133    754       O  
ATOM   5740  CB  PRO A 325      56.603 -16.516 -24.287  1.00 17.62           C  
ANISOU 5740  CB  PRO A 325     1103   2658   2935   -240   -213    847       C  
ATOM   5741  CG  PRO A 325      56.324 -17.313 -23.056  1.00 19.39           C  
ANISOU 5741  CG  PRO A 325     1341   2890   3134   -231   -263    835       C  
ATOM   5742  CD  PRO A 325      55.242 -16.568 -22.309  1.00 20.68           C  
ANISOU 5742  CD  PRO A 325     1563   3037   3257   -285   -320    772       C  
ATOM   5743  N   ILE A 326      54.812 -16.754 -26.896  1.00 15.59           N  
ANISOU 5743  N   ILE A 326      911   2379   2631   -197    -65    818       N  
ATOM   5744  CA  ILE A 326      54.332 -17.718 -27.869  1.00 15.45           C  
ANISOU 5744  CA  ILE A 326      911   2365   2593   -145     11    825       C  
ATOM   5745  C   ILE A 326      55.251 -18.936 -27.845  1.00 16.05           C  
ANISOU 5745  C   ILE A 326      949   2466   2684    -63     71    861       C  
ATOM   5746  O   ILE A 326      56.450 -18.817 -28.098  1.00 19.31           O  
ANISOU 5746  O   ILE A 326     1282   2916   3139    -40    114    922       O  
ATOM   5747  CB  ILE A 326      54.287 -17.114 -29.285  1.00 18.96           C  
ANISOU 5747  CB  ILE A 326     1388   2804   3011   -153     64    843       C  
ATOM   5748  CG1 ILE A 326      53.225 -16.014 -29.357  1.00 21.25           C  
ANISOU 5748  CG1 ILE A 326     1726   3052   3295   -222     -5    806       C  
ATOM   5749  CG2 ILE A 326      53.990 -18.190 -30.311  1.00 23.61           C  
ANISOU 5749  CG2 ILE A 326     2071   3370   3528    -81    140    819       C  
ATOM   5750  CD1 ILE A 326      53.165 -15.311 -30.696  1.00 24.25           C  
ANISOU 5750  CD1 ILE A 326     2145   3421   3647   -242     25    836       C  
ATOM   5751  N   LEU A 327      54.701 -20.102 -27.514  1.00 15.29           N  
ANISOU 5751  N   LEU A 327      918   2335   2556    -18     69    824       N  
ATOM   5752  CA  LEU A 327      55.497 -21.325 -27.431  1.00 15.96           C  
ANISOU 5752  CA  LEU A 327      979   2423   2662     70    115    853       C  
ATOM   5753  C   LEU A 327      55.562 -22.092 -28.749  1.00 16.49           C  
ANISOU 5753  C   LEU A 327     1120   2460   2685    154    217    836       C  
ATOM   5754  O   LEU A 327      54.747 -21.889 -29.652  1.00 16.21           O  
ANISOU 5754  O   LEU A 327     1184   2392   2583    137    231    792       O  
ATOM   5755  CB  LEU A 327      54.953 -22.244 -26.335  1.00 15.64           C  
ANISOU 5755  CB  LEU A 327      979   2350   2614     74     53    832       C  
ATOM   5756  CG  LEU A 327      54.893 -21.636 -24.933  1.00 15.65           C  
ANISOU 5756  CG  LEU A 327      936   2381   2630      2    -41    844       C  
ATOM   5757  CD1 LEU A 327      54.521 -22.704 -23.918  1.00 15.37           C  
ANISOU 5757  CD1 LEU A 327      943   2320   2576     17    -82    844       C  
ATOM   5758  CD2 LEU A 327      56.226 -20.983 -24.582  1.00 16.07           C  
ANISOU 5758  CD2 LEU A 327      884   2481   2742    -11    -66    902       C  
ATOM   5759  N   TYR A 328      56.547 -22.978 -28.845  1.00 18.70           N  
ANISOU 5759  N   TYR A 328     1356   2748   3001    249    282    871       N  
ATOM   5760  CA  TYR A 328      56.715 -23.813 -30.025  1.00 18.23           C  
ANISOU 5760  CA  TYR A 328     1384   2653   2891    351    391    844       C  
ATOM   5761  C   TYR A 328      56.220 -25.226 -29.784  1.00 18.31           C  
ANISOU 5761  C   TYR A 328     1498   2577   2881    412    367    796       C  
ATOM   5762  O   TYR A 328      56.236 -25.715 -28.652  1.00 18.11           O  
ANISOU 5762  O   TYR A 328     1431   2540   2908    404    294    817       O  
ATOM   5763  CB  TYR A 328      58.182 -23.844 -30.463  1.00 19.59           C  
ANISOU 5763  CB  TYR A 328     1436   2883   3122    438    508    915       C  
ATOM   5764  CG  TYR A 328      58.561 -22.656 -31.297  1.00 19.91           C  
ANISOU 5764  CG  TYR A 328     1427   2988   3149    394    575    957       C  
ATOM   5765  CD1 TYR A 328      58.766 -21.412 -30.714  1.00 26.64           C  
ANISOU 5765  CD1 TYR A 328     2164   3893   4065    284    501   1012       C  
ATOM   5766  CD2 TYR A 328      58.687 -22.771 -32.675  1.00 23.19           C  
ANISOU 5766  CD2 TYR A 328     1929   3404   3479    458    707    942       C  
ATOM   5767  CE1 TYR A 328      59.101 -20.322 -31.478  1.00 30.21           C  
ANISOU 5767  CE1 TYR A 328     2574   4393   4512    235    553   1062       C  
ATOM   5768  CE2 TYR A 328      59.021 -21.690 -33.448  1.00 24.19           C  
ANISOU 5768  CE2 TYR A 328     2016   3589   3585    411    771    995       C  
ATOM   5769  CZ  TYR A 328      59.225 -20.468 -32.845  1.00 26.81           C  
ANISOU 5769  CZ  TYR A 328     2220   3969   3997    296    692   1059       C  
ATOM   5770  OH  TYR A 328      59.557 -19.383 -33.615  1.00 36.14           O  
ANISOU 5770  OH  TYR A 328     3365   5200   5168    240    747   1124       O  
ATOM   5771  N   SER A 329      55.770 -25.873 -30.853  1.00 18.99           N  
ANISOU 5771  N   SER A 329     1732   2597   2886    466    417    735       N  
ATOM   5772  CA  SER A 329      55.494 -27.297 -30.802  1.00 19.24           C  
ANISOU 5772  CA  SER A 329     1872   2531   2907    538    404    692       C  
ATOM   5773  C   SER A 329      56.807 -28.042 -30.609  1.00 20.44           C  
ANISOU 5773  C   SER A 329     1940   2692   3135    667    483    736       C  
ATOM   5774  O   SER A 329      57.849 -27.610 -31.104  1.00 21.57           O  
ANISOU 5774  O   SER A 329     1988   2905   3304    726    592    779       O  
ATOM   5775  CB  SER A 329      54.791 -27.765 -32.074  1.00 21.96           C  
ANISOU 5775  CB  SER A 329     2410   2793   3140    566    430    612       C  
ATOM   5776  OG  SER A 329      54.452 -29.136 -31.987  1.00 22.59           O  
ANISOU 5776  OG  SER A 329     2608   2759   3217    622    393    567       O  
ATOM   5777  N   GLU A 330      56.755 -29.147 -29.875  1.00 20.69           N  
ANISOU 5777  N   GLU A 330     1995   2652   3212    708    427    738       N  
ATOM   5778  CA  GLU A 330      57.922 -29.993 -29.681  1.00 23.57           C  
ANISOU 5778  CA  GLU A 330     2289   3003   3663    844    488    779       C  
ATOM   5779  C   GLU A 330      57.898 -31.160 -30.632  1.00 29.03           C  
ANISOU 5779  C   GLU A 330     3144   3582   4306    973    562    705       C  
ATOM   5780  O   GLU A 330      57.248 -32.169 -30.363  1.00 26.89           O  
ANISOU 5780  O   GLU A 330     2995   3195   4026    979    484    667       O  
ATOM   5781  CB  GLU A 330      57.994 -30.536 -28.264  1.00 29.28           C  
ANISOU 5781  CB  GLU A 330     2946   3707   4473    821    373    837       C  
ATOM   5782  CG  GLU A 330      58.706 -29.676 -27.271  1.00 30.97           C  
ANISOU 5782  CG  GLU A 330     2971   4029   4767    763    324    929       C  
ATOM   5783  CD  GLU A 330      59.121 -30.495 -26.079  1.00 32.35           C  
ANISOU 5783  CD  GLU A 330     3093   4174   5027    791    234    994       C  
ATOM   5784  OE1 GLU A 330      58.263 -30.698 -25.203  1.00 29.57           O  
ANISOU 5784  OE1 GLU A 330     2805   3790   4639    702    126    993       O  
ATOM   5785  OE2 GLU A 330      60.289 -30.941 -26.024  1.00 33.69           O  
ANISOU 5785  OE2 GLU A 330     3153   4350   5298    903    275   1055       O  
ATOM   5786  N   TYR A 331      58.601 -31.008 -31.744  1.00 29.96           N  
ANISOU 5786  N   TYR A 331     3271   3728   4385   1075    714    687       N  
ATOM   5787  CA  TYR A 331      58.867 -32.102 -32.657  1.00 32.10           C  
ANISOU 5787  CA  TYR A 331     3691   3898   4609   1232    815    615       C  
ATOM   5788  C   TYR A 331      60.135 -31.716 -33.404  1.00 31.49           C  
ANISOU 5788  C   TYR A 331     3503   3912   4550   1354   1010    653       C  
ATOM   5789  O   TYR A 331      60.446 -30.532 -33.528  1.00 32.68           O  
ANISOU 5789  O   TYR A 331     3526   4187   4704   1282   1052    713       O  
ATOM   5790  CB  TYR A 331      57.698 -32.336 -33.619  1.00 28.72           C  
ANISOU 5790  CB  TYR A 331     3515   3373   4025   1191    782    503       C  
ATOM   5791  CG  TYR A 331      57.453 -31.183 -34.575  1.00 30.33           C  
ANISOU 5791  CG  TYR A 331     3748   3660   4114   1123    841    490       C  
ATOM   5792  CD1 TYR A 331      56.607 -30.132 -34.237  1.00 28.51           C  
ANISOU 5792  CD1 TYR A 331     3475   3487   3870    953    731    515       C  
ATOM   5793  CD2 TYR A 331      58.084 -31.139 -35.812  1.00 29.70           C  
ANISOU 5793  CD2 TYR A 331     3744   3602   3940   1236   1013    457       C  
ATOM   5794  CE1 TYR A 331      56.392 -29.070 -35.115  1.00 24.97           C  
ANISOU 5794  CE1 TYR A 331     3057   3104   3325    892    774    512       C  
ATOM   5795  CE2 TYR A 331      57.878 -30.086 -36.692  1.00 30.93           C  
ANISOU 5795  CE2 TYR A 331     3936   3832   3983   1169   1064    459       C  
ATOM   5796  CZ  TYR A 331      57.034 -29.054 -36.344  1.00 31.66           C  
ANISOU 5796  CZ  TYR A 331     3984   3972   4074    995    936    489       C  
ATOM   5797  OH  TYR A 331      56.840 -28.013 -37.229  1.00 32.88           O  
ANISOU 5797  OH  TYR A 331     4178   4190   4125    931    976    500       O  
ATOM   5798  N   ASP A 332      60.880 -32.695 -33.896  1.00 34.94           N  
ANISOU 5798  N   ASP A 332     3984   4287   5006   1541   1136    624       N  
ATOM   5799  CA  ASP A 332      62.112 -32.366 -34.590  1.00 33.91           C  
ANISOU 5799  CA  ASP A 332     3728   4251   4903   1669   1346    671       C  
ATOM   5800  C   ASP A 332      61.718 -32.193 -36.059  1.00 35.34           C  
ANISOU 5800  C   ASP A 332     4125   4418   4886   1698   1468    576       C  
ATOM   5801  O   ASP A 332      61.192 -33.114 -36.684  1.00 34.37           O  
ANISOU 5801  O   ASP A 332     4248   4161   4651   1772   1472    459       O  
ATOM   5802  CB  ASP A 332      63.187 -33.444 -34.341  1.00 37.60           C  
ANISOU 5802  CB  ASP A 332     4109   4668   5508   1871   1435    697       C  
ATOM   5803  CG  ASP A 332      64.412 -33.318 -35.251  1.00 39.39           C  
ANISOU 5803  CG  ASP A 332     4259   4976   5730   1981   1645    715       C  
ATOM   5804  OD1 ASP A 332      64.463 -32.441 -36.140  1.00 43.50           O  
ANISOU 5804  OD1 ASP A 332     4794   5587   6145   1945   1762    720       O  
ATOM   5805  OD2 ASP A 332      65.373 -34.085 -35.036  1.00 42.05           O  
ANISOU 5805  OD2 ASP A 332     4518   5288   6171   2079   1674    732       O  
ATOM   5806  N   PRO A 333      61.942 -30.981 -36.598  1.00 34.76           N  
ANISOU 5806  N   PRO A 333     3971   4475   4761   1626   1553    630       N  
ATOM   5807  CA  PRO A 333      61.505 -30.577 -37.940  1.00 33.79           C  
ANISOU 5807  CA  PRO A 333     4047   4359   4434   1616   1646    563       C  
ATOM   5808  C   PRO A 333      62.276 -31.261 -39.065  1.00 37.16           C  
ANISOU 5808  C   PRO A 333     4585   4764   4771   1827   1885    510       C  
ATOM   5809  O   PRO A 333      61.937 -31.070 -40.231  1.00 36.80           O  
ANISOU 5809  O   PRO A 333     4743   4712   4528   1836   1970    444       O  
ATOM   5810  CB  PRO A 333      61.758 -29.065 -37.944  1.00 35.10           C  
ANISOU 5810  CB  PRO A 333     4035   4679   4624   1483   1666    674       C  
ATOM   5811  CG  PRO A 333      62.890 -28.884 -36.988  1.00 34.66           C  
ANISOU 5811  CG  PRO A 333     3675   4711   4786   1512   1693    800       C  
ATOM   5812  CD  PRO A 333      62.639 -29.888 -35.897  1.00 34.15           C  
ANISOU 5812  CD  PRO A 333     3608   4544   4826   1537   1544    770       C  
ATOM   5813  N   THR A 334      63.294 -32.043 -38.723  1.00 36.22           N  
ANISOU 5813  N   THR A 334     4339   4632   4790   1999   1993    538       N  
ATOM   5814  CA  THR A 334      64.035 -32.792 -39.730  1.00 38.97           C  
ANISOU 5814  CA  THR A 334     4805   4946   5057   2163   2172    473       C  
ATOM   5815  C   THR A 334      63.430 -34.181 -39.918  1.00 39.69           C  
ANISOU 5815  C   THR A 334     5171   4838   5072   2290   2130    322       C  
ATOM   5816  O   THR A 334      63.770 -34.896 -40.859  1.00 42.00           O  
ANISOU 5816  O   THR A 334     5639   5068   5252   2417   2250    231       O  
ATOM   5817  CB  THR A 334      65.527 -32.933 -39.359  1.00 41.45           C  
ANISOU 5817  CB  THR A 334     4856   5337   5556   2215   2239    572       C  
ATOM   5818  OG1 THR A 334      65.666 -33.849 -38.265  1.00 40.45           O  
ANISOU 5818  OG1 THR A 334     4650   5123   5595   2261   2114    576       O  
ATOM   5819  CG2 THR A 334      66.125 -31.581 -38.982  1.00 39.95           C  
ANISOU 5819  CG2 THR A 334     4395   5314   5470   2065   2223    723       C  
ATOM   5820  N   ARG A 335      62.531 -34.556 -39.014  1.00 37.86           N  
ANISOU 5820  N   ARG A 335     4982   4503   4901   2212   1919    300       N  
ATOM   5821  CA  ARG A 335      61.892 -35.865 -39.063  1.00 40.83           C  
ANISOU 5821  CA  ARG A 335     5613   4673   5229   2280   1818    171       C  
ATOM   5822  C   ARG A 335      60.590 -35.791 -39.850  1.00 41.00           C  
ANISOU 5822  C   ARG A 335     5939   4607   5031   2159   1702     56       C  
ATOM   5823  O   ARG A 335      59.968 -34.731 -39.915  1.00 37.42           O  
ANISOU 5823  O   ARG A 335     5456   4246   4517   1980   1623     96       O  
ATOM   5824  CB  ARG A 335      61.630 -36.385 -37.646  1.00 42.37           C  
ANISOU 5824  CB  ARG A 335     5689   4800   5611   2213   1612    224       C  
ATOM   5825  N   PRO A 336      60.175 -36.915 -40.460  1.00 43.53           N  
ANISOU 5825  N   PRO A 336     6558   4741   5239   2257   1681    -86       N  
ATOM   5826  CA  PRO A 336      58.898 -36.929 -41.181  1.00 41.60           C  
ANISOU 5826  CA  PRO A 336     6610   4396   4799   2132   1534   -192       C  
ATOM   5827  C   PRO A 336      57.735 -36.614 -40.254  1.00 40.87           C  
ANISOU 5827  C   PRO A 336     6453   4289   4788   1898   1264   -142       C  
ATOM   5828  O   PRO A 336      57.736 -37.044 -39.101  1.00 40.77           O  
ANISOU 5828  O   PRO A 336     6297   4242   4953   1873   1160    -85       O  
ATOM   5829  CB  PRO A 336      58.797 -38.364 -41.714  1.00 44.75           C  
ANISOU 5829  CB  PRO A 336     7310   4574   5121   2289   1532   -342       C  
ATOM   5830  CG  PRO A 336      59.769 -39.152 -40.914  1.00 48.05           C  
ANISOU 5830  CG  PRO A 336     7558   4956   5743   2455   1608   -300       C  
ATOM   5831  CD  PRO A 336      60.867 -38.212 -40.538  1.00 47.86           C  
ANISOU 5831  CD  PRO A 336     7191   5152   5841   2489   1781   -156       C  
ATOM   5832  N   SER A 341      49.283 -38.414 -33.938  1.00 39.89           N  
ANISOU 5832  N   SER A 341     6187   3676   5293    644   -302    150       N  
ATOM   5833  CA  SER A 341      50.479 -37.577 -33.930  1.00 39.18           C  
ANISOU 5833  CA  SER A 341     5953   3749   5185    754   -124    168       C  
ATOM   5834  C   SER A 341      50.171 -36.138 -33.521  1.00 33.70           C  
ANISOU 5834  C   SER A 341     5066   3240   4500    638   -111    236       C  
ATOM   5835  O   SER A 341      50.805 -35.580 -32.620  1.00 24.24           O  
ANISOU 5835  O   SER A 341     3670   2169   3372    649    -46    312       O  
ATOM   5836  CB  SER A 341      51.141 -37.592 -35.310  1.00 36.34           C  
ANISOU 5836  CB  SER A 341     5757   3362   4688    893     -6     63       C  
ATOM   5837  OG  SER A 341      52.526 -37.309 -35.218  1.00 35.68           O  
ANISOU 5837  OG  SER A 341     5545   3385   4625   1043    177     87       O  
ATOM   5838  N   MET A 342      49.193 -35.541 -34.191  1.00 25.63           N  
ANISOU 5838  N   MET A 342     2909   3504   3324    446    230  -1007       N  
ATOM   5839  CA  MET A 342      48.883 -34.132 -33.989  1.00 26.12           C  
ANISOU 5839  CA  MET A 342     2922   3702   3299    391    185   -874       C  
ATOM   5840  C   MET A 342      48.327 -33.851 -32.597  1.00 23.99           C  
ANISOU 5840  C   MET A 342     2643   3328   3145    301    170   -749       C  
ATOM   5841  O   MET A 342      48.680 -32.845 -31.985  1.00 21.44           O  
ANISOU 5841  O   MET A 342     2286   3073   2788    292    166   -596       O  
ATOM   5842  CB  MET A 342      47.893 -33.649 -35.046  1.00 26.86           C  
ANISOU 5842  CB  MET A 342     3005   3925   3276    357    114   -985       C  
ATOM   5843  CG  MET A 342      47.935 -32.152 -35.284  1.00 31.69           C  
ANISOU 5843  CG  MET A 342     3576   4713   3750    357     92   -851       C  
ATOM   5844  SD  MET A 342      49.438 -31.634 -36.138  1.00 53.74           S  
ANISOU 5844  SD  MET A 342     6354   7670   6395    481    170   -774       S  
ATOM   5845  CE  MET A 342      49.687 -32.981 -37.289  1.00 37.98           C  
ANISOU 5845  CE  MET A 342     4402   5678   4349    581    193   -999       C  
ATOM   5846  N   MET A 343      47.498 -34.762 -32.102  1.00 21.58           N  
ANISOU 5846  N   MET A 343     2365   2858   2978    236    166   -818       N  
ATOM   5847  CA  MET A 343      46.869 -34.543 -30.782  1.00 20.37           C  
ANISOU 5847  CA  MET A 343     2204   2612   2924    160    164   -699       C  
ATOM   5848  C   MET A 343      47.953 -34.522 -29.701  1.00 18.25           C  
ANISOU 5848  C   MET A 343     1943   2305   2688    225    216   -536       C  
ATOM   5849  O   MET A 343      47.855 -33.748 -28.794  1.00 19.38           O  
ANISOU 5849  O   MET A 343     2062   2481   2819    199    199   -402       O  
ATOM   5850  CB  MET A 343      45.834 -35.627 -30.458  1.00 20.71           C  
ANISOU 5850  CB  MET A 343     2272   2471   3127     80    176   -795       C  
ATOM   5851  CG  MET A 343      45.057 -35.372 -29.177  1.00 19.10           C  
ANISOU 5851  CG  MET A 343     2057   2185   3017      5    188   -666       C  
ATOM   5852  SD  MET A 343      44.239 -33.748 -29.136  1.00 23.54           S  
ANISOU 5852  SD  MET A 343     2554   2927   3463    -59    106   -605       S  
ATOM   5853  CE  MET A 343      43.365 -33.945 -27.589  1.00 23.30           C  
ANISOU 5853  CE  MET A 343     2519   2774   3560   -131    144   -481       C  
ATOM   5854  N   GLY A 344      48.959 -35.369 -29.833  1.00 19.92           N  
ANISOU 5854  N   GLY A 344     2183   2453   2932    322    273   -558       N  
ATOM   5855  CA  GLY A 344      50.026 -35.390 -28.829  1.00 20.15           C  
ANISOU 5855  CA  GLY A 344     2206   2470   2980    407    314   -415       C  
ATOM   5856  C   GLY A 344      50.808 -34.089 -28.873  1.00 23.59           C  
ANISOU 5856  C   GLY A 344     2574   3093   3296    427    284   -318       C  
ATOM   5857  O   GLY A 344      51.185 -33.611 -27.852  1.00 17.32           O  
ANISOU 5857  O   GLY A 344     1751   2321   2507    435    274   -188       O  
ATOM   5858  N   LEU A 345      51.039 -33.572 -30.066  1.00 18.79           N  
ANISOU 5858  N   LEU A 345     1938   2619   2581    435    273   -381       N  
ATOM   5859  CA  LEU A 345      51.800 -32.315 -30.209  1.00 20.59           C  
ANISOU 5859  CA  LEU A 345     2100   3011   2715    441    262   -287       C  
ATOM   5860  C   LEU A 345      51.001 -31.170 -29.580  1.00 18.38           C  
ANISOU 5860  C   LEU A 345     1801   2760   2421    343    205   -206       C  
ATOM   5861  O   LEU A 345      51.567 -30.356 -28.907  1.00 17.90           O  
ANISOU 5861  O   LEU A 345     1696   2748   2357    336    193    -97       O  
ATOM   5862  CB  LEU A 345      52.040 -32.028 -31.694  1.00 20.37           C  
ANISOU 5862  CB  LEU A 345     2055   3116   2568    476    280   -359       C  
ATOM   5863  CG  LEU A 345      53.007 -32.946 -32.439  1.00 25.13           C  
ANISOU 5863  CG  LEU A 345     2663   3737   3150    594    345   -435       C  
ATOM   5864  CD1 LEU A 345      53.073 -32.531 -33.882  1.00 26.17           C  
ANISOU 5864  CD1 LEU A 345     2781   4027   3135    626    362   -493       C  
ATOM   5865  CD2 LEU A 345      54.386 -32.952 -31.824  1.00 23.30           C  
ANISOU 5865  CD2 LEU A 345     2370   3528   2954    670    390   -329       C  
ATOM   5866  N   LEU A 346      49.715 -31.126 -29.871  1.00 15.86           N  
ANISOU 5866  N   LEU A 346     1512   2414   2099    272    167   -272       N  
ATOM   5867  CA  LEU A 346      48.847 -30.037 -29.371  1.00 15.41           C  
ANISOU 5867  CA  LEU A 346     1443   2386   2028    191    116   -207       C  
ATOM   5868  C   LEU A 346      48.662 -30.148 -27.857  1.00 14.07           C  
ANISOU 5868  C   LEU A 346     1281   2123   1942    168    112   -121       C  
ATOM   5869  O   LEU A 346      48.587 -29.159 -27.218  1.00 14.97           O  
ANISOU 5869  O   LEU A 346     1373   2278   2036    136     81    -37       O  
ATOM   5870  CB  LEU A 346      47.502 -30.142 -30.077  1.00 16.02           C  
ANISOU 5870  CB  LEU A 346     1534   2468   2083    134     75   -307       C  
ATOM   5871  CG  LEU A 346      47.516 -29.819 -31.563  1.00 18.95           C  
ANISOU 5871  CG  LEU A 346     1901   2965   2334    168     64   -390       C  
ATOM   5872  CD1 LEU A 346      46.112 -29.917 -32.114  1.00 19.67           C  
ANISOU 5872  CD1 LEU A 346     1994   3074   2405    118      5   -499       C  
ATOM   5873  CD2 LEU A 346      48.091 -28.448 -31.801  1.00 23.62           C  
ANISOU 5873  CD2 LEU A 346     2461   3684   2828    187     72   -277       C  
ATOM   5874  N   THR A 347      48.593 -31.363 -27.357  1.00 13.71           N  
ANISOU 5874  N   THR A 347     1273   1949   1990    190    147   -144       N  
ATOM   5875  CA  THR A 347      48.411 -31.585 -25.912  1.00 14.01           C  
ANISOU 5875  CA  THR A 347     1327   1903   2094    189    158    -49       C  
ATOM   5876  C   THR A 347      49.658 -31.139 -25.156  1.00 16.33           C  
ANISOU 5876  C   THR A 347     1590   2261   2356    259    154     54       C  
ATOM   5877  O   THR A 347      49.520 -30.500 -24.178  1.00 16.51           O  
ANISOU 5877  O   THR A 347     1600   2309   2363    245    125    135       O  
ATOM   5878  CB  THR A 347      48.079 -33.046 -25.631  1.00 15.71           C  
ANISOU 5878  CB  THR A 347     1596   1949   2425    208    216    -81       C  
ATOM   5879  OG1 THR A 347      46.845 -33.349 -26.271  1.00 15.64           O  
ANISOU 5879  OG1 THR A 347     1597   1882   2465    120    209   -189       O  
ATOM   5880  CG2 THR A 347      47.995 -33.302 -24.151  1.00 15.45           C  
ANISOU 5880  CG2 THR A 347     1586   1844   2442    232    243     45       C  
ATOM   5881  N   ASN A 348      50.825 -31.481 -25.676  1.00 15.69           N  
ANISOU 5881  N   ASN A 348     1486   2216   2261    337    181     40       N  
ATOM   5882  CA  ASN A 348      52.098 -31.063 -25.035  1.00 13.93           C  
ANISOU 5882  CA  ASN A 348     1205   2077   2011    402    170    122       C  
ATOM   5883  C   ASN A 348      52.257 -29.535 -25.074  1.00 16.61           C  
ANISOU 5883  C   ASN A 348     1482   2539   2288    339    120    154       C  
ATOM   5884  O   ASN A 348      52.747 -28.956 -24.138  1.00 14.45           O  
ANISOU 5884  O   ASN A 348     1166   2316   2008    347     84    218       O  
ATOM   5885  CB  ASN A 348      53.271 -31.771 -25.715  1.00 14.91           C  
ANISOU 5885  CB  ASN A 348     1302   2227   2136    501    217     93       C  
ATOM   5886  CG  ASN A 348      54.599 -31.337 -25.147  1.00 22.73           C  
ANISOU 5886  CG  ASN A 348     2205   3324   3106    565    200    167       C  
ATOM   5887  OD1 ASN A 348      55.214 -30.433 -25.634  1.00 18.57           O  
ANISOU 5887  OD1 ASN A 348     1601   2918   2538    533    186    173       O  
ATOM   5888  ND2 ASN A 348      54.972 -31.942 -24.048  1.00 28.91           N  
ANISOU 5888  ND2 ASN A 348     2995   4068   3923    657    203    228       N  
ATOM   5889  N   LEU A 349      51.875 -28.926 -26.182  1.00 13.03           N  
ANISOU 5889  N   LEU A 349     1026   2134   1791    281    118    107       N  
ATOM   5890  CA  LEU A 349      51.918 -27.457 -26.336  1.00 12.44           C  
ANISOU 5890  CA  LEU A 349      909   2147   1673    217     85    145       C  
ATOM   5891  C   LEU A 349      51.007 -26.807 -25.278  1.00 12.37           C  
ANISOU 5891  C   LEU A 349      922   2102   1674    159     35    182       C  
ATOM   5892  O   LEU A 349      51.451 -25.936 -24.567  1.00 13.15           O  
ANISOU 5892  O   LEU A 349      983   2241   1773    140      0    229       O  
ATOM   5893  CB  LEU A 349      51.480 -27.135 -27.765  1.00 12.55           C  
ANISOU 5893  CB  LEU A 349      932   2212   1625    189    102    100       C  
ATOM   5894  CG  LEU A 349      51.270 -25.657 -28.059  1.00 16.94           C  
ANISOU 5894  CG  LEU A 349     1467   2831   2140    126     83    150       C  
ATOM   5895  CD1 LEU A 349      52.546 -24.880 -27.885  1.00 18.17           C  
ANISOU 5895  CD1 LEU A 349     1543   3049   2310    123    101    215       C  
ATOM   5896  CD2 LEU A 349      50.752 -25.493 -29.469  1.00 16.43           C  
ANISOU 5896  CD2 LEU A 349     1428   2822   1995    129    101    111       C  
ATOM   5897  N   ALA A 350      49.771 -27.293 -25.189  1.00 11.84           N  
ANISOU 5897  N   ALA A 350      912   1962   1623    133     32    151       N  
ATOM   5898  CA  ALA A 350      48.806 -26.760 -24.204  1.00 11.25           C  
ANISOU 5898  CA  ALA A 350      859   1858   1556     91     -2    184       C  
ATOM   5899  C   ALA A 350      49.300 -26.986 -22.766  1.00 12.21           C  
ANISOU 5899  C   ALA A 350      980   1961   1696    139    -11    245       C  
ATOM   5900  O   ALA A 350      49.145 -26.156 -21.972  1.00 12.44           O  
ANISOU 5900  O   ALA A 350     1005   2016   1705    121    -51    279       O  
ATOM   5901  CB  ALA A 350      47.462 -27.388 -24.448  1.00 11.29           C  
ANISOU 5901  CB  ALA A 350      906   1793   1590     56      9    137       C  
ATOM   5902  N   ASP A 351      49.925 -28.122 -22.528  1.00 12.61           N  
ANISOU 5902  N   ASP A 351     1039   1974   1779    212     24    256       N  
ATOM   5903  CA  ASP A 351      50.484 -28.413 -21.191  1.00 13.65           C  
ANISOU 5903  CA  ASP A 351     1169   2109   1909    285     14    324       C  
ATOM   5904  C   ASP A 351      51.511 -27.336 -20.830  1.00 14.44           C  
ANISOU 5904  C   ASP A 351     1198   2322   1967    289    -47    339       C  
ATOM   5905  O   ASP A 351      51.485 -26.864 -19.747  1.00 13.49           O  
ANISOU 5905  O   ASP A 351     1075   2235   1816    304    -92    371       O  
ATOM   5906  CB  ASP A 351      51.134 -29.799 -21.165  1.00 15.14           C  
ANISOU 5906  CB  ASP A 351     1372   2244   2135    384     65    341       C  
ATOM   5907  CG  ASP A 351      50.204 -30.999 -21.107  1.00 19.99           C  
ANISOU 5907  CG  ASP A 351     2063   2715   2819    384    130    338       C  
ATOM   5908  OD1 ASP A 351      49.017 -30.812 -21.008  1.00 19.52           O  
ANISOU 5908  OD1 ASP A 351     2033   2610   2774    309    133    332       O  
ATOM   5909  OD2 ASP A 351      50.706 -32.096 -21.263  1.00 19.03           O  
ANISOU 5909  OD2 ASP A 351     1967   2518   2747    460    184    341       O  
ATOM   5910  N   ARG A 352      52.365 -26.963 -21.765  1.00 12.19           N  
ANISOU 5910  N   ARG A 352      852   2098   1683    272    -45    311       N  
ATOM   5911  CA  ARG A 352      53.398 -25.956 -21.450  1.00 12.39           C  
ANISOU 5911  CA  ARG A 352      789   2221   1697    258    -95    317       C  
ATOM   5912  C   ARG A 352      52.804 -24.551 -21.408  1.00 12.88           C  
ANISOU 5912  C   ARG A 352      853   2291   1750    160   -135    304       C  
ATOM   5913  O   ARG A 352      53.256 -23.767 -20.640  1.00 13.04           O  
ANISOU 5913  O   ARG A 352      863   2325   1765    135   -184    285       O  
ATOM   5914  CB  ARG A 352      54.514 -26.074 -22.483  1.00 12.97           C  
ANISOU 5914  CB  ARG A 352      785   2356   1788    274    -59    304       C  
ATOM   5915  CG  ARG A 352      55.413 -27.281 -22.253  1.00 13.85           C  
ANISOU 5915  CG  ARG A 352      870   2482   1911    394    -35    319       C  
ATOM   5916  CD  ARG A 352      56.496 -27.442 -23.302  1.00 14.54           C  
ANISOU 5916  CD  ARG A 352      895   2621   2009    416     15    297       C  
ATOM   5917  NE  ARG A 352      55.975 -27.910 -24.567  1.00 14.42           N  
ANISOU 5917  NE  ARG A 352      926   2567   1985    412     82    262       N  
ATOM   5918  CZ  ARG A 352      55.998 -27.239 -25.694  1.00 14.41           C  
ANISOU 5918  CZ  ARG A 352      901   2614   1961    352    114    246       C  
ATOM   5919  NH1 ARG A 352      56.541 -26.049 -25.767  1.00 14.41           N  
ANISOU 5919  NH1 ARG A 352      839   2671   1967    279     97    270       N  
ATOM   5920  NH2 ARG A 352      55.475 -27.774 -26.767  1.00 14.69           N  
ANISOU 5920  NH2 ARG A 352      996   2619   1966    363    162    197       N  
ATOM   5921  N   GLU A 353      51.766 -24.299 -22.191  1.00 14.16           N  
ANISOU 5921  N   GLU A 353     1067   2408   1907    104   -109    291       N  
ATOM   5922  CA  GLU A 353      51.153 -22.955 -22.193  1.00 11.12           C  
ANISOU 5922  CA  GLU A 353      693   2016   1513     30   -139    289       C  
ATOM   5923  C   GLU A 353      50.416 -22.702 -20.875  1.00 13.55           C  
ANISOU 5923  C   GLU A 353     1040   2302   1805     38   -184    293       C  
ATOM   5924  O   GLU A 353      50.408 -21.594 -20.439  1.00 13.93           O  
ANISOU 5924  O   GLU A 353     1099   2342   1851     -2   -221    273       O  
ATOM   5925  CB  GLU A 353      50.117 -22.855 -23.317  1.00 10.74           C  
ANISOU 5925  CB  GLU A 353      691   1941   1448     -6   -106    278       C  
ATOM   5926  CG  GLU A 353      50.699 -22.750 -24.712  1.00 12.05           C  
ANISOU 5926  CG  GLU A 353      825   2151   1604    -14    -62    279       C  
ATOM   5927  CD  GLU A 353      49.591 -22.619 -25.739  1.00 19.07           C  
ANISOU 5927  CD  GLU A 353     1760   3035   2450    -29    -45    263       C  
ATOM   5928  OE1 GLU A 353      49.046 -23.623 -26.131  1.00 13.61           O  
ANISOU 5928  OE1 GLU A 353     1100   2326   1746     -2    -32    217       O  
ATOM   5929  OE2 GLU A 353      49.311 -21.497 -26.082  1.00 17.85           O  
ANISOU 5929  OE2 GLU A 353     1611   2892   2281    -66    -48    294       O  
ATOM   5930  N   LEU A 354      49.874 -23.755 -20.271  1.00 12.57           N  
ANISOU 5930  N   LEU A 354      962   2143   1670     92   -167    309       N  
ATOM   5931  CA  LEU A 354      49.113 -23.572 -19.010  1.00 14.86           C  
ANISOU 5931  CA  LEU A 354     1294   2421   1930    113   -191    325       C  
ATOM   5932  C   LEU A 354      50.017 -23.062 -17.884  1.00 14.02           C  
ANISOU 5932  C   LEU A 354     1152   2382   1792    152   -254    320       C  
ATOM   5933  O   LEU A 354      49.629 -22.227 -17.151  1.00 11.80           O  
ANISOU 5933  O   LEU A 354      899   2107   1479    143   -292    297       O  
ATOM   5934  CB  LEU A 354      48.428 -24.893 -18.657  1.00 13.59           C  
ANISOU 5934  CB  LEU A 354     1184   2204   1777    165   -137    363       C  
ATOM   5935  CG  LEU A 354      47.586 -24.838 -17.380  1.00 15.05           C  
ANISOU 5935  CG  LEU A 354     1413   2384   1923    197   -137    400       C  
ATOM   5936  CD1 LEU A 354      46.413 -23.912 -17.565  1.00 14.00           C  
ANISOU 5936  CD1 LEU A 354     1296   2237   1788    132   -143    373       C  
ATOM   5937  CD2 LEU A 354      47.102 -26.211 -16.979  1.00 15.88           C  
ANISOU 5937  CD2 LEU A 354     1561   2420   2052    249    -63    460       C  
ATOM   5938  N   VAL A 355      51.253 -23.547 -17.861  1.00 15.00           N  
ANISOU 5938  N   VAL A 355     1235   2540   1923    193   -260    315       N  
ATOM   5939  CA  VAL A 355      52.212 -23.070 -16.832  1.00 12.19           C  
ANISOU 5939  CA  VAL A 355      857   2233   1541    220   -321    277       C  
ATOM   5940  C   VAL A 355      52.419 -21.558 -16.978  1.00 12.20           C  
ANISOU 5940  C   VAL A 355      833   2230   1574    129   -367    210       C  
ATOM   5941  O   VAL A 355      52.413 -20.872 -16.015  1.00 14.62           O  
ANISOU 5941  O   VAL A 355     1148   2555   1854    133   -427    168       O  
ATOM   5942  CB  VAL A 355      53.547 -23.824 -16.977  1.00 17.93           C  
ANISOU 5942  CB  VAL A 355     1528   3003   2283    275   -319    281       C  
ATOM   5943  CG1 VAL A 355      54.433 -23.542 -15.791  1.00 20.03           C  
ANISOU 5943  CG1 VAL A 355     1765   3330   2517    312   -392    242       C  
ATOM   5944  CG2 VAL A 355      53.312 -25.309 -17.106  1.00 16.49           C  
ANISOU 5944  CG2 VAL A 355     1373   2802   2091    372   -261    354       C  
ATOM   5945  N   HIS A 356      52.576 -21.091 -18.204  1.00 12.26           N  
ANISOU 5945  N   HIS A 356      812   2211   1637     54   -334    205       N  
ATOM   5946  CA  HIS A 356      52.758 -19.637 -18.421  1.00 12.44           C  
ANISOU 5946  CA  HIS A 356      809   2211   1706    -33   -359    162       C  
ATOM   5947  C   HIS A 356      51.443 -18.884 -18.157  1.00 14.06           C  
ANISOU 5947  C   HIS A 356     1075   2375   1891    -58   -372    160       C  
ATOM   5948  O   HIS A 356      51.477 -17.788 -17.741  1.00 13.94           O  
ANISOU 5948  O   HIS A 356     1047   2348   1902   -103   -419    114       O  
ATOM   5949  CB  HIS A 356      53.217 -19.421 -19.861  1.00 12.47           C  
ANISOU 5949  CB  HIS A 356      773   2202   1764    -94   -300    184       C  
ATOM   5950  CG  HIS A 356      54.622 -19.850 -20.108  1.00 13.26           C  
ANISOU 5950  CG  HIS A 356      793   2349   1897    -78   -288    176       C  
ATOM   5951  ND1 HIS A 356      55.664 -18.989 -19.942  1.00 20.71           N  
ANISOU 5951  ND1 HIS A 356     1652   3307   2909   -131   -315    133       N  
ATOM   5952  CD2 HIS A 356      55.147 -21.007 -20.557  1.00 13.37           C  
ANISOU 5952  CD2 HIS A 356      789   2399   1893    -15   -251    204       C  
ATOM   5953  CE1 HIS A 356      56.768 -19.620 -20.246  1.00 23.30           C  
ANISOU 5953  CE1 HIS A 356     1912   3686   3255    -98   -295    138       C  
ATOM   5954  NE2 HIS A 356      56.500 -20.840 -20.611  1.00 17.00           N  
ANISOU 5954  NE2 HIS A 356     1157   2902   2400    -23   -256    182       N  
ATOM   5955  N   MET A 357      50.316 -19.533 -18.386  1.00 13.57           N  
ANISOU 5955  N   MET A 357     1070   2294   1793    -31   -332    206       N  
ATOM   5956  CA  MET A 357      49.000 -18.895 -18.159  1.00 12.19           C  
ANISOU 5956  CA  MET A 357      945   2090   1598    -43   -340    209       C  
ATOM   5957  C   MET A 357      48.821 -18.582 -16.672  1.00 15.79           C  
ANISOU 5957  C   MET A 357     1419   2575   2004      2   -398    172       C  
ATOM   5958  O   MET A 357      48.262 -17.570 -16.357  1.00 14.52           O  
ANISOU 5958  O   MET A 357     1283   2394   1841    -18   -427    140       O  
ATOM   5959  CB  MET A 357      47.878 -19.823 -18.628  1.00 18.09           C  
ANISOU 5959  CB  MET A 357     1730   2822   2323    -19   -290    256       C  
ATOM   5960  CG  MET A 357      46.552 -19.109 -18.601  1.00 15.87           C  
ANISOU 5960  CG  MET A 357     1497   2502   2029    -33   -283    254       C  
ATOM   5961  SD  MET A 357      45.133 -20.231 -18.814  1.00 11.35           S  
ANISOU 5961  SD  MET A 357      957   1911   1444     -9   -227    284       S  
ATOM   5962  CE  MET A 357      45.538 -20.940 -20.418  1.00 15.23           C  
ANISOU 5962  CE  MET A 357     1421   2399   1966    -42   -193    285       C  
ATOM   5963  N   ILE A 358      49.306 -19.470 -15.817  1.00 12.83           N  
ANISOU 5963  N   ILE A 358     1046   2246   1584     76   -411    177       N  
ATOM   5964  CA  ILE A 358      49.213 -19.229 -14.357  1.00 14.06           C  
ANISOU 5964  CA  ILE A 358     1229   2446   1668    139   -461    144       C  
ATOM   5965  C   ILE A 358      50.043 -17.985 -13.999  1.00 16.90           C  
ANISOU 5965  C   ILE A 358     1548   2819   2055     94   -543     49       C  
ATOM   5966  O   ILE A 358      49.587 -17.178 -13.258  1.00 16.94           O  
ANISOU 5966  O   ILE A 358     1579   2837   2020    107   -591     -9       O  
ATOM   5967  CB  ILE A 358      49.614 -20.509 -13.602  1.00 16.26           C  
ANISOU 5967  CB  ILE A 358     1520   2772   1885    239   -447    188       C  
ATOM   5968  CG1 ILE A 358      48.452 -21.485 -13.411  1.00 24.99           C  
ANISOU 5968  CG1 ILE A 358     2682   3866   2947    298   -376    275       C  
ATOM   5969  CG2 ILE A 358      50.157 -20.149 -12.239  1.00 17.72           C  
ANISOU 5969  CG2 ILE A 358     1709   3023   2001    294   -517    130       C  
ATOM   5970  CD1 ILE A 358      47.609 -21.750 -14.594  1.00 28.83           C  
ANISOU 5970  CD1 ILE A 358     3163   4293   3499    240   -315    321       C  
ATOM   5971  N   ASN A 359      51.201 -17.835 -14.611  1.00 13.24           N  
ANISOU 5971  N   ASN A 359     1014   2350   1666     39   -556     27       N  
ATOM   5972  CA  ASN A 359      52.052 -16.648 -14.365  1.00 14.22           C  
ANISOU 5972  CA  ASN A 359     1080   2474   1850    -29   -628    -60       C  
ATOM   5973  C   ASN A 359      51.344 -15.376 -14.836  1.00 16.71           C  
ANISOU 5973  C   ASN A 359     1401   2728   2222   -115   -632    -95       C  
ATOM   5974  O   ASN A 359      51.401 -14.395 -14.164  1.00 17.39           O  
ANISOU 5974  O   ASN A 359     1483   2801   2325   -148   -695   -190       O  
ATOM   5975  CB  ASN A 359      53.432 -16.816 -15.000  1.00 20.29           C  
ANISOU 5975  CB  ASN A 359     1758   3248   2703    -75   -622    -59       C  
ATOM   5976  CG  ASN A 359      54.305 -15.588 -14.854  1.00 29.44           C  
ANISOU 5976  CG  ASN A 359     2842   4394   3949   -174   -683   -135       C  
ATOM   5977  OD1 ASN A 359      54.263 -14.695 -15.676  1.00 34.91           O  
ANISOU 5977  OD1 ASN A 359     3507   5020   4738   -276   -657   -140       O  
ATOM   5978  ND2 ASN A 359      55.085 -15.536 -13.796  1.00 30.03           N  
ANISOU 5978  ND2 ASN A 359     2884   4539   3989   -147   -755   -193       N  
ATOM   5979  N   TRP A 360      50.688 -15.452 -15.980  1.00 15.08           N  
ANISOU 5979  N   TRP A 360     1214   2472   2042   -148   -556    -18       N  
ATOM   5980  CA  TRP A 360      49.943 -14.309 -16.557  1.00 13.80           C  
ANISOU 5980  CA  TRP A 360     1106   2202   1937   -207   -524    -16       C  
ATOM   5981  C   TRP A 360      48.759 -13.954 -15.663  1.00 17.11           C  
ANISOU 5981  C   TRP A 360     1612   2599   2290   -148   -544    -52       C  
ATOM   5982  O   TRP A 360      48.573 -12.821 -15.381  1.00 17.37           O  
ANISOU 5982  O   TRP A 360     1675   2560   2366   -179   -569   -117       O  
ATOM   5983  CB  TRP A 360      49.459 -14.702 -17.952  1.00 12.97           C  
ANISOU 5983  CB  TRP A 360     1021   2059   1846   -224   -435     84       C  
ATOM   5984  CG  TRP A 360      48.343 -13.836 -18.428  1.00 12.75           C  
ANISOU 5984  CG  TRP A 360     1067   1946   1832   -233   -401    108       C  
ATOM   5985  CD1 TRP A 360      48.436 -12.592 -18.953  1.00 13.96           C  
ANISOU 5985  CD1 TRP A 360     1230   2004   2068   -296   -383    110       C  
ATOM   5986  CD2 TRP A 360      46.943 -14.135 -18.373  1.00 12.05           C  
ANISOU 5986  CD2 TRP A 360     1045   1856   1677   -170   -377    139       C  
ATOM   5987  NE1 TRP A 360      47.198 -12.101 -19.231  1.00 13.96           N  
ANISOU 5987  NE1 TRP A 360     1308   1950   2046   -259   -353    145       N  
ATOM   5988  CE2 TRP A 360      46.266 -13.028 -18.896  1.00 14.93           C  
ANISOU 5988  CE2 TRP A 360     1456   2138   2077   -185   -353    157       C  
ATOM   5989  CE3 TRP A 360      46.206 -15.245 -17.970  1.00 12.99           C  
ANISOU 5989  CE3 TRP A 360     1182   2032   1720   -104   -367    158       C  
ATOM   5990  CZ2 TRP A 360      44.885 -13.000 -19.022  1.00 13.99           C  
ANISOU 5990  CZ2 TRP A 360     1390   2014   1911   -128   -331    185       C  
ATOM   5991  CZ3 TRP A 360      44.843 -15.213 -18.078  1.00 14.45           C  
ANISOU 5991  CZ3 TRP A 360     1413   2203   1873    -68   -338    183       C  
ATOM   5992  CH2 TRP A 360      44.200 -14.099 -18.593  1.00 14.27           C  
ANISOU 5992  CH2 TRP A 360     1425   2119   1877    -76   -326    192       C  
ATOM   5993  N   ALA A 361      48.009 -14.955 -15.222  1.00 13.86           N  
ANISOU 5993  N   ALA A 361     1238   2242   1784    -62   -523     -8       N  
ATOM   5994  CA  ALA A 361      46.810 -14.732 -14.380  1.00 18.77           C  
ANISOU 5994  CA  ALA A 361     1933   2863   2335      6   -522    -24       C  
ATOM   5995  C   ALA A 361      47.179 -13.981 -13.093  1.00 22.27           C  
ANISOU 5995  C   ALA A 361     2384   3336   2741     36   -604   -139       C  
ATOM   5996  O   ALA A 361      46.517 -13.065 -12.719  1.00 15.05           O  
ANISOU 5996  O   ALA A 361     1526   2376   1817     55   -613   -194       O  
ATOM   5997  CB  ALA A 361      46.154 -16.048 -14.069  1.00 11.88           C  
ANISOU 5997  CB  ALA A 361     1081   2050   1381     85   -476     49       C  
ATOM   5998  N   LYS A 362      48.316 -14.331 -12.508  1.00 16.01           N  
ANISOU 5998  N   LYS A 362     1532   2628   1924     49   -670   -186       N  
ATOM   5999  CA  LYS A 362      48.811 -13.640 -11.297  1.00 17.32           C  
ANISOU 5999  CA  LYS A 362     1693   2849   2040     84   -767   -318       C  
ATOM   6000  C   LYS A 362      49.201 -12.179 -11.566  1.00 16.91           C  
ANISOU 6000  C   LYS A 362     1626   2691   2107    -21   -811   -433       C  
ATOM   6001  O   LYS A 362      49.269 -11.460 -10.627  1.00 20.78           O  
ANISOU 6001  O   LYS A 362     2132   3195   2570     -1   -889   -568       O  
ATOM   6002  CB  LYS A 362      49.947 -14.458 -10.682  1.00 18.32           C  
ANISOU 6002  CB  LYS A 362     1777   3059   2125    115   -792   -311       C  
ATOM   6003  CG  LYS A 362      49.541 -15.798 -10.107  1.00 22.36           C  
ANISOU 6003  CG  LYS A 362     2337   3642   2516    236   -741   -215       C  
ATOM   6004  CD  LYS A 362      50.704 -16.615  -9.643  1.00 26.59           C  
ANISOU 6004  CD  LYS A 362     2827   4243   3033    271   -759   -196       C  
ATOM   6005  CE  LYS A 362      51.585 -15.857  -8.678  1.00 34.37           C  
ANISOU 6005  CE  LYS A 362     3777   5290   3992    275   -854   -321       C  
ATOM   6006  NZ  LYS A 362      51.083 -15.898  -7.290  1.00 35.84           N  
ANISOU 6006  NZ  LYS A 362     4029   5554   4034    394   -870   -360       N  
ATOM   6007  N   ARG A 363      49.453 -11.773 -12.799  1.00 16.26           N  
ANISOU 6007  N   ARG A 363     1519   2502   2157   -128   -756   -379       N  
ATOM   6008  CA  ARG A 363      49.791 -10.373 -13.127  1.00 17.15           C  
ANISOU 6008  CA  ARG A 363     1621   2486   2409   -236   -773   -461       C  
ATOM   6009  C   ARG A 363      48.580  -9.582 -13.628  1.00 21.30           C  
ANISOU 6009  C   ARG A 363     2245   2873   2976   -237   -704   -419       C  
ATOM   6010  O   ARG A 363      48.732  -8.419 -13.943  1.00 22.34           O  
ANISOU 6010  O   ARG A 363     2389   2868   3231   -315   -699   -469       O  
ATOM   6011  CB  ARG A 363      50.951 -10.383 -14.107  1.00 20.26           C  
ANISOU 6011  CB  ARG A 363     1912   2853   2932   -352   -750   -424       C  
ATOM   6012  CG  ARG A 363      52.206 -10.958 -13.474  1.00 22.27           C  
ANISOU 6012  CG  ARG A 363     2065   3234   3164   -356   -816   -476       C  
ATOM   6013  CD  ARG A 363      53.339 -10.827 -14.440  1.00 26.10           C  
ANISOU 6013  CD  ARG A 363     2456   3689   3773   -471   -766   -429       C  
ATOM   6014  NE  ARG A 363      53.609  -9.443 -14.783  1.00 32.28           N  
ANISOU 6014  NE  ARG A 363     3227   4325   4713   -596   -756   -493       N  
ATOM   6015  CZ  ARG A 363      54.553  -9.063 -15.630  1.00 34.87           C  
ANISOU 6015  CZ  ARG A 363     3482   4606   5163   -708   -697   -456       C  
ATOM   6016  NH1 ARG A 363      55.320  -9.953 -16.226  1.00 32.40           N  
ANISOU 6016  NH1 ARG A 363     3093   4395   4822   -706   -652   -369       N  
ATOM   6017  NH2 ARG A 363      54.723  -7.789 -15.900  1.00 36.37           N  
ANISOU 6017  NH2 ARG A 363     3678   4641   5500   -817   -673   -503       N  
ATOM   6018  N   VAL A 364      47.428 -10.231 -13.696  1.00 16.56           N  
ANISOU 6018  N   VAL A 364     1706   2304   2282   -150   -647   -326       N  
ATOM   6019  CA  VAL A 364      46.213  -9.480 -14.098  1.00 16.04           C  
ANISOU 6019  CA  VAL A 364     1725   2140   2230   -120   -594   -296       C  
ATOM   6020  C   VAL A 364      45.768  -8.712 -12.861  1.00 18.62           C  
ANISOU 6020  C   VAL A 364     2111   2455   2510    -56   -649   -427       C  
ATOM   6021  O   VAL A 364      45.558  -9.333 -11.867  1.00 18.62           O  
ANISOU 6021  O   VAL A 364     2118   2574   2381     34   -683   -464       O  
ATOM   6022  CB  VAL A 364      45.111 -10.431 -14.579  1.00 16.85           C  
ANISOU 6022  CB  VAL A 364     1854   2300   2250    -48   -525   -174       C  
ATOM   6023  CG1 VAL A 364      43.785  -9.717 -14.748  1.00 15.49           C  
ANISOU 6023  CG1 VAL A 364     1754   2053   2076      6   -485   -158       C  
ATOM   6024  CG2 VAL A 364      45.512 -11.126 -15.855  1.00 16.63           C  
ANISOU 6024  CG2 VAL A 364     1777   2283   2260   -103   -475    -65       C  
ATOM   6025  N   PRO A 365      45.689  -7.376 -12.911  1.00 19.10           N  
ANISOU 6025  N   PRO A 365     2216   2367   2672    -94   -652   -499       N  
ATOM   6026  CA  PRO A 365      45.309  -6.589 -11.755  1.00 21.45           C  
ANISOU 6026  CA  PRO A 365     2577   2640   2934    -30   -707   -651       C  
ATOM   6027  C   PRO A 365      44.059  -7.092 -11.040  1.00 17.75           C  
ANISOU 6027  C   PRO A 365     2165   2273   2306    117   -680   -623       C  
ATOM   6028  O   PRO A 365      43.116  -7.337 -11.671  1.00 23.94           O  
ANISOU 6028  O   PRO A 365     2974   3045   3077    158   -601   -502       O  
ATOM   6029  CB  PRO A 365      45.118  -5.192 -12.336  1.00 25.22           C  
ANISOU 6029  CB  PRO A 365     3111   2908   3563    -82   -669   -669       C  
ATOM   6030  CG  PRO A 365      46.130  -5.166 -13.437  1.00 24.55           C  
ANISOU 6030  CG  PRO A 365     2958   2754   3617   -218   -639   -593       C  
ATOM   6031  CD  PRO A 365      46.022  -6.544 -14.053  1.00 22.79           C  
ANISOU 6031  CD  PRO A 365     2681   2677   3302   -197   -603   -448       C  
ATOM   6032  N   GLY A 366      44.178  -7.314  -9.742  1.00 21.77           N  
ANISOU 6032  N   GLY A 366     2684   2895   2692    198   -744   -733       N  
ATOM   6033  CA  GLY A 366      43.081  -7.765  -8.884  1.00 24.70           C  
ANISOU 6033  CA  GLY A 366     3106   3371   2910    341   -706   -705       C  
ATOM   6034  C   GLY A 366      42.984  -9.269  -8.728  1.00 25.24           C  
ANISOU 6034  C   GLY A 366     3132   3602   2857    393   -678   -592       C  
ATOM   6035  O   GLY A 366      42.318  -9.706  -7.842  1.00 24.24           O  
ANISOU 6035  O   GLY A 366     3036   3589   2587    514   -659   -588       O  
ATOM   6036  N   PHE A 367      43.646 -10.033  -9.585  1.00 23.45           N  
ANISOU 6036  N   PHE A 367     2839   3383   2687    310   -666   -496       N  
ATOM   6037  CA  PHE A 367      43.484 -11.500  -9.524  1.00 19.32           C  
ANISOU 6037  CA  PHE A 367     2285   2976   2078    355   -621   -373       C  
ATOM   6038  C   PHE A 367      44.116 -12.100  -8.274  1.00 20.34           C  
ANISOU 6038  C   PHE A 367     2405   3252   2070    442   -678   -418       C  
ATOM   6039  O   PHE A 367      43.517 -12.906  -7.655  1.00 20.11           O  
ANISOU 6039  O   PHE A 367     2397   3320   1925    541   -624   -338       O  
ATOM   6040  CB  PHE A 367      44.058 -12.184 -10.761  1.00 14.95           C  
ANISOU 6040  CB  PHE A 367     1670   2390   1622    254   -596   -276       C  
ATOM   6041  CG  PHE A 367      43.772 -13.657 -10.844  1.00 15.07           C  
ANISOU 6041  CG  PHE A 367     1663   2484   1580    292   -535   -150       C  
ATOM   6042  CD1 PHE A 367      42.542 -14.119 -11.257  1.00 14.66           C  
ANISOU 6042  CD1 PHE A 367     1627   2418   1524    314   -447    -57       C  
ATOM   6043  CD2 PHE A 367      44.737 -14.585 -10.511  1.00 15.97           C  
ANISOU 6043  CD2 PHE A 367     1735   2679   1654    306   -564   -130       C  
ATOM   6044  CE1 PHE A 367      42.297 -15.472 -11.348  1.00 13.96           C  
ANISOU 6044  CE1 PHE A 367     1517   2377   1409    333   -386     48       C  
ATOM   6045  CE2 PHE A 367      44.490 -15.936 -10.608  1.00 15.95           C  
ANISOU 6045  CE2 PHE A 367     1723   2721   1617    342   -497    -13       C  
ATOM   6046  CZ  PHE A 367      43.264 -16.378 -11.020  1.00 12.94           C  
ANISOU 6046  CZ  PHE A 367     1362   2306   1249    347   -406     72       C  
ATOM   6047  N   VAL A 368      45.283 -11.612  -7.878  1.00 18.43           N  
ANISOU 6047  N   VAL A 368     2127   3034   1840    408   -784   -542       N  
ATOM   6048  CA  VAL A 368      45.930 -12.222  -6.681  1.00 21.35           C  
ANISOU 6048  CA  VAL A 368     2485   3551   2078    499   -832   -574       C  
ATOM   6049  C   VAL A 368      45.375 -11.668  -5.376  1.00 22.52           C  
ANISOU 6049  C   VAL A 368     2702   3757   2098    616   -848   -673       C  
ATOM   6050  O   VAL A 368      45.779 -12.150  -4.359  1.00 26.85           O  
ANISOU 6050  O   VAL A 368     3253   4408   2540    701   -853   -681       O  
ATOM   6051  CB  VAL A 368      47.455 -12.118  -6.713  1.00 27.95           C  
ANISOU 6051  CB  VAL A 368     3245   4384   2991    412   -908   -651       C  
ATOM   6052  CG1 VAL A 368      48.040 -12.764  -7.936  1.00 27.64           C  
ANISOU 6052  CG1 VAL A 368     3135   4300   3065    312   -879   -547       C  
ATOM   6053  CG2 VAL A 368      47.905 -10.697  -6.580  1.00 26.83           C  
ANISOU 6053  CG2 VAL A 368     3100   4159   2935    339   -995   -837       C  
ATOM   6054  N   ASP A 369      44.442 -10.723  -5.430  1.00 21.90           N  
ANISOU 6054  N   ASP A 369     2681   3611   2029    632   -850   -747       N  
ATOM   6055  CA  ASP A 369      43.726 -10.203  -4.248  1.00 22.71           C  
ANISOU 6055  CA  ASP A 369     2856   3770   2002    761   -845   -835       C  
ATOM   6056  C   ASP A 369      42.685 -11.235  -3.835  1.00 22.34           C  
ANISOU 6056  C   ASP A 369     2838   3826   1824    883   -727   -674       C  
ATOM   6057  O   ASP A 369      42.244 -11.205  -2.725  1.00 23.45           O  
ANISOU 6057  O   ASP A 369     3017   4053   1838   1008   -697   -695       O  
ATOM   6058  CB  ASP A 369      43.057  -8.860  -4.536  1.00 27.35           C  
ANISOU 6058  CB  ASP A 369     3504   4216   2673    740   -844   -941       C  
ATOM   6059  CG  ASP A 369      43.999  -7.756  -4.954  1.00 33.90           C  
ANISOU 6059  CG  ASP A 369     4312   4909   3661    610   -941  -1101       C  
ATOM   6060  OD1 ASP A 369      45.112  -7.766  -4.523  1.00 35.49           O  
ANISOU 6060  OD1 ASP A 369     4461   5168   3856    578  -1031  -1197       O  
ATOM   6061  OD2 ASP A 369      43.589  -6.923  -5.728  1.00 36.25           O  
ANISOU 6061  OD2 ASP A 369     4636   5027   4112    533   -901  -1100       O  
ATOM   6062  N   LEU A 370      42.273 -12.097  -4.755  1.00 18.74           N  
ANISOU 6062  N   LEU A 370     2353   3351   1418    840   -651   -508       N  
ATOM   6063  CA  LEU A 370      41.290 -13.139  -4.436  1.00 18.39           C  
ANISOU 6063  CA  LEU A 370     2320   3378   1290    925   -524   -344       C  
ATOM   6064  C   LEU A 370      41.944 -14.255  -3.622  1.00 18.98           C  
ANISOU 6064  C   LEU A 370     2377   3535   1300    975   -491   -265       C  
ATOM   6065  O   LEU A 370      43.151 -14.412  -3.657  1.00 19.66           O  
ANISOU 6065  O   LEU A 370     2427   3625   1416    931   -564   -310       O  
ATOM   6066  CB  LEU A 370      40.759 -13.741  -5.745  1.00 16.79           C  
ANISOU 6066  CB  LEU A 370     2078   3075   1226    824   -435   -203       C  
ATOM   6067  CG  LEU A 370      40.117 -12.753  -6.712  1.00 16.22           C  
ANISOU 6067  CG  LEU A 370     2011   2868   1284    748   -421   -240       C  
ATOM   6068  CD1 LEU A 370      39.812 -13.443  -8.027  1.00 14.80           C  
ANISOU 6068  CD1 LEU A 370     1780   2615   1229    646   -360   -116       C  
ATOM   6069  CD2 LEU A 370      38.847 -12.158  -6.129  1.00 20.41           C  
ANISOU 6069  CD2 LEU A 370     2588   3423   1745    854   -363   -263       C  
ATOM   6070  N   THR A 371      41.110 -15.115  -3.079  1.00 18.67           N  
ANISOU 6070  N   THR A 371     2357   3560   1179   1071   -375   -143       N  
ATOM   6071  CA  THR A 371      41.618 -16.291  -2.358  1.00 20.65           C  
ANISOU 6071  CA  THR A 371     2596   3874   1378   1129   -325    -42       C  
ATOM   6072  C   THR A 371      42.197 -17.279  -3.366  1.00 19.37           C  
ANISOU 6072  C   THR A 371     2390   3646   1325   1028   -310     57       C  
ATOM   6073  O   THR A 371      41.802 -17.291  -4.508  1.00 19.30           O  
ANISOU 6073  O   THR A 371     2359   3554   1420    930   -298     91       O  
ATOM   6074  CB  THR A 371      40.499 -16.951  -1.556  1.00 20.30           C  
ANISOU 6074  CB  THR A 371     2572   3888   1252   1239   -185     88       C  
ATOM   6075  OG1 THR A 371      39.527 -17.498  -2.437  1.00 19.19           O  
ANISOU 6075  OG1 THR A 371     2412   3681   1199   1174    -86    210       O  
ATOM   6076  CG2 THR A 371      39.851 -15.992  -0.588  1.00 21.28           C  
ANISOU 6076  CG2 THR A 371     2737   4079   1270   1349   -191     -7       C  
ATOM   6077  N   LEU A 372      43.075 -18.151  -2.910  1.00 18.68           N  
ANISOU 6077  N   LEU A 372     2289   3598   1210   1062   -313    101       N  
ATOM   6078  CA  LEU A 372      43.640 -19.181  -3.811  1.00 17.75           C  
ANISOU 6078  CA  LEU A 372     2136   3419   1188    989   -290    195       C  
ATOM   6079  C   LEU A 372      42.517 -20.076  -4.325  1.00 17.98           C  
ANISOU 6079  C   LEU A 372     2168   3389   1273    969   -160    347       C  
ATOM   6080  O   LEU A 372      42.523 -20.407  -5.457  1.00 19.78           O  
ANISOU 6080  O   LEU A 372     2365   3535   1614    870   -152    388       O  
ATOM   6081  CB  LEU A 372      44.683 -19.991  -3.044  1.00 20.32           C  
ANISOU 6081  CB  LEU A 372     2456   3810   1457   1064   -300    226       C  
ATOM   6082  CG  LEU A 372      46.052 -19.335  -3.040  1.00 24.27           C  
ANISOU 6082  CG  LEU A 372     2914   4336   1972   1024   -436     94       C  
ATOM   6083  CD1 LEU A 372      47.035 -20.166  -2.236  1.00 29.57           C  
ANISOU 6083  CD1 LEU A 372     3575   5095   2565   1123   -444    128       C  
ATOM   6084  CD2 LEU A 372      46.565 -19.193  -4.458  1.00 29.60           C  
ANISOU 6084  CD2 LEU A 372     3541   4911   2793    881   -471     87       C  
ATOM   6085  N   HIS A 373      41.561 -20.429  -3.492  1.00 19.98           N  
ANISOU 6085  N   HIS A 373     2450   3686   1455   1061    -55    430       N  
ATOM   6086  CA  HIS A 373      40.443 -21.266  -3.958  1.00 19.46           C  
ANISOU 6086  CA  HIS A 373     2374   3562   1459   1033     78    574       C  
ATOM   6087  C   HIS A 373      39.709 -20.555  -5.109  1.00 18.12           C  
ANISOU 6087  C   HIS A 373     2178   3334   1373    932     67    546       C  
ATOM   6088  O   HIS A 373      39.392 -21.193  -6.062  1.00 16.95           O  
ANISOU 6088  O   HIS A 373     1997   3111   1331    849    117    628       O  
ATOM   6089  CB  HIS A 373      39.492 -21.536  -2.789  1.00 24.75           C  
ANISOU 6089  CB  HIS A 373     3065   4290   2050   1144    194    657       C  
ATOM   6090  CG  HIS A 373      38.208 -22.067  -3.283  1.00 29.61           C  
ANISOU 6090  CG  HIS A 373     3652   4842   2755   1093    325    777       C  
ATOM   6091  ND1 HIS A 373      38.069 -23.357  -3.690  1.00 36.70           N  
ANISOU 6091  ND1 HIS A 373     4531   5653   3760   1047    425    911       N  
ATOM   6092  CD2 HIS A 373      37.041 -21.456  -3.536  1.00 30.60           C  
ANISOU 6092  CD2 HIS A 373     3756   4972   2897   1072    371    772       C  
ATOM   6093  CE1 HIS A 373      36.858 -23.535  -4.146  1.00 35.24           C  
ANISOU 6093  CE1 HIS A 373     4307   5419   3662    985    525    977       C  
ATOM   6094  NE2 HIS A 373      36.207 -22.390  -4.056  1.00 35.50           N  
ANISOU 6094  NE2 HIS A 373     4333   5515   3638   1002    495    898       N  
ATOM   6095  N   ASP A 374      39.450 -19.271  -4.957  1.00 18.19           N  
ANISOU 6095  N   ASP A 374     2202   3378   1333    948      2    430       N  
ATOM   6096  CA  ASP A 374      38.703 -18.526  -6.007  1.00 15.80           C  
ANISOU 6096  CA  ASP A 374     1873   3017   1114    866     -8    398       C  
ATOM   6097  C   ASP A 374      39.561 -18.406  -7.278  1.00 14.62           C  
ANISOU 6097  C   ASP A 374     1689   2771   1095    735    -95    338       C  
ATOM   6098  O   ASP A 374      39.023 -18.491  -8.350  1.00 14.81           O  
ANISOU 6098  O   ASP A 374     1674   2710   1242    636    -67    353       O  
ATOM   6099  CB  ASP A 374      38.166 -17.212  -5.441  1.00 16.37           C  
ANISOU 6099  CB  ASP A 374     1978   3127   1114    927    -47    281       C  
ATOM   6100  CG  ASP A 374      36.944 -17.390  -4.557  1.00 21.01           C  
ANISOU 6100  CG  ASP A 374     2580   3794   1607   1036     73    352       C  
ATOM   6101  OD1 ASP A 374      36.389 -18.442  -4.552  1.00 21.13           O  
ANISOU 6101  OD1 ASP A 374     2567   3814   1647   1035    196    499       O  
ATOM   6102  OD2 ASP A 374      36.611 -16.428  -3.899  1.00 23.04           O  
ANISOU 6102  OD2 ASP A 374     2876   4106   1774   1123     53    259       O  
ATOM   6103  N   GLN A 375      40.864 -18.198  -7.118  1.00 16.38           N  
ANISOU 6103  N   GLN A 375     1918   3022   1285    742   -198    271       N  
ATOM   6104  CA  GLN A 375      41.797 -18.137  -8.270  1.00 14.12           C  
ANISOU 6104  CA  GLN A 375     1589   2657   1118    626   -262    233       C  
ATOM   6105  C   GLN A 375      41.730 -19.466  -9.029  1.00 13.46           C  
ANISOU 6105  C   GLN A 375     1475   2520   1120    573   -187    348       C  
ATOM   6106  O   GLN A 375      41.642 -19.470 -10.231  1.00 12.55           O  
ANISOU 6106  O   GLN A 375     1326   2323   1120    469   -183    342       O  
ATOM   6107  CB  GLN A 375      43.235 -17.867  -7.802  1.00 14.69           C  
ANISOU 6107  CB  GLN A 375     1655   2769   1159    634   -367    142       C  
ATOM   6108  CG  GLN A 375      43.458 -16.484  -7.229  1.00 15.49           C  
ANISOU 6108  CG  GLN A 375     1777   2896   1212    654   -460     -8       C  
ATOM   6109  CD  GLN A 375      44.870 -16.281  -6.735  1.00 16.34           C  
ANISOU 6109  CD  GLN A 375     1860   3035   1313    644   -552   -101       C  
ATOM   6110  OE1 GLN A 375      45.804 -16.708  -7.345  1.00 18.60           O  
ANISOU 6110  OE1 GLN A 375     2096   3294   1677    576   -573    -80       O  
ATOM   6111  NE2 GLN A 375      45.014 -15.633  -5.602  1.00 17.68           N  
ANISOU 6111  NE2 GLN A 375     2058   3269   1390    716   -604   -208       N  
ATOM   6112  N   VAL A 376      41.776 -20.569  -8.309  1.00 16.42           N  
ANISOU 6112  N   VAL A 376     1865   2939   1434    653   -126    450       N  
ATOM   6113  CA  VAL A 376      41.722 -21.915  -8.934  1.00 15.08           C  
ANISOU 6113  CA  VAL A 376     1677   2698   1355    611    -45    554       C  
ATOM   6114  C   VAL A 376      40.382 -22.078  -9.653  1.00 15.37           C  
ANISOU 6114  C   VAL A 376     1689   2657   1492    530     44    587       C  
ATOM   6115  O   VAL A 376      40.370 -22.538 -10.731  1.00 15.06           O  
ANISOU 6115  O   VAL A 376     1616   2537   1569    436     59    589       O  
ATOM   6116  CB  VAL A 376      41.940 -23.033  -7.905  1.00 17.72           C  
ANISOU 6116  CB  VAL A 376     2046   3066   1622    717     30    664       C  
ATOM   6117  CG1 VAL A 376      41.725 -24.405  -8.507  1.00 14.96           C  
ANISOU 6117  CG1 VAL A 376     1683   2618   1381    676    122    778       C  
ATOM   6118  CG2 VAL A 376      43.312 -22.941  -7.271  1.00 20.84           C  
ANISOU 6118  CG2 VAL A 376     2451   3519   1949    772    -53    593       C  
ATOM   6119  N   HIS A 377      39.310 -21.686  -9.000  1.00 13.66           N  
ANISOU 6119  N   HIS A 377     1483   2480   1227    573     97    602       N  
ATOM   6120  CA  HIS A 377      37.978 -21.819  -9.627  1.00 13.43           C  
ANISOU 6120  CA  HIS A 377     1409   2400   1292    503    175    626       C  
ATOM   6121  C   HIS A 377      37.925 -21.038 -10.938  1.00 14.28           C  
ANISOU 6121  C   HIS A 377     1480   2460   1487    403    104    534       C  
ATOM   6122  O   HIS A 377      37.398 -21.545 -11.874  1.00 14.46           O  
ANISOU 6122  O   HIS A 377     1453   2427   1614    319    137    544       O  
ATOM   6123  CB  HIS A 377      36.906 -21.268  -8.685  1.00 14.23           C  
ANISOU 6123  CB  HIS A 377     1517   2572   1318    579    239    649       C  
ATOM   6124  CG  HIS A 377      35.547 -21.381  -9.279  1.00 20.22           C  
ANISOU 6124  CG  HIS A 377     2207   3299   2178    510    312    666       C  
ATOM   6125  ND1 HIS A 377      34.903 -22.561  -9.379  1.00 24.71           N  
ANISOU 6125  ND1 HIS A 377     2727   3823   2838    462    429    762       N  
ATOM   6126  CD2 HIS A 377      34.758 -20.466  -9.872  1.00 22.46           C  
ANISOU 6126  CD2 HIS A 377     2452   3588   2494    481    280    596       C  
ATOM   6127  CE1 HIS A 377      33.754 -22.362  -9.985  1.00 25.19           C  
ANISOU 6127  CE1 HIS A 377     2709   3878   2981    400    458    739       C  
ATOM   6128  NE2 HIS A 377      33.648 -21.111 -10.298  1.00 22.70           N  
ANISOU 6128  NE2 HIS A 377     2401   3600   2624    420    368    644       N  
ATOM   6129  N   LEU A 378      38.426 -19.822 -10.922  1.00 11.48           N  
ANISOU 6129  N   LEU A 378     1149   2126   1087    418      9    443       N  
ATOM   6130  CA  LEU A 378      38.366 -18.996 -12.146  1.00 10.73           C  
ANISOU 6130  CA  LEU A 378     1031   1983   1064    341    -46    377       C  
ATOM   6131  C   LEU A 378      39.196 -19.631 -13.252  1.00 15.14           C  
ANISOU 6131  C   LEU A 378     1564   2489   1701    259    -71    378       C  
ATOM   6132  O   LEU A 378      38.731 -19.709 -14.328  1.00 15.56           O  
ANISOU 6132  O   LEU A 378     1581   2509   1824    193    -65    371       O  
ATOM   6133  CB  LEU A 378      38.824 -17.578 -11.839  1.00 12.74           C  
ANISOU 6133  CB  LEU A 378     1323   2244   1273    371   -128    287       C  
ATOM   6134  CG  LEU A 378      37.867 -16.772 -10.976  1.00 14.77           C  
ANISOU 6134  CG  LEU A 378     1609   2542   1462    455   -108    259       C  
ATOM   6135  CD1 LEU A 378      38.438 -15.404 -10.724  1.00 15.47           C  
ANISOU 6135  CD1 LEU A 378     1742   2607   1528    473   -194    150       C  
ATOM   6136  CD2 LEU A 378      36.458 -16.687 -11.557  1.00 13.02           C  
ANISOU 6136  CD2 LEU A 378     1342   2311   1292    442    -47    292       C  
ATOM   6137  N   LEU A 379      40.392 -20.089 -12.932  1.00 10.57           N  
ANISOU 6137  N   LEU A 379     1000   1917   1098    274   -101    383       N  
ATOM   6138  CA  LEU A 379      41.258 -20.687 -13.969  1.00 10.10           C  
ANISOU 6138  CA  LEU A 379      916   1817   1104    213   -118    382       C  
ATOM   6139  C   LEU A 379      40.712 -22.017 -14.463  1.00 12.71           C  
ANISOU 6139  C   LEU A 379     1225   2103   1503    179    -41    437       C  
ATOM   6140  O   LEU A 379      40.766 -22.251 -15.617  1.00 17.05           O  
ANISOU 6140  O   LEU A 379     1747   2613   2117    114    -46    413       O  
ATOM   6141  CB  LEU A 379      42.671 -20.826 -13.414  1.00 17.03           C  
ANISOU 6141  CB  LEU A 379     1801   2728   1940    252   -168    373       C  
ATOM   6142  CG  LEU A 379      43.535 -19.615 -13.704  1.00 22.38           C  
ANISOU 6142  CG  LEU A 379     2468   3415   2620    220   -257    291       C  
ATOM   6143  CD1 LEU A 379      44.721 -19.581 -12.762  1.00 29.63           C  
ANISOU 6143  CD1 LEU A 379     3382   4400   3476    278   -319    264       C  
ATOM   6144  CD2 LEU A 379      43.979 -19.640 -15.158  1.00 21.20           C  
ANISOU 6144  CD2 LEU A 379     2284   3219   2553    136   -261    281       C  
ATOM   6145  N   GLU A 380      40.108 -22.799 -13.584  1.00 12.50           N  
ANISOU 6145  N   GLU A 380     1211   2077   1460    226     35    508       N  
ATOM   6146  CA  GLU A 380      39.496 -24.097 -13.935  1.00 14.09           C  
ANISOU 6146  CA  GLU A 380     1389   2212   1751    183    122    557       C  
ATOM   6147  C   GLU A 380      38.375 -23.863 -14.951  1.00 15.67           C  
ANISOU 6147  C   GLU A 380     1535   2394   2026     98    127    508       C  
ATOM   6148  O   GLU A 380      38.230 -24.595 -15.878  1.00 15.01           O  
ANISOU 6148  O   GLU A 380     1419   2254   2032     29    146    485       O  
ATOM   6149  CB  GLU A 380      38.946 -24.717 -12.657  1.00 19.65           C  
ANISOU 6149  CB  GLU A 380     2115   2921   2429    248    220    658       C  
ATOM   6150  CG  GLU A 380      38.322 -26.050 -12.898  1.00 22.56           C  
ANISOU 6150  CG  GLU A 380     2464   3193   2913    198    326    721       C  
ATOM   6151  CD  GLU A 380      38.015 -26.805 -11.618  1.00 32.17           C  
ANISOU 6151  CD  GLU A 380     3713   4406   4103    274    443    852       C  
ATOM   6152  OE1 GLU A 380      37.582 -26.183 -10.661  1.00 33.39           O  
ANISOU 6152  OE1 GLU A 380     3881   4650   4158    346    459    884       O  
ATOM   6153  OE2 GLU A 380      38.236 -27.986 -11.624  1.00 35.48           O  
ANISOU 6153  OE2 GLU A 380     4148   4730   4602    269    526    928       O  
ATOM   6154  N   SER A 381      37.632 -22.785 -14.728  1.00 11.95           N  
ANISOU 6154  N   SER A 381     1051   1975   1513    114    104    482       N  
ATOM   6155  CA ASER A 381      36.544 -22.425 -15.678  0.62 11.87           C  
ANISOU 6155  CA ASER A 381      980   1974   1556     59    100    440       C  
ATOM   6156  CA BSER A 381      36.542 -22.395 -15.672  0.38 12.21           C  
ANISOU 6156  CA BSER A 381     1023   2017   1600     59    100    441       C  
ATOM   6157  C   SER A 381      36.881 -21.777 -17.069  1.00 13.12           C  
ANISOU 6157  C   SER A 381     1131   2134   1721     20     18    372       C  
ATOM   6158  O   SER A 381      36.394 -22.014 -18.231  1.00 14.56           O  
ANISOU 6158  O   SER A 381     1260   2321   1951    -31      9    333       O  
ATOM   6159  CB ASER A 381      35.479 -21.624 -14.966  0.62 15.84           C  
ANISOU 6159  CB ASER A 381     1474   2537   2008    114    112    446       C  
ATOM   6160  CB BSER A 381      35.515 -21.550 -14.956  0.38 15.14           C  
ANISOU 6160  CB BSER A 381     1385   2448   1920    114    114    448       C  
ATOM   6161  OG ASER A 381      34.542 -21.095 -15.893  0.62 17.64           O  
ANISOU 6161  OG ASER A 381     1632   2789   2281     78    100    408       O  
ATOM   6162  OG BSER A 381      35.157 -22.134 -13.713  0.38 13.99           O  
ANISOU 6162  OG BSER A 381     1248   2317   1751    163    203    521       O  
ATOM   6163  N   ALA A 382      38.025 -21.084 -17.017  1.00 11.08           N  
ANISOU 6163  N   ALA A 382      919   1878   1410     46    -39    358       N  
ATOM   6164  CA  ALA A 382      38.515 -20.249 -18.140  1.00 10.02           C  
ANISOU 6164  CA  ALA A 382      785   1749   1275     22   -100    316       C  
ATOM   6165  C   ALA A 382      39.723 -20.747 -18.939  1.00 11.47           C  
ANISOU 6165  C   ALA A 382      971   1911   1475    -13   -120    302       C  
ATOM   6166  O   ALA A 382      39.941 -20.195 -19.964  1.00 10.96           O  
ANISOU 6166  O   ALA A 382      900   1857   1408    -33   -152    280       O  
ATOM   6167  CB  ALA A 382      38.832 -18.865 -17.632  1.00 11.28           C  
ANISOU 6167  CB  ALA A 382      984   1917   1386     63   -142    304       C  
ATOM   6168  N   TRP A 383      40.469 -21.718 -18.454  1.00  9.47           N  
ANISOU 6168  N   TRP A 383      730   1634   1235     -6    -96    323       N  
ATOM   6169  CA  TRP A 383      41.762 -22.042 -19.113  1.00  9.48           C  
ANISOU 6169  CA  TRP A 383      733   1627   1242    -17   -117    310       C  
ATOM   6170  C   TRP A 383      41.642 -22.372 -20.607  1.00  9.26           C  
ANISOU 6170  C   TRP A 383      679   1597   1241    -60   -118    272       C  
ATOM   6171  O   TRP A 383      42.453 -21.874 -21.327  1.00 10.55           O  
ANISOU 6171  O   TRP A 383      840   1780   1389    -67   -142    261       O  
ATOM   6172  CB  TRP A 383      42.539 -23.095 -18.305  1.00 11.70           C  
ANISOU 6172  CB  TRP A 383     1029   1886   1531     20    -86    346       C  
ATOM   6173  CG  TRP A 383      42.003 -24.478 -18.412  1.00 12.82           C  
ANISOU 6173  CG  TRP A 383     1166   1970   1735      5    -21    361       C  
ATOM   6174  CD1 TRP A 383      41.053 -25.050 -17.630  1.00 19.37           C  
ANISOU 6174  CD1 TRP A 383     2000   2769   2591     12     40    405       C  
ATOM   6175  CD2 TRP A 383      42.324 -25.442 -19.420  1.00 12.22           C  
ANISOU 6175  CD2 TRP A 383     1079   1849   1713    -22     -2    328       C  
ATOM   6176  NE1 TRP A 383      40.780 -26.308 -18.075  1.00 21.28           N  
ANISOU 6176  NE1 TRP A 383     2233   2933   2919    -23     98    401       N  
ATOM   6177  CE2 TRP A 383      41.546 -26.574 -19.172  1.00 17.00           C  
ANISOU 6177  CE2 TRP A 383     1686   2380   2393    -41     67    344       C  
ATOM   6178  CE3 TRP A 383      43.231 -25.468 -20.480  1.00 14.94           C  
ANISOU 6178  CE3 TRP A 383     1413   2208   2054    -31    -29    284       C  
ATOM   6179  CZ2 TRP A 383      41.626 -27.709 -19.965  1.00 17.09           C  
ANISOU 6179  CZ2 TRP A 383     1694   2318   2482    -71    100    299       C  
ATOM   6180  CZ3 TRP A 383      43.309 -26.587 -21.260  1.00 15.50           C  
ANISOU 6180  CZ3 TRP A 383     1483   2227   2181    -45      4    243       C  
ATOM   6181  CH2 TRP A 383      42.519 -27.690 -21.009  1.00 15.18           C  
ANISOU 6181  CH2 TRP A 383     1449   2098   2219    -67     63    242       C  
ATOM   6182  N   LEU A 384      40.658 -23.154 -21.024  1.00  8.57           N  
ANISOU 6182  N   LEU A 384      568   1494   1194    -88    -90    247       N  
ATOM   6183  CA  LEU A 384      40.609 -23.526 -22.451  1.00  8.74           C  
ANISOU 6183  CA  LEU A 384      565   1529   1225   -118   -102    189       C  
ATOM   6184  C   LEU A 384      40.101 -22.365 -23.301  1.00 10.34           C  
ANISOU 6184  C   LEU A 384      754   1799   1376   -114   -146    174       C  
ATOM   6185  O   LEU A 384      40.577 -22.203 -24.377  1.00 14.32           O  
ANISOU 6185  O   LEU A 384     1256   2339   1844   -111   -164    151       O  
ATOM   6186  CB  LEU A 384      39.774 -24.788 -22.618  1.00  9.67           C  
ANISOU 6186  CB  LEU A 384      653   1606   1415   -158    -68    143       C  
ATOM   6187  CG  LEU A 384      39.729 -25.282 -24.054  1.00 16.94           C  
ANISOU 6187  CG  LEU A 384     1551   2546   2340   -184    -90     51       C  
ATOM   6188  CD1 LEU A 384      41.126 -25.704 -24.487  1.00 13.29           C  
ANISOU 6188  CD1 LEU A 384     1122   2068   1859   -156    -81     48       C  
ATOM   6189  CD2 LEU A 384      38.782 -26.457 -24.138  1.00 10.65           C  
ANISOU 6189  CD2 LEU A 384      713   1696   1638   -242    -64    -17       C  
ATOM   6190  N   GLU A 385      39.257 -21.521 -22.714  1.00  9.47           N  
ANISOU 6190  N   GLU A 385      637   1708   1254   -101   -156    195       N  
ATOM   6191  CA  GLU A 385      38.814 -20.310 -23.440  1.00  9.34           C  
ANISOU 6191  CA  GLU A 385      620   1741   1186    -74   -193    204       C  
ATOM   6192  C   GLU A 385      40.043 -19.418 -23.636  1.00  9.11           C  
ANISOU 6192  C   GLU A 385      633   1699   1128    -61   -202    241       C  
ATOM   6193  O   GLU A 385      40.161 -18.826 -24.680  1.00 11.32           O  
ANISOU 6193  O   GLU A 385      917   2015   1369    -46   -213    254       O  
ATOM   6194  CB  GLU A 385      37.827 -19.520 -22.590  1.00  9.40           C  
ANISOU 6194  CB  GLU A 385      624   1756   1190    -44   -194    227       C  
ATOM   6195  CG  GLU A 385      36.456 -20.124 -22.481  1.00 14.17           C  
ANISOU 6195  CG  GLU A 385     1165   2388   1830    -57   -178    200       C  
ATOM   6196  CD  GLU A 385      35.578 -19.250 -21.599  1.00 32.70           C  
ANISOU 6196  CD  GLU A 385     3507   4750   4165    -10   -169    230       C  
ATOM   6197  OE1 GLU A 385      34.855 -18.396 -22.149  1.00 18.11           O  
ANISOU 6197  OE1 GLU A 385     1651   2944   2288     31   -197    226       O  
ATOM   6198  OE2 GLU A 385      35.621 -19.426 -20.365  1.00 34.16           O  
ANISOU 6198  OE2 GLU A 385     3712   4904   4363     -1   -129    257       O  
ATOM   6199  N   ILE A 386      40.922 -19.328 -22.640  1.00  8.82           N  
ANISOU 6199  N   ILE A 386      621   1620   1111    -64   -193    262       N  
ATOM   6200  CA  ILE A 386      42.139 -18.482 -22.732  1.00  8.81           C  
ANISOU 6200  CA  ILE A 386      640   1601   1108    -69   -202    286       C  
ATOM   6201  C   ILE A 386      43.099 -19.059 -23.774  1.00  9.08           C  
ANISOU 6201  C   ILE A 386      657   1658   1137    -85   -186    285       C  
ATOM   6202  O   ILE A 386      43.605 -18.325 -24.547  1.00 11.25           O  
ANISOU 6202  O   ILE A 386      935   1942   1400    -89   -179    315       O  
ATOM   6203  CB  ILE A 386      42.777 -18.331 -21.345  1.00 12.75           C  
ANISOU 6203  CB  ILE A 386     1153   2070   1624    -66   -213    285       C  
ATOM   6204  CG1 ILE A 386      41.839 -17.550 -20.432  1.00 16.71           C  
ANISOU 6204  CG1 ILE A 386     1679   2558   2113    -36   -225    281       C  
ATOM   6205  CG2 ILE A 386      44.116 -17.622 -21.461  1.00 14.85           C  
ANISOU 6205  CG2 ILE A 386     1412   2321   1910    -91   -226    292       C  
ATOM   6206  CD1 ILE A 386      41.659 -16.165 -20.846  1.00 25.43           C  
ANISOU 6206  CD1 ILE A 386     2807   3636   3219    -29   -239    290       C  
ATOM   6207  N   LEU A 387      43.241 -20.364 -23.819  1.00 10.71           N  
ANISOU 6207  N   LEU A 387      847   1866   1356    -88   -170    255       N  
ATOM   6208  CA  LEU A 387      44.076 -20.954 -24.891  1.00  9.93           C  
ANISOU 6208  CA  LEU A 387      733   1795   1245    -88   -150    239       C  
ATOM   6209  C   LEU A 387      43.447 -20.659 -26.259  1.00  9.62           C  
ANISOU 6209  C   LEU A 387      691   1813   1150    -76   -154    225       C  
ATOM   6210  O   LEU A 387      44.139 -20.402 -27.155  1.00 11.41           O  
ANISOU 6210  O   LEU A 387      915   2081   1340    -63   -135    244       O  
ATOM   6211  CB  LEU A 387      44.207 -22.463 -24.692  1.00 11.88           C  
ANISOU 6211  CB  LEU A 387      973   2015   1524    -83   -129    199       C  
ATOM   6212  CG  LEU A 387      45.087 -22.888 -23.517  1.00 12.48           C  
ANISOU 6212  CG  LEU A 387     1052   2055   1635    -66   -119    225       C  
ATOM   6213  CD1 LEU A 387      45.160 -24.393 -23.494  1.00 13.94           C  
ANISOU 6213  CD1 LEU A 387     1242   2196   1859    -49    -84    197       C  
ATOM   6214  CD2 LEU A 387      46.482 -22.270 -23.600  1.00 13.54           C  
ANISOU 6214  CD2 LEU A 387     1162   2220   1762    -61   -124    251       C  
ATOM   6215  N   MET A 388      42.135 -20.753 -26.350  1.00  9.89           N  
ANISOU 6215  N   MET A 388      719   1864   1173    -73   -177    195       N  
ATOM   6216  CA  MET A 388      41.452 -20.556 -27.649  1.00 10.26           C  
ANISOU 6216  CA  MET A 388      755   1992   1153    -46   -197    171       C  
ATOM   6217  C   MET A 388      41.513 -19.101 -28.108  1.00 10.47           C  
ANISOU 6217  C   MET A 388      804   2048   1126     -9   -197    250       C  
ATOM   6218  O   MET A 388      41.830 -18.874 -29.254  1.00 12.66           O  
ANISOU 6218  O   MET A 388     1087   2393   1331     27   -186    268       O  
ATOM   6219  CB  MET A 388      40.012 -21.038 -27.544  1.00 10.50           C  
ANISOU 6219  CB  MET A 388      749   2044   1196    -54   -229    109       C  
ATOM   6220  CG  MET A 388      39.914 -22.520 -27.553  1.00 10.79           C  
ANISOU 6220  CG  MET A 388      760   2052   1287    -93   -221     18       C  
ATOM   6221  SD  MET A 388      38.174 -23.049 -27.364  1.00 12.46           S  
ANISOU 6221  SD  MET A 388      906   2279   1550   -128   -249    -54       S  
ATOM   6222  CE  MET A 388      38.322 -24.760 -27.879  1.00 12.08           C  
ANISOU 6222  CE  MET A 388      836   2183   1572   -180   -236   -178       C  
ATOM   6223  N   ILE A 389      41.279 -18.140 -27.224  1.00 11.95           N  
ANISOU 6223  N   ILE A 389     1011   2183   1347    -10   -201    299       N  
ATOM   6224  CA  ILE A 389      41.395 -16.728 -27.672  1.00 10.89           C  
ANISOU 6224  CA  ILE A 389      908   2046   1184     24   -189    380       C  
ATOM   6225  C   ILE A 389      42.843 -16.423 -28.084  1.00 12.18           C  
ANISOU 6225  C   ILE A 389     1083   2183   1360      1   -142    433       C  
ATOM   6226  O   ILE A 389      43.014 -15.717 -29.013  1.00 13.84           O  
ANISOU 6226  O   ILE A 389     1313   2416   1529     33   -109    506       O  
ATOM   6227  CB  ILE A 389      40.804 -15.717 -26.683  1.00 12.16           C  
ANISOU 6227  CB  ILE A 389     1095   2138   1389     32   -201    407       C  
ATOM   6228  CG1 ILE A 389      40.521 -14.390 -27.390  1.00 11.46           C  
ANISOU 6228  CG1 ILE A 389     1043   2042   1269     88   -187    489       C  
ATOM   6229  CG2 ILE A 389      41.680 -15.553 -25.454  1.00 12.40           C  
ANISOU 6229  CG2 ILE A 389     1137   2082   1492    -18   -193    399       C  
ATOM   6230  CD1 ILE A 389      39.988 -13.354 -26.493  1.00 11.54           C  
ANISOU 6230  CD1 ILE A 389     1089   1968   1328    107   -192    510       C  
ATOM   6231  N   GLY A 390      43.823 -17.001 -27.410  1.00 11.90           N  
ANISOU 6231  N   GLY A 390     1029   2111   1380    -47   -132    405       N  
ATOM   6232  CA  GLY A 390      45.221 -16.822 -27.821  1.00 14.46           C  
ANISOU 6232  CA  GLY A 390     1337   2431   1726    -72    -87    444       C  
ATOM   6233  C   GLY A 390      45.448 -17.395 -29.194  1.00 11.53           C  
ANISOU 6233  C   GLY A 390      957   2150   1276    -34    -53    450       C  
ATOM   6234  O   GLY A 390      46.084 -16.730 -29.978  1.00 13.81           O  
ANISOU 6234  O   GLY A 390     1247   2460   1539    -22      1    526       O  
ATOM   6235  N   LEU A 391      44.928 -18.579 -29.452  1.00 11.65           N  
ANISOU 6235  N   LEU A 391      961   2213   1251    -13    -78    368       N  
ATOM   6236  CA  LEU A 391      45.091 -19.221 -30.772  1.00 11.82           C  
ANISOU 6236  CA  LEU A 391      977   2330   1184     34    -57    339       C  
ATOM   6237  C   LEU A 391      44.447 -18.367 -31.870  1.00 12.59           C  
ANISOU 6237  C   LEU A 391     1097   2507   1177     96    -54    394       C  
ATOM   6238  O   LEU A 391      45.043 -18.168 -32.885  1.00 14.10           O  
ANISOU 6238  O   LEU A 391     1294   2773   1289    142     -4    440       O  
ATOM   6239  CB  LEU A 391      44.444 -20.597 -30.695  1.00 11.70           C  
ANISOU 6239  CB  LEU A 391      950   2327   1169     34    -96    217       C  
ATOM   6240  CG  LEU A 391      44.349 -21.335 -32.022  1.00 12.57           C  
ANISOU 6240  CG  LEU A 391     1057   2538   1181     87    -96    143       C  
ATOM   6241  CD1 LEU A 391      45.752 -21.539 -32.575  1.00 13.03           C  
ANISOU 6241  CD1 LEU A 391     1111   2629   1212    113    -29    169       C  
ATOM   6242  CD2 LEU A 391      43.687 -22.667 -31.829  1.00 12.62           C  
ANISOU 6242  CD2 LEU A 391     1049   2522   1225     65   -137      8       C  
ATOM   6243  N   VAL A 392      43.275 -17.842 -31.582  1.00 11.69           N  
ANISOU 6243  N   VAL A 392      996   2388   1057    111   -102    396       N  
ATOM   6244  CA  VAL A 392      42.550 -17.044 -32.591  1.00 12.54           C  
ANISOU 6244  CA  VAL A 392     1126   2579   1061    191   -108    454       C  
ATOM   6245  C   VAL A 392      43.334 -15.769 -32.866  1.00 13.10           C  
ANISOU 6245  C   VAL A 392     1232   2608   1136    205    -33    603       C  
ATOM   6246  O   VAL A 392      43.448 -15.418 -33.990  1.00 17.55           O  
ANISOU 6246  O   VAL A 392     1817   3257   1595    280      8    678       O  
ATOM   6247  CB  VAL A 392      41.112 -16.784 -32.114  1.00 14.29           C  
ANISOU 6247  CB  VAL A 392     1339   2798   1290    210   -174    429       C  
ATOM   6248  CG1 VAL A 392      40.454 -15.750 -32.977  1.00 21.19           C  
ANISOU 6248  CG1 VAL A 392     2240   3741   2068    307   -175    520       C  
ATOM   6249  CG2 VAL A 392      40.306 -18.059 -32.134  1.00 16.45           C  
ANISOU 6249  CG2 VAL A 392     1563   3133   1553    197   -238    286       C  
ATOM   6250  N   TRP A 393      43.863 -15.142 -31.828  1.00 14.12           N  
ANISOU 6250  N   TRP A 393     1368   2608   1390    134    -11    642       N  
ATOM   6251  CA  TRP A 393      44.649 -13.892 -31.945  1.00 14.34           C  
ANISOU 6251  CA  TRP A 393     1422   2560   1468    119     65    769       C  
ATOM   6252  C   TRP A 393      45.896 -14.132 -32.791  1.00 15.14           C  
ANISOU 6252  C   TRP A 393     1501   2711   1540    115    150    826       C  
ATOM   6253  O   TRP A 393      46.138 -13.368 -33.679  1.00 18.67           O  
ANISOU 6253  O   TRP A 393     1975   3175   1944    158    226    951       O  
ATOM   6254  CB  TRP A 393      45.010 -13.356 -30.552  1.00 13.77           C  
ANISOU 6254  CB  TRP A 393     1346   2343   1543     30     54    754       C  
ATOM   6255  CG  TRP A 393      45.991 -12.224 -30.582  1.00 15.69           C  
ANISOU 6255  CG  TRP A 393     1598   2488   1875    -18    132    857       C  
ATOM   6256  CD1 TRP A 393      47.308 -12.261 -30.242  1.00 18.50           C  
ANISOU 6256  CD1 TRP A 393     1903   2801   2326   -105    170    854       C  
ATOM   6257  CD2 TRP A 393      45.746 -10.887 -31.031  1.00 18.95           C  
ANISOU 6257  CD2 TRP A 393     2067   2829   2304     15    188    980       C  
ATOM   6258  NE1 TRP A 393      47.890 -11.050 -30.453  1.00 20.44           N  
ANISOU 6258  NE1 TRP A 393     2160   2948   2659   -145    247    958       N  
ATOM   6259  CE2 TRP A 393      46.959 -10.190 -30.936  1.00 20.83           C  
ANISOU 6259  CE2 TRP A 393     2285   2965   2665    -71    265   1043       C  
ATOM   6260  CE3 TRP A 393      44.625 -10.215 -31.484  1.00 20.95           C  
ANISOU 6260  CE3 TRP A 393     2382   3093   2487    115    182   1045       C  
ATOM   6261  CZ2 TRP A 393      47.073  -8.853 -31.287  1.00 23.67           C  
ANISOU 6261  CZ2 TRP A 393     2693   3209   3092    -72    348   1174       C  
ATOM   6262  CZ3 TRP A 393      44.747  -8.912 -31.888  1.00 21.83           C  
ANISOU 6262  CZ3 TRP A 393     2549   3098   2649    136    261   1184       C  
ATOM   6263  CH2 TRP A 393      45.950  -8.242 -31.765  1.00 23.54           C  
ANISOU 6263  CH2 TRP A 393     2753   3190   3000     38    348   1249       C  
ATOM   6264  N   ARG A 394      46.608 -15.225 -32.565  1.00 14.40           N  
ANISOU 6264  N   ARG A 394     1359   2644   1467     75    147    745       N  
ATOM   6265  CA  ARG A 394      47.840 -15.469 -33.348  1.00 18.67           C  
ANISOU 6265  CA  ARG A 394     1867   3241   1984     79    235    796       C  
ATOM   6266  C   ARG A 394      47.539 -16.001 -34.761  1.00 18.81           C  
ANISOU 6266  C   ARG A 394     1901   3415   1832    183    252    783       C  
ATOM   6267  O   ARG A 394      48.422 -15.990 -35.576  1.00 20.34           O  
ANISOU 6267  O   ARG A 394     2074   3680   1974    213    336    834       O  
ATOM   6268  CB  ARG A 394      48.875 -16.184 -32.483  1.00 25.06           C  
ANISOU 6268  CB  ARG A 394     2613   4022   2886     11    231    722       C  
ATOM   6269  CG  ARG A 394      48.633 -17.661 -32.291  1.00 23.68           C  
ANISOU 6269  CG  ARG A 394     2429   3889   2679     33    166    586       C  
ATOM   6270  CD  ARG A 394      49.652 -18.163 -31.279  1.00 20.27           C  
ANISOU 6270  CD  ARG A 394     1940   3411   2349    -21    163    540       C  
ATOM   6271  NE  ARG A 394      49.277 -19.520 -30.995  1.00 15.80           N  
ANISOU 6271  NE  ARG A 394     1378   2851   1775      1    112    427       N  
ATOM   6272  CZ  ARG A 394      48.714 -19.903 -29.872  1.00 12.02           C  
ANISOU 6272  CZ  ARG A 394      908   2300   1357    -29     49    376       C  
ATOM   6273  NH1 ARG A 394      48.498 -19.024 -28.927  1.00 15.68           N  
ANISOU 6273  NH1 ARG A 394     1381   2697   1881    -74     20    412       N  
ATOM   6274  NH2 ARG A 394      48.361 -21.148 -29.728  1.00 15.34           N  
ANISOU 6274  NH2 ARG A 394     1335   2712   1780     -9     24    291       N  
ATOM   6275  N   SER A 395      46.311 -16.396 -35.032  1.00 15.79           N  
ANISOU 6275  N   SER A 395     1546   3094   1359    243    171    711       N  
ATOM   6276  CA  SER A 395      45.911 -16.897 -36.362  1.00 33.57           C  
ANISOU 6276  CA  SER A 395     3811   5508   3435    350    166    677       C  
ATOM   6277  C   SER A 395      45.259 -15.790 -37.208  1.00 27.39           C  
ANISOU 6277  C   SER A 395     3075   4785   2546    448    185    789       C  
ATOM   6278  O   SER A 395      44.935 -16.074 -38.334  1.00 20.82           O  
ANISOU 6278  O   SER A 395     2253   4066   1593    543    172    744       O  
ATOM   6279  CB  SER A 395      44.990 -18.082 -36.231  1.00 20.83           C  
ANISOU 6279  CB  SER A 395     2183   3939   1794    356     58    498       C  
ATOM   6280  OG  SER A 395      45.548 -19.120 -35.466  1.00 16.07           O  
ANISOU 6280  OG  SER A 395     1548   3266   1292    284     50    397       O  
ATOM   6281  N   MET A 396      45.124 -14.584 -36.692  1.00 20.02           N  
ANISO