CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  VIRAL PROTEIN 20-AUG-20 7JVB  ***

elNémo ID: 210623041704144478

Job options:

ID        	=	 210623041704144478
JOBID     	=	 VIRAL PROTEIN 20-AUG-20 7JVB
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    VIRAL PROTEIN                           20-AUG-20   7JVB              
TITLE     CRYSTAL STRUCTURE OF THE SARS-COV-2 SPIKE RECEPTOR-BINDING DOMAIN     
TITLE    2 (RBD) WITH NANOBODY NB20                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPIKE PROTEIN S1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN,SPIKE GLYCOPROTEIN;      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NANOBODY NB20;                                             
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2, COVID-19 VIRUS;              
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: S, 2;                                                          
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  11 ORGANISM_TAXID: 9844;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    SARS-COV-2, COVID-19, NANOBODY, SPIKE PROTEIN, RECEPTOR-BINDING       
KEYWDS   2 DOMAIN, VIRAL PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XIANG,Z.XIAO,H.LIU,Z.SANG,D.SCHNEIDMAN-DUHOVNY,C.ZHANG,Y.SHI        
REVDAT   3   27-JAN-21 7JVB    1       COMPND                                   
REVDAT   2   30-DEC-20 7JVB    1       JRNL                                     
REVDAT   1   02-DEC-20 7JVB    0                                                
JRNL        AUTH   Y.XIANG,S.NAMBULLI,Z.XIAO,H.LIU,Z.SANG,W.P.DUPREX,           
JRNL        AUTH 2 D.SCHNEIDMAN-DUHOVNY,C.ZHANG,Y.SHI                           
JRNL        TITL   VERSATILE AND MULTIVALENT NANOBODIES EFFICIENTLY NEUTRALIZE  
JRNL        TITL 2 SARS-COV-2.                                                  
JRNL        REF    SCIENCE                       V. 370  1479 2020              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   33154108                                                     
JRNL        DOI    10.1126/SCIENCE.ABE4747                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17335                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.283                           
REMARK   3   R VALUE            (WORKING SET) : 0.281                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 870                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.9590 -  5.9677    0.99     3050   162  0.2730 0.3254        
REMARK   3     2  5.9677 -  4.7394    1.00     2843   151  0.2727 0.3203        
REMARK   3     3  4.7394 -  4.1411    0.99     2782   146  0.2539 0.2951        
REMARK   3     4  4.1411 -  3.7628    0.99     2763   146  0.2968 0.3120        
REMARK   3     5  3.7628 -  3.4933    0.98     2714   143  0.3187 0.3378        
REMARK   3     6  3.4933 -  3.2875    0.84     2313   122  0.3487 0.3703        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 98.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           4865                                  
REMARK   3   ANGLE     :  1.663           6617                                  
REMARK   3   CHIRALITY :  0.054            713                                  
REMARK   3   PLANARITY :  0.004            861                                  
REMARK   3   DIHEDRAL  : 16.092           1716                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1778 -15.3348 -27.1171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8428 T22:   1.0227                                     
REMARK   3      T33:   0.4437 T12:  -0.3202                                     
REMARK   3      T13:   0.1095 T23:  -0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3738 L22:   0.5598                                     
REMARK   3      L33:   1.2292 L12:  -0.5500                                     
REMARK   3      L13:  -0.2263 L23:   0.4366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0208 S12:   0.2411 S13:  -0.1372                       
REMARK   3      S21:   0.1075 S22:  -0.1789 S23:   0.1076                       
REMARK   3      S31:  -0.0376 S32:  -0.1693 S33:   0.1663                       
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 7JVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000251427.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17442                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.287                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.15600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59100                            
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: 6WAQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 6.5, 1 M     
REMARK 280  SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      217.51850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.35800            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.35800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      108.75925            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.35800            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.35800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      326.27775            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.35800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.35800            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      108.75925            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.35800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.35800            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      326.27775            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      217.51850            
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 APPLY THE FOLLOWING TO CHAINS: A, 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     VAL A   320                                                      
REMARK 465     GLN A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ILE A   326                                                      
REMARK 465     VAL A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     PHE A   329                                                      
REMARK 465     PRO A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     LYS A   528                                                      
REMARK 465     LYS A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     THR A   531                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     LEU A   533                                                      
REMARK 465     VAL A   534                                                      
REMARK 465     LYS A   535                                                      
REMARK 465     ASN A   536                                                      
REMARK 465     LYS A   537                                                      
REMARK 465     CYS A   538                                                      
REMARK 465     VAL A   539                                                      
REMARK 465     ASN A   540                                                      
REMARK 465     PHE A   541                                                      
REMARK 465     GLY B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     VAL B   320                                                      
REMARK 465     GLN B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     THR B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     ILE B   326                                                      
REMARK 465     VAL B   327                                                      
REMARK 465     ARG B   328                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     PRO B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ILE B   332                                                      
REMARK 465     THR B   333                                                      
REMARK 465     PRO B   527                                                      
REMARK 465     LYS B   528                                                      
REMARK 465     LYS B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     THR B   531                                                      
REMARK 465     ASN B   532                                                      
REMARK 465     LEU B   533                                                      
REMARK 465     VAL B   534                                                      
REMARK 465     LYS B   535                                                      
REMARK 465     ASN B   536                                                      
REMARK 465     LYS B   537                                                      
REMARK 465     CYS B   538                                                      
REMARK 465     VAL B   539                                                      
REMARK 465     ASN B   540                                                      
REMARK 465     PHE B   541                                                      
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 A 364    CG   OD1  OD2                                       
REMARK 470     TYR A 369    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 406    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 473    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 518    CG   CD1  CD2                                       
REMARK 470     GLN C   1    CG   CD   OE1  NE2                                  
REMARK 470     GLN C  13    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  41    CG   CD   CE   NZ                                   
REMARK 470     GLU C 103    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 106    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 364    CG   OD1  OD2                                       
REMARK 470     TYR B 369    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 473    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B 518    CG   CD1  CD2                                       
REMARK 470     GLN D  13    CG   CD   OE1  NE2                                  
REMARK 470     ARG D  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  41    CG   CD   CE   NZ                                   
REMARK 470     GLU D  42    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  44    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 103    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   CYS A   480     SG   CYS A   488              1.99            
REMARK 500   CB   CYS B   480     SG   CYS B   488              2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 496   N   -  CA  -  C   ANGL. DEV. = -20.5 DEGREES          
REMARK 500    GLY D 108   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 422      -70.45   -112.86                                   
REMARK 500    LEU A 518     -169.57   -101.82                                   
REMARK 500    THR A 523      -44.50   -141.54                                   
REMARK 500    GLU C  42      164.41     66.75                                   
REMARK 500    VAL C  46      -62.70   -125.48                                   
REMARK 500    PRO C  86      -19.69    -47.88                                   
REMARK 500    TRP C 107     -169.54   -124.77                                   
REMARK 500    PRO B 337      109.29    -59.32                                   
REMARK 500    GLU B 484      138.84    -38.83                                   
REMARK 500    LEU B 518     -168.39   -100.42                                   
REMARK 500    THR B 523      -44.89   -140.89                                   
REMARK 500    SER D  25      -70.96    -77.45                                   
REMARK 500    ARG D  43      118.70    -31.91                                   
REMARK 500    VAL D  46      -63.94   -125.95                                   
REMARK 500    PRO D  86      -19.18    -47.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7JVB A  319   541  UNP    P0DTC2   SPIKE_SARS2    319    541             
DBREF  7JVB C    1   117  PDB    7JVB     7JVB             1    117             
DBREF  7JVB B  319   541  UNP    P0DTC2   SPIKE_SARS2    319    541             
DBREF  7JVB D    1   117  PDB    7JVB     7JVB             1    117             
SEQADV 7JVB GLY A  318  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7JVB GLY B  318  UNP  P0DTC2              EXPRESSION TAG                 
SEQRES   1 A  224  GLY ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO          
SEQRES   2 A  224  ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN          
SEQRES   3 A  224  ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS          
SEQRES   4 A  224  ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR          
SEQRES   5 A  224  ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL          
SEQRES   6 A  224  SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL          
SEQRES   7 A  224  TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG          
SEQRES   8 A  224  GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR          
SEQRES   9 A  224  ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE          
SEQRES  10 A  224  ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY          
SEQRES  11 A  224  ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN          
SEQRES  12 A  224  LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR          
SEQRES  13 A  224  GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE          
SEQRES  14 A  224  ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO          
SEQRES  15 A  224  THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL          
SEQRES  16 A  224  LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS          
SEQRES  17 A  224  GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS          
SEQRES  18 A  224  VAL ASN PHE                                                  
SEQRES   1 C  117  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 C  117  ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY          
SEQRES   3 C  117  ALA GLY ALA HIS ARG VAL GLY TRP PHE ARG ARG ALA PRO          
SEQRES   4 C  117  GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE GLY ALA SER          
SEQRES   5 C  117  GLY GLY MET THR ASN TYR LEU ASP SER VAL LYS GLY ARG          
SEQRES   6 C  117  PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR ILE TYR          
SEQRES   7 C  117  LEU GLN MET ASN SER LEU LYS PRO GLN ASP THR ALA VAL          
SEQRES   8 C  117  TYR TYR CYS ALA ALA ARG ASP ILE GLU THR ALA GLU TYR          
SEQRES   9 C  117  ILE TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER          
SEQRES   1 B  224  GLY ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO          
SEQRES   2 B  224  ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN          
SEQRES   3 B  224  ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS          
SEQRES   4 B  224  ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR          
SEQRES   5 B  224  ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL          
SEQRES   6 B  224  SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL          
SEQRES   7 B  224  TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG          
SEQRES   8 B  224  GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR          
SEQRES   9 B  224  ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE          
SEQRES  10 B  224  ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY          
SEQRES  11 B  224  ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN          
SEQRES  12 B  224  LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR          
SEQRES  13 B  224  GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE          
SEQRES  14 B  224  ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO          
SEQRES  15 B  224  THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL          
SEQRES  16 B  224  LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS          
SEQRES  17 B  224  GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS          
SEQRES  18 B  224  VAL ASN PHE                                                  
SEQRES   1 D  117  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 D  117  ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY          
SEQRES   3 D  117  ALA GLY ALA HIS ARG VAL GLY TRP PHE ARG ARG ALA PRO          
SEQRES   4 D  117  GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE GLY ALA SER          
SEQRES   5 D  117  GLY GLY MET THR ASN TYR LEU ASP SER VAL LYS GLY ARG          
SEQRES   6 D  117  PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR ILE TYR          
SEQRES   7 D  117  LEU GLN MET ASN SER LEU LYS PRO GLN ASP THR ALA VAL          
SEQRES   8 D  117  TYR TYR CYS ALA ALA ARG ASP ILE GLU THR ALA GLU TYR          
SEQRES   9 D  117  ILE TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER          
HET    CAC  A 601       5                                                       
HET    CAC  C 201       5                                                       
HET    CAC  B 601       5                                                       
HET    CAC  D 201       5                                                       
HETNAM     CAC CACODYLATE ION                                                   
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   5  CAC    4(C2 H6 AS O2 1-)                                            
HELIX    1 AA1 SER A  349  TRP A  353  5                                   5    
HELIX    2 AA2 TYR A  365  SER A  371  1                                   7    
HELIX    3 AA3 PRO A  384  ASN A  388  5                                   5    
HELIX    4 AA4 ASP A  405  ILE A  410  5                                   6    
HELIX    5 AA5 GLY A  416  ASN A  422  1                                   7    
HELIX    6 AA6 SER A  438  SER A  443  1                                   6    
HELIX    7 AA7 SER B  349  TRP B  353  5                                   5    
HELIX    8 AA8 TYR B  365  SER B  371  1                                   7    
HELIX    9 AA9 PRO B  384  ASN B  388  5                                   5    
HELIX   10 AB1 ASP B  405  ILE B  410  5                                   6    
HELIX   11 AB2 GLY B  416  ASN B  422  1                                   7    
HELIX   12 AB3 SER B  438  SER B  443  1                                   6    
SHEET    1 AA1 5 ASN A 354  ARG A 357  0                                        
SHEET    2 AA1 5 ASN A 394  ARG A 403 -1  O  ALA A 397   N  LYS A 356           
SHEET    3 AA1 5 PRO A 507  GLU A 516 -1  O  TYR A 508   N  ILE A 402           
SHEET    4 AA1 5 GLY A 431  ASN A 437 -1  N  ILE A 434   O  VAL A 511           
SHEET    5 AA1 5 THR A 376  TYR A 380 -1  N  TYR A 380   O  GLY A 431           
SHEET    1 AA2 2 CYS A 361  VAL A 362  0                                        
SHEET    2 AA2 2 VAL A 524  CYS A 525  1  O  CYS A 525   N  CYS A 361           
SHEET    1 AA3 2 TYR A 473  GLN A 474  0                                        
SHEET    2 AA3 2 CYS A 488  TYR A 489 -1  O  TYR A 489   N  TYR A 473           
SHEET    1 AA4 4 LEU C   4  SER C   7  0                                        
SHEET    2 AA4 4 SER C  17  VAL C  24 -1  O  ALA C  23   N  VAL C   5           
SHEET    3 AA4 4 THR C  76  ASN C  82 -1  O  MET C  81   N  LEU C  18           
SHEET    4 AA4 4 PHE C  66  ASP C  71 -1  N  ASP C  71   O  THR C  76           
SHEET    1 AA5 6 GLY C  10  GLN C  13  0                                        
SHEET    2 AA5 6 THR C 111  SER C 116  1  O  THR C 114   N  VAL C  12           
SHEET    3 AA5 6 ALA C  90  ALA C  96 -1  N  ALA C  90   O  VAL C 113           
SHEET    4 AA5 6 VAL C  32  ARG C  37 -1  N  PHE C  35   O  TYR C  93           
SHEET    5 AA5 6 GLU C  44  ILE C  49 -1  O  ILE C  49   N  VAL C  32           
SHEET    6 AA5 6 ASN C  57  TYR C  58 -1  O  ASN C  57   N  ALA C  48           
SHEET    1 AA6 4 THR B 376  TYR B 380  0                                        
SHEET    2 AA6 4 GLY B 431  ASN B 437 -1  O  GLY B 431   N  TYR B 380           
SHEET    3 AA6 4 PRO B 507  GLU B 516 -1  O  VAL B 511   N  ILE B 434           
SHEET    4 AA6 4 ASN B 394  ARG B 403 -1  N  PHE B 400   O  VAL B 510           
SHEET    1 AA7 2 LEU B 452  ARG B 454  0                                        
SHEET    2 AA7 2 LEU B 492  SER B 494 -1  O  GLN B 493   N  TYR B 453           
SHEET    1 AA8 4 LEU D   4  SER D   7  0                                        
SHEET    2 AA8 4 SER D  17  VAL D  24 -1  O  SER D  21   N  SER D   7           
SHEET    3 AA8 4 THR D  76  ASN D  82 -1  O  MET D  81   N  LEU D  18           
SHEET    4 AA8 4 PHE D  66  ASP D  71 -1  N  THR D  67   O  GLN D  80           
SHEET    1 AA9 5 GLY D  10  GLN D  13  0                                        
SHEET    2 AA9 5 THR D 111  SER D 116  1  O  THR D 114   N  VAL D  12           
SHEET    3 AA9 5 ALA D  90  ARG D  97 -1  N  TYR D  92   O  THR D 111           
SHEET    4 AA9 5 ARG D  31  ARG D  37 -1  N  PHE D  35   O  TYR D  93           
SHEET    5 AA9 5 GLU D  44  ILE D  49 -1  O  ILE D  49   N  VAL D  32           
SHEET    1 AB1 4 GLY D  10  GLN D  13  0                                        
SHEET    2 AB1 4 THR D 111  SER D 116  1  O  THR D 114   N  VAL D  12           
SHEET    3 AB1 4 ALA D  90  ARG D  97 -1  N  TYR D  92   O  THR D 111           
SHEET    4 AB1 4 TYR D 106  TRP D 107 -1  O  TYR D 106   N  ALA D  96           
SSBOND   1 CYS A  336    CYS A  361                          1555   1555  2.03  
SSBOND   2 CYS A  379    CYS A  432                          1555   1555  2.03  
SSBOND   3 CYS A  391    CYS A  525                          1555   1555  2.03  
SSBOND   4 CYS A  480    CYS A  488                          1555   1555  2.03  
SSBOND   5 CYS C   22    CYS C   94                          1555   1555  2.04  
SSBOND   6 CYS B  336    CYS B  361                          1555   1555  2.03  
SSBOND   7 CYS B  379    CYS B  432                          1555   1555  2.03  
SSBOND   8 CYS B  391    CYS B  525                          1555   1555  2.03  
SSBOND   9 CYS B  480    CYS B  488                          1555   1555  2.03  
SSBOND  10 CYS D   22    CYS D   94                          1555   1555  2.04  
CRYST1   70.716   70.716  435.037  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014141  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002299        0.00000                         
ATOM      1  N   ASN A 334       1.111  15.400  -8.551  1.00118.44           N  
ANISOU    1  N   ASN A 334    16690  15201  13113  -4433    238  -1135       N  
ATOM      2  CA  ASN A 334       0.003  15.921  -9.341  1.00127.82           C  
ANISOU    2  CA  ASN A 334    17993  16243  14330  -4369    302  -1011       C  
ATOM      3  C   ASN A 334      -1.315  15.876  -8.573  1.00121.53           C  
ANISOU    3  C   ASN A 334    17269  15475  13432  -4217    266  -1066       C  
ATOM      4  O   ASN A 334      -1.369  15.380  -7.451  1.00116.80           O  
ANISOU    4  O   ASN A 334    16631  15014  12732  -4161    198  -1186       O  
ATOM      5  CB  ASN A 334      -0.132  15.140 -10.648  1.00145.86           C  
ANISOU    5  CB  ASN A 334    20276  18580  16563  -4352    373   -802       C  
ATOM      6  CG  ASN A 334      -0.486  13.682 -10.419  1.00152.49           C  
ANISOU    6  CG  ASN A 334    21073  19642  17225  -4253    347   -764       C  
ATOM      7  OD1 ASN A 334      -1.662  13.322 -10.330  1.00148.67           O  
ANISOU    7  OD1 ASN A 334    20647  19197  16646  -4129    350   -727       O  
ATOM      8  ND2 ASN A 334       0.531  12.833 -10.317  1.00154.65           N  
ANISOU    8  ND2 ASN A 334    21244  20061  17456  -4307    324   -776       N  
ATOM      9  N   LEU A 335      -2.373  16.387  -9.192  1.00129.14           N  
ANISOU    9  N   LEU A 335    18335  16316  14417  -4144    314   -973       N  
ATOM     10  CA  LEU A 335      -3.694  16.439  -8.570  1.00120.32           C  
ANISOU   10  CA  LEU A 335    17286  15216  13212  -3999    290  -1019       C  
ATOM     11  C   LEU A 335      -4.654  15.429  -9.200  1.00121.17           C  
ANISOU   11  C   LEU A 335    17410  15444  13186  -3888    327   -872       C  
ATOM     12  O   LEU A 335      -4.497  15.047 -10.360  1.00127.47           O  
ANISOU   12  O   LEU A 335    18198  16244  13989  -3914    385   -718       O  
ATOM     13  CB  LEU A 335      -4.273  17.851  -8.674  1.00119.80           C  
ANISOU   13  CB  LEU A 335    17327  14923  13270  -3982    308  -1052       C  
ATOM     14  CG  LEU A 335      -3.426  18.951  -8.035  1.00132.90           C  
ANISOU   14  CG  LEU A 335    18978  16437  15079  -4092    274  -1213       C  
ATOM     15  CD1 LEU A 335      -4.097  20.311  -8.180  1.00137.21           C  
ANISOU   15  CD1 LEU A 335    19642  16744  15747  -4061    298  -1235       C  
ATOM     16  CD2 LEU A 335      -3.157  18.632  -6.575  1.00142.08           C  
ANISOU   16  CD2 LEU A 335    20074  17744  16166  -4074    182  -1411       C  
ATOM     17  N   CYS A 336      -5.648  14.997  -8.429  1.00116.78           N  
ANISOU   17  N   CYS A 336    16871  14990  12509  -3766    296   -926       N  
ATOM     18  CA  CYS A 336      -6.589  13.974  -8.881  1.00117.08           C  
ANISOU   18  CA  CYS A 336    16911  15155  12419  -3666    328   -812       C  
ATOM     19  C   CYS A 336      -7.637  14.528  -9.849  1.00118.42           C  
ANISOU   19  C   CYS A 336    17164  15213  12617  -3592    382   -705       C  
ATOM     20  O   CYS A 336      -8.036  15.689  -9.738  1.00118.25           O  
ANISOU   20  O   CYS A 336    17217  15035  12678  -3568    381   -755       O  
ATOM     21  CB  CYS A 336      -7.277  13.323  -7.677  1.00120.21           C  
ANISOU   21  CB  CYS A 336    17293  15703  12678  -3567    284   -907       C  
ATOM     22  SG  CYS A 336      -6.223  12.170  -6.759  1.00120.63           S  
ANISOU   22  SG  CYS A 336    17245  15951  12639  -3612    234   -973       S  
ATOM     23  N   PRO A 337      -8.084  13.690 -10.803  1.00119.07           N  
ANISOU   23  N   PRO A 337    17233  15379  12630  -3551    429   -564       N  
ATOM     24  CA  PRO A 337      -9.024  14.082 -11.861  1.00114.10           C  
ANISOU   24  CA  PRO A 337    16669  14675  12011  -3474    481   -450       C  
ATOM     25  C   PRO A 337     -10.307  14.590 -11.197  1.00107.84           C  
ANISOU   25  C   PRO A 337    15937  13859  11178  -3348    461   -531       C  
ATOM     26  O   PRO A 337     -11.044  13.808 -10.593  1.00 85.89           O  
ANISOU   26  O   PRO A 337    13129  11224   8282  -3272    444   -571       O  
ATOM     27  CB  PRO A 337      -9.191  12.789 -12.673  1.00103.87           C  
ANISOU   27  CB  PRO A 337    15315  13532  10618  -3452    516   -329       C  
ATOM     28  CG  PRO A 337      -8.780  11.694 -11.750  1.00 96.37           C  
ANISOU   28  CG  PRO A 337    14290  12743   9582  -3476    477   -399       C  
ATOM     29  CD  PRO A 337      -7.668  12.284 -10.950  1.00108.38           C  
ANISOU   29  CD  PRO A 337    15796  14202  11182  -3572    433   -507       C  
ATOM     30  N   PHE A 338     -10.552  15.893 -11.306  1.00135.15           N  
ANISOU   30  N   PHE A 338    19479  17134  14737  -3328    466   -555       N  
ATOM     31  CA  PHE A 338     -11.844  16.507 -11.008  1.00150.33           C  
ANISOU   31  CA  PHE A 338    21472  19014  16633  -3194    458   -603       C  
ATOM     32  C   PHE A 338     -12.740  16.528 -12.239  1.00149.02           C  
ANISOU   32  C   PHE A 338    21345  18835  16440  -3100    511   -461       C  
ATOM     33  O   PHE A 338     -13.886  16.085 -12.194  1.00142.25           O  
ANISOU   33  O   PHE A 338    20482  18086  15479  -2983    512   -462       O  
ATOM     34  CB  PHE A 338     -11.650  17.934 -10.472  1.00161.27           C  
ANISOU   34  CB  PHE A 338    22933  20198  18145  -3210    433   -710       C  
ATOM     35  CG  PHE A 338     -12.813  18.861 -10.743  1.00161.01           C  
ANISOU   35  CG  PHE A 338    22997  20049  18130  -3079    448   -701       C  
ATOM     36  CD1 PHE A 338     -14.053  18.636 -10.164  1.00158.87           C  
ANISOU   36  CD1 PHE A 338    22730  19885  17750  -2941    425   -766       C  
ATOM     37  CD2 PHE A 338     -12.653  19.976 -11.551  1.00156.17           C  
ANISOU   37  CD2 PHE A 338    22471  19220  17645  -3090    486   -628       C  
ATOM     38  CE1 PHE A 338     -15.115  19.490 -10.406  1.00152.16           C  
ANISOU   38  CE1 PHE A 338    21964  18937  16912  -2811    435   -764       C  
ATOM     39  CE2 PHE A 338     -13.712  20.838 -11.793  1.00152.47           C  
ANISOU   39  CE2 PHE A 338    22098  18644  17191  -2956    498   -618       C  
ATOM     40  CZ  PHE A 338     -14.944  20.592 -11.219  1.00150.06           C  
ANISOU   40  CZ  PHE A 338    21790  18455  16771  -2813    468   -690       C  
ATOM     41  N   GLY A 339     -12.198  17.041 -13.338  1.00153.99           N  
ANISOU   41  N   GLY A 339    22010  19339  17159  -3151    557   -342       N  
ATOM     42  CA  GLY A 339     -12.948  17.173 -14.571  1.00145.84           C  
ANISOU   42  CA  GLY A 339    21020  18288  16105  -3057    607   -202       C  
ATOM     43  C   GLY A 339     -13.229  15.845 -15.239  1.00131.62           C  
ANISOU   43  C   GLY A 339    19140  16686  14185  -3031    628   -113       C  
ATOM     44  O   GLY A 339     -14.304  15.643 -15.799  1.00136.66           O  
ANISOU   44  O   GLY A 339    19786  17390  14747  -2910    646    -63       O  
ATOM     45  N   GLU A 340     -12.265  14.932 -15.165  1.00115.97           N  
ANISOU   45  N   GLU A 340    17077  14800  12188  -3141    624   -104       N  
ATOM     46  CA  GLU A 340     -12.382  13.641 -15.835  1.00112.81           C  
ANISOU   46  CA  GLU A 340    16599  14574  11689  -3131    646    -22       C  
ATOM     47  C   GLU A 340     -13.562  12.830 -15.317  1.00115.45           C  
ANISOU   47  C   GLU A 340    16899  15065  11903  -3029    628    -81       C  
ATOM     48  O   GLU A 340     -14.099  11.982 -16.026  1.00125.80           O  
ANISOU   48  O   GLU A 340    18165  16497  13135  -2980    653    -14       O  
ATOM     49  CB  GLU A 340     -11.095  12.831 -15.676  1.00100.00           C  
ANISOU   49  CB  GLU A 340    14898  13022  10075  -3263    638    -21       C  
ATOM     50  CG  GLU A 340      -9.870  13.496 -16.281  1.00105.44           C  
ANISOU   50  CG  GLU A 340    15600  13582  10880  -3378    665     44       C  
ATOM     51  CD  GLU A 340      -8.671  12.571 -16.331  1.00111.53           C  
ANISOU   51  CD  GLU A 340    16280  14452  11642  -3492    662     60       C  
ATOM     52  OE1 GLU A 340      -8.863  11.343 -16.195  1.00110.39           O  
ANISOU   52  OE1 GLU A 340    16071  14475  11398  -3468    650     56       O  
ATOM     53  OE2 GLU A 340      -7.540  13.073 -16.508  1.00111.85           O  
ANISOU   53  OE2 GLU A 340    16314  14403  11781  -3605    673     74       O  
ATOM     54  N   VAL A 341     -13.954  13.087 -14.078  1.00106.35           N  
ANISOU   54  N   VAL A 341    15762  13911  10736  -3000    588   -210       N  
ATOM     55  CA  VAL A 341     -15.062  12.362 -13.470  1.00112.13           C  
ANISOU   55  CA  VAL A 341    16460  14789  11356  -2911    578   -272       C  
ATOM     56  C   VAL A 341     -16.393  13.103 -13.360  1.00101.29           C  
ANISOU   56  C   VAL A 341    15141  13383   9960  -2773    575   -315       C  
ATOM     57  O   VAL A 341     -17.439  12.575 -13.723  1.00 80.43           O  
ANISOU   57  O   VAL A 341    12470  10852   7237  -2684    594   -293       O  
ATOM     58  CB  VAL A 341     -14.733  11.957 -12.033  1.00125.45           C  
ANISOU   58  CB  VAL A 341    18115  16543  13009  -2952    537   -395       C  
ATOM     59  CG1 VAL A 341     -15.842  11.086 -11.473  1.00126.36           C  
ANISOU   59  CG1 VAL A 341    18189  16818  13006  -2870    541   -439       C  
ATOM     60  CG2 VAL A 341     -13.410  11.212 -12.001  1.00130.84           C  
ANISOU   60  CG2 VAL A 341    18740  17269  13705  -3076    531   -368       C  
ATOM     61  N   PHE A 342     -16.349  14.311 -12.810  1.00114.51           N  
ANISOU   61  N   PHE A 342    16889  14910  11708  -2757    550   -387       N  
ATOM     62  CA  PHE A 342     -17.542  15.139 -12.662  1.00116.47           C  
ANISOU   62  CA  PHE A 342    17199  15111  11945  -2621    543   -436       C  
ATOM     63  C   PHE A 342     -17.886  15.881 -13.946  1.00118.91           C  
ANISOU   63  C   PHE A 342    17570  15313  12297  -2551    577   -321       C  
ATOM     64  O   PHE A 342     -19.015  15.806 -14.434  1.00116.22           O  
ANISOU   64  O   PHE A 342    17228  15041  11888  -2425    591   -295       O  
ATOM     65  CB  PHE A 342     -17.354  16.144 -11.528  1.00120.93           C  
ANISOU   65  CB  PHE A 342    17819  15555  12572  -2624    499   -570       C  
ATOM     66  CG  PHE A 342     -17.412  15.522 -10.174  1.00125.62           C  
ANISOU   66  CG  PHE A 342    18360  16279  13092  -2637    463   -697       C  
ATOM     67  CD1 PHE A 342     -16.325  14.832  -9.670  1.00131.73           C  
ANISOU   67  CD1 PHE A 342    19078  17110  13863  -2757    447   -717       C  
ATOM     68  CD2 PHE A 342     -18.562  15.608  -9.409  1.00122.01           C  
ANISOU   68  CD2 PHE A 342    17904  15896  12557  -2522    447   -793       C  
ATOM     69  CE1 PHE A 342     -16.380  14.244  -8.424  1.00126.67           C  
ANISOU   69  CE1 PHE A 342    18391  16595  13141  -2757    417   -823       C  
ATOM     70  CE2 PHE A 342     -18.622  15.025  -8.164  1.00118.82           C  
ANISOU   70  CE2 PHE A 342    17453  15620  12075  -2528    421   -899       C  
ATOM     71  CZ  PHE A 342     -17.528  14.341  -7.670  1.00120.29           C  
ANISOU   71  CZ  PHE A 342    17590  15859  12256  -2643    407   -911       C  
ATOM     72  N   ASN A 343     -16.909  16.589 -14.497  1.00115.50           N  
ANISOU   72  N   ASN A 343    17191  14718  11977  -2630    593   -252       N  
ATOM     73  CA  ASN A 343     -17.146  17.382 -15.693  1.00118.70           C  
ANISOU   73  CA  ASN A 343    17669  15003  12427  -2562    633   -132       C  
ATOM     74  C   ASN A 343     -17.065  16.549 -16.971  1.00130.77           C  
ANISOU   74  C   ASN A 343    19144  16642  13899  -2564    675     12       C  
ATOM     75  O   ASN A 343     -16.993  17.095 -18.072  1.00143.97           O  
ANISOU   75  O   ASN A 343    20869  18227  15606  -2530    715    136       O  
ATOM     76  CB  ASN A 343     -16.165  18.555 -15.761  1.00118.13           C  
ANISOU   76  CB  ASN A 343    17682  14696  12507  -2647    644   -112       C  
ATOM     77  CG  ASN A 343     -16.453  19.618 -14.719  1.00119.26           C  
ANISOU   77  CG  ASN A 343    17898  14701  12716  -2609    605   -250       C  
ATOM     78  OD1 ASN A 343     -17.586  19.760 -14.256  1.00118.44           O  
ANISOU   78  OD1 ASN A 343    17810  14647  12546  -2477    580   -325       O  
ATOM     79  ND2 ASN A 343     -15.438  20.400 -14.373  1.00117.71           N  
ANISOU   79  ND2 ASN A 343    17744  14327  12653  -2723    601   -288       N  
ATOM     80  N   ALA A 344     -17.068  15.226 -16.822  1.00119.89           N  
ANISOU   80  N   ALA A 344    17664  15454  12433  -2602    669     -3       N  
ATOM     81  CA  ALA A 344     -17.110  14.333 -17.974  1.00103.34           C  
ANISOU   81  CA  ALA A 344    15508  13484  10274  -2593    704    110       C  
ATOM     82  C   ALA A 344     -18.405  14.545 -18.754  1.00113.16           C  
ANISOU   82  C   ALA A 344    16769  14777  11448  -2427    718    151       C  
ATOM     83  O   ALA A 344     -19.471  14.716 -18.162  1.00115.71           O  
ANISOU   83  O   ALA A 344    17099  15141  11725  -2324    696     62       O  
ATOM     84  CB  ALA A 344     -16.982  12.884 -17.532  1.00 81.76           C  
ANISOU   84  CB  ALA A 344    12668  10935   7464  -2655    693     66       C  
ATOM     85  N   THR A 345     -18.311  14.535 -20.080  1.00126.19           N  
ANISOU   85  N   THR A 345    18423  16436  13086  -2394    756    283       N  
ATOM     86  CA  THR A 345     -19.475  14.782 -20.928  1.00124.70           C  
ANISOU   86  CA  THR A 345    18250  16302  12828  -2226    768    330       C  
ATOM     87  C   THR A 345     -20.414  13.581 -20.944  1.00118.84           C  
ANISOU   87  C   THR A 345    17399  15786  11968  -2170    757    273       C  
ATOM     88  O   THR A 345     -21.632  13.732 -20.878  1.00110.52           O  
ANISOU   88  O   THR A 345    16340  14800  10853  -2036    744    220       O  
ATOM     89  CB  THR A 345     -19.075  15.113 -22.382  1.00120.02           C  
ANISOU   89  CB  THR A 345    17691  15665  12245  -2198    813    494       C  
ATOM     90  OG1 THR A 345     -18.055  16.120 -22.391  1.00127.05           O  
ANISOU   90  OG1 THR A 345    18674  16342  13257  -2281    835    555       O  
ATOM     91  CG2 THR A 345     -20.281  15.618 -23.158  1.00116.44           C  
ANISOU   91  CG2 THR A 345    17274  15245  11724  -2003    819    536       C  
ATOM     92  N   ARG A 346     -19.836  12.390 -21.053  1.00125.64           N  
ANISOU   92  N   ARG A 346    18171  16764  12804  -2274    765    283       N  
ATOM     93  CA  ARG A 346     -20.619  11.162 -21.143  1.00143.27           C  
ANISOU   93  CA  ARG A 346    20296  19200  14939  -2242    764    234       C  
ATOM     94  C   ARG A 346     -20.689  10.391 -19.822  1.00146.52           C  
ANISOU   94  C   ARG A 346    20656  19679  15336  -2316    744    115       C  
ATOM     95  O   ARG A 346     -19.674   9.898 -19.331  1.00160.59           O  
ANISOU   95  O   ARG A 346    22420  21443  17153  -2445    741    111       O  
ATOM     96  CB  ARG A 346     -20.044  10.250 -22.234  1.00159.06           C  
ANISOU   96  CB  ARG A 346    22229  21296  16912  -2292    789    323       C  
ATOM     97  CG  ARG A 346     -20.184  10.786 -23.654  1.00167.04           C  
ANISOU   97  CG  ARG A 346    23270  22297  17902  -2193    813    442       C  
ATOM     98  CD  ARG A 346     -19.632   9.799 -24.677  1.00178.46           C  
ANISOU   98  CD  ARG A 346    24637  23859  19311  -2240    835    514       C  
ATOM     99  NE  ARG A 346     -19.693  10.325 -26.040  1.00200.22           N  
ANISOU   99  NE  ARG A 346    27423  26614  22038  -2143    861    635       N  
ATOM    100  CZ  ARG A 346     -19.175   9.717 -27.104  1.00216.33           C  
ANISOU  100  CZ  ARG A 346    29411  28740  24043  -2162    884    717       C  
ATOM    101  NH1 ARG A 346     -18.554   8.553 -26.966  1.00223.79           N  
ANISOU  101  NH1 ARG A 346    30272  29773  24987  -2276    883    686       N  
ATOM    102  NH2 ARG A 346     -19.277  10.271 -28.305  1.00215.06           N  
ANISOU  102  NH2 ARG A 346    29284  28582  23846  -2058    909    830       N  
ATOM    103  N   PHE A 347     -21.896  10.223 -19.317  1.00141.15           N  
ANISOU  103  N   PHE A 347    19944  19092  14595  -2229    735     24       N  
ATOM    104  CA  PHE A 347     -22.088   9.439 -18.124  1.00119.07           C  
ANISOU  104  CA  PHE A 347    17096  16376  11771  -2285    727    -78       C  
ATOM    105  C   PHE A 347     -22.743   8.167 -18.585  1.00110.79           C  
ANISOU  105  C   PHE A 347    15939  15508  10648  -2275    751    -89       C  
ATOM    106  O   PHE A 347     -23.549   8.183 -19.502  1.00120.88           O  
ANISOU  106  O   PHE A 347    17185  16859  11883  -2176    760    -70       O  
ATOM    107  CB  PHE A 347     -23.004  10.157 -17.148  1.00115.45           C  
ANISOU  107  CB  PHE A 347    16673  15897  11297  -2199    707   -181       C  
ATOM    108  CG  PHE A 347     -22.271  10.975 -16.138  1.00118.02           C  
ANISOU  108  CG  PHE A 347    17076  16075  11689  -2253    680   -224       C  
ATOM    109  CD1 PHE A 347     -20.981  10.652 -15.786  1.00114.90           C  
ANISOU  109  CD1 PHE A 347    16683  15630  11344  -2390    675   -203       C  
ATOM    110  CD2 PHE A 347     -22.864  12.069 -15.555  1.00120.81           C  
ANISOU  110  CD2 PHE A 347    17497  16347  12058  -2163    656   -293       C  
ATOM    111  CE1 PHE A 347     -20.291  11.401 -14.868  1.00105.58           C  
ANISOU  111  CE1 PHE A 347    15564  14325  10227  -2442    646   -256       C  
ATOM    112  CE2 PHE A 347     -22.183  12.822 -14.635  1.00121.39           C  
ANISOU  112  CE2 PHE A 347    17637  16286  12198  -2213    628   -346       C  
ATOM    113  CZ  PHE A 347     -20.894  12.489 -14.293  1.00112.59           C  
ANISOU  113  CZ  PHE A 347    16519  15128  11133  -2355    622   -330       C  
ATOM    114  N   ALA A 348     -22.494   7.065 -17.880  1.00 78.71           N  
ANISOU  114  N   ALA A 348    11816  11522   6568  -2368    761   -131       N  
ATOM    115  CA  ALA A 348     -23.084   5.771 -18.205  1.00 73.05           C  
ANISOU  115  CA  ALA A 348    10997  10965   5796  -2376    790   -151       C  
ATOM    116  C   ALA A 348     -24.483   5.641 -17.634  1.00 68.15           C  
ANISOU  116  C   ALA A 348    10331  10445   5119  -2297    799   -251       C  
ATOM    117  O   ALA A 348     -25.018   6.584 -17.064  1.00 68.92           O  
ANISOU  117  O   ALA A 348    10478  10496   5213  -2222    781   -300       O  
ATOM    118  CB  ALA A 348     -22.205   4.647 -17.692  1.00 72.87           C  
ANISOU  118  CB  ALA A 348    10938  10967   5784  -2506    803   -146       C  
ATOM    119  N   SER A 349     -25.097   4.485 -17.845  1.00 67.62           N  
ANISOU  119  N   SER A 349    10165  10517   5010  -2312    831   -283       N  
ATOM    120  CA  SER A 349     -26.403   4.222 -17.266  1.00 98.62           C  
ANISOU  120  CA  SER A 349    14033  14554   8886  -2256    850   -381       C  
ATOM    121  C   SER A 349     -26.225   3.527 -15.921  1.00111.67           C  
ANISOU  121  C   SER A 349    15676  16222  10533  -2345    873   -428       C  
ATOM    122  O   SER A 349     -25.156   2.988 -15.632  1.00116.67           O  
ANISOU  122  O   SER A 349    16328  16808  11193  -2447    876   -384       O  
ATOM    123  CB  SER A 349     -27.258   3.381 -18.208  1.00 99.10           C  
ANISOU  123  CB  SER A 349    13984  14760   8909  -2224    877   -403       C  
ATOM    124  OG  SER A 349     -28.619   3.448 -17.825  1.00123.95           O  
ANISOU  124  OG  SER A 349    17076  18010  12010  -2144    890   -500       O  
ATOM    125  N   VAL A 350     -27.277   3.532 -15.109  1.00114.60           N  
ANISOU  125  N   VAL A 350    16016  16667  10862  -2298    892   -515       N  
ATOM    126  CA  VAL A 350     -27.197   3.022 -13.744  1.00121.01           C  
ANISOU  126  CA  VAL A 350    16828  17495  11654  -2362    917   -558       C  
ATOM    127  C   VAL A 350     -26.858   1.532 -13.678  1.00118.85           C  
ANISOU  127  C   VAL A 350    16494  17282  11381  -2472    965   -532       C  
ATOM    128  O   VAL A 350     -26.046   1.116 -12.852  1.00139.10           O  
ANISOU  128  O   VAL A 350    19092  19808  13950  -2549    972   -510       O  
ATOM    129  CB  VAL A 350     -28.515   3.289 -12.976  1.00115.10           C  
ANISOU  129  CB  VAL A 350    16046  16836  10853  -2282    936   -657       C  
ATOM    130  CG1 VAL A 350     -29.721   2.781 -13.759  1.00112.81           C  
ANISOU  130  CG1 VAL A 350    15649  16679  10534  -2233    969   -699       C  
ATOM    131  CG2 VAL A 350     -28.463   2.670 -11.593  1.00112.14           C  
ANISOU  131  CG2 VAL A 350    15666  16495  10446  -2345    972   -691       C  
ATOM    132  N   TYR A 351     -27.460   0.731 -14.552  1.00 90.88           N  
ANISOU  132  N   TYR A 351    12864  13832   7835  -2476    998   -538       N  
ATOM    133  CA  TYR A 351     -27.246  -0.712 -14.513  1.00 93.41           C  
ANISOU  133  CA  TYR A 351    13125  14202   8164  -2577   1050   -523       C  
ATOM    134  C   TYR A 351     -25.878  -1.077 -15.074  1.00 82.22           C  
ANISOU  134  C   TYR A 351    11742  12708   6789  -2650   1029   -435       C  
ATOM    135  O   TYR A 351     -25.392  -2.189 -14.868  1.00 91.62           O  
ANISOU  135  O   TYR A 351    12912  13907   7992  -2736   1064   -409       O  
ATOM    136  CB  TYR A 351     -28.347  -1.446 -15.281  1.00100.05           C  
ANISOU  136  CB  TYR A 351    13852  15165   8995  -2562   1091   -575       C  
ATOM    137  CG  TYR A 351     -28.329  -1.156 -16.758  1.00123.61           C  
ANISOU  137  CG  TYR A 351    16810  18163  11992  -2508   1056   -551       C  
ATOM    138  CD1 TYR A 351     -28.920  -0.006 -17.260  1.00142.59           C  
ANISOU  138  CD1 TYR A 351    19228  20577  14372  -2386   1015   -571       C  
ATOM    139  CD2 TYR A 351     -27.704  -2.017 -17.651  1.00128.63           C  
ANISOU  139  CD2 TYR A 351    17411  18805  12658  -2570   1063   -506       C  
ATOM    140  CE1 TYR A 351     -28.901   0.276 -18.607  1.00147.68           C  
ANISOU  140  CE1 TYR A 351    19854  21241  15016  -2324    986   -540       C  
ATOM    141  CE2 TYR A 351     -27.678  -1.744 -19.003  1.00131.56           C  
ANISOU  141  CE2 TYR A 351    17757  19201  13028  -2512   1032   -483       C  
ATOM    142  CZ  TYR A 351     -28.277  -0.594 -19.476  1.00147.99           C  
ANISOU  142  CZ  TYR A 351    19854  21296  15078  -2388    994   -496       C  
ATOM    143  OH  TYR A 351     -28.260  -0.311 -20.821  1.00163.50           O  
ANISOU  143  OH  TYR A 351    21798  23294  17031  -2319    966   -465       O  
ATOM    144  N   ALA A 352     -25.269  -0.144 -15.799  1.00 76.25           N  
ANISOU  144  N   ALA A 352    11039  11876   6056  -2612    977   -386       N  
ATOM    145  CA  ALA A 352     -23.939  -0.359 -16.358  1.00 81.86           C  
ANISOU  145  CA  ALA A 352    11780  12518   6806  -2677    957   -303       C  
ATOM    146  C   ALA A 352     -22.888   0.632 -15.866  1.00 85.32           C  
ANISOU  146  C   ALA A 352    12315  12832   7271  -2689    911   -265       C  
ATOM    147  O   ALA A 352     -22.005   1.041 -16.622  1.00 87.13           O  
ANISOU  147  O   ALA A 352    12575  12995   7535  -2704    884   -198       O  
ATOM    148  CB  ALA A 352     -23.999  -0.407 -17.867  1.00 85.66           C  
ANISOU  148  CB  ALA A 352    12219  13032   7295  -2643    948   -268       C  
ATOM    149  N   TRP A 353     -22.995   1.012 -14.596  1.00 78.70           N  
ANISOU  149  N   TRP A 353    11517  11969   6415  -2685    905   -312       N  
ATOM    150  CA  TRP A 353     -22.142   2.038 -13.997  1.00 72.54           C  
ANISOU  150  CA  TRP A 353    10822  11077   5661  -2692    859   -304       C  
ATOM    151  C   TRP A 353     -20.664   1.756 -14.252  1.00 65.30           C  
ANISOU  151  C   TRP A 353     9926  10097   4786  -2780    841   -234       C  
ATOM    152  O   TRP A 353     -20.241   0.605 -14.303  1.00 72.78           O  
ANISOU  152  O   TRP A 353    10833  11092   5727  -2843    866   -206       O  
ATOM    153  CB  TRP A 353     -22.409   2.143 -12.487  1.00 85.36           C  
ANISOU  153  CB  TRP A 353    12471  12715   7249  -2686    861   -374       C  
ATOM    154  CG  TRP A 353     -22.422   0.814 -11.751  1.00 74.87           C  
ANISOU  154  CG  TRP A 353    11099  11468   5881  -2745    908   -380       C  
ATOM    155  CD1 TRP A 353     -23.467  -0.062 -11.650  1.00 65.63           C  
ANISOU  155  CD1 TRP A 353     9862  10400   4673  -2737    966   -409       C  
ATOM    156  CD2 TRP A 353     -21.338   0.226 -11.018  1.00 68.13           C  
ANISOU  156  CD2 TRP A 353    10268  10596   5024  -2818    904   -352       C  
ATOM    157  NE1 TRP A 353     -23.101  -1.156 -10.904  1.00 65.32           N  
ANISOU  157  NE1 TRP A 353     9812  10396   4612  -2803   1004   -392       N  
ATOM    158  CE2 TRP A 353     -21.800  -1.004 -10.505  1.00 79.30           C  
ANISOU  158  CE2 TRP A 353    11638  12097   6397  -2845    964   -356       C  
ATOM    159  CE3 TRP A 353     -20.026   0.620 -10.747  1.00 75.00           C  
ANISOU  159  CE3 TRP A 353    11188  11387   5923  -2861    856   -328       C  
ATOM    160  CZ2 TRP A 353     -20.991  -1.842  -9.737  1.00 85.50           C  
ANISOU  160  CZ2 TRP A 353    12436  12889   7160  -2901    978   -326       C  
ATOM    161  CZ3 TRP A 353     -19.226  -0.212  -9.986  1.00 82.02           C  
ANISOU  161  CZ3 TRP A 353    12079  12298   6787  -2916    863   -310       C  
ATOM    162  CH2 TRP A 353     -19.711  -1.429  -9.490  1.00 89.02           C  
ANISOU  162  CH2 TRP A 353    12930  13269   7625  -2930    923   -305       C  
ATOM    163  N   ASN A 354     -19.881   2.811 -14.435  1.00 65.69           N  
ANISOU  163  N   ASN A 354    10037  10038   4883  -2784    800   -207       N  
ATOM    164  CA  ASN A 354     -18.467   2.643 -14.747  1.00 98.37           C  
ANISOU  164  CA  ASN A 354    14188  14122   9065  -2867    784   -144       C  
ATOM    165  C   ASN A 354     -17.561   2.999 -13.578  1.00 90.42           C  
ANISOU  165  C   ASN A 354    13226  13055   8074  -2917    750   -178       C  
ATOM    166  O   ASN A 354     -17.753   4.016 -12.912  1.00 89.02           O  
ANISOU  166  O   ASN A 354    13100  12816   7907  -2882    723   -233       O  
ATOM    167  CB  ASN A 354     -18.086   3.472 -15.973  1.00110.89           C  
ANISOU  167  CB  ASN A 354    15800  15633  10701  -2853    771    -75       C  
ATOM    168  CG  ASN A 354     -18.682   2.922 -17.249  1.00128.09           C  
ANISOU  168  CG  ASN A 354    17921  17889  12857  -2813    799    -32       C  
ATOM    169  OD1 ASN A 354     -19.075   1.756 -17.310  1.00126.52           O  
ANISOU  169  OD1 ASN A 354    17657  17792  12622  -2827    827    -47       O  
ATOM    170  ND2 ASN A 354     -18.750   3.755 -18.279  1.00139.33           N  
ANISOU  170  ND2 ASN A 354    19371  19267  14302  -2761    794     21       N  
ATOM    171  N   ARG A 355     -16.587   2.136 -13.310  1.00 85.62           N  
ANISOU  171  N   ARG A 355    12596  12473   7463  -2992    750   -153       N  
ATOM    172  CA  ARG A 355     -15.637   2.403 -12.245  1.00 97.85           C  
ANISOU  172  CA  ARG A 355    14176  13984   9019  -3036    713   -190       C  
ATOM    173  C   ARG A 355     -14.554   3.367 -12.699  1.00 97.37           C  
ANISOU  173  C   ARG A 355    14146  13814   9035  -3083    677   -164       C  
ATOM    174  O   ARG A 355     -14.316   3.543 -13.892  1.00 91.66           O  
ANISOU  174  O   ARG A 355    13416  13057   8353  -3095    689    -94       O  
ATOM    175  CB  ARG A 355     -14.991   1.109 -11.754  1.00110.32           C  
ANISOU  175  CB  ARG A 355    15719  15637  10559  -3087    726   -173       C  
ATOM    176  CG  ARG A 355     -15.971   0.012 -11.422  1.00117.45           C  
ANISOU  176  CG  ARG A 355    16589  16638  11399  -3058    776   -182       C  
ATOM    177  CD  ARG A 355     -15.725  -0.510 -10.020  1.00111.22           C  
ANISOU  177  CD  ARG A 355    15811  15895  10552  -3063    775   -219       C  
ATOM    178  NE  ARG A 355     -16.139   0.462  -9.011  1.00 98.84           N  
ANISOU  178  NE  ARG A 355    14283  14309   8961  -3016    749   -298       N  
ATOM    179  CZ  ARG A 355     -16.233   0.190  -7.715  1.00100.89           C  
ANISOU  179  CZ  ARG A 355    14556  14624   9154  -2994    751   -343       C  
ATOM    180  NH1 ARG A 355     -15.930  -1.021  -7.269  1.00106.57           N  
ANISOU  180  NH1 ARG A 355    15257  15410   9824  -3015    782   -307       N  
ATOM    181  NH2 ARG A 355     -16.625   1.128  -6.863  1.00 97.01           N  
ANISOU  181  NH2 ARG A 355    14098  14120   8641  -2946    723   -424       N  
ATOM    182  N   LYS A 356     -13.898   3.986 -11.724  1.00 96.78           N  
ANISOU  182  N   LYS A 356    14104  13690   8978  -3109    636   -225       N  
ATOM    183  CA  LYS A 356     -12.777   4.871 -11.986  1.00 95.46           C  
ANISOU  183  CA  LYS A 356    13961  13418   8893  -3171    604   -216       C  
ATOM    184  C   LYS A 356     -11.986   4.670 -10.697  1.00109.51           C  
ANISOU  184  C   LYS A 356    15733  15228  10649  -3208    565   -289       C  
ATOM    185  O   LYS A 356     -12.401   5.107  -9.626  1.00116.00           O  
ANISOU  185  O   LYS A 356    16582  16050  11441  -3168    542   -378       O  
ATOM    186  CB  LYS A 356     -13.271   6.278 -12.333  1.00 85.34           C  
ANISOU  186  CB  LYS A 356    12738  12016   7672  -3130    598   -229       C  
ATOM    187  CG  LYS A 356     -12.171   7.278 -12.668  1.00 79.18           C  
ANISOU  187  CG  LYS A 356    11986  11105   6992  -3201    577   -215       C  
ATOM    188  CD  LYS A 356     -11.317   6.799 -13.828  1.00 75.72           C  
ANISOU  188  CD  LYS A 356    11509  10676   6584  -3267    601   -109       C  
ATOM    189  CE  LYS A 356     -10.136   7.728 -14.065  1.00 83.23           C  
ANISOU  189  CE  LYS A 356    12480  11507   7638  -3354    588    -98       C  
ATOM    190  NZ  LYS A 356     -10.572   9.142 -14.233  1.00 90.86           N  
ANISOU  190  NZ  LYS A 356    13522  12324   8676  -3322    590   -109       N  
ATOM    191  N   ARG A 357     -10.796   4.111 -10.819  1.00103.50           N  
ANISOU  191  N   ARG A 357    14935  14492   9900  -3279    554   -259       N  
ATOM    192  CA  ARG A 357      -9.894   3.903  -9.691  1.00 79.06           C  
ANISOU  192  CA  ARG A 357    11825  11437   6779  -3312    511   -326       C  
ATOM    193  C   ARG A 357      -8.964   5.109  -9.677  1.00 86.71           C  
ANISOU  193  C   ARG A 357    12809  12296   7841  -3374    470   -371       C  
ATOM    194  O   ARG A 357      -8.215   5.337 -10.625  1.00105.74           O  
ANISOU  194  O   ARG A 357    15202  14651  10322  -3439    479   -311       O  
ATOM    195  CB  ARG A 357      -9.082   2.608  -9.824  1.00 80.01           C  
ANISOU  195  CB  ARG A 357    11891  11649   6859  -3348    519   -272       C  
ATOM    196  CG  ARG A 357      -8.009   2.415  -8.759  1.00 93.38           C  
ANISOU  196  CG  ARG A 357    13564  13392   8524  -3374    470   -337       C  
ATOM    197  CD  ARG A 357      -7.297   1.071  -8.912  1.00113.33           C  
ANISOU  197  CD  ARG A 357    16044  16013  11005  -3391    481   -277       C  
ATOM    198  NE  ARG A 357      -6.581   0.963 -10.183  1.00138.30           N  
ANISOU  198  NE  ARG A 357    19170  19147  14232  -3453    494   -202       N  
ATOM    199  CZ  ARG A 357      -5.312   1.316 -10.368  1.00143.77           C  
ANISOU  199  CZ  ARG A 357    19829  19821  14978  -3523    461   -213       C  
ATOM    200  NH1 ARG A 357      -4.597   1.801  -9.361  1.00130.51           N  
ANISOU  200  NH1 ARG A 357    18142  18147  13298  -3542    407   -306       N  
ATOM    201  NH2 ARG A 357      -4.755   1.179 -11.565  1.00149.94           N  
ANISOU  201  NH2 ARG A 357    20576  20586  15810  -3573    483   -137       N  
ATOM    202  N   ILE A 358      -9.016   5.875  -8.592  1.00 90.76           N  
ANISOU  202  N   ILE A 358    13350  12779   8354  -3356    428   -482       N  
ATOM    203  CA  ILE A 358      -8.203   7.080  -8.452  1.00 92.08           C  
ANISOU  203  CA  ILE A 358    13533  12833   8621  -3419    389   -549       C  
ATOM    204  C   ILE A 358      -7.115   6.884  -7.403  1.00 94.24           C  
ANISOU  204  C   ILE A 358    13765  13171   8872  -3459    333   -640       C  
ATOM    205  O   ILE A 358      -7.311   7.201  -6.233  1.00 96.52           O  
ANISOU  205  O   ILE A 358    14068  13487   9120  -3418    293   -752       O  
ATOM    206  CB  ILE A 358      -9.066   8.297  -8.059  1.00 81.46           C  
ANISOU  206  CB  ILE A 358    12253  11386   7311  -3366    376   -626       C  
ATOM    207  CG1 ILE A 358     -10.345   8.342  -8.894  1.00 84.78           C  
ANISOU  207  CG1 ILE A 358    12710  11782   7721  -3293    427   -548       C  
ATOM    208  CG2 ILE A 358      -8.285   9.584  -8.227  1.00 72.53           C  
ANISOU  208  CG2 ILE A 358    11145  10102   6311  -3441    352   -673       C  
ATOM    209  CD1 ILE A 358     -11.393   9.283  -8.350  1.00 80.31           C  
ANISOU  209  CD1 ILE A 358    12204  11155   7155  -3210    415   -629       C  
ATOM    210  N   SER A 359      -5.974   6.345  -7.822  1.00 99.18           N  
ANISOU  210  N   SER A 359    14334  13835   9517  -3532    328   -597       N  
ATOM    211  CA  SER A 359      -4.882   6.053  -6.898  1.00112.18           C  
ANISOU  211  CA  SER A 359    15929  15563  11132  -3563    273   -680       C  
ATOM    212  C   SER A 359      -3.617   6.839  -7.215  1.00109.52           C  
ANISOU  212  C   SER A 359    15555  15148  10909  -3674    246   -719       C  
ATOM    213  O   SER A 359      -3.511   7.464  -8.268  1.00118.16           O  
ANISOU  213  O   SER A 359    16663  16128  12105  -3733    281   -655       O  
ATOM    214  CB  SER A 359      -4.568   4.556  -6.911  1.00126.50           C  
ANISOU  214  CB  SER A 359    17697  17518  12849  -3540    287   -610       C  
ATOM    215  OG  SER A 359      -5.696   3.796  -6.516  1.00146.46           O  
ANISOU  215  OG  SER A 359    20256  20116  15275  -3448    318   -581       O  
ATOM    216  N   ASN A 360      -2.669   6.806  -6.283  1.00123.09           N  
ANISOU  216  N   ASN A 360    17223  16936  12608  -3699    186   -826       N  
ATOM    217  CA  ASN A 360      -1.358   7.420  -6.462  1.00121.27           C  
ANISOU  217  CA  ASN A 360    16936  16660  12480  -3812    156   -880       C  
ATOM    218  C   ASN A 360      -1.442   8.899  -6.825  1.00119.59           C  
ANISOU  218  C   ASN A 360    16765  16261  12412  -3878    165   -921       C  
ATOM    219  O   ASN A 360      -0.761   9.361  -7.740  1.00125.06           O  
ANISOU  219  O   ASN A 360    17438  16865  13216  -3978    194   -872       O  
ATOM    220  CB  ASN A 360      -0.571   6.662  -7.533  1.00125.87           C  
ANISOU  220  CB  ASN A 360    17462  17285  13078  -3870    191   -763       C  
ATOM    221  CG  ASN A 360      -0.232   5.244  -7.114  1.00131.16           C  
ANISOU  221  CG  ASN A 360    18085  18130  13620  -3814    174   -739       C  
ATOM    222  OD1 ASN A 360      -0.126   4.945  -5.927  1.00145.91           O  
ANISOU  222  OD1 ASN A 360    19941  20096  15403  -3757    123   -830       O  
ATOM    223  ND2 ASN A 360      -0.073   4.361  -8.091  1.00128.71           N  
ANISOU  223  ND2 ASN A 360    17751  17860  13295  -3821    218   -613       N  
ATOM    224  N   CYS A 361      -2.276   9.639  -6.101  1.00111.14           N  
ANISOU  224  N   CYS A 361    15756  15130  11341  -3821    145  -1010       N  
ATOM    225  CA  CYS A 361      -2.468  11.059  -6.375  1.00120.50           C  
ANISOU  225  CA  CYS A 361    16996  16124  12663  -3868    155  -1053       C  
ATOM    226  C   CYS A 361      -2.965  11.826  -5.155  1.00121.61           C  
ANISOU  226  C   CYS A 361    17175  16238  12795  -3813    101  -1216       C  
ATOM    227  O   CYS A 361      -3.351  11.233  -4.149  1.00135.58           O  
ANISOU  227  O   CYS A 361    18936  18143  14437  -3723     65  -1278       O  
ATOM    228  CB  CYS A 361      -3.469  11.233  -7.515  1.00122.67           C  
ANISOU  228  CB  CYS A 361    17344  16301  12966  -3832    227   -909       C  
ATOM    229  SG  CYS A 361      -5.093  10.525  -7.139  1.00115.18           S  
ANISOU  229  SG  CYS A 361    16447  15445  11870  -3673    242   -875       S  
ATOM    230  N   VAL A 362      -2.958  13.152  -5.257  1.00123.31           N  
ANISOU  230  N   VAL A 362    17434  16273  13147  -3863    100  -1282       N  
ATOM    231  CA  VAL A 362      -3.458  14.014  -4.190  1.00120.45           C  
ANISOU  231  CA  VAL A 362    17113  15861  12793  -3811     50  -1445       C  
ATOM    232  C   VAL A 362      -4.790  14.645  -4.592  1.00133.83           C  
ANISOU  232  C   VAL A 362    18911  17430  14509  -3729     91  -1393       C  
ATOM    233  O   VAL A 362      -4.909  15.220  -5.674  1.00150.28           O  
ANISOU  233  O   VAL A 362    21042  19360  16698  -3770    146  -1291       O  
ATOM    234  CB  VAL A 362      -2.451  15.128  -3.844  1.00 95.60           C  
ANISOU  234  CB  VAL A 362    13938  12593   9792  -3925      8  -1594       C  
ATOM    235  CG1 VAL A 362      -3.025  16.053  -2.783  1.00 95.49           C  
ANISOU  235  CG1 VAL A 362    13971  12519   9791  -3864    -44  -1770       C  
ATOM    236  CG2 VAL A 362      -1.131  14.527  -3.386  1.00102.57           C  
ANISOU  236  CG2 VAL A 362    14706  13619  10646  -3998    -41  -1665       C  
ATOM    237  N   ALA A 363      -5.787  14.551  -3.717  1.00126.42           N  
ANISOU  237  N   ALA A 363    18004  16562  13466  -3607     66  -1462       N  
ATOM    238  CA  ALA A 363      -7.116  15.071  -4.024  1.00113.59           C  
ANISOU  238  CA  ALA A 363    16469  14847  11844  -3512    101  -1423       C  
ATOM    239  C   ALA A 363      -7.608  16.060  -2.973  1.00115.98           C  
ANISOU  239  C   ALA A 363    16815  15089  12164  -3450     50  -1599       C  
ATOM    240  O   ALA A 363      -7.577  15.777  -1.775  1.00121.54           O  
ANISOU  240  O   ALA A 363    17484  15925  12771  -3402     -5  -1726       O  
ATOM    241  CB  ALA A 363      -8.103  13.929  -4.166  1.00107.78           C  
ANISOU  241  CB  ALA A 363    15732  14262  10959  -3409    137  -1315       C  
ATOM    242  N   ASP A 364      -8.075  17.217  -3.431  1.00108.69           N  
ANISOU  242  N   ASP A 364    15972  13967  11358  -3443     70  -1604       N  
ATOM    243  CA  ASP A 364      -8.640  18.226  -2.543  1.00111.26           C  
ANISOU  243  CA  ASP A 364    16350  14214  11710  -3374     27  -1767       C  
ATOM    244  C   ASP A 364     -10.128  18.408  -2.822  1.00114.55           C  
ANISOU  244  C   ASP A 364    16843  14605  12076  -3237     62  -1709       C  
ATOM    245  O   ASP A 364     -10.515  18.874  -3.894  1.00116.07           O  
ANISOU  245  O   ASP A 364    17098  14657  12348  -3232    115  -1592       O  
ATOM    246  CB  ASP A 364      -7.902  19.560  -2.700  1.00107.58           C  
ANISOU  246  CB  ASP A 364    15917  13517  11440  -3477     14  -1854       C  
ATOM    247  N   TYR A 365     -10.957  18.033  -1.853  1.00116.32           N  
ANISOU  247  N   TYR A 365    17059  14977  12162  -3120     34  -1789       N  
ATOM    248  CA  TYR A 365     -12.406  18.111  -2.000  1.00103.32           C  
ANISOU  248  CA  TYR A 365    15466  13341  10448  -2982     65  -1749       C  
ATOM    249  C   TYR A 365     -12.917  19.527  -1.757  1.00129.11           C  
ANISOU  249  C   TYR A 365    18815  16427  13812  -2925     42  -1865       C  
ATOM    250  O   TYR A 365     -14.117  19.783  -1.846  1.00119.24           O  
ANISOU  250  O   TYR A 365    17615  15170  12520  -2802     61  -1852       O  
ATOM    251  CB  TYR A 365     -13.094  17.153  -1.031  1.00 81.77           C  
ANISOU  251  CB  TYR A 365    12691  10843   7534  -2884     53  -1790       C  
ATOM    252  CG  TYR A 365     -12.609  15.727  -1.113  1.00 83.38           C  
ANISOU  252  CG  TYR A 365    12820  11224   7637  -2930     74  -1689       C  
ATOM    253  CD1 TYR A 365     -11.476  15.323  -0.422  1.00 93.58           C  
ANISOU  253  CD1 TYR A 365    14050  12601   8906  -3001     28  -1758       C  
ATOM    254  CD2 TYR A 365     -13.293  14.780  -1.860  1.00 78.82           C  
ANISOU  254  CD2 TYR A 365    12231  10732   6987  -2895    136  -1534       C  
ATOM    255  CE1 TYR A 365     -11.025  14.021  -0.485  1.00 99.57           C  
ANISOU  255  CE1 TYR A 365    14746  13515   9573  -3031     47  -1665       C  
ATOM    256  CE2 TYR A 365     -12.851  13.470  -1.929  1.00 85.90           C  
ANISOU  256  CE2 TYR A 365    13063  11776   7798  -2935    157  -1446       C  
ATOM    257  CZ  TYR A 365     -11.716  13.097  -1.238  1.00 91.62           C  
ANISOU  257  CZ  TYR A 365    13736  12573   8501  -3000    113  -1508       C  
ATOM    258  OH  TYR A 365     -11.267  11.798  -1.295  1.00 91.29           O  
ANISOU  258  OH  TYR A 365    13637  12673   8375  -3029    133  -1419       O  
ATOM    259  N   SER A 366     -11.999  20.439  -1.449  1.00141.22           N  
ANISOU  259  N   SER A 366    20361  17817  15480  -3013      2  -1983       N  
ATOM    260  CA  SER A 366     -12.352  21.821  -1.141  1.00150.96           C  
ANISOU  260  CA  SER A 366    21674  18860  16823  -2970    -25  -2112       C  
ATOM    261  C   SER A 366     -13.044  22.497  -2.318  1.00160.45           C  
ANISOU  261  C   SER A 366    22972  19876  18115  -2926     36  -1981       C  
ATOM    262  O   SER A 366     -13.980  23.276  -2.136  1.00169.30           O  
ANISOU  262  O   SER A 366    24165  20912  19248  -2810     29  -2041       O  
ATOM    263  CB  SER A 366     -11.104  22.613  -0.743  1.00153.38           C  
ANISOU  263  CB  SER A 366    21966  19033  17279  -3101    -70  -2253       C  
ATOM    264  OG  SER A 366     -10.480  22.047   0.397  1.00152.41           O  
ANISOU  264  OG  SER A 366    21752  19093  17063  -3124   -134  -2390       O  
ATOM    265  N   VAL A 367     -12.579  22.190  -3.524  1.00154.86           N  
ANISOU  265  N   VAL A 367    22263  19114  17462  -3010     94  -1802       N  
ATOM    266  CA  VAL A 367     -13.162  22.748  -4.738  1.00140.01           C  
ANISOU  266  CA  VAL A 367    20470  17073  15654  -2965    156  -1655       C  
ATOM    267  C   VAL A 367     -14.572  22.218  -4.983  1.00128.47           C  
ANISOU  267  C   VAL A 367    19021  15742  14050  -2805    180  -1578       C  
ATOM    268  O   VAL A 367     -15.409  22.912  -5.562  1.00133.58           O  
ANISOU  268  O   VAL A 367    19750  16271  14732  -2706    207  -1528       O  
ATOM    269  CB  VAL A 367     -12.288  22.446  -5.971  1.00126.56           C  
ANISOU  269  CB  VAL A 367    18752  15311  14025  -3091    215  -1477       C  
ATOM    270  CG1 VAL A 367     -11.030  23.301  -5.952  1.00132.73           C  
ANISOU  270  CG1 VAL A 367    19544  15901  14987  -3245    208  -1541       C  
ATOM    271  CG2 VAL A 367     -11.933  20.967  -6.023  1.00109.86           C  
ANISOU  271  CG2 VAL A 367    16531  13432  11779  -3133    220  -1402       C  
ATOM    272  N   LEU A 368     -14.831  20.990  -4.542  1.00112.69           N  
ANISOU  272  N   LEU A 368    16938  13986  11893  -2779    173  -1570       N  
ATOM    273  CA  LEU A 368     -16.143  20.378  -4.724  1.00106.03           C  
ANISOU  273  CA  LEU A 368    16087  13286  10913  -2642    199  -1508       C  
ATOM    274  C   LEU A 368     -17.187  20.982  -3.786  1.00115.04           C  
ANISOU  274  C   LEU A 368    17264  14443  12004  -2502    163  -1655       C  
ATOM    275  O   LEU A 368     -18.298  21.298  -4.211  1.00117.84           O  
ANISOU  275  O   LEU A 368    17664  14778  12333  -2377    186  -1617       O  
ATOM    276  CB  LEU A 368     -16.059  18.860  -4.522  1.00 94.57           C  
ANISOU  276  CB  LEU A 368    14536  12076   9319  -2669    211  -1454       C  
ATOM    277  CG  LEU A 368     -15.078  18.107  -5.429  1.00 88.95           C  
ANISOU  277  CG  LEU A 368    13779  11380   8637  -2795    245  -1311       C  
ATOM    278  CD1 LEU A 368     -15.161  16.601  -5.226  1.00 79.11           C  
ANISOU  278  CD1 LEU A 368    12445  10364   7248  -2799    259  -1259       C  
ATOM    279  CD2 LEU A 368     -15.334  18.458  -6.883  1.00 89.30           C  
ANISOU  279  CD2 LEU A 368    13875  11303   8751  -2784    300  -1154       C  
ATOM    280  N   TYR A 369     -16.822  21.152  -2.518  1.00119.16           N  
ANISOU  280  N   TYR A 369    17760  15007  12507  -2515    105  -1827       N  
ATOM    281  CA  TYR A 369     -17.746  21.660  -1.505  1.00124.30           C  
ANISOU  281  CA  TYR A 369    18433  15698  13097  -2382     67  -1983       C  
ATOM    282  C   TYR A 369     -18.183  23.099  -1.775  1.00141.68           C  
ANISOU  282  C   TYR A 369    20741  17667  15424  -2311     59  -2037       C  
ATOM    283  O   TYR A 369     -19.305  23.484  -1.446  1.00117.04           O  
ANISOU  283  O   TYR A 369    17653  14571  12247  -2164     51  -2101       O  
ATOM    284  CB  TYR A 369     -17.111  21.567  -0.116  1.00118.50           C  
ANISOU  284  CB  TYR A 369    17647  15059  12319  -2417      2  -2160       C  
ATOM    285  N   ASN A 370     -17.291  23.889  -2.363  1.00190.85           N  
ANISOU  285  N   ASN A 370    27023  23669  21823  -2414     64  -2011       N  
ATOM    286  CA  ASN A 370     -17.561  25.299  -2.633  1.00205.97           C  
ANISOU  286  CA  ASN A 370    29050  25329  23879  -2362     62  -2055       C  
ATOM    287  C   ASN A 370     -18.626  25.518  -3.703  1.00198.72           C  
ANISOU  287  C   ASN A 370    28200  24356  22949  -2238    115  -1910       C  
ATOM    288  O   ASN A 370     -19.457  26.420  -3.587  1.00204.53           O  
ANISOU  288  O   ASN A 370    29013  24986  23711  -2107    104  -1974       O  
ATOM    289  CB  ASN A 370     -16.272  26.013  -3.046  1.00221.01           C  
ANISOU  289  CB  ASN A 370    30993  27005  25978  -2522     68  -2048       C  
ATOM    290  CG  ASN A 370     -15.342  26.256  -1.877  1.00232.40           C  
ANISOU  290  CG  ASN A 370    32389  28447  27467  -2617      1  -2249       C  
ATOM    291  OD1 ASN A 370     -15.364  25.523  -0.888  1.00235.39           O  
ANISOU  291  OD1 ASN A 370    32683  29044  27710  -2597    -43  -2349       O  
ATOM    292  ND2 ASN A 370     -14.517  27.290  -1.984  1.00234.67           N  
ANISOU  292  ND2 ASN A 370    32728  28491  27945  -2719     -4  -2312       N  
ATOM    293  N   SER A 371     -18.590  24.700  -4.749  1.00186.57           N  
ANISOU  293  N   SER A 371    26629  22891  21367  -2272    170  -1720       N  
ATOM    294  CA  SER A 371     -19.559  24.804  -5.833  1.00171.82           C  
ANISOU  294  CA  SER A 371    24811  21000  19473  -2153    218  -1576       C  
ATOM    295  C   SER A 371     -20.968  24.503  -5.334  1.00155.01           C  
ANISOU  295  C   SER A 371    22655  19047  17193  -1980    204  -1639       C  
ATOM    296  O   SER A 371     -21.200  23.492  -4.671  1.00147.76           O  
ANISOU  296  O   SER A 371    21643  18359  16141  -1981    193  -1681       O  
ATOM    297  CB  SER A 371     -19.191  23.863  -6.983  1.00169.97           C  
ANISOU  297  CB  SER A 371    24530  20844  19209  -2229    274  -1377       C  
ATOM    298  OG  SER A 371     -18.848  22.576  -6.498  1.00168.52           O  
ANISOU  298  OG  SER A 371    24232  20884  18914  -2304    265  -1387       O  
ATOM    299  N   ALA A 372     -21.902  25.394  -5.646  1.00159.27           N  
ANISOU  299  N   ALA A 372    23278  19479  17756  -1830    208  -1645       N  
ATOM    300  CA  ALA A 372     -23.280  25.262  -5.184  1.00152.54           C  
ANISOU  300  CA  ALA A 372    22402  18783  16772  -1656    194  -1718       C  
ATOM    301  C   ALA A 372     -24.149  24.568  -6.228  1.00161.60           C  
ANISOU  301  C   ALA A 372    23515  20064  17821  -1573    243  -1564       C  
ATOM    302  O   ALA A 372     -25.374  24.552  -6.116  1.00165.27           O  
ANISOU  302  O   ALA A 372    23965  20643  18189  -1417    241  -1601       O  
ATOM    303  CB  ALA A 372     -23.855  26.626  -4.838  1.00147.62           C  
ANISOU  303  CB  ALA A 372    21883  17984  16221  -1522    163  -1834       C  
ATOM    304  N   SER A 373     -23.509  24.014  -7.252  1.00151.26           N  
ANISOU  304  N   SER A 373    22188  18746  16539  -1675    286  -1399       N  
ATOM    305  CA  SER A 373     -24.224  23.339  -8.328  1.00139.41           C  
ANISOU  305  CA  SER A 373    20648  17370  14951  -1607    330  -1255       C  
ATOM    306  C   SER A 373     -24.895  22.041  -7.863  1.00120.84           C  
ANISOU  306  C   SER A 373    18169  15305  12437  -1590    335  -1285       C  
ATOM    307  O   SER A 373     -25.965  21.679  -8.355  1.00130.18           O  
ANISOU  307  O   SER A 373    19315  16618  13528  -1475    357  -1245       O  
ATOM    308  CB  SER A 373     -23.270  23.058  -9.494  1.00141.15           C  
ANISOU  308  CB  SER A 373    20877  17513  15240  -1728    373  -1081       C  
ATOM    309  OG  SER A 373     -22.058  22.488  -9.036  1.00141.04           O  
ANISOU  309  OG  SER A 373    20811  17517  15260  -1908    365  -1098       O  
ATOM    310  N   PHE A 374     -24.264  21.347  -6.919  1.00119.01           N  
ANISOU  310  N   PHE A 374    17872  15172  12173  -1703    318  -1358       N  
ATOM    311  CA  PHE A 374     -24.758  20.059  -6.418  1.00101.24           C  
ANISOU  311  CA  PHE A 374    15507  13181   9780  -1708    332  -1376       C  
ATOM    312  C   PHE A 374     -26.093  20.157  -5.677  1.00101.20           C  
ANISOU  312  C   PHE A 374    15475  13307   9669  -1555    322  -1492       C  
ATOM    313  O   PHE A 374     -26.387  21.167  -5.036  1.00103.87           O  
ANISOU  313  O   PHE A 374    15874  13553  10038  -1469    284  -1613       O  
ATOM    314  CB  PHE A 374     -23.722  19.427  -5.491  1.00 92.73           C  
ANISOU  314  CB  PHE A 374    14381  12161   8693  -1849    313  -1430       C  
ATOM    315  CG  PHE A 374     -22.398  19.170  -6.145  1.00 81.41           C  
ANISOU  315  CG  PHE A 374    12951  10635   7347  -2004    325  -1325       C  
ATOM    316  CD1 PHE A 374     -22.269  18.186  -7.108  1.00 80.05           C  
ANISOU  316  CD1 PHE A 374    12725  10549   7141  -2058    369  -1180       C  
ATOM    317  CD2 PHE A 374     -21.286  19.921  -5.807  1.00 82.34           C  
ANISOU  317  CD2 PHE A 374    13120  10583   7583  -2097    291  -1379       C  
ATOM    318  CE1 PHE A 374     -21.053  17.945  -7.708  1.00 79.58           C  
ANISOU  318  CE1 PHE A 374    12664  10416   7158  -2196    381  -1086       C  
ATOM    319  CE2 PHE A 374     -20.069  19.690  -6.405  1.00 81.91           C  
ANISOU  319  CE2 PHE A 374    13060  10454   7608  -2242    305  -1286       C  
ATOM    320  CZ  PHE A 374     -19.951  18.699  -7.358  1.00 97.66           C  
ANISOU  320  CZ  PHE A 374    15002  12543   9561  -2288    350  -1136       C  
ATOM    321  N   SER A 375     -26.885  19.090  -5.745  1.00104.99           N  
ANISOU  321  N   SER A 375    15859  14004  10028  -1526    357  -1463       N  
ATOM    322  CA  SER A 375     -28.202  19.072  -5.115  1.00109.00           C  
ANISOU  322  CA  SER A 375    16324  14662  10429  -1387    358  -1564       C  
ATOM    323  C   SER A 375     -28.234  18.195  -3.872  1.00 95.62           C  
ANISOU  323  C   SER A 375    14549  13152   8632  -1434    364  -1648       C  
ATOM    324  O   SER A 375     -29.085  18.377  -3.003  1.00 84.96           O  
ANISOU  324  O   SER A 375    13175  11903   7204  -1333    356  -1765       O  
ATOM    325  CB  SER A 375     -29.263  18.587  -6.105  1.00122.90           C  
ANISOU  325  CB  SER A 375    18028  16542  12124  -1302    400  -1483       C  
ATOM    326  OG  SER A 375     -30.429  18.148  -5.425  1.00126.84           O  
ANISOU  326  OG  SER A 375    18446  17243  12503  -1212    416  -1572       O  
ATOM    327  N   THR A 376     -27.302  17.248  -3.794  1.00 92.46           N  
ANISOU  327  N   THR A 376    14106  12797   8227  -1580    380  -1585       N  
ATOM    328  CA  THR A 376     -27.197  16.340  -2.655  1.00 80.15           C  
ANISOU  328  CA  THR A 376    12478  11406   6570  -1630    391  -1641       C  
ATOM    329  C   THR A 376     -25.755  15.918  -2.424  1.00 90.23           C  
ANISOU  329  C   THR A 376    13760  12634   7891  -1781    375  -1606       C  
ATOM    330  O   THR A 376     -25.154  15.242  -3.257  1.00 78.52           O  
ANISOU  330  O   THR A 376    12256  11138   6440  -1878    402  -1482       O  
ATOM    331  CB  THR A 376     -28.047  15.073  -2.843  1.00 79.09           C  
ANISOU  331  CB  THR A 376    12242  11481   6326  -1625    457  -1582       C  
ATOM    332  OG1 THR A 376     -27.886  14.583  -4.179  1.00 97.35           O  
ANISOU  332  OG1 THR A 376    14539  13767   8683  -1678    488  -1443       O  
ATOM    333  CG2 THR A 376     -29.516  15.365  -2.588  1.00 79.82           C  
ANISOU  333  CG2 THR A 376    12303  11683   6343  -1475    472  -1663       C  
ATOM    334  N   PHE A 377     -25.205  16.320  -1.285  1.00100.75           N  
ANISOU  334  N   PHE A 377    15113  13947   9219  -1794    330  -1723       N  
ATOM    335  CA  PHE A 377     -23.815  16.032  -0.960  1.00102.69           C  
ANISOU  335  CA  PHE A 377    15360  14153   9506  -1925    304  -1714       C  
ATOM    336  C   PHE A 377     -23.726  15.249   0.348  1.00106.73           C  
ANISOU  336  C   PHE A 377    15815  14846   9894  -1933    304  -1784       C  
ATOM    337  O   PHE A 377     -23.408  15.805   1.395  1.00121.43           O  
ANISOU  337  O   PHE A 377    17695  16700  11742  -1910    253  -1916       O  
ATOM    338  CB  PHE A 377     -23.017  17.333  -0.877  1.00 93.48           C  
ANISOU  338  CB  PHE A 377    14275  12775   8470  -1946    242  -1794       C  
ATOM    339  CG  PHE A 377     -21.546  17.133  -0.685  1.00104.79           C  
ANISOU  339  CG  PHE A 377    15701  14154   9959  -2086    214  -1788       C  
ATOM    340  CD1 PHE A 377     -20.769  16.603  -1.700  1.00 97.96           C  
ANISOU  340  CD1 PHE A 377    14824  13242   9154  -2198    241  -1646       C  
ATOM    341  CD2 PHE A 377     -20.935  17.487   0.503  1.00134.55           C  
ANISOU  341  CD2 PHE A 377    19471  17932  13720  -2101    157  -1933       C  
ATOM    342  CE1 PHE A 377     -19.413  16.422  -1.530  1.00107.03           C  
ANISOU  342  CE1 PHE A 377    15960  14353  10355  -2323    214  -1646       C  
ATOM    343  CE2 PHE A 377     -19.578  17.308   0.680  1.00142.17           C  
ANISOU  343  CE2 PHE A 377    20421  18862  14735  -2225    127  -1938       C  
ATOM    344  CZ  PHE A 377     -18.815  16.775  -0.340  1.00127.77           C  
ANISOU  344  CZ  PHE A 377    18583  16990  12973  -2338    156  -1793       C  
ATOM    345  N   LYS A 378     -24.025  13.956   0.281  1.00103.73           N  
ANISOU  345  N   LYS A 378    15365  14626   9420  -1961    363  -1694       N  
ATOM    346  CA  LYS A 378     -24.041  13.107   1.469  1.00 85.42           C  
ANISOU  346  CA  LYS A 378    12995  12488   6973  -1959    379  -1735       C  
ATOM    347  C   LYS A 378     -22.720  12.402   1.718  1.00100.88           C  
ANISOU  347  C   LYS A 378    14938  14459   8931  -2074    366  -1690       C  
ATOM    348  O   LYS A 378     -21.936  12.182   0.798  1.00107.92           O  
ANISOU  348  O   LYS A 378    15837  15260   9909  -2169    367  -1592       O  
ATOM    349  CB  LYS A 378     -25.144  12.054   1.361  1.00 82.40           C  
ANISOU  349  CB  LYS A 378    12545  12275   6487  -1926    461  -1667       C  
ATOM    350  CG  LYS A 378     -24.966  11.111   0.206  1.00 94.30           C  
ANISOU  350  CG  LYS A 378    14046  13826   7958  -1797    476  -1736       C  
ATOM    351  CD  LYS A 378     -26.080  10.096   0.148  1.00 95.42           C  
ANISOU  351  CD  LYS A 378    14108  14147   7999  -1778    562  -1681       C  
ATOM    352  CE  LYS A 378     -27.366  10.795  -0.209  1.00124.38           C  
ANISOU  352  CE  LYS A 378    17761  17874  11625  -1644    572  -1768       C  
ATOM    353  NZ  LYS A 378     -28.530   9.880  -0.293  1.00137.92           N  
ANISOU  353  NZ  LYS A 378    19396  19798  13211  -1610    647  -1779       N  
ATOM    354  N   CYS A 379     -22.494  12.036   2.973  1.00 97.76           N  
ANISOU  354  N   CYS A 379    14521  14190   8433  -2057    354  -1761       N  
ATOM    355  CA  CYS A 379     -21.355  11.209   3.341  1.00 86.93           C  
ANISOU  355  CA  CYS A 379    13126  12872   7031  -2144    346  -1718       C  
ATOM    356  C   CYS A 379     -21.754  10.212   4.418  1.00 77.93           C  
ANISOU  356  C   CYS A 379    11943  11938   5729  -2099    391  -1718       C  
ATOM    357  O   CYS A 379     -22.610  10.493   5.256  1.00 78.76           O  
ANISOU  357  O   CYS A 379    12043  12136   5747  -2001    398  -1807       O  
ATOM    358  CB  CYS A 379     -20.176  12.067   3.800  1.00 80.79           C  
ANISOU  358  CB  CYS A 379    12380  11995   6321  -2181    258  -1826       C  
ATOM    359  SG  CYS A 379     -19.108  12.601   2.441  1.00125.44           S  
ANISOU  359  SG  CYS A 379    18068  17429  12163  -2302    229  -1754       S  
ATOM    360  N   TYR A 380     -21.144   9.033   4.369  1.00 77.05           N  
ANISOU  360  N   TYR A 380    11802  11896   5578  -2170    425  -1611       N  
ATOM    361  CA  TYR A 380     -21.452   7.966   5.306  1.00 78.44           C  
ANISOU  361  CA  TYR A 380    11944  12254   5604  -2136    481  -1580       C  
ATOM    362  C   TYR A 380     -20.176   7.419   5.941  1.00100.36           C  
ANISOU  362  C   TYR A 380    14717  15080   8334  -2178    447  -1571       C  
ATOM    363  O   TYR A 380     -19.379   6.751   5.279  1.00 95.88           O  
ANISOU  363  O   TYR A 380    14141  14471   7816  -2266    455  -1468       O  
ATOM    364  CB  TYR A 380     -22.213   6.837   4.605  1.00 75.97           C  
ANISOU  364  CB  TYR A 380    11595  11997   5272  -2166    582  -1441       C  
ATOM    365  CG  TYR A 380     -23.614   7.192   4.150  1.00 93.36           C  
ANISOU  365  CG  TYR A 380    13783  14205   7486  -2107    626  -1457       C  
ATOM    366  CD1 TYR A 380     -23.837   7.798   2.918  1.00 91.64           C  
ANISOU  366  CD1 TYR A 380    13577  13854   7387  -2125    610  -1436       C  
ATOM    367  CD2 TYR A 380     -24.716   6.898   4.941  1.00 96.59           C  
ANISOU  367  CD2 TYR A 380    14160  14760   7779  -2029    686  -1489       C  
ATOM    368  CE1 TYR A 380     -25.120   8.114   2.497  1.00 89.05           C  
ANISOU  368  CE1 TYR A 380    13231  13544   7061  -2059    646  -1454       C  
ATOM    369  CE2 TYR A 380     -26.001   7.208   4.527  1.00 93.61           C  
ANISOU  369  CE2 TYR A 380    13758  14401   7409  -1973    724  -1511       C  
ATOM    370  CZ  TYR A 380     -26.197   7.816   3.306  1.00 97.28           C  
ANISOU  370  CZ  TYR A 380    14235  14737   7991  -1984    701  -1497       C  
ATOM    371  OH  TYR A 380     -27.473   8.126   2.897  1.00102.81           O  
ANISOU  371  OH  TYR A 380    14905  15467   8689  -1916    734  -1524       O  
ATOM    372  N   GLY A 381     -19.992   7.709   7.227  1.00106.91           N  
ANISOU  372  N   GLY A 381    15549  16007   9064  -2108    406  -1683       N  
ATOM    373  CA  GLY A 381     -18.848   7.228   7.982  1.00 98.87           C  
ANISOU  373  CA  GLY A 381    14524  15065   7979  -2122    368  -1692       C  
ATOM    374  C   GLY A 381     -17.655   8.161   7.915  1.00 94.52           C  
ANISOU  374  C   GLY A 381    13985  14402   7528  -2169    261  -1796       C  
ATOM    375  O   GLY A 381     -16.584   7.850   8.438  1.00 90.34           O  
ANISOU  375  O   GLY A 381    13440  13927   6958  -2188    217  -1816       O  
ATOM    376  N   VAL A 382     -17.834   9.304   7.258  1.00 98.77           N  
ANISOU  376  N   VAL A 382    14548  14780   8199  -2188    224  -1862       N  
ATOM    377  CA  VAL A 382     -16.769  10.297   7.123  1.00107.78           C  
ANISOU  377  CA  VAL A 382    15703  15788   9459  -2245    132  -1965       C  
ATOM    378  C   VAL A 382     -17.344  11.706   7.319  1.00123.90           C  
ANISOU  378  C   VAL A 382    17780  17732  11564  -2186     86  -2116       C  
ATOM    379  O   VAL A 382     -18.531  11.929   7.086  1.00139.02           O  
ANISOU  379  O   VAL A 382    19713  19639  13470  -2123    130  -2103       O  
ATOM    380  CB  VAL A 382     -16.076  10.214   5.736  1.00100.67           C  
ANISOU  380  CB  VAL A 382    14806  14735   8708  -2369    140  -1852       C  
ATOM    381  CG1 VAL A 382     -14.755  10.968   5.747  1.00110.26           C  
ANISOU  381  CG1 VAL A 382    16018  15848  10027  -2444     54  -1947       C  
ATOM    382  CG2 VAL A 382     -15.824   8.770   5.334  1.00 99.25           C  
ANISOU  382  CG2 VAL A 382    14596  14641   8473  -2415    202  -1686       C  
ATOM    383  N   SER A 383     -16.510  12.653   7.744  1.00123.27           N  
ANISOU  383  N   SER A 383    17709  17578  11551  -2205     -2  -2264       N  
ATOM    384  CA  SER A 383     -16.951  14.037   7.922  1.00144.47           C  
ANISOU  384  CA  SER A 383    20433  20145  14313  -2154    -49  -2417       C  
ATOM    385  C   SER A 383     -16.826  14.847   6.628  1.00163.50           C  
ANISOU  385  C   SER A 383    22888  22316  16917  -2232    -49  -2372       C  
ATOM    386  O   SER A 383     -15.759  14.878   6.013  1.00170.76           O  
ANISOU  386  O   SER A 383    23803  23134  17944  -2347    -69  -2332       O  
ATOM    387  CB  SER A 383     -16.153  14.714   9.038  1.00150.18           C  
ANISOU  387  CB  SER A 383    21143  20898  15022  -2135   -144  -2617       C  
ATOM    388  OG  SER A 383     -14.764  14.661   8.769  1.00151.82           O  
ANISOU  388  OG  SER A 383    21325  21045  15313  -2252   -189  -2617       O  
ATOM    389  N   PRO A 384     -17.915  15.525   6.227  1.00171.81           N  
ANISOU  389  N   PRO A 384    23986  23284  18012  -2164    -25  -2381       N  
ATOM    390  CA  PRO A 384     -17.998  16.324   4.996  1.00155.82           C  
ANISOU  390  CA  PRO A 384    22014  21037  16154  -2209    -15  -2327       C  
ATOM    391  C   PRO A 384     -16.942  17.421   4.891  1.00140.91           C  
ANISOU  391  C   PRO A 384    20156  18956  14426  -2290    -83  -2430       C  
ATOM    392  O   PRO A 384     -16.324  17.569   3.838  1.00132.24           O  
ANISOU  392  O   PRO A 384    19076  17710  13457  -2393    -68  -2334       O  
ATOM    393  CB  PRO A 384     -19.400  16.945   5.071  1.00164.86           C  
ANISOU  393  CB  PRO A 384    23196  22171  17273  -2078      3  -2377       C  
ATOM    394  CG  PRO A 384     -19.789  16.856   6.507  1.00180.10           C  
ANISOU  394  CG  PRO A 384    25096  24278  19055  -1977    -23  -2516       C  
ATOM    395  CD  PRO A 384     -19.166  15.591   7.000  1.00181.68           C  
ANISOU  395  CD  PRO A 384    25236  24658  19138  -2025     -6  -2450       C  
ATOM    396  N   THR A 385     -16.745  18.186   5.959  1.00133.59           N  
ANISOU  396  N   THR A 385    19234  18032  13493  -2246   -152  -2626       N  
ATOM    397  CA  THR A 385     -15.862  19.340   5.884  1.00128.56           C  
ANISOU  397  CA  THR A 385    18628  17194  13024  -2321   -213  -2746       C  
ATOM    398  C   THR A 385     -14.404  18.934   6.070  1.00136.92           C  
ANISOU  398  C   THR A 385    19629  18286  14108  -2446   -251  -2763       C  
ATOM    399  O   THR A 385     -13.509  19.525   5.469  1.00146.19           O  
ANISOU  399  O   THR A 385    20816  19285  15444  -2562   -268  -2769       O  
ATOM    400  CB  THR A 385     -16.236  20.400   6.944  1.00109.39           C  
ANISOU  400  CB  THR A 385    16225  14744  10593  -2223   -278  -2973       C  
ATOM    401  OG1 THR A 385     -17.646  20.648   6.902  1.00 93.54           O  
ANISOU  401  OG1 THR A 385    14260  12751   8531  -2089   -244  -2963       O  
ATOM    402  CG2 THR A 385     -15.478  21.703   6.696  1.00107.61           C  
ANISOU  402  CG2 THR A 385    16047  14268  10574  -2304   -329  -3090       C  
ATOM    403  N   LYS A 386     -14.169  17.910   6.883  1.00130.56           N  
ANISOU  403  N   LYS A 386    18759  17709  13140  -2420   -260  -2765       N  
ATOM    404  CA  LYS A 386     -12.806  17.487   7.178  1.00126.51           C  
ANISOU  404  CA  LYS A 386    18183  17257  12629  -2516   -304  -2795       C  
ATOM    405  C   LYS A 386     -12.354  16.381   6.230  1.00122.57           C  
ANISOU  405  C   LYS A 386    17656  16790  12126  -2603   -245  -2585       C  
ATOM    406  O   LYS A 386     -11.471  15.590   6.563  1.00124.05           O  
ANISOU  406  O   LYS A 386    17783  17103  12247  -2645   -264  -2569       O  
ATOM    407  CB  LYS A 386     -12.675  17.030   8.632  1.00130.09           C  
ANISOU  407  CB  LYS A 386    18582  17942  12904  -2429   -354  -2922       C  
ATOM    408  CG  LYS A 386     -13.067  18.088   9.658  1.00138.86           C  
ANISOU  408  CG  LYS A 386    19711  19046  14003  -2335   -419  -3150       C  
ATOM    409  CD  LYS A 386     -12.420  19.435   9.359  1.00143.29           C  
ANISOU  409  CD  LYS A 386    20300  19369  14776  -2423   -475  -3288       C  
ATOM    410  CE  LYS A 386     -10.915  19.406   9.566  1.00147.35           C  
ANISOU  410  CE  LYS A 386    20747  19892  15348  -2541   -536  -3369       C  
ATOM    411  NZ  LYS A 386     -10.278  20.663   9.085  1.00153.08           N  
ANISOU  411  NZ  LYS A 386    21499  20360  16305  -2653   -570  -3475       N  
ATOM    412  N   LEU A 387     -12.974  16.326   5.055  1.00111.48           N  
ANISOU  412  N   LEU A 387    16294  15277  10787  -2620   -176  -2428       N  
ATOM    413  CA  LEU A 387     -12.554  15.400   4.012  1.00105.25           C  
ANISOU  413  CA  LEU A 387    15483  14492  10016  -2706   -120  -2235       C  
ATOM    414  C   LEU A 387     -11.133  15.700   3.569  1.00113.33           C  
ANISOU  414  C   LEU A 387    16479  15408  11173  -2847   -154  -2249       C  
ATOM    415  O   LEU A 387     -10.331  14.793   3.352  1.00113.61           O  
ANISOU  415  O   LEU A 387    16461  15530  11175  -2912   -146  -2165       O  
ATOM    416  CB  LEU A 387     -13.483  15.470   2.799  1.00106.18           C  
ANISOU  416  CB  LEU A 387    15651  14502  10190  -2692    -48  -2087       C  
ATOM    417  CG  LEU A 387     -14.879  14.860   2.884  1.00104.17           C  
ANISOU  417  CG  LEU A 387    15405  14368   9808  -2576      7  -2020       C  
ATOM    418  CD1 LEU A 387     -15.682  15.211   1.645  1.00 81.85           C  
ANISOU  418  CD1 LEU A 387    12627  11411   7063  -2563     61  -1908       C  
ATOM    419  CD2 LEU A 387     -14.780  13.356   3.046  1.00110.75           C  
ANISOU  419  CD2 LEU A 387    16181  15391  10506  -2581     47  -1910       C  
ATOM    420  N   ASN A 388     -10.835  16.989   3.456  1.00122.96           N  
ANISOU  420  N   ASN A 388    17735  16440  12546  -2892   -190  -2360       N  
ATOM    421  CA  ASN A 388      -9.578  17.462   2.893  1.00153.20           C  
ANISOU  421  CA  ASN A 388    21545  20131  16534  -3039   -208  -2371       C  
ATOM    422  C   ASN A 388      -8.339  16.965   3.641  1.00171.86           C  
ANISOU  422  C   ASN A 388    23818  22631  18849  -3098   -268  -2461       C  
ATOM    423  O   ASN A 388      -7.326  16.638   3.023  1.00196.58           O  
ANISOU  423  O   ASN A 388    26904  25742  22045  -3213   -259  -2391       O  
ATOM    424  CB  ASN A 388      -9.587  18.993   2.857  1.00158.42           C  
ANISOU  424  CB  ASN A 388    22265  20564  17363  -3064   -235  -2501       C  
ATOM    425  CG  ASN A 388      -8.640  19.559   1.820  1.00167.94           C  
ANISOU  425  CG  ASN A 388    23479  21570  18762  -3217   -213  -2443       C  
ATOM    426  OD1 ASN A 388      -8.379  18.931   0.794  1.00170.23           O  
ANISOU  426  OD1 ASN A 388    23757  21856  19067  -3279   -156  -2263       O  
ATOM    427  ND2 ASN A 388      -8.130  20.757   2.075  1.00171.43           N  
ANISOU  427  ND2 ASN A 388    23940  21841  19355  -3280   -254  -2598       N  
ATOM    428  N   ASP A 389      -8.417  16.922   4.965  1.00157.62           N  
ANISOU  428  N   ASP A 389    21985  20976  16928  -3013   -329  -2618       N  
ATOM    429  CA  ASP A 389      -7.277  16.528   5.792  1.00149.71           C  
ANISOU  429  CA  ASP A 389    20896  20120  15866  -3047   -396  -2727       C  
ATOM    430  C   ASP A 389      -7.068  15.013   5.892  1.00144.90           C  
ANISOU  430  C   ASP A 389    20237  19725  15093  -3016   -371  -2594       C  
ATOM    431  O   ASP A 389      -5.966  14.554   6.203  1.00144.23           O  
ANISOU  431  O   ASP A 389    20078  19743  14979  -3064   -414  -2630       O  
ATOM    432  CB  ASP A 389      -7.428  17.128   7.187  1.00144.95           C  
ANISOU  432  CB  ASP A 389    20281  19597  15195  -2956   -476  -2959       C  
ATOM    433  CG  ASP A 389      -7.324  18.639   7.175  1.00147.88           C  
ANISOU  433  CG  ASP A 389    20688  19750  15748  -3007   -515  -3124       C  
ATOM    434  OD1 ASP A 389      -6.471  19.168   6.431  1.00151.05           O  
ANISOU  434  OD1 ASP A 389    21080  19984  16327  -3149   -512  -3119       O  
ATOM    435  OD2 ASP A 389      -8.105  19.299   7.892  1.00152.26           O  
ANISOU  435  OD2 ASP A 389    21283  20297  16273  -2905   -543  -3256       O  
ATOM    436  N   LEU A 390      -8.119  14.240   5.636  1.00142.99           N  
ANISOU  436  N   LEU A 390    20033  19550  14747  -2935   -302  -2444       N  
ATOM    437  CA  LEU A 390      -8.069  12.786   5.799  1.00127.00           C  
ANISOU  437  CA  LEU A 390    17972  17718  12564  -2893   -270  -2317       C  
ATOM    438  C   LEU A 390      -7.434  12.074   4.598  1.00141.22           C  
ANISOU  438  C   LEU A 390    19751  19476  14430  -2998   -222  -2142       C  
ATOM    439  O   LEU A 390      -7.576  12.521   3.463  1.00156.72           O  
ANISOU  439  O   LEU A 390    21748  21270  16528  -3069   -181  -2059       O  
ATOM    440  CB  LEU A 390      -9.481  12.247   6.048  1.00108.16           C  
ANISOU  440  CB  LEU A 390    15629  15420  10047  -2771   -210  -2238       C  
ATOM    441  CG  LEU A 390      -9.629  10.747   6.291  1.00108.98           C  
ANISOU  441  CG  LEU A 390    15708  15713   9986  -2718   -162  -2105       C  
ATOM    442  CD1 LEU A 390      -8.741  10.301   7.440  1.00113.11           C  
ANISOU  442  CD1 LEU A 390    16177  16413  10388  -2680   -225  -2199       C  
ATOM    443  CD2 LEU A 390     -11.080  10.412   6.577  1.00115.30           C  
ANISOU  443  CD2 LEU A 390    16548  16582  10678  -2608    -99  -2053       C  
ATOM    444  N   CYS A 391      -6.749  10.958   4.855  1.00131.24           N  
ANISOU  444  N   CYS A 391    18433  18369  13063  -2996   -227  -2085       N  
ATOM    445  CA  CYS A 391      -6.035  10.221   3.808  1.00145.40           C  
ANISOU  445  CA  CYS A 391    20196  20142  14907  -3087   -191  -1936       C  
ATOM    446  C   CYS A 391      -6.441   8.744   3.722  1.00129.03           C  
ANISOU  446  C   CYS A 391    18122  18208  12695  -3026   -130  -1774       C  
ATOM    447  O   CYS A 391      -6.602   8.078   4.743  1.00127.97           O  
ANISOU  447  O   CYS A 391    17978  18239  12405  -2931   -141  -1798       O  
ATOM    448  CB  CYS A 391      -4.525  10.320   4.038  1.00172.32           C  
ANISOU  448  CB  CYS A 391    23527  23587  18358  -3168   -260  -2029       C  
ATOM    449  SG  CYS A 391      -3.902  12.003   4.250  1.00226.67           S  
ANISOU  449  SG  CYS A 391    30398  30313  25414  -3255   -333  -2242       S  
ATOM    450  N   PHE A 392      -6.577   8.235   2.496  1.00125.04           N  
ANISOU  450  N   PHE A 392    17628  17634  12248  -3082    -64  -1610       N  
ATOM    451  CA  PHE A 392      -6.972   6.843   2.266  1.00125.60           C  
ANISOU  451  CA  PHE A 392    17699  17810  12213  -3039      1  -1455       C  
ATOM    452  C   PHE A 392      -5.989   6.068   1.388  1.00138.23           C  
ANISOU  452  C   PHE A 392    19255  19413  13852  -3120     15  -1346       C  
ATOM    453  O   PHE A 392      -5.083   6.645   0.790  1.00137.10           O  
ANISOU  453  O   PHE A 392    19082  19182  13829  -3217    -14  -1372       O  
ATOM    454  CB  PHE A 392      -8.353   6.790   1.615  1.00116.51           C  
ANISOU  454  CB  PHE A 392    16602  16596  11072  -3005     77  -1358       C  
ATOM    455  CG  PHE A 392      -9.475   7.103   2.550  1.00116.65           C  
ANISOU  455  CG  PHE A 392    16655  16663  11002  -2900     82  -1433       C  
ATOM    456  CD1 PHE A 392      -9.941   6.148   3.435  1.00125.22           C  
ANISOU  456  CD1 PHE A 392    17739  17910  11929  -2810    109  -1407       C  
ATOM    457  CD2 PHE A 392     -10.068   8.354   2.544  1.00118.70           C  
ANISOU  457  CD2 PHE A 392    16953  16810  11339  -2887     63  -1527       C  
ATOM    458  CE1 PHE A 392     -10.981   6.432   4.294  1.00137.63           C  
ANISOU  458  CE1 PHE A 392    19339  19540  13416  -2713    119  -1475       C  
ATOM    459  CE2 PHE A 392     -11.109   8.645   3.402  1.00125.40           C  
ANISOU  459  CE2 PHE A 392    17830  17713  12103  -2784     67  -1602       C  
ATOM    460  CZ  PHE A 392     -11.566   7.684   4.278  1.00133.68           C  
ANISOU  460  CZ  PHE A 392    18869  18934  12989  -2698     96  -1577       C  
ATOM    461  N   THR A 393      -6.199   4.760   1.285  1.00129.67           N  
ANISOU  461  N   THR A 393    18168  18427  12673  -3080     66  -1221       N  
ATOM    462  CA  THR A 393      -5.392   3.929   0.396  1.00122.80           C  
ANISOU  462  CA  THR A 393    17261  17563  11834  -3143     86  -1109       C  
ATOM    463  C   THR A 393      -5.811   4.116  -1.056  1.00131.94           C  
ANISOU  463  C   THR A 393    18437  18587  13107  -3211    143  -1004       C  
ATOM    464  O   THR A 393      -5.062   4.675  -1.854  1.00146.86           O  
ANISOU  464  O   THR A 393    20302  20385  15113  -3303    128  -1003       O  
ATOM    465  CB  THR A 393      -5.487   2.438   0.764  1.00110.97           C  
ANISOU  465  CB  THR A 393    15760  16203  10200  -3073    124  -1012       C  
ATOM    466  OG1 THR A 393      -5.049   2.246   2.116  1.00126.67           O  
ANISOU  466  OG1 THR A 393    17733  18327  12067  -2997     72  -1101       O  
ATOM    467  CG2 THR A 393      -4.621   1.604  -0.168  1.00 71.80           C  
ANISOU  467  CG2 THR A 393    10760  11244   5276  -3133    141   -907       C  
ATOM    468  N   ASN A 394      -7.017   3.663  -1.390  1.00137.42           N  
ANISOU  468  N   ASN A 394    19171  19277  13767  -3164    211   -917       N  
ATOM    469  CA  ASN A 394      -7.545   3.798  -2.747  1.00122.18           C  
ANISOU  469  CA  ASN A 394    17256  17239  11928  -3208    265   -820       C  
ATOM    470  C   ASN A 394      -9.003   4.231  -2.749  1.00114.01           C  
ANISOU  470  C   ASN A 394    16270  16164  10884  -3147    303   -824       C  
ATOM    471  O   ASN A 394      -9.733   4.001  -1.783  1.00131.32           O  
ANISOU  471  O   ASN A 394    18481  18437  12979  -3068    311   -865       O  
ATOM    472  CB  ASN A 394      -7.419   2.485  -3.521  1.00109.52           C  
ANISOU  472  CB  ASN A 394    15629  15687  10299  -3222    317   -685       C  
ATOM    473  CG  ASN A 394      -5.984   2.063  -3.732  1.00114.62           C  
ANISOU  473  CG  ASN A 394    16221  16366  10962  -3281    283   -671       C  
ATOM    474  OD1 ASN A 394      -5.132   2.868  -4.107  1.00115.65           O  
ANISOU  474  OD1 ASN A 394    16328  16428  11186  -3355    245   -713       O  
ATOM    475  ND2 ASN A 394      -5.710   0.789  -3.494  1.00117.65           N  
ANISOU  475  ND2 ASN A 394    16586  16854  11260  -3248    300   -610       N  
ATOM    476  N   VAL A 395      -9.416   4.851  -3.849  1.00 86.81           N  
ANISOU  476  N   VAL A 395    12845  12602   7536  -3179    329   -780       N  
ATOM    477  CA  VAL A 395     -10.777   5.350  -3.999  1.00 83.91           C  
ANISOU  477  CA  VAL A 395    12521  12192   7170  -3119    362   -784       C  
ATOM    478  C   VAL A 395     -11.389   4.806  -5.287  1.00 84.23           C  
ANISOU  478  C   VAL A 395    12557  12214   7235  -3126    426   -660       C  
ATOM    479  O   VAL A 395     -10.677   4.568  -6.260  1.00105.69           O  
ANISOU  479  O   VAL A 395    15251  14896  10011  -3192    434   -585       O  
ATOM    480  CB  VAL A 395     -10.806   6.895  -4.023  1.00 80.71           C  
ANISOU  480  CB  VAL A 395    12155  11651   6862  -3128    323   -872       C  
ATOM    481  CG1 VAL A 395     -12.235   7.420  -4.080  1.00 84.35           C  
ANISOU  481  CG1 VAL A 395    12660  12078   7312  -3046    352   -887       C  
ATOM    482  CG2 VAL A 395     -10.081   7.462  -2.814  1.00 77.72           C  
ANISOU  482  CG2 VAL A 395    11770  11288   6472  -3131    253  -1012       C  
ATOM    483  N   TYR A 396     -12.703   4.603  -5.293  1.00 69.56           N  
ANISOU  483  N   TYR A 396    10713  10388   5328  -3057    470   -646       N  
ATOM    484  CA  TYR A 396     -13.381   4.086  -6.473  1.00 80.29           C  
ANISOU  484  CA  TYR A 396    12058  11744   6703  -3055    527   -546       C  
ATOM    485  C   TYR A 396     -14.616   4.912  -6.832  1.00103.92           C  
ANISOU  485  C   TYR A 396    15082  14685   9717  -2991    544   -567       C  
ATOM    486  O   TYR A 396     -15.644   4.849  -6.156  1.00107.72           O  
ANISOU  486  O   TYR A 396    15569  15227  10132  -2921    563   -614       O  
ATOM    487  CB  TYR A 396     -13.757   2.621  -6.268  1.00 67.45           C  
ANISOU  487  CB  TYR A 396    10399  10239   4991  -3039    578   -492       C  
ATOM    488  CG  TYR A 396     -12.568   1.685  -6.215  1.00 75.32           C  
ANISOU  488  CG  TYR A 396    11365  11281   5972  -3094    569   -446       C  
ATOM    489  CD1 TYR A 396     -11.850   1.382  -7.366  1.00103.10           C  
ANISOU  489  CD1 TYR A 396    14858  14765   9553  -3156    574   -369       C  
ATOM    490  CD2 TYR A 396     -12.169   1.101  -5.025  1.00 83.99           C  
ANISOU  490  CD2 TYR A 396    12460  12465   6987  -3074    556   -478       C  
ATOM    491  CE1 TYR A 396     -10.762   0.526  -7.328  1.00115.37           C  
ANISOU  491  CE1 TYR A 396    16380  16364  11091  -3198    564   -331       C  
ATOM    492  CE2 TYR A 396     -11.084   0.243  -4.977  1.00 92.99           C  
ANISOU  492  CE2 TYR A 396    13573  13649   8108  -3110    545   -436       C  
ATOM    493  CZ  TYR A 396     -10.385  -0.041  -6.130  1.00105.99           C  
ANISOU  493  CZ  TYR A 396    15192  15257   9822  -3173    548   -366       C  
ATOM    494  OH  TYR A 396      -9.304  -0.895  -6.091  1.00101.64           O  
ANISOU  494  OH  TYR A 396    14613  14756   9252  -3201    536   -328       O  
ATOM    495  N   ALA A 397     -14.495   5.688  -7.907  1.00118.78           N  
ANISOU  495  N   ALA A 397    16984  16459  11689  -3011    541   -529       N  
ATOM    496  CA  ALA A 397     -15.580   6.537  -8.389  1.00109.85           C  
ANISOU  496  CA  ALA A 397    15887  15269  10582  -2941    554   -538       C  
ATOM    497  C   ALA A 397     -16.507   5.777  -9.328  1.00103.03           C  
ANISOU  497  C   ALA A 397    14988  14472   9686  -2907    608   -462       C  
ATOM    498  O   ALA A 397     -16.058   5.143 -10.280  1.00123.40           O  
ANISOU  498  O   ALA A 397    17537  17063  12286  -2954    630   -376       O  
ATOM    499  CB  ALA A 397     -15.019   7.767  -9.086  1.00107.66           C  
ANISOU  499  CB  ALA A 397    15655  14837  10414  -2970    529   -526       C  
ATOM    500  N   ASP A 398     -17.803   5.844  -9.047  1.00 85.35           N  
ANISOU  500  N   ASP A 398    12749  12284   7396  -2822    630   -504       N  
ATOM    501  CA  ASP A 398     -18.809   5.189  -9.872  1.00 89.86           C  
ANISOU  501  CA  ASP A 398    13277  12929   7936  -2783    680   -455       C  
ATOM    502  C   ASP A 398     -19.662   6.226 -10.598  1.00 92.71           C  
ANISOU  502  C   ASP A 398    13669  13229   8328  -2701    676   -460       C  
ATOM    503  O   ASP A 398     -20.255   7.098  -9.970  1.00 79.81           O  
ANISOU  503  O   ASP A 398    12072  11565   6687  -2633    656   -537       O  
ATOM    504  CB  ASP A 398     -19.679   4.275  -9.010  1.00102.38           C  
ANISOU  504  CB  ASP A 398    14823  14644   9432  -2753    718   -496       C  
ATOM    505  CG  ASP A 398     -18.860   3.259  -8.229  1.00106.07           C  
ANISOU  505  CG  ASP A 398    15272  15168   9861  -2818    725   -483       C  
ATOM    506  OD1 ASP A 398     -17.740   2.927  -8.677  1.00105.58           O  
ANISOU  506  OD1 ASP A 398    15205  15072   9838  -2889    710   -426       O  
ATOM    507  OD2 ASP A 398     -19.327   2.804  -7.162  1.00 96.09           O  
ANISOU  507  OD2 ASP A 398    13999  13986   8524  -2793    746   -527       O  
ATOM    508  N   SER A 399     -19.705   6.145 -11.923  1.00141.72           N  
ANISOU  508  N   SER A 399    19860  19422  14565  -2700    694   -380       N  
ATOM    509  CA  SER A 399     -20.430   7.130 -12.720  1.00151.94           C  
ANISOU  509  CA  SER A 399    21187  20658  15884  -2612    691   -369       C  
ATOM    510  C   SER A 399     -21.698   6.557 -13.342  1.00141.03           C  
ANISOU  510  C   SER A 399    19745  19394  14445  -2538    727   -365       C  
ATOM    511  O   SER A 399     -21.654   5.535 -14.027  1.00145.48           O  
ANISOU  511  O   SER A 399    20247  20037  14991  -2574    757   -315       O  
ATOM    512  CB  SER A 399     -19.529   7.692 -13.824  1.00170.11           C  
ANISOU  512  CB  SER A 399    23524  22848  18261  -2648    682   -278       C  
ATOM    513  OG  SER A 399     -18.304   8.162 -13.295  1.00180.94           O  
ANISOU  513  OG  SER A 399    24936  24117  19694  -2731    652   -287       O  
ATOM    514  N   PHE A 400     -22.827   7.219 -13.095  1.00 89.82           N  
ANISOU  514  N   PHE A 400    13273  12924   7932  -2432    723   -429       N  
ATOM    515  CA  PHE A 400     -24.096   6.826 -13.698  1.00 76.52           C  
ANISOU  515  CA  PHE A 400    11526  11355   6195  -2351    753   -441       C  
ATOM    516  C   PHE A 400     -25.151   7.912 -13.516  1.00 72.29           C  
ANISOU  516  C   PHE A 400    11024  10802   5642  -2220    736   -506       C  
ATOM    517  O   PHE A 400     -24.908   8.926 -12.859  1.00 70.81           O  
ANISOU  517  O   PHE A 400    10912  10507   5486  -2195    702   -545       O  
ATOM    518  CB  PHE A 400     -24.602   5.512 -13.115  1.00 85.27           C  
ANISOU  518  CB  PHE A 400    12549  12606   7242  -2391    795   -480       C  
ATOM    519  CG  PHE A 400     -24.724   5.521 -11.628  1.00111.45           C  
ANISOU  519  CG  PHE A 400    15880  15942  10525  -2399    794   -558       C  
ATOM    520  CD1 PHE A 400     -23.634   5.237 -10.825  1.00114.26           C  
ANISOU  520  CD1 PHE A 400    16264  16256  10892  -2487    782   -550       C  
ATOM    521  CD2 PHE A 400     -25.936   5.818 -11.030  1.00112.78           C  
ANISOU  521  CD2 PHE A 400    16029  16180  10641  -2311    805   -644       C  
ATOM    522  CE1 PHE A 400     -23.752   5.248  -9.453  1.00102.95           C  
ANISOU  522  CE1 PHE A 400    14845  14856   9416  -2482    780   -622       C  
ATOM    523  CE2 PHE A 400     -26.060   5.830  -9.661  1.00114.81           C  
ANISOU  523  CE2 PHE A 400    16298  16467  10857  -2311    807   -715       C  
ATOM    524  CZ  PHE A 400     -24.967   5.545  -8.870  1.00114.93           C  
ANISOU  524  CZ  PHE A 400    16346  16444  10880  -2394    794   -703       C  
ATOM    525  N   VAL A 401     -26.323   7.682 -14.100  1.00 70.17           N  
ANISOU  525  N   VAL A 401    10694  10643   5325  -2133    756   -525       N  
ATOM    526  CA  VAL A 401     -27.400   8.667 -14.125  1.00 90.13           C  
ANISOU  526  CA  VAL A 401    13244  13171   7829  -1990    740   -581       C  
ATOM    527  C   VAL A 401     -28.747   8.009 -13.847  1.00 90.34           C  
ANISOU  527  C   VAL A 401    13172  13374   7780  -1934    772   -664       C  
ATOM    528  O   VAL A 401     -29.054   6.956 -14.403  1.00 97.46           O  
ANISOU  528  O   VAL A 401    13983  14392   8656  -1970    807   -649       O  
ATOM    529  CB  VAL A 401     -27.470   9.388 -15.492  1.00101.78           C  
ANISOU  529  CB  VAL A 401    14755  14589   9328  -1904    725   -505       C  
ATOM    530  CG1 VAL A 401     -28.735  10.221 -15.607  1.00100.87           C  
ANISOU  530  CG1 VAL A 401    14647  14508   9173  -1737    712   -565       C  
ATOM    531  CG2 VAL A 401     -26.239  10.252 -15.711  1.00106.21           C  
ANISOU  531  CG2 VAL A 401    15422  14960   9972  -1949    701   -428       C  
ATOM    532  N   ILE A 402     -29.544   8.621 -12.977  1.00 72.00           N  
ANISOU  532  N   ILE A 402    10862  11072   5425  -1850    762   -757       N  
ATOM    533  CA  ILE A 402     -30.866   8.090 -12.651  1.00 90.80           C  
ANISOU  533  CA  ILE A 402    13144  13623   7733  -1795    796   -843       C  
ATOM    534  C   ILE A 402     -31.935   9.177 -12.565  1.00 91.96           C  
ANISOU  534  C   ILE A 402    13308  13783   7848  -1631    771   -919       C  
ATOM    535  O   ILE A 402     -31.658  10.359 -12.784  1.00 86.11           O  
ANISOU  535  O   ILE A 402    12666  12906   7146  -1556    727   -900       O  
ATOM    536  CB  ILE A 402     -30.857   7.325 -11.315  1.00 94.03           C  
ANISOU  536  CB  ILE A 402    13518  14100   8108  -1878    832   -898       C  
ATOM    537  CG1 ILE A 402     -30.372   8.236 -10.190  1.00 97.95           C  
ANISOU  537  CG1 ILE A 402    14109  14491   8617  -1864    794   -942       C  
ATOM    538  CG2 ILE A 402     -29.986   6.088 -11.403  1.00 90.76           C  
ANISOU  538  CG2 ILE A 402    13072  13698   7713  -2025    865   -829       C  
ATOM    539  CD1 ILE A 402     -30.236   7.529  -8.868  1.00109.09           C  
ANISOU  539  CD1 ILE A 402    15496  15969   9984  -1938    825   -985       C  
ATOM    540  N   ARG A 403     -33.162   8.753 -12.275  1.00 87.09           N  
ANISOU  540  N   ARG A 403    12594  13331   7165  -1577    802  -1005       N  
ATOM    541  CA  ARG A 403     -34.282   9.664 -12.053  1.00 79.32           C  
ANISOU  541  CA  ARG A 403    11609  12391   6139  -1417    782  -1095       C  
ATOM    542  C   ARG A 403     -34.066  10.526 -10.806  1.00 95.60           C  
ANISOU  542  C   ARG A 403    13757  14362   8206  -1390    754  -1156       C  
ATOM    543  O   ARG A 403     -33.125  10.299 -10.044  1.00 95.03           O  
ANISOU  543  O   ARG A 403    13729  14218   8160  -1500    755  -1138       O  
ATOM    544  CB  ARG A 403     -35.587   8.880 -11.922  1.00 75.06           C  
ANISOU  544  CB  ARG A 403    10927  12065   5527  -1388    830  -1181       C  
ATOM    545  CG  ARG A 403     -36.807   9.650 -12.381  1.00 84.15           C  
ANISOU  545  CG  ARG A 403    12045  13296   6633  -1206    807  -1251       C  
ATOM    546  CD  ARG A 403     -38.090   9.023 -11.876  1.00105.14           C  
ANISOU  546  CD  ARG A 403    14565  16163   9221  -1182    856  -1363       C  
ATOM    547  NE  ARG A 403     -38.214   7.627 -12.279  1.00128.98           N  
ANISOU  547  NE  ARG A 403    17464  19303  12238  -1302    914  -1349       N  
ATOM    548  CZ  ARG A 403     -39.288   6.880 -12.048  1.00140.87           C  
ANISOU  548  CZ  ARG A 403    18832  20996  13698  -1310    970  -1437       C  
ATOM    549  NH1 ARG A 403     -40.333   7.398 -11.416  1.00136.50           N  
ANISOU  549  NH1 ARG A 403    18236  20541  13087  -1200    973  -1544       N  
ATOM    550  NH2 ARG A 403     -39.319   5.617 -12.449  1.00147.50           N  
ANISOU  550  NH2 ARG A 403    19571  21922  14552  -1430   1025  -1423       N  
ATOM    551  N   GLY A 404     -34.923  11.526 -10.612  1.00102.68           N  
ANISOU  551  N   GLY A 404    14676  15264   9075  -1236    726  -1234       N  
ATOM    552  CA  GLY A 404     -34.843  12.378  -9.438  1.00104.87           C  
ANISOU  552  CA  GLY A 404    15028  15466   9352  -1193    697  -1312       C  
ATOM    553  C   GLY A 404     -35.315  11.716  -8.155  1.00113.08           C  
ANISOU  553  C   GLY A 404    15994  16648  10322  -1234    738  -1402       C  
ATOM    554  O   GLY A 404     -34.744  11.931  -7.086  1.00117.13           O  
ANISOU  554  O   GLY A 404    16562  17104  10840  -1276    725  -1437       O  
ATOM    555  N   ASP A 405     -36.355  10.897  -8.267  1.00119.27           N  
ANISOU  555  N   ASP A 405    16651  17623  11042  -1221    790  -1440       N  
ATOM    556  CA  ASP A 405     -36.924  10.191  -7.122  1.00112.86           C  
ANISOU  556  CA  ASP A 405    15758  16963  10160  -1259    845  -1515       C  
ATOM    557  C   ASP A 405     -36.070   8.988  -6.755  1.00114.97           C  
ANISOU  557  C   ASP A 405    16007  17237  10439  -1436    893  -1445       C  
ATOM    558  O   ASP A 405     -36.166   8.456  -5.650  1.00 92.75           O  
ANISOU  558  O   ASP A 405    13162  14504   7574  -1486    937  -1482       O  
ATOM    559  CB  ASP A 405     -38.359   9.747  -7.411  1.00127.17           C  
ANISOU  559  CB  ASP A 405    17434  18977  11910  -1191    891  -1584       C  
ATOM    560  CG  ASP A 405     -39.340  10.904  -7.409  1.00134.51           C  
ANISOU  560  CG  ASP A 405    18370  19935  12803   -999    850  -1680       C  
ATOM    561  OD1 ASP A 405     -39.006  11.970  -6.848  1.00138.61           O  
ANISOU  561  OD1 ASP A 405    18997  20332  13336   -927    797  -1712       O  
ATOM    562  OD2 ASP A 405     -40.443  10.751  -7.976  1.00135.49           O  
ANISOU  562  OD2 ASP A 405    18389  20203  12885   -917    868  -1729       O  
ATOM    563  N   GLU A 406     -35.264   8.542  -7.712  1.00130.07           N  
ANISOU  563  N   GLU A 406    17936  19072  12412  -1522    888  -1342       N  
ATOM    564  CA  GLU A 406     -34.422   7.367  -7.529  1.00141.15           C  
ANISOU  564  CA  GLU A 406    19323  20477  13832  -1682    930  -1268       C  
ATOM    565  C   GLU A 406     -33.134   7.687  -6.774  1.00141.85           C  
ANISOU  565  C   GLU A 406    19518  20429  13951  -1746    894  -1236       C  
ATOM    566  O   GLU A 406     -32.436   6.780  -6.321  1.00137.84           O  
ANISOU  566  O   GLU A 406    19003  19929  13439  -1863    926  -1189       O  
ATOM    567  CB  GLU A 406     -34.088   6.746  -8.890  1.00139.42           C  
ANISOU  567  CB  GLU A 406    19071  20240  13662  -1742    937  -1179       C  
ATOM    568  N   VAL A 407     -32.829   8.975  -6.627  1.00111.74           N  
ANISOU  568  N   VAL A 407    15799  16490  10167  -1667    826  -1268       N  
ATOM    569  CA  VAL A 407     -31.647   9.403  -5.883  1.00102.14           C  
ANISOU  569  CA  VAL A 407    14676  15147   8983  -1720    784  -1263       C  
ATOM    570  C   VAL A 407     -31.735   8.993  -4.416  1.00101.06           C  
ANISOU  570  C   VAL A 407    14520  15106   8772  -1742    812  -1328       C  
ATOM    571  O   VAL A 407     -30.723   8.722  -3.766  1.00 88.07           O  
ANISOU  571  O   VAL A 407    12913  13417   7131  -1825    802  -1306       O  
ATOM    572  CB  VAL A 407     -31.453  10.935  -5.981  1.00 95.16           C  
ANISOU  572  CB  VAL A 407    13894  14108   8153  -1623    712  -1303       C  
ATOM    573  CG1 VAL A 407     -30.120  11.358  -5.387  1.00 75.75           C  
ANISOU  573  CG1 VAL A 407    11524  11508   5748  -1697    666  -1298       C  
ATOM    574  CG2 VAL A 407     -31.547  11.390  -7.430  1.00115.44           C  
ANISOU  574  CG2 VAL A 407    16484  16598  10780  -1576    694  -1234       C  
ATOM    575  N   ARG A 408     -32.962   8.919  -3.913  1.00107.32           N  
ANISOU  575  N   ARG A 408    15247  16042   9489  -1664    850  -1407       N  
ATOM    576  CA  ARG A 408     -33.227   8.490  -2.544  1.00 91.91           C  
ANISOU  576  CA  ARG A 408    13264  14208   7450  -1671    890  -1466       C  
ATOM    577  C   ARG A 408     -32.810   7.037  -2.305  1.00 96.04           C  
ANISOU  577  C   ARG A 408    13739  14804   7949  -1804    961  -1385       C  
ATOM    578  O   ARG A 408     -32.450   6.666  -1.188  1.00108.19           O  
ANISOU  578  O   ARG A 408    15289  16387   9429  -1836    982  -1396       O  
ATOM    579  CB  ARG A 408     -34.708   8.702  -2.218  1.00 77.03           C  
ANISOU  579  CB  ARG A 408    11306  12470   5492  -1558    924  -1563       C  
ATOM    580  CG  ARG A 408     -35.155  10.148  -2.446  1.00 78.03           C  
ANISOU  580  CG  ARG A 408    11485  12522   5640  -1410    854  -1645       C  
ATOM    581  CD  ARG A 408     -36.584  10.394  -2.017  1.00 81.62           C  
ANISOU  581  CD  ARG A 408    11866  13133   6015  -1288    882  -1753       C  
ATOM    582  NE  ARG A 408     -37.494   9.394  -2.560  1.00 93.32           N  
ANISOU  582  NE  ARG A 408    13222  14768   7466  -1318    959  -1730       N  
ATOM    583  CZ  ARG A 408     -38.816   9.449  -2.444  1.00112.02           C  
ANISOU  583  CZ  ARG A 408    15498  17292   9772  -1225    995  -1816       C  
ATOM    584  NH1 ARG A 408     -39.384  10.464  -1.808  1.00111.23           N  
ANISOU  584  NH1 ARG A 408    15422  17213   9628  -1086    958  -1925       N  
ATOM    585  NH2 ARG A 408     -39.570   8.493  -2.969  1.00121.31           N  
ANISOU  585  NH2 ARG A 408    16555  18605  10933  -1270   1066  -1800       N  
ATOM    586  N   GLN A 409     -32.866   6.224  -3.359  1.00 89.61           N  
ANISOU  586  N   GLN A 409    12873  14001   7175  -1871    998  -1307       N  
ATOM    587  CA  GLN A 409     -32.519   4.804  -3.278  1.00 90.87           C  
ANISOU  587  CA  GLN A 409    12986  14216   7324  -1995   1069  -1227       C  
ATOM    588  C   GLN A 409     -31.011   4.563  -3.204  1.00 80.48           C  
ANISOU  588  C   GLN A 409    11744  12784   6050  -2087   1034  -1148       C  
ATOM    589  O   GLN A 409     -30.572   3.457  -2.890  1.00 72.34           O  
ANISOU  589  O   GLN A 409    10696  11789   5002  -2178   1086  -1086       O  
ATOM    590  CB  GLN A 409     -33.104   4.040  -4.468  1.00 92.59           C  
ANISOU  590  CB  GLN A 409    13118  14485   7578  -2033   1115  -1187       C  
ATOM    591  CG  GLN A 409     -34.622   4.015  -4.511  1.00 94.97           C  
ANISOU  591  CG  GLN A 409    13320  14931   7833  -1961   1164  -1267       C  
ATOM    592  CD  GLN A 409     -35.158   2.837  -5.301  1.00110.60           C  
ANISOU  592  CD  GLN A 409    15193  16996   9834  -2036   1236  -1236       C  
ATOM    593  OE1 GLN A 409     -34.430   1.889  -5.594  1.00105.00           O  
ANISOU  593  OE1 GLN A 409    14486  16247   9163  -2148   1264  -1153       O  
ATOM    594  NE2 GLN A 409     -36.437   2.893  -5.652  1.00124.26           N  
ANISOU  594  NE2 GLN A 409    16826  18847  11541  -1972   1266  -1310       N  
ATOM    595  N   ILE A 410     -30.221   5.570  -3.562  1.00 90.69           N  
ANISOU  595  N   ILE A 410    13118  13937   7403  -2064    950  -1148       N  
ATOM    596  CA  ILE A 410     -28.768   5.447  -3.477  1.00116.54           C  
ANISOU  596  CA  ILE A 410    16455  17107  10719  -2148    912  -1087       C  
ATOM    597  C   ILE A 410     -28.301   5.700  -2.040  1.00127.32           C  
ANISOU  597  C   ILE A 410    17863  18487  12024  -2135    890  -1145       C  
ATOM    598  O   ILE A 410     -27.829   6.789  -1.702  1.00123.17           O  
ANISOU  598  O   ILE A 410    17403  17872  11523  -2092    818  -1205       O  
ATOM    599  CB  ILE A 410     -28.058   6.417  -4.439  1.00130.50           C  
ANISOU  599  CB  ILE A 410    18287  18715  12582  -2141    838  -1063       C  
ATOM    600  CG1 ILE A 410     -28.687   6.328  -5.826  1.00146.39           C  
ANISOU  600  CG1 ILE A 410    20257  20732  14634  -2120    855  -1019       C  
ATOM    601  CG2 ILE A 410     -26.570   6.101  -4.529  1.00130.05           C  
ANISOU  601  CG2 ILE A 410    18271  18567  12573  -2245    810   -991       C  
ATOM    602  CD1 ILE A 410     -28.531   4.968  -6.471  1.00161.91           C  
ANISOU  602  CD1 ILE A 410    22158  22756  16606  -2216    911   -935       C  
ATOM    603  N   ALA A 411     -28.447   4.680  -1.200  1.00112.49           N  
ANISOU  603  N   ALA A 411    15948  16725  10068  -2169    955  -1128       N  
ATOM    604  CA  ALA A 411     -28.067   4.754   0.203  1.00 82.99           C  
ANISOU  604  CA  ALA A 411    12243  13037   6252  -2148    945  -1175       C  
ATOM    605  C   ALA A 411     -28.024   3.345   0.788  1.00 94.52           C  
ANISOU  605  C   ALA A 411    13667  14605   7643  -2211   1031  -1104       C  
ATOM    606  O   ALA A 411     -28.663   2.438   0.260  1.00105.08           O  
ANISOU  606  O   ALA A 411    14943  15997   8986  -2253   1108  -1049       O  
ATOM    607  CB  ALA A 411     -29.048   5.630   0.970  1.00 84.24           C  
ANISOU  607  CB  ALA A 411    12397  13262   6349  -2032    936  -1295       C  
ATOM    608  N   PRO A 412     -27.274   3.151   1.884  1.00100.98           N  
ANISOU  608  N   PRO A 412    14520  15452   8394  -2214   1018  -1107       N  
ATOM    609  CA  PRO A 412     -27.246   1.829   2.521  1.00 77.54           C  
ANISOU  609  CA  PRO A 412    11528  12583   5350  -2259   1106  -1030       C  
ATOM    610  C   PRO A 412     -28.615   1.408   3.051  1.00 82.58           C  
ANISOU  610  C   PRO A 412    12107  13362   5910  -2220   1204  -1052       C  
ATOM    611  O   PRO A 412     -29.403   2.262   3.460  1.00 74.95           O  
ANISOU  611  O   PRO A 412    11129  12445   4905  -2132   1188  -1151       O  
ATOM    612  CB  PRO A 412     -26.256   2.015   3.672  1.00 74.00           C  
ANISOU  612  CB  PRO A 412    11134  12150   4831  -2234   1056  -1055       C  
ATOM    613  CG  PRO A 412     -25.389   3.142   3.246  1.00 79.56           C  
ANISOU  613  CG  PRO A 412    11886  12724   5619  -2231    941  -1112       C  
ATOM    614  CD  PRO A 412     -26.292   4.070   2.487  1.00101.43           C  
ANISOU  614  CD  PRO A 412    14643  15443   8452  -2185    923  -1172       C  
ATOM    615  N   GLY A 413     -28.890   0.107   3.014  1.00 98.82           N  
ANISOU  615  N   GLY A 413    14122  15476   7948  -2287   1306   -961       N  
ATOM    616  CA  GLY A 413     -30.124  -0.453   3.540  1.00103.23           C  
ANISOU  616  CA  GLY A 413    14618  16168   8436  -2271   1417   -968       C  
ATOM    617  C   GLY A 413     -31.405   0.039   2.895  1.00110.87           C  
ANISOU  617  C   GLY A 413    15515  17173   9437  -2234   1434  -1042       C  
ATOM    618  O   GLY A 413     -32.460   0.047   3.532  1.00106.44           O  
ANISOU  618  O   GLY A 413    14904  16735   8805  -2186   1499  -1093       O  
ATOM    619  N   GLN A 414     -31.319   0.425   1.623  1.00129.03           N  
ANISOU  619  N   GLN A 414    17806  19377  11841  -2252   1378  -1046       N  
ATOM    620  CA  GLN A 414     -32.481   0.877   0.860  1.00115.41           C  
ANISOU  620  CA  GLN A 414    16013  17687  10150  -2209   1386  -1112       C  
ATOM    621  C   GLN A 414     -33.061  -0.230  -0.007  1.00101.57           C  
ANISOU  621  C   GLN A 414    14176  15969   8448  -2295   1472  -1058       C  
ATOM    622  O   GLN A 414     -32.381  -1.204  -0.321  1.00 98.50           O  
ANISOU  622  O   GLN A 414    13797  15532   8098  -2390   1503   -965       O  
ATOM    623  CB  GLN A 414     -32.120   2.074  -0.023  1.00 93.53           C  
ANISOU  623  CB  GLN A 414    13286  14798   7454  -2158   1272  -1153       C  
ATOM    624  CG  GLN A 414     -31.883   3.352   0.740  1.00 93.49           C  
ANISOU  624  CG  GLN A 414    13348  14761   7413  -2059   1190  -1241       C  
ATOM    625  CD  GLN A 414     -33.128   3.821   1.463  1.00102.52           C  
ANISOU  625  CD  GLN A 414    14446  16032   8477  -1958   1221  -1344       C  
ATOM    626  OE1 GLN A 414     -33.184   3.810   2.690  1.00119.52           O  
ANISOU  626  OE1 GLN A 414    16609  18267  10536  -1924   1243  -1380       O  
ATOM    627  NE2 GLN A 414     -34.140   4.223   0.704  1.00 88.10           N  
ANISOU  627  NE2 GLN A 414    12563  14234   6677  -1904   1223  -1394       N  
ATOM    628  N   THR A 415     -34.325  -0.077  -0.380  1.00 97.81           N  
ANISOU  628  N   THR A 415    13612  15580   7971  -2256   1508  -1126       N  
ATOM    629  CA  THR A 415     -34.976  -1.034  -1.265  1.00111.50           C  
ANISOU  629  CA  THR A 415    15252  17355   9759  -2332   1583  -1102       C  
ATOM    630  C   THR A 415     -35.694  -0.327  -2.414  1.00107.89           C  
ANISOU  630  C   THR A 415    14738  16904   9350  -2269   1532  -1173       C  
ATOM    631  O   THR A 415     -35.971   0.871  -2.342  1.00 89.34           O  
ANISOU  631  O   THR A 415    12414  14552   6977  -2156   1461  -1247       O  
ATOM    632  CB  THR A 415     -35.970  -1.916  -0.494  1.00124.97           C  
ANISOU  632  CB  THR A 415    16874  19201  11407  -2369   1716  -1112       C  
ATOM    633  OG1 THR A 415     -36.485  -2.930  -1.365  1.00142.32           O  
ANISOU  633  OG1 THR A 415    18979  21422  13673  -2461   1790  -1091       O  
ATOM    634  CG2 THR A 415     -37.120  -1.079   0.039  1.00126.25           C  
ANISOU  634  CG2 THR A 415    16984  19484  11500  -2260   1721  -1226       C  
ATOM    635  N   GLY A 416     -35.996  -1.070  -3.476  1.00106.74           N  
ANISOU  635  N   GLY A 416    14518  16769   9269  -2335   1567  -1153       N  
ATOM    636  CA  GLY A 416     -36.622  -0.481  -4.648  1.00115.58           C  
ANISOU  636  CA  GLY A 416    15583  17905  10428  -2270   1517  -1213       C  
ATOM    637  C   GLY A 416     -36.054  -0.975  -5.964  1.00 98.82           C  
ANISOU  637  C   GLY A 416    13451  15707   8389  -2335   1492  -1153       C  
ATOM    638  O   GLY A 416     -35.101  -1.747  -5.987  1.00100.93           O  
ANISOU  638  O   GLY A 416    13761  15898   8691  -2432   1508  -1066       O  
ATOM    639  N   LYS A 417     -36.652  -0.537  -7.068  1.00 91.73           N  
ANISOU  639  N   LYS A 417    12496  14840   7518  -2272   1452  -1204       N  
ATOM    640  CA  LYS A 417     -36.247  -1.009  -8.390  1.00102.40           C  
ANISOU  640  CA  LYS A 417    13824  16146   8938  -2320   1431  -1159       C  
ATOM    641  C   LYS A 417     -34.789  -0.669  -8.698  1.00 99.28           C  
ANISOU  641  C   LYS A 417    13549  15592   8581  -2340   1356  -1065       C  
ATOM    642  O   LYS A 417     -34.093  -1.442  -9.355  1.00107.02           O  
ANISOU  642  O   LYS A 417    14529  16521   9613  -2426   1363   -998       O  
ATOM    643  CB  LYS A 417     -37.154  -0.407  -9.470  1.00107.08           C  
ANISOU  643  CB  LYS A 417    14341  16812   9533  -2218   1389  -1234       C  
ATOM    644  CG  LYS A 417     -38.617  -0.798  -9.350  1.00121.73           C  
ANISOU  644  CG  LYS A 417    16054  18840  11359  -2203   1460  -1340       C  
ATOM    645  CD  LYS A 417     -39.503   0.101 -10.200  1.00119.11           C  
ANISOU  645  CD  LYS A 417    15665  18586  11006  -2060   1401  -1424       C  
ATOM    646  CE  LYS A 417     -40.974  -0.247 -10.016  1.00125.04           C  
ANISOU  646  CE  LYS A 417    16263  19524  11723  -2041   1470  -1543       C  
ATOM    647  NZ  LYS A 417     -41.869   0.681 -10.762  1.00123.56           N  
ANISOU  647  NZ  LYS A 417    16019  19427  11501  -1881   1408  -1632       N  
ATOM    648  N   ILE A 418     -34.321   0.472  -8.196  1.00 84.60           N  
ANISOU  648  N   ILE A 418    11788  13656   6699  -2265   1287  -1065       N  
ATOM    649  CA  ILE A 418     -32.949   0.911  -8.455  1.00 80.88           C  
ANISOU  649  CA  ILE A 418    11427  13036   6269  -2284   1216   -986       C  
ATOM    650  C   ILE A 418     -31.932   0.222  -7.553  1.00 88.23           C  
ANISOU  650  C   ILE A 418    12413  13914   7195  -2382   1242   -922       C  
ATOM    651  O   ILE A 418     -30.893  -0.245  -8.017  1.00 81.22           O  
ANISOU  651  O   ILE A 418    11559  12947   6353  -2455   1226   -843       O  
ATOM    652  CB  ILE A 418     -32.790   2.434  -8.275  1.00 80.52           C  
ANISOU  652  CB  ILE A 418    11467  12912   6214  -2172   1133  -1018       C  
ATOM    653  CG1 ILE A 418     -33.709   3.190  -9.241  1.00 94.54           C  
ANISOU  653  CG1 ILE A 418    13203  14726   7991  -2056   1100  -1069       C  
ATOM    654  CG2 ILE A 418     -31.329   2.847  -8.466  1.00 70.43           C  
ANISOU  654  CG2 ILE A 418    10296  11478   4987  -2211   1069   -940       C  
ATOM    655  CD1 ILE A 418     -33.413   2.937 -10.694  1.00101.19           C  
ANISOU  655  CD1 ILE A 418    14023  15541   8884  -2074   1080  -1011       C  
ATOM    656  N   ALA A 419     -32.226   0.187  -6.259  1.00100.40           N  
ANISOU  656  N   ALA A 419    13964  15510   8675  -2372   1279   -956       N  
ATOM    657  CA  ALA A 419     -31.302  -0.367  -5.275  1.00 85.74           C  
ANISOU  657  CA  ALA A 419    12165  13617   6795  -2440   1299   -899       C  
ATOM    658  C   ALA A 419     -31.176  -1.885  -5.385  1.00102.90           C  
ANISOU  658  C   ALA A 419    14292  15820   8987  -2552   1385   -833       C  
ATOM    659  O   ALA A 419     -30.079  -2.430  -5.271  1.00103.81           O  
ANISOU  659  O   ALA A 419    14458  15865   9120  -2618   1379   -756       O  
ATOM    660  CB  ALA A 419     -31.739   0.021  -3.873  1.00 81.40           C  
ANISOU  660  CB  ALA A 419    11633  13135   6161  -2384   1319   -957       C  
ATOM    661  N   ASP A 420     -32.301  -2.565  -5.588  1.00108.08           N  
ANISOU  661  N   ASP A 420    14848  16576   9641  -2573   1466   -868       N  
ATOM    662  CA  ASP A 420     -32.315  -4.024  -5.600  1.00106.57           C  
ANISOU  662  CA  ASP A 420    14610  16408   9473  -2682   1561   -815       C  
ATOM    663  C   ASP A 420     -31.692  -4.629  -6.851  1.00 96.86           C  
ANISOU  663  C   ASP A 420    13367  15110   8326  -2748   1541   -763       C  
ATOM    664  O   ASP A 420     -30.955  -5.615  -6.767  1.00 88.16           O  
ANISOU  664  O   ASP A 420    12289  13959   7249  -2832   1577   -688       O  
ATOM    665  CB  ASP A 420     -33.750  -4.542  -5.467  1.00111.39           C  
ANISOU  665  CB  ASP A 420    15107  17147  10069  -2694   1658   -881       C  
ATOM    666  CG  ASP A 420     -34.432  -4.050  -4.211  1.00116.73           C  
ANISOU  666  CG  ASP A 420    15785  17909  10657  -2631   1691   -932       C  
ATOM    667  OD1 ASP A 420     -33.722  -3.658  -3.262  1.00123.71           O  
ANISOU  667  OD1 ASP A 420    16760  18756  11488  -2601   1661   -902       O  
ATOM    668  OD2 ASP A 420     -35.680  -4.051  -4.178  1.00117.01           O  
ANISOU  668  OD2 ASP A 420    15725  18060  10675  -2608   1746  -1011       O  
ATOM    669  N   TYR A 421     -31.979  -4.031  -8.005  1.00 95.50           N  
ANISOU  669  N   TYR A 421    13158  14937   8189  -2700   1483   -803       N  
ATOM    670  CA  TYR A 421     -31.677  -4.668  -9.286  1.00 85.41           C  
ANISOU  670  CA  TYR A 421    11840  13631   6980  -2754   1476   -774       C  
ATOM    671  C   TYR A 421     -30.611  -3.962 -10.128  1.00 89.34           C  
ANISOU  671  C   TYR A 421    12407  14029   7510  -2725   1378   -725       C  
ATOM    672  O   TYR A 421     -30.096  -4.535 -11.082  1.00 91.27           O  
ANISOU  672  O   TYR A 421    12633  14240   7804  -2773   1370   -685       O  
ATOM    673  CB  TYR A 421     -32.959  -4.793 -10.118  1.00 68.98           C  
ANISOU  673  CB  TYR A 421     9637  11658   4914  -2729   1504   -861       C  
ATOM    674  CG  TYR A 421     -34.114  -5.476  -9.409  1.00 77.26           C  
ANISOU  674  CG  TYR A 421    10598  12816   5942  -2766   1609   -920       C  
ATOM    675  CD1 TYR A 421     -33.982  -6.762  -8.895  1.00 95.46           C  
ANISOU  675  CD1 TYR A 421    12888  15112   8269  -2878   1705   -876       C  
ATOM    676  CD2 TYR A 421     -35.346  -4.844  -9.277  1.00 75.90           C  
ANISOU  676  CD2 TYR A 421    10354  12756   5729  -2686   1616  -1019       C  
ATOM    677  CE1 TYR A 421     -35.040  -7.393  -8.255  1.00 96.29           C  
ANISOU  677  CE1 TYR A 421    12913  15312   8361  -2920   1813   -924       C  
ATOM    678  CE2 TYR A 421     -36.408  -5.467  -8.641  1.00 97.80           C  
ANISOU  678  CE2 TYR A 421    13037  15637   8485  -2725   1719  -1075       C  
ATOM    679  CZ  TYR A 421     -36.249  -6.741  -8.132  1.00103.03           C  
ANISOU  679  CZ  TYR A 421    13689  16285   9175  -2848   1820  -1025       C  
ATOM    680  OH  TYR A 421     -37.299  -7.367  -7.497  1.00108.73           O  
ANISOU  680  OH  TYR A 421    14322  17108   9885  -2896   1934  -1074       O  
ATOM    681  N   ASN A 422     -30.279  -2.724  -9.783  1.00 98.07           N  
ANISOU  681  N   ASN A 422    13589  15085   8589  -2648   1307   -731       N  
ATOM    682  CA  ASN A 422     -29.314  -1.948 -10.561  1.00 78.59           C  
ANISOU  682  CA  ASN A 422    11187  12516   6157  -2622   1221   -684       C  
ATOM    683  C   ASN A 422     -28.017  -1.675  -9.798  1.00 85.28           C  
ANISOU  683  C   ASN A 422    12136  13264   7003  -2652   1182   -628       C  
ATOM    684  O   ASN A 422     -26.970  -2.220 -10.139  1.00 79.15           O  
ANISOU  684  O   ASN A 422    11384  12428   6261  -2720   1172   -558       O  
ATOM    685  CB  ASN A 422     -29.945  -0.630 -11.020  1.00 81.85           C  
ANISOU  685  CB  ASN A 422    11607  12934   6559  -2504   1165   -737       C  
ATOM    686  CG  ASN A 422     -31.132  -0.840 -11.950  1.00 88.88           C  
ANISOU  686  CG  ASN A 422    12392  13931   7449  -2460   1188   -794       C  
ATOM    687  OD1 ASN A 422     -31.011  -0.704 -13.167  1.00101.99           O  
ANISOU  687  OD1 ASN A 422    14034  15582   9137  -2436   1155   -773       O  
ATOM    688  ND2 ASN A 422     -32.282  -1.186 -11.379  1.00 74.43           N  
ANISOU  688  ND2 ASN A 422    10485  12213   5582  -2449   1248   -870       N  
ATOM    689  N   TYR A 423     -28.085  -0.818  -8.780  1.00 96.46           N  
ANISOU  689  N   TYR A 423    13605  14668   8377  -2597   1157   -668       N  
ATOM    690  CA  TYR A 423     -26.906  -0.463  -7.985  1.00 88.15           C  
ANISOU  690  CA  TYR A 423    12641  13534   7318  -2617   1113   -637       C  
ATOM    691  C   TYR A 423     -27.195  -0.539  -6.492  1.00 92.72           C  
ANISOU  691  C   TYR A 423    13235  14169   7824  -2601   1145   -677       C  
ATOM    692  O   TYR A 423     -28.153   0.066  -6.016  1.00111.89           O  
ANISOU  692  O   TYR A 423    15648  16653  10211  -2527   1152   -751       O  
ATOM    693  CB  TYR A 423     -26.424   0.940  -8.345  1.00 82.70           C  
ANISOU  693  CB  TYR A 423    12016  12745   6661  -2560   1027   -649       C  
ATOM    694  CG  TYR A 423     -25.089   1.309  -7.745  1.00 74.96           C  
ANISOU  694  CG  TYR A 423    11115  11674   5693  -2595    975   -623       C  
ATOM    695  CD1 TYR A 423     -23.936   0.621  -8.100  1.00 86.95           C  
ANISOU  695  CD1 TYR A 423    12642  13148   7246  -2678    970   -547       C  
ATOM    696  CD2 TYR A 423     -24.972   2.362  -6.848  1.00 74.59           C  
ANISOU  696  CD2 TYR A 423    11126  11590   5627  -2541    929   -685       C  
ATOM    697  CE1 TYR A 423     -22.706   0.956  -7.563  1.00 90.28           C  
ANISOU  697  CE1 TYR A 423    13124  13501   7679  -2710    920   -533       C  
ATOM    698  CE2 TYR A 423     -23.741   2.708  -6.306  1.00 80.52           C  
ANISOU  698  CE2 TYR A 423    11937  12264   6392  -2576    878   -677       C  
ATOM    699  CZ  TYR A 423     -22.611   2.001  -6.668  1.00 83.94           C  
ANISOU  699  CZ  TYR A 423    12372  12663   6857  -2661    874   -600       C  
ATOM    700  OH  TYR A 423     -21.383   2.334  -6.140  1.00 70.42           O  
ANISOU  700  OH  TYR A 423    10708  10889   5158  -2696    822   -601       O  
ATOM    701  N   LYS A 424     -26.370  -1.275  -5.751  1.00 99.83           N  
ANISOU  701  N   LYS A 424    14167  15063   8703  -2660   1165   -628       N  
ATOM    702  CA  LYS A 424     -26.630  -1.484  -4.324  1.00102.90           C  
ANISOU  702  CA  LYS A 424    14569  15520   9009  -2641   1204   -653       C  
ATOM    703  C   LYS A 424     -25.417  -1.177  -3.451  1.00 99.10           C  
ANISOU  703  C   LYS A 424    14164  14990   8499  -2642   1149   -640       C  
ATOM    704  O   LYS A 424     -24.298  -1.599  -3.752  1.00104.72           O  
ANISOU  704  O   LYS A 424    14902  15643   9245  -2699   1125   -576       O  
ATOM    705  CB  LYS A 424     -27.091  -2.923  -4.074  1.00103.61           C  
ANISOU  705  CB  LYS A 424    14607  15683   9075  -2702   1311   -608       C  
ATOM    706  CG  LYS A 424     -27.509  -3.198  -2.645  1.00117.89           C  
ANISOU  706  CG  LYS A 424    16425  17578  10792  -2677   1370   -624       C  
ATOM    707  CD  LYS A 424     -28.577  -2.217  -2.183  1.00141.01           C  
ANISOU  707  CD  LYS A 424    19332  20574  13673  -2588   1363   -723       C  
ATOM    708  CE  LYS A 424     -29.025  -2.517  -0.760  1.00148.45           C  
ANISOU  708  CE  LYS A 424    20276  21616  14512  -2560   1430   -737       C  
ATOM    709  NZ  LYS A 424     -29.994  -1.509  -0.251  1.00147.80           N  
ANISOU  709  NZ  LYS A 424    20175  21604  14378  -2464   1416   -842       N  
ATOM    710  N   LEU A 425     -25.657  -0.478  -2.344  1.00 89.62           N  
ANISOU  710  N   LEU A 425    12993  13829   7232  -2575   1131   -708       N  
ATOM    711  CA  LEU A 425     -24.595  -0.143  -1.404  1.00 87.35           C  
ANISOU  711  CA  LEU A 425    12767  13516   6906  -2565   1076   -718       C  
ATOM    712  C   LEU A 425     -24.705  -0.985  -0.144  1.00108.29           C  
ANISOU  712  C   LEU A 425    15420  16270   9455  -2558   1141   -698       C  
ATOM    713  O   LEU A 425     -25.807  -1.239   0.346  1.00117.13           O  
ANISOU  713  O   LEU A 425    16503  17482  10517  -2526   1213   -722       O  
ATOM    714  CB  LEU A 425     -24.641   1.344  -1.041  1.00 70.48           C  
ANISOU  714  CB  LEU A 425    10670  11342   4769  -2488    996   -820       C  
ATOM    715  CG  LEU A 425     -24.311   2.364  -2.128  1.00 70.22           C  
ANISOU  715  CG  LEU A 425    10659  11185   4836  -2487    923   -834       C  
ATOM    716  CD1 LEU A 425     -24.504   3.780  -1.620  1.00 71.12           C  
ANISOU  716  CD1 LEU A 425    10816  11260   4948  -2405    858   -941       C  
ATOM    717  CD2 LEU A 425     -22.880   2.160  -2.583  1.00 69.59           C  
ANISOU  717  CD2 LEU A 425    10609  11018   4815  -2563    879   -770       C  
ATOM    718  N   PRO A 426     -23.555  -1.401   0.403  1.00 89.26           N  
ANISOU  718  N   PRO A 426    13051  13849   7016  -2582   1117   -654       N  
ATOM    719  CA  PRO A 426     -23.553  -2.231   1.613  1.00108.68           C  
ANISOU  719  CA  PRO A 426    15522  16405   9368  -2564   1180   -620       C  
ATOM    720  C   PRO A 426     -23.946  -1.445   2.862  1.00109.89           C  
ANISOU  720  C   PRO A 426    15693  16639   9422  -2473   1160   -713       C  
ATOM    721  O   PRO A 426     -24.146  -0.230   2.798  1.00110.36           O  
ANISOU  721  O   PRO A 426    15760  16666   9505  -2425   1091   -810       O  
ATOM    722  CB  PRO A 426     -22.102  -2.719   1.694  1.00106.96           C  
ANISOU  722  CB  PRO A 426    15342  16144   9153  -2602   1138   -558       C  
ATOM    723  CG  PRO A 426     -21.313  -1.654   1.002  1.00 84.67           C  
ANISOU  723  CG  PRO A 426    12536  13220   6415  -2614   1029   -607       C  
ATOM    724  CD  PRO A 426     -22.194  -1.150  -0.106  1.00 69.69           C  
ANISOU  724  CD  PRO A 426    10606  11274   4601  -2623   1036   -630       C  
ATOM    725  N   ASP A 427     -24.066  -2.143   3.986  1.00111.04           N  
ANISOU  725  N   ASP A 427    15847  16887   9455  -2443   1224   -681       N  
ATOM    726  CA  ASP A 427     -24.428  -1.498   5.239  1.00122.09           C  
ANISOU  726  CA  ASP A 427    17260  18384  10744  -2349   1211   -766       C  
ATOM    727  C   ASP A 427     -23.209  -0.837   5.868  1.00109.31           C  
ANISOU  727  C   ASP A 427    15691  16749   9094  -2311   1103   -822       C  
ATOM    728  O   ASP A 427     -23.324   0.179   6.556  1.00107.43           O  
ANISOU  728  O   ASP A 427    15465  16544   8809  -2236   1043   -935       O  
ATOM    729  CB  ASP A 427     -25.048  -2.514   6.200  1.00141.40           C  
ANISOU  729  CB  ASP A 427    19695  20956  13073  -2328   1330   -703       C  
ATOM    730  CG  ASP A 427     -25.503  -1.884   7.502  1.00158.13           C  
ANISOU  730  CG  ASP A 427    21823  23197  15064  -2223   1326   -790       C  
ATOM    731  OD1 ASP A 427     -26.553  -1.208   7.497  1.00158.37           O  
ANISOU  731  OD1 ASP A 427    21818  23264  15093  -2182   1337   -873       O  
ATOM    732  OD2 ASP A 427     -24.815  -2.068   8.531  1.00164.67           O  
ANISOU  732  OD2 ASP A 427    22689  24091  15787  -2173   1310   -779       O  
ATOM    733  N   ASP A 428     -22.037  -1.401   5.596  1.00 88.85           N  
ANISOU  733  N   ASP A 428    13122  14107   6531  -2363   1074   -751       N  
ATOM    734  CA  ASP A 428     -20.790  -0.885   6.143  1.00102.80           C  
ANISOU  734  CA  ASP A 428    14922  15864   8272  -2337    972   -803       C  
ATOM    735  C   ASP A 428     -20.142   0.087   5.176  1.00109.03           C  
ANISOU  735  C   ASP A 428    15715  16518   9193  -2383    873   -859       C  
ATOM    736  O   ASP A 428     -18.923   0.265   5.180  1.00113.04           O  
ANISOU  736  O   ASP A 428    16239  16986   9725  -2406    797   -872       O  
ATOM    737  CB  ASP A 428     -19.825  -2.031   6.443  1.00112.95           C  
ANISOU  737  CB  ASP A 428    16228  17182   9507  -2357    993   -698       C  
ATOM    738  CG  ASP A 428     -19.417  -2.786   5.189  1.00112.76           C  
ANISOU  738  CG  ASP A 428    16192  17058   9594  -2454   1016   -596       C  
ATOM    739  OD1 ASP A 428     -20.181  -3.668   4.745  1.00110.79           O  
ANISOU  739  OD1 ASP A 428    15924  16809   9364  -2492   1116   -512       O  
ATOM    740  OD2 ASP A 428     -18.334  -2.487   4.643  1.00105.35           O  
ANISOU  740  OD2 ASP A 428    15259  16043   8726  -2494    934   -605       O  
ATOM    741  N   PHE A 429     -20.970   0.723   4.356  1.00120.30           N  
ANISOU  741  N   PHE A 429    17125  17879  10703  -2394    877   -892       N  
ATOM    742  CA  PHE A 429     -20.478   1.624   3.323  1.00127.75           C  
ANISOU  742  CA  PHE A 429    18077  18686  11777  -2438    801   -926       C  
ATOM    743  C   PHE A 429     -19.773   2.845   3.898  1.00137.77           C  
ANISOU  743  C   PHE A 429    19376  19917  13055  -2403    696  -1049       C  
ATOM    744  O   PHE A 429     -20.390   3.689   4.548  1.00145.22           O  
ANISOU  744  O   PHE A 429    20328  20889  13960  -2329    674  -1155       O  
ATOM    745  CB  PHE A 429     -21.624   2.073   2.418  1.00126.41           C  
ANISOU  745  CB  PHE A 429    17886  18469  11675  -2433    831   -937       C  
ATOM    746  CG  PHE A 429     -21.235   3.146   1.443  1.00122.63           C  
ANISOU  746  CG  PHE A 429    17425  17849  11318  -2458    757   -972       C  
ATOM    747  CD1 PHE A 429     -20.383   2.866   0.389  1.00111.99           C  
ANISOU  747  CD1 PHE A 429    16077  16412  10062  -2540    740   -895       C  
ATOM    748  CD2 PHE A 429     -21.723   4.435   1.577  1.00117.29           C  
ANISOU  748  CD2 PHE A 429    16770  17128  10666  -2394    709  -1080       C  
ATOM    749  CE1 PHE A 429     -20.021   3.854  -0.510  1.00 98.03           C  
ANISOU  749  CE1 PHE A 429    14329  14515   8404  -2563    682   -915       C  
ATOM    750  CE2 PHE A 429     -21.364   5.427   0.676  1.00 90.50           C  
ANISOU  750  CE2 PHE A 429    13403  13592   7390  -2415    650  -1101       C  
ATOM    751  CZ  PHE A 429     -20.515   5.133  -0.367  1.00 84.68           C  
ANISOU  751  CZ  PHE A 429    12665  12769   6739  -2502    640  -1014       C  
ATOM    752  N   THR A 430     -18.469   2.918   3.662  1.00128.91           N  
ANISOU  752  N   THR A 430    18264  18732  11985  -2458    632  -1041       N  
ATOM    753  CA  THR A 430     -17.677   4.070   4.059  1.00120.05           C  
ANISOU  753  CA  THR A 430    17162  17554  10897  -2447    531  -1161       C  
ATOM    754  C   THR A 430     -17.343   4.906   2.828  1.00111.03           C  
ANISOU  754  C   THR A 430    16030  16246   9910  -2514    490  -1163       C  
ATOM    755  O   THR A 430     -16.346   4.655   2.154  1.00101.92           O  
ANISOU  755  O   THR A 430    14869  15031   8826  -2592    468  -1106       O  
ATOM    756  CB  THR A 430     -16.380   3.644   4.765  1.00128.21           C  
ANISOU  756  CB  THR A 430    18192  18646  11876  -2460    483  -1168       C  
ATOM    757  OG1 THR A 430     -15.584   2.854   3.873  1.00132.53           O  
ANISOU  757  OG1 THR A 430    18725  19147  12482  -2544    497  -1055       O  
ATOM    758  CG2 THR A 430     -16.698   2.830   6.014  1.00130.87           C  
ANISOU  758  CG2 THR A 430    18527  19151  12047  -2380    528  -1156       C  
ATOM    759  N   GLY A 431     -18.190   5.886   2.527  1.00106.57           N  
ANISOU  759  N   GLY A 431    15482  15613   9396  -2476    483  -1224       N  
ATOM    760  CA  GLY A 431     -17.997   6.721   1.357  1.00 97.09           C  
ANISOU  760  CA  GLY A 431    14301  14253   8337  -2524    454  -1215       C  
ATOM    761  C   GLY A 431     -18.907   7.935   1.295  1.00104.39           C  
ANISOU  761  C   GLY A 431    15256  15106   9301  -2456    436  -1304       C  
ATOM    762  O   GLY A 431     -19.344   8.443   2.325  1.00112.90           O  
ANISOU  762  O   GLY A 431    16344  16239  10314  -2377    414  -1415       O  
ATOM    763  N   CYS A 432     -19.187   8.405   0.082  1.00 98.71           N  
ANISOU  763  N   CYS A 432    14551  14269   8684  -2476    445  -1254       N  
ATOM    764  CA  CYS A 432     -20.030   9.584  -0.110  1.00 88.52           C  
ANISOU  764  CA  CYS A 432    13298  12896   7441  -2403    428  -1327       C  
ATOM    765  C   CYS A 432     -20.966   9.445  -1.309  1.00 83.90           C  
ANISOU  765  C   CYS A 432    12702  12287   6888  -2383    481  -1239       C  
ATOM    766  O   CYS A 432     -20.694   8.685  -2.238  1.00 74.72           O  
ANISOU  766  O   CYS A 432    11514  11122   5752  -2448    516  -1124       O  
ATOM    767  CB  CYS A 432     -19.165  10.833  -0.289  1.00 85.19           C  
ANISOU  767  CB  CYS A 432    12926  12304   7138  -2436    357  -1394       C  
ATOM    768  SG  CYS A 432     -18.194  11.314   1.159  1.00 97.63           S  
ANISOU  768  SG  CYS A 432    14508  13900   8686  -2442    278  -1546       S  
ATOM    769  N   VAL A 433     -22.051  10.213  -1.296  1.00 74.72           N  
ANISOU  769  N   VAL A 433    11558  11111   5721  -2286    482  -1301       N  
ATOM    770  CA  VAL A 433     -23.036  10.186  -2.374  1.00 74.32           C  
ANISOU  770  CA  VAL A 433    11495  11054   5691  -2245    525  -1237       C  
ATOM    771  C   VAL A 433     -23.294  11.587  -2.908  1.00 89.17           C  
ANISOU  771  C   VAL A 433    13437  12782   7660  -2183    485  -1280       C  
ATOM    772  O   VAL A 433     -23.815  12.453  -2.205  1.00 76.28           O  
ANISOU  772  O   VAL A 433    11836  11135   6012  -2095    455  -1393       O  
ATOM    773  CB  VAL A 433     -24.366   9.546  -1.915  1.00 74.28           C  
ANISOU  773  CB  VAL A 433    11433  11214   5575  -2171    583  -1258       C  
ATOM    774  CG1 VAL A 433     -25.491   9.856  -2.889  1.00 74.29           C  
ANISOU  774  CG1 VAL A 433    11421  11208   5597  -2100    609  -1237       C  
ATOM    775  CG2 VAL A 433     -24.194   8.047  -1.725  1.00 73.33           C  
ANISOU  775  CG2 VAL A 433    11255  11221   5387  -2242    642  -1179       C  
ATOM    776  N   ILE A 434     -22.949  11.785  -4.175  1.00 96.09           N  
ANISOU  776  N   ILE A 434    14334  13549   8626  -2222    489  -1185       N  
ATOM    777  CA  ILE A 434     -23.080  13.082  -4.815  1.00 85.54           C  
ANISOU  777  CA  ILE A 434    13069  12050   7383  -2168    459  -1198       C  
ATOM    778  C   ILE A 434     -24.003  12.988  -6.020  1.00 77.47           C  
ANISOU  778  C   ILE A 434    12031  11044   6359  -2105    498  -1116       C  
ATOM    779  O   ILE A 434     -23.894  12.063  -6.824  1.00 77.95           O  
ANISOU  779  O   ILE A 434    12044  11166   6409  -2159    537  -1013       O  
ATOM    780  CB  ILE A 434     -21.714  13.622  -5.267  1.00 75.91           C  
ANISOU  780  CB  ILE A 434    11899  10661   6282  -2269    427  -1159       C  
ATOM    781  CG1 ILE A 434     -20.771  13.767  -4.077  1.00 76.40           C  
ANISOU  781  CG1 ILE A 434    11967  10714   6348  -2328    380  -1258       C  
ATOM    782  CG2 ILE A 434     -21.875  14.941  -5.989  1.00 76.94           C  
ANISOU  782  CG2 ILE A 434    12110  10609   6514  -2214    410  -1154       C  
ATOM    783  CD1 ILE A 434     -19.363  14.125  -4.471  1.00 76.56           C  
ANISOU  783  CD1 ILE A 434    12014  10594   6480  -2445    353  -1225       C  
ATOM    784  N   ALA A 435     -24.921  13.940  -6.134  1.00 76.33           N  
ANISOU  784  N   ALA A 435    11925  10853   6222  -1982    486  -1168       N  
ATOM    785  CA  ALA A 435     -25.835  13.977  -7.264  1.00 85.73           C  
ANISOU  785  CA  ALA A 435    13103  12065   7406  -1900    515  -1102       C  
ATOM    786  C   ALA A 435     -26.299  15.398  -7.549  1.00 93.80           C  
ANISOU  786  C   ALA A 435    14210  12945   8484  -1781    484  -1140       C  
ATOM    787  O   ALA A 435     -26.685  16.128  -6.639  1.00 83.82           O  
ANISOU  787  O   ALA A 435    12979  11658   7209  -1707    453  -1258       O  
ATOM    788  CB  ALA A 435     -27.026  13.074  -7.006  1.00 79.01           C  
ANISOU  788  CB  ALA A 435    12160  11420   6441  -1845    557  -1130       C  
ATOM    789  N   TRP A 436     -26.258  15.787  -8.819  1.00104.02           N  
ANISOU  789  N   TRP A 436    15541  14145   9835  -1756    493  -1038       N  
ATOM    790  CA  TRP A 436     -26.706  17.115  -9.217  1.00 99.99           C  
ANISOU  790  CA  TRP A 436    15121  13490   9380  -1633    471  -1052       C  
ATOM    791  C   TRP A 436     -27.671  17.025 -10.386  1.00105.09           C  
ANISOU  791  C   TRP A 436    15743  14203   9984  -1521    498   -976       C  
ATOM    792  O   TRP A 436     -27.749  15.999 -11.063  1.00111.99           O  
ANISOU  792  O   TRP A 436    16539  15202  10812  -1564    532   -899       O  
ATOM    793  CB  TRP A 436     -25.515  18.011  -9.563  1.00 93.32           C  
ANISOU  793  CB  TRP A 436    14377  12412   8670  -1707    452  -1002       C  
ATOM    794  CG  TRP A 436     -24.703  17.578 -10.747  1.00 86.34           C  
ANISOU  794  CG  TRP A 436    13488  11487   7831  -1802    483   -848       C  
ATOM    795  CD1 TRP A 436     -24.820  18.028 -12.026  1.00 95.62           C  
ANISOU  795  CD1 TRP A 436    14709  12580   9043  -1745    504   -732       C  
ATOM    796  CD2 TRP A 436     -23.645  16.612 -10.757  1.00100.20           C  
ANISOU  796  CD2 TRP A 436    15188  13290   9592  -1960    496   -795       C  
ATOM    797  NE1 TRP A 436     -23.898  17.409 -12.832  1.00104.66           N  
ANISOU  797  NE1 TRP A 436    15828  13722  10216  -1862    531   -612       N  
ATOM    798  CE2 TRP A 436     -23.167  16.534 -12.077  1.00 97.84           C  
ANISOU  798  CE2 TRP A 436    14902  12936   9337  -1996    525   -651       C  
ATOM    799  CE3 TRP A 436     -23.057  15.809  -9.774  1.00120.94           C  
ANISOU  799  CE3 TRP A 436    17758  16007  12187  -2066    486   -854       C  
ATOM    800  CZ2 TRP A 436     -22.128  15.680 -12.442  1.00100.74           C  
ANISOU  800  CZ2 TRP A 436    15222  13335   9720  -2136    543   -572       C  
ATOM    801  CZ3 TRP A 436     -22.025  14.962 -10.140  1.00114.69           C  
ANISOU  801  CZ3 TRP A 436    16924  15242  11412  -2201    503   -772       C  
ATOM    802  CH2 TRP A 436     -21.571  14.906 -11.463  1.00104.54           C  
ANISOU  802  CH2 TRP A 436    15648  13899  10174  -2236    530   -636       C  
ATOM    803  N   ASN A 437     -28.428  18.096 -10.597  1.00105.16           N  
ANISOU  803  N   ASN A 437    15816  14134  10005  -1369    480  -1007       N  
ATOM    804  CA  ASN A 437     -29.427  18.128 -11.655  1.00 99.53           C  
ANISOU  804  CA  ASN A 437    15082  13494   9241  -1234    497   -951       C  
ATOM    805  C   ASN A 437     -28.805  18.310 -13.036  1.00106.91           C  
ANISOU  805  C   ASN A 437    16065  14320  10235  -1256    515   -793       C  
ATOM    806  O   ASN A 437     -27.951  19.178 -13.241  1.00 99.05           O  
ANISOU  806  O   ASN A 437    15176  13114   9345  -1292    507   -742       O  
ATOM    807  CB  ASN A 437     -30.445  19.232 -11.384  1.00 90.01           C  
ANISOU  807  CB  ASN A 437    13933  12245   8023  -1048    470  -1038       C  
ATOM    808  CG  ASN A 437     -31.531  19.288 -12.435  1.00 97.59           C  
ANISOU  808  CG  ASN A 437    14863  13298   8918   -889    482   -991       C  
ATOM    809  OD1 ASN A 437     -31.452  20.068 -13.386  1.00118.40           O  
ANISOU  809  OD1 ASN A 437    17584  15802  11600   -808    480   -900       O  
ATOM    810  ND2 ASN A 437     -32.549  18.451 -12.277  1.00 81.97           N  
ANISOU  810  ND2 ASN A 437    12762  11553   6832   -842    497  -1052       N  
ATOM    811  N   SER A 438     -29.240  17.480 -13.978  1.00113.06           N  
ANISOU  811  N   SER A 438    16762  15248  10947  -1236    543   -721       N  
ATOM    812  CA  SER A 438     -28.744  17.541 -15.346  1.00113.52           C  
ANISOU  812  CA  SER A 438    16852  15242  11039  -1243    564   -570       C  
ATOM    813  C   SER A 438     -29.884  17.578 -16.361  1.00114.06           C  
ANISOU  813  C   SER A 438    16885  15425  11026  -1072    571   -537       C  
ATOM    814  O   SER A 438     -29.712  17.187 -17.516  1.00113.44           O  
ANISOU  814  O   SER A 438    16781  15390  10930  -1072    593   -427       O  
ATOM    815  CB  SER A 438     -27.823  16.352 -15.618  1.00102.83           C  
ANISOU  815  CB  SER A 438    15425  13958   9687  -1416    590   -502       C  
ATOM    816  OG  SER A 438     -28.546  15.132 -15.633  1.00 95.90           O  
ANISOU  816  OG  SER A 438    14417  13308   8713  -1419    608   -540       O  
ATOM    817  N   ASN A 439     -31.041  18.064 -15.922  1.00107.53           N  
ANISOU  817  N   ASN A 439    16053  14656  10147   -918    550   -638       N  
ATOM    818  CA  ASN A 439     -32.210  18.193 -16.785  1.00116.02           C  
ANISOU  818  CA  ASN A 439    17091  15850  11139   -734    549   -628       C  
ATOM    819  C   ASN A 439     -31.946  19.114 -17.965  1.00133.37           C  
ANISOU  819  C   ASN A 439    19399  17899  13377   -635    551   -492       C  
ATOM    820  O   ASN A 439     -32.454  18.897 -19.063  1.00135.42           O  
ANISOU  820  O   ASN A 439    19617  18266  13570   -534    560   -426       O  
ATOM    821  CB  ASN A 439     -33.408  18.706 -15.989  1.00111.62           C  
ANISOU  821  CB  ASN A 439    16521  15360  10529   -583    523   -769       C  
ATOM    822  CG  ASN A 439     -34.591  19.043 -16.870  1.00119.00           C  
ANISOU  822  CG  ASN A 439    17430  16400  11383   -370    514   -763       C  
ATOM    823  OD1 ASN A 439     -35.180  18.165 -17.499  1.00124.25           O  
ANISOU  823  OD1 ASN A 439    17973  17269  11966   -349    529   -761       O  
ATOM    824  ND2 ASN A 439     -34.940  20.323 -16.931  1.00124.56           N  
ANISOU  824  ND2 ASN A 439    18249  16965  12111   -206    488   -766       N  
ATOM    825  N   ASN A 440     -31.155  20.152 -17.728  1.00132.64           N  
ANISOU  825  N   ASN A 440    19447  17558  13393   -661    545   -453       N  
ATOM    826  CA  ASN A 440     -30.783  21.087 -18.781  1.00135.17           C  
ANISOU  826  CA  ASN A 440    19889  17702  13766   -584    559   -310       C  
ATOM    827  C   ASN A 440     -29.877  20.444 -19.821  1.00125.00           C  
ANISOU  827  C   ASN A 440    18578  16427  12489   -698    596   -162       C  
ATOM    828  O   ASN A 440     -29.878  20.836 -20.988  1.00132.26           O  
ANISOU  828  O   ASN A 440    19549  17308  13397   -603    615    -32       O  
ATOM    829  CB  ASN A 440     -30.096  22.315 -18.184  1.00141.38           C  
ANISOU  829  CB  ASN A 440    20828  18206  14683   -611    551   -316       C  
ATOM    830  CG  ASN A 440     -30.882  22.923 -17.043  1.00150.81           C  
ANISOU  830  CG  ASN A 440    22043  19384  15872   -512    511   -478       C  
ATOM    831  OD1 ASN A 440     -32.101  22.764 -16.961  1.00154.95           O  
ANISOU  831  OD1 ASN A 440    22501  20081  16294   -363    493   -557       O  
ATOM    832  ND2 ASN A 440     -30.189  23.625 -16.153  1.00151.94           N  
ANISOU  832  ND2 ASN A 440    22274  19329  16126   -594    497   -537       N  
ATOM    833  N   LEU A 441     -29.103  19.451 -19.393  1.00125.45           N  
ANISOU  833  N   LEU A 441    18558  16544  12564   -893    606   -181       N  
ATOM    834  CA  LEU A 441     -28.069  18.872 -20.242  1.00124.33           C  
ANISOU  834  CA  LEU A 441    18399  16393  12447  -1021    639    -50       C  
ATOM    835  C   LEU A 441     -28.371  17.442 -20.696  1.00129.40           C  
ANISOU  835  C   LEU A 441    18890  17285  12992  -1061    649    -56       C  
ATOM    836  O   LEU A 441     -27.712  16.928 -21.597  1.00133.77           O  
ANISOU  836  O   LEU A 441    19418  17865  13544  -1128    675     53       O  
ATOM    837  CB  LEU A 441     -26.721  18.909 -19.514  1.00120.02           C  
ANISOU  837  CB  LEU A 441    17894  15692  12014  -1223    644    -51       C  
ATOM    838  CG  LEU A 441     -26.294  20.267 -18.940  1.00124.65           C  
ANISOU  838  CG  LEU A 441    18623  16021  12719  -1219    634    -68       C  
ATOM    839  CD1 LEU A 441     -24.882  20.199 -18.376  1.00132.29           C  
ANISOU  839  CD1 LEU A 441    19610  16860  13794  -1429    640    -67       C  
ATOM    840  CD2 LEU A 441     -26.407  21.370 -19.981  1.00117.28           C  
ANISOU  840  CD2 LEU A 441    17809  14932  11818  -1086    657     60       C  
ATOM    841  N   ASP A 442     -29.358  16.794 -20.082  1.00126.01           N  
ANISOU  841  N   ASP A 442    18357  17038  12484  -1022    633   -184       N  
ATOM    842  CA  ASP A 442     -29.666  15.405 -20.432  1.00118.56           C  
ANISOU  842  CA  ASP A 442    17265  16320  11461  -1072    647   -205       C  
ATOM    843  C   ASP A 442     -31.109  15.199 -20.881  1.00127.35           C  
ANISOU  843  C   ASP A 442    18291  17631  12466   -902    637   -267       C  
ATOM    844  O   ASP A 442     -31.567  14.064 -21.007  1.00128.20           O  
ANISOU  844  O   ASP A 442    18265  17935  12511   -938    648   -319       O  
ATOM    845  CB  ASP A 442     -29.371  14.475 -19.254  1.00101.56           C  
ANISOU  845  CB  ASP A 442    15041  14229   9319  -1232    650   -301       C  
ATOM    846  CG  ASP A 442     -27.890  14.292 -19.017  1.00102.82           C  
ANISOU  846  CG  ASP A 442    15244  14257   9565  -1414    661   -237       C  
ATOM    847  OD1 ASP A 442     -27.118  14.404 -19.992  1.00103.29           O  
ANISOU  847  OD1 ASP A 442    15340  14246   9658  -1446    677   -112       O  
ATOM    848  OD2 ASP A 442     -27.500  14.020 -17.861  1.00108.81           O  
ANISOU  848  OD2 ASP A 442    15996  14996  10352  -1522    654   -312       O  
ATOM    849  N   SER A 443     -31.827  16.290 -21.114  1.00129.99           N  
ANISOU  849  N   SER A 443    18697  17911  12781   -716    617   -267       N  
ATOM    850  CA  SER A 443     -33.198  16.187 -21.592  1.00128.93           C  
ANISOU  850  CA  SER A 443    18478  17970  12540   -537    603   -329       C  
ATOM    851  C   SER A 443     -33.326  16.812 -22.982  1.00144.73           C  
ANISOU  851  C   SER A 443    20534  19951  14504   -377    602   -205       C  
ATOM    852  O   SER A 443     -32.823  17.909 -23.230  1.00149.51           O  
ANISOU  852  O   SER A 443    21287  20351  15169   -324    604   -106       O  
ATOM    853  CB  SER A 443     -34.158  16.848 -20.598  1.00108.85           C  
ANISOU  853  CB  SER A 443    15950  15429   9979   -423    577   -460       C  
ATOM    854  OG  SER A 443     -35.482  16.874 -21.091  1.00 97.41           O  
ANISOU  854  OG  SER A 443    14422  14162   8427   -233    560   -520       O  
ATOM    855  N   LYS A 444     -34.005  16.105 -23.882  1.00146.95           N  
ANISOU  855  N   LYS A 444    20698  20449  14688   -299    601   -213       N  
ATOM    856  CA  LYS A 444     -34.230  16.577 -25.247  1.00141.51           C  
ANISOU  856  CA  LYS A 444    20041  19788  13937   -129    598   -103       C  
ATOM    857  C   LYS A 444     -35.638  17.131 -25.390  1.00144.02           C  
ANISOU  857  C   LYS A 444    20332  20226  14162    112    565   -183       C  
ATOM    858  O   LYS A 444     -36.503  16.864 -24.554  1.00147.23           O  
ANISOU  858  O   LYS A 444    20654  20747  14541    129    548   -335       O  
ATOM    859  CB  LYS A 444     -34.017  15.450 -26.262  1.00141.92           C  
ANISOU  859  CB  LYS A 444    19976  20014  13932   -186    613    -62       C  
ATOM    860  CG  LYS A 444     -32.612  14.874 -26.312  1.00149.42           C  
ANISOU  860  CG  LYS A 444    20946  20864  14961   -404    646     28       C  
ATOM    861  CD  LYS A 444     -32.516  13.786 -27.378  1.00147.39           C  
ANISOU  861  CD  LYS A 444    20570  20793  14639   -433    656     56       C  
ATOM    862  CE  LYS A 444     -31.182  13.058 -27.321  1.00141.48           C  
ANISOU  862  CE  LYS A 444    19821  19971  13964   -654    686    121       C  
ATOM    863  NZ  LYS A 444     -31.138  11.901 -28.261  1.00132.11           N  
ANISOU  863  NZ  LYS A 444    18506  18974  12715   -687    694    124       N  
ATOM    864  N   VAL A 445     -35.863  17.912 -26.442  1.00131.83           N  
ANISOU  864  N   VAL A 445    18861  18659  12568    304    557    -78       N  
ATOM    865  CA  VAL A 445     -37.182  18.478 -26.697  1.00123.82           C  
ANISOU  865  CA  VAL A 445    17825  17766  11456    558    522   -144       C  
ATOM    866  C   VAL A 445     -38.201  17.361 -26.890  1.00116.04           C  
ANISOU  866  C   VAL A 445    16628  17097  10364    585    505   -285       C  
ATOM    867  O   VAL A 445     -39.275  17.378 -26.289  1.00127.33           O  
ANISOU  867  O   VAL A 445    17980  18652  11749    673    480   -432       O  
ATOM    868  CB  VAL A 445     -37.175  19.394 -27.927  1.00127.46           C  
ANISOU  868  CB  VAL A 445    18397  18164  11869    764    522     13       C  
ATOM    869  CG1 VAL A 445     -38.557  19.987 -28.144  1.00134.93           C  
ANISOU  869  CG1 VAL A 445    19318  19242  12706   1041    480    -62       C  
ATOM    870  CG2 VAL A 445     -36.145  20.499 -27.756  1.00124.37           C  
ANISOU  870  CG2 VAL A 445    18215  17443  11597    723    550    156       C  
ATOM    871  N   GLY A 446     -37.857  16.388 -27.728  1.00 95.10           N  
ANISOU  871  N   GLY A 446    13880  14577   7678    506    519   -247       N  
ATOM    872  CA  GLY A 446     -38.667  15.194 -27.876  1.00 99.77           C  
ANISOU  872  CA  GLY A 446    14264  15451   8193    484    511   -387       C  
ATOM    873  C   GLY A 446     -38.579  14.310 -26.645  1.00108.89           C  
ANISOU  873  C   GLY A 446    15336  16624   9414    268    531   -509       C  
ATOM    874  O   GLY A 446     -39.552  13.660 -26.257  1.00104.66           O  
ANISOU  874  O   GLY A 446    14651  16284   8832    273    526   -664       O  
ATOM    875  N   GLY A 447     -37.402  14.291 -26.026  1.00111.86           N  
ANISOU  875  N   GLY A 447    15808  16797   9897     78    558   -437       N  
ATOM    876  CA  GLY A 447     -37.169  13.499 -24.833  1.00111.81           C  
ANISOU  876  CA  GLY A 447    15744  16786   9951   -126    581   -530       C  
ATOM    877  C   GLY A 447     -35.992  12.563 -25.020  1.00116.30           C  
ANISOU  877  C   GLY A 447    16299  17312  10579   -339    612   -457       C  
ATOM    878  O   GLY A 447     -35.759  12.064 -26.119  1.00129.18           O  
ANISOU  878  O   GLY A 447    17881  19028  12173   -333    616   -396       O  
ATOM    879  N   ASN A 448     -35.257  12.311 -23.941  1.00118.95           N  
ANISOU  879  N   ASN A 448    16673  17526  10998   -520    632   -469       N  
ATOM    880  CA  ASN A 448     -34.106  11.414 -23.991  1.00109.62           C  
ANISOU  880  CA  ASN A 448    15478  16299   9873   -723    660   -407       C  
ATOM    881  C   ASN A 448     -34.474  10.023 -23.487  1.00106.51           C  
ANISOU  881  C   ASN A 448    14933  16070   9467   -852    684   -521       C  
ATOM    882  O   ASN A 448     -34.924   9.859 -22.351  1.00121.75           O  
ANISOU  882  O   ASN A 448    16833  18021  11407   -896    693   -623       O  
ATOM    883  CB  ASN A 448     -32.951  11.991 -23.164  1.00102.13           C  
ANISOU  883  CB  ASN A 448    14669  15111   9025   -843    667   -341       C  
ATOM    884  CG  ASN A 448     -31.641  11.234 -23.356  1.00 94.20           C  
ANISOU  884  CG  ASN A 448    13668  14047   8078  -1031    691   -257       C  
ATOM    885  OD1 ASN A 448     -31.626  10.066 -23.742  1.00 96.02           O  
ANISOU  885  OD1 ASN A 448    13786  14416   8283  -1108    708   -277       O  
ATOM    886  ND2 ASN A 448     -30.532  11.906 -23.073  1.00 82.94           N  
ANISOU  886  ND2 ASN A 448    12368  12411   6734  -1105    694   -169       N  
ATOM    887  N   TYR A 449     -34.237   9.020 -24.323  1.00 94.91           N  
ANISOU  887  N   TYR A 449    13373  14710   7980   -915    699   -501       N  
ATOM    888  CA  TYR A 449     -34.619   7.652 -24.003  1.00 98.00           C  
ANISOU  888  CA  TYR A 449    13617  15255   8364  -1033    727   -606       C  
ATOM    889  C   TYR A 449     -33.403   6.735 -24.030  1.00 95.36           C  
ANISOU  889  C   TYR A 449    13286  14856   8090  -1223    754   -539       C  
ATOM    890  O   TYR A 449     -33.527   5.512 -23.934  1.00 76.32           O  
ANISOU  890  O   TYR A 449    10763  12551   5683  -1331    783   -603       O  
ATOM    891  CB  TYR A 449     -35.689   7.167 -24.986  1.00 90.54           C  
ANISOU  891  CB  TYR A 449    12528  14536   7337   -920    718   -684       C  
ATOM    892  CG  TYR A 449     -36.863   8.113 -25.107  1.00 92.40           C  
ANISOU  892  CG  TYR A 449    12758  14848   7502   -708    685   -744       C  
ATOM    893  CD1 TYR A 449     -37.887   8.098 -24.171  1.00 91.67           C  
ANISOU  893  CD1 TYR A 449    12599  14840   7392   -683    692   -878       C  
ATOM    894  CD2 TYR A 449     -36.932   9.042 -26.137  1.00 93.00           C  
ANISOU  894  CD2 TYR A 449    12899  14910   7525   -527    650   -661       C  
ATOM    895  CE1 TYR A 449     -38.962   8.962 -24.270  1.00 89.85           C  
ANISOU  895  CE1 TYR A 449    12359  14686   7094   -481    659   -939       C  
ATOM    896  CE2 TYR A 449     -38.004   9.914 -26.242  1.00 93.79           C  
ANISOU  896  CE2 TYR A 449    12999  15080   7557   -319    618   -714       C  
ATOM    897  CZ  TYR A 449     -39.014   9.869 -25.304  1.00 85.94           C  
ANISOU  897  CZ  TYR A 449    11932  14175   6548   -297    620   -858       C  
ATOM    898  OH  TYR A 449     -40.082  10.730 -25.396  1.00 80.72           O  
ANISOU  898  OH  TYR A 449    11265  13590   5816    -83    586   -917       O  
ATOM    899  N   ASN A 450     -32.228   7.343 -24.147  1.00 93.63           N  
ANISOU  899  N   ASN A 450    13195  14457   7921  -1262    748   -412       N  
ATOM    900  CA  ASN A 450     -30.977   6.600 -24.194  1.00 97.39           C  
ANISOU  900  CA  ASN A 450    13684  14864   8454  -1431    769   -341       C  
ATOM    901  C   ASN A 450     -30.552   6.094 -22.819  1.00 97.95           C  
ANISOU  901  C   ASN A 450    13766  14869   8581  -1586    790   -385       C  
ATOM    902  O   ASN A 450     -29.801   5.126 -22.712  1.00 91.26           O  
ANISOU  902  O   ASN A 450    12888  14019   7768  -1727    813   -366       O  
ATOM    903  CB  ASN A 450     -29.876   7.458 -24.809  1.00102.77           C  
ANISOU  903  CB  ASN A 450    14492  15386   9170  -1419    758   -193       C  
ATOM    904  CG  ASN A 450     -30.123   7.749 -26.279  1.00108.78           C  
ANISOU  904  CG  ASN A 450    15238  16226   9868  -1280    746   -127       C  
ATOM    905  OD1 ASN A 450     -29.879   6.905 -27.144  1.00110.29           O  
ANISOU  905  OD1 ASN A 450    15352  16521  10034  -1312    755   -108       O  
ATOM    906  ND2 ASN A 450     -30.605   8.953 -26.570  1.00115.38           N  
ANISOU  906  ND2 ASN A 450    16152  17013  10675  -1116    726    -91       N  
ATOM    907  N   TYR A 451     -31.016   6.761 -21.768  1.00 99.14           N  
ANISOU  907  N   TYR A 451    13963  14969   8737  -1550    783   -443       N  
ATOM    908  CA  TYR A 451     -30.736   6.303 -20.413  1.00 92.12           C  
ANISOU  908  CA  TYR A 451    13079  14041   7883  -1676    803   -493       C  
ATOM    909  C   TYR A 451     -31.692   5.175 -20.042  1.00 94.41           C  
ANISOU  909  C   TYR A 451    13232  14502   8136  -1712    839   -604       C  
ATOM    910  O   TYR A 451     -32.913   5.343 -20.062  1.00 80.68           O  
ANISOU  910  O   TYR A 451    11427  12881   6347  -1606    838   -692       O  
ATOM    911  CB  TYR A 451     -30.844   7.449 -19.404  1.00 79.42           C  
ANISOU  911  CB  TYR A 451    11569  12317   6290  -1622    781   -521       C  
ATOM    912  CG  TYR A 451     -29.742   8.472 -19.526  1.00 71.99           C  
ANISOU  912  CG  TYR A 451    10765  11177   5409  -1630    756   -420       C  
ATOM    913  CD1 TYR A 451     -28.432   8.152 -19.195  1.00 71.22           C  
ANISOU  913  CD1 TYR A 451    10711  10975   5372  -1778    763   -360       C  
ATOM    914  CD2 TYR A 451     -30.011   9.761 -19.966  1.00 84.72           C  
ANISOU  914  CD2 TYR A 451    12462  12705   7021  -1489    728   -387       C  
ATOM    915  CE1 TYR A 451     -27.419   9.087 -19.307  1.00 74.57           C  
ANISOU  915  CE1 TYR A 451    11252  11221   5861  -1797    744   -276       C  
ATOM    916  CE2 TYR A 451     -29.008  10.701 -20.077  1.00 88.55           C  
ANISOU  916  CE2 TYR A 451    13074  12996   7574  -1507    714   -295       C  
ATOM    917  CZ  TYR A 451     -27.715  10.359 -19.747  1.00 83.23           C  
ANISOU  917  CZ  TYR A 451    12433  12226   6965  -1667    723   -243       C  
ATOM    918  OH  TYR A 451     -26.714  11.295 -19.859  1.00 80.21           O  
ANISOU  918  OH  TYR A 451    12165  11653   6658  -1695    714   -160       O  
ATOM    919  N   LEU A 452     -31.128   4.026 -19.696  1.00102.21           N  
ANISOU  919  N   LEU A 452    14179  15503   9154  -1861    873   -600       N  
ATOM    920  CA  LEU A 452     -31.929   2.842 -19.424  1.00102.78           C  
ANISOU  920  CA  LEU A 452    14124  15722   9206  -1916    919   -692       C  
ATOM    921  C   LEU A 452     -31.735   2.359 -17.988  1.00 97.73           C  
ANISOU  921  C   LEU A 452    13499  15048   8585  -2025    956   -722       C  
ATOM    922  O   LEU A 452     -30.777   2.740 -17.317  1.00109.63           O  
ANISOU  922  O   LEU A 452    15106  16424  10123  -2077    942   -666       O  
ATOM    923  CB  LEU A 452     -31.573   1.723 -20.404  1.00111.33           C  
ANISOU  923  CB  LEU A 452    15129  16868  10303  -1989    937   -667       C  
ATOM    924  CG  LEU A 452     -31.456   2.060 -21.891  1.00102.40           C  
ANISOU  924  CG  LEU A 452    13990  15768   9151  -1898    902   -615       C  
ATOM    925  CD1 LEU A 452     -31.035   0.821 -22.664  1.00 91.74           C  
ANISOU  925  CD1 LEU A 452    12560  14481   7818  -1988    924   -606       C  
ATOM    926  CD2 LEU A 452     -32.752   2.626 -22.449  1.00108.04           C  
ANISOU  926  CD2 LEU A 452    14642  16608   9801  -1735    881   -688       C  
ATOM    927  N   TYR A 453     -32.657   1.530 -17.513  1.00102.80           N  
ANISOU  927  N   TYR A 453    14039  15814   9207  -2057   1006   -812       N  
ATOM    928  CA  TYR A 453     -32.542   0.955 -16.178  1.00 97.61           C  
ANISOU  928  CA  TYR A 453    13389  15142   8558  -2157   1052   -833       C  
ATOM    929  C   TYR A 453     -33.169  -0.430 -16.065  1.00 95.93           C  
ANISOU  929  C   TYR A 453    13054  15047   8348  -2246   1125   -891       C  
ATOM    930  O   TYR A 453     -34.235  -0.691 -16.616  1.00104.30           O  
ANISOU  930  O   TYR A 453    14004  16238   9388  -2200   1142   -971       O  
ATOM    931  CB  TYR A 453     -33.173   1.883 -15.137  1.00 94.50           C  
ANISOU  931  CB  TYR A 453    13032  14747   8125  -2076   1043   -893       C  
ATOM    932  CG  TYR A 453     -34.668   2.057 -15.284  1.00 92.22           C  
ANISOU  932  CG  TYR A 453    12644  14608   7789  -1973   1057  -1000       C  
ATOM    933  CD1 TYR A 453     -35.196   2.931 -16.225  1.00118.43           C  
ANISOU  933  CD1 TYR A 453    15957  17957  11083  -1830   1007  -1016       C  
ATOM    934  CD2 TYR A 453     -35.551   1.315 -14.515  1.00 78.24           C  
ANISOU  934  CD2 TYR A 453    10779  12953   5995  -2018   1123  -1083       C  
ATOM    935  CE1 TYR A 453     -36.559   3.091 -16.365  1.00119.64           C  
ANISOU  935  CE1 TYR A 453    16012  18260  11187  -1727   1014  -1121       C  
ATOM    936  CE2 TYR A 453     -36.913   1.463 -14.655  1.00 75.14           C  
ANISOU  936  CE2 TYR A 453    10282  12708   5559  -1928   1137  -1189       C  
ATOM    937  CZ  TYR A 453     -37.411   2.349 -15.579  1.00 96.56           C  
ANISOU  937  CZ  TYR A 453    12987  15456   8244  -1780   1079  -1212       C  
ATOM    938  OH  TYR A 453     -38.771   2.494 -15.716  1.00 97.63           O  
ANISOU  938  OH  TYR A 453    13011  15752   8332  -1681   1088  -1326       O  
ATOM    939  N   ARG A 454     -32.523  -1.294 -15.290  1.00 77.58           N  
ANISOU  939  N   ARG A 454    10751  12676   6049  -2370   1170   -855       N  
ATOM    940  CA  ARG A 454     -32.999  -2.652 -15.070  1.00 75.78           C  
ANISOU  940  CA  ARG A 454    10426  12530   5838  -2470   1250   -896       C  
ATOM    941  C   ARG A 454     -34.290  -2.617 -14.261  1.00 79.16           C  
ANISOU  941  C   ARG A 454    10783  13067   6225  -2438   1300   -994       C  
ATOM    942  O   ARG A 454     -34.512  -1.691 -13.483  1.00 77.95           O  
ANISOU  942  O   ARG A 454    10685  12901   6032  -2366   1279  -1012       O  
ATOM    943  CB  ARG A 454     -31.930  -3.476 -14.349  1.00 80.66           C  
ANISOU  943  CB  ARG A 454    11105  13057   6486  -2593   1284   -819       C  
ATOM    944  CG  ARG A 454     -32.362  -4.873 -13.963  1.00 85.16           C  
ANISOU  944  CG  ARG A 454    11595  13684   7078  -2699   1378   -847       C  
ATOM    945  CD  ARG A 454     -32.509  -5.741 -15.177  1.00 98.35           C  
ANISOU  945  CD  ARG A 454    13173  15401   8794  -2740   1392   -870       C  
ATOM    946  NE  ARG A 454     -31.240  -5.867 -15.881  1.00109.79           N  
ANISOU  946  NE  ARG A 454    14684  16758  10275  -2768   1344   -783       N  
ATOM    947  CZ  ARG A 454     -30.393  -6.873 -15.699  1.00110.27           C  
ANISOU  947  CZ  ARG A 454    14769  16752  10374  -2870   1378   -725       C  
ATOM    948  NH1 ARG A 454     -30.679  -7.829 -14.822  1.00104.10           N  
ANISOU  948  NH1 ARG A 454    13967  15978   9607  -2954   1462   -735       N  
ATOM    949  NH2 ARG A 454     -29.255  -6.920 -16.379  1.00115.70           N  
ANISOU  949  NH2 ARG A 454    15506  17368  11087  -2886   1331   -652       N  
ATOM    950  N   LEU A 455     -35.150  -3.610 -14.458  1.00 69.62           N  
ANISOU  950  N   LEU A 455     9450  11970   5031  -2493   1368  -1063       N  
ATOM    951  CA  LEU A 455     -36.422  -3.658 -13.748  1.00 77.32           C  
ANISOU  951  CA  LEU A 455    10340  13064   5972  -2473   1426  -1161       C  
ATOM    952  C   LEU A 455     -36.752  -5.014 -13.133  1.00 82.87           C  
ANISOU  952  C   LEU A 455    10972  13808   6707  -2609   1536  -1179       C  
ATOM    953  O   LEU A 455     -37.700  -5.127 -12.355  1.00118.91           O  
ANISOU  953  O   LEU A 455    15475  18462  11244  -2612   1601  -1246       O  
ATOM    954  CB  LEU A 455     -37.569  -3.332 -14.702  1.00 88.91           C  
ANISOU  954  CB  LEU A 455    11691  14671   7421  -2376   1403  -1266       C  
ATOM    955  CG  LEU A 455     -37.988  -1.863 -14.751  1.00 96.74           C  
ANISOU  955  CG  LEU A 455    12723  15680   8353  -2209   1329  -1295       C  
ATOM    956  CD1 LEU A 455     -39.149  -1.662 -15.712  1.00103.39           C  
ANISOU  956  CD1 LEU A 455    13438  16678   9169  -2107   1309  -1401       C  
ATOM    957  CD2 LEU A 455     -38.359  -1.379 -13.358  1.00 98.78           C  
ANISOU  957  CD2 LEU A 455    13020  15944   8569  -2186   1357  -1321       C  
ATOM    958  N   PHE A 456     -35.989  -6.041 -13.487  1.00 70.11           N  
ANISOU  958  N   PHE A 456     9365  12125   5149  -2718   1563  -1120       N  
ATOM    959  CA  PHE A 456     -36.275  -7.391 -13.001  1.00 82.90           C  
ANISOU  959  CA  PHE A 456    10923  13764   6812  -2850   1674  -1131       C  
ATOM    960  C   PHE A 456     -34.994  -8.220 -12.900  1.00 98.23           C  
ANISOU  960  C   PHE A 456    12949  15574   8799  -2949   1688  -1020       C  
ATOM    961  O   PHE A 456     -34.035  -7.982 -13.631  1.00104.37           O  
ANISOU  961  O   PHE A 456    13786  16277   9592  -2930   1614   -963       O  
ATOM    962  CB  PHE A 456     -37.328  -8.114 -13.848  1.00 80.81           C  
ANISOU  962  CB  PHE A 456    10496  13619   6589  -2885   1719  -1243       C  
ATOM    963  CG  PHE A 456     -38.688  -7.470 -13.795  1.00 94.30           C  
ANISOU  963  CG  PHE A 456    12102  15477   8250  -2797   1722  -1362       C  
ATOM    964  CD1 PHE A 456     -39.534  -7.700 -12.720  1.00128.21           C  
ANISOU  964  CD1 PHE A 456    16347  19841  12524  -2833   1813  -1407       C  
ATOM    965  CD2 PHE A 456     -39.110  -6.619 -14.802  1.00 81.62           C  
ANISOU  965  CD2 PHE A 456    10450  13948   6613  -2670   1636  -1425       C  
ATOM    966  CE1 PHE A 456     -40.783  -7.104 -12.656  1.00132.59           C  
ANISOU  966  CE1 PHE A 456    16801  20544  13032  -2748   1816  -1522       C  
ATOM    967  CE2 PHE A 456     -40.356  -6.020 -14.746  1.00103.88           C  
ANISOU  967  CE2 PHE A 456    13175  16912   9384  -2577   1635  -1537       C  
ATOM    968  CZ  PHE A 456     -41.195  -6.263 -13.671  1.00128.36           C  
ANISOU  968  CZ  PHE A 456    16219  20085  12468  -2617   1724  -1590       C  
ATOM    969  N   ARG A 457     -34.983  -9.177 -11.971  1.00 89.65           N  
ANISOU  969  N   ARG A 457    11871  14463   7730  -3050   1786   -988       N  
ATOM    970  CA  ARG A 457     -33.825 -10.042 -11.746  1.00 95.50           C  
ANISOU  970  CA  ARG A 457    12694  15084   8509  -3137   1809   -883       C  
ATOM    971  C   ARG A 457     -34.190 -11.189 -10.803  1.00108.38           C  
ANISOU  971  C   ARG A 457    14305  16714  10162  -3242   1940   -865       C  
ATOM    972  O   ARG A 457     -34.973 -11.002  -9.870  1.00111.59           O  
ANISOU  972  O   ARG A 457    14691  17187  10523  -3231   2000   -893       O  
ATOM    973  CB  ARG A 457     -32.647  -9.245 -11.174  1.00 91.23           C  
ANISOU  973  CB  ARG A 457    12295  14450   7920  -3084   1735   -788       C  
ATOM    974  CG  ARG A 457     -31.332 -10.009 -11.173  1.00 84.52           C  
ANISOU  974  CG  ARG A 457    11525  13485   7105  -3153   1733   -686       C  
ATOM    975  CD  ARG A 457     -30.172  -9.163 -10.666  1.00 83.26           C  
ANISOU  975  CD  ARG A 457    11489  13246   6899  -3101   1653   -609       C  
ATOM    976  NE  ARG A 457     -28.885  -9.758 -11.015  1.00 87.23           N  
ANISOU  976  NE  ARG A 457    12050  13654   7439  -3149   1628   -526       N  
ATOM    977  CZ  ARG A 457     -28.299 -10.735 -10.329  1.00101.57           C  
ANISOU  977  CZ  ARG A 457    13912  15418   9262  -3215   1686   -456       C  
ATOM    978  NH1 ARG A 457     -28.887 -11.244  -9.254  1.00112.76           N  
ANISOU  978  NH1 ARG A 457    15328  16865  10652  -3243   1778   -452       N  
ATOM    979  NH2 ARG A 457     -27.125 -11.213 -10.722  1.00 97.32           N  
ANISOU  979  NH2 ARG A 457    13421  14801   8756  -3246   1654   -388       N  
ATOM    980  N   LYS A 458     -33.640 -12.374 -11.069  1.00117.32           N  
ANISOU  980  N   LYS A 458    15444  17770  11363  -3340   1989   -817       N  
ATOM    981  CA  LYS A 458     -33.885 -13.569 -10.256  1.00132.15           C  
ANISOU  981  CA  LYS A 458    17316  19621  13275  -3446   2121   -783       C  
ATOM    982  C   LYS A 458     -33.681 -13.311  -8.758  1.00126.56           C  
ANISOU  982  C   LYS A 458    16703  18898  12486  -3423   2161   -705       C  
ATOM    983  O   LYS A 458     -34.575 -13.557  -7.951  1.00125.72           O  
ANISOU  983  O   LYS A 458    16554  18855  12359  -3451   2260   -728       O  
ATOM    984  CB  LYS A 458     -32.986 -14.725 -10.736  1.00141.30           C  
ANISOU  984  CB  LYS A 458    18508  20668  14513  -3530   2143   -720       C  
ATOM    985  CG  LYS A 458     -31.492 -14.409 -10.768  1.00143.04           C  
ANISOU  985  CG  LYS A 458    18855  20789  14706  -3487   2051   -616       C  
ATOM    986  CD  LYS A 458     -30.651 -15.632 -11.092  1.00142.08           C  
ANISOU  986  CD  LYS A 458    18766  20562  14656  -3565   2084   -553       C  
ATOM    987  CE  LYS A 458     -29.168 -15.281 -11.083  1.00135.69           C  
ANISOU  987  CE  LYS A 458    18073  19672  13813  -3518   1992   -456       C  
ATOM    988  NZ  LYS A 458     -28.715 -14.813  -9.739  1.00127.83           N  
ANISOU  988  NZ  LYS A 458    17181  18659  12731  -3476   1992   -377       N  
ATOM    989  N   SER A 459     -32.495 -12.827  -8.403  1.00124.26           N  
ANISOU  989  N   SER A 459    16534  18533  12148  -3372   2085   -617       N  
ATOM    990  CA  SER A 459     -32.155 -12.479  -7.032  1.00119.67           C  
ANISOU  990  CA  SER A 459    16047  17943  11478  -3332   2100   -549       C  
ATOM    991  C   SER A 459     -31.636 -11.044  -6.975  1.00103.56           C  
ANISOU  991  C   SER A 459    14069  15906   9372  -3221   1971   -558       C  
ATOM    992  O   SER A 459     -31.168 -10.521  -7.981  1.00 87.88           O  
ANISOU  992  O   SER A 459    12084  13889   7416  -3190   1875   -575       O  
ATOM    993  CB  SER A 459     -31.112 -13.456  -6.483  1.00119.06           C  
ANISOU  993  CB  SER A 459    16063  17764  11408  -3386   2143   -428       C  
ATOM    994  OG  SER A 459     -29.941 -13.454  -7.284  1.00 96.44           O  
ANISOU  994  OG  SER A 459    13248  14816   8580  -3380   2052   -388       O  
ATOM    995  N   ASN A 460     -31.716 -10.415  -5.806  1.00101.62           N  
ANISOU  995  N   ASN A 460    13876  15697   9039  -3163   1973   -549       N  
ATOM    996  CA  ASN A 460     -31.220  -9.053  -5.628  1.00 75.89           C  
ANISOU  996  CA  ASN A 460    10682  12430   5724  -3062   1857   -565       C  
ATOM    997  C   ASN A 460     -29.706  -9.018  -5.809  1.00 68.78           C  
ANISOU  997  C   ASN A 460     9876  11421   4835  -3065   1778   -484       C  
ATOM    998  O   ASN A 460     -29.037 -10.032  -5.625  1.00 73.98           O  
ANISOU  998  O   ASN A 460    10570  12025   5513  -3127   1822   -405       O  
ATOM    999  CB  ASN A 460     -31.599  -8.514  -4.248  1.00 91.37           C  
ANISOU  999  CB  ASN A 460    12676  14455   7586  -3003   1883   -578       C  
ATOM   1000  CG  ASN A 460     -33.100  -8.458  -4.031  1.00112.84           C  
ANISOU 1000  CG  ASN A 460    15294  17293  10285  -2993   1959   -663       C  
ATOM   1001  OD1 ASN A 460     -33.851  -9.268  -4.575  1.00126.96           O  
ANISOU 1001  OD1 ASN A 460    16990  19116  12133  -3064   2038   -691       O  
ATOM   1002  ND2 ASN A 460     -33.542  -7.511  -3.215  1.00104.42           N  
ANISOU 1002  ND2 ASN A 460    14242  16297   9137  -2905   1938   -714       N  
ATOM   1003  N   LEU A 461     -29.164  -7.867  -6.194  1.00 68.26           N  
ANISOU 1003  N   LEU A 461     9851  11322   4763  -2998   1664   -504       N  
ATOM   1004  CA  LEU A 461     -27.722  -7.749  -6.404  1.00 68.90           C  
ANISOU 1004  CA  LEU A 461    10012  11308   4859  -3004   1587   -437       C  
ATOM   1005  C   LEU A 461     -26.930  -7.608  -5.106  1.00 72.92           C  
ANISOU 1005  C   LEU A 461    10610  11800   5296  -2980   1574   -392       C  
ATOM   1006  O   LEU A 461     -27.404  -7.015  -4.140  1.00 92.50           O  
ANISOU 1006  O   LEU A 461    13105  14336   7706  -2924   1581   -431       O  
ATOM   1007  CB  LEU A 461     -27.406  -6.558  -7.316  1.00 89.10           C  
ANISOU 1007  CB  LEU A 461    12581  13830   7445  -2949   1477   -471       C  
ATOM   1008  CG  LEU A 461     -27.683  -6.669  -8.820  1.00 94.58           C  
ANISOU 1008  CG  LEU A 461    13208  14522   8208  -2963   1460   -492       C  
ATOM   1009  CD1 LEU A 461     -27.370  -5.351  -9.503  1.00 89.86           C  
ANISOU 1009  CD1 LEU A 461    12638  13885   7619  -2893   1358   -511       C  
ATOM   1010  CD2 LEU A 461     -26.877  -7.790  -9.453  1.00 96.76           C  
ANISOU 1010  CD2 LEU A 461    13480  14746   8540  -3043   1478   -426       C  
ATOM   1011  N   LYS A 462     -25.703  -8.120  -5.109  1.00 83.61           N  
ANISOU 1011  N   LYS A 462    12018  13086   6662  -3013   1550   -316       N  
ATOM   1012  CA  LYS A 462     -24.770  -7.915  -4.006  1.00 81.71           C  
ANISOU 1012  CA  LYS A 462    11859  12833   6353  -2981   1517   -279       C  
ATOM   1013  C   LYS A 462     -24.213  -6.499  -4.106  1.00 88.06           C  
ANISOU 1013  C   LYS A 462    12700  13606   7152  -2923   1400   -328       C  
ATOM   1014  O   LYS A 462     -24.340  -5.868  -5.151  1.00105.58           O  
ANISOU 1014  O   LYS A 462    14892  15792   9430  -2918   1350   -361       O  
ATOM   1015  CB  LYS A 462     -23.638  -8.948  -4.047  1.00 76.11           C  
ANISOU 1015  CB  LYS A 462    11190  12068   5661  -3029   1527   -187       C  
ATOM   1016  CG  LYS A 462     -24.080 -10.380  -3.801  1.00 88.97           C  
ANISOU 1016  CG  LYS A 462    12801  13707   7295  -3084   1648   -129       C  
ATOM   1017  CD  LYS A 462     -22.880 -11.317  -3.757  1.00105.69           C  
ANISOU 1017  CD  LYS A 462    14971  15765   9422  -3111   1648    -37       C  
ATOM   1018  CE  LYS A 462     -23.289 -12.738  -3.404  1.00112.47           C  
ANISOU 1018  CE  LYS A 462    15829  16618  10288  -3161   1776     29       C  
ATOM   1019  NZ  LYS A 462     -22.109 -13.647  -3.318  1.00112.52           N  
ANISOU 1019  NZ  LYS A 462    15894  16562  10298  -3172   1775    121       N  
ATOM   1020  N   PRO A 463     -23.604  -5.988  -3.024  1.00 76.75           N  
ANISOU 1020  N   PRO A 463    11329  12183   5651  -2878   1359   -335       N  
ATOM   1021  CA  PRO A 463     -22.989  -4.658  -3.099  1.00 84.63           C  
ANISOU 1021  CA  PRO A 463    12362  13134   6658  -2835   1249   -387       C  
ATOM   1022  C   PRO A 463     -21.917  -4.578  -4.179  1.00 95.81           C  
ANISOU 1022  C   PRO A 463    13787  14462   8153  -2879   1185   -349       C  
ATOM   1023  O   PRO A 463     -21.125  -5.509  -4.325  1.00107.52           O  
ANISOU 1023  O   PRO A 463    15279  15926   9650  -2926   1200   -279       O  
ATOM   1024  CB  PRO A 463     -22.366  -4.484  -1.716  1.00 90.87           C  
ANISOU 1024  CB  PRO A 463    13209  13959   7360  -2793   1226   -394       C  
ATOM   1025  CG  PRO A 463     -23.180  -5.341  -0.833  1.00101.32           C  
ANISOU 1025  CG  PRO A 463    14519  15369   8608  -2783   1330   -370       C  
ATOM   1026  CD  PRO A 463     -23.567  -6.529  -1.655  1.00 90.02           C  
ANISOU 1026  CD  PRO A 463    13043  13923   7237  -2856   1413   -305       C  
ATOM   1027  N   PHE A 464     -21.919  -3.481  -4.930  1.00 92.02           N  
ANISOU 1027  N   PHE A 464    13307  13932   7726  -2859   1118   -392       N  
ATOM   1028  CA  PHE A 464     -20.947  -3.241  -5.992  1.00 99.07           C  
ANISOU 1028  CA  PHE A 464    14207  14742   8692  -2896   1060   -356       C  
ATOM   1029  C   PHE A 464     -20.943  -4.340  -7.062  1.00 83.17           C  
ANISOU 1029  C   PHE A 464    12147  12726   6728  -2954   1105   -294       C  
ATOM   1030  O   PHE A 464     -19.910  -4.609  -7.679  1.00 68.85           O  
ANISOU 1030  O   PHE A 464    10340  10865   4955  -2995   1074   -244       O  
ATOM   1031  CB  PHE A 464     -19.541  -3.094  -5.395  1.00 98.07           C  
ANISOU 1031  CB  PHE A 464    14129  14581   8552  -2911   1001   -339       C  
ATOM   1032  CG  PHE A 464     -19.346  -1.834  -4.597  1.00 90.86           C  
ANISOU 1032  CG  PHE A 464    13258  13649   7615  -2862    935   -416       C  
ATOM   1033  CD1 PHE A 464     -20.309  -0.837  -4.598  1.00 90.48           C  
ANISOU 1033  CD1 PHE A 464    13211  13597   7569  -2806    925   -485       C  
ATOM   1034  CD2 PHE A 464     -18.195  -1.646  -3.848  1.00 99.65           C  
ANISOU 1034  CD2 PHE A 464    14407  14753   8704  -2867    881   -426       C  
ATOM   1035  CE1 PHE A 464     -20.127   0.322  -3.867  1.00 95.73           C  
ANISOU 1035  CE1 PHE A 464    13916  14236   8219  -2760    864   -564       C  
ATOM   1036  CE2 PHE A 464     -18.008  -0.488  -3.114  1.00101.10           C  
ANISOU 1036  CE2 PHE A 464    14624  14918   8872  -2825    818   -511       C  
ATOM   1037  CZ  PHE A 464     -18.975   0.497  -3.124  1.00 93.09           C  
ANISOU 1037  CZ  PHE A 464    13615  13888   7867  -2773    811   -581       C  
ATOM   1038  N   GLU A 465     -22.101  -4.947  -7.305  1.00 89.91           N  
ANISOU 1038  N   GLU A 465    12947  13634   7580  -2957   1177   -306       N  
ATOM   1039  CA  GLU A 465     -22.209  -5.990  -8.319  1.00 97.06           C  
ANISOU 1039  CA  GLU A 465    13801  14542   8537  -3010   1222   -266       C  
ATOM   1040  C   GLU A 465     -22.849  -5.451  -9.584  1.00110.05           C  
ANISOU 1040  C   GLU A 465    15396  16189  10229  -2990   1202   -299       C  
ATOM   1041  O   GLU A 465     -23.998  -5.006  -9.571  1.00120.00           O  
ANISOU 1041  O   GLU A 465    16623  17499  11474  -2946   1220   -359       O  
ATOM   1042  CB  GLU A 465     -23.026  -7.181  -7.811  1.00 87.86           C  
ANISOU 1042  CB  GLU A 465    12600  13434   7349  -3040   1324   -258       C  
ATOM   1043  CG  GLU A 465     -23.029  -8.374  -8.763  1.00101.36           C  
ANISOU 1043  CG  GLU A 465    14260  15134   9119  -3103   1372   -224       C  
ATOM   1044  CD  GLU A 465     -24.043  -9.439  -8.377  1.00100.06           C  
ANISOU 1044  CD  GLU A 465    14050  15018   8951  -3140   1482   -231       C  
ATOM   1045  OE1 GLU A 465     -24.659  -9.317  -7.299  1.00108.70           O  
ANISOU 1045  OE1 GLU A 465    15155  16158   9987  -3116   1526   -249       O  
ATOM   1046  OE2 GLU A 465     -24.232 -10.399  -9.156  1.00104.99           O  
ANISOU 1046  OE2 GLU A 465    14623  15635   9633  -3194   1527   -223       O  
ATOM   1047  N   ARG A 466     -22.102  -5.518 -10.680  1.00 97.22           N  
ANISOU 1047  N   ARG A 466    13764  14519   8656  -3016   1165   -260       N  
ATOM   1048  CA  ARG A 466     -22.587  -5.065 -11.972  1.00 66.70           C  
ANISOU 1048  CA  ARG A 466     9854  10661   4827  -2990   1144   -280       C  
ATOM   1049  C   ARG A 466     -23.006  -6.226 -12.851  1.00 78.84           C  
ANISOU 1049  C   ARG A 466    11317  12243   6397  -3031   1196   -276       C  
ATOM   1050  O   ARG A 466     -22.194  -7.072 -13.219  1.00108.13           O  
ANISOU 1050  O   ARG A 466    15024  15928  10134  -3083   1202   -228       O  
ATOM   1051  CB  ARG A 466     -21.526  -4.193 -12.653  1.00 80.54           C  
ANISOU 1051  CB  ARG A 466    11649  12340   6611  -2982   1068   -241       C  
ATOM   1052  CG  ARG A 466     -21.920  -3.639 -14.016  1.00 94.80           C  
ANISOU 1052  CG  ARG A 466    13422  14153   8447  -2942   1045   -244       C  
ATOM   1053  CD  ARG A 466     -21.316  -2.261 -14.229  1.00100.54           C  
ANISOU 1053  CD  ARG A 466    14210  14800   9191  -2906    980   -226       C  
ATOM   1054  NE  ARG A 466     -19.876  -2.178 -13.994  1.00110.30           N  
ANISOU 1054  NE  ARG A 466    15496  15965  10450  -2959    944   -175       N  
ATOM   1055  CZ  ARG A 466     -18.931  -2.564 -14.844  1.00121.54           C  
ANISOU 1055  CZ  ARG A 466    16906  17368  11905  -3003    932   -116       C  
ATOM   1056  NH1 ARG A 466     -19.251  -3.056 -16.032  1.00126.75           N  
ANISOU 1056  NH1 ARG A 466    17511  18071  12578  -2997    951    -98       N  
ATOM   1057  NH2 ARG A 466     -17.656  -2.432 -14.504  1.00117.70           N  
ANISOU 1057  NH2 ARG A 466    16458  16826  11436  -3050    899    -81       N  
ATOM   1058  N   ASP A 467     -24.305  -6.281 -13.126  1.00 71.39           N  
ANISOU 1058  N   ASP A 467    10307  11370   5449  -3004   1234   -339       N  
ATOM   1059  CA  ASP A 467     -24.875  -7.266 -14.031  1.00 89.15           C  
ANISOU 1059  CA  ASP A 467    12470  13672   7733  -3037   1280   -362       C  
ATOM   1060  C   ASP A 467     -25.394  -6.570 -15.285  1.00 90.45           C  
ANISOU 1060  C   ASP A 467    12585  13876   7906  -2974   1238   -398       C  
ATOM   1061  O   ASP A 467     -26.296  -5.732 -15.207  1.00 85.54           O  
ANISOU 1061  O   ASP A 467    11949  13298   7256  -2905   1227   -452       O  
ATOM   1062  CB  ASP A 467     -25.999  -8.039 -13.352  1.00 91.75           C  
ANISOU 1062  CB  ASP A 467    12744  14065   8052  -3065   1367   -414       C  
ATOM   1063  CG  ASP A 467     -26.841  -8.816 -14.338  1.00112.59           C  
ANISOU 1063  CG  ASP A 467    15278  16771  10732  -3090   1409   -470       C  
ATOM   1064  OD1 ASP A 467     -27.837  -8.253 -14.840  1.00118.33           O  
ANISOU 1064  OD1 ASP A 467    15942  17571  11447  -3033   1398   -542       O  
ATOM   1065  OD2 ASP A 467     -26.493  -9.979 -14.630  1.00117.00           O  
ANISOU 1065  OD2 ASP A 467    15813  17309  11334  -3161   1449   -450       O  
ATOM   1066  N   ILE A 468     -24.855  -6.950 -16.440  1.00 91.88           N  
ANISOU 1066  N   ILE A 468    12738  14052   8119  -2991   1217   -371       N  
ATOM   1067  CA  ILE A 468     -25.160  -6.258 -17.684  1.00 86.79           C  
ANISOU 1067  CA  ILE A 468    12058  13446   7473  -2921   1173   -388       C  
ATOM   1068  C   ILE A 468     -25.758  -7.223 -18.710  1.00 99.53           C  
ANISOU 1068  C   ILE A 468    13566  15143   9109  -2937   1204   -440       C  
ATOM   1069  O   ILE A 468     -26.003  -6.861 -19.863  1.00 88.38           O  
ANISOU 1069  O   ILE A 468    12109  13782   7688  -2877   1170   -456       O  
ATOM   1070  CB  ILE A 468     -23.894  -5.584 -18.263  1.00 82.01           C  
ANISOU 1070  CB  ILE A 468    11519  12765   6877  -2909   1110   -306       C  
ATOM   1071  CG1 ILE A 468     -24.262  -4.450 -19.224  1.00101.99           C  
ANISOU 1071  CG1 ILE A 468    14047  15316   9390  -2813   1064   -307       C  
ATOM   1072  CG2 ILE A 468     -22.987  -6.617 -18.922  1.00 78.91           C  
ANISOU 1072  CG2 ILE A 468    11103  12361   6517  -2974   1117   -264       C  
ATOM   1073  CD1 ILE A 468     -23.078  -3.884 -19.992  1.00106.47           C  
ANISOU 1073  CD1 ILE A 468    14665  15816   9971  -2807   1017   -221       C  
ATOM   1074  N   SER A 469     -26.015  -8.449 -18.266  1.00104.99           N  
ANISOU 1074  N   SER A 469    14215  15849   9828  -3015   1270   -468       N  
ATOM   1075  CA  SER A 469     -26.598  -9.480 -19.116  1.00110.35           C  
ANISOU 1075  CA  SER A 469    14788  16598  10541  -3047   1307   -534       C  
ATOM   1076  C   SER A 469     -27.942  -9.037 -19.697  1.00 88.92           C  
ANISOU 1076  C   SER A 469    11982  14000   7805  -2976   1304   -631       C  
ATOM   1077  O   SER A 469     -28.753  -8.417 -19.012  1.00 75.90           O  
ANISOU 1077  O   SER A 469    10333  12381   6123  -2936   1315   -669       O  
ATOM   1078  CB  SER A 469     -26.760 -10.783 -18.330  1.00120.63           C  
ANISOU 1078  CB  SER A 469    16073  17879  11884  -3146   1391   -548       C  
ATOM   1079  OG  SER A 469     -27.638 -10.617 -17.230  1.00124.60           O  
ANISOU 1079  OG  SER A 469    16574  18403  12364  -3149   1441   -581       O  
ATOM   1080  N   THR A 470     -28.163  -9.344 -20.970  1.00106.70           N  
ANISOU 1080  N   THR A 470    14150  16324  10066  -2952   1285   -678       N  
ATOM   1081  CA  THR A 470     -29.350  -8.876 -21.673  1.00115.20           C  
ANISOU 1081  CA  THR A 470    15134  17525  11111  -2866   1269   -772       C  
ATOM   1082  C   THR A 470     -30.390  -9.985 -21.720  1.00109.13           C  
ANISOU 1082  C   THR A 470    14239  16843  10381  -2927   1336   -890       C  
ATOM   1083  O   THR A 470     -31.494  -9.798 -22.231  1.00111.73           O  
ANISOU 1083  O   THR A 470    14467  17295  10690  -2869   1332   -992       O  
ATOM   1084  CB  THR A 470     -29.021  -8.437 -23.119  1.00127.38           C  
ANISOU 1084  CB  THR A 470    16655  19117  12626  -2782   1202   -757       C  
ATOM   1085  OG1 THR A 470     -27.725  -7.828 -23.165  1.00140.09           O  
ANISOU 1085  OG1 THR A 470    18378  20623  14228  -2773   1158   -634       O  
ATOM   1086  CG2 THR A 470     -30.067  -7.465 -23.650  1.00123.75           C  
ANISOU 1086  CG2 THR A 470    16146  18766  12107  -2653   1166   -817       C  
ATOM   1087  N   GLU A 471     -30.030 -11.133 -21.155  1.00104.46           N  
ANISOU 1087  N   GLU A 471    13656  16186   9850  -3044   1400   -877       N  
ATOM   1088  CA  GLU A 471     -30.901 -12.301 -21.133  1.00106.72           C  
ANISOU 1088  CA  GLU A 471    13830  16524  10193  -3127   1478   -981       C  
ATOM   1089  C   GLU A 471     -32.260 -11.995 -20.505  1.00 90.27           C  
ANISOU 1089  C   GLU A 471    11680  14527   8090  -3111   1522  -1068       C  
ATOM   1090  O   GLU A 471     -32.334 -11.382 -19.445  1.00 86.60           O  
ANISOU 1090  O   GLU A 471    11286  14028   7590  -3095   1534  -1022       O  
ATOM   1091  CB  GLU A 471     -30.214 -13.449 -20.383  1.00115.59           C  
ANISOU 1091  CB  GLU A 471    15007  17531  11380  -3248   1547   -923       C  
ATOM   1092  CG  GLU A 471     -28.893 -13.896 -21.010  1.00132.09           C  
ANISOU 1092  CG  GLU A 471    17150  19544  13494  -3267   1509   -850       C  
ATOM   1093  CD  GLU A 471     -28.184 -14.974 -20.206  1.00142.25           C  
ANISOU 1093  CD  GLU A 471    18501  20713  14836  -3369   1573   -786       C  
ATOM   1094  OE1 GLU A 471     -28.612 -15.251 -19.066  1.00145.84           O  
ANISOU 1094  OE1 GLU A 471    18980  21135  15299  -3420   1646   -775       O  
ATOM   1095  OE2 GLU A 471     -27.197 -15.544 -20.715  1.00145.67           O  
ANISOU 1095  OE2 GLU A 471    18961  21090  15297  -3392   1553   -743       O  
ATOM   1096  N   ILE A 472     -33.332 -12.381 -21.193  1.00 91.58           N  
ANISOU 1096  N   ILE A 472    11703  14819   8276  -3107   1540  -1202       N  
ATOM   1097  CA  ILE A 472     -34.691 -12.168 -20.699  1.00100.52           C  
ANISOU 1097  CA  ILE A 472    12747  16055   9392  -3094   1585  -1303       C  
ATOM   1098  C   ILE A 472     -34.983 -13.078 -19.504  1.00107.12           C  
ANISOU 1098  C   ILE A 472    13583  16834  10284  -3224   1699  -1302       C  
ATOM   1099  O   ILE A 472     -34.544 -14.226 -19.470  1.00109.82           O  
ANISOU 1099  O   ILE A 472    13928  17098  10701  -3334   1756  -1285       O  
ATOM   1100  CB  ILE A 472     -35.747 -12.402 -21.814  1.00 98.16           C  
ANISOU 1100  CB  ILE A 472    12278  15919   9101  -3058   1572  -1461       C  
ATOM   1101  CG1 ILE A 472     -35.586 -13.790 -22.438  1.00 99.25           C  
ANISOU 1101  CG1 ILE A 472    12338  16043   9330  -3169   1615  -1523       C  
ATOM   1102  CG2 ILE A 472     -35.632 -11.340 -22.893  1.00101.04           C  
ANISOU 1102  CG2 ILE A 472    12644  16358   9387  -2904   1463  -1458       C  
ATOM   1103  CD1 ILE A 472     -36.572 -14.819 -21.922  1.00104.58           C  
ANISOU 1103  CD1 ILE A 472    12901  16750  10084  -3292   1725  -1633       C  
ATOM   1104  N   TYR A 473     -35.724 -12.561 -18.527  1.00107.51           N  
ANISOU 1104  N   TYR A 473    13634  16922  10295  -3204   1736  -1316       N  
ATOM   1105  CA  TYR A 473     -36.023 -13.314 -17.307  1.00106.36           C  
ANISOU 1105  CA  TYR A 473    13497  16730  10187  -3315   1852  -1300       C  
ATOM   1106  C   TYR A 473     -37.476 -13.790 -17.264  1.00110.44           C  
ANISOU 1106  C   TYR A 473    13853  17372  10737  -3364   1933  -1444       C  
ATOM   1107  O   TYR A 473     -38.383 -13.073 -17.685  1.00115.56           O  
ANISOU 1107  O   TYR A 473    14410  18159  11340  -3274   1893  -1544       O  
ATOM   1108  CB  TYR A 473     -35.713 -12.469 -16.068  1.00 97.06           C  
ANISOU 1108  CB  TYR A 473    12442  15500   8938  -3269   1847  -1204       C  
ATOM   1109  N   GLN A 474     -37.684 -15.000 -16.749  1.00103.97           N  
ANISOU 1109  N   GLN A 474    13001  16504   9998  -3504   2050  -1454       N  
ATOM   1110  CA  GLN A 474     -39.017 -15.597 -16.678  1.00110.09           C  
ANISOU 1110  CA  GLN A 474    13617  17386  10824  -3579   2145  -1591       C  
ATOM   1111  C   GLN A 474     -39.701 -15.319 -15.334  1.00128.39           C  
ANISOU 1111  C   GLN A 474    15946  19735  13100  -3593   2229  -1573       C  
ATOM   1112  O   GLN A 474     -39.385 -15.931 -14.312  1.00144.48           O  
ANISOU 1112  O   GLN A 474    18062  21673  15162  -3681   2323  -1479       O  
ATOM   1113  CB  GLN A 474     -38.947 -17.115 -16.958  1.00 96.61           C  
ANISOU 1113  CB  GLN A 474    11857  15606   9245  -3733   2237  -1625       C  
ATOM   1114  CG  GLN A 474     -38.088 -17.979 -16.017  1.00 97.49           C  
ANISOU 1114  CG  GLN A 474    12099  15539   9402  -3837   2324  -1482       C  
ATOM   1115  CD  GLN A 474     -36.622 -17.573 -15.941  1.00102.74           C  
ANISOU 1115  CD  GLN A 474    12935  16085  10017  -3772   2238  -1329       C  
ATOM   1116  OE1 GLN A 474     -36.141 -16.771 -16.738  1.00 98.78           O  
ANISOU 1116  OE1 GLN A 474    12454  15614   9463  -3667   2117  -1326       O  
ATOM   1117  NE2 GLN A 474     -35.909 -18.123 -14.966  1.00116.98           N  
ANISOU 1117  NE2 GLN A 474    14859  17756  11832  -3833   2304  -1199       N  
ATOM   1118  N   ALA A 475     -40.629 -14.368 -15.341  1.00140.58           N  
ANISOU 1118  N   ALA A 475    17415  21425  14575  -3493   2193  -1659       N  
ATOM   1119  CA  ALA A 475     -41.394 -14.042 -14.144  1.00142.36           C  
ANISOU 1119  CA  ALA A 475    17629  21707  14752  -3493   2268  -1663       C  
ATOM   1120  C   ALA A 475     -42.310 -15.198 -13.751  1.00137.81           C  
ANISOU 1120  C   ALA A 475    16930  21168  14263  -3645   2421  -1739       C  
ATOM   1121  O   ALA A 475     -42.309 -15.653 -12.606  1.00155.46           O  
ANISOU 1121  O   ALA A 475    19220  23344  16505  -3725   2531  -1662       O  
ATOM   1122  CB  ALA A 475     -42.210 -12.771 -14.364  1.00155.72           C  
ANISOU 1122  CB  ALA A 475    19259  23555  16354  -3342   2189  -1754       C  
ATOM   1123  N   GLY A 476     -43.080 -15.670 -14.722  1.00121.39           N  
ANISOU 1123  N   GLY A 476    14684  19188  12249  -3684   2428  -1892       N  
ATOM   1124  CA  GLY A 476     -44.014 -16.761 -14.533  1.00112.91           C  
ANISOU 1124  CA  GLY A 476    13470  18156  11276  -3837   2569  -1992       C  
ATOM   1125  C   GLY A 476     -43.370 -18.132 -14.568  1.00115.63           C  
ANISOU 1125  C   GLY A 476    13855  18336  11742  -3994   2655  -1934       C  
ATOM   1126  O   GLY A 476     -42.192 -18.282 -14.892  1.00122.90           O  
ANISOU 1126  O   GLY A 476    14900  19125  12671  -3979   2594  -1831       O  
ATOM   1127  N   SER A 477     -44.160 -19.135 -14.214  1.00103.13           N  
ANISOU 1127  N   SER A 477    12166  16760  10257  -4146   2803  -2001       N  
ATOM   1128  CA  SER A 477     -43.708 -20.517 -14.203  1.00117.00           C  
ANISOU 1128  CA  SER A 477    13952  18356  12145  -4306   2905  -1959       C  
ATOM   1129  C   SER A 477     -43.304 -21.022 -15.582  1.00132.69           C  
ANISOU 1129  C   SER A 477    15886  20317  14212  -4320   2828  -2045       C  
ATOM   1130  O   SER A 477     -42.327 -21.761 -15.715  1.00145.63           O  
ANISOU 1130  O   SER A 477    17628  21791  15914  -4375   2837  -1954       O  
ATOM   1131  CB  SER A 477     -44.807 -21.410 -13.628  1.00123.12           C  
ANISOU 1131  CB  SER A 477    14601  19161  13017  -4467   3084  -2036       C  
ATOM   1132  OG  SER A 477     -46.061 -21.116 -14.224  1.00126.36           O  
ANISOU 1132  OG  SER A 477    14802  19775  13436  -4456   3071  -2241       O  
ATOM   1133  N   THR A 478     -44.049 -20.614 -16.608  1.00146.44           N  
ANISOU 1133  N   THR A 478    17467  22230  15944  -4259   2749  -2221       N  
ATOM   1134  CA  THR A 478     -43.818 -21.111 -17.965  1.00142.60           C  
ANISOU 1134  CA  THR A 478    16903  21751  15528  -4268   2679  -2331       C  
ATOM   1135  C   THR A 478     -42.448 -20.719 -18.506  1.00145.15           C  
ANISOU 1135  C   THR A 478    17379  21977  15793  -4163   2550  -2208       C  
ATOM   1136  O   THR A 478     -42.084 -19.541 -18.510  1.00146.08           O  
ANISOU 1136  O   THR A 478    17577  22141  15787  -4012   2442  -2137       O  
ATOM   1137  CB  THR A 478     -44.895 -20.608 -18.949  1.00126.51           C  
ANISOU 1137  CB  THR A 478    14663  19945  13462  -4192   2606  -2543       C  
ATOM   1138  OG1 THR A 478     -44.762 -19.194 -19.138  1.00129.86           O  
ANISOU 1138  OG1 THR A 478    15138  20470  13734  -3995   2471  -2504       O  
ATOM   1139  CG2 THR A 478     -46.283 -20.926 -18.423  1.00109.45           C  
ANISOU 1139  CG2 THR A 478    12333  17900  11352  -4291   2730  -2677       C  
ATOM   1140  N   PRO A 479     -41.681 -21.717 -18.968  1.00135.80           N  
ANISOU 1140  N   PRO A 479    16235  20655  14706  -4246   2566  -2185       N  
ATOM   1141  CA  PRO A 479     -40.360 -21.512 -19.577  1.00139.22           C  
ANISOU 1141  CA  PRO A 479    16797  21000  15101  -4163   2452  -2082       C  
ATOM   1142  C   PRO A 479     -40.402 -20.711 -20.875  1.00142.30           C  
ANISOU 1142  C   PRO A 479    17111  21540  15417  -4020   2303  -2178       C  
ATOM   1143  O   PRO A 479     -41.205 -21.031 -21.752  1.00134.39           O  
ANISOU 1143  O   PRO A 479    15937  20665  14461  -4036   2294  -2362       O  
ATOM   1144  CB  PRO A 479     -39.879 -22.940 -19.843  1.00130.53           C  
ANISOU 1144  CB  PRO A 479    15703  19749  14142  -4302   2525  -2091       C  
ATOM   1145  CG  PRO A 479     -41.136 -23.749 -19.937  1.00132.59           C  
ANISOU 1145  CG  PRO A 479    15780  20078  14518  -4434   2635  -2270       C  
ATOM   1146  CD  PRO A 479     -42.040 -23.143 -18.912  1.00132.25           C  
ANISOU 1146  CD  PRO A 479    15711  20121  14417  -4430   2701  -2258       C  
ATOM   1147  N   CYS A 480     -39.578 -19.669 -20.979  1.00161.01           N  
ANISOU 1147  N   CYS A 480    19605  23901  17673  -3880   2191  -2058       N  
ATOM   1148  CA  CYS A 480     -39.477 -18.882 -22.212  1.00173.87           C  
ANISOU 1148  CA  CYS A 480    21187  25653  19223  -3734   2052  -2117       C  
ATOM   1149  C   CYS A 480     -38.060 -18.812 -22.788  1.00173.82           C  
ANISOU 1149  C   CYS A 480    21308  25542  19193  -3681   1967  -1997       C  
ATOM   1150  O   CYS A 480     -37.329 -17.858 -22.534  1.00173.07           O  
ANISOU 1150  O   CYS A 480    21344  25407  19007  -3583   1899  -1861       O  
ATOM   1151  CB  CYS A 480     -40.017 -17.466 -21.990  1.00181.06           C  
ANISOU 1151  CB  CYS A 480    22099  26689  20008  -3588   1987  -2109       C  
ATOM   1152  SG  CYS A 480     -41.667 -17.390 -21.209  1.00190.15           S  
ANISOU 1152  SG  CYS A 480    23103  27979  21165  -3631   2083  -2241       S  
ATOM   1153  N   ASN A 481     -37.683 -19.833 -23.549  1.00173.04           N  
ANISOU 1153  N   ASN A 481    21166  25399  19180  -3750   1974  -2055       N  
ATOM   1154  CA  ASN A 481     -36.398 -19.863 -24.238  1.00164.80           C  
ANISOU 1154  CA  ASN A 481    20218  24280  18118  -3701   1894  -1966       C  
ATOM   1155  C   ASN A 481     -36.304 -18.807 -25.335  1.00155.74           C  
ANISOU 1155  C   ASN A 481    19042  23272  16859  -3534   1762  -1988       C  
ATOM   1156  O   ASN A 481     -35.211 -18.385 -25.715  1.00152.31           O  
ANISOU 1156  O   ASN A 481    18714  22785  16372  -3463   1688  -1873       O  
ATOM   1157  CB  ASN A 481     -36.161 -21.248 -24.844  1.00157.11           C  
ANISOU 1157  CB  ASN A 481    19184  23243  17266  -3810   1936  -2050       C  
ATOM   1158  CG  ASN A 481     -36.067 -22.324 -23.793  1.00158.43           C  
ANISOU 1158  CG  ASN A 481    19409  23242  17547  -3968   2068  -1998       C  
ATOM   1159  OD1 ASN A 481     -35.851 -22.029 -22.618  1.00164.54           O  
ANISOU 1159  OD1 ASN A 481    20298  23929  18291  -3984   2117  -1862       O  
ATOM   1160  ND2 ASN A 481     -36.211 -23.578 -24.204  1.00148.87           N  
ANISOU 1160  ND2 ASN A 481    18120  21981  16464  -4081   2130  -2105       N  
ATOM   1161  N   GLY A 482     -37.454 -18.374 -25.836  1.00146.31           N  
ANISOU 1161  N   GLY A 482    17703  22259  15627  -3470   1737  -2133       N  
ATOM   1162  CA  GLY A 482     -37.485 -17.392 -26.900  1.00134.32           C  
ANISOU 1162  CA  GLY A 482    16151  20886  13999  -3300   1618  -2159       C  
ATOM   1163  C   GLY A 482     -37.528 -16.082 -26.148  1.00137.04           C  
ANISOU 1163  C   GLY A 482    16598  21226  14245  -3203   1590  -2043       C  
ATOM   1164  O   GLY A 482     -36.839 -15.904 -25.140  1.00141.12           O  
ANISOU 1164  O   GLY A 482    17261  21594  14763  -3243   1621  -1894       O  
ATOM   1165  N   VAL A 483     -38.402 -15.186 -26.548  1.00132.74           N  
ANISOU 1165  N   VAL A 483    15973  20846  13616  -3076   1536  -2121       N  
ATOM   1166  CA  VAL A 483     -38.302 -13.758 -26.257  1.00136.46           C  
ANISOU 1166  CA  VAL A 483    16544  21327  13976  -2935   1474  -2015       C  
ATOM   1167  C   VAL A 483     -39.729 -13.356 -25.860  1.00127.26           C  
ANISOU 1167  C   VAL A 483    15263  20306  12783  -2897   1500  -2138       C  
ATOM   1168  O   VAL A 483     -40.614 -14.209 -25.745  1.00126.09           O  
ANISOU 1168  O   VAL A 483    14974  20228  12707  -2996   1571  -2282       O  
ATOM   1169  CB  VAL A 483     -38.005 -12.848 -27.474  1.00132.04           C  
ANISOU 1169  CB  VAL A 483    15993  20862  13314  -2758   1359  -1993       C  
ATOM   1170  CG1 VAL A 483     -37.449 -11.512 -27.038  1.00129.03           C  
ANISOU 1170  CG1 VAL A 483    15772  20405  12849  -2650   1308  -1832       C  
ATOM   1171  CG2 VAL A 483     -36.972 -13.498 -28.361  1.00127.12           C  
ANISOU 1171  CG2 VAL A 483    15393  20187  12719  -2786   1329  -1958       C  
ATOM   1172  N   GLU A 484     -39.939 -12.060 -25.654  1.00101.04           N  
ANISOU 1172  N   GLU A 484    12001  17027   9363  -2755   1445  -2084       N  
ATOM   1173  CA  GLU A 484     -41.052 -11.448 -24.947  1.00 84.20           C  
ANISOU 1173  CA  GLU A 484     9814  14987   7190  -2707   1469  -2148       C  
ATOM   1174  C   GLU A 484     -42.442 -12.046 -25.175  1.00 99.09           C  
ANISOU 1174  C   GLU A 484    11486  17056   9109  -2743   1514  -2359       C  
ATOM   1175  O   GLU A 484     -42.827 -12.397 -26.290  1.00110.86           O  
ANISOU 1175  O   GLU A 484    12843  18681  10599  -2706   1476  -2488       O  
ATOM   1176  CB  GLU A 484     -41.108  -9.953 -25.300  1.00 74.55           C  
ANISOU 1176  CB  GLU A 484     8655  13826   5847  -2502   1370  -2095       C  
ATOM   1177  CG  GLU A 484     -39.851  -9.193 -24.866  1.00 82.72           C  
ANISOU 1177  CG  GLU A 484     9901  14677   6852  -2471   1335  -1894       C  
ATOM   1178  CD  GLU A 484     -39.571  -7.917 -25.651  1.00 86.54           C  
ANISOU 1178  CD  GLU A 484    10455  15190   7235  -2280   1231  -1825       C  
ATOM   1179  OE1 GLU A 484     -40.447  -7.027 -25.676  1.00 84.03           O  
ANISOU 1179  OE1 GLU A 484    10099  14983   6845  -2144   1198  -1879       O  
ATOM   1180  OE2 GLU A 484     -38.463  -7.786 -26.212  1.00 89.57           O  
ANISOU 1180  OE2 GLU A 484    10937  15482   7613  -2265   1188  -1711       O  
ATOM   1181  N   GLY A 485     -43.187 -12.133 -24.077  1.00105.35           N  
ANISOU 1181  N   GLY A 485    12245  17857   9927  -2813   1598  -2395       N  
ATOM   1182  CA  GLY A 485     -44.509 -12.723 -24.046  1.00113.44           C  
ANISOU 1182  CA  GLY A 485    13069  19038  10995  -2874   1663  -2587       C  
ATOM   1183  C   GLY A 485     -45.085 -12.506 -22.660  1.00117.64           C  
ANISOU 1183  C   GLY A 485    13619  19551  11528  -2925   1749  -2566       C  
ATOM   1184  O   GLY A 485     -44.677 -11.578 -21.961  1.00112.38           O  
ANISOU 1184  O   GLY A 485    13099  18808  10793  -2847   1722  -2436       O  
ATOM   1185  N   PHE A 486     -46.020 -13.351 -22.245  1.00130.06           N  
ANISOU 1185  N   PHE A 486    15045  21192  13178  -3056   1855  -2695       N  
ATOM   1186  CA  PHE A 486     -46.597 -13.187 -20.923  1.00117.75           C  
ANISOU 1186  CA  PHE A 486    13497  19629  11615  -3106   1946  -2676       C  
ATOM   1187  C   PHE A 486     -45.616 -13.745 -19.898  1.00124.36           C  
ANISOU 1187  C   PHE A 486    14500  20241  12510  -3241   2028  -2504       C  
ATOM   1188  O   PHE A 486     -45.177 -14.889 -20.014  1.00127.35           O  
ANISOU 1188  O   PHE A 486    14878  20517  12994  -3389   2091  -2494       O  
ATOM   1189  CB  PHE A 486     -47.954 -13.887 -20.839  1.00117.77           C  
ANISOU 1189  CB  PHE A 486    13277  19790  11680  -3203   2040  -2873       C  
ATOM   1190  CG  PHE A 486     -48.860 -13.328 -19.787  1.00124.35           C  
ANISOU 1190  CG  PHE A 486    14074  20712  12463  -3177   2097  -2898       C  
ATOM   1191  CD1 PHE A 486     -49.436 -12.082 -19.974  1.00131.22           C  
ANISOU 1191  CD1 PHE A 486    14916  21731  13210  -2978   2005  -2944       C  
ATOM   1192  CD2 PHE A 486     -49.147 -14.030 -18.627  1.00120.15           C  
ANISOU 1192  CD2 PHE A 486    13535  20117  12000  -3341   2245  -2874       C  
ATOM   1193  CE1 PHE A 486     -50.278 -11.540 -19.024  1.00133.89           C  
ANISOU 1193  CE1 PHE A 486    15217  22159  13496  -2942   2053  -2975       C  
ATOM   1194  CE2 PHE A 486     -49.993 -13.491 -17.674  1.00124.23           C  
ANISOU 1194  CE2 PHE A 486    14011  20730  12459  -3309   2297  -2901       C  
ATOM   1195  CZ  PHE A 486     -50.555 -12.244 -17.875  1.00130.41           C  
ANISOU 1195  CZ  PHE A 486    14763  21666  13120  -3109   2199  -2956       C  
ATOM   1196  N   ASN A 487     -45.274 -12.936 -18.901  1.00119.46           N  
ANISOU 1196  N   ASN A 487    14022  19547  11818  -3184   2024  -2373       N  
ATOM   1197  CA  ASN A 487     -44.283 -13.324 -17.893  1.00128.68           C  
ANISOU 1197  CA  ASN A 487    15360  20515  13018  -3283   2086  -2202       C  
ATOM   1198  C   ASN A 487     -42.931 -13.752 -18.454  1.00127.12           C  
ANISOU 1198  C   ASN A 487    15281  20159  12860  -3315   2039  -2091       C  
ATOM   1199  O   ASN A 487     -42.266 -14.629 -17.900  1.00121.02           O  
ANISOU 1199  O   ASN A 487    14586  19238  12157  -3444   2116  -2001       O  
ATOM   1200  CB  ASN A 487     -44.838 -14.428 -17.004  1.00133.26           C  
ANISOU 1200  CB  ASN A 487    15873  21073  13687  -3463   2246  -2233       C  
ATOM   1201  CG  ASN A 487     -45.889 -13.923 -16.048  1.00136.68           C  
ANISOU 1201  CG  ASN A 487    16244  21623  14065  -3437   2307  -2282       C  
ATOM   1202  OD1 ASN A 487     -45.889 -12.749 -15.669  1.00146.50           O  
ANISOU 1202  OD1 ASN A 487    17559  22901  15202  -3295   2238  -2240       O  
ATOM   1203  ND2 ASN A 487     -46.780 -14.809 -15.632  1.00131.88           N  
ANISOU 1203  ND2 ASN A 487    15504  21070  13533  -3576   2440  -2373       N  
ATOM   1204  N   CYS A 488     -42.552 -13.142 -19.570  1.00134.21           N  
ANISOU 1204  N   CYS A 488    16188  21095  13711  -3191   1917  -2099       N  
ATOM   1205  CA  CYS A 488     -41.234 -13.315 -20.160  1.00129.51           C  
ANISOU 1205  CA  CYS A 488    15708  20367  13131  -3191   1857  -1989       C  
ATOM   1206  C   CYS A 488     -40.869 -11.955 -20.722  1.00109.99           C  
ANISOU 1206  C   CYS A 488    13311  17927  10553  -3007   1727  -1936       C  
ATOM   1207  O   CYS A 488     -41.330 -11.582 -21.795  1.00105.02           O  
ANISOU 1207  O   CYS A 488    12587  17430   9885  -2902   1656  -2029       O  
ATOM   1208  CB  CYS A 488     -41.226 -14.391 -21.245  1.00144.66           C  
ANISOU 1208  CB  CYS A 488    17517  22312  15135  -3268   1863  -2088       C  
ATOM   1209  SG  CYS A 488     -40.349 -15.908 -20.796  1.00175.64           S  
ANISOU 1209  SG  CYS A 488    21509  26040  19188  -3466   1966  -2010       S  
ATOM   1210  N   TYR A 489     -40.087 -11.191 -19.970  1.00113.42           N  
ANISOU 1210  N   TYR A 489    13911  18244  10938  -2963   1701  -1790       N  
ATOM   1211  CA  TYR A 489     -39.939  -9.767 -20.251  1.00112.02           C  
ANISOU 1211  CA  TYR A 489    13807  18093  10665  -2790   1596  -1745       C  
ATOM   1212  C   TYR A 489     -38.505  -9.359 -20.553  1.00103.98           C  
ANISOU 1212  C   TYR A 489    12946  16929   9632  -2758   1526  -1594       C  
ATOM   1213  O   TYR A 489     -37.556 -10.045 -20.175  1.00101.30           O  
ANISOU 1213  O   TYR A 489    12689  16456   9345  -2866   1560  -1503       O  
ATOM   1214  CB  TYR A 489     -40.464  -8.938 -19.074  1.00125.62           C  
ANISOU 1214  CB  TYR A 489    15573  19827  12331  -2739   1617  -1732       C  
ATOM   1215  CG  TYR A 489     -41.873  -9.286 -18.643  1.00141.79           C  
ANISOU 1215  CG  TYR A 489    17466  22021  14387  -2773   1695  -1874       C  
ATOM   1216  CD1 TYR A 489     -42.831  -9.681 -19.569  1.00156.13           C  
ANISOU 1216  CD1 TYR A 489    19102  24001  16220  -2760   1695  -2031       C  
ATOM   1217  CD2 TYR A 489     -42.250  -9.211 -17.307  1.00135.24           C  
ANISOU 1217  CD2 TYR A 489    16663  21179  13545  -2814   1771  -1858       C  
ATOM   1218  CE1 TYR A 489     -44.114 -10.004 -19.175  1.00157.46           C  
ANISOU 1218  CE1 TYR A 489    19118  24309  16401  -2799   1770  -2169       C  
ATOM   1219  CE2 TYR A 489     -43.534  -9.525 -16.908  1.00139.28           C  
ANISOU 1219  CE2 TYR A 489    17026  21830  14063  -2849   1850  -1986       C  
ATOM   1220  CZ  TYR A 489     -44.463  -9.916 -17.846  1.00145.76           C  
ANISOU 1220  CZ  TYR A 489    17666  22807  14909  -2845   1849  -2143       C  
ATOM   1221  OH  TYR A 489     -45.745 -10.234 -17.458  1.00137.30           O  
ANISOU 1221  OH  TYR A 489    16435  21883  13849  -2887   1931  -2279       O  
ATOM   1222  N   PHE A 490     -38.355  -8.233 -21.240  1.00 92.36           N  
ANISOU 1222  N   PHE A 490    11516  15486   8089  -2606   1429  -1567       N  
ATOM   1223  CA  PHE A 490     -37.036  -7.667 -21.462  1.00 94.46           C  
ANISOU 1223  CA  PHE A 490    11934  15617   8339  -2570   1365  -1421       C  
ATOM   1224  C   PHE A 490     -36.652  -6.865 -20.223  1.00 97.04           C  
ANISOU 1224  C   PHE A 490    12397  15835   8639  -2557   1368  -1328       C  
ATOM   1225  O   PHE A 490     -37.383  -5.967 -19.812  1.00 81.83           O  
ANISOU 1225  O   PHE A 490    10469  13965   6659  -2461   1352  -1366       O  
ATOM   1226  CB  PHE A 490     -37.018  -6.798 -22.725  1.00 90.20           C  
ANISOU 1226  CB  PHE A 490    11388  15146   7737  -2415   1271  -1420       C  
ATOM   1227  CG  PHE A 490     -35.649  -6.329 -23.117  1.00 83.59           C  
ANISOU 1227  CG  PHE A 490    10690  14178   6893  -2393   1215  -1274       C  
ATOM   1228  CD1 PHE A 490     -34.757  -7.193 -23.721  1.00 69.10           C  
ANISOU 1228  CD1 PHE A 490     8857  12293   5104  -2475   1218  -1234       C  
ATOM   1229  CD2 PHE A 490     -35.264  -5.022 -22.899  1.00 83.68           C  
ANISOU 1229  CD2 PHE A 490    10824  14116   6855  -2289   1161  -1183       C  
ATOM   1230  CE1 PHE A 490     -33.504  -6.768 -24.078  1.00 68.32           C  
ANISOU 1230  CE1 PHE A 490     8876  12085   4999  -2458   1171  -1103       C  
ATOM   1231  CE2 PHE A 490     -34.014  -4.585 -23.260  1.00 87.17           C  
ANISOU 1231  CE2 PHE A 490    11384  14437   7298  -2279   1117  -1053       C  
ATOM   1232  CZ  PHE A 490     -33.129  -5.465 -23.845  1.00 81.94           C  
ANISOU 1232  CZ  PHE A 490    10718  13737   6678  -2365   1123  -1012       C  
ATOM   1233  N   PRO A 491     -35.497  -7.197 -19.627  1.00 96.14           N  
ANISOU 1233  N   PRO A 491    12398  15571   8559  -2648   1385  -1215       N  
ATOM   1234  CA  PRO A 491     -35.031  -6.678 -18.333  1.00100.91           C  
ANISOU 1234  CA  PRO A 491    13125  16070   9146  -2661   1396  -1135       C  
ATOM   1235  C   PRO A 491     -35.023  -5.154 -18.206  1.00106.33           C  
ANISOU 1235  C   PRO A 491    13894  16737   9769  -2523   1323  -1105       C  
ATOM   1236  O   PRO A 491     -35.351  -4.635 -17.142  1.00134.45           O  
ANISOU 1236  O   PRO A 491    17495  20287  13301  -2501   1339  -1112       O  
ATOM   1237  CB  PRO A 491     -33.607  -7.231 -18.238  1.00105.09           C  
ANISOU 1237  CB  PRO A 491    13753  16459   9718  -2752   1396  -1020       C  
ATOM   1238  CG  PRO A 491     -33.658  -8.494 -19.023  1.00107.75           C  
ANISOU 1238  CG  PRO A 491    13993  16834  10114  -2836   1433  -1065       C  
ATOM   1239  CD  PRO A 491     -34.568  -8.202 -20.179  1.00106.12           C  
ANISOU 1239  CD  PRO A 491    13670  16768   9883  -2744   1395  -1168       C  
ATOM   1240  N   LEU A 492     -34.641  -4.449 -19.261  1.00 72.71           N  
ANISOU 1240  N   LEU A 492     9666  12470   5491  -2429   1247  -1069       N  
ATOM   1241  CA  LEU A 492     -34.417  -3.012 -19.156  1.00 71.14           C  
ANISOU 1241  CA  LEU A 492     9571  12212   5247  -2309   1181  -1018       C  
ATOM   1242  C   LEU A 492     -35.685  -2.193 -19.398  1.00 73.90           C  
ANISOU 1242  C   LEU A 492     9855  12683   5539  -2165   1156  -1111       C  
ATOM   1243  O   LEU A 492     -36.760  -2.738 -19.619  1.00 75.94           O  
ANISOU 1243  O   LEU A 492     9979  13085   5789  -2161   1190  -1222       O  
ATOM   1244  CB  LEU A 492     -33.335  -2.579 -20.142  1.00 75.62           C  
ANISOU 1244  CB  LEU A 492    10214  12696   5821  -2275   1119   -918       C  
ATOM   1245  CG  LEU A 492     -31.881  -2.873 -19.758  1.00 81.39           C  
ANISOU 1245  CG  LEU A 492    11050  13278   6596  -2381   1120   -806       C  
ATOM   1246  CD1 LEU A 492     -31.580  -4.362 -19.605  1.00 79.44           C  
ANISOU 1246  CD1 LEU A 492    10748  13036   6398  -2522   1180   -814       C  
ATOM   1247  CD2 LEU A 492     -30.942  -2.246 -20.765  1.00 95.97           C  
ANISOU 1247  CD2 LEU A 492    12965  15057   8442  -2331   1060   -713       C  
ATOM   1248  N   GLN A 493     -35.524  -0.870 -19.372  1.00 70.29           N  
ANISOU 1248  N   GLN A 493     9496  12164   5046  -2046   1097  -1066       N  
ATOM   1249  CA  GLN A 493     -36.591   0.110 -19.615  1.00 71.31           C  
ANISOU 1249  CA  GLN A 493     9593  12386   5116  -1882   1061  -1136       C  
ATOM   1250  C   GLN A 493     -35.927   1.478 -19.770  1.00 79.20           C  
ANISOU 1250  C   GLN A 493    10739  13254   6101  -1776    995  -1042       C  
ATOM   1251  O   GLN A 493     -34.836   1.673 -19.255  1.00 70.72           O  
ANISOU 1251  O   GLN A 493     9779  12028   5064  -1847    989   -951       O  
ATOM   1252  CB  GLN A 493     -37.576   0.138 -18.454  1.00 76.67           C  
ANISOU 1252  CB  GLN A 493    10224  13135   5773  -1880   1105  -1231       C  
ATOM   1253  CG  GLN A 493     -38.813   0.989 -18.668  1.00 92.93           C  
ANISOU 1253  CG  GLN A 493    12224  15318   7767  -1712   1075  -1325       C  
ATOM   1254  CD  GLN A 493     -39.397   0.837 -20.048  1.00103.81           C  
ANISOU 1254  CD  GLN A 493    13493  16833   9117  -1626   1045  -1377       C  
ATOM   1255  OE1 GLN A 493     -39.685  -0.268 -20.487  1.00113.84           O  
ANISOU 1255  OE1 GLN A 493    14641  18203  10411  -1710   1084  -1437       O  
ATOM   1256  NE2 GLN A 493     -39.587   1.950 -20.737  1.00102.21           N  
ANISOU 1256  NE2 GLN A 493    13336  16636   8863  -1451    978  -1358       N  
ATOM   1257  N   SER A 494     -36.538   2.430 -20.472  1.00 84.59           N  
ANISOU 1257  N   SER A 494    11420  13988   6733  -1608    946  -1060       N  
ATOM   1258  CA  SER A 494     -35.871   3.718 -20.592  1.00 92.18           C  
ANISOU 1258  CA  SER A 494    12531  14801   7693  -1518    893   -962       C  
ATOM   1259  C   SER A 494     -36.551   4.885 -19.942  1.00 90.81           C  
ANISOU 1259  C   SER A 494    12409  14608   7485  -1387    868  -1006       C  
ATOM   1260  O   SER A 494     -37.739   4.848 -19.714  1.00 89.48           O  
ANISOU 1260  O   SER A 494    12145  14581   7272  -1316    879  -1118       O  
ATOM   1261  CB  SER A 494     -35.835   4.027 -22.052  1.00109.09           C  
ANISOU 1261  CB  SER A 494    14663  16983   9804  -1409    853   -915       C  
ATOM   1262  OG  SER A 494     -37.166   4.258 -22.435  1.00126.55           O  
ANISOU 1262  OG  SER A 494    16775  19361  11949  -1266    839  -1019       O  
ATOM   1263  N   TYR A 495     -35.805   5.949 -19.686  1.00 96.11           N  
ANISOU 1263  N   TYR A 495    13230  15108   8181  -1350    833   -923       N  
ATOM   1264  CA  TYR A 495     -36.378   7.122 -19.040  1.00114.00           C  
ANISOU 1264  CA  TYR A 495    15560  17333  10422  -1222    806   -965       C  
ATOM   1265  C   TYR A 495     -36.889   8.165 -20.009  1.00105.68           C  
ANISOU 1265  C   TYR A 495    14538  16292   9325  -1023    759   -946       C  
ATOM   1266  O   TYR A 495     -36.246   8.460 -20.999  1.00 92.47           O  
ANISOU 1266  O   TYR A 495    12923  14549   7662   -993    737   -842       O  
ATOM   1267  CB  TYR A 495     -35.349   7.804 -18.153  1.00130.89           C  
ANISOU 1267  CB  TYR A 495    17846  19269  12617  -1281    794   -902       C  
ATOM   1268  CG  TYR A 495     -34.798   6.981 -17.018  1.00140.79           C  
ANISOU 1268  CG  TYR A 495    19093  20497  13904  -1451    833   -917       C  
ATOM   1269  CD1 TYR A 495     -35.630   6.355 -16.111  1.00139.30           C  
ANISOU 1269  CD1 TYR A 495    18813  20432  13682  -1484    875  -1020       C  
ATOM   1270  CD2 TYR A 495     -33.438   6.848 -16.848  1.00145.47           C  
ANISOU 1270  CD2 TYR A 495    19770  20944  14556  -1574    831   -824       C  
ATOM   1271  CE1 TYR A 495     -35.113   5.603 -15.075  1.00128.96           C  
ANISOU 1271  CE1 TYR A 495    17505  19100  12395  -1628    916  -1021       C  
ATOM   1272  CE2 TYR A 495     -32.916   6.103 -15.818  1.00139.13           C  
ANISOU 1272  CE2 TYR A 495    18965  20124  13774  -1714    864   -834       C  
ATOM   1273  CZ  TYR A 495     -33.756   5.487 -14.939  1.00127.53           C  
ANISOU 1273  CZ  TYR A 495    17413  18776  12267  -1736    907   -927       C  
ATOM   1274  OH  TYR A 495     -33.212   4.756 -13.924  1.00122.68           O  
ANISOU 1274  OH  TYR A 495    16804  18142  11665  -1865    943   -923       O  
ATOM   1275  N   GLY A 496     -38.038   8.757 -19.712  1.00101.69           N  
ANISOU 1275  N   GLY A 496    13998  15874   8766   -879    744  -1042       N  
ATOM   1276  CA  GLY A 496     -38.602   9.786 -20.569  1.00 96.03           C  
ANISOU 1276  CA  GLY A 496    13315  15174   7999   -668    698  -1028       C  
ATOM   1277  C   GLY A 496     -38.055  10.898 -19.708  1.00103.41           C  
ANISOU 1277  C   GLY A 496    14410  15900   8980   -650    678   -988       C  
ATOM   1278  O   GLY A 496     -38.536  11.146 -18.617  1.00125.64           O  
ANISOU 1278  O   GLY A 496    17224  18724  11790   -639    683  -1077       O  
ATOM   1279  N   PHE A 497     -37.044  11.576 -20.226  1.00 78.10           N  
ANISOU 1279  N   PHE A 497    11339  12511   5823   -647    658   -857       N  
ATOM   1280  CA  PHE A 497     -36.564  12.847 -19.711  1.00103.49           C  
ANISOU 1280  CA  PHE A 497    14718  15515   9089   -595    633   -813       C  
ATOM   1281  C   PHE A 497     -36.980  14.089 -20.496  1.00105.36           C  
ANISOU 1281  C   PHE A 497    15041  15692   9298   -379    596   -765       C  
ATOM   1282  O   PHE A 497     -36.293  14.492 -21.420  1.00 92.92           O  
ANISOU 1282  O   PHE A 497    13549  14009   7747   -356    591   -635       O  
ATOM   1283  CB  PHE A 497     -35.047  12.811 -19.619  1.00106.92           C  
ANISOU 1283  CB  PHE A 497    15254  15758   9614   -759    643   -699       C  
ATOM   1284  CG  PHE A 497     -34.533  11.899 -18.552  1.00110.52           C  
ANISOU 1284  CG  PHE A 497    15668  16222  10104   -951    672   -745       C  
ATOM   1285  CD1 PHE A 497     -35.322  11.562 -17.484  1.00104.88           C  
ANISOU 1285  CD1 PHE A 497    14880  15613   9354   -958    685   -871       C  
ATOM   1286  CD2 PHE A 497     -33.258  11.391 -18.617  1.00113.42           C  
ANISOU 1286  CD2 PHE A 497    16068  16492  10532  -1116    687   -657       C  
ATOM   1287  CE1 PHE A 497     -34.851  10.731 -16.501  1.00100.91           C  
ANISOU 1287  CE1 PHE A 497    14347  15119   8874  -1122    716   -901       C  
ATOM   1288  CE2 PHE A 497     -32.780  10.556 -17.637  1.00104.67           C  
ANISOU 1288  CE2 PHE A 497    14927  15394   9448  -1277    712   -694       C  
ATOM   1289  CZ  PHE A 497     -33.576  10.231 -16.575  1.00 96.60           C  
ANISOU 1289  CZ  PHE A 497    13841  14475   8388  -1278    727   -811       C  
ATOM   1290  N   GLN A 498     -38.069  14.731 -20.093  1.00126.43           N  
ANISOU 1290  N   GLN A 498    17698  18423  11918   -218    574   -864       N  
ATOM   1291  CA  GLN A 498     -38.515  15.937 -20.774  1.00130.87           C  
ANISOU 1291  CA  GLN A 498    18349  18924  12450      5    539   -820       C  
ATOM   1292  C   GLN A 498     -38.251  17.129 -19.867  1.00122.43           C  
ANISOU 1292  C   GLN A 498    17432  17640  11447     45    520   -829       C  
ATOM   1293  O   GLN A 498     -38.294  16.999 -18.645  1.00140.98           O  
ANISOU 1293  O   GLN A 498    19765  19981  13818    -37    525   -927       O  
ATOM   1294  CB  GLN A 498     -40.005  15.834 -21.100  1.00140.36           C  
ANISOU 1294  CB  GLN A 498    19421  20366  13542    187    521   -933       C  
ATOM   1295  CG  GLN A 498     -40.338  14.764 -22.117  1.00140.09           C  
ANISOU 1295  CG  GLN A 498    19236  20548  13443    172    532   -937       C  
ATOM   1296  CD  GLN A 498     -41.818  14.700 -22.417  1.00150.75           C  
ANISOU 1296  CD  GLN A 498    20448  22143  14686    353    512  -1064       C  
ATOM   1297  OE1 GLN A 498     -42.643  15.114 -21.605  1.00154.09           O  
ANISOU 1297  OE1 GLN A 498    20850  22614  15084    438    501  -1177       O  
ATOM   1298  NE2 GLN A 498     -42.163  14.178 -23.588  1.00150.26           N  
ANISOU 1298  NE2 GLN A 498    20285  22251  14557    416    504  -1053       N  
ATOM   1299  N   PRO A 499     -37.989  18.305 -20.458  1.00106.00           N  
ANISOU 1299  N   PRO A 499    15499  15384   9395    177    500   -729       N  
ATOM   1300  CA  PRO A 499     -37.726  19.480 -19.626  1.00110.04           C  
ANISOU 1300  CA  PRO A 499    16158  15671   9980    216    482   -744       C  
ATOM   1301  C   PRO A 499     -39.015  20.092 -19.092  1.00131.69           C  
ANISOU 1301  C   PRO A 499    18877  18500  12658    412    451   -879       C  
ATOM   1302  O   PRO A 499     -38.983  21.147 -18.458  1.00135.12           O  
ANISOU 1302  O   PRO A 499    19432  18764  13144    484    430   -908       O  
ATOM   1303  CB  PRO A 499     -37.007  20.439 -20.582  1.00113.76           C  
ANISOU 1303  CB  PRO A 499    16789  15927  10508    283    483   -577       C  
ATOM   1304  CG  PRO A 499     -37.308  19.933 -21.978  1.00122.14           C  
ANISOU 1304  CG  PRO A 499    17777  17148  11483    365    491   -492       C  
ATOM   1305  CD  PRO A 499     -38.077  18.648 -21.886  1.00118.34           C  
ANISOU 1305  CD  PRO A 499    17094  16958  10913    321    494   -609       C  
ATOM   1306  N   THR A 500     -40.136  19.425 -19.353  1.00133.26           N  
ANISOU 1306  N   THR A 500    18917  18966  12748    497    448   -967       N  
ATOM   1307  CA  THR A 500     -41.429  19.843 -18.824  1.00132.29           C  
ANISOU 1307  CA  THR A 500    18740  18971  12553    676    422  -1112       C  
ATOM   1308  C   THR A 500     -41.938  18.815 -17.820  1.00128.96           C  
ANISOU 1308  C   THR A 500    18157  18745  12095    553    445  -1259       C  
ATOM   1309  O   THR A 500     -42.984  19.001 -17.198  1.00126.45           O  
ANISOU 1309  O   THR A 500    17771  18555  11717    665    433  -1395       O  
ATOM   1310  CB  THR A 500     -42.469  20.026 -19.939  1.00113.39           C  
ANISOU 1310  CB  THR A 500    16284  16747  10054    907    398  -1111       C  
ATOM   1311  OG1 THR A 500     -42.627  18.794 -20.653  1.00 91.78           O  
ANISOU 1311  OG1 THR A 500    13386  14226   7260    825    420  -1109       O  
ATOM   1312  CG2 THR A 500     -42.023  21.115 -20.899  1.00106.60           C  
ANISOU 1312  CG2 THR A 500    15595  15689   9221   1050    381   -955       C  
ATOM   1313  N   ASN A 501     -41.190  17.726 -17.674  1.00125.65           N  
ANISOU 1313  N   ASN A 501    17679  18349  11711    326    483  -1226       N  
ATOM   1314  CA  ASN A 501     -41.498  16.718 -16.672  1.00124.43           C  
ANISOU 1314  CA  ASN A 501    17394  18347  11537    186    517  -1341       C  
ATOM   1315  C   ASN A 501     -41.209  17.227 -15.272  1.00129.73           C  
ANISOU 1315  C   ASN A 501    18145  18895  12253    138    513  -1407       C  
ATOM   1316  O   ASN A 501     -40.500  18.217 -15.094  1.00136.23           O  
ANISOU 1316  O   ASN A 501    19127  19487  13147    161    487  -1353       O  
ATOM   1317  CB  ASN A 501     -40.706  15.435 -16.926  1.00118.60           C  
ANISOU 1317  CB  ASN A 501    16587  17646  10828    -36    559  -1277       C  
ATOM   1318  CG  ASN A 501     -41.442  14.469 -17.826  1.00131.97           C  
ANISOU 1318  CG  ASN A 501    18115  19575  12451    -19    577  -1304       C  
ATOM   1319  OD1 ASN A 501     -42.630  14.642 -18.103  1.00135.37           O  
ANISOU 1319  OD1 ASN A 501    18456  20174  12803    145    561  -1394       O  
ATOM   1320  ND2 ASN A 501     -40.743  13.438 -18.282  1.00141.54           N  
ANISOU 1320  ND2 ASN A 501    19280  20808  13692   -185    607  -1238       N  
ATOM   1321  N   GLY A 502     -41.772  16.547 -14.281  1.00115.34           N  
ANISOU 1321  N   GLY A 502    16207  17229  10388     73    543  -1527       N  
ATOM   1322  CA  GLY A 502     -41.549  16.897 -12.893  1.00127.20           C  
ANISOU 1322  CA  GLY A 502    17764  18651  11914     26    542  -1601       C  
ATOM   1323  C   GLY A 502     -40.096  16.740 -12.487  1.00124.18           C  
ANISOU 1323  C   GLY A 502    17482  18079  11624   -165    550  -1516       C  
ATOM   1324  O   GLY A 502     -39.331  16.037 -13.150  1.00107.18           O  
ANISOU 1324  O   GLY A 502    15319  15899   9505   -296    570  -1411       O  
ATOM   1325  N   VAL A 503     -39.714  17.419 -11.408  1.00132.52           N  
ANISOU 1325  N   VAL A 503    18630  19006  12716   -174    530  -1569       N  
ATOM   1326  CA  VAL A 503     -38.353  17.348 -10.887  1.00118.18           C  
ANISOU 1326  CA  VAL A 503    16903  17017  10983   -346    530  -1511       C  
ATOM   1327  C   VAL A 503     -38.046  15.935 -10.392  1.00111.81           C  
ANISOU 1327  C   VAL A 503    15988  16343  10151   -535    582  -1510       C  
ATOM   1328  O   VAL A 503     -36.895  15.497 -10.387  1.00105.82           O  
ANISOU 1328  O   VAL A 503    15269  15487   9452   -694    592  -1429       O  
ATOM   1329  CB  VAL A 503     -38.129  18.358  -9.753  1.00102.31           C  
ANISOU 1329  CB  VAL A 503    14997  14869   9008   -303    495  -1598       C  
ATOM   1330  CG1 VAL A 503     -36.645  18.485  -9.442  1.00 92.13           C  
ANISOU 1330  CG1 VAL A 503    13812  13377   7818   -462    484  -1533       C  
ATOM   1331  CG2 VAL A 503     -38.697  19.713 -10.142  1.00 93.51           C  
ANISOU 1331  CG2 VAL A 503    13975  13648   7906    -91    449  -1623       C  
ATOM   1332  N   GLY A 504     -39.086  15.231  -9.957  1.00112.35           N  
ANISOU 1332  N   GLY A 504    15920  16633  10133   -516    619  -1602       N  
ATOM   1333  CA  GLY A 504     -38.937  13.845  -9.560  1.00121.76           C  
ANISOU 1333  CA  GLY A 504    17006  17958  11300   -684    680  -1596       C  
ATOM   1334  C   GLY A 504     -38.605  12.950 -10.740  1.00133.22           C  
ANISOU 1334  C   GLY A 504    18403  19442  12773   -773    704  -1491       C  
ATOM   1335  O   GLY A 504     -37.975  11.908 -10.574  1.00133.38           O  
ANISOU 1335  O   GLY A 504    18386  19482  12809   -939    744  -1444       O  
ATOM   1336  N   TYR A 505     -39.014  13.374 -11.934  1.00136.91           N  
ANISOU 1336  N   TYR A 505    18870  19913  13236   -654    678  -1456       N  
ATOM   1337  CA  TYR A 505     -38.796  12.599 -13.153  1.00131.65           C  
ANISOU 1337  CA  TYR A 505    18146  19295  12580   -711    695  -1368       C  
ATOM   1338  C   TYR A 505     -37.615  13.131 -13.963  1.00116.23           C  
ANISOU 1338  C   TYR A 505    16323  17137  10703   -737    663  -1233       C  
ATOM   1339  O   TYR A 505     -37.174  12.497 -14.921  1.00112.42           O  
ANISOU 1339  O   TYR A 505    15810  16668  10235   -804    676  -1146       O  
ATOM   1340  CB  TYR A 505     -40.062  12.595 -14.013  1.00146.54           C  
ANISOU 1340  CB  TYR A 505    19925  21357  14396   -560    691  -1422       C  
ATOM   1341  CG  TYR A 505     -41.266  11.988 -13.325  1.00157.00           C  
ANISOU 1341  CG  TYR A 505    21100  22903  15649   -545    732  -1557       C  
ATOM   1342  CD1 TYR A 505     -41.116  10.977 -12.385  1.00152.85           C  
ANISOU 1342  CD1 TYR A 505    20509  22443  15124   -710    791  -1588       C  
ATOM   1343  CD2 TYR A 505     -42.551  12.427 -13.614  1.00168.40           C  
ANISOU 1343  CD2 TYR A 505    22467  24493  17023   -364    715  -1652       C  
ATOM   1344  CE1 TYR A 505     -42.211  10.418 -11.752  1.00152.34           C  
ANISOU 1344  CE1 TYR A 505    20307  22577  14997   -705    840  -1704       C  
ATOM   1345  CE2 TYR A 505     -43.654  11.874 -12.987  1.00164.80           C  
ANISOU 1345  CE2 TYR A 505    21865  24248  16505   -358    758  -1780       C  
ATOM   1346  CZ  TYR A 505     -43.478  10.871 -12.057  1.00159.55           C  
ANISOU 1346  CZ  TYR A 505    21138  23637  15846   -534    824  -1803       C  
ATOM   1347  OH  TYR A 505     -44.569  10.315 -11.427  1.00152.86           O  
ANISOU 1347  OH  TYR A 505    20144  22995  14939   -535    878  -1922       O  
ATOM   1348  N   GLN A 506     -37.114  14.300 -13.579  1.00 95.14           N  
ANISOU 1348  N   GLN A 506    13793  14276   8081   -684    624  -1219       N  
ATOM   1349  CA  GLN A 506     -35.943  14.886 -14.222  1.00 89.22           C  
ANISOU 1349  CA  GLN A 506    13172  13313   7415   -721    601  -1093       C  
ATOM   1350  C   GLN A 506     -34.690  14.065 -13.910  1.00 93.33           C  
ANISOU 1350  C   GLN A 506    13699  13773   7990   -935    625  -1031       C  
ATOM   1351  O   GLN A 506     -34.655  13.341 -12.917  1.00 96.03           O  
ANISOU 1351  O   GLN A 506    13984  14191   8312  -1036    649  -1093       O  
ATOM   1352  CB  GLN A 506     -35.772  16.339 -13.776  1.00 92.00           C  
ANISOU 1352  CB  GLN A 506    13668  13471   7816   -619    559  -1113       C  
ATOM   1353  CG  GLN A 506     -36.690  17.306 -14.506  1.00102.73           C  
ANISOU 1353  CG  GLN A 506    15062  14829   9143   -397    530  -1118       C  
ATOM   1354  CD  GLN A 506     -36.633  18.708 -13.938  1.00113.28           C  
ANISOU 1354  CD  GLN A 506    16537  15973  10529   -291    492  -1157       C  
ATOM   1355  OE1 GLN A 506     -35.601  19.144 -13.430  1.00116.57           O  
ANISOU 1355  OE1 GLN A 506    17056  16199  11035   -390    482  -1133       O  
ATOM   1356  NE2 GLN A 506     -37.744  19.429 -14.037  1.00113.45           N  
ANISOU 1356  NE2 GLN A 506    16560  16047  10498    -84    468  -1224       N  
ATOM   1357  N   PRO A 507     -33.660  14.160 -14.765  1.00104.95           N  
ANISOU 1357  N   PRO A 507    15237  15116   9525   -998    620   -905       N  
ATOM   1358  CA  PRO A 507     -32.467  13.332 -14.562  1.00111.11           C  
ANISOU 1358  CA  PRO A 507    16013  15852  10351  -1193    641   -845       C  
ATOM   1359  C   PRO A 507     -31.491  13.897 -13.532  1.00100.48           C  
ANISOU 1359  C   PRO A 507    14766  14338   9074  -1276    620   -862       C  
ATOM   1360  O   PRO A 507     -31.485  15.102 -13.273  1.00105.56           O  
ANISOU 1360  O   PRO A 507    15510  14842   9757  -1191    588   -887       O  
ATOM   1361  CB  PRO A 507     -31.826  13.312 -15.950  1.00105.13           C  
ANISOU 1361  CB  PRO A 507    15283  15034   9627  -1208    644   -710       C  
ATOM   1362  CG  PRO A 507     -32.208  14.615 -16.540  1.00100.42           C  
ANISOU 1362  CG  PRO A 507    14779  14334   9041  -1039    615   -681       C  
ATOM   1363  CD  PRO A 507     -33.592  14.922 -16.025  1.00106.58           C  
ANISOU 1363  CD  PRO A 507    15513  15233   9751   -890    603   -806       C  
ATOM   1364  N   TYR A 508     -30.674  13.024 -12.950  1.00 81.90           N  
ANISOU 1364  N   TYR A 508    12382  12000   6735  -1437    639   -853       N  
ATOM   1365  CA  TYR A 508     -29.632  13.444 -12.021  1.00 83.04           C  
ANISOU 1365  CA  TYR A 508    12607  12003   6941  -1528    616   -870       C  
ATOM   1366  C   TYR A 508     -28.381  12.602 -12.239  1.00 77.83           C  
ANISOU 1366  C   TYR A 508    11934  11316   6321  -1696    632   -784       C  
ATOM   1367  O   TYR A 508     -28.450  11.376 -12.357  1.00 73.76           O  
ANISOU 1367  O   TYR A 508    11327  10936   5762  -1767    667   -765       O  
ATOM   1368  CB  TYR A 508     -30.082  13.341 -10.556  1.00 86.95           C  
ANISOU 1368  CB  TYR A 508    13076  12575   7387  -1522    614   -998       C  
ATOM   1369  CG  TYR A 508     -30.955  14.485 -10.075  1.00 82.03           C  
ANISOU 1369  CG  TYR A 508    12500  11920   6749  -1367    583  -1097       C  
ATOM   1370  CD1 TYR A 508     -32.330  14.450 -10.239  1.00 87.31           C  
ANISOU 1370  CD1 TYR A 508    13101  12732   7341  -1235    596  -1155       C  
ATOM   1371  CD2 TYR A 508     -30.399  15.606  -9.473  1.00 78.49           C  
ANISOU 1371  CD2 TYR A 508    12160  11296   6366  -1350    540  -1142       C  
ATOM   1372  CE1 TYR A 508     -33.134  15.489  -9.801  1.00 79.33           C  
ANISOU 1372  CE1 TYR A 508    12132  11698   6312  -1083    566  -1249       C  
ATOM   1373  CE2 TYR A 508     -31.195  16.657  -9.039  1.00 89.14           C  
ANISOU 1373  CE2 TYR A 508    13555  12608   7704  -1202    511  -1238       C  
ATOM   1374  CZ  TYR A 508     -32.563  16.590  -9.208  1.00 87.93           C  
ANISOU 1374  CZ  TYR A 508    13337  12606   7468  -1064    523  -1289       C  
ATOM   1375  OH  TYR A 508     -33.367  17.623  -8.781  1.00 81.63           O  
ANISOU 1375  OH  TYR A 508    12582  11778   6655   -906    493  -1388       O  
ATOM   1376  N   ARG A 509     -27.243  13.276 -12.338  1.00 82.21           N  
ANISOU 1376  N   ARG A 509    12580  11693   6965  -1757    609   -733       N  
ATOM   1377  CA  ARG A 509     -25.962  12.612 -12.521  1.00 95.40           C  
ANISOU 1377  CA  ARG A 509    14242  13326   8678  -1911    618   -656       C  
ATOM   1378  C   ARG A 509     -25.372  12.256 -11.160  1.00110.77           C  
ANISOU 1378  C   ARG A 509    16182  15286  10620  -2005    606   -732       C  
ATOM   1379  O   ARG A 509     -25.015  13.136 -10.378  1.00112.80           O  
ANISOU 1379  O   ARG A 509    16507  15433  10919  -2000    571   -798       O  
ATOM   1380  CB  ARG A 509     -25.007  13.506 -13.307  1.00 99.65           C  
ANISOU 1380  CB  ARG A 509    14873  13676   9315  -1937    605   -565       C  
ATOM   1381  CG  ARG A 509     -25.510  13.851 -14.700  1.00113.86           C  
ANISOU 1381  CG  ARG A 509    16687  15466  11111  -1837    620   -474       C  
ATOM   1382  CD  ARG A 509     -24.572  14.815 -15.402  1.00126.72           C  
ANISOU 1382  CD  ARG A 509    18416  16893  12838  -1861    616   -377       C  
ATOM   1383  NE  ARG A 509     -24.806  14.861 -16.842  1.00127.94           N  
ANISOU 1383  NE  ARG A 509    18572  17063  12977  -1791    640   -260       N  
ATOM   1384  CZ  ARG A 509     -24.023  15.506 -17.700  1.00121.00           C  
ANISOU 1384  CZ  ARG A 509    17767  16038  12169  -1811    654   -145       C  
ATOM   1385  NH1 ARG A 509     -22.950  16.151 -17.262  1.00124.34           N  
ANISOU 1385  NH1 ARG A 509    18264  16284  12696  -1912    647   -138       N  
ATOM   1386  NH2 ARG A 509     -24.306  15.500 -18.994  1.00108.07           N  
ANISOU 1386  NH2 ARG A 509    16125  14437  10498  -1732    677    -39       N  
ATOM   1387  N   VAL A 510     -25.284  10.960 -10.879  1.00122.63           N  
ANISOU 1387  N   VAL A 510    17602  16924  12068  -2084    636   -724       N  
ATOM   1388  CA  VAL A 510     -24.881  10.485  -9.559  1.00111.25           C  
ANISOU 1388  CA  VAL A 510    16145  15529  10596  -2152    631   -792       C  
ATOM   1389  C   VAL A 510     -23.465   9.916  -9.530  1.00111.86           C  
ANISOU 1389  C   VAL A 510    16224  15564  10714  -2290    627   -732       C  
ATOM   1390  O   VAL A 510     -23.118   9.047 -10.329  1.00125.00           O  
ANISOU 1390  O   VAL A 510    17843  17270  12380  -2353    654   -645       O  
ATOM   1391  CB  VAL A 510     -25.847   9.409  -9.036  1.00 99.80           C  
ANISOU 1391  CB  VAL A 510    14604  14266   9048  -2135    676   -833       C  
ATOM   1392  CG1 VAL A 510     -25.433   8.952  -7.648  1.00116.48           C  
ANISOU 1392  CG1 VAL A 510    16710  16429  11118  -2191    675   -892       C  
ATOM   1393  CG2 VAL A 510     -27.270   9.936  -9.032  1.00 85.76           C  
ANISOU 1393  CG2 VAL A 510    12809  12550   7224  -1997    681   -903       C  
ATOM   1394  N   VAL A 511     -22.650  10.418  -8.610  1.00 89.26           N  
ANISOU 1394  N   VAL A 511    13408  12624   7883  -2334    588   -788       N  
ATOM   1395  CA  VAL A 511     -21.310   9.885  -8.411  1.00 84.01           C  
ANISOU 1395  CA  VAL A 511    12736  11938   7246  -2457    578   -752       C  
ATOM   1396  C   VAL A 511     -21.148   9.368  -6.979  1.00 82.98           C  
ANISOU 1396  C   VAL A 511    12583  11898   7046  -2478    569   -833       C  
ATOM   1397  O   VAL A 511     -21.508  10.047  -6.020  1.00 85.33           O  
ANISOU 1397  O   VAL A 511    12909  12189   7322  -2419    542   -937       O  
ATOM   1398  CB  VAL A 511     -20.236  10.940  -8.706  1.00 78.17           C  
ANISOU 1398  CB  VAL A 511    12065  11019   6616  -2506    539   -740       C  
ATOM   1399  CG1 VAL A 511     -18.868  10.284  -8.776  1.00 77.42           C  
ANISOU 1399  CG1 VAL A 511    11946  10920   6550  -2635    534   -687       C  
ATOM   1400  CG2 VAL A 511     -20.538  11.645 -10.013  1.00 73.89           C  
ANISOU 1400  CG2 VAL A 511    11563  10379   6134  -2459    551   -662       C  
ATOM   1401  N   VAL A 512     -20.623   8.154  -6.846  1.00 77.04           N  
ANISOU 1401  N   VAL A 512    11780  11236   6254  -2554    594   -783       N  
ATOM   1402  CA  VAL A 512     -20.446   7.518  -5.545  1.00 70.85           C  
ANISOU 1402  CA  VAL A 512    10975  10552   5392  -2568    594   -838       C  
ATOM   1403  C   VAL A 512     -18.990   7.166  -5.289  1.00 70.60           C  
ANISOU 1403  C   VAL A 512    10944  10495   5385  -2665    565   -815       C  
ATOM   1404  O   VAL A 512     -18.398   6.370  -6.014  1.00 75.55           O  
ANISOU 1404  O   VAL A 512    11542  11132   6031  -2733    586   -723       O  
ATOM   1405  CB  VAL A 512     -21.289   6.240  -5.428  1.00 70.17           C  
ANISOU 1405  CB  VAL A 512    10825  10617   5218  -2556    661   -804       C  
ATOM   1406  CG1 VAL A 512     -20.895   5.454  -4.195  1.00 70.15           C  
ANISOU 1406  CG1 VAL A 512    10808  10709   5136  -2581    670   -829       C  
ATOM   1407  CG2 VAL A 512     -22.772   6.582  -5.418  1.00 70.93           C  
ANISOU 1407  CG2 VAL A 512    10908  10767   5276  -2456    687   -854       C  
ATOM   1408  N   LEU A 513     -18.422   7.741  -4.238  1.00 71.39           N  
ANISOU 1408  N   LEU A 513    11072  10572   5479  -2664    515   -907       N  
ATOM   1409  CA  LEU A 513     -17.025   7.503  -3.908  1.00 79.09           C  
ANISOU 1409  CA  LEU A 513    12042  11534   6475  -2747    479   -906       C  
ATOM   1410  C   LEU A 513     -16.892   6.563  -2.731  1.00 92.99           C  
ANISOU 1410  C   LEU A 513    13772  13436   8123  -2737    487   -932       C  
ATOM   1411  O   LEU A 513     -17.289   6.904  -1.625  1.00116.23           O  
ANISOU 1411  O   LEU A 513    16728  16431  11002  -2673    469  -1029       O  
ATOM   1412  CB  LEU A 513     -16.312   8.816  -3.588  1.00 72.45           C  
ANISOU 1412  CB  LEU A 513    11244  10567   5715  -2764    412   -999       C  
ATOM   1413  CG  LEU A 513     -16.472   9.926  -4.623  1.00 80.75           C  
ANISOU 1413  CG  LEU A 513    12343  11458   6882  -2763    407   -977       C  
ATOM   1414  CD1 LEU A 513     -15.989  11.246  -4.053  1.00 74.22           C  
ANISOU 1414  CD1 LEU A 513    11564  10507   6130  -2766    347  -1094       C  
ATOM   1415  CD2 LEU A 513     -15.721   9.575  -5.898  1.00 94.69           C  
ANISOU 1415  CD2 LEU A 513    14092  13168   8717  -2848    429   -853       C  
ATOM   1416  N   SER A 514     -16.348   5.374  -2.966  1.00 80.00           N  
ANISOU 1416  N   SER A 514    12092  11855   6450  -2791    516   -844       N  
ATOM   1417  CA  SER A 514     -16.093   4.440  -1.877  1.00 93.11           C  
ANISOU 1417  CA  SER A 514    13733  13642   8004  -2778    526   -852       C  
ATOM   1418  C   SER A 514     -14.606   4.450  -1.540  1.00113.32           C  
ANISOU 1418  C   SER A 514    16288  16189  10582  -2835    467   -872       C  
ATOM   1419  O   SER A 514     -13.770   4.676  -2.414  1.00122.56           O  
ANISOU 1419  O   SER A 514    17452  17272  11844  -2907    445   -834       O  
ATOM   1420  CB  SER A 514     -16.557   3.028  -2.236  1.00 75.56           C  
ANISOU 1420  CB  SER A 514    11476  11503   5729  -2788    603   -745       C  
ATOM   1421  OG  SER A 514     -15.841   2.521  -3.346  1.00 85.65           O  
ANISOU 1421  OG  SER A 514    12734  12734   7075  -2863    611   -653       O  
ATOM   1422  N   PHE A 515     -14.280   4.211  -0.273  1.00111.78           N  
ANISOU 1422  N   PHE A 515    16090  16089  10293  -2798    442   -934       N  
ATOM   1423  CA  PHE A 515     -12.892   4.244   0.177  1.00 97.32           C  
ANISOU 1423  CA  PHE A 515    14245  14268   8465  -2838    379   -974       C  
ATOM   1424  C   PHE A 515     -12.407   2.874   0.622  1.00105.27           C  
ANISOU 1424  C   PHE A 515    15227  15396   9374  -2833    404   -903       C  
ATOM   1425  O   PHE A 515     -13.204   1.965   0.857  1.00110.43           O  
ANISOU 1425  O   PHE A 515    15883  16130   9947  -2790    472   -839       O  
ATOM   1426  CB  PHE A 515     -12.720   5.240   1.321  1.00 91.32           C  
ANISOU 1426  CB  PHE A 515    13500  13521   7679  -2792    310  -1128       C  
ATOM   1427  CG  PHE A 515     -13.227   6.615   1.010  1.00100.56           C  
ANISOU 1427  CG  PHE A 515    14702  14562   8942  -2785    285  -1208       C  
ATOM   1428  CD1 PHE A 515     -12.477   7.482   0.236  1.00103.35           C  
ANISOU 1428  CD1 PHE A 515    15063  14772   9434  -2864    246  -1225       C  
ATOM   1429  CD2 PHE A 515     -14.457   7.040   1.486  1.00109.63           C  
ANISOU 1429  CD2 PHE A 515    15877  15735  10044  -2698    304  -1263       C  
ATOM   1430  CE1 PHE A 515     -12.938   8.752  -0.050  1.00111.19           C  
ANISOU 1430  CE1 PHE A 515    16097  15632  10518  -2853    228  -1291       C  
ATOM   1431  CE2 PHE A 515     -14.925   8.311   1.202  1.00107.39           C  
ANISOU 1431  CE2 PHE A 515    15629  15328   9847  -2680    279  -1337       C  
ATOM   1432  CZ  PHE A 515     -14.165   9.167   0.433  1.00107.67           C  
ANISOU 1432  CZ  PHE A 515    15680  15207  10022  -2756    242  -1348       C  
ATOM   1433  N   GLU A 516     -11.092   2.739   0.749  1.00103.54           N  
ANISOU 1433  N   GLU A 516    14985  15189   9165  -2875    352   -916       N  
ATOM   1434  CA  GLU A 516     -10.489   1.459   1.088  1.00119.61           C  
ANISOU 1434  CA  GLU A 516    17001  17330  11116  -2864    370   -843       C  
ATOM   1435  C   GLU A 516      -9.178   1.668   1.839  1.00119.47           C  
ANISOU 1435  C   GLU A 516    16959  17366  11070  -2866    287   -926       C  
ATOM   1436  O   GLU A 516      -8.463   2.640   1.587  1.00118.55           O  
ANISOU 1436  O   GLU A 516    16825  17173  11046  -2922    224  -1007       O  
ATOM   1437  CB  GLU A 516     -10.253   0.638  -0.181  1.00112.33           C  
ANISOU 1437  CB  GLU A 516    16061  16362  10258  -2931    416   -714       C  
ATOM   1438  CG  GLU A 516      -9.774  -0.781   0.059  1.00122.51           C  
ANISOU 1438  CG  GLU A 516    17337  17743  11466  -2914    447   -626       C  
ATOM   1439  CD  GLU A 516      -9.578  -1.542  -1.236  1.00134.39           C  
ANISOU 1439  CD  GLU A 516    18823  19198  13041  -2977    490   -512       C  
ATOM   1440  OE1 GLU A 516      -9.750  -0.932  -2.312  1.00129.26           O  
ANISOU 1440  OE1 GLU A 516    18166  18451  12497  -3033    491   -503       O  
ATOM   1441  OE2 GLU A 516      -9.258  -2.748  -1.179  1.00140.36           O  
ANISOU 1441  OE2 GLU A 516    19573  20012  13745  -2965    523   -433       O  
ATOM   1442  N   LEU A 517      -8.871   0.754   2.759  1.00122.82           N  
ANISOU 1442  N   LEU A 517    17378  17922  11365  -2802    291   -907       N  
ATOM   1443  CA  LEU A 517      -7.644   0.834   3.545  1.00104.79           C  
ANISOU 1443  CA  LEU A 517    15064  15719   9032  -2784    210   -988       C  
ATOM   1444  C   LEU A 517      -6.972  -0.516   3.749  1.00111.55           C  
ANISOU 1444  C   LEU A 517    15907  16677   9798  -2752    229   -893       C  
ATOM   1445  O   LEU A 517      -7.487  -1.374   4.462  1.00111.83           O  
ANISOU 1445  O   LEU A 517    15972  16808   9711  -2670    280   -834       O  
ATOM   1446  CB  LEU A 517      -7.933   1.468   4.901  1.00 79.46           C  
ANISOU 1446  CB  LEU A 517    11868  12597   5727  -2697    167  -1121       C  
ATOM   1447  CG  LEU A 517      -8.133   2.980   4.863  1.00 84.33           C  
ANISOU 1447  CG  LEU A 517    12487  13114   6442  -2728    113  -1260       C  
ATOM   1448  CD1 LEU A 517      -9.202   3.404   5.848  1.00102.55           C  
ANISOU 1448  CD1 LEU A 517    14827  15479   8659  -2632    123  -1337       C  
ATOM   1449  CD2 LEU A 517      -6.815   3.683   5.158  1.00 77.90           C  
ANISOU 1449  CD2 LEU A 517    11626  12301   5673  -2769     13  -1390       C  
ATOM   1450  N   LEU A 518      -5.818  -0.697   3.115  1.00119.15           N  
ANISOU 1450  N   LEU A 518    16829  17619  10825  -2816    192   -875       N  
ATOM   1451  CA  LEU A 518      -5.033  -1.913   3.284  1.00125.71           C  
ANISOU 1451  CA  LEU A 518    17645  18544  11577  -2781    197   -795       C  
ATOM   1452  C   LEU A 518      -3.862  -1.674   4.230  1.00124.03           C  
ANISOU 1452  C   LEU A 518    17389  18443  11294  -2737    102   -907       C  
ATOM   1453  O   LEU A 518      -3.773  -0.619   4.856  1.00136.14           O  
ANISOU 1453  O   LEU A 518    18907  19988  12830  -2731     38  -1049       O  
ATOM   1454  CB  LEU A 518      -4.529  -2.420   1.933  1.00135.46           C  
ANISOU 1454  CB  LEU A 518    18854  19700  12915  -2867    222   -697       C  
ATOM   1455  N   HIS A 519      -2.950  -2.641   4.299  1.00129.42           N  
ANISOU 1455  N   HIS A 519    18048  19208  11916  -2706     91   -849       N  
ATOM   1456  CA  HIS A 519      -1.787  -2.548   5.177  1.00157.01           C  
ANISOU 1456  CA  HIS A 519    21493  22832  15331  -2653     -2   -951       C  
ATOM   1457  C   HIS A 519      -0.853  -1.429   4.734  1.00154.55           C  
ANISOU 1457  C   HIS A 519    21109  22466  15147  -2756    -85  -1081       C  
ATOM   1458  O   HIS A 519      -0.202  -0.785   5.556  1.00170.32           O  
ANISOU 1458  O   HIS A 519    23062  24544  17109  -2731   -171  -1229       O  
ATOM   1459  CB  HIS A 519      -1.025  -3.876   5.221  1.00172.59           C  
ANISOU 1459  CB  HIS A 519    23458  24898  17219  -2592      9   -849       C  
ATOM   1460  CG  HIS A 519      -1.833  -5.024   5.740  1.00184.09           C  
ANISOU 1460  CG  HIS A 519    24989  26407  18551  -2488     95   -719       C  
ATOM   1461  ND1 HIS A 519      -2.854  -5.604   5.020  1.00186.67           N  
ANISOU 1461  ND1 HIS A 519    25367  26633  18925  -2523    199   -589       N  
ATOM   1462  CD2 HIS A 519      -1.764  -5.705   6.909  1.00186.85           C  
ANISOU 1462  CD2 HIS A 519    25368  26898  18729  -2352     96   -697       C  
ATOM   1463  CE1 HIS A 519      -3.382  -6.590   5.723  1.00188.07           C  
ANISOU 1463  CE1 HIS A 519    25603  26878  18978  -2423    266   -494       C  
ATOM   1464  NE2 HIS A 519      -2.740  -6.671   6.874  1.00188.04           N  
ANISOU 1464  NE2 HIS A 519    25592  27020  18836  -2315    208   -549       N  
ATOM   1465  N   ALA A 520      -0.783  -1.215   3.425  1.00136.74           N  
ANISOU 1465  N   ALA A 520    18839  20076  13039  -2873    -56  -1026       N  
ATOM   1466  CA  ALA A 520       0.000  -0.122   2.870  1.00144.92           C  
ANISOU 1466  CA  ALA A 520    19815  21034  14215  -2988   -114  -1130       C  
ATOM   1467  C   ALA A 520      -0.927   1.028   2.509  1.00156.76           C  
ANISOU 1467  C   ALA A 520    21353  22388  15822  -3048    -93  -1172       C  
ATOM   1468  O   ALA A 520      -1.665   0.953   1.529  1.00180.49           O  
ANISOU 1468  O   ALA A 520    24396  25282  18901  -3093    -23  -1067       O  
ATOM   1469  CB  ALA A 520       0.776  -0.585   1.650  1.00147.36           C  
ANISOU 1469  CB  ALA A 520    20080  21297  14614  -3074    -96  -1041       C  
ATOM   1470  N   PRO A 521      -0.899   2.101   3.309  1.00150.80           N  
ANISOU 1470  N   PRO A 521    20588  21636  15074  -3042   -155  -1332       N  
ATOM   1471  CA  PRO A 521      -1.868   3.184   3.152  1.00149.42           C  
ANISOU 1471  CA  PRO A 521    20461  21330  14983  -3071   -137  -1381       C  
ATOM   1472  C   PRO A 521      -1.311   4.428   2.452  1.00141.30           C  
ANISOU 1472  C   PRO A 521    19400  20156  14132  -3200   -171  -1464       C  
ATOM   1473  O   PRO A 521      -2.044   5.404   2.295  1.00150.45           O  
ANISOU 1473  O   PRO A 521    20602  21192  15370  -3223   -159  -1508       O  
ATOM   1474  CB  PRO A 521      -2.242   3.503   4.601  1.00164.16           C  
ANISOU 1474  CB  PRO A 521    22342  23302  16729  -2964   -183  -1508       C  
ATOM   1475  CG  PRO A 521      -1.002   3.099   5.421  1.00171.47           C  
ANISOU 1475  CG  PRO A 521    23198  24390  17561  -2921   -261  -1589       C  
ATOM   1476  CD  PRO A 521      -0.094   2.274   4.528  1.00165.60           C  
ANISOU 1476  CD  PRO A 521    22412  23653  16856  -2980   -245  -1479       C  
ATOM   1477  N   ALA A 522      -0.052   4.392   2.026  1.00127.66           N  
ANISOU 1477  N   ALA A 522    17600  18440  12467  -3280   -206  -1482       N  
ATOM   1478  CA  ALA A 522       0.583   5.579   1.458  1.00131.00           C  
ANISOU 1478  CA  ALA A 522    17984  18730  13059  -3410   -234  -1568       C  
ATOM   1479  C   ALA A 522       0.411   5.681  -0.056  1.00144.30           C  
ANISOU 1479  C   ALA A 522    19690  20264  14874  -3507   -161  -1430       C  
ATOM   1480  O   ALA A 522       1.332   5.378  -0.812  1.00152.09           O  
ANISOU 1480  O   ALA A 522    20620  21253  15916  -3583   -156  -1378       O  
ATOM   1481  CB  ALA A 522       2.064   5.596   1.818  1.00120.15           C  
ANISOU 1481  CB  ALA A 522    16508  17453  11692  -3454   -310  -1678       C  
ATOM   1482  N   THR A 523      -0.768   6.122  -0.490  1.00158.68           N  
ANISOU 1482  N   THR A 523    21590  21965  16738  -3496   -108  -1375       N  
ATOM   1483  CA  THR A 523      -1.045   6.331  -1.912  1.00168.12           C  
ANISOU 1483  CA  THR A 523    22812  23018  18049  -3572    -40  -1250       C  
ATOM   1484  C   THR A 523      -1.893   7.573  -2.164  1.00161.96           C  
ANISOU 1484  C   THR A 523    22098  22070  17370  -3591    -21  -1285       C  
ATOM   1485  O   THR A 523      -1.616   8.346  -3.080  1.00155.74           O  
ANISOU 1485  O   THR A 523    21313  21139  16721  -3686      1  -1260       O  
ATOM   1486  CB  THR A 523      -1.764   5.122  -2.540  1.00175.71           C  
ANISOU 1486  CB  THR A 523    23803  24025  18934  -3516     31  -1080       C  
ATOM   1487  OG1 THR A 523      -2.744   4.620  -1.625  1.00189.50           O  
ANISOU 1487  OG1 THR A 523    25594  25856  20550  -3399     39  -1087       O  
ATOM   1488  CG2 THR A 523      -0.775   4.022  -2.859  1.00174.65           C  
ANISOU 1488  CG2 THR A 523    23605  23996  18758  -3534     29  -1011       C  
ATOM   1489  N   VAL A 524      -2.936   7.750  -1.360  1.00152.81           N  
ANISOU 1489  N   VAL A 524    20993  20929  16137  -3494    -26  -1337       N  
ATOM   1490  CA  VAL A 524      -3.850   8.875  -1.524  1.00134.56           C  
ANISOU 1490  CA  VAL A 524    18751  18470  13907  -3487    -11  -1373       C  
ATOM   1491  C   VAL A 524      -3.908   9.689  -0.241  1.00146.40           C  
ANISOU 1491  C   VAL A 524    20255  19984  15386  -3444    -79  -1561       C  
ATOM   1492  O   VAL A 524      -4.087   9.138   0.843  1.00155.21           O  
ANISOU 1492  O   VAL A 524    21360  21250  16364  -3353   -109  -1618       O  
ATOM   1493  CB  VAL A 524      -5.268   8.406  -1.896  1.00109.46           C  
ANISOU 1493  CB  VAL A 524    15633  15291  10664  -3402     56  -1259       C  
ATOM   1494  CG1 VAL A 524      -6.194   9.595  -2.067  1.00 99.33           C  
ANISOU 1494  CG1 VAL A 524    14419  13860   9460  -3383     68  -1300       C  
ATOM   1495  CG2 VAL A 524      -5.230   7.572  -3.162  1.00104.57           C  
ANISOU 1495  CG2 VAL A 524    15003  14667  10061  -3439    120  -1086       C  
ATOM   1496  N   CYS A 525      -3.763  11.003  -0.366  1.00148.90           N  
ANISOU 1496  N   CYS A 525    20592  20142  15841  -3507   -100  -1656       N  
ATOM   1497  CA  CYS A 525      -3.786  11.872   0.798  1.00165.86           C  
ANISOU 1497  CA  CYS A 525    22743  22288  17988  -3473   -168  -1852       C  
ATOM   1498  C   CYS A 525      -4.220  13.290   0.442  1.00146.76           C  
ANISOU 1498  C   CYS A 525    20387  19653  15721  -3510   -161  -1912       C  
ATOM   1499  O   CYS A 525      -4.326  13.649  -0.731  1.00136.33           O  
ANISOU 1499  O   CYS A 525    19102  18181  14515  -3574   -105  -1799       O  
ATOM   1500  CB  CYS A 525      -2.405  11.897   1.460  1.00217.42           C  
ANISOU 1500  CB  CYS A 525    29183  28904  24525  -3533   -244  -1987       C  
ATOM   1501  SG  CYS A 525      -2.377  12.675   3.086  1.00266.14           S  
ANISOU 1501  SG  CYS A 525    35337  35139  30645  -3466   -341  -2245       S  
ATOM   1502  N   GLY A 526      -4.521  14.083   1.460  1.00133.01           N  
ANISOU 1502  N   GLY A 526    18664  17899  13973  -3458   -215  -2085       N  
ATOM   1503  CA  GLY A 526      -4.966  15.448   1.256  1.00140.14           C  
ANISOU 1503  CA  GLY A 526    19635  18595  15018  -3478   -213  -2159       C  
ATOM   1504  C   GLY A 526      -3.822  16.426   1.113  1.00149.86           C  
ANISOU 1504  C   GLY A 526    20832  19685  16425  -3617   -247  -2271       C  
ATOM   1505  O   GLY A 526      -2.659  16.034   1.155  1.00163.65           O  
ANISOU 1505  O   GLY A 526    22492  21507  18180  -3701   -274  -2295       O  
ATOM   1506  N   PRO A 527      -4.159  17.783   0.936  1.00146.17           N  
ANISOU 1506  N   PRO A 527    20434  18995  16110  -3644   -243  -2347       N  
ATOM   1507  CA  PRO A 527      -3.155  18.837   0.774  1.00141.38           C  
ANISOU 1507  CA  PRO A 527    19805  18219  15696  -3787   -263  -2458       C  
ATOM   1508  C   PRO A 527      -2.265  18.962   1.997  1.00137.10           C  
ANISOU 1508  C   PRO A 527    19171  17792  15130  -3811   -359  -2685       C  
ATOM   1509  O   PRO A 527      -1.097  18.596   1.900  1.00130.70           O  
ANISOU 1509  O   PRO A 527    18267  17049  14343  -3912   -377  -2699       O  
ATOM   1510  CB  PRO A 527      -3.996  20.103   0.600  1.00139.66           C  
ANISOU 1510  CB  PRO A 527    19694  17771  15598  -3758   -243  -2500       C  
ATOM   1511  CG  PRO A 527      -5.326  19.771   1.174  1.00143.06           C  
ANISOU 1511  CG  PRO A 527    20177  18307  15872  -3584   -249  -2497       C  
ATOM   1512  CD  PRO A 527      -5.530  18.312   0.922  1.00144.09           C  
ANISOU 1512  CD  PRO A 527    20271  18643  15836  -3533   -217  -2332       C  
TER    1513      PRO A 527                                                      
ATOM   1514  N   GLN C   1     -54.644   8.249 -24.032  1.00133.81           N  
ANISOU 1514  N   GLN C   1    16047  22944  11850    844    567  -2844       N  
ATOM   1515  CA  GLN C   1     -53.807   7.122 -23.635  1.00127.17           C  
ANISOU 1515  CA  GLN C   1    15211  21985  11124    543    645  -2793       C  
ATOM   1516  C   GLN C   1     -52.755   6.819 -24.699  1.00145.28           C  
ANISOU 1516  C   GLN C   1    17588  24170  13442    498    618  -2658       C  
ATOM   1517  O   GLN C   1     -52.011   7.702 -25.115  1.00160.15           O  
ANISOU 1517  O   GLN C   1    19660  25884  15306    614    566  -2501       O  
ATOM   1518  CB  GLN C   1     -54.667   5.883 -23.374  1.00110.45           C  
ANISOU 1518  CB  GLN C   1    12841  20089   9035    382    716  -2979       C  
ATOM   1519  N   VAL C   2     -52.701   5.565 -25.134  1.00157.58           N  
ANISOU 1519  N   VAL C   2    19003  25824  15046    326    657  -2721       N  
ATOM   1520  CA  VAL C   2     -51.757   5.144 -26.166  1.00152.35           C  
ANISOU 1520  CA  VAL C   2    18394  25087  14405    275    635  -2614       C  
ATOM   1521  C   VAL C   2     -52.451   4.351 -27.264  1.00160.83           C  
ANISOU 1521  C   VAL C   2    19247  26424  15436    306    614  -2763       C  
ATOM   1522  O   VAL C   2     -53.025   3.293 -27.009  1.00178.97           O  
ANISOU 1522  O   VAL C   2    21358  28861  17783    150    672  -2915       O  
ATOM   1523  CB  VAL C   2     -50.632   4.270 -25.581  1.00136.72           C  
ANISOU 1523  CB  VAL C   2    16495  22904  12550     -8    707  -2515       C  
ATOM   1524  CG1 VAL C   2     -49.702   3.798 -26.686  1.00125.95           C  
ANISOU 1524  CG1 VAL C   2    15168  21484  11202    -55    684  -2419       C  
ATOM   1525  CG2 VAL C   2     -49.870   5.018 -24.501  1.00144.07           C  
ANISOU 1525  CG2 VAL C   2    17638  23579  13522    -46    723  -2374       C  
ATOM   1526  N   GLN C   3     -52.386   4.865 -28.487  1.00149.93           N  
ANISOU 1526  N   GLN C   3    17891  25111  13966    507    535  -2719       N  
ATOM   1527  CA  GLN C   3     -53.053   4.236 -29.621  1.00154.18           C  
ANISOU 1527  CA  GLN C   3    18222  25917  14443    575    500  -2866       C  
ATOM   1528  C   GLN C   3     -52.070   3.796 -30.707  1.00151.56           C  
ANISOU 1528  C   GLN C   3    17941  25526  14117    535    477  -2760       C  
ATOM   1529  O   GLN C   3     -50.985   4.363 -30.839  1.00158.31           O  
ANISOU 1529  O   GLN C   3    19008  26159  14982    551    464  -2556       O  
ATOM   1530  CB  GLN C   3     -54.099   5.188 -30.208  1.00154.77           C  
ANISOU 1530  CB  GLN C   3    18232  26202  14373    891    419  -2947       C  
ATOM   1531  CG  GLN C   3     -55.313   5.390 -29.316  1.00153.74           C  
ANISOU 1531  CG  GLN C   3    17974  26216  14223    935    438  -3113       C  
ATOM   1532  CD  GLN C   3     -56.190   4.158 -29.240  1.00166.02           C  
ANISOU 1532  CD  GLN C   3    19252  28008  15819    780    488  -3344       C  
ATOM   1533  OE1 GLN C   3     -56.119   3.281 -30.098  1.00175.19           O  
ANISOU 1533  OE1 GLN C   3    20291  29282  16993    710    482  -3413       O  
ATOM   1534  NE2 GLN C   3     -57.022   4.086 -28.207  1.00168.12           N  
ANISOU 1534  NE2 GLN C   3    19418  28350  16111    724    540  -3469       N  
ATOM   1535  N   LEU C   4     -52.452   2.785 -31.482  1.00138.95           N  
ANISOU 1535  N   LEU C   4    16145  24133  12516    482    474  -2906       N  
ATOM   1536  CA  LEU C   4     -51.579   2.254 -32.527  1.00129.60           C  
ANISOU 1536  CA  LEU C   4    14986  22921  11337    439    454  -2832       C  
ATOM   1537  C   LEU C   4     -52.316   1.999 -33.838  1.00132.38           C  
ANISOU 1537  C   LEU C   4    15147  23573  11580    606    387  -2981       C  
ATOM   1538  O   LEU C   4     -53.458   1.538 -33.844  1.00128.27           O  
ANISOU 1538  O   LEU C   4    14401  23294  11041    618    386  -3203       O  
ATOM   1539  CB  LEU C   4     -50.905   0.963 -32.059  1.00114.72           C  
ANISOU 1539  CB  LEU C   4    13074  20916   9598    124    536  -2839       C  
ATOM   1540  CG  LEU C   4     -49.948   1.081 -30.875  1.00106.62           C  
ANISOU 1540  CG  LEU C   4    12244  19587   8678    -54    600  -2674       C  
ATOM   1541  CD1 LEU C   4     -49.445  -0.292 -30.470  1.00115.67           C  
ANISOU 1541  CD1 LEU C   4    13337  20656   9959   -347    681  -2706       C  
ATOM   1542  CD2 LEU C   4     -48.787   2.003 -31.219  1.00 85.77           C  
ANISOU 1542  CD2 LEU C   4     9845  16735   6008     39    561  -2437       C  
ATOM   1543  N   VAL C   5     -51.644   2.283 -34.951  1.00147.80           N  
ANISOU 1543  N   VAL C   5    17184  25516  13459    731    332  -2862       N  
ATOM   1544  CA  VAL C   5     -52.216   2.074 -36.280  1.00154.11           C  
ANISOU 1544  CA  VAL C   5    17817  26599  14138    907    261  -2987       C  
ATOM   1545  C   VAL C   5     -51.185   1.487 -37.243  1.00145.41           C  
ANISOU 1545  C   VAL C   5    16755  25452  13044    843    252  -2898       C  
ATOM   1546  O   VAL C   5     -50.155   2.104 -37.516  1.00153.62           O  
ANISOU 1546  O   VAL C   5    18003  26303  14064    893    242  -2673       O  
ATOM   1547  CB  VAL C   5     -52.758   3.389 -36.885  1.00162.18           C  
ANISOU 1547  CB  VAL C   5    18894  27737  14991   1257    177  -2938       C  
ATOM   1548  CG1 VAL C   5     -53.136   3.183 -38.342  1.00159.13           C  
ANISOU 1548  CG1 VAL C   5    18363  27630  14470   1448    101  -3033       C  
ATOM   1549  CG2 VAL C   5     -53.951   3.898 -36.090  1.00170.03           C  
ANISOU 1549  CG2 VAL C   5    19804  28840  15960   1352    174  -3069       C  
ATOM   1550  N   GLU C   6     -51.470   0.295 -37.757  1.00126.83           N  
ANISOU 1550  N   GLU C   6    14195  23273  10721    731    256  -3082       N  
ATOM   1551  CA  GLU C   6     -50.567  -0.373 -38.689  1.00113.51           C  
ANISOU 1551  CA  GLU C   6    12518  21570   9041    669    246  -3030       C  
ATOM   1552  C   GLU C   6     -50.897  -0.035 -40.141  1.00127.11           C  
ANISOU 1552  C   GLU C   6    14161  23546  10588    944    153  -3071       C  
ATOM   1553  O   GLU C   6     -51.989   0.452 -40.441  1.00137.56           O  
ANISOU 1553  O   GLU C   6    15368  25104  11797   1158     97  -3196       O  
ATOM   1554  CB  GLU C   6     -50.616  -1.891 -38.490  1.00103.83           C  
ANISOU 1554  CB  GLU C   6    11121  20380   7952    394    303  -3206       C  
ATOM   1555  CG  GLU C   6     -50.237  -2.366 -37.099  1.00116.90           C  
ANISOU 1555  CG  GLU C   6    12849  21790   9777    115    402  -3162       C  
ATOM   1556  CD  GLU C   6     -51.435  -2.515 -36.179  1.00133.00           C  
ANISOU 1556  CD  GLU C   6    14742  23932  11860     59    441  -3342       C  
ATOM   1557  OE1 GLU C   6     -51.248  -2.951 -35.024  1.00127.04           O  
ANISOU 1557  OE1 GLU C   6    14028  23006  11237   -163    527  -3322       O  
ATOM   1558  OE2 GLU C   6     -52.564  -2.205 -36.616  1.00141.36           O  
ANISOU 1558  OE2 GLU C   6    15640  25252  12817    241    388  -3503       O  
ATOM   1559  N   SER C   7     -49.950  -0.308 -41.034  1.00126.85           N  
ANISOU 1559  N   SER C   7    14191  23478  10530    943    137  -2966       N  
ATOM   1560  CA  SER C   7     -50.136  -0.101 -42.467  1.00120.12           C  
ANISOU 1560  CA  SER C   7    13265  22868   9506   1192     54  -2995       C  
ATOM   1561  C   SER C   7     -49.019  -0.762 -43.278  1.00123.44           C  
ANISOU 1561  C   SER C   7    13725  23236   9941   1105     58  -2913       C  
ATOM   1562  O   SER C   7     -47.868  -0.818 -42.842  1.00115.92           O  
ANISOU 1562  O   SER C   7    12949  22008   9087    940    113  -2727       O  
ATOM   1563  CB  SER C   7     -50.208   1.395 -42.786  1.00111.34           C  
ANISOU 1563  CB  SER C   7    12315  21746   8242   1495      4  -2817       C  
ATOM   1564  OG  SER C   7     -49.056   2.075 -42.319  1.00118.45           O  
ANISOU 1564  OG  SER C   7    13486  22320   9198   1436     48  -2538       O  
ATOM   1565  N   GLY C   8     -49.362  -1.260 -44.463  1.00138.48           N  
ANISOU 1565  N   GLY C   8    15458  25415  11742   1223     -2  -3060       N  
ATOM   1566  CA  GLY C   8     -48.371  -1.838 -45.352  1.00155.56           C  
ANISOU 1566  CA  GLY C   8    17645  27566  13893   1178     -8  -2994       C  
ATOM   1567  C   GLY C   8     -48.527  -3.325 -45.607  1.00175.29           C  
ANISOU 1567  C   GLY C   8    19927  30190  16484    986      2  -3237       C  
ATOM   1568  O   GLY C   8     -47.643  -3.957 -46.187  1.00164.96           O  
ANISOU 1568  O   GLY C   8    18638  28841  15197    903      8  -3196       O  
ATOM   1569  N   GLY C   9     -49.648  -3.892 -45.174  1.00203.12           N  
ANISOU 1569  N   GLY C   9    23245  33865  20068    912      6  -3493       N  
ATOM   1570  CA  GLY C   9     -49.915  -5.300 -45.397  1.00205.43           C  
ANISOU 1570  CA  GLY C   9    23317  34277  20458    727     19  -3746       C  
ATOM   1571  C   GLY C   9     -50.306  -5.595 -46.833  1.00203.96           C  
ANISOU 1571  C   GLY C   9    22949  34422  20125    920    -70  -3913       C  
ATOM   1572  O   GLY C   9     -50.535  -4.677 -47.619  1.00209.90           O  
ANISOU 1572  O   GLY C   9    23729  35322  20702   1214   -145  -3837       O  
ATOM   1573  N   GLY C  10     -50.388  -6.878 -47.177  1.00179.47           N  
ANISOU 1573  N   GLY C  10    19661  31418  17111    759    -64  -4133       N  
ATOM   1574  CA  GLY C  10     -50.817  -7.276 -48.506  1.00151.62           C  
ANISOU 1574  CA  GLY C  10    15933  28132  13545    917   -152  -4280       C  
ATOM   1575  C   GLY C  10     -50.371  -8.662 -48.941  1.00139.82           C  
ANISOU 1575  C   GLY C  10    14317  26638  12172    719   -135  -4429       C  
ATOM   1576  O   GLY C  10     -50.078  -9.523 -48.112  1.00130.98           O  
ANISOU 1576  O   GLY C  10    13202  25369  11194    429    -51  -4501       O  
ATOM   1577  N   LEU C  11     -50.340  -8.877 -50.254  1.00130.37           N  
ANISOU 1577  N   LEU C  11    13009  25611  10914    883   -214  -4481       N  
ATOM   1578  CA  LEU C  11     -49.987 -10.175 -50.825  1.00117.38           C  
ANISOU 1578  CA  LEU C  11    11228  23995   9375    731   -211  -4642       C  
ATOM   1579  C   LEU C  11     -48.576 -10.163 -51.405  1.00104.81           C  
ANISOU 1579  C   LEU C  11     9819  22276   7728    747   -209  -4428       C  
ATOM   1580  O   LEU C  11     -48.150  -9.178 -52.006  1.00 98.68           O  
ANISOU 1580  O   LEU C  11     9180  21516   6798    978   -252  -4211       O  
ATOM   1581  CB  LEU C  11     -50.996 -10.577 -51.902  1.00114.74           C  
ANISOU 1581  CB  LEU C  11    10605  23964   9029    888   -299  -4891       C  
ATOM   1582  CG  LEU C  11     -50.691 -11.847 -52.700  1.00107.19           C  
ANISOU 1582  CG  LEU C  11     9490  23071   8165    783   -313  -5070       C  
ATOM   1583  CD1 LEU C  11     -50.602 -13.062 -51.792  1.00101.68           C  
ANISOU 1583  CD1 LEU C  11     8739  22223   7672    425   -219  -5236       C  
ATOM   1584  CD2 LEU C  11     -51.741 -12.057 -53.777  1.00118.45           C  
ANISOU 1584  CD2 LEU C  11    10632  24814   9559    977   -405  -5302       C  
ATOM   1585  N   VAL C  12     -47.862 -11.270 -51.229  1.00105.91           N  
ANISOU 1585  N   VAL C  12     9956  22291   7995    500   -156  -4493       N  
ATOM   1586  CA  VAL C  12     -46.466 -11.368 -51.634  1.00 99.88           C  
ANISOU 1586  CA  VAL C  12     9364  21389   7198    475   -142  -4299       C  
ATOM   1587  C   VAL C  12     -46.132 -12.775 -52.139  1.00106.26           C  
ANISOU 1587  C   VAL C  12    10030  22217   8126    316   -139  -4490       C  
ATOM   1588  O   VAL C  12     -46.623 -13.767 -51.600  1.00110.65           O  
ANISOU 1588  O   VAL C  12    10447  22756   8838     98    -96  -4718       O  
ATOM   1589  CB  VAL C  12     -45.538 -10.983 -50.456  1.00101.10           C  
ANISOU 1589  CB  VAL C  12     9782  21258   7375    304    -52  -4071       C  
ATOM   1590  CG1 VAL C  12     -45.873 -11.798 -49.220  1.00119.55           C  
ANISOU 1590  CG1 VAL C  12    12071  23430   9923      6     33  -4200       C  
ATOM   1591  CG2 VAL C  12     -44.078 -11.145 -50.821  1.00106.17           C  
ANISOU 1591  CG2 VAL C  12    10588  21754   7998    258    -32  -3879       C  
ATOM   1592  N   GLN C  13     -45.330 -12.858 -53.199  1.00122.55           N  
ANISOU 1592  N   GLN C  13    12124  24323  10119    431   -181  -4404       N  
ATOM   1593  CA  GLN C  13     -44.853 -14.146 -53.691  1.00111.34           C  
ANISOU 1593  CA  GLN C  13    10597  22901   8805    290   -177  -4559       C  
ATOM   1594  C   GLN C  13     -43.648 -14.594 -52.870  1.00 94.49           C  
ANISOU 1594  C   GLN C  13     8656  20492   6756     39    -89  -4430       C  
ATOM   1595  O   GLN C  13     -43.084 -13.808 -52.115  1.00 93.01           O  
ANISOU 1595  O   GLN C  13     8687  20135   6520     13    -41  -4194       O  
ATOM   1596  CB  GLN C  13     -44.491 -14.061 -55.174  1.00111.53           C  
ANISOU 1596  CB  GLN C  13    10568  23095   8713    524   -258  -4524       C  
ATOM   1597  N   ALA C  14     -43.258 -15.856 -53.014  1.00 94.39           N  
ANISOU 1597  N   ALA C  14     8559  20433   6870   -141    -67  -4588       N  
ATOM   1598  CA  ALA C  14     -42.094 -16.381 -52.307  1.00 96.53           C  
ANISOU 1598  CA  ALA C  14     9000  20454   7223   -373     13  -4482       C  
ATOM   1599  C   ALA C  14     -40.861 -15.533 -52.614  1.00104.58           C  
ANISOU 1599  C   ALA C  14    10245  21381   8108   -253      9  -4160       C  
ATOM   1600  O   ALA C  14     -40.565 -15.241 -53.772  1.00129.57           O  
ANISOU 1600  O   ALA C  14    13388  24684  11158    -45    -56  -4098       O  
ATOM   1601  CB  ALA C  14     -41.854 -17.837 -52.678  1.00115.95           C  
ANISOU 1601  CB  ALA C  14    11324  22907   9823   -533     21  -4704       C  
ATOM   1602  N   GLY C  15     -40.169 -15.121 -51.561  1.00 89.50           N  
ANISOU 1602  N   GLY C  15     8547  19166   6292   -383     83  -3910       N  
ATOM   1603  CA  GLY C  15     -39.089 -14.154 -51.657  1.00 88.41           C  
ANISOU 1603  CA  GLY C  15     8633  18907   6051   -284     91  -3586       C  
ATOM   1604  C   GLY C  15     -39.655 -12.749 -51.586  1.00 88.83           C  
ANISOU 1604  C   GLY C  15     8759  19035   5959    -81     65  -3447       C  
ATOM   1605  O   GLY C  15     -40.809 -12.564 -51.210  1.00108.24           O  
ANISOU 1605  O   GLY C  15    11115  21587   8424    -56     53  -3584       O  
ATOM   1606  N   GLY C  16     -38.858 -11.753 -51.950  1.00 88.42           N  
ANISOU 1606  N   GLY C  16     8880  18941   5775     66     58  -3177       N  
ATOM   1607  CA  GLY C  16     -39.359 -10.391 -51.978  1.00105.60           C  
ANISOU 1607  CA  GLY C  16    11134  21184   7806    278     33  -3038       C  
ATOM   1608  C   GLY C  16     -39.340  -9.697 -50.629  1.00100.39           C  
ANISOU 1608  C   GLY C  16    10639  20252   7251    167     95  -2869       C  
ATOM   1609  O   GLY C  16     -38.877 -10.262 -49.640  1.00110.67           O  
ANISOU 1609  O   GLY C  16    12004  21309   8735    -78    161  -2845       O  
ATOM   1610  N   SER C  17     -39.875  -8.480 -50.578  1.00 88.34           N  
ANISOU 1610  N   SER C  17     9181  18775   5608    354     73  -2760       N  
ATOM   1611  CA  SER C  17     -39.779  -7.671 -49.370  1.00 87.21           C  
ANISOU 1611  CA  SER C  17     9212  18377   5545    278    127  -2581       C  
ATOM   1612  C   SER C  17     -41.059  -6.945 -48.964  1.00 99.89           C  
ANISOU 1612  C   SER C  17    10767  20084   7103    401    102  -2657       C  
ATOM   1613  O   SER C  17     -41.885  -6.598 -49.798  1.00 94.56           O  
ANISOU 1613  O   SER C  17     9976  19680   6271    630     34  -2759       O  
ATOM   1614  CB  SER C  17     -38.659  -6.643 -49.537  1.00103.01           C  
ANISOU 1614  CB  SER C  17    11447  20220   7474    362    147  -2260       C  
ATOM   1615  OG  SER C  17     -37.432  -7.280 -49.849  1.00111.94           O  
ANISOU 1615  OG  SER C  17    12628  21252   8653    243    174  -2181       O  
ATOM   1616  N   LEU C  18     -41.204  -6.722 -47.662  1.00100.70           N  
ANISOU 1616  N   LEU C  18    10955  19971   7336    253    157  -2607       N  
ATOM   1617  CA  LEU C  18     -42.313  -5.951 -47.109  1.00100.47           C  
ANISOU 1617  CA  LEU C  18    10904  19997   7272    356    143  -2651       C  
ATOM   1618  C   LEU C  18     -41.827  -5.043 -45.988  1.00106.91           C  
ANISOU 1618  C   LEU C  18    11944  20520   8155    291    197  -2418       C  
ATOM   1619  O   LEU C  18     -40.992  -5.435 -45.174  1.00116.92           O  
ANISOU 1619  O   LEU C  18    13317  21538   9569     68    261  -2327       O  
ATOM   1620  CB  LEU C  18     -43.414  -6.870 -46.591  1.00 97.60           C  
ANISOU 1620  CB  LEU C  18    10331  19740   7015    223    152  -2938       C  
ATOM   1621  CG  LEU C  18     -44.270  -7.552 -47.650  1.00 96.50           C  
ANISOU 1621  CG  LEU C  18     9938  19936   6792    330     85  -3213       C  
ATOM   1622  CD1 LEU C  18     -45.249  -8.514 -47.003  1.00 90.52           C  
ANISOU 1622  CD1 LEU C  18     8983  19236   6174    151    114  -3487       C  
ATOM   1623  CD2 LEU C  18     -45.013  -6.491 -48.435  1.00107.10           C  
ANISOU 1623  CD2 LEU C  18    11249  21522   7921    655      6  -3205       C  
ATOM   1624  N   ARG C  19     -42.358  -3.828 -45.944  1.00106.59           N  
ANISOU 1624  N   ARG C  19    11976  20515   8009    493    170  -2329       N  
ATOM   1625  CA  ARG C  19     -41.971  -2.888 -44.904  1.00102.61           C  
ANISOU 1625  CA  ARG C  19    11681  19743   7564    450    215  -2125       C  
ATOM   1626  C   ARG C  19     -43.214  -2.346 -44.205  1.00108.40           C  
ANISOU 1626  C   ARG C  19    12360  20541   8288    526    204  -2228       C  
ATOM   1627  O   ARG C  19     -43.871  -1.428 -44.705  1.00103.15           O  
ANISOU 1627  O   ARG C  19    11694  20022   7477    780    152  -2212       O  
ATOM   1628  CB  ARG C  19     -41.140  -1.748 -45.485  1.00 90.27           C  
ANISOU 1628  CB  ARG C  19    10316  18093   5890    620    206  -1855       C  
ATOM   1629  CG  ARG C  19     -40.789  -0.680 -44.474  1.00 91.86           C  
ANISOU 1629  CG  ARG C  19    10729  18025   6147    596    246  -1654       C  
ATOM   1630  CD  ARG C  19     -40.018   0.441 -45.123  1.00 96.85           C  
ANISOU 1630  CD  ARG C  19    11548  18576   6674    766    242  -1396       C  
ATOM   1631  NE  ARG C  19     -40.939   1.453 -45.630  1.00113.70           N  
ANISOU 1631  NE  ARG C  19    13679  20869   8653   1056    190  -1389       N  
ATOM   1632  CZ  ARG C  19     -40.673   2.282 -46.633  1.00120.19           C  
ANISOU 1632  CZ  ARG C  19    14589  21752   9324   1286    167  -1229       C  
ATOM   1633  NH1 ARG C  19     -39.503   2.224 -47.257  1.00105.55           N  
ANISOU 1633  NH1 ARG C  19    12829  19821   7456   1253    193  -1064       N  
ATOM   1634  NH2 ARG C  19     -41.583   3.168 -47.015  1.00125.52           N  
ANISOU 1634  NH2 ARG C  19    15259  22571   9860   1554    121  -1232       N  
ATOM   1635  N   LEU C  20     -43.543  -2.934 -43.059  1.00113.16           N  
ANISOU 1635  N   LEU C  20    12915  21041   9040    313    254  -2335       N  
ATOM   1636  CA  LEU C  20     -44.723  -2.539 -42.300  1.00105.31           C  
ANISOU 1636  CA  LEU C  20    11854  20109   8050    357    253  -2449       C  
ATOM   1637  C   LEU C  20     -44.433  -1.364 -41.370  1.00110.77           C  
ANISOU 1637  C   LEU C  20    12760  20567   8760    384    279  -2246       C  
ATOM   1638  O   LEU C  20     -43.353  -1.279 -40.787  1.00105.61           O  
ANISOU 1638  O   LEU C  20    12278  19651   8199    238    328  -2071       O  
ATOM   1639  CB  LEU C  20     -45.257  -3.723 -41.488  1.00 86.72           C  
ANISOU 1639  CB  LEU C  20     9343  17761   5847    114    304  -2659       C  
ATOM   1640  CG  LEU C  20     -46.122  -4.745 -42.235  1.00 87.99           C  
ANISOU 1640  CG  LEU C  20     9236  18207   5990    117    271  -2940       C  
ATOM   1641  CD1 LEU C  20     -45.288  -5.553 -43.217  1.00 87.72           C  
ANISOU 1641  CD1 LEU C  20     9172  18206   5953     72    257  -2943       C  
ATOM   1642  CD2 LEU C  20     -46.851  -5.660 -41.271  1.00 93.84           C  
ANISOU 1642  CD2 LEU C  20     9833  18943   6879   -103    332  -3137       C  
ATOM   1643  N   SER C  21     -45.396  -0.452 -41.247  1.00119.59           N  
ANISOU 1643  N   SER C  21    13865  21786   9788    579    244  -2278       N  
ATOM   1644  CA  SER C  21     -45.258   0.699 -40.356  1.00118.20           C  
ANISOU 1644  CA  SER C  21    13881  21403   9629    622    264  -2112       C  
ATOM   1645  C   SER C  21     -46.238   0.639 -39.191  1.00114.51           C  
ANISOU 1645  C   SER C  21    13334  20945   9232    546    291  -2256       C  
ATOM   1646  O   SER C  21     -47.111  -0.234 -39.137  1.00103.58           O  
ANISOU 1646  O   SER C  21    11736  19744   7873    477    294  -2485       O  
ATOM   1647  CB  SER C  21     -45.450   2.011 -41.119  1.00112.86           C  
ANISOU 1647  CB  SER C  21    13302  20793   8788    933    206  -1987       C  
ATOM   1648  OG  SER C  21     -44.322   2.312 -41.920  1.00112.85           O  
ANISOU 1648  OG  SER C  21    13442  20696   8741    981    204  -1783       O  
ATOM   1649  N   CYS C  22     -46.099   1.587 -38.270  1.00124.87           N  
ANISOU 1649  N   CYS C  22    14812  22060  10572    561    313  -2126       N  
ATOM   1650  CA  CYS C  22     -46.930   1.629 -37.077  1.00131.19           C  
ANISOU 1650  CA  CYS C  22    15561  22848  11435    492    344  -2237       C  
ATOM   1651  C   CYS C  22     -46.955   3.044 -36.505  1.00120.39           C  
ANISOU 1651  C   CYS C  22    14377  21335  10031    639    333  -2093       C  
ATOM   1652  O   CYS C  22     -45.915   3.596 -36.146  1.00111.39           O  
ANISOU 1652  O   CYS C  22    13446  19939   8940    587    357  -1891       O  
ATOM   1653  CB  CYS C  22     -46.414   0.632 -36.035  1.00138.87           C  
ANISOU 1653  CB  CYS C  22    16534  23654  12577    177    425  -2259       C  
ATOM   1654  SG  CYS C  22     -47.566   0.262 -34.689  1.00143.26           S  
ANISOU 1654  SG  CYS C  22    16958  24261  13212     55    477  -2448       S  
ATOM   1655  N   ALA C  23     -48.146   3.635 -36.457  1.00126.34           N  
ANISOU 1655  N   ALA C  23    15048  22259  10698    830    294  -2205       N  
ATOM   1656  CA  ALA C  23     -48.319   5.000 -35.966  1.00126.98           C  
ANISOU 1656  CA  ALA C  23    15288  22223  10736    999    277  -2093       C  
ATOM   1657  C   ALA C  23     -48.672   5.004 -34.479  1.00144.52           C  
ANISOU 1657  C   ALA C  23    17518  24336  13059    856    328  -2154       C  
ATOM   1658  O   ALA C  23     -49.440   4.160 -34.017  1.00158.71           O  
ANISOU 1658  O   ALA C  23    19130  26274  14899    738    356  -2347       O  
ATOM   1659  CB  ALA C  23     -49.389   5.719 -36.767  1.00117.94           C  
ANISOU 1659  CB  ALA C  23    14061  21323   9428   1315    202  -2170       C  
ATOM   1660  N   VAL C  24     -48.115   5.958 -33.735  1.00137.31           N  
ANISOU 1660  N   VAL C  24    16815  23173  12182    865    344  -1993       N  
ATOM   1661  CA  VAL C  24     -48.284   5.994 -32.284  1.00120.13           C  
ANISOU 1661  CA  VAL C  24    14670  20872  10101    724    394  -2030       C  
ATOM   1662  C   VAL C  24     -48.927   7.296 -31.785  1.00113.70           C  
ANISOU 1662  C   VAL C  24    13943  20030   9228    932    363  -2015       C  
ATOM   1663  O   VAL C  24     -48.592   8.382 -32.255  1.00109.05           O  
ANISOU 1663  O   VAL C  24    13514  19341   8580   1119    324  -1868       O  
ATOM   1664  CB  VAL C  24     -46.926   5.801 -31.585  1.00107.60           C  
ANISOU 1664  CB  VAL C  24    13253  18990   8640    495    449  -1870       C  
ATOM   1665  CG1 VAL C  24     -47.108   5.651 -30.085  1.00136.49           C  
ANISOU 1665  CG1 VAL C  24    16920  22548  12391    335    505  -1925       C  
ATOM   1666  CG2 VAL C  24     -46.204   4.588 -32.157  1.00 84.79           C  
ANISOU 1666  CG2 VAL C  24    10297  16116   5804    312    475  -1868       C  
ATOM   1667  N   SER C  25     -49.840   7.173 -30.822  1.00122.09           N  
ANISOU 1667  N   SER C  25    14902  21175  10311    896    386  -2166       N  
ATOM   1668  CA  SER C  25     -50.567   8.318 -30.268  1.00134.97           C  
ANISOU 1668  CA  SER C  25    16591  22803  11888   1090    358  -2184       C  
ATOM   1669  C   SER C  25     -49.799   9.038 -29.153  1.00132.31           C  
ANISOU 1669  C   SER C  25    16471  22165  11636   1010    390  -2046       C  
ATOM   1670  O   SER C  25     -50.240   9.054 -28.001  1.00113.74           O  
ANISOU 1670  O   SER C  25    14094  19796   9325    940    423  -2129       O  
ATOM   1671  CB  SER C  25     -51.923   7.863 -29.732  1.00152.68           C  
ANISOU 1671  CB  SER C  25    18612  25290  14110   1092    371  -2419       C  
ATOM   1672  OG  SER C  25     -52.686   8.965 -29.276  1.00167.48           O  
ANISOU 1672  OG  SER C  25    20528  27188  15918   1301    338  -2450       O  
ATOM   1673  N   GLY C  26     -48.662   9.631 -29.492  1.00143.51           N  
ANISOU 1673  N   GLY C  26    18095  23354  13078   1021    381  -1842       N  
ATOM   1674  CA  GLY C  26     -47.886  10.410 -28.542  1.00141.59           C  
ANISOU 1674  CA  GLY C  26    18061  22822  12913    962    402  -1712       C  
ATOM   1675  C   GLY C  26     -47.154   9.671 -27.438  1.00141.59           C  
ANISOU 1675  C   GLY C  26    18087  22671  13039    671    469  -1702       C  
ATOM   1676  O   GLY C  26     -46.492  10.288 -26.601  1.00155.91           O  
ANISOU 1676  O   GLY C  26    20066  24254  14918    615    484  -1608       O  
ATOM   1677  N   ALA C  27     -47.275   8.349 -27.429  1.00128.20           N  
ANISOU 1677  N   ALA C  27    16228  21105  11379    489    508  -1803       N  
ATOM   1678  CA  ALA C  27     -46.609   7.534 -26.421  1.00118.01           C  
ANISOU 1678  CA  ALA C  27    14951  19687  10200    217    576  -1794       C  
ATOM   1679  C   ALA C  27     -45.096   7.646 -26.570  1.00113.04           C  
ANISOU 1679  C   ALA C  27    14503  18808   9639    107    584  -1601       C  
ATOM   1680  O   ALA C  27     -44.580   7.713 -27.688  1.00119.15           O  
ANISOU 1680  O   ALA C  27    15313  19576  10383    168    555  -1508       O  
ATOM   1681  CB  ALA C  27     -47.049   6.093 -26.524  1.00115.93           C  
ANISOU 1681  CB  ALA C  27    14480  19608   9961     57    619  -1934       C  
ATOM   1682  N   GLY C  28     -44.391   7.668 -25.445  1.00 92.41           N  
ANISOU 1682  N   GLY C  28    11997  16001   7112    -50    622  -1544       N  
ATOM   1683  CA  GLY C  28     -42.942   7.702 -25.461  1.00 80.80           C  
ANISOU 1683  CA  GLY C  28    10683  14302   5715   -175    634  -1378       C  
ATOM   1684  C   GLY C  28     -42.369   6.776 -24.410  1.00100.36           C  
ANISOU 1684  C   GLY C  28    13152  16696   8285   -426    695  -1390       C  
ATOM   1685  O   GLY C  28     -43.060   6.408 -23.459  1.00124.61           O  
ANISOU 1685  O   GLY C  28    16140  19842  11365   -485    730  -1505       O  
ATOM   1686  N   ALA C  29     -41.108   6.393 -24.595  1.00 94.66           N  
ANISOU 1686  N   ALA C  29    12514  15828   7625   -567    710  -1269       N  
ATOM   1687  CA  ALA C  29     -40.399   5.507 -23.669  1.00 99.12           C  
ANISOU 1687  CA  ALA C  29    13087  16299   8275   -798    765  -1258       C  
ATOM   1688  C   ALA C  29     -41.096   4.167 -23.456  1.00 99.43           C  
ANISOU 1688  C   ALA C  29    12944  16511   8325   -918    816  -1394       C  
ATOM   1689  O   ALA C  29     -41.297   3.739 -22.322  1.00108.90           O  
ANISOU 1689  O   ALA C  29    14117  17701   9560  -1031    865  -1450       O  
ATOM   1690  CB  ALA C  29     -40.194   6.206 -22.312  1.00 85.78           C  
ANISOU 1690  CB  ALA C  29    11514  14460   6620   -824    775  -1241       C  
ATOM   1691  N   HIS C  30     -41.448   3.505 -24.549  1.00 85.55           N  
ANISOU 1691  N   HIS C  30    11059  14908   6537   -895    807  -1447       N  
ATOM   1692  CA  HIS C  30     -42.030   2.172 -24.487  1.00 90.66           C  
ANISOU 1692  CA  HIS C  30    11530  15707   7211  -1023    858  -1576       C  
ATOM   1693  C   HIS C  30     -41.235   1.194 -25.344  1.00 96.53           C  
ANISOU 1693  C   HIS C  30    12243  16442   7993  -1134    867  -1533       C  
ATOM   1694  O   HIS C  30     -40.735   1.561 -26.407  1.00110.61           O  
ANISOU 1694  O   HIS C  30    14073  18212   9740  -1043    819  -1453       O  
ATOM   1695  CB  HIS C  30     -43.483   2.186 -24.963  1.00 86.32           C  
ANISOU 1695  CB  HIS C  30    10809  15401   6588   -885    841  -1738       C  
ATOM   1696  CG  HIS C  30     -44.420   2.917 -24.060  1.00103.14           C  
ANISOU 1696  CG  HIS C  30    12929  17577   8682   -791    843  -1814       C  
ATOM   1697  ND1 HIS C  30     -44.921   2.359 -22.894  1.00111.52           N  
ANISOU 1697  ND1 HIS C  30    13922  18669   9782   -917    911  -1902       N  
ATOM   1698  CD2 HIS C  30     -44.971   4.149 -24.146  1.00101.30           C  
ANISOU 1698  CD2 HIS C  30    12746  17369   8375   -579    789  -1817       C  
ATOM   1699  CE1 HIS C  30     -45.727   3.222 -22.312  1.00115.16           C  
ANISOU 1699  CE1 HIS C  30    14385  19180  10191   -786    896  -1960       C  
ATOM   1700  NE2 HIS C  30     -45.779   4.315 -23.046  1.00108.48           N  
ANISOU 1700  NE2 HIS C  30    13611  18328   9279   -579    820  -1914       N  
ATOM   1701  N   ARG C  31     -41.132  -0.053 -24.899  1.00 94.53           N  
ANISOU 1701  N   ARG C  31    11910  16196   7809  -1325    930  -1586       N  
ATOM   1702  CA  ARG C  31     -40.563  -1.090 -25.749  1.00 89.91           C  
ANISOU 1702  CA  ARG C  31    11268  15632   7260  -1423    939  -1579       C  
ATOM   1703  C   ARG C  31     -41.645  -1.584 -26.686  1.00106.15           C  
ANISOU 1703  C   ARG C  31    13133  17925   9274  -1351    925  -1736       C  
ATOM   1704  O   ARG C  31     -42.780  -1.802 -26.266  1.00114.98           O  
ANISOU 1704  O   ARG C  31    14125  19179  10385  -1346    953  -1878       O  
ATOM   1705  CB  ARG C  31     -40.009  -2.262 -24.944  1.00 74.02           C  
ANISOU 1705  CB  ARG C  31     9254  13527   5345  -1649   1014  -1572       C  
ATOM   1706  CG  ARG C  31     -39.303  -3.286 -25.821  1.00 73.45           C  
ANISOU 1706  CG  ARG C  31     9140  13452   5314  -1744   1019  -1556       C  
ATOM   1707  CD  ARG C  31     -38.654  -4.405 -25.033  1.00 72.55           C  
ANISOU 1707  CD  ARG C  31     9044  13225   5295  -1955   1091  -1531       C  
ATOM   1708  NE  ARG C  31     -37.896  -5.307 -25.897  1.00 73.48           N  
ANISOU 1708  NE  ARG C  31     9138  13329   5453  -2031   1090  -1510       N  
ATOM   1709  CZ  ARG C  31     -36.653  -5.076 -26.307  1.00 97.16           C  
ANISOU 1709  CZ  ARG C  31    12255  16207   8454  -2033   1056  -1373       C  
ATOM   1710  NH1 ARG C  31     -36.024  -3.971 -25.934  1.00107.01           N  
ANISOU 1710  NH1 ARG C  31    13654  17330   9676  -1971   1024  -1246       N  
ATOM   1711  NH2 ARG C  31     -36.038  -5.949 -27.091  1.00105.61           N  
ANISOU 1711  NH2 ARG C  31    13289  17281   9556  -2098   1057  -1369       N  
ATOM   1712  N   VAL C  32     -41.298  -1.756 -27.956  1.00119.11           N  
ANISOU 1712  N   VAL C  32    14746  19626  10884  -1292    882  -1718       N  
ATOM   1713  CA  VAL C  32     -42.270  -2.151 -28.967  1.00111.67           C  
ANISOU 1713  CA  VAL C  32    13621  18922   9888  -1202    855  -1871       C  
ATOM   1714  C   VAL C  32     -41.818  -3.408 -29.698  1.00100.20           C  
ANISOU 1714  C   VAL C  32    12080  17506   8486  -1326    872  -1913       C  
ATOM   1715  O   VAL C  32     -40.635  -3.571 -30.011  1.00 75.83           O  
ANISOU 1715  O   VAL C  32     9097  14288   5427  -1384    867  -1786       O  
ATOM   1716  CB  VAL C  32     -42.515  -1.023 -29.988  1.00 78.11           C  
ANISOU 1716  CB  VAL C  32     9399  14761   5517   -952    772  -1833       C  
ATOM   1717  CG1 VAL C  32     -43.409  -1.502 -31.126  1.00 90.92           C  
ANISOU 1717  CG1 VAL C  32    10827  16644   7076   -854    737  -1993       C  
ATOM   1718  CG2 VAL C  32     -43.121   0.190 -29.306  1.00 78.76           C  
ANISOU 1718  CG2 VAL C  32     9551  14823   5550   -814    754  -1817       C  
ATOM   1719  N   GLY C  33     -42.766  -4.312 -29.926  1.00106.00           N  
ANISOU 1719  N   GLY C  33    12618  18417   9239  -1373    896  -2101       N  
ATOM   1720  CA  GLY C  33     -42.512  -5.513 -30.696  1.00104.94           C  
ANISOU 1720  CA  GLY C  33    12377  18342   9152  -1475    907  -2176       C  
ATOM   1721  C   GLY C  33     -43.654  -5.833 -31.640  1.00 98.73           C  
ANISOU 1721  C   GLY C  33    11379  17823   8311  -1377    873  -2377       C  
ATOM   1722  O   GLY C  33     -44.736  -5.258 -31.527  1.00109.60           O  
ANISOU 1722  O   GLY C  33    12674  19342   9625  -1255    854  -2472       O  
ATOM   1723  N   TRP C  34     -43.418  -6.749 -32.573  1.00 90.22           N  
ANISOU 1723  N   TRP C  34    10205  16821   7255  -1424    863  -2450       N  
ATOM   1724  CA  TRP C  34     -44.459  -7.149 -33.513  1.00 95.21           C  
ANISOU 1724  CA  TRP C  34    10620  17716   7839  -1340    827  -2660       C  
ATOM   1725  C   TRP C  34     -44.988  -8.548 -33.205  1.00 87.34           C  
ANISOU 1725  C   TRP C  34     9454  16766   6966  -1544    901  -2845       C  
ATOM   1726  O   TRP C  34     -44.243  -9.424 -32.766  1.00 90.40           O  
ANISOU 1726  O   TRP C  34     9894  16988   7467  -1738    963  -2796       O  
ATOM   1727  CB  TRP C  34     -43.934  -7.093 -34.947  1.00 96.09           C  
ANISOU 1727  CB  TRP C  34    10724  17918   7867  -1211    752  -2634       C  
ATOM   1728  CG  TRP C  34     -43.704  -5.701 -35.449  1.00 89.79           C  
ANISOU 1728  CG  TRP C  34    10053  17130   6932   -977    679  -2486       C  
ATOM   1729  CD1 TRP C  34     -42.591  -4.941 -35.259  1.00 89.37           C  
ANISOU 1729  CD1 TRP C  34    10216  16873   6867   -954    673  -2256       C  
ATOM   1730  CD2 TRP C  34     -44.604  -4.903 -36.229  1.00 82.79           C  
ANISOU 1730  CD2 TRP C  34     9087  16465   5906   -730    606  -2557       C  
ATOM   1731  NE1 TRP C  34     -42.738  -3.721 -35.869  1.00 80.50           N  
ANISOU 1731  NE1 TRP C  34     9159  15815   5612   -717    608  -2173       N  
ATOM   1732  CE2 TRP C  34     -43.966  -3.671 -36.471  1.00 82.04           C  
ANISOU 1732  CE2 TRP C  34     9179  16272   5722   -568    564  -2350       C  
ATOM   1733  CE3 TRP C  34     -45.887  -5.114 -36.748  1.00 94.50           C  
ANISOU 1733  CE3 TRP C  34    10354  18222   7329   -629    572  -2780       C  
ATOM   1734  CZ2 TRP C  34     -44.567  -2.651 -37.207  1.00 83.33           C  
ANISOU 1734  CZ2 TRP C  34     9333  16592   5736   -301    492  -2345       C  
ATOM   1735  CZ3 TRP C  34     -46.484  -4.097 -37.480  1.00 85.15           C  
ANISOU 1735  CZ3 TRP C  34     9153  17211   5990   -357    494  -2783       C  
ATOM   1736  CH2 TRP C  34     -45.823  -2.883 -37.702  1.00 84.86           C  
ANISOU 1736  CH2 TRP C  34     9317  17062   5864   -193    456  -2561       C  
ATOM   1737  N   PHE C  35     -46.282  -8.745 -33.435  1.00 82.36           N  
ANISOU 1737  N   PHE C  35     8619  16360   6314  -1498    895  -3057       N  
ATOM   1738  CA  PHE C  35     -46.918 -10.039 -33.220  1.00 99.56           C  
ANISOU 1738  CA  PHE C  35    10615  18601   8612  -1687    967  -3255       C  
ATOM   1739  C   PHE C  35     -47.695 -10.445 -34.460  1.00107.60           C  
ANISOU 1739  C   PHE C  35    11413  19890   9582  -1595    908  -3476       C  
ATOM   1740  O   PHE C  35     -48.425  -9.641 -35.035  1.00112.19           O  
ANISOU 1740  O   PHE C  35    11920  20673  10034  -1383    833  -3542       O  
ATOM   1741  CB  PHE C  35     -47.849 -10.004 -32.003  1.00124.68           C  
ANISOU 1741  CB  PHE C  35    13741  21788  11844  -1770   1045  -3323       C  
ATOM   1742  CG  PHE C  35     -47.131  -9.885 -30.692  1.00123.66           C  
ANISOU 1742  CG  PHE C  35    13801  21401  11781  -1900   1118  -3139       C  
ATOM   1743  CD1 PHE C  35     -46.665  -8.662 -30.245  1.00109.88           C  
ANISOU 1743  CD1 PHE C  35    12243  19550   9957  -1776   1081  -2955       C  
ATOM   1744  CD2 PHE C  35     -46.929 -11.004 -29.903  1.00118.89           C  
ANISOU 1744  CD2 PHE C  35    13189  20662  11321  -2141   1226  -3152       C  
ATOM   1745  CE1 PHE C  35     -46.006  -8.560 -29.040  1.00107.28           C  
ANISOU 1745  CE1 PHE C  35    12078  18998   9685  -1891   1143  -2801       C  
ATOM   1746  CE2 PHE C  35     -46.271 -10.908 -28.697  1.00115.04           C  
ANISOU 1746  CE2 PHE C  35    12873  19955  10884  -2248   1291  -2984       C  
ATOM   1747  CZ  PHE C  35     -45.809  -9.684 -28.264  1.00111.29           C  
ANISOU 1747  CZ  PHE C  35    12573  19388  10323  -2122   1246  -2814       C  
ATOM   1748  N   ARG C  36     -47.549 -11.706 -34.853  1.00105.76           N  
ANISOU 1748  N   ARG C  36    11071  19661   9452  -1751    942  -3597       N  
ATOM   1749  CA  ARG C  36     -48.213 -12.214 -36.045  1.00108.98           C  
ANISOU 1749  CA  ARG C  36    11261  20322   9826  -1681    886  -3825       C  
ATOM   1750  C   ARG C  36     -49.201 -13.324 -35.720  1.00111.96           C  
ANISOU 1750  C   ARG C  36    11419  20787  10334  -1864    964  -4072       C  
ATOM   1751  O   ARG C  36     -49.038 -14.056 -34.741  1.00107.64           O  
ANISOU 1751  O   ARG C  36    10906  20058   9933  -2088   1072  -4047       O  
ATOM   1752  CB  ARG C  36     -47.186 -12.709 -37.059  1.00100.05           C  
ANISOU 1752  CB  ARG C  36    10172  19153   8689  -1676    842  -3781       C  
ATOM   1753  CG  ARG C  36     -46.369 -13.893 -36.599  1.00 94.17           C  
ANISOU 1753  CG  ARG C  36     9483  18187   8112  -1927    927  -3747       C  
ATOM   1754  CD  ARG C  36     -45.372 -14.285 -37.663  1.00 84.83           C  
ANISOU 1754  CD  ARG C  36     8338  16989   6906  -1894    873  -3707       C  
ATOM   1755  NE  ARG C  36     -44.877 -15.646 -37.497  1.00 93.38           N  
ANISOU 1755  NE  ARG C  36     9399  17930   8152  -2120    945  -3764       N  
ATOM   1756  CZ  ARG C  36     -43.735 -16.080 -38.018  1.00109.68           C  
ANISOU 1756  CZ  ARG C  36    11553  19888  10233  -2147    927  -3675       C  
ATOM   1757  NH1 ARG C  36     -42.977 -15.250 -38.724  1.00106.54           N  
ANISOU 1757  NH1 ARG C  36    11269  19512   9698  -1971    846  -3521       N  
ATOM   1758  NH2 ARG C  36     -43.345 -17.333 -37.828  1.00122.96           N  
ANISOU 1758  NH2 ARG C  36    13213  21438  12069  -2348    995  -3734       N  
ATOM   1759  N   ARG C  37     -50.236 -13.439 -36.543  1.00118.37           N  
ANISOU 1759  N   ARG C  37    12002  21880  11091  -1764    911  -4310       N  
ATOM   1760  CA  ARG C  37     -51.264 -14.436 -36.310  1.00122.67           C  
ANISOU 1760  CA  ARG C  37    12316  22533  11759  -1930    982  -4567       C  
ATOM   1761  C   ARG C  37     -51.212 -15.548 -37.354  1.00106.35           C  
ANISOU 1761  C   ARG C  37    10090  20562   9756  -1999    960  -4762       C  
ATOM   1762  O   ARG C  37     -51.906 -15.507 -38.370  1.00 93.03           O  
ANISOU 1762  O   ARG C  37     8215  19149   7984  -1858    878  -4962       O  
ATOM   1763  CB  ARG C  37     -52.642 -13.770 -36.322  1.00125.35           C  
ANISOU 1763  CB  ARG C  37    12483  23140  12005  -1784    946  -4730       C  
ATOM   1764  N   ALA C  38     -50.364 -16.538 -37.080  1.00107.51           N  
ANISOU 1764  N   ALA C  38    10317  20482  10050  -2209   1033  -4703       N  
ATOM   1765  CA  ALA C  38     -50.287 -17.771 -37.855  1.00107.31           C  
ANISOU 1765  CA  ALA C  38    10149  20496  10127  -2325   1038  -4893       C  
ATOM   1766  C   ALA C  38     -51.461 -18.696 -37.540  1.00133.66           C  
ANISOU 1766  C   ALA C  38    13246  23930  13608  -2504   1122  -5166       C  
ATOM   1767  O   ALA C  38     -51.875 -18.796 -36.387  1.00154.26           O  
ANISOU 1767  O   ALA C  38    15870  26432  16308  -2648   1228  -5136       O  
ATOM   1768  CB  ALA C  38     -48.970 -18.478 -37.591  1.00 99.20           C  
ANISOU 1768  CB  ALA C  38     9303  19178   9211  -2483   1092  -4726       C  
ATOM   1769  N   PRO C  39     -52.005 -19.374 -38.560  1.00139.71           N  
ANISOU 1769  N   PRO C  39    13784  24903  14394  -2497   1076  -5438       N  
ATOM   1770  CA  PRO C  39     -53.155 -20.270 -38.376  1.00140.93           C  
ANISOU 1770  CA  PRO C  39    13686  25169  14691  -2668   1152  -5726       C  
ATOM   1771  C   PRO C  39     -52.893 -21.403 -37.373  1.00150.40           C  
ANISOU 1771  C   PRO C  39    14936  26086  16125  -2983   1312  -5698       C  
ATOM   1772  O   PRO C  39     -53.806 -21.789 -36.644  1.00142.87           O  
ANISOU 1772  O   PRO C  39    13853  25148  15281  -3137   1414  -5821       O  
ATOM   1773  CB  PRO C  39     -53.384 -20.833 -39.779  1.00131.03           C  
ANISOU 1773  CB  PRO C  39    12229  24141  13415  -2598   1060  -5986       C  
ATOM   1774  CG  PRO C  39     -52.842 -19.796 -40.688  1.00125.29           C  
ANISOU 1774  CG  PRO C  39    11602  23540  12465  -2304    916  -5857       C  
ATOM   1775  CD  PRO C  39     -51.643 -19.234 -39.981  1.00128.92           C  
ANISOU 1775  CD  PRO C  39    12374  23710  12901  -2305    945  -5500       C  
ATOM   1776  N   GLY C  40     -51.680 -21.952 -37.369  1.00159.91           N  
ANISOU 1776  N   GLY C  40    16315  27044  17401  -3074   1336  -5544       N  
ATOM   1777  CA  GLY C  40     -51.337 -23.032 -36.456  1.00163.51           C  
ANISOU 1777  CA  GLY C  40    16838  27218  18070  -3353   1484  -5497       C  
ATOM   1778  C   GLY C  40     -51.274 -22.710 -34.970  1.00165.14           C  
ANISOU 1778  C   GLY C  40    17204  27224  18316  -3455   1598  -5283       C  
ATOM   1779  O   GLY C  40     -51.819 -23.451 -34.153  1.00145.47           O  
ANISOU 1779  O   GLY C  40    14646  24643  15984  -3669   1733  -5354       O  
ATOM   1780  N   LYS C  41     -50.544 -21.657 -34.661  1.00177.29           N  
ANISOU 1780  N   LYS C  41    18959  28687  19716  -3307   1544  -5022       N  
ATOM   1781  CA  LYS C  41     -50.366 -21.262 -33.294  1.00175.59           C  
ANISOU 1781  CA  LYS C  41    18911  28287  19517  -3377   1635  -4809       C  
ATOM   1782  C   LYS C  41     -50.976 -19.958 -32.880  1.00178.30           C  
ANISOU 1782  C   LYS C  41    19268  28768  19709  -3208   1593  -4748       C  
ATOM   1783  O   LYS C  41     -51.502 -19.915 -31.771  1.00191.35           O  
ANISOU 1783  O   LYS C  41    20925  30368  21413  -3309   1694  -4717       O  
ATOM   1784  CB  LYS C  41     -48.884 -21.117 -32.955  1.00170.83           C  
ANISOU 1784  CB  LYS C  41    18587  27422  18899  -3375   1630  -4521       C  
ATOM   1785  N   GLU C  42     -50.744 -18.877 -33.676  1.00164.46           N  
ANISOU 1785  N   GLU C  42    17561  27154  17771  -2952   1451  -4690       N  
ATOM   1786  CA  GLU C  42     -51.232 -17.497 -33.556  1.00139.06           C  
ANISOU 1786  CA  GLU C  42    14369  24085  14384  -2735   1380  -4630       C  
ATOM   1787  C   GLU C  42     -50.666 -16.778 -32.326  1.00132.46           C  
ANISOU 1787  C   GLU C  42    13767  23037  13523  -2744   1428  -4362       C  
ATOM   1788  O   GLU C  42     -50.141 -17.403 -31.400  1.00113.43           O  
ANISOU 1788  O   GLU C  42    11468  20394  11235  -2936   1535  -4250       O  
ATOM   1789  CB  GLU C  42     -52.768 -17.464 -33.606  1.00112.34           C  
ANISOU 1789  CB  GLU C  42    10725  20968  10992  -2714   1390  -4887       C  
ATOM   1790  CG  GLU C  42     -53.365 -16.089 -33.881  1.00114.29           C  
ANISOU 1790  CG  GLU C  42    10952  21430  11044  -2442   1284  -4882       C  
ATOM   1791  CD  GLU C  42     -54.879 -16.058 -33.811  1.00134.13           C  
ANISOU 1791  CD  GLU C  42    13208  24205  13550  -2425   1301  -5132       C  
ATOM   1792  OE1 GLU C  42     -55.514 -17.083 -34.128  1.00147.83           O  
ANISOU 1792  OE1 GLU C  42    14727  26043  15401  -2568   1346  -5374       O  
ATOM   1793  OE2 GLU C  42     -55.432 -15.000 -33.437  1.00138.61           O  
ANISOU 1793  OE2 GLU C  42    13789  24877  13998  -2267   1268  -5093       O  
ATOM   1794  N   ARG C  43     -50.808 -15.452 -32.344  1.00152.08           N  
ANISOU 1794  N   ARG C  43    16322  25613  15847  -2525   1345  -4270       N  
ATOM   1795  CA  ARG C  43     -50.376 -14.534 -31.293  1.00153.19           C  
ANISOU 1795  CA  ARG C  43    16672  25597  15936  -2484   1365  -4039       C  
ATOM   1796  C   ARG C  43     -49.002 -14.770 -30.678  1.00150.09           C  
ANISOU 1796  C   ARG C  43    16519  24903  15607  -2598   1410  -3800       C  
ATOM   1797  O   ARG C  43     -48.864 -14.950 -29.467  1.00177.11           O  
ANISOU 1797  O   ARG C  43    20033  28161  19101  -2735   1509  -3700       O  
ATOM   1798  CB  ARG C  43     -51.434 -14.444 -30.188  1.00165.78           C  
ANISOU 1798  CB  ARG C  43    18182  27242  17566  -2558   1456  -4111       C  
ATOM   1799  CG  ARG C  43     -51.136 -13.407 -29.104  1.00174.40           C  
ANISOU 1799  CG  ARG C  43    19468  28206  18589  -2492   1468  -3902       C  
ATOM   1800  CD  ARG C  43     -50.938 -12.019 -29.708  1.00174.61           C  
ANISOU 1800  CD  ARG C  43    19589  28314  18442  -2217   1334  -3809       C  
ATOM   1801  NE  ARG C  43     -52.101 -11.563 -30.467  1.00175.92           N  
ANISOU 1801  NE  ARG C  43    19557  28775  18510  -2043   1261  -4006       N  
ATOM   1802  CZ  ARG C  43     -53.105 -10.860 -29.950  1.00178.25           C  
ANISOU 1802  CZ  ARG C  43    19780  29208  18741  -1949   1264  -4073       C  
ATOM   1803  NH1 ARG C  43     -53.094 -10.532 -28.663  1.00179.14           N  
ANISOU 1803  NH1 ARG C  43    20001  29188  18877  -2015   1339  -3961       N  
ATOM   1804  NH2 ARG C  43     -54.121 -10.487 -30.719  1.00171.00           N  
ANISOU 1804  NH2 ARG C  43    18675  28567  17728  -1780   1191  -4258       N  
ATOM   1805  N   GLU C  44     -47.989 -14.799 -31.534  1.00115.18           N  
ANISOU 1805  N   GLU C  44    12189  20422  11154  -2538   1338  -3714       N  
ATOM   1806  CA  GLU C  44     -46.641 -15.125 -31.097  1.00109.40           C  
ANISOU 1806  CA  GLU C  44    11662  19421  10483  -2645   1373  -3508       C  
ATOM   1807  C   GLU C  44     -45.678 -13.967 -31.353  1.00109.75           C  
ANISOU 1807  C   GLU C  44    11905  19397  10400  -2469   1281  -3294       C  
ATOM   1808  O   GLU C  44     -45.861 -13.181 -32.289  1.00 97.10           O  
ANISOU 1808  O   GLU C  44    10270  17953   8670  -2267   1178  -3317       O  
ATOM   1809  CB  GLU C  44     -46.140 -16.395 -31.777  1.00103.41           C  
ANISOU 1809  CB  GLU C  44    10845  18612   9832  -2775   1392  -3589       C  
ATOM   1810  CG  GLU C  44     -45.579 -16.193 -33.162  1.00104.45           C  
ANISOU 1810  CG  GLU C  44    10973  18839   9875  -2624   1276  -3597       C  
ATOM   1811  CD  GLU C  44     -44.742 -17.371 -33.606  1.00117.88           C  
ANISOU 1811  CD  GLU C  44    12684  20421  11683  -2758   1300  -3612       C  
ATOM   1812  OE1 GLU C  44     -44.376 -18.188 -32.738  1.00126.98           O  
ANISOU 1812  OE1 GLU C  44    13901  21373  12971  -2954   1403  -3559       O  
ATOM   1813  OE2 GLU C  44     -44.453 -17.484 -34.816  1.00122.42           O  
ANISOU 1813  OE2 GLU C  44    13204  21105  12206  -2662   1218  -3677       O  
ATOM   1814  N   PHE C  45     -44.641 -13.887 -30.524  1.00106.16           N  
ANISOU 1814  N   PHE C  45    11653  18704   9981  -2548   1320  -3086       N  
ATOM   1815  CA  PHE C  45     -43.634 -12.838 -30.624  1.00100.94           C  
ANISOU 1815  CA  PHE C  45    11189  17943   9222  -2414   1248  -2874       C  
ATOM   1816  C   PHE C  45     -42.911 -12.912 -31.955  1.00102.42           C  
ANISOU 1816  C   PHE C  45    11381  18175   9360  -2325   1165  -2860       C  
ATOM   1817  O   PHE C  45     -42.689 -13.998 -32.481  1.00 89.57           O  
ANISOU 1817  O   PHE C  45     9674  16548   7810  -2427   1183  -2950       O  
ATOM   1818  CB  PHE C  45     -42.619 -12.957 -29.482  1.00100.75           C  
ANISOU 1818  CB  PHE C  45    11359  17658   9263  -2544   1313  -2679       C  
ATOM   1819  CG  PHE C  45     -41.485 -11.974 -29.575  1.00 98.17           C  
ANISOU 1819  CG  PHE C  45    11230  17214   8856  -2434   1246  -2469       C  
ATOM   1820  CD1 PHE C  45     -41.613 -10.690 -29.070  1.00 87.95           C  
ANISOU 1820  CD1 PHE C  45    10035  15908   7474  -2309   1213  -2371       C  
ATOM   1821  CD2 PHE C  45     -40.297 -12.327 -30.192  1.00 99.19           C  
ANISOU 1821  CD2 PHE C  45    11442  17246   9000  -2455   1217  -2375       C  
ATOM   1822  CE1 PHE C  45     -40.572  -9.794 -29.162  1.00 81.53           C  
ANISOU 1822  CE1 PHE C  45     9399  14977   6600  -2220   1157  -2185       C  
ATOM   1823  CE2 PHE C  45     -39.255 -11.429 -30.297  1.00 88.00           C  
ANISOU 1823  CE2 PHE C  45    10197  15724   7515  -2364   1161  -2186       C  
ATOM   1824  CZ  PHE C  45     -39.390 -10.167 -29.776  1.00 84.83           C  
ANISOU 1824  CZ  PHE C  45     9893  15302   7037  -2252   1134  -2091       C  
ATOM   1825  N   VAL C  46     -42.554 -11.753 -32.502  1.00109.33           N  
ANISOU 1825  N   VAL C  46    12348  19087  10105  -2131   1076  -2747       N  
ATOM   1826  CA  VAL C  46     -41.810 -11.702 -33.759  1.00101.28           C  
ANISOU 1826  CA  VAL C  46    11349  18113   9022  -2029   1000  -2708       C  
ATOM   1827  C   VAL C  46     -40.521 -10.887 -33.624  1.00102.19           C  
ANISOU 1827  C   VAL C  46    11688  18050   9090  -1977    971  -2458       C  
ATOM   1828  O   VAL C  46     -39.423 -11.424 -33.773  1.00 75.85           O  
ANISOU 1828  O   VAL C  46     8432  14583   5803  -2064    982  -2368       O  
ATOM   1829  CB  VAL C  46     -42.661 -11.102 -34.891  1.00102.02           C  
ANISOU 1829  CB  VAL C  46    11311  18470   8984  -1815    912  -2828       C  
ATOM   1830  CG1 VAL C  46     -41.878 -11.097 -36.189  1.00 86.23           C  
ANISOU 1830  CG1 VAL C  46     9329  16524   6911  -1710    840  -2783       C  
ATOM   1831  CG2 VAL C  46     -43.950 -11.879 -35.054  1.00112.21           C  
ANISOU 1831  CG2 VAL C  46    12363  19953  10319  -1864    935  -3092       C  
ATOM   1832  N   ALA C  47     -40.655  -9.598 -33.322  1.00106.26           N  
ANISOU 1832  N   ALA C  47    12301  18556   9516  -1839    937  -2352       N  
ATOM   1833  CA  ALA C  47     -39.492  -8.721 -33.200  1.00115.21           C  
ANISOU 1833  CA  ALA C  47    13641  19523  10609  -1786    911  -2124       C  
ATOM   1834  C   ALA C  47     -39.634  -7.800 -31.993  1.00124.96           C  
ANISOU 1834  C   ALA C  47    14996  20641  11841  -1776    934  -2027       C  
ATOM   1835  O   ALA C  47     -40.678  -7.788 -31.352  1.00128.87           O  
ANISOU 1835  O   ALA C  47    15408  21207  12348  -1788    964  -2136       O  
ATOM   1836  CB  ALA C  47     -39.303  -7.917 -34.469  1.00118.91           C  
ANISOU 1836  CB  ALA C  47    14125  20107  10949  -1578    825  -2074       C  
ATOM   1837  N   ALA C  48     -38.599  -7.017 -31.692  1.00108.83           N  
ANISOU 1837  N   ALA C  48    13141  18427   9781  -1754    919  -1831       N  
ATOM   1838  CA  ALA C  48     -38.624  -6.163 -30.503  1.00 93.50           C  
ANISOU 1838  CA  ALA C  48    11321  16360   7844  -1753    940  -1741       C  
ATOM   1839  C   ALA C  48     -37.627  -5.013 -30.566  1.00 87.80           C  
ANISOU 1839  C   ALA C  48    10788  15498   7076  -1664    898  -1544       C  
ATOM   1840  O   ALA C  48     -36.435  -5.220 -30.807  1.00 79.96           O  
ANISOU 1840  O   ALA C  48     9885  14387   6111  -1726    897  -1428       O  
ATOM   1841  CB  ALA C  48     -38.363  -6.991 -29.261  1.00100.06           C  
ANISOU 1841  CB  ALA C  48    12180  17052   8787  -1959   1022  -1737       C  
ATOM   1842  N   ILE C  49     -38.121  -3.802 -30.326  1.00 88.10           N  
ANISOU 1842  N   ILE C  49    10882  15545   7046  -1521    867  -1511       N  
ATOM   1843  CA  ILE C  49     -37.277  -2.617 -30.380  1.00 93.57           C  
ANISOU 1843  CA  ILE C  49    11751  16099   7701  -1431    832  -1333       C  
ATOM   1844  C   ILE C  49     -37.333  -1.796 -29.087  1.00 95.61           C  
ANISOU 1844  C   ILE C  49    12124  16220   7981  -1442    850  -1278       C  
ATOM   1845  O   ILE C  49     -38.381  -1.673 -28.454  1.00 94.29           O  
ANISOU 1845  O   ILE C  49    11891  16129   7805  -1415    865  -1383       O  
ATOM   1846  CB  ILE C  49     -37.670  -1.705 -31.575  1.00 74.54           C  
ANISOU 1846  CB  ILE C  49     9331  13817   5174  -1203    765  -1316       C  
ATOM   1847  CG1 ILE C  49     -36.680  -0.549 -31.741  1.00 74.28           C  
ANISOU 1847  CG1 ILE C  49     9486  13622   5114  -1125    739  -1117       C  
ATOM   1848  CG2 ILE C  49     -39.101  -1.201 -31.429  1.00 75.76           C  
ANISOU 1848  CG2 ILE C  49     9394  14126   5267  -1066    746  -1443       C  
ATOM   1849  CD1 ILE C  49     -35.264  -1.009 -31.942  1.00 73.19           C  
ANISOU 1849  CD1 ILE C  49     9427  13349   5031  -1252    756   -996       C  
ATOM   1850  N   GLY C  50     -36.185  -1.262 -28.686  1.00 72.47           N  
ANISOU 1850  N   GLY C  50     9359  13094   5082  -1485    849  -1120       N  
ATOM   1851  CA  GLY C  50     -36.137  -0.386 -27.546  1.00 80.62           C  
ANISOU 1851  CA  GLY C  50    10508  13992   6131  -1481    857  -1067       C  
ATOM   1852  C   GLY C  50     -36.640   0.994 -27.934  1.00 94.63           C  
ANISOU 1852  C   GLY C  50    12340  15791   7826  -1273    806  -1034       C  
ATOM   1853  O   GLY C  50     -36.720   1.309 -29.113  1.00 99.64           O  
ANISOU 1853  O   GLY C  50    12954  16512   8394  -1142    766  -1011       O  
ATOM   1854  N   ALA C  51     -36.977   1.816 -26.944  1.00103.11           N  
ANISOU 1854  N   ALA C  51    13486  16789   8902  -1236    807  -1033       N  
ATOM   1855  CA  ALA C  51     -37.419   3.188 -27.187  1.00 91.71           C  
ANISOU 1855  CA  ALA C  51    12115  15337   7392  -1037    762   -997       C  
ATOM   1856  C   ALA C  51     -36.277   4.036 -27.729  1.00 90.89           C  
ANISOU 1856  C   ALA C  51    12170  15071   7292   -993    736   -821       C  
ATOM   1857  O   ALA C  51     -36.492   4.963 -28.510  1.00 97.42           O  
ANISOU 1857  O   ALA C  51    13044  15917   8054   -816    699   -768       O  
ATOM   1858  CB  ALA C  51     -37.986   3.804 -25.921  1.00 90.45           C  
ANISOU 1858  CB  ALA C  51    11998  15126   7244  -1020    772  -1045       C  
ATOM   1859  N   SER C  52     -35.062   3.722 -27.290  1.00 83.59           N  
ANISOU 1859  N   SER C  52    11330  13986   6444  -1155    761   -731       N  
ATOM   1860  CA  SER C  52     -33.865   4.414 -27.755  1.00 92.73           C  
ANISOU 1860  CA  SER C  52    12629  14985   7620  -1148    748   -566       C  
ATOM   1861  C   SER C  52     -33.469   3.947 -29.151  1.00 95.38           C  
ANISOU 1861  C   SER C  52    12914  15411   7917  -1119    738   -517       C  
ATOM   1862  O   SER C  52     -32.723   4.623 -29.857  1.00 95.68           O  
ANISOU 1862  O   SER C  52    13049  15366   7941  -1061    726   -382       O  
ATOM   1863  CB  SER C  52     -32.703   4.176 -26.790  1.00 93.43           C  
ANISOU 1863  CB  SER C  52    12806  14892   7802  -1333    776   -502       C  
ATOM   1864  OG  SER C  52     -32.388   2.794 -26.715  1.00 81.89           O  
ANISOU 1864  OG  SER C  52    11253  13486   6376  -1487    807   -547       O  
ATOM   1865  N   GLY C  53     -33.993   2.789 -29.541  1.00 97.45           N  
ANISOU 1865  N   GLY C  53    13021  15844   8160  -1159    747   -631       N  
ATOM   1866  CA  GLY C  53     -33.665   2.175 -30.815  1.00 96.83           C  
ANISOU 1866  CA  GLY C  53    12874  15874   8044  -1141    737   -613       C  
ATOM   1867  C   GLY C  53     -32.685   1.024 -30.672  1.00 98.05           C  
ANISOU 1867  C   GLY C  53    13007  15975   8272  -1336    769   -599       C  
ATOM   1868  O   GLY C  53     -32.409   0.300 -31.625  1.00118.86           O  
ANISOU 1868  O   GLY C  53    15569  18705  10887  -1346    765   -608       O  
ATOM   1869  N   GLY C  54     -32.148   0.862 -29.470  1.00 98.83           N  
ANISOU 1869  N   GLY C  54    13172  15925   8453  -1483    799   -578       N  
ATOM   1870  CA  GLY C  54     -31.250  -0.234 -29.165  1.00 96.85           C  
ANISOU 1870  CA  GLY C  54    12909  15616   8274  -1664    831   -567       C  
ATOM   1871  C   GLY C  54     -31.978  -1.404 -28.528  1.00 93.19           C  
ANISOU 1871  C   GLY C  54    12324  15237   7847  -1767    867   -712       C  
ATOM   1872  O   GLY C  54     -33.213  -1.428 -28.482  1.00 70.36           O  
ANISOU 1872  O   GLY C  54     9338  12475   4921  -1698    866   -831       O  
ATOM   1873  N   MET C  55     -31.207  -2.375 -28.044  1.00100.19           N  
ANISOU 1873  N   MET C  55    13214  16050   8804  -1931    902   -700       N  
ATOM   1874  CA  MET C  55     -31.757  -3.538 -27.361  1.00 99.86           C  
ANISOU 1874  CA  MET C  55    13077  16056   8811  -2047    950   -816       C  
ATOM   1875  C   MET C  55     -32.803  -4.221 -28.222  1.00 87.07           C  
ANISOU 1875  C   MET C  55    11293  14630   7160  -1999    949   -956       C  
ATOM   1876  O   MET C  55     -33.930  -4.455 -27.787  1.00 78.32           O  
ANISOU 1876  O   MET C  55    10093  13614   6052  -1996    972  -1078       O  
ATOM   1877  CB  MET C  55     -32.361  -3.134 -26.018  1.00100.45           C  
ANISOU 1877  CB  MET C  55    13185  16083   8899  -2065    975   -850       C  
ATOM   1878  CG  MET C  55     -31.468  -2.243 -25.175  1.00101.62           C  
ANISOU 1878  CG  MET C  55    13490  16054   9066  -2084    965   -731       C  
ATOM   1879  SD  MET C  55     -29.733  -2.694 -25.263  1.00129.66           S  
ANISOU 1879  SD  MET C  55    17129  19463  12672  -2206    967   -603       S  
ATOM   1880  CE  MET C  55     -29.001  -1.085 -25.567  1.00128.75           C  
ANISOU 1880  CE  MET C  55    17157  19230  12531  -2104    917   -469       C  
ATOM   1881  N   THR C  56     -32.420  -4.510 -29.459  1.00100.42           N  
ANISOU 1881  N   THR C  56    12941  16390   8822  -1958    921   -943       N  
ATOM   1882  CA  THR C  56     -33.295  -5.191 -30.391  1.00 88.48           C  
ANISOU 1882  CA  THR C  56    11269  15071   7280  -1910    912  -1083       C  
ATOM   1883  C   THR C  56     -33.390  -6.667 -30.055  1.00 95.41           C  
ANISOU 1883  C   THR C  56    12050  15961   8242  -2073    965  -1187       C  
ATOM   1884  O   THR C  56     -32.456  -7.251 -29.512  1.00 87.68           O  
ANISOU 1884  O   THR C  56    11136  14846   7331  -2205    998  -1120       O  
ATOM   1885  CB  THR C  56     -32.808  -5.041 -31.836  1.00 86.18           C  
ANISOU 1885  CB  THR C  56    10963  14857   6923  -1808    865  -1036       C  
ATOM   1886  OG1 THR C  56     -31.500  -5.613 -31.959  1.00101.18           O  
ANISOU 1886  OG1 THR C  56    12923  16649   8873  -1917    878   -945       O  
ATOM   1887  CG2 THR C  56     -32.749  -3.576 -32.227  1.00 79.07           C  
ANISOU 1887  CG2 THR C  56    10163  13940   5939  -1640    821   -923       C  
ATOM   1888  N   ASN C  57     -34.537  -7.260 -30.351  1.00 87.39           N  
ANISOU 1888  N   ASN C  57    10877  15104   7222  -2061    976  -1354       N  
ATOM   1889  CA  ASN C  57     -34.690  -8.693 -30.195  1.00 95.45           C  
ANISOU 1889  CA  ASN C  57    11796  16141   8331  -2211   1030  -1464       C  
ATOM   1890  C   ASN C  57     -35.650  -9.266 -31.234  1.00107.76           C  
ANISOU 1890  C   ASN C  57    13171  17909   9866  -2157   1011  -1641       C  
ATOM   1891  O   ASN C  57     -36.685  -8.670 -31.537  1.00109.20           O  
ANISOU 1891  O   ASN C  57    13274  18238   9979  -2031    981  -1725       O  
ATOM   1892  CB  ASN C  57     -35.155  -9.036 -28.786  1.00 80.51           C  
ANISOU 1892  CB  ASN C  57     9909  14172   6507  -2332   1101  -1497       C  
ATOM   1893  CG  ASN C  57     -34.695 -10.411 -28.351  1.00102.87           C  
ANISOU 1893  CG  ASN C  57    12725  16915   9445  -2513   1168  -1517       C  
ATOM   1894  OD1 ASN C  57     -34.609 -11.331 -29.163  1.00112.46           O  
ANISOU 1894  OD1 ASN C  57    13850  18187  10693  -2552   1169  -1594       O  
ATOM   1895  ND2 ASN C  57     -34.393 -10.561 -27.067  1.00117.08           N  
ANISOU 1895  ND2 ASN C  57    14613  18576  11298  -2619   1225  -1450       N  
ATOM   1896  N   TYR C  58     -35.290 -10.425 -31.777  1.00101.40           N  
ANISOU 1896  N   TYR C  58    12294  17118   9117  -2247   1027  -1704       N  
ATOM   1897  CA  TYR C  58     -36.072 -11.084 -32.817  1.00 83.22           C  
ANISOU 1897  CA  TYR C  58     9811  15009   6800  -2209   1007  -1884       C  
ATOM   1898  C   TYR C  58     -36.322 -12.553 -32.479  1.00 78.99           C  
ANISOU 1898  C   TYR C  58     9174  14449   6389  -2389   1077  -2016       C  
ATOM   1899  O   TYR C  58     -36.067 -12.998 -31.362  1.00 72.17           O  
ANISOU 1899  O   TYR C  58     8377  13432   5613  -2531   1147  -1967       O  
ATOM   1900  CB  TYR C  58     -35.350 -10.996 -34.170  1.00 76.08           C  
ANISOU 1900  CB  TYR C  58     8907  14174   5825  -2106    942  -1844       C  
ATOM   1901  CG  TYR C  58     -34.898  -9.607 -34.587  1.00 76.40           C  
ANISOU 1901  CG  TYR C  58     9066  14211   5752  -1939    882  -1686       C  
ATOM   1902  CD1 TYR C  58     -35.747  -8.760 -35.289  1.00 75.26           C  
ANISOU 1902  CD1 TYR C  58     8862  14240   5495  -1751    827  -1734       C  
ATOM   1903  CD2 TYR C  58     -33.622  -9.148 -34.287  1.00 83.08           C  
ANISOU 1903  CD2 TYR C  58    10082  14880   6605  -1968    884  -1491       C  
ATOM   1904  CE1 TYR C  58     -35.339  -7.495 -35.680  1.00 84.13           C  
ANISOU 1904  CE1 TYR C  58    10102  15345   6518  -1596    781  -1581       C  
ATOM   1905  CE2 TYR C  58     -33.206  -7.883 -34.669  1.00 95.54           C  
ANISOU 1905  CE2 TYR C  58    11768  16440   8091  -1826    839  -1347       C  
ATOM   1906  CZ  TYR C  58     -34.068  -7.061 -35.366  1.00 87.51           C  
ANISOU 1906  CZ  TYR C  58    10699  15583   6966  -1641    791  -1387       C  
ATOM   1907  OH  TYR C  58     -33.656  -5.801 -35.748  1.00 73.05           O  
ANISOU 1907  OH  TYR C  58     8987  13720   5050  -1499    754  -1233       O  
ATOM   1908  N   LEU C  59     -36.809 -13.306 -33.461  1.00 82.12           N  
ANISOU 1908  N   LEU C  59     9411  14998   6793  -2378   1060  -2183       N  
ATOM   1909  CA  LEU C  59     -36.943 -14.755 -33.335  1.00 79.76           C  
ANISOU 1909  CA  LEU C  59     9016  14668   6621  -2548   1124  -2312       C  
ATOM   1910  C   LEU C  59     -35.656 -15.424 -33.796  1.00101.85           C  
ANISOU 1910  C   LEU C  59    11883  17359   9457  -2603   1117  -2236       C  
ATOM   1911  O   LEU C  59     -34.754 -14.755 -34.296  1.00115.39           O  
ANISOU 1911  O   LEU C  59    13699  19052  11092  -2506   1061  -2098       O  
ATOM   1912  CB  LEU C  59     -38.127 -15.260 -34.156  1.00 75.44           C  
ANISOU 1912  CB  LEU C  59     8251  14341   6073  -2515   1108  -2553       C  
ATOM   1913  CG  LEU C  59     -39.481 -14.732 -33.698  1.00 76.38           C  
ANISOU 1913  CG  LEU C  59     8275  14584   6163  -2470   1121  -2656       C  
ATOM   1914  CD1 LEU C  59     -40.616 -15.368 -34.472  1.00 82.05           C  
ANISOU 1914  CD1 LEU C  59     8762  15519   6895  -2460   1111  -2912       C  
ATOM   1915  CD2 LEU C  59     -39.618 -15.031 -32.230  1.00 82.13           C  
ANISOU 1915  CD2 LEU C  59     9065  15149   6991  -2630   1221  -2608       C  
ATOM   1916  N   ASP C  60     -35.563 -16.738 -33.635  1.00 98.56           N  
ANISOU 1916  N   ASP C  60    11412  16871   9163  -2758   1177  -2324       N  
ATOM   1917  CA  ASP C  60     -34.414 -17.459 -34.164  1.00122.46           C  
ANISOU 1917  CA  ASP C  60    14486  19816  12227  -2801   1166  -2278       C  
ATOM   1918  C   ASP C  60     -34.773 -18.095 -35.503  1.00127.51           C  
ANISOU 1918  C   ASP C  60    14960  20631  12856  -2752   1122  -2464       C  
ATOM   1919  O   ASP C  60     -33.896 -18.398 -36.312  1.00124.24           O  
ANISOU 1919  O   ASP C  60    14565  20219  12422  -2720   1082  -2437       O  
ATOM   1920  CB  ASP C  60     -33.919 -18.510 -33.167  1.00140.41           C  
ANISOU 1920  CB  ASP C  60    16827  21883  14641  -2989   1257  -2240       C  
ATOM   1921  CG  ASP C  60     -33.229 -17.889 -31.959  1.00158.94           C  
ANISOU 1921  CG  ASP C  60    19356  24054  16980  -3019   1286  -2033       C  
ATOM   1922  OD1 ASP C  60     -33.934 -17.483 -31.011  1.00164.86           O  
ANISOU 1922  OD1 ASP C  60    20118  24787  17735  -3044   1329  -2024       O  
ATOM   1923  OD2 ASP C  60     -31.982 -17.803 -31.957  1.00160.89           O  
ANISOU 1923  OD2 ASP C  60    19729  24190  17214  -3016   1266  -1886       O  
ATOM   1924  N   SER C  61     -36.072 -18.269 -35.736  1.00134.45           N  
ANISOU 1924  N   SER C  61    15671  21670  13744  -2741   1126  -2660       N  
ATOM   1925  CA  SER C  61     -36.567 -18.767 -37.013  1.00128.02           C  
ANISOU 1925  CA  SER C  61    14680  21056  12906  -2678   1074  -2862       C  
ATOM   1926  C   SER C  61     -36.636 -17.634 -38.017  1.00127.89           C  
ANISOU 1926  C   SER C  61    14649  21229  12713  -2454    973  -2829       C  
ATOM   1927  O   SER C  61     -36.815 -17.858 -39.213  1.00144.78           O  
ANISOU 1927  O   SER C  61    16667  23549  14793  -2358    913  -2958       O  
ATOM   1928  CB  SER C  61     -37.953 -19.387 -36.861  1.00124.52           C  
ANISOU 1928  CB  SER C  61    14049  20720  12543  -2756   1119  -3097       C  
ATOM   1929  OG  SER C  61     -38.909 -18.388 -36.542  1.00120.11           O  
ANISOU 1929  OG  SER C  61    13457  20278  11902  -2661   1103  -3105       O  
ATOM   1930  N   VAL C  62     -36.509 -16.410 -37.515  1.00116.72           N  
ANISOU 1930  N   VAL C  62    13361  19773  11213  -2365    958  -2656       N  
ATOM   1931  CA  VAL C  62     -36.593 -15.212 -38.338  1.00107.19           C  
ANISOU 1931  CA  VAL C  62    12167  18721   9840  -2147    873  -2595       C  
ATOM   1932  C   VAL C  62     -35.364 -14.343 -38.111  1.00103.64           C  
ANISOU 1932  C   VAL C  62    11925  18118   9335  -2102    859  -2334       C  
ATOM   1933  O   VAL C  62     -35.320 -13.174 -38.508  1.00 74.81           O  
ANISOU 1933  O   VAL C  62     8334  14532   5558  -1936    806  -2229       O  
ATOM   1934  CB  VAL C  62     -37.864 -14.403 -38.020  1.00 76.90           C  
ANISOU 1934  CB  VAL C  62     8265  15010   5944  -2056    863  -2662       C  
ATOM   1935  CG1 VAL C  62     -38.253 -13.550 -39.188  1.00104.66           C  
ANISOU 1935  CG1 VAL C  62    11720  18752   9296  -1823    771  -2689       C  
ATOM   1936  CG2 VAL C  62     -39.009 -15.337 -37.664  1.00 77.95           C  
ANISOU 1936  CG2 VAL C  62     8222  15213   6183  -2178    915  -2892       C  
ATOM   1937  N   LYS C  63     -34.365 -14.928 -37.459  1.00129.51           N  
ANISOU 1937  N   LYS C  63    15311  21188  12711  -2250    909  -2233       N  
ATOM   1938  CA  LYS C  63     -33.124 -14.226 -37.167  1.00154.58           C  
ANISOU 1938  CA  LYS C  63    18673  24208  15853  -2234    902  -1998       C  
ATOM   1939  C   LYS C  63     -32.361 -13.890 -38.446  1.00157.73           C  
ANISOU 1939  C   LYS C  63    19086  24700  16145  -2101    837  -1933       C  
ATOM   1940  O   LYS C  63     -31.767 -14.769 -39.072  1.00177.33           O  
ANISOU 1940  O   LYS C  63    21526  27195  18657  -2141    832  -1980       O  
ATOM   1941  CB  LYS C  63     -32.254 -15.067 -36.229  1.00175.78           C  
ANISOU 1941  CB  LYS C  63    21450  26673  18666  -2419    968  -1928       C  
ATOM   1942  CG  LYS C  63     -31.194 -14.271 -35.490  1.00181.84           C  
ANISOU 1942  CG  LYS C  63    22409  27263  19418  -2430    974  -1701       C  
ATOM   1943  CD  LYS C  63     -31.246 -14.564 -33.997  1.00180.05           C  
ANISOU 1943  CD  LYS C  63    22254  26864  19293  -2576   1047  -1664       C  
ATOM   1944  CE  LYS C  63     -30.160 -13.814 -33.243  1.00169.07           C  
ANISOU 1944  CE  LYS C  63    21045  25304  17889  -2589   1049  -1455       C  
ATOM   1945  NZ  LYS C  63     -28.796 -14.273 -33.620  1.00164.27           N  
ANISOU 1945  NZ  LYS C  63    20502  24615  17300  -2626   1039  -1364       N  
ATOM   1946  N   GLY C  64     -32.385 -12.619 -38.834  1.00125.54           N  
ANISOU 1946  N   GLY C  64    15069  20688  11944  -1938    790  -1823       N  
ATOM   1947  CA  GLY C  64     -31.632 -12.160 -39.988  1.00114.21           C  
ANISOU 1947  CA  GLY C  64    13664  19333  10398  -1804    738  -1730       C  
ATOM   1948  C   GLY C  64     -32.428 -11.978 -41.271  1.00 99.27           C  
ANISOU 1948  C   GLY C  64    11633  17704   8382  -1624    677  -1854       C  
ATOM   1949  O   GLY C  64     -31.869 -11.635 -42.311  1.00 74.44           O  
ANISOU 1949  O   GLY C  64     8502  14650   5131  -1500    636  -1783       O  
ATOM   1950  N   ARG C  65     -33.736 -12.181 -41.199  1.00102.96           N  
ANISOU 1950  N   ARG C  65    11963  18303   8855  -1604    671  -2037       N  
ATOM   1951  CA  ARG C  65     -34.596 -11.964 -42.359  1.00 86.48           C  
ANISOU 1951  CA  ARG C  65     9733  16484   6641  -1420    606  -2170       C  
ATOM   1952  C   ARG C  65     -35.459 -10.734 -42.127  1.00 87.57           C  
ANISOU 1952  C   ARG C  65     9897  16687   6689  -1274    584  -2129       C  
ATOM   1953  O   ARG C  65     -35.785 -10.010 -43.063  1.00 86.05           O  
ANISOU 1953  O   ARG C  65     9674  16671   6351  -1069    526  -2119       O  
ATOM   1954  CB  ARG C  65     -35.467 -13.195 -42.634  1.00 88.48           C  
ANISOU 1954  CB  ARG C  65     9780  16876   6964  -1493    608  -2445       C  
ATOM   1955  CG  ARG C  65     -34.684 -14.487 -42.817  1.00 89.77           C  
ANISOU 1955  CG  ARG C  65     9915  16963   7232  -1641    634  -2504       C  
ATOM   1956  CD  ARG C  65     -35.569 -15.599 -43.362  1.00 89.98           C  
ANISOU 1956  CD  ARG C  65     9725  17157   7307  -1677    623  -2790       C  
ATOM   1957  NE  ARG C  65     -36.507 -16.114 -42.365  1.00 89.92           N  
ANISOU 1957  NE  ARG C  65     9645  17091   7429  -1826    682  -2923       N  
ATOM   1958  CZ  ARG C  65     -37.779 -15.742 -42.259  1.00 86.38           C  
ANISOU 1958  CZ  ARG C  65     9084  16789   6947  -1763    670  -3051       C  
ATOM   1959  NH1 ARG C  65     -38.281 -14.828 -43.078  1.00 81.89           N  
ANISOU 1959  NH1 ARG C  65     8468  16433   6214  -1542    595  -3060       N  
ATOM   1960  NH2 ARG C  65     -38.550 -16.275 -41.322  1.00 79.87           N  
ANISOU 1960  NH2 ARG C  65     8195  15901   6249  -1915    735  -3164       N  
ATOM   1961  N   PHE C  66     -35.808 -10.489 -40.868  1.00 95.99           N  
ANISOU 1961  N   PHE C  66    11023  17610   7838  -1373    630  -2100       N  
ATOM   1962  CA  PHE C  66     -36.527  -9.275 -40.505  1.00 84.66           C  
ANISOU 1962  CA  PHE C  66     9635  16203   6328  -1243    613  -2045       C  
ATOM   1963  C   PHE C  66     -35.584  -8.308 -39.809  1.00 97.94           C  
ANISOU 1963  C   PHE C  66    11536  17660   8016  -1255    635  -1796       C  
ATOM   1964  O   PHE C  66     -34.631  -8.725 -39.146  1.00104.01           O  
ANISOU 1964  O   PHE C  66    12402  18233   8884  -1417    680  -1703       O  
ATOM   1965  CB  PHE C  66     -37.715  -9.576 -39.593  1.00 85.86           C  
ANISOU 1965  CB  PHE C  66     9689  16380   6556  -1324    647  -2204       C  
ATOM   1966  CG  PHE C  66     -38.820 -10.352 -40.252  1.00 98.88           C  
ANISOU 1966  CG  PHE C  66    11108  18268   8194  -1296    624  -2465       C  
ATOM   1967  CD1 PHE C  66     -38.747 -10.715 -41.590  1.00 98.41           C  
ANISOU 1967  CD1 PHE C  66    10943  18394   8053  -1191    567  -2553       C  
ATOM   1968  CD2 PHE C  66     -39.955 -10.699 -39.531  1.00107.70           C  
ANISOU 1968  CD2 PHE C  66    12107  19433   9379  -1373    658  -2630       C  
ATOM   1969  CE1 PHE C  66     -39.771 -11.430 -42.188  1.00103.32           C  
ANISOU 1969  CE1 PHE C  66    11345  19244   8669  -1168    542  -2810       C  
ATOM   1970  CE2 PHE C  66     -40.982 -11.415 -40.126  1.00109.30           C  
ANISOU 1970  CE2 PHE C  66    12088  19859   9583  -1358    639  -2884       C  
ATOM   1971  CZ  PHE C  66     -40.890 -11.777 -41.456  1.00102.26           C  
ANISOU 1971  CZ  PHE C  66    11091  19150   8614  -1255    577  -2979       C  
ATOM   1972  N   THR C  67     -35.848  -7.017 -39.963  1.00 94.20           N  
ANISOU 1972  N   THR C  67    11139  17216   7436  -1081    602  -1692       N  
ATOM   1973  CA  THR C  67     -35.052  -5.997 -39.295  1.00102.12           C  
ANISOU 1973  CA  THR C  67    12344  18007   8448  -1085    621  -1470       C  
ATOM   1974  C   THR C  67     -35.928  -4.838 -38.839  1.00 98.53           C  
ANISOU 1974  C   THR C  67    11932  17566   7938   -955    606  -1449       C  
ATOM   1975  O   THR C  67     -36.561  -4.166 -39.654  1.00 90.78           O  
ANISOU 1975  O   THR C  67    10910  16750   6833   -749    557  -1467       O  
ATOM   1976  CB  THR C  67     -33.936  -5.470 -40.207  1.00109.80           C  
ANISOU 1976  CB  THR C  67    13423  18952   9345   -997    600  -1290       C  
ATOM   1977  OG1 THR C  67     -33.044  -6.543 -40.532  1.00126.50           O  
ANISOU 1977  OG1 THR C  67    15507  21039  11517  -1125    617  -1305       O  
ATOM   1978  CG2 THR C  67     -33.157  -4.371 -39.513  1.00104.74           C  
ANISOU 1978  CG2 THR C  67    12984  18089   8723  -1007    622  -1073       C  
ATOM   1979  N   ILE C  68     -35.936  -4.590 -37.534  1.00 99.80           N  
ANISOU 1979  N   ILE C  68    12178  17555   8186  -1064    647  -1409       N  
ATOM   1980  CA  ILE C  68     -36.809  -3.579 -36.954  1.00 96.89           C  
ANISOU 1980  CA  ILE C  68    11843  17192   7779   -957    636  -1409       C  
ATOM   1981  C   ILE C  68     -36.025  -2.308 -36.631  1.00 89.22           C  
ANISOU 1981  C   ILE C  68    11078  16030   6789   -899    636  -1190       C  
ATOM   1982  O   ILE C  68     -34.837  -2.356 -36.303  1.00 74.60           O  
ANISOU 1982  O   ILE C  68     9346  13996   5003  -1018    663  -1055       O  
ATOM   1983  CB  ILE C  68     -37.511  -4.111 -35.675  1.00 89.30           C  
ANISOU 1983  CB  ILE C  68    10825  16188   6919  -1104    684  -1531       C  
ATOM   1984  CG1 ILE C  68     -38.666  -3.196 -35.255  1.00 84.91           C  
ANISOU 1984  CG1 ILE C  68    10252  15705   6306   -968    665  -1584       C  
ATOM   1985  CG2 ILE C  68     -36.519  -4.283 -34.535  1.00 88.21           C  
ANISOU 1985  CG2 ILE C  68    10823  15799   6893  -1292    738  -1414       C  
ATOM   1986  CD1 ILE C  68     -39.522  -3.766 -34.135  1.00 76.67           C  
ANISOU 1986  CD1 ILE C  68     9118  14669   5344  -1095    714  -1727       C  
ATOM   1987  N   SER C  69     -36.694  -1.169 -36.775  1.00 78.94           N  
ANISOU 1987  N   SER C  69     9814  14779   5400   -710    603  -1161       N  
ATOM   1988  CA  SER C  69     -36.115   0.136 -36.483  1.00 82.38           C  
ANISOU 1988  CA  SER C  69    10442  15037   5821   -637    602   -968       C  
ATOM   1989  C   SER C  69     -37.248   1.124 -36.258  1.00 93.03           C  
ANISOU 1989  C   SER C  69    11793  16453   7103   -460    574  -1010       C  
ATOM   1990  O   SER C  69     -38.409   0.804 -36.515  1.00104.55           O  
ANISOU 1990  O   SER C  69    13097  18120   8509   -378    549  -1179       O  
ATOM   1991  CB  SER C  69     -35.203   0.608 -37.619  1.00 97.77           C  
ANISOU 1991  CB  SER C  69    12475  16974   7699   -538    585   -806       C  
ATOM   1992  OG  SER C  69     -35.954   1.162 -38.688  1.00101.88           O  
ANISOU 1992  OG  SER C  69    12943  17686   8079   -300    537   -826       O  
ATOM   1993  N   ARG C  70     -36.922   2.315 -35.769  1.00 97.71           N  
ANISOU 1993  N   ARG C  70    12555  16872   7700   -403    577   -866       N  
ATOM   1994  CA  ARG C  70     -37.951   3.307 -35.481  1.00103.62           C  
ANISOU 1994  CA  ARG C  70    13320  17662   8389   -230    550   -900       C  
ATOM   1995  C   ARG C  70     -37.492   4.733 -35.748  1.00 90.78           C  
ANISOU 1995  C   ARG C  70    11879  15895   6718    -78    537   -708       C  
ATOM   1996  O   ARG C  70     -36.295   5.010 -35.822  1.00 90.82           O  
ANISOU 1996  O   ARG C  70    12018  15721   6767   -151    561   -544       O  
ATOM   1997  CB  ARG C  70     -38.403   3.187 -34.027  1.00112.23           C  
ANISOU 1997  CB  ARG C  70    14405  18669   9569   -354    580   -988       C  
ATOM   1998  CG  ARG C  70     -37.327   3.553 -33.025  1.00116.45           C  
ANISOU 1998  CG  ARG C  70    15110  18930  10207   -502    617   -852       C  
ATOM   1999  CD  ARG C  70     -37.938   4.106 -31.752  1.00129.15           C  
ANISOU 1999  CD  ARG C  70    16759  20462  11852   -507    628   -903       C  
ATOM   2000  NE  ARG C  70     -38.770   3.122 -31.068  1.00139.05           N  
ANISOU 2000  NE  ARG C  70    17859  21834  13140   -614    653  -1082       N  
ATOM   2001  CZ  ARG C  70     -39.497   3.385 -29.987  1.00142.72           C  
ANISOU 2001  CZ  ARG C  70    18315  22288  13626   -621    667  -1162       C  
ATOM   2002  NH1 ARG C  70     -40.225   2.431 -29.425  1.00141.65           N  
ANISOU 2002  NH1 ARG C  70    18034  22265  13523   -728    701  -1318       N  
ATOM   2003  NH2 ARG C  70     -39.496   4.606 -29.468  1.00142.73           N  
ANISOU 2003  NH2 ARG C  70    18451  22163  13616   -522    652  -1087       N  
ATOM   2004  N   ASP C  71     -38.456   5.640 -35.863  1.00 80.95           N  
ANISOU 2004  N   ASP C  71    10641  14727   5390    132    503   -734       N  
ATOM   2005  CA  ASP C  71     -38.152   7.057 -35.995  1.00 98.61           C  
ANISOU 2005  CA  ASP C  71    13062  16811   7594    284    496   -561       C  
ATOM   2006  C   ASP C  71     -39.001   7.829 -34.990  1.00122.53           C  
ANISOU 2006  C   ASP C  71    16129  19787  10638    355    487   -622       C  
ATOM   2007  O   ASP C  71     -40.138   8.204 -35.282  1.00122.62           O  
ANISOU 2007  O   ASP C  71    16068  19966  10555    551    448   -712       O  
ATOM   2008  CB  ASP C  71     -38.415   7.549 -37.422  1.00103.43           C  
ANISOU 2008  CB  ASP C  71    13665  17574   8059    530    459   -495       C  
ATOM   2009  CG  ASP C  71     -37.707   8.863 -37.729  1.00111.21           C  
ANISOU 2009  CG  ASP C  71    14863  18362   9029    644    472   -267       C  
ATOM   2010  OD1 ASP C  71     -37.283   9.554 -36.778  1.00112.24           O  
ANISOU 2010  OD1 ASP C  71    15137  18253   9255    569    497   -191       O  
ATOM   2011  OD2 ASP C  71     -37.585   9.208 -38.926  1.00107.40           O  
ANISOU 2011  OD2 ASP C  71    14404  17966   8439    812    458   -167       O  
ATOM   2012  N   ASN C  72     -38.446   8.040 -33.799  1.00133.80           N  
ANISOU 2012  N   ASN C  72    17662  20994  12181    197    520   -582       N  
ATOM   2013  CA  ASN C  72     -39.137   8.773 -32.739  1.00140.02           C  
ANISOU 2013  CA  ASN C  72    18496  21713  12992    247    514   -639       C  
ATOM   2014  C   ASN C  72     -39.486  10.189 -33.169  1.00136.60           C  
ANISOU 2014  C   ASN C  72    18186  21232  12486    499    483   -544       C  
ATOM   2015  O   ASN C  72     -40.519  10.731 -32.772  1.00134.77           O  
ANISOU 2015  O   ASN C  72    17930  21064  12211    639    458   -634       O  
ATOM   2016  CB  ASN C  72     -38.287   8.820 -31.465  1.00144.18           C  
ANISOU 2016  CB  ASN C  72    19134  21997  13652     40    554   -591       C  
ATOM   2017  CG  ASN C  72     -38.261   7.497 -30.724  1.00142.09           C  
ANISOU 2017  CG  ASN C  72    18746  21786  13456   -184    586   -714       C  
ATOM   2018  OD1 ASN C  72     -39.290   6.839 -30.571  1.00129.30           O  
ANISOU 2018  OD1 ASN C  72    16967  20355  11805   -177    582   -879       O  
ATOM   2019  ND2 ASN C  72     -37.084   7.109 -30.247  1.00147.36           N  
ANISOU 2019  ND2 ASN C  72    19487  22285  14219   -384    620   -633       N  
ATOM   2020  N   ALA C  73     -38.617  10.780 -33.982  1.00143.02           N  
ANISOU 2020  N   ALA C  73    19130  21931  13283    558    490   -359       N  
ATOM   2021  CA  ALA C  73     -38.844  12.118 -34.504  1.00148.52           C  
ANISOU 2021  CA  ALA C  73    19957  22562  13909    799    470   -241       C  
ATOM   2022  C   ALA C  73     -40.079  12.135 -35.396  1.00166.55           C  
ANISOU 2022  C   ALA C  73    22116  25125  16041   1048    421   -335       C  
ATOM   2023  O   ALA C  73     -40.845  13.099 -35.395  1.00179.08           O  
ANISOU 2023  O   ALA C  73    23755  26721  17565   1263    392   -335       O  
ATOM   2024  CB  ALA C  73     -37.623  12.606 -35.269  1.00139.81           C  
ANISOU 2024  CB  ALA C  73    19006  21295  12821    793    500    -19       C  
ATOM   2025  N   LYS C  74     -40.272  11.060 -36.152  1.00170.64           N  
ANISOU 2025  N   LYS C  74    22465  25873  16499   1023    408   -423       N  
ATOM   2026  CA  LYS C  74     -41.407  10.961 -37.058  1.00156.58           C  
ANISOU 2026  CA  LYS C  74    20540  24384  14568   1250    356   -531       C  
ATOM   2027  C   LYS C  74     -42.534  10.164 -36.404  1.00151.52           C  
ANISOU 2027  C   LYS C  74    19699  23939  13932   1198    338   -779       C  
ATOM   2028  O   LYS C  74     -43.595   9.965 -36.997  1.00150.24           O  
ANISOU 2028  O   LYS C  74    19385  24043  13658   1363    293   -914       O  
ATOM   2029  CB  LYS C  74     -40.979  10.322 -38.383  1.00143.97           C  
ANISOU 2029  CB  LYS C  74    18872  22940  12890   1278    350   -487       C  
ATOM   2030  CG  LYS C  74     -41.858  10.695 -39.571  1.00129.84           C  
ANISOU 2030  CG  LYS C  74    17013  21398  10921   1581    295   -509       C  
ATOM   2031  CD  LYS C  74     -41.031  10.881 -40.834  1.00124.56           C  
ANISOU 2031  CD  LYS C  74    16421  20732  10173   1670    304   -325       C  
ATOM   2032  CE  LYS C  74     -40.261   9.620 -41.179  1.00129.24           C  
ANISOU 2032  CE  LYS C  74    16913  21382  10810   1457    326   -359       C  
ATOM   2033  NZ  LYS C  74     -41.177   8.491 -41.495  1.00137.07           N  
ANISOU 2033  NZ  LYS C  74    17656  22680  11745   1458    284   -601       N  
ATOM   2034  N   ASN C  75     -42.288   9.719 -35.173  1.00143.97           N  
ANISOU 2034  N   ASN C  75    18744  22853  13106    967    376   -838       N  
ATOM   2035  CA  ASN C  75     -43.294   9.046 -34.354  1.00144.86           C  
ANISOU 2035  CA  ASN C  75    18690  23109  13242    894    375  -1055       C  
ATOM   2036  C   ASN C  75     -43.876   7.805 -35.028  1.00135.24           C  
ANISOU 2036  C   ASN C  75    17239  22172  11975    862    362  -1224       C  
ATOM   2037  O   ASN C  75     -45.092   7.617 -35.058  1.00141.80           O  
ANISOU 2037  O   ASN C  75    17909  23227  12742    964    333  -1401       O  
ATOM   2038  CB  ASN C  75     -44.422  10.024 -33.994  1.00157.01           C  
ANISOU 2038  CB  ASN C  75    20235  24707  14714   1112    340  -1121       C  
ATOM   2039  CG  ASN C  75     -45.238   9.567 -32.796  1.00160.90           C  
ANISOU 2039  CG  ASN C  75    20611  25263  15261   1003    358  -1306       C  
ATOM   2040  OD1 ASN C  75     -44.731   8.879 -31.909  1.00158.01           O  
ANISOU 2040  OD1 ASN C  75    20242  24787  15008    757    407  -1326       O  
ATOM   2041  ND2 ASN C  75     -46.509   9.950 -32.765  1.00164.77           N  
ANISOU 2041  ND2 ASN C  75    21004  25936  15666   1192    320  -1439       N  
ATOM   2042  N   THR C  76     -43.009   6.965 -35.581  1.00125.15           N  
ANISOU 2042  N   THR C  76    15939  20883  10730    721    381  -1178       N  
ATOM   2043  CA  THR C  76     -43.468   5.729 -36.205  1.00118.79           C  
ANISOU 2043  CA  THR C  76    14917  20322   9895    669    371  -1345       C  
ATOM   2044  C   THR C  76     -42.379   4.659 -36.218  1.00104.50           C  
ANISOU 2044  C   THR C  76    13104  18419   8183    421    414  -1307       C  
ATOM   2045  O   THR C  76     -41.184   4.965 -36.168  1.00 85.02           O  
ANISOU 2045  O   THR C  76    10801  15737   5767    343    439  -1125       O  
ATOM   2046  CB  THR C  76     -43.972   5.971 -37.645  1.00121.80           C  
ANISOU 2046  CB  THR C  76    15222  20939  10117    924    311  -1361       C  
ATOM   2047  OG1 THR C  76     -44.452   4.739 -38.199  1.00119.87           O  
ANISOU 2047  OG1 THR C  76    14754  20938   9853    864    298  -1549       O  
ATOM   2048  CG2 THR C  76     -42.864   6.534 -38.524  1.00112.73           C  
ANISOU 2048  CG2 THR C  76    14238  19669   8926    997    310  -1133       C  
ATOM   2049  N   ILE C  77     -42.806   3.402 -36.268  1.00105.86           N  
ANISOU 2049  N   ILE C  77    13085  18752   8386    296    424  -1486       N  
ATOM   2050  CA  ILE C  77     -41.886   2.274 -36.217  1.00113.29           C  
ANISOU 2050  CA  ILE C  77    14005  19614   9425     60    466  -1477       C  
ATOM   2051  C   ILE C  77     -42.051   1.359 -37.423  1.00128.64           C  
ANISOU 2051  C   ILE C  77    15784  21783  11310     89    438  -1585       C  
ATOM   2052  O   ILE C  77     -43.168   0.982 -37.784  1.00135.49           O  
ANISOU 2052  O   ILE C  77    16468  22892  12121    172    409  -1775       O  
ATOM   2053  CB  ILE C  77     -42.088   1.471 -34.925  1.00114.11           C  
ANISOU 2053  CB  ILE C  77    14051  19647   9657   -171    522  -1586       C  
ATOM   2054  CG1 ILE C  77     -41.868   2.385 -33.720  1.00144.62           C  
ANISOU 2054  CG1 ILE C  77    18081  23294  13573   -196    546  -1482       C  
ATOM   2055  CG2 ILE C  77     -41.144   0.284 -34.870  1.00102.03           C  
ANISOU 2055  CG2 ILE C  77    12505  18032   8228   -405    566  -1574       C  
ATOM   2056  CD1 ILE C  77     -42.070   1.717 -32.396  1.00159.34           C  
ANISOU 2056  CD1 ILE C  77    19905  25091  15548   -401    604  -1571       C  
ATOM   2057  N   TYR C  78     -40.930   0.995 -38.037  1.00118.15           N  
ANISOU 2057  N   TYR C  78    14515  20380   9996     19    447  -1473       N  
ATOM   2058  CA  TYR C  78     -40.958   0.178 -39.239  1.00111.28           C  
ANISOU 2058  CA  TYR C  78    13503  19713   9064     56    418  -1563       C  
ATOM   2059  C   TYR C  78     -40.488  -1.246 -38.967  1.00120.83           C  
ANISOU 2059  C   TYR C  78    14626  20889  10396   -197    461  -1654       C  
ATOM   2060  O   TYR C  78     -39.722  -1.494 -38.032  1.00123.46           O  
ANISOU 2060  O   TYR C  78    15059  21001  10849   -392    514  -1575       O  
ATOM   2061  CB  TYR C  78     -40.094   0.808 -40.332  1.00105.36           C  
ANISOU 2061  CB  TYR C  78    12870  18945   8218    198    394  -1375       C  
ATOM   2062  CG  TYR C  78     -40.175   2.317 -40.407  1.00118.69           C  
ANISOU 2062  CG  TYR C  78    14716  20561   9821    408    374  -1213       C  
ATOM   2063  CD1 TYR C  78     -41.232   2.946 -41.054  1.00121.88           C  
ANISOU 2063  CD1 TYR C  78    15053  21172  10083    669    318  -1276       C  
ATOM   2064  CD2 TYR C  78     -39.177   3.114 -39.858  1.00128.25           C  
ANISOU 2064  CD2 TYR C  78    16142  21495  11094    351    410  -1000       C  
ATOM   2065  CE1 TYR C  78     -41.306   4.325 -41.130  1.00119.47           C  
ANISOU 2065  CE1 TYR C  78    14902  20789   9704    869    303  -1122       C  
ATOM   2066  CE2 TYR C  78     -39.241   4.494 -39.935  1.00129.80           C  
ANISOU 2066  CE2 TYR C  78    16488  21607  11224    538    397   -853       C  
ATOM   2067  CZ  TYR C  78     -40.307   5.093 -40.572  1.00121.85           C  
ANISOU 2067  CZ  TYR C  78    15421  20797  10078    799    345   -910       C  
ATOM   2068  OH  TYR C  78     -40.373   6.464 -40.649  1.00116.16           O  
ANISOU 2068  OH  TYR C  78    14858  19981   9296    993    335   -759       O  
ATOM   2069  N   LEU C  79     -40.971  -2.182 -39.780  1.00123.96           N  
ANISOU 2069  N   LEU C  79    14832  21505  10759   -187    437  -1830       N  
ATOM   2070  CA  LEU C  79     -40.500  -3.562 -39.732  1.00108.48           C  
ANISOU 2070  CA  LEU C  79    12787  19522   8908   -406    473  -1919       C  
ATOM   2071  C   LEU C  79     -40.173  -4.072 -41.129  1.00103.90           C  
ANISOU 2071  C   LEU C  79    12123  19108   8248   -327    432  -1955       C  
ATOM   2072  O   LEU C  79     -41.068  -4.420 -41.900  1.00 90.68           O  
ANISOU 2072  O   LEU C  79    10269  17688   6497   -217    387  -2136       O  
ATOM   2073  CB  LEU C  79     -41.534  -4.472 -39.073  1.00100.02           C  
ANISOU 2073  CB  LEU C  79    11540  18541   7922   -534    502  -2150       C  
ATOM   2074  CG  LEU C  79     -41.162  -5.956 -39.101  1.00 90.25           C  
ANISOU 2074  CG  LEU C  79    10202  17290   6800   -750    541  -2262       C  
ATOM   2075  CD1 LEU C  79     -39.827  -6.184 -38.408  1.00 78.87           C  
ANISOU 2075  CD1 LEU C  79     8931  15570   5465   -933    595  -2086       C  
ATOM   2076  CD2 LEU C  79     -42.255  -6.807 -38.470  1.00 91.64           C  
ANISOU 2076  CD2 LEU C  79    10202  17555   7064   -874    579  -2489       C  
ATOM   2077  N   GLN C  80     -38.885  -4.108 -41.453  1.00119.55           N  
ANISOU 2077  N   GLN C  80    14227  20953  10243   -379    445  -1788       N  
ATOM   2078  CA  GLN C  80     -38.432  -4.611 -42.743  1.00114.08           C  
ANISOU 2078  CA  GLN C  80    13466  20403   9475   -314    412  -1807       C  
ATOM   2079  C   GLN C  80     -38.500  -6.134 -42.774  1.00104.82           C  
ANISOU 2079  C   GLN C  80    12133  19290   8403   -494    430  -2004       C  
ATOM   2080  O   GLN C  80     -38.039  -6.803 -41.849  1.00103.37           O  
ANISOU 2080  O   GLN C  80    11987  18922   8366   -716    488  -2000       O  
ATOM   2081  CB  GLN C  80     -37.010  -4.128 -43.036  1.00117.07           C  
ANISOU 2081  CB  GLN C  80    14028  20613   9838   -317    428  -1560       C  
ATOM   2082  CG  GLN C  80     -36.545  -4.394 -44.457  1.00127.97           C  
ANISOU 2082  CG  GLN C  80    15356  22157  11108   -202    391  -1549       C  
ATOM   2083  CD  GLN C  80     -37.435  -3.727 -45.491  1.00128.84           C  
ANISOU 2083  CD  GLN C  80    15391  22525  11039     77    327  -1594       C  
ATOM   2084  OE1 GLN C  80     -37.848  -2.578 -45.327  1.00133.01           O  
ANISOU 2084  OE1 GLN C  80    16008  23033  11497    227    315  -1497       O  
ATOM   2085  NE2 GLN C  80     -37.731  -4.445 -46.567  1.00125.17           N  
ANISOU 2085  NE2 GLN C  80    14761  22305  10493    155    283  -1747       N  
ATOM   2086  N   MET C  81     -39.090  -6.678 -43.834  1.00101.15           N  
ANISOU 2086  N   MET C  81    11489  19083   7859   -393    381  -2181       N  
ATOM   2087  CA  MET C  81     -39.258  -8.121 -43.972  1.00 95.23           C  
ANISOU 2087  CA  MET C  81    10572  18407   7204   -549    394  -2394       C  
ATOM   2088  C   MET C  81     -38.682  -8.629 -45.288  1.00 97.65           C  
ANISOU 2088  C   MET C  81    10816  18854   7432   -477    353  -2421       C  
ATOM   2089  O   MET C  81     -39.189  -8.303 -46.354  1.00118.18           O  
ANISOU 2089  O   MET C  81    13325  21697   9881   -265    288  -2486       O  
ATOM   2090  CB  MET C  81     -40.737  -8.494 -43.880  1.00 83.25           C  
ANISOU 2090  CB  MET C  81     8849  17091   5693   -528    376  -2654       C  
ATOM   2091  CG  MET C  81     -41.368  -8.221 -42.526  1.00 82.86           C  
ANISOU 2091  CG  MET C  81     8830  16917   5735   -629    426  -2663       C  
ATOM   2092  SD  MET C  81     -43.171  -8.301 -42.579  1.00 87.44           S  
ANISOU 2092  SD  MET C  81     9172  17777   6276   -537    395  -2944       S  
ATOM   2093  CE  MET C  81     -43.434 -10.005 -43.050  1.00 97.86           C  
ANISOU 2093  CE  MET C  81    10263  19218   7700   -705    408  -3220       C  
ATOM   2094  N   ASN C  82     -37.641  -9.451 -45.209  1.00 90.69           N  
ANISOU 2094  N   ASN C  82     9979  17829   6649   -646    389  -2379       N  
ATOM   2095  CA  ASN C  82     -36.981  -9.974 -46.402  1.00 86.65           C  
ANISOU 2095  CA  ASN C  82     9417  17434   6070   -589    356  -2398       C  
ATOM   2096  C   ASN C  82     -37.046 -11.494 -46.469  1.00 84.83           C  
ANISOU 2096  C   ASN C  82     9034  17233   5962   -761    371  -2619       C  
ATOM   2097  O   ASN C  82     -37.209 -12.155 -45.448  1.00107.84           O  
ANISOU 2097  O   ASN C  82    11939  19997   9037   -965    428  -2686       O  
ATOM   2098  CB  ASN C  82     -35.518  -9.520 -46.451  1.00 89.92           C  
ANISOU 2098  CB  ASN C  82    10029  17663   6473   -607    380  -2132       C  
ATOM   2099  CG  ASN C  82     -35.372  -8.010 -46.460  1.00 91.92           C  
ANISOU 2099  CG  ASN C  82    10440  17871   6613   -441    371  -1906       C  
ATOM   2100  OD1 ASN C  82     -36.298  -7.287 -46.828  1.00 97.09           O  
ANISOU 2100  OD1 ASN C  82    11048  18689   7152   -251    329  -1944       O  
ATOM   2101  ND2 ASN C  82     -34.208  -7.526 -46.037  1.00 79.49           N  
ANISOU 2101  ND2 ASN C  82     9053  16070   5077   -511    412  -1673       N  
ATOM   2102  N   SER C  83     -36.929 -12.032 -47.677  1.00 82.65           N  
ANISOU 2102  N   SER C  83     8643  17153   5608   -673    322  -2730       N  
ATOM   2103  CA  SER C  83     -36.899 -13.476 -47.908  1.00 86.53           C  
ANISOU 2103  CA  SER C  83     8991  17677   6209   -818    330  -2943       C  
ATOM   2104  C   SER C  83     -38.088 -14.181 -47.274  1.00 88.78           C  
ANISOU 2104  C   SER C  83     9119  17997   6616   -943    353  -3186       C  
ATOM   2105  O   SER C  83     -37.918 -15.098 -46.472  1.00 97.21           O  
ANISOU 2105  O   SER C  83    10187  18889   7861  -1168    417  -3243       O  
ATOM   2106  CB  SER C  83     -35.606 -14.076 -47.351  1.00 88.11           C  
ANISOU 2106  CB  SER C  83     9325  17613   6541  -1014    391  -2811       C  
ATOM   2107  OG  SER C  83     -34.465 -13.370 -47.807  1.00 85.69           O  
ANISOU 2107  OG  SER C  83     9169  17253   6134   -920    381  -2572       O  
ATOM   2108  N   LEU C  84     -39.290 -13.776 -47.656  1.00 84.91           N  
ANISOU 2108  N   LEU C  84     8492  17741   6030   -793    304  -3332       N  
ATOM   2109  CA  LEU C  84     -40.483 -14.309 -47.022  1.00 94.77           C  
ANISOU 2109  CA  LEU C  84     9588  19034   7387   -904    330  -3557       C  
ATOM   2110  C   LEU C  84     -40.662 -15.798 -47.290  1.00109.97           C  
ANISOU 2110  C   LEU C  84    11339  21004   9443  -1062    344  -3814       C  
ATOM   2111  O   LEU C  84     -40.029 -16.365 -48.178  1.00125.37           O  
ANISOU 2111  O   LEU C  84    13255  23015  11366  -1038    312  -3856       O  
ATOM   2112  CB  LEU C  84     -41.708 -13.527 -47.482  1.00 88.93           C  
ANISOU 2112  CB  LEU C  84     8726  18563   6499   -687    264  -3665       C  
ATOM   2113  CG  LEU C  84     -41.661 -12.108 -46.912  1.00107.83           C  
ANISOU 2113  CG  LEU C  84    11300  20861   8809   -570    269  -3422       C  
ATOM   2114  CD1 LEU C  84     -42.893 -11.310 -47.280  1.00106.72           C  
ANISOU 2114  CD1 LEU C  84    11049  20973   8526   -349    207  -3523       C  
ATOM   2115  CD2 LEU C  84     -41.473 -12.143 -45.399  1.00103.95           C  
ANISOU 2115  CD2 LEU C  84    10934  20079   8483   -787    359  -3317       C  
ATOM   2116  N   LYS C  85     -41.513 -16.429 -46.490  1.00103.76           N  
ANISOU 2116  N   LYS C  85    10446  20175   8803  -1230    398  -3984       N  
ATOM   2117  CA  LYS C  85     -41.713 -17.869 -46.548  1.00108.69           C  
ANISOU 2117  CA  LYS C  85    10918  20792   9588  -1416    432  -4223       C  
ATOM   2118  C   LYS C  85     -43.181 -18.168 -46.278  1.00115.98           C  
ANISOU 2118  C   LYS C  85    11634  21865  10569  -1461    444  -4483       C  
ATOM   2119  O   LYS C  85     -43.807 -17.479 -45.476  1.00130.48           O  
ANISOU 2119  O   LYS C  85    13502  23676  12399  -1454    471  -4426       O  
ATOM   2120  CB  LYS C  85     -40.811 -18.570 -45.523  1.00122.81           C  
ANISOU 2120  CB  LYS C  85    12854  22247  11562  -1663    530  -4096       C  
ATOM   2121  CG  LYS C  85     -40.728 -20.084 -45.652  1.00128.77           C  
ANISOU 2121  CG  LYS C  85    13494  22947  12486  -1852    569  -4300       C  
ATOM   2122  CD  LYS C  85     -39.734 -20.682 -44.661  1.00120.20           C  
ANISOU 2122  CD  LYS C  85    12580  21529  11563  -2065    661  -4140       C  
ATOM   2123  CE  LYS C  85     -38.297 -20.410 -45.066  1.00100.98           C  
ANISOU 2123  CE  LYS C  85    10317  18997   9054  -1997    632  -3919       C  
ATOM   2124  NZ  LYS C  85     -37.326 -21.123 -44.188  1.00 91.89           N  
ANISOU 2124  NZ  LYS C  85     9310  17544   8059  -2197    715  -3794       N  
ATOM   2125  N   PRO C  86     -43.746 -19.176 -46.964  1.00108.03           N  
ANISOU 2125  N   PRO C  86    10406  21023   9617  -1504    422  -4778       N  
ATOM   2126  CA  PRO C  86     -45.134 -19.613 -46.759  1.00123.03           C  
ANISOU 2126  CA  PRO C  86    12081  23072  11593  -1573    439  -5059       C  
ATOM   2127  C   PRO C  86     -45.522 -19.813 -45.293  1.00132.79           C  
ANISOU 2127  C   PRO C  86    13365  24088  13001  -1794    554  -5020       C  
ATOM   2128  O   PRO C  86     -46.706 -19.825 -44.972  1.00126.90           O  
ANISOU 2128  O   PRO C  86    12463  23466  12288  -1822    573  -5195       O  
ATOM   2129  CB  PRO C  86     -45.185 -20.941 -47.505  1.00107.74           C  
ANISOU 2129  CB  PRO C  86     9965  21215   9758  -1672    429  -5331       C  
ATOM   2130  CG  PRO C  86     -44.245 -20.741 -48.630  1.00112.26           C  
ANISOU 2130  CG  PRO C  86    10598  21874  10182  -1498    345  -5244       C  
ATOM   2131  CD  PRO C  86     -43.130 -19.865 -48.111  1.00105.81           C  
ANISOU 2131  CD  PRO C  86    10062  20837   9305  -1459    368  -4875       C  
ATOM   2132  N   GLN C  87     -44.533 -19.975 -44.422  1.00135.00           N  
ANISOU 2132  N   GLN C  87    13854  24057  13384  -1944    632  -4796       N  
ATOM   2133  CA  GLN C  87     -44.775 -20.044 -42.990  1.00136.65           C  
ANISOU 2133  CA  GLN C  87    14140  24050  13729  -2130    742  -4714       C  
ATOM   2134  C   GLN C  87     -45.133 -18.669 -42.438  1.00132.81           C  
ANISOU 2134  C   GLN C  87    13750  23595  13118  -1990    725  -4549       C  
ATOM   2135  O   GLN C  87     -45.934 -18.547 -41.512  1.00150.29           O  
ANISOU 2135  O   GLN C  87    15927  25782  15393  -2073    786  -4585       O  
ATOM   2136  CB  GLN C  87     -43.544 -20.593 -42.273  1.00146.96           C  
ANISOU 2136  CB  GLN C  87    15646  25029  15163  -2307    820  -4517       C  
ATOM   2137  CG  GLN C  87     -43.015 -21.888 -42.859  1.00167.22           C  
ANISOU 2137  CG  GLN C  87    18149  27542  17844  -2424    830  -4650       C  
ATOM   2138  CD  GLN C  87     -41.724 -22.330 -42.208  1.00184.20           C  
ANISOU 2138  CD  GLN C  87    20509  29383  20096  -2563    896  -4437       C  
ATOM   2139  OE1 GLN C  87     -41.046 -21.540 -41.551  1.00188.66           O  
ANISOU 2139  OE1 GLN C  87    21274  29801  20608  -2532    909  -4174       O  
ATOM   2140  NE2 GLN C  87     -41.371 -23.598 -42.390  1.00190.18           N  
ANISOU 2140  NE2 GLN C  87    21220  30040  21000  -2713    935  -4556       N  
ATOM   2141  N   ASP C  88     -44.533 -17.635 -43.018  1.00121.18           N  
ANISOU 2141  N   ASP C  88    12399  22175  11467  -1776    644  -4368       N  
ATOM   2142  CA  ASP C  88     -44.670 -16.274 -42.507  1.00103.96           C  
ANISOU 2142  CA  ASP C  88    10348  19982   9170  -1637    628  -4177       C  
ATOM   2143  C   ASP C  88     -46.005 -15.614 -42.836  1.00101.97           C  
ANISOU 2143  C   ASP C  88     9932  20011   8802  -1463    571  -4335       C  
ATOM   2144  O   ASP C  88     -46.251 -14.486 -42.414  1.00108.49           O  
ANISOU 2144  O   ASP C  88    10850  20839   9533  -1338    556  -4201       O  
ATOM   2145  CB  ASP C  88     -43.532 -15.404 -43.036  1.00103.75           C  
ANISOU 2145  CB  ASP C  88    10515  19901   9005  -1474    569  -3924       C  
ATOM   2146  CG  ASP C  88     -42.171 -15.963 -42.692  1.00119.17           C  
ANISOU 2146  CG  ASP C  88    12633  21585  11059  -1630    621  -3757       C  
ATOM   2147  OD1 ASP C  88     -42.098 -17.157 -42.331  1.00122.72           O  
ANISOU 2147  OD1 ASP C  88    13027  21927  11675  -1839    686  -3868       O  
ATOM   2148  OD2 ASP C  88     -41.179 -15.212 -42.783  1.00118.57           O  
ANISOU 2148  OD2 ASP C  88    12743  21407  10902  -1543    598  -3518       O  
ATOM   2149  N   THR C  89     -46.859 -16.300 -43.586  1.00 98.72           N  
ANISOU 2149  N   THR C  89     9275  19836   8397  -1451    536  -4625       N  
ATOM   2150  CA  THR C  89     -48.187 -15.770 -43.870  1.00107.27           C  
ANISOU 2150  CA  THR C  89    10178  21202   9378  -1295    484  -4803       C  
ATOM   2151  C   THR C  89     -48.992 -15.614 -42.568  1.00114.81           C  
ANISOU 2151  C   THR C  89    11119  22074  10427  -1419    568  -4818       C  
ATOM   2152  O   THR C  89     -49.242 -16.582 -41.846  1.00113.69           O  
ANISOU 2152  O   THR C  89    10910  21817  10470  -1664    664  -4925       O  
ATOM   2153  CB  THR C  89     -48.952 -16.657 -44.897  1.00108.57           C  
ANISOU 2153  CB  THR C  89    10061  21643   9549  -1280    434  -5142       C  
ATOM   2154  OG1 THR C  89     -50.236 -16.082 -45.164  1.00116.23           O  
ANISOU 2154  OG1 THR C  89    10853  22902  10406  -1113    377  -5313       O  
ATOM   2155  CG2 THR C  89     -49.141 -18.078 -44.389  1.00110.16           C  
ANISOU 2155  CG2 THR C  89    10148  21723   9985  -1579    530  -5327       C  
ATOM   2156  N   ALA C  90     -49.358 -14.373 -42.257  1.00114.60           N  
ANISOU 2156  N   ALA C  90    11169  22099  10274  -1247    536  -4696       N  
ATOM   2157  CA  ALA C  90     -49.973 -14.052 -40.972  1.00118.93           C  
ANISOU 2157  CA  ALA C  90    11744  22553  10891  -1341    613  -4665       C  
ATOM   2158  C   ALA C  90     -50.519 -12.629 -40.929  1.00122.11           C  
ANISOU 2158  C   ALA C  90    12192  23081  11121  -1091    551  -4579       C  
ATOM   2159  O   ALA C  90     -50.197 -11.801 -41.782  1.00131.87           O  
ANISOU 2159  O   ALA C  90    13498  24415  12190   -854    458  -4478       O  
ATOM   2160  CB  ALA C  90     -48.972 -14.251 -39.844  1.00117.65           C  
ANISOU 2160  CB  ALA C  90    11805  22038  10858  -1542    710  -4435       C  
ATOM   2161  N   VAL C  91     -51.362 -12.358 -39.939  1.00113.90           N  
ANISOU 2161  N   VAL C  91    11113  22042  10124  -1142    605  -4621       N  
ATOM   2162  CA  VAL C  91     -51.776 -10.994 -39.647  1.00110.03           C  
ANISOU 2162  CA  VAL C  91    10704  21608   9494   -931    562  -4510       C  
ATOM   2163  C   VAL C  91     -50.815 -10.397 -38.628  1.00114.46           C  
ANISOU 2163  C   VAL C  91    11545  21854  10091   -996    615  -4213       C  
ATOM   2164  O   VAL C  91     -50.615 -10.966 -37.559  1.00111.39           O  
ANISOU 2164  O   VAL C  91    11205  21266   9851  -1227    717  -4177       O  
ATOM   2165  CB  VAL C  91     -53.203 -10.926 -39.095  1.00105.98           C  
ANISOU 2165  CB  VAL C  91    10000  21273   8993   -934    588  -4712       C  
ATOM   2166  CG1 VAL C  91     -53.653  -9.476 -38.990  1.00109.77           C  
ANISOU 2166  CG1 VAL C  91    10556  21845   9308   -671    524  -4613       C  
ATOM   2167  CG2 VAL C  91     -54.148 -11.707 -39.977  1.00112.56           C  
ANISOU 2167  CG2 VAL C  91    10536  22404   9827   -923    550  -5034       C  
ATOM   2168  N   TYR C  92     -50.227  -9.253 -38.955  1.00116.68           N  
ANISOU 2168  N   TYR C  92    12006  22091  10234   -790    549  -4003       N  
ATOM   2169  CA  TYR C  92     -49.152  -8.697 -38.143  1.00116.30           C  
ANISOU 2169  CA  TYR C  92    12227  21743  10220   -848    590  -3722       C  
ATOM   2170  C   TYR C  92     -49.609  -7.532 -37.271  1.00119.53           C  
ANISOU 2170  C   TYR C  92    12733  22110  10574   -743    594  -3625       C  
ATOM   2171  O   TYR C  92     -49.898  -6.443 -37.771  1.00124.16           O  
ANISOU 2171  O   TYR C  92    13355  22812  11010   -491    517  -3575       O  
ATOM   2172  CB  TYR C  92     -47.993  -8.255 -39.036  1.00114.21           C  
ANISOU 2172  CB  TYR C  92    12120  21409   9865   -725    528  -3532       C  
ATOM   2173  CG  TYR C  92     -47.103  -9.393 -39.476  1.00108.92           C  
ANISOU 2173  CG  TYR C  92    11443  20654   9288   -890    552  -3543       C  
ATOM   2174  CD1 TYR C  92     -47.527 -10.311 -40.428  1.00 93.60           C  
ANISOU 2174  CD1 TYR C  92     9293  18920   7350   -896    521  -3769       C  
ATOM   2175  CD2 TYR C  92     -45.835  -9.550 -38.933  1.00112.46           C  
ANISOU 2175  CD2 TYR C  92    12090  20818   9822  -1035    603  -3336       C  
ATOM   2176  CE1 TYR C  92     -46.714 -11.354 -40.824  1.00 87.31           C  
ANISOU 2176  CE1 TYR C  92     8491  18040   6642  -1042    542  -3786       C  
ATOM   2177  CE2 TYR C  92     -45.017 -10.586 -39.323  1.00103.49           C  
ANISOU 2177  CE2 TYR C  92    10949  19604   8769  -1177    624  -3347       C  
ATOM   2178  CZ  TYR C  92     -45.458 -11.485 -40.268  1.00 91.44           C  
ANISOU 2178  CZ  TYR C  92     9220  18278   7247  -1179    594  -3571       C  
ATOM   2179  OH  TYR C  92     -44.638 -12.518 -40.653  1.00 95.30           O  
ANISOU 2179  OH  TYR C  92     9706  18683   7821  -1315    613  -3587       O  
ATOM   2180  N   TYR C  93     -49.665  -7.770 -35.964  1.00115.20           N  
ANISOU 2180  N   TYR C  93    12232  21395  10145   -931    686  -3596       N  
ATOM   2181  CA  TYR C  93     -50.070  -6.753 -35.000  1.00 99.51           C  
ANISOU 2181  CA  TYR C  93    10336  19352   8120   -856    699  -3513       C  
ATOM   2182  C   TYR C  93     -48.883  -5.913 -34.529  1.00 91.23           C  
ANISOU 2182  C   TYR C  93     9569  18035   7059   -834    699  -3228       C  
ATOM   2183  O   TYR C  93     -47.731  -6.348 -34.592  1.00 84.55           O  
ANISOU 2183  O   TYR C  93     8842  17007   6277   -954    720  -3099       O  
ATOM   2184  CB  TYR C  93     -50.740  -7.403 -33.785  1.00 98.59           C  
ANISOU 2184  CB  TYR C  93    10129  19201   8130  -1065    803  -3623       C  
ATOM   2185  CG  TYR C  93     -51.784  -8.451 -34.108  1.00 96.42           C  
ANISOU 2185  CG  TYR C  93     9576  19145   7914  -1157    830  -3905       C  
ATOM   2186  CD1 TYR C  93     -53.071  -8.089 -34.485  1.00 91.48           C  
ANISOU 2186  CD1 TYR C  93     8756  18803   7198   -999    782  -4099       C  
ATOM   2187  CD2 TYR C  93     -51.476  -9.803 -34.046  1.00109.23           C  
ANISOU 2187  CD2 TYR C  93    11129  20689   9685  -1402    903  -3981       C  
ATOM   2188  CE1 TYR C  93     -54.025  -9.048 -34.777  1.00 95.11           C  
ANISOU 2188  CE1 TYR C  93     8951  19468   7718  -1093    808  -4370       C  
ATOM   2189  CE2 TYR C  93     -52.420 -10.767 -34.339  1.00110.63           C  
ANISOU 2189  CE2 TYR C  93    11051  21053   9930  -1499    933  -4245       C  
ATOM   2190  CZ  TYR C  93     -53.691 -10.386 -34.704  1.00102.09           C  
ANISOU 2190  CZ  TYR C  93     9771  20257   8761  -1349    885  -4443       C  
ATOM   2191  OH  TYR C  93     -54.624 -11.351 -34.995  1.00 95.75           O  
ANISOU 2191  OH  TYR C  93     8704  19644   8034  -1456    916  -4718       O  
ATOM   2192  N   CYS C  94     -49.181  -4.715 -34.042  1.00 87.64           N  
ANISOU 2192  N   CYS C  94     9212  17559   6527   -683    675  -3142       N  
ATOM   2193  CA  CYS C  94     -48.171  -3.836 -33.473  1.00110.94           C  
ANISOU 2193  CA  CYS C  94    12421  20256   9475   -665    678  -2892       C  
ATOM   2194  C   CYS C  94     -48.557  -3.535 -32.020  1.00132.17           C  
ANISOU 2194  C   CYS C  94    15158  22841  12220   -748    742  -2880       C  
ATOM   2195  O   CYS C  94     -49.722  -3.250 -31.731  1.00134.72           O  
ANISOU 2195  O   CYS C  94    15359  23326  12502   -666    739  -3018       O  
ATOM   2196  CB  CYS C  94     -48.048  -2.556 -34.302  1.00120.29           C  
ANISOU 2196  CB  CYS C  94    13708  21488  10510   -386    586  -2778       C  
ATOM   2197  SG  CYS C  94     -46.797  -1.374 -33.755  1.00130.12           S  
ANISOU 2197  SG  CYS C  94    15266  22422  11751   -349    585  -2477       S  
ATOM   2198  N   ALA C  95     -47.590  -3.607 -31.108  1.00137.12           N  
ANISOU 2198  N   ALA C  95    15956  23209  12935   -905    798  -2722       N  
ATOM   2199  CA  ALA C  95     -47.895  -3.505 -29.680  1.00133.72           C  
ANISOU 2199  CA  ALA C  95    15562  22682  12564  -1010    868  -2717       C  
ATOM   2200  C   ALA C  95     -46.974  -2.539 -28.932  1.00129.15           C  
ANISOU 2200  C   ALA C  95    15228  21861  11982   -987    865  -2502       C  
ATOM   2201  O   ALA C  95     -45.800  -2.394 -29.273  1.00119.35           O  
ANISOU 2201  O   ALA C  95    14136  20461  10751  -1003    844  -2342       O  
ATOM   2202  CB  ALA C  95     -47.832  -4.884 -29.041  1.00132.62           C  
ANISOU 2202  CB  ALA C  95    15340  22489  12560  -1279    968  -2790       C  
ATOM   2203  N   ALA C  96     -47.519  -1.893 -27.900  1.00124.10           N  
ANISOU 2203  N   ALA C  96    14622  21200  11330   -954    886  -2509       N  
ATOM   2204  CA  ALA C  96     -46.757  -0.969 -27.062  1.00111.01           C  
ANISOU 2204  CA  ALA C  96    13182  19320   9675   -937    885  -2334       C  
ATOM   2205  C   ALA C  96     -46.734  -1.408 -25.597  1.00107.79           C  
ANISOU 2205  C   ALA C  96    12799  18803   9352  -1122    975  -2334       C  
ATOM   2206  O   ALA C  96     -47.784  -1.597 -24.981  1.00116.66           O  
ANISOU 2206  O   ALA C  96    13797  20053  10476  -1140   1018  -2468       O  
ATOM   2207  CB  ALA C  96     -47.334   0.436 -27.181  1.00 95.83           C  
ANISOU 2207  CB  ALA C  96    11311  17455   7645   -686    817  -2322       C  
ATOM   2208  N   ARG C  97     -45.540  -1.604 -25.048  1.00115.85           N  
ANISOU 2208  N   ARG C  97    13975  19601  10441  -1259   1006  -2185       N  
ATOM   2209  CA  ARG C  97     -45.404  -2.045 -23.660  1.00120.37           C  
ANISOU 2209  CA  ARG C  97    14585  20065  11085  -1430   1090  -2168       C  
ATOM   2210  C   ARG C  97     -45.355  -0.895 -22.676  1.00126.07           C  
ANISOU 2210  C   ARG C  97    15445  20685  11770  -1345   1077  -2095       C  
ATOM   2211  O   ARG C  97     -44.616   0.067 -22.853  1.00133.62           O  
ANISOU 2211  O   ARG C  97    16561  21511  12697  -1245   1018  -1968       O  
ATOM   2212  CB  ARG C  97     -44.172  -2.929 -23.473  1.00108.97           C  
ANISOU 2212  CB  ARG C  97    13227  18444   9731  -1623   1134  -2058       C  
ATOM   2213  CG  ARG C  97     -42.933  -2.190 -23.001  1.00 94.20           C  
ANISOU 2213  CG  ARG C  97    11576  16349   7865  -1620   1108  -1873       C  
ATOM   2214  CD  ARG C  97     -42.386  -2.761 -21.706  1.00 79.05           C  
ANISOU 2214  CD  ARG C  97     9729  14290   6018  -1800   1186  -1816       C  
ATOM   2215  NE  ARG C  97     -41.749  -4.062 -21.870  1.00 82.45           N  
ANISOU 2215  NE  ARG C  97    10130  14667   6530  -1978   1237  -1797       N  
ATOM   2216  CZ  ARG C  97     -40.474  -4.303 -21.597  1.00 76.53           C  
ANISOU 2216  CZ  ARG C  97     9513  13738   5826  -2075   1244  -1663       C  
ATOM   2217  NH1 ARG C  97     -39.969  -5.515 -21.757  1.00 72.95           N  
ANISOU 2217  NH1 ARG C  97     9028  13245   5446  -2226   1292  -1656       N  
ATOM   2218  NH2 ARG C  97     -39.701  -3.328 -21.160  1.00 72.92           N  
ANISOU 2218  NH2 ARG C  97     9219  13143   5345  -2019   1204  -1541       N  
ATOM   2219  N   ASP C  98     -46.157  -1.013 -21.631  1.00118.10           N  
ANISOU 2219  N   ASP C  98    14369  19738  10765  -1388   1137  -2182       N  
ATOM   2220  CA  ASP C  98     -46.228  -0.002 -20.587  1.00131.54           C  
ANISOU 2220  CA  ASP C  98    16183  21363  12432  -1313   1130  -2139       C  
ATOM   2221  C   ASP C  98     -44.945  -0.006 -19.766  1.00133.43           C  
ANISOU 2221  C   ASP C  98    16604  21367  12726  -1434   1153  -1985       C  
ATOM   2222  O   ASP C  98     -44.279  -1.035 -19.646  1.00137.67           O  
ANISOU 2222  O   ASP C  98    17144  21831  13334  -1610   1206  -1941       O  
ATOM   2223  CB  ASP C  98     -47.443  -0.238 -19.690  1.00134.30           C  
ANISOU 2223  CB  ASP C  98    16396  21862  12769  -1336   1197  -2280       C  
ATOM   2224  CG  ASP C  98     -47.846   1.003 -18.921  1.00131.32           C  
ANISOU 2224  CG  ASP C  98    16096  21474  12324  -1185   1166  -2281       C  
ATOM   2225  OD1 ASP C  98     -46.984   1.880 -18.704  1.00127.04           O  
ANISOU 2225  OD1 ASP C  98    15740  20756  11775  -1125   1117  -2154       O  
ATOM   2226  OD2 ASP C  98     -49.031   1.106 -18.541  1.00130.97           O  
ANISOU 2226  OD2 ASP C  98    15923  21602  12239  -1126   1191  -2416       O  
ATOM   2227  N   ILE C  99     -44.590   1.157 -19.226  1.00132.15           N  
ANISOU 2227  N   ILE C  99    16592  21088  12531  -1332   1110  -1908       N  
ATOM   2228  CA  ILE C  99     -43.358   1.304 -18.461  1.00122.99           C  
ANISOU 2228  CA  ILE C  99    15604  19711  11414  -1427   1118  -1770       C  
ATOM   2229  C   ILE C  99     -43.353   0.417 -17.215  1.00113.36           C  
ANISOU 2229  C   ILE C  99    14359  18474  10237  -1602   1213  -1787       C  
ATOM   2230  O   ILE C  99     -42.379  -0.294 -16.962  1.00102.99           O  
ANISOU 2230  O   ILE C  99    13109  17041   8982  -1750   1247  -1700       O  
ATOM   2231  CB  ILE C  99     -43.137   2.776 -18.037  1.00118.84           C  
ANISOU 2231  CB  ILE C  99    15229  19076  10849  -1279   1056  -1714       C  
ATOM   2232  CG1 ILE C  99     -43.314   3.718 -19.233  1.00106.10           C  
ANISOU 2232  CG1 ILE C  99    13640  17489   9186  -1084    972  -1698       C  
ATOM   2233  CG2 ILE C  99     -41.761   2.959 -17.416  1.00116.44           C  
ANISOU 2233  CG2 ILE C  99    15099  18550  10595  -1374   1053  -1577       C  
ATOM   2234  CD1 ILE C  99     -43.232   5.191 -18.864  1.00103.89           C  
ANISOU 2234  CD1 ILE C  99    13502  17100   8871   -926    915  -1655       C  
ATOM   2235  N   GLU C 100     -44.448   0.445 -16.456  1.00114.49           N  
ANISOU 2235  N   GLU C 100    14408  18747  10347  -1578   1258  -1898       N  
ATOM   2236  CA  GLU C 100     -44.552  -0.339 -15.225  1.00118.94           C  
ANISOU 2236  CA  GLU C 100    14945  19309  10937  -1729   1357  -1911       C  
ATOM   2237  C   GLU C 100     -44.632  -1.835 -15.489  1.00107.40           C  
ANISOU 2237  C   GLU C 100    13365  17898   9542  -1905   1440  -1941       C  
ATOM   2238  O   GLU C 100     -43.754  -2.594 -15.085  1.00113.71           O  
ANISOU 2238  O   GLU C 100    14230  18576  10397  -2053   1487  -1852       O  
ATOM   2239  CB  GLU C 100     -45.765   0.090 -14.396  1.00134.76           C  
ANISOU 2239  CB  GLU C 100    16867  21455  12882  -1651   1390  -2027       C  
ATOM   2240  CG  GLU C 100     -45.618   1.431 -13.701  1.00143.69           C  
ANISOU 2240  CG  GLU C 100    18131  22509  13957  -1512   1332  -1997       C  
ATOM   2241  CD  GLU C 100     -46.663   1.633 -12.618  1.00148.56           C  
ANISOU 2241  CD  GLU C 100    18672  23253  14520  -1474   1385  -2100       C  
ATOM   2242  OE1 GLU C 100     -47.573   0.785 -12.499  1.00148.22           O  
ANISOU 2242  OE1 GLU C 100    18465  23370  14482  -1549   1466  -2197       O  
ATOM   2243  OE2 GLU C 100     -46.573   2.638 -11.881  1.00150.91           O  
ANISOU 2243  OE2 GLU C 100    19072  23492  14774  -1373   1348  -2089       O  
ATOM   2244  N   THR C 101     -45.702  -2.262 -16.149  1.00109.96           N  
ANISOU 2244  N   THR C 101    13511  18405   9863  -1887   1458  -2074       N  
ATOM   2245  CA  THR C 101     -45.877  -3.674 -16.445  1.00114.78           C  
ANISOU 2245  CA  THR C 101    13996  19067  10548  -2054   1538  -2124       C  
ATOM   2246  C   THR C 101     -45.611  -3.964 -17.913  1.00133.76           C  
ANISOU 2246  C   THR C 101    16352  21495  12973  -2031   1478  -2138       C  
ATOM   2247  O   THR C 101     -46.213  -3.366 -18.810  1.00134.98           O  
ANISOU 2247  O   THR C 101    16436  21775  13074  -1880   1407  -2214       O  
ATOM   2248  CB  THR C 101     -47.289  -4.158 -16.092  1.00 99.43           C  
ANISOU 2248  CB  THR C 101    11859  17320   8601  -2087   1620  -2284       C  
ATOM   2249  OG1 THR C 101     -48.259  -3.282 -16.680  1.00 89.42           O  
ANISOU 2249  OG1 THR C 101    10500  16218   7258  -1901   1550  -2397       O  
ATOM   2250  CG2 THR C 101     -47.475  -4.176 -14.587  1.00115.16           C  
ANISOU 2250  CG2 THR C 101    13888  19287  10580  -2151   1706  -2261       C  
ATOM   2251  N   ALA C 102     -44.702  -4.900 -18.146  1.00126.58           N  
ANISOU 2251  N   ALA C 102    15483  20473  12139  -2175   1507  -2064       N  
ATOM   2252  CA  ALA C 102     -44.302  -5.245 -19.493  1.00111.91           C  
ANISOU 2252  CA  ALA C 102    13592  18626  10303  -2163   1454  -2066       C  
ATOM   2253  C   ALA C 102     -45.253  -6.285 -20.049  1.00111.50           C  
ANISOU 2253  C   ALA C 102    13331  18738  10295  -2239   1506  -2226       C  
ATOM   2254  O   ALA C 102     -44.877  -7.434 -20.230  1.00132.48           O  
ANISOU 2254  O   ALA C 102    15954  21346  13035  -2392   1561  -2226       O  
ATOM   2255  CB  ALA C 102     -42.879  -5.768 -19.500  1.00104.54           C  
ANISOU 2255  CB  ALA C 102    12792  17500   9429  -2277   1458  -1922       C  
ATOM   2256  N   GLU C 103     -46.486  -5.889 -20.332  1.00111.36           N  
ANISOU 2256  N   GLU C 103    13171  18917  10225  -2129   1489  -2370       N  
ATOM   2257  CA  GLU C 103     -47.473  -6.859 -20.778  1.00112.84           C  
ANISOU 2257  CA  GLU C 103    13142  19274  10458  -2208   1543  -2544       C  
ATOM   2258  C   GLU C 103     -48.021  -6.505 -22.159  1.00130.07           C  
ANISOU 2258  C   GLU C 103    15207  21632  12582  -2051   1450  -2656       C  
ATOM   2259  O   GLU C 103     -48.829  -7.249 -22.724  1.00125.23           O  
ANISOU 2259  O   GLU C 103    14401  21180  12001  -2096   1475  -2819       O  
ATOM   2260  CB  GLU C 103     -48.614  -6.952 -19.762  1.00 81.06           C  
ANISOU 2260  CB  GLU C 103     9006  15361   6430  -2249   1631  -2649       C  
ATOM   2261  N   TYR C 104     -47.545  -5.390 -22.707  1.00107.95           N  
ANISOU 2261  N   TYR C 104    12524  18796   9697  -1870   1344  -2566       N  
ATOM   2262  CA  TYR C 104     -48.062  -4.874 -23.975  1.00103.26           C  
ANISOU 2262  CA  TYR C 104    11838  18372   9022  -1684   1249  -2652       C  
ATOM   2263  C   TYR C 104     -49.544  -4.586 -23.949  1.00 94.14           C  
ANISOU 2263  C   TYR C 104    10504  17453   7811  -1580   1249  -2833       C  
ATOM   2264  O   TYR C 104     -50.314  -5.164 -24.714  1.00 86.77           O  
ANISOU 2264  O   TYR C 104     9378  16710   6882  -1578   1245  -2997       O  
ATOM   2265  CB  TYR C 104     -47.696  -5.797 -25.137  1.00108.58           C  
ANISOU 2265  CB  TYR C 104    12433  19081   9739  -1746   1233  -2693       C  
ATOM   2266  CG  TYR C 104     -46.225  -5.806 -25.490  1.00 96.49           C  
ANISOU 2266  CG  TYR C 104    11079  17351   8230  -1779   1200  -2513       C  
ATOM   2267  CD1 TYR C 104     -45.655  -4.751 -26.193  1.00 85.68           C  
ANISOU 2267  CD1 TYR C 104     9832  15946   6777  -1601   1104  -2402       C  
ATOM   2268  CD2 TYR C 104     -45.413  -6.876 -25.142  1.00 86.13           C  
ANISOU 2268  CD2 TYR C 104     9811  15892   7025  -1985   1269  -2456       C  
ATOM   2269  CE1 TYR C 104     -44.316  -4.755 -26.524  1.00 86.64           C  
ANISOU 2269  CE1 TYR C 104    10104  15895   6919  -1637   1080  -2242       C  
ATOM   2270  CE2 TYR C 104     -44.070  -6.889 -25.472  1.00 77.24           C  
ANISOU 2270  CE2 TYR C 104     8836  14598   5915  -2011   1238  -2299       C  
ATOM   2271  CZ  TYR C 104     -43.528  -5.825 -26.161  1.00 83.27           C  
ANISOU 2271  CZ  TYR C 104     9709  15336   6595  -1840   1144  -2195       C  
ATOM   2272  OH  TYR C 104     -42.192  -5.830 -26.490  1.00 91.22           O  
ANISOU 2272  OH  TYR C 104    10858  16182   7620  -1872   1119  -2042       O  
ATOM   2273  N   ILE C 105     -49.954  -3.714 -23.035  1.00 98.80           N  
ANISOU 2273  N   ILE C 105    11150  18039   8352  -1498   1254  -2814       N  
ATOM   2274  CA  ILE C 105     -51.381  -3.388 -22.863  1.00107.94           C  
ANISOU 2274  CA  ILE C 105    12138  19422   9451  -1395   1258  -2986       C  
ATOM   2275  C   ILE C 105     -51.960  -2.629 -24.054  1.00 93.09           C  
ANISOU 2275  C   ILE C 105    10184  17723   7464  -1153   1148  -3065       C  
ATOM   2276  O   ILE C 105     -53.053  -2.962 -24.515  1.00 86.91           O  
ANISOU 2276  O   ILE C 105     9188  17174   6659  -1115   1148  -3254       O  
ATOM   2277  CB  ILE C 105     -51.576  -2.581 -21.563  1.00104.18           C  
ANISOU 2277  CB  ILE C 105    11760  18883   8942  -1355   1286  -2934       C  
ATOM   2278  CG1 ILE C 105     -50.562  -1.439 -21.451  1.00103.53           C  
ANISOU 2278  CG1 ILE C 105    11920  18603   8814  -1234   1212  -2748       C  
ATOM   2279  CG2 ILE C 105     -51.448  -3.498 -20.364  1.00 96.94           C  
ANISOU 2279  CG2 ILE C 105    10840  17876   8116  -1588   1414  -2917       C  
ATOM   2280  CD1 ILE C 105     -51.184  -0.059 -21.529  1.00 99.96           C  
ANISOU 2280  CD1 ILE C 105    11496  18232   8252   -980   1131  -2773       C  
ATOM   2281  N   TYR C 106     -51.260  -1.603 -24.530  1.00 90.50           N  
ANISOU 2281  N   TYR C 106    10026  17291   7067   -986   1057  -2925       N  
ATOM   2282  CA  TYR C 106     -51.710  -0.853 -25.697  1.00124.52           C  
ANISOU 2282  CA  TYR C 106    14289  21756  11267   -742    953  -2972       C  
ATOM   2283  C   TYR C 106     -51.478  -1.644 -26.988  1.00141.38           C  
ANISOU 2283  C   TYR C 106    16327  23979  13413   -768    923  -3021       C  
ATOM   2284  O   TYR C 106     -50.351  -2.040 -27.287  1.00146.33           O  
ANISOU 2284  O   TYR C 106    17065  24442  14092   -869    926  -2895       O  
ATOM   2285  CB  TYR C 106     -50.998   0.500 -25.769  1.00126.96           C  
ANISOU 2285  CB  TYR C 106    14825  21906  11508   -562    878  -2792       C  
ATOM   2286  N   TRP C 107     -52.524  -1.849 -27.788  1.00136.50           N  
ANISOU 2286  N   TRP C 107    15499  23626  12739   -667    888  -3208       N  
ATOM   2287  CA  TRP C 107     -52.378  -2.585 -29.046  1.00136.36           C  
ANISOU 2287  CA  TRP C 107    15372  23715  12722   -676    853  -3277       C  
ATOM   2288  C   TRP C 107     -52.869  -1.808 -30.266  1.00154.65           C  
ANISOU 2288  C   TRP C 107    17633  26232  14895   -394    741  -3328       C  
ATOM   2289  O   TRP C 107     -53.143  -0.618 -30.192  1.00159.44           O  
ANISOU 2289  O   TRP C 107    18323  26852  15403   -182    686  -3272       O  
ATOM   2290  CB  TRP C 107     -53.088  -3.935 -28.987  1.00116.27           C  
ANISOU 2290  CB  TRP C 107    12593  21313  10270   -870    927  -3484       C  
ATOM   2291  CG  TRP C 107     -52.377  -4.950 -28.181  1.00110.65           C  
ANISOU 2291  CG  TRP C 107    11939  20399   9704  -1152   1033  -3419       C  
ATOM   2292  CD1 TRP C 107     -52.228  -4.949 -26.849  1.00122.43           C  
ANISOU 2292  CD1 TRP C 107    13522  21739  11257  -1281   1116  -3342       C  
ATOM   2293  CD2 TRP C 107     -51.726  -6.128 -28.651  1.00111.73           C  
ANISOU 2293  CD2 TRP C 107    12046  20469   9939  -1332   1066  -3427       C  
ATOM   2294  NE1 TRP C 107     -51.519  -6.037 -26.445  1.00120.41           N  
ANISOU 2294  NE1 TRP C 107    13301  21322  11127  -1524   1201  -3292       N  
ATOM   2295  CE2 TRP C 107     -51.201  -6.783 -27.541  1.00101.03           C  
ANISOU 2295  CE2 TRP C 107    10773  18911   8701  -1561   1172  -3345       C  
ATOM   2296  CE3 TRP C 107     -51.537  -6.690 -29.904  1.00124.20           C  
ANISOU 2296  CE3 TRP C 107    13536  22142  11512  -1312   1016  -3499       C  
ATOM   2297  CZ2 TRP C 107     -50.501  -7.966 -27.637  1.00 99.68           C  
ANISOU 2297  CZ2 TRP C 107    10605  18621   8647  -1767   1230  -3327       C  
ATOM   2298  CZ3 TRP C 107     -50.838  -7.869 -29.996  1.00122.02           C  
ANISOU 2298  CZ3 TRP C 107    13259  21749  11356  -1523   1073  -3490       C  
ATOM   2299  CH2 TRP C 107     -50.330  -8.493 -28.873  1.00109.40           C  
ANISOU 2299  CH2 TRP C 107    11750  19941   9878  -1746   1178  -3403       C  
ATOM   2300  N   GLY C 108     -52.958  -2.511 -31.391  1.00170.94           N  
ANISOU 2300  N   GLY C 108    19557  28446  16946   -389    707  -3434       N  
ATOM   2301  CA  GLY C 108     -53.403  -1.969 -32.668  1.00178.00           C  
ANISOU 2301  CA  GLY C 108    20375  29557  17699   -129    602  -3495       C  
ATOM   2302  C   GLY C 108     -54.223  -3.031 -33.384  1.00183.74           C  
ANISOU 2302  C   GLY C 108    20825  30547  18441   -182    601  -3749       C  
ATOM   2303  O   GLY C 108     -54.135  -4.203 -33.033  1.00194.18           O  
ANISOU 2303  O   GLY C 108    22059  31826  19896   -433    680  -3831       O  
ATOM   2304  N   GLN C 109     -55.021  -2.651 -34.375  1.00160.55           N  
ANISOU 2304  N   GLN C 109    17748  27880  15372     52    513  -3879       N  
ATOM   2305  CA  GLN C 109     -55.865  -3.630 -35.068  1.00138.83           C  
ANISOU 2305  CA  GLN C 109    14715  25402  12632     10    504  -4146       C  
ATOM   2306  C   GLN C 109     -55.118  -4.743 -35.805  1.00124.08           C  
ANISOU 2306  C   GLN C 109    12810  23494  10840   -147    515  -4167       C  
ATOM   2307  O   GLN C 109     -55.482  -5.913 -35.721  1.00111.92           O  
ANISOU 2307  O   GLN C 109    11091  22021   9413   -350    573  -4348       O  
ATOM   2308  CB  GLN C 109     -56.803  -2.908 -36.025  1.00127.52           C  
ANISOU 2308  CB  GLN C 109    13153  24275  11023    323    396  -4270       C  
ATOM   2309  CG  GLN C 109     -57.823  -2.030 -35.323  1.00136.03           C  
ANISOU 2309  CG  GLN C 109    14193  25455  12035    468    389  -4326       C  
ATOM   2310  CD  GLN C 109     -58.890  -2.837 -34.614  1.00143.75           C  
ANISOU 2310  CD  GLN C 109    14931  26580  13108    292    465  -4568       C  
ATOM   2311  OE1 GLN C 109     -58.641  -3.948 -34.150  1.00149.61           O  
ANISOU 2311  OE1 GLN C 109    15619  27220  14005      4    558  -4617       O  
ATOM   2312  NE2 GLN C 109     -60.092  -2.281 -34.531  1.00144.82           N  
ANISOU 2312  NE2 GLN C 109    14920  26955  13151    469    429  -4721       N  
ATOM   2313  N   GLY C 110     -54.054  -4.371 -36.495  1.00132.14           N  
ANISOU 2313  N   GLY C 110    14007  24397  11804    -57    464  -3977       N  
ATOM   2314  CA  GLY C 110     -53.218  -5.299 -37.244  1.00137.17           C  
ANISOU 2314  CA  GLY C 110    14637  24986  12496   -177    465  -3970       C  
ATOM   2315  C   GLY C 110     -53.571  -5.419 -38.714  1.00138.02           C  
ANISOU 2315  C   GLY C 110    14589  25371  12481     10    369  -4109       C  
ATOM   2316  O   GLY C 110     -54.651  -5.009 -39.119  1.00139.87           O  
ANISOU 2316  O   GLY C 110    14668  25872  12606    202    310  -4265       O  
ATOM   2317  N   THR C 111     -52.664  -5.960 -39.524  1.00137.18           N  
ANISOU 2317  N   THR C 111    14522  25215  12384    -32    351  -4055       N  
ATOM   2318  CA  THR C 111     -52.946  -6.123 -40.948  1.00147.27           C  
ANISOU 2318  CA  THR C 111    15651  26765  13539    146    259  -4189       C  
ATOM   2319  C   THR C 111     -52.655  -7.528 -41.436  1.00139.84           C  
ANISOU 2319  C   THR C 111    14573  25852  12707    -51    283  -4340       C  
ATOM   2320  O   THR C 111     -52.303  -8.408 -40.644  1.00145.13           O  
ANISOU 2320  O   THR C 111    15257  26331  13554   -331    377  -4347       O  
ATOM   2321  CB  THR C 111     -52.184  -5.129 -41.820  1.00140.44           C  
ANISOU 2321  CB  THR C 111    14968  25880  12514    394    182  -3970       C  
ATOM   2322  OG1 THR C 111     -50.791  -5.236 -41.543  1.00128.37           O  
ANISOU 2322  OG1 THR C 111    13659  24047  11067    248    230  -3735       O  
ATOM   2323  CG2 THR C 111     -52.643  -3.725 -41.535  1.00144.35           C  
ANISOU 2323  CG2 THR C 111    15567  26392  12886    631    144  -3858       C  
ATOM   2324  N   GLN C 112     -52.797  -7.741 -42.742  1.00121.85           N  
ANISOU 2324  N   GLN C 112    12165  23812  10319    100    200  -4462       N  
ATOM   2325  CA  GLN C 112     -52.577  -9.081 -43.270  1.00107.64           C  
ANISOU 2325  CA  GLN C 112    10220  22057   8620    -74    216  -4632       C  
ATOM   2326  C   GLN C 112     -51.330  -9.189 -44.138  1.00108.83           C  
ANISOU 2326  C   GLN C 112    10505  22121   8724    -34    181  -4475       C  
ATOM   2327  O   GLN C 112     -50.922  -8.229 -44.787  1.00100.57           O  
ANISOU 2327  O   GLN C 112     9585  21111   7515    202    115  -4306       O  
ATOM   2328  CB  GLN C 112     -53.792  -9.541 -44.082  1.00 98.43           C  
ANISOU 2328  CB  GLN C 112     8746  21259   7394     22    153  -4964       C  
ATOM   2329  CG  GLN C 112     -54.487 -10.783 -43.534  1.00102.28           C  
ANISOU 2329  CG  GLN C 112     9018  21772   8072   -252    232  -5227       C  
ATOM   2330  CD  GLN C 112     -53.654 -12.051 -43.680  1.00117.46           C  
ANISOU 2330  CD  GLN C 112    10941  23536  10152   -498    285  -5258       C  
ATOM   2331  OE1 GLN C 112     -52.599 -12.054 -44.316  1.00119.29           O  
ANISOU 2331  OE1 GLN C 112    11306  23680  10338   -452    252  -5111       O  
ATOM   2332  NE2 GLN C 112     -54.133 -13.139 -43.087  1.00121.78           N  
ANISOU 2332  NE2 GLN C 112    11339  24045  10888   -762    372  -5450       N  
ATOM   2333  N   VAL C 113     -50.730 -10.375 -44.126  1.00110.57           N  
ANISOU 2333  N   VAL C 113    10697  22223   9093   -270    233  -4532       N  
ATOM   2334  CA  VAL C 113     -49.595 -10.703 -44.981  1.00108.45           C  
ANISOU 2334  CA  VAL C 113    10514  21895   8795   -258    205  -4431       C  
ATOM   2335  C   VAL C 113     -49.721 -12.146 -45.469  1.00117.48           C  
ANISOU 2335  C   VAL C 113    11455  23130  10051   -424    217  -4687       C  
ATOM   2336  O   VAL C 113     -49.840 -13.067 -44.657  1.00119.73           O  
ANISOU 2336  O   VAL C 113    11688  23275  10528   -689    305  -4782       O  
ATOM   2337  CB  VAL C 113     -48.252 -10.518 -44.250  1.00 91.60           C  
ANISOU 2337  CB  VAL C 113     8656  19402   6744   -394    272  -4131       C  
ATOM   2338  CG1 VAL C 113     -47.149 -11.285 -44.953  1.00 90.91           C  
ANISOU 2338  CG1 VAL C 113     8609  19243   6690   -470    268  -4091       C  
ATOM   2339  CG2 VAL C 113     -47.903  -9.040 -44.139  1.00 91.06           C  
ANISOU 2339  CG2 VAL C 113     8800  19260   6539   -189    240  -3866       C  
ATOM   2340  N   THR C 114     -49.704 -12.339 -46.789  1.00118.50           N  
ANISOU 2340  N   THR C 114    11471  23492  10061   -266    130  -4801       N  
ATOM   2341  CA  THR C 114     -49.925 -13.662 -47.368  1.00 96.66           C  
ANISOU 2341  CA  THR C 114     8491  20848   7388   -395    126  -5078       C  
ATOM   2342  C   THR C 114     -48.786 -14.096 -48.285  1.00 96.12           C  
ANISOU 2342  C   THR C 114     8490  20744   7286   -376     94  -5006       C  
ATOM   2343  O   THR C 114     -48.482 -13.413 -49.256  1.00104.66           O  
ANISOU 2343  O   THR C 114     9616  21937   8211   -127     11  -4888       O  
ATOM   2344  CB  THR C 114     -51.224 -13.713 -48.186  1.00 99.10           C  
ANISOU 2344  CB  THR C 114     8517  21487   7649   -226     43  -5340       C  
ATOM   2345  OG1 THR C 114     -52.311 -13.177 -47.424  1.00 99.76           O  
ANISOU 2345  OG1 THR C 114     8532  21643   7729   -204     62  -5407       O  
ATOM   2346  CG2 THR C 114     -51.532 -15.141 -48.608  1.00100.20           C  
ANISOU 2346  CG2 THR C 114     8424  21704   7945   -399     55  -5632       C  
ATOM   2347  N   VAL C 115     -48.165 -15.231 -47.976  1.00104.58           N  
ANISOU 2347  N   VAL C 115     9571  21621   8543   -632    163  -5044       N  
ATOM   2348  CA  VAL C 115     -47.067 -15.757 -48.788  1.00103.73           C  
ANISOU 2348  CA  VAL C 115     9520  21470   8421   -635    139  -4991       C  
ATOM   2349  C   VAL C 115     -47.441 -17.062 -49.494  1.00119.86           C  
ANISOU 2349  C   VAL C 115    11322  23671  10547   -728    119  -5318       C  
ATOM   2350  O   VAL C 115     -47.729 -18.066 -48.845  1.00123.67           O  
ANISOU 2350  O   VAL C 115    11719  24034  11236   -979    196  -5471       O  
ATOM   2351  CB  VAL C 115     -45.800 -15.999 -47.939  1.00 92.56           C  
ANISOU 2351  CB  VAL C 115     8343  19680   7145   -838    227  -4741       C  
ATOM   2352  CG1 VAL C 115     -44.654 -16.460 -48.809  1.00 92.09           C  
ANISOU 2352  CG1 VAL C 115     8342  19593   7055   -819    198  -4679       C  
ATOM   2353  CG2 VAL C 115     -45.429 -14.747 -47.165  1.00111.37           C  
ANISOU 2353  CG2 VAL C 115    10958  21893   9466   -768    251  -4435       C  
ATOM   2354  N   SER C 116     -47.416 -17.040 -50.825  1.00129.86           N  
ANISOU 2354  N   SER C 116    12486  25128  11727   -517     23  -5362       N  
ATOM   2355  CA  SER C 116     -47.736 -18.218 -51.631  1.00134.53           C  
ANISOU 2355  CA  SER C 116    12844  25844  12428   -569     -4  -5637       C  
ATOM   2356  C   SER C 116     -46.510 -18.701 -52.395  1.00134.55           C  
ANISOU 2356  C   SER C 116    12931  25776  12417   -561    -24  -5554       C  
ATOM   2357  O   SER C 116     -45.586 -17.931 -52.655  1.00146.26           O  
ANISOU 2357  O   SER C 116    14609  27200  13763   -428    -47  -5288       O  
ATOM   2358  CB  SER C 116     -48.875 -17.918 -52.608  1.00130.54           C  
ANISOU 2358  CB  SER C 116    12100  25648  11851   -326   -100  -5802       C  
ATOM   2359  OG  SER C 116     -50.053 -17.539 -51.920  1.00137.85           O  
ANISOU 2359  OG  SER C 116    12926  26655  12797   -336    -83  -5902       O  
ATOM   2360  N   SER C 117     -46.494 -19.987 -52.725  1.00121.43           N  
ANISOU 2360  N   SER C 117    11121  24113  10903   -712    -10  -5782       N  
ATOM   2361  CA  SER C 117     -45.381 -20.570 -53.467  1.00124.20           C  
ANISOU 2361  CA  SER C 117    11528  24407  11255   -711    -28  -5738       C  
ATOM   2362  C   SER C 117     -45.835 -21.420 -54.656  1.00128.70           C  
ANISOU 2362  C   SER C 117    11842  25178  11878   -635    -90  -6002       C  
ATOM   2363  O   SER C 117     -46.612 -20.972 -55.501  1.00115.22           O  
ANISOU 2363  O   SER C 117     9978  23724  10077   -404   -171  -6078       O  
ATOM   2364  CB  SER C 117     -44.516 -21.396 -52.515  1.00123.07           C  
ANISOU 2364  CB  SER C 117    11528  23976  11255  -1012     71  -5709       C  
ATOM   2365  OG  SER C 117     -45.316 -22.302 -51.773  1.00124.01           O  
ANISOU 2365  OG  SER C 117    11512  24038  11569  -1255    142  -5954       O  
TER    2366      SER C 117                                                      
END



If you find results from this site helpful for your research, please cite one of our papers:

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