CNRS Nantes University US2B US2B
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***  7UJC   ***

elNémo ID: 240508194650189588

Job options:

ID        	=	 240508194650189588
JOBID     	=	 7UJC 
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 7UJC 

HEADER    TRANSCRIPTION                           30-MAR-22   7UJC              
TITLE     RALOXIFENE IN COMPLEX WITH ESTROGEN RECEPTOR ALPHA LIGAND BINDING     
TITLE    2 DOMAIN Y537S MUTATION                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTROGEN RECEPTOR;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3 
COMPND   5 GROUP A MEMBER 1;                                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ESR1, ESR, NR3A1;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA HELICAL BUNDLE, HORMONE RECEPTOR, BREAST CANCER, ACTIVATING     
KEYWDS   2 MUTATION, TRANSCRIPTION                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.HOSFIELD,G.L.GREENE,S.W.FANNING                                   
REVDAT   2   18-OCT-23 7UJC    1       REMARK                                   
REVDAT   1   15-JUN-22 7UJC    0                                                
SPRSDE     15-JUN-22 7UJC      7KCA                                             
JRNL        AUTH   D.J.HOSFIELD,S.WEBER,N.S.LI,M.SUAVAGE,C.F.JOINER,            
JRNL        AUTH 2 G.R.HANCOCK,E.A.SULLIVAN,E.NDUKWE,R.HAN,S.CUSH,M.LAINE,      
JRNL        AUTH 3 S.C.MADER,G.L.GREENE,S.W.FANNING                             
JRNL        TITL   STEREOSPECIFIC LASOFOXIFENE DERIVATIVES REVEAL THE INTERPLAY 
JRNL        TITL 2 BETWEEN ESTROGEN RECEPTOR ALPHA STABILITY AND ANTAGONISTIC   
JRNL        TITL 3 ACTIVITY IN ESR1 MUTANT BREAST CANCER CELLS.                 
JRNL        REF    ELIFE                         V.  11       2022              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   35575456                                                     
JRNL        DOI    10.7554/ELIFE.72512                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 39306                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.220                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2051                            
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 29.1800 -  4.4000    0.90     2802   158  0.1840 0.2094        
REMARK   3     2  4.4000 -  3.4900    0.96     2926   169  0.1606 0.2010        
REMARK   3     3  3.4900 -  3.0500    0.99     3011   152  0.1864 0.2408        
REMARK   3     4  3.0500 -  2.7700    0.99     2993   168  0.1959 0.2174        
REMARK   3     5  2.7700 -  2.5700    0.99     2966   172  0.1910 0.2384        
REMARK   3     6  2.5700 -  2.4200    0.99     3024   163  0.1867 0.2353        
REMARK   3     7  2.4200 -  2.3000    0.99     3006   162  0.1978 0.2324        
REMARK   3     8  2.3000 -  2.2000    0.95     2829   163  0.2061 0.2854        
REMARK   3     9  2.2000 -  2.1200    0.90     2705   139  0.2111 0.2291        
REMARK   3    10  2.1200 -  2.0400    0.83     2484   142  0.2233 0.2522        
REMARK   3    11  2.0400 -  1.9800    0.75     2235   117  0.2227 0.2343        
REMARK   3    12  1.9800 -  1.9200    0.65     1944   113  0.2218 0.2657        
REMARK   3    13  1.9200 -  1.8700    0.56     1678    98  0.2364 0.2879        
REMARK   3    14  1.8700 -  1.8300    0.50     1500    78  0.2387 0.2790        
REMARK   3    15  1.8300 -  1.7800    0.38     1152    57  0.2544 0.3169        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 306 THROUGH 549)                  
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3441 -21.5663  22.5252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1262 T22:   0.0900                                     
REMARK   3      T33:   0.1257 T12:   0.0485                                     
REMARK   3      T13:  -0.0042 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5374 L22:   1.1669                                     
REMARK   3      L33:   2.3689 L12:   0.0034                                     
REMARK   3      L13:  -0.3826 L23:  -0.2415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0340 S12:   0.2119 S13:  -0.0026                       
REMARK   3      S21:   0.0555 S22:   0.0118 S23:  -0.0264                       
REMARK   3      S31:   0.0060 S32:  -0.0762 S33:  -0.0131                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 306 THROUGH 546)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1241 -33.6387  23.2919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1509 T22:   0.2663                                     
REMARK   3      T33:   0.1558 T12:   0.0616                                     
REMARK   3      T13:   0.0240 T23:   0.0557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1972 L22:   3.8610                                     
REMARK   3      L33:   0.8818 L12:  -1.3978                                     
REMARK   3      L13:   0.0970 L23:   0.2865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0110 S12:   0.0985 S13:   0.1596                       
REMARK   3      S21:   0.0555 S22:  -0.1130 S23:  -0.2531                       
REMARK   3      S31:   0.0689 S32:   0.2137 S33:   0.0484                       
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 7UJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1000264272.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39306                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 2.4700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 5UFX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8,000, MGCL2, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.27850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.92050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.27850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.92050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     ASN A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     TYR A   301                                                      
REMARK 465     PHE A   302                                                      
REMARK 465     GLN A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     MET A   305                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     THR A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     LEU A   462                                                      
REMARK 465     SER A   463                                                      
REMARK 465     SER A   464                                                      
REMARK 465     LYS A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     VAL A   533                                                      
REMARK 465     VAL A   534                                                      
REMARK 465     PRO A   535                                                      
REMARK 465     HIS A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     PRO A   552                                                      
REMARK 465     THR A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     HIS B   292                                                      
REMARK 465     HIS B   293                                                      
REMARK 465     HIS B   294                                                      
REMARK 465     HIS B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     ASN B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     TYR B   301                                                      
REMARK 465     PHE B   302                                                      
REMARK 465     GLN B   303                                                      
REMARK 465     SER B   304                                                      
REMARK 465     MET B   305                                                      
REMARK 465     PRO B   333                                                      
REMARK 465     THR B   334                                                      
REMARK 465     ARG B   335                                                      
REMARK 465     PRO B   336                                                      
REMARK 465     PHE B   337                                                      
REMARK 465     SER B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     THR B   460                                                      
REMARK 465     PHE B   461                                                      
REMARK 465     LEU B   462                                                      
REMARK 465     SER B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     THR B   465                                                      
REMARK 465     LEU B   466                                                      
REMARK 465     LYS B   467                                                      
REMARK 465     SER B   468                                                      
REMARK 465     LEU B   469                                                      
REMARK 465     LYS B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     LYS B   531                                                      
REMARK 465     ASN B   532                                                      
REMARK 465     VAL B   533                                                      
REMARK 465     VAL B   534                                                      
REMARK 465     HIS B   547                                                      
REMARK 465     ARG B   548                                                      
REMARK 465     LEU B   549                                                      
REMARK 465     HIS B   550                                                      
REMARK 465     ALA B   551                                                      
REMARK 465     PRO B   552                                                      
REMARK 465     THR B   553                                                      
REMARK 465     SER B   554                                                      
REMARK 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     LEU A 306    CG   CD1  CD2                                       
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 418    CG2                                                 
REMARK 470     MET A 437    CG   SD   CE                                        
REMARK 470     THR A 460    CG2                                                 
REMARK 470     ARG A 477    CZ   NH1  NH2                                       
REMARK 470     LYS A 481    CD   CE   NZ                                        
REMARK 470     ASP A 538    CG   OD1  OD2                                       
REMARK 470     LEU A 541    CG   CD1  CD2                                       
REMARK 470     ARG A 548    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 323    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 331    CD1  CE1                                            
REMARK 470     ASP B 332    CG   OD1  OD2                                       
REMARK 470     LYS B 362    CE   NZ                                             
REMARK 470     GLU B 397    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 416    NZ                                                  
REMARK 470     GLU B 419    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 423    CG   CD   OE1  OE2                                  
REMARK 470     MET B 437    CG   SD   CE                                        
REMARK 470     GLU B 470    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 471    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 472    CG   CD   CE   NZ                                   
REMARK 470     ARG B 477    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 526    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ASP B 545    CG   OD1  OD2                                       
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    LEU B 408       67.07   -152.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 877        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 878        DISTANCE =  6.20 ANGSTROMS                       
DBREF  7UJC A  306   554  UNP    P03372   ESR1_HUMAN     306    554             
DBREF  7UJC B  306   554  UNP    P03372   ESR1_HUMAN     306    554             
SEQADV 7UJC HIS A  292  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS A  293  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS A  294  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS A  295  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS A  296  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS A  297  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC GLU A  298  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC ASN A  299  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC LEU A  300  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC TYR A  301  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC PHE A  302  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC GLN A  303  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC SER A  304  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC MET A  305  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC SER A  381  UNP  P03372    CYS   381 CONFLICT                       
SEQADV 7UJC SER A  417  UNP  P03372    CYS   417 CONFLICT                       
SEQADV 7UJC SER A  530  UNP  P03372    CYS   530 CONFLICT                       
SEQADV 7UJC SER A  537  UNP  P03372    TYR   537 ENGINEERED MUTATION            
SEQADV 7UJC HIS B  292  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS B  293  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS B  294  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS B  295  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS B  296  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC HIS B  297  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC GLU B  298  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC ASN B  299  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC LEU B  300  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC TYR B  301  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC PHE B  302  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC GLN B  303  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC SER B  304  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC MET B  305  UNP  P03372              EXPRESSION TAG                 
SEQADV 7UJC SER B  381  UNP  P03372    CYS   381 CONFLICT                       
SEQADV 7UJC SER B  417  UNP  P03372    CYS   417 CONFLICT                       
SEQADV 7UJC SER B  530  UNP  P03372    CYS   530 CONFLICT                       
SEQADV 7UJC SER B  537  UNP  P03372    TYR   537 ENGINEERED MUTATION            
SEQRES   1 A  263  HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN SER          
SEQRES   2 A  263  MET LEU ALA LEU SER LEU THR ALA ASP GLN MET VAL SER          
SEQRES   3 A  263  ALA LEU LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU          
SEQRES   4 A  263  TYR ASP PRO THR ARG PRO PHE SER GLU ALA SER MET MET          
SEQRES   5 A  263  GLY LEU LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS          
SEQRES   6 A  263  MET ILE ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP          
SEQRES   7 A  263  LEU THR LEU HIS ASP GLN VAL HIS LEU LEU GLU SER ALA          
SEQRES   8 A  263  TRP LEU GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER          
SEQRES   9 A  263  MET GLU HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU          
SEQRES  10 A  263  LEU LEU ASP ARG ASN GLN GLY LYS SER VAL GLU GLY MET          
SEQRES  11 A  263  VAL GLU ILE PHE ASP MET LEU LEU ALA THR SER SER ARG          
SEQRES  12 A  263  PHE ARG MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS          
SEQRES  13 A  263  LEU LYS SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR          
SEQRES  14 A  263  PHE LEU SER SER THR LEU LYS SER LEU GLU GLU LYS ASP          
SEQRES  15 A  263  HIS ILE HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU          
SEQRES  16 A  263  ILE HIS LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN          
SEQRES  17 A  263  GLN HIS GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER          
SEQRES  18 A  263  HIS ILE ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU          
SEQRES  19 A  263  TYR SER MET LYS SER LYS ASN VAL VAL PRO LEU SER ASP          
SEQRES  20 A  263  LEU LEU LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA          
SEQRES  21 A  263  PRO THR SER                                                  
SEQRES   1 B  263  HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN SER          
SEQRES   2 B  263  MET LEU ALA LEU SER LEU THR ALA ASP GLN MET VAL SER          
SEQRES   3 B  263  ALA LEU LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU          
SEQRES   4 B  263  TYR ASP PRO THR ARG PRO PHE SER GLU ALA SER MET MET          
SEQRES   5 B  263  GLY LEU LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS          
SEQRES   6 B  263  MET ILE ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP          
SEQRES   7 B  263  LEU THR LEU HIS ASP GLN VAL HIS LEU LEU GLU SER ALA          
SEQRES   8 B  263  TRP LEU GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER          
SEQRES   9 B  263  MET GLU HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU          
SEQRES  10 B  263  LEU LEU ASP ARG ASN GLN GLY LYS SER VAL GLU GLY MET          
SEQRES  11 B  263  VAL GLU ILE PHE ASP MET LEU LEU ALA THR SER SER ARG          
SEQRES  12 B  263  PHE ARG MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS          
SEQRES  13 B  263  LEU LYS SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR          
SEQRES  14 B  263  PHE LEU SER SER THR LEU LYS SER LEU GLU GLU LYS ASP          
SEQRES  15 B  263  HIS ILE HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU          
SEQRES  16 B  263  ILE HIS LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN          
SEQRES  17 B  263  GLN HIS GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER          
SEQRES  18 B  263  HIS ILE ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU          
SEQRES  19 B  263  TYR SER MET LYS SER LYS ASN VAL VAL PRO LEU SER ASP          
SEQRES  20 B  263  LEU LEU LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA          
SEQRES  21 B  263  PRO THR SER                                                  
HET    RAL  A 601      34                                                       
HET    RAL  B 601      34                                                       
HETNAM     RAL RALOXIFENE                                                       
FORMUL   3  RAL    2(C28 H27 N O4 S)                                            
FORMUL   5  HOH   *302(H2 O)                                                    
HELIX    1   1 LEU A  306  GLU A  323  1                                  18
HELIX    2   2 SER A  341  LYS A  362  1                                  22
HELIX    3   3 GLY A  366  MET A  396  1                                  31
HELIX    4   4 ARG A  412  SER A  417  1                                   6
HELIX    5   5 MET A  421  MET A  438  1                                  18
HELIX    6   6 GLN A  441  SER A  456  1                                  16
HELIX    7   7 LEU A  466  ALA A  493  1                                  28
HELIX    8   8 THR A  496  MET A  528  1                                  33
HELIX    9   9 SER A  537  ASP A  545  1                                   9
SHEET    1   1 1 LYS A 401  ALA A 405  0
SHEET    2   2 1 LEU A 408  ASP A 411  0
CRYST1  102.557   57.841   87.938  90.00 103.74  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009751  0.000000  0.002384        0.00000                         
SCALE2      0.000000  0.017289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011707        0.00000                         
ATOM      1  N   LEU A 306      10.882  -5.547   5.683  1.00 51.28           N
ANISOU    1  N   LEU A 306     6202   6979   6302    270    329   2236       N
ATOM      2  CA  LEU A 306       9.925  -5.148   6.716  1.00 53.33           C
ANISOU    2  CA  LEU A 306     6556   7029   6679    334    290   2173       C
ATOM      3  C   LEU A 306      10.330  -5.624   8.130  1.00 46.78           C
ANISOU    3  C   LEU A 306     5775   6045   5954    289    271   2025       C
ATOM      4  O   LEU A 306      10.736  -4.816   8.974  1.00 47.59           O
ANISOU    4  O   LEU A 306     5963   5913   6206    233    277   2019       O
ATOM      5  CB  LEU A 306       8.526  -5.670   6.368  1.00 57.72           C
ANISOU    5  CB  LEU A 306     7074   7726   7131    452    247   2131       C
ATOM      6  N   ALA A 307      10.209  -6.932   8.386  1.00 44.60           N
ANISOU    6  N   ALA A 307     5448   5902   5597    312    246   1902       N
ATOM      7  CA  ALA A 307      10.519  -7.466   9.707  1.00 43.11           C
ANISOU    7  CA  ALA A 307     5299   5584   5495    284    224   1770       C
ATOM      8  C   ALA A 307      11.976  -7.230  10.085  1.00 44.05           C
ANISOU    8  C   ALA A 307     5413   5622   5700    156    256   1794       C
ATOM      9  O   ALA A 307      12.287  -7.022  11.268  1.00 35.45           O
ANISOU    9  O   ALA A 307     4386   4341   4741    109    237   1721       O
ATOM     10  CB  ALA A 307      10.215  -8.960   9.767  1.00 40.92           C
ANISOU   10  CB  ALA A 307     4964   5480   5102    330    199   1653       C
ATOM     11  N   LEU A 308      12.883  -7.255   9.105  1.00 39.40           N
ANISOU   11  N   LEU A 308     4743   5189   5038     91    303   1886       N
ATOM     12  CA  LEU A 308      14.288  -7.061   9.437  1.00 36.13           C
ANISOU   12  CA  LEU A 308     4298   4726   4704    -43    336   1906       C
ATOM     13  C   LEU A 308      14.612  -5.610   9.753  1.00 42.48           C
ANISOU   13  C   LEU A 308     5183   5296   5661   -126    347   1979       C
ATOM     14  O   LEU A 308      15.728  -5.326  10.204  1.00 45.66           O
ANISOU   14  O   LEU A 308     5568   5625   6156   -257    363   1978       O
ATOM     15  CB  LEU A 308      15.176  -7.564   8.293  1.00 39.34           C
ANISOU   15  CB  LEU A 308     4580   5393   4976    -84    392   1963       C
ATOM     16  CG  LEU A 308      15.164  -9.076   8.022  1.00 41.07           C
ANISOU   16  CG  LEU A 308     4716   5850   5039    -25    398   1859       C
ATOM     17  CD1 LEU A 308      16.089  -9.465   6.861  1.00 41.95           C
ANISOU   17  CD1 LEU A 308     4709   6215   5017    -59    464   1889       C
ATOM     18  CD2 LEU A 308      15.560  -9.822   9.270  1.00 35.30           C
ANISOU   18  CD2 LEU A 308     3992   5025   4396    -41    357   1661       C
ATOM     19  N   SER A 309      13.683  -4.688   9.506  1.00 38.89           N
ANISOU   19  N   SER A 309     4813   4731   5233    -58    341   2039       N
ATOM     20  CA  SER A 309      13.942  -3.276   9.720  1.00 42.86           C
ANISOU   20  CA  SER A 309     5409   5004   5870   -128    360   2110       C
ATOM     21  C   SER A 309      13.386  -2.783  11.044  1.00 43.63           C
ANISOU   21  C   SER A 309     5634   4842   6100   -108    322   1994       C
ATOM     22  O   SER A 309      13.624  -1.629  11.412  1.00 41.49           O
ANISOU   22  O   SER A 309     5460   4355   5948   -175    337   2018       O
ATOM     23  CB  SER A 309      13.362  -2.451   8.562  1.00 45.56           C
ANISOU   23  CB  SER A 309     5768   5383   6161    -66    388   2268       C
ATOM     24  OG  SER A 309      12.009  -2.142   8.830  1.00 49.16           O
ANISOU   24  OG  SER A 309     6299   5748   6631     65    353   2240       O
ATOM     25  N   LEU A 310      12.688  -3.642  11.776  1.00 38.36           N
ANISOU   25  N   LEU A 310     4971   4195   5408    -23    277   1861       N
ATOM     26  CA  LEU A 310      12.101  -3.248  13.043  1.00 37.94           C
ANISOU   26  CA  LEU A 310     5034   3925   5456      8    242   1735       C
ATOM     27  C   LEU A 310      13.191  -2.979  14.067  1.00 33.75           C
ANISOU   27  C   LEU A 310     4540   3238   5047   -138    237   1654       C
ATOM     28  O   LEU A 310      14.147  -3.754  14.196  1.00 36.81           O
ANISOU   28  O   LEU A 310     4835   3727   5425   -226    231   1630       O
ATOM     29  CB  LEU A 310      11.183  -4.359  13.567  1.00 36.59           C
ANISOU   29  CB  LEU A 310     4842   3843   5217    122    199   1610       C
ATOM     30  CG  LEU A 310       9.929  -4.696  12.748  1.00 37.87           C
ANISOU   30  CG  LEU A 310     4965   4162   5264    260    191   1651       C
ATOM     31  CD1 LEU A 310       9.174  -5.809  13.393  1.00 39.53           C
ANISOU   31  CD1 LEU A 310     5154   4445   5422    337    152   1513       C
ATOM     32  CD2 LEU A 310       9.044  -3.466  12.558  1.00 37.73           C
ANISOU   32  CD2 LEU A 310     5025   4018   5292    331    199   1718       C
ATOM     33  N   THR A 311      13.021  -1.896  14.827  1.00 36.27           N
ANISOU   33  N   THR A 311     4989   3316   5476   -165    234   1603       N
ATOM     34  CA  THR A 311      13.790  -1.697  16.048  1.00 39.12           C
ANISOU   34  CA  THR A 311     5399   3522   5941   -290    212   1472       C
ATOM     35  C   THR A 311      13.434  -2.747  17.112  1.00 34.45           C
ANISOU   35  C   THR A 311     4795   2966   5327   -233    159   1309       C
ATOM     36  O   THR A 311      12.473  -3.515  17.003  1.00 26.61           O
ANISOU   36  O   THR A 311     3779   2084   4248    -92    144   1287       O
ATOM     37  CB  THR A 311      13.557  -0.299  16.610  1.00 35.56           C
ANISOU   37  CB  THR A 311     5108   2809   5594   -318    223   1437       C
ATOM     38  OG1 THR A 311      12.235  -0.206  17.154  1.00 36.45           O
ANISOU   38  OG1 THR A 311     5309   2854   5687   -161    200   1356       O
ATOM     39  CG2 THR A 311      13.745   0.755  15.538  1.00 31.61           C
ANISOU   39  CG2 THR A 311     4636   2257   5118   -354    275   1612       C
ATOM     40  N   ALA A 312      14.234  -2.786  18.169  1.00 33.63           N
ANISOU   40  N   ALA A 312     4703   2775   5299   -353    127   1190       N
ATOM     41  CA  ALA A 312      13.914  -3.706  19.254  1.00 36.44           C
ANISOU   41  CA  ALA A 312     5058   3151   5636   -302     72   1036       C
ATOM     42  C   ALA A 312      12.580  -3.345  19.892  1.00 33.82           C
ANISOU   42  C   ALA A 312     4850   2716   5284   -161     72    944       C
ATOM     43  O   ALA A 312      11.773  -4.230  20.200  1.00 29.09           O
ANISOU   43  O   ALA A 312     4232   2207   4613    -42     51    882       O
ATOM     44  CB  ALA A 312      15.023  -3.695  20.300  1.00 35.87           C
ANISOU   44  CB  ALA A 312     4973   3010   5644   -468     21    919       C
ATOM     45  N   ASP A 313      12.325  -2.042  20.074  1.00 29.43           N
ANISOU   45  N   ASP A 313     4419   1975   4788   -173     96    939       N
ATOM     46  CA  ASP A 313      11.067  -1.596  20.662  1.00 33.87           C
ANISOU   46  CA  ASP A 313     5092   2444   5334    -38     90    861       C
ATOM     47  C   ASP A 313       9.889  -1.986  19.789  1.00 31.44           C
ANISOU   47  C   ASP A 313     4728   2275   4941    126     96    954       C
ATOM     48  O   ASP A 313       8.855  -2.433  20.289  1.00 28.63           O
ANISOU   48  O   ASP A 313     4375   1968   4535    244     73    875       O
ATOM     49  CB  ASP A 313      11.090  -0.082  20.857  1.00 39.49           C
ANISOU   49  CB  ASP A 313     5943   2926   6136    -84    107    863       C
ATOM     50  CG  ASP A 313      11.667   0.308  22.196  1.00 46.96           C
ANISOU   50  CG  ASP A 313     6983   3720   7139   -197     85    688       C
ATOM     51  OD1 ASP A 313      11.307  -0.334  23.214  1.00 50.61           O
ANISOU   51  OD1 ASP A 313     7454   4220   7557   -148     54    542       O
ATOM     52  OD2 ASP A 313      12.522   1.216  22.230  1.00 51.29           O
ANISOU   52  OD2 ASP A 313     7592   4126   7770   -347    100    692       O
ATOM     53  N   GLN A 314      10.044  -1.860  18.475  1.00 30.27           N
ANISOU   53  N   GLN A 314     4515   2215   4770    124    125   1120       N
ATOM     54  CA  GLN A 314       8.970  -2.229  17.556  1.00 29.16           C
ANISOU   54  CA  GLN A 314     4308   2231   4541    262    127   1208       C
ATOM     55  C   GLN A 314       8.768  -3.744  17.475  1.00 30.00           C
ANISOU   55  C   GLN A 314     4304   2551   4545    305    106   1163       C
ATOM     56  O   GLN A 314       7.640  -4.209  17.258  1.00 26.11           O
ANISOU   56  O   GLN A 314     3772   2169   3980    420     93   1154       O
ATOM     57  CB  GLN A 314       9.285  -1.643  16.181  1.00 33.21           C
ANISOU   57  CB  GLN A 314     4786   2787   5047    237    165   1396       C
ATOM     58  CG  GLN A 314       9.250  -0.127  16.179  1.00 30.23           C
ANISOU   58  CG  GLN A 314     4527   2190   4769    220    188   1456       C
ATOM     59  CD  GLN A 314       9.904   0.436  14.921  1.00 38.93           C
ANISOU   59  CD  GLN A 314     5597   3322   5874    154    231   1644       C
ATOM     60  OE1 GLN A 314      10.498  -0.309  14.136  1.00 39.80           O
ANISOU   60  OE1 GLN A 314     5592   3621   5909    109    244   1715       O
ATOM     61  NE2 GLN A 314       9.788   1.743  14.718  1.00 44.51           N
ANISOU   61  NE2 GLN A 314     6404   3846   6661    151    255   1728       N
ATOM     62  N   MET A 315       9.827  -4.538  17.632  1.00 24.78           N
ANISOU   62  N   MET A 315     3583   1950   3881    210     99   1137       N
ATOM     63  CA  MET A 315       9.634  -5.994  17.735  1.00 26.14           C
ANISOU   63  CA  MET A 315     3671   2292   3969    256     75   1077       C
ATOM     64  C   MET A 315       8.832  -6.373  18.980  1.00 27.15           C
ANISOU   64  C   MET A 315     3852   2371   4091    323     45    919       C
ATOM     65  O   MET A 315       7.843  -7.127  18.898  1.00 23.28           O
ANISOU   65  O   MET A 315     3322   2001   3522    416     33    886       O
ATOM     66  CB  MET A 315      11.005  -6.680  17.694  1.00 22.19           C
ANISOU   66  CB  MET A 315     3093   1851   3486    143     69   1094       C
ATOM     67  CG  MET A 315      11.013  -8.218  17.753  1.00 31.71           C
ANISOU   67  CG  MET A 315     4215   3248   4588    178     41   1005       C
ATOM     68  SD  MET A 315      10.294  -9.083  16.362  1.00 37.82           S
ANISOU   68  SD  MET A 315     4897   4258   5216    272     60   1084       S
ATOM     69  CE  MET A 315      11.674  -9.177  15.252  1.00 30.84           C
ANISOU   69  CE  MET A 315     3915   3517   4288    170     92   1176       C
ATOM     70  N   VAL A 316       9.219  -5.832  20.137  1.00 21.78           N
ANISOU   70  N   VAL A 316     3261   1525   3489    267     33    818       N
ATOM     71  CA  VAL A 316       8.477  -6.097  21.382  1.00 25.32           C
ANISOU   71  CA  VAL A 316     3765   1935   3921    329      9    670       C
ATOM     72  C   VAL A 316       6.995  -5.788  21.190  1.00 27.17           C
ANISOU   72  C   VAL A 316     4005   2199   4120    455     11    680       C
ATOM     73  O   VAL A 316       6.131  -6.624  21.481  1.00 22.69           O
ANISOU   73  O   VAL A 316     3390   1740   3491    526     -3    624       O
ATOM     74  CB  VAL A 316       9.055  -5.284  22.560  1.00 29.45           C
ANISOU   74  CB  VAL A 316     4396   2269   4525    249      2    562       C
ATOM     75  CG1 VAL A 316       8.160  -5.447  23.805  1.00 28.33           C
ANISOU   75  CG1 VAL A 316     4309   2103   4352    327    -22    418       C
ATOM     76  CG2 VAL A 316      10.489  -5.721  22.889  1.00 25.19           C
ANISOU   76  CG2 VAL A 316     3809   1725   4037    105    -23    533       C
ATOM     77  N   SER A 317       6.684  -4.586  20.663  1.00 23.00           N
ANISOU   77  N   SER A 317     3522   1576   3641    478     30    763       N
ATOM     78  CA  SER A 317       5.288  -4.160  20.517  1.00 23.48           C
ANISOU   78  CA  SER A 317     3575   1652   3694    601     34    782       C
ATOM     79  C   SER A 317       4.499  -5.087  19.620  1.00 25.79           C
ANISOU   79  C   SER A 317     3751   2157   3890    668     35    844       C
ATOM     80  O   SER A 317       3.349  -5.414  19.919  1.00 28.83           O
ANISOU   80  O   SER A 317     4098   2612   4245    751     32    800       O
ATOM     81  CB  SER A 317       5.184  -2.748  19.932  1.00 32.70           C
ANISOU   81  CB  SER A 317     4804   2685   4935    619     57    888       C
ATOM     82  OG  SER A 317       5.777  -1.805  20.776  1.00 35.50           O
ANISOU   82  OG  SER A 317     5277   2827   5385    556     54    819       O
ATOM     83  N   ALA A 318       5.063  -5.432  18.459  1.00 25.89           N
ANISOU   83  N   ALA A 318     3703   2278   3856    630     46    953       N
ATOM     84  CA  ALA A 318       4.385  -6.339  17.543  1.00 26.55           C
ANISOU   84  CA  ALA A 318     3677   2574   3838    682     43   1003       C
ATOM     85  C   ALA A 318       4.144  -7.704  18.185  1.00 25.64           C
ANISOU   85  C   ALA A 318     3517   2559   3665    683     22    885       C
ATOM     86  O   ALA A 318       3.084  -8.315  17.987  1.00 24.95           O
ANISOU   86  O   ALA A 318     3365   2599   3516    744     17    872       O
ATOM     87  CB  ALA A 318       5.208  -6.500  16.265  1.00 22.78           C
ANISOU   87  CB  ALA A 318     3142   2201   3314    631     58   1128       C
ATOM     88  N   LEU A 319       5.118  -8.216  18.931  1.00 26.83           N
ANISOU   88  N   LEU A 319     3697   2659   3837    613     12    806       N
ATOM     89  CA  LEU A 319       4.901  -9.511  19.568  1.00 27.31           C
ANISOU   89  CA  LEU A 319     3723   2804   3848    618     -6    701       C
ATOM     90  C   LEU A 319       3.842  -9.417  20.671  1.00 23.91           C
ANISOU   90  C   LEU A 319     3321   2330   3433    670    -10    606       C
ATOM     91  O   LEU A 319       2.948 -10.278  20.763  1.00 20.21           O
ANISOU   91  O   LEU A 319     2796   1972   2909    708     -9    570       O
ATOM     92  CB  LEU A 319       6.225 -10.056  20.100  1.00 23.26           C
ANISOU   92  CB  LEU A 319     3228   2252   3358    541    -15    654       C
ATOM     93  CG  LEU A 319       7.267 -10.487  19.041  1.00 24.42           C
ANISOU   93  CG  LEU A 319     3309   2487   3484    493     -6    748       C
ATOM     94  CD1 LEU A 319       8.497 -11.011  19.730  1.00 25.32           C
ANISOU   94  CD1 LEU A 319     3420   2581   3619    407    -27    667       C
ATOM     95  CD2 LEU A 319       6.694 -11.573  18.108  1.00 22.54           C
ANISOU   95  CD2 LEU A 319     2982   2443   3140    541     -6    771       C
ATOM     96  N   LEU A 320       3.892  -8.352  21.483  1.00 20.37           N
ANISOU   96  N   LEU A 320     2953   1724   3061    671     -7    568       N
ATOM     97  CA  LEU A 320       2.896  -8.183  22.553  1.00 28.96           C
ANISOU   97  CA  LEU A 320     4058   2780   4167    728      2    482       C
ATOM     98  C   LEU A 320       1.500  -8.057  21.966  1.00 26.74           C
ANISOU   98  C   LEU A 320     3714   2588   3856    821     22    540       C
ATOM     99  O   LEU A 320       0.541  -8.655  22.476  1.00 23.28           O
ANISOU   99  O   LEU A 320     3234   2230   3382    864     37    491       O
ATOM    100  CB  LEU A 320       3.221  -6.953  23.408  1.00 30.01           C
ANISOU  100  CB  LEU A 320     4287   2723   4392    718      5    431       C
ATOM    101  CG  LEU A 320       4.374  -7.085  24.409  1.00 27.33           C
ANISOU  101  CG  LEU A 320     4005   2296   4085    630    -13    336       C
ATOM    102  CD1 LEU A 320       4.583  -5.737  25.152  1.00 29.40           C
ANISOU  102  CD1 LEU A 320     4363   2363   4444    617     -6    278       C
ATOM    103  CD2 LEU A 320       4.126  -8.260  25.401  1.00 21.59           C
ANISOU  103  CD2 LEU A 320     3242   1663   3297    633     -5    239       C
ATOM    104  N  AASP A 321       1.364  -7.323  20.872  0.49 25.06           N
ANISOU  104  N  AASP A 321     3491   2378   3653    851     28    655       N
ATOM    105  N  BASP A 321       1.374  -7.306  20.877  0.51 25.06           N
ANISOU  105  N  BASP A 321     3492   2375   3654    851     28    655       N
ATOM    106  CA AASP A 321       0.047  -7.154  20.261  0.49 30.42           C
ANISOU  106  CA AASP A 321     4103   3155   4302    946     44    724       C
ATOM    107  CA BASP A 321       0.077  -7.130  20.224  0.51 30.43           C
ANISOU  107  CA BASP A 321     4105   3154   4304    945     44    727       C
ATOM    108  C  AASP A 321      -0.407  -8.380  19.484  0.49 29.35           C
ANISOU  108  C  AASP A 321     3860   3226   4065    945     35    751       C
ATOM    109  C  BASP A 321      -0.407  -8.415  19.574  0.51 29.35           C
ANISOU  109  C  BASP A 321     3863   3223   4067    943     35    743       C
ATOM    110  O  AASP A 321      -1.605  -8.538  19.250  0.49 29.87           O
ANISOU  110  O  AASP A 321     3855   3400   4093   1014     44    777       O
ATOM    111  O  BASP A 321      -1.614  -8.659  19.523  0.51 29.72           O
ANISOU  111  O  BASP A 321     3842   3371   4078   1010     46    751       O
ATOM    112  CB AASP A 321       0.031  -5.944  19.334  0.49 28.52           C
ANISOU  112  CB AASP A 321     3882   2853   4101    986     54    850       C
ATOM    113  CB BASP A 321       0.157  -6.028  19.174  0.51 28.41           C
ANISOU  113  CB BASP A 321     3863   2854   4079    975     52    861       C
ATOM    114  CG AASP A 321      -1.378  -5.497  19.005  0.49 33.90           C
ANISOU  114  CG AASP A 321     4508   3596   4775   1103     72    912       C
ATOM    115  CG BASP A 321       0.458  -4.673  19.779  0.51 30.80           C
ANISOU  115  CG BASP A 321     4274   2937   4490    987     63    850       C
ATOM    116  OD1AASP A 321      -2.069  -5.024  19.931  0.49 32.50           O
ANISOU  116  OD1AASP A 321     4359   3338   4650   1168     92    850       O
ATOM    117  OD1BASP A 321       0.517  -4.559  21.019  0.51 35.60           O
ANISOU  117  OD1BASP A 321     4940   3441   5146    978     64    730       O
ATOM    118  OD2AASP A 321      -1.791  -5.613  17.838  0.49 38.21           O
ANISOU  118  OD2AASP A 321     4976   4280   5260   1134     69   1023       O
ATOM    119  OD2BASP A 321       0.637  -3.717  19.014  0.51 30.75           O
ANISOU  119  OD2BASP A 321     4299   2862   4523   1003     73    962       O
ATOM    120  N   ALA A 322       0.515  -9.241  19.077  1.00 25.65           N
ANISOU  120  N   ALA A 322     3377   2818   3553    870     18    746       N
ATOM    121  CA  ALA A 322       0.150 -10.482  18.436  1.00 28.40           C
ANISOU  121  CA  ALA A 322     3634   3351   3808    864      6    749       C
ATOM    122  C   ALA A 322      -0.376 -11.509  19.413  1.00 21.93           C
ANISOU  122  C   ALA A 322     2798   2566   2970    862      7    643       C
ATOM    123  O   ALA A 322      -0.872 -12.552  18.956  1.00 21.60           O
ANISOU  123  O   ALA A 322     2678   2674   2855    863     -3    639       O
ATOM    124  CB  ALA A 322       1.347 -11.100  17.716  1.00 22.10           C
ANISOU  124  CB  ALA A 322     2824   2603   2969    796     -7    773       C
ATOM    125  N   GLU A 323      -0.267 -11.260  20.715  1.00 19.92           N
ANISOU  125  N   GLU A 323     2612   2186   2772    856     19    559       N
ATOM    126  CA  GLU A 323      -0.529 -12.323  21.686  1.00 17.72           C
ANISOU  126  CA  GLU A 323     2328   1938   2468    840     25    467       C
ATOM    127  C   GLU A 323      -1.955 -12.895  21.563  1.00 22.13           C
ANISOU  127  C   GLU A 323     2797   2634   2976    897     40    478       C
ATOM    128  O   GLU A 323      -2.931 -12.142  21.421  1.00 21.03           O
ANISOU  128  O   GLU A 323     2626   2518   2847    967     57    523       O
ATOM    129  CB  GLU A 323      -0.265 -11.769  23.081  1.00 21.93           C
ANISOU  129  CB  GLU A 323     2943   2333   3057    834     39    387       C
ATOM    130  CG  GLU A 323      -0.253 -12.785  24.129  1.00 42.29           C
ANISOU  130  CG  GLU A 323     5533   4930   5604    807     47    303       C
ATOM    131  CD  GLU A 323       1.021 -13.625  24.172  1.00 23.88           C
ANISOU  131  CD  GLU A 323     3227   2586   3260    730     19    273       C
ATOM    132  OE1 GLU A 323       1.872 -13.690  23.187  1.00 22.89           O
ANISOU  132  OE1 GLU A 323     3089   2472   3136    696     -5    320       O
ATOM    133  OE2 GLU A 323       1.156 -14.188  25.255  1.00 26.48           O
ANISOU  133  OE2 GLU A 323     3588   2898   3573    711     25    206       O
ATOM    134  N   PRO A 324      -2.130 -14.220  21.588  1.00 21.36           N
ANISOU  134  N   PRO A 324     2653   2637   2827    872     33    443       N
ATOM    135  CA  PRO A 324      -3.517 -14.783  21.519  1.00 18.77           C
ANISOU  135  CA  PRO A 324     2222   2455   2455    918     44    453       C
ATOM    136  C   PRO A 324      -4.220 -14.606  22.848  1.00 21.70           C
ANISOU  136  C   PRO A 324     2616   2778   2851    957     88    404       C
ATOM    137  O   PRO A 324      -3.563 -14.374  23.870  1.00 19.37           O
ANISOU  137  O   PRO A 324     2417   2353   2589    936    103    344       O
ATOM    138  CB  PRO A 324      -3.296 -16.262  21.246  1.00 16.88           C
ANISOU  138  CB  PRO A 324     1935   2312   2167    867     22    416       C
ATOM    139  CG  PRO A 324      -1.948 -16.521  21.913  1.00 21.54           C
ANISOU  139  CG  PRO A 324     2638   2754   2790    805     23    354       C
ATOM    140  CD  PRO A 324      -1.113 -15.275  21.704  1.00 20.29           C
ANISOU  140  CD  PRO A 324     2546   2486   2677    808     16    393       C
ATOM    141  N   PRO A 325      -5.545 -14.719  22.877  1.00 21.32           N
ANISOU  141  N   PRO A 325     2471   2851   2778   1012    109    426       N
ATOM    142  CA  PRO A 325      -6.270 -14.615  24.144  1.00 19.03           C
ANISOU  142  CA  PRO A 325     2190   2541   2500   1057    163    382       C
ATOM    143  C   PRO A 325      -6.092 -15.874  24.981  1.00 16.76           C
ANISOU  143  C   PRO A 325     1908   2271   2188   1013    182    321       C
ATOM    144  O   PRO A 325      -5.734 -16.941  24.471  1.00 19.54           O
ANISOU  144  O   PRO A 325     2232   2676   2515    925    150    307       O
ATOM    145  CB  PRO A 325      -7.738 -14.460  23.690  1.00 20.00           C
ANISOU  145  CB  PRO A 325     2176   2825   2597   1121    175    439       C
ATOM    146  CG  PRO A 325      -7.819 -15.176  22.352  1.00 22.61           C
ANISOU  146  CG  PRO A 325     2402   3310   2877   1074    120    486       C
ATOM    147  CD  PRO A 325      -6.438 -14.955  21.716  1.00 23.07           C
ANISOU  147  CD  PRO A 325     2557   3260   2949   1028     82    493       C
ATOM    148  N   ILE A 326      -6.339 -15.721  26.276  1.00 16.82           N
ANISOU  148  N   ILE A 326     1964   2228   2197   1041    234    273       N
ATOM    149  CA  ILE A 326      -6.383 -16.863  27.196  1.00 21.52           C
ANISOU  149  CA  ILE A 326     2565   2853   2759    985    265    225       C
ATOM    150  C   ILE A 326      -7.767 -17.494  27.091  1.00 16.43           C
ANISOU  150  C   ILE A 326     1774   2384   2085    969    295    249       C
ATOM    151  O   ILE A 326      -8.770 -16.831  27.339  1.00 19.09           O
ANISOU  151  O   ILE A 326     2039   2793   2422   1077    343    275       O
ATOM    152  CB  ILE A 326      -6.049 -16.421  28.633  1.00 22.72           C
ANISOU  152  CB  ILE A 326     2827   2902   2903   1027    311    168       C
ATOM    153  CG1 ILE A 326      -4.580 -15.947  28.701  1.00 24.63           C
ANISOU  153  CG1 ILE A 326     3198   2989   3170    981    260    133       C
ATOM    154  CG2 ILE A 326      -6.330 -17.519  29.640  1.00 21.25           C
ANISOU  154  CG2 ILE A 326     2639   2772   2665    951    348    139       C
ATOM    155  CD1 ILE A 326      -4.208 -15.259  30.015  1.00 25.62           C
ANISOU  155  CD1 ILE A 326     3428   3026   3282    997    284     63       C
ATOM    156  N   LEU A 327      -7.827 -18.751  26.644  1.00 14.86           N
ANISOU  156  N   LEU A 327     1525   2256   1866    835    268    238       N
ATOM    157  CA  LEU A 327      -9.127 -19.394  26.436  1.00 16.13           C
ANISOU  157  CA  LEU A 327     1534   2593   2003    788    288    256       C
ATOM    158  C   LEU A 327      -9.588 -20.090  27.710  1.00 16.05           C
ANISOU  158  C   LEU A 327     1527   2596   1974    737    358    235       C
ATOM    159  O   LEU A 327      -8.803 -20.381  28.609  1.00 15.77           O
ANISOU  159  O   LEU A 327     1615   2441   1934    710    375    206       O
ATOM    160  CB  LEU A 327      -9.057 -20.410  25.291  1.00 15.18           C
ANISOU  160  CB  LEU A 327     1355   2541   1872    653    229    240       C
ATOM    161  CG  LEU A 327      -8.613 -19.825  23.947  1.00 17.65           C
ANISOU  161  CG  LEU A 327     1653   2876   2178    692    161    267       C
ATOM    162  CD1 LEU A 327      -8.788 -20.936  22.780  1.00 17.27           C
ANISOU  162  CD1 LEU A 327     1524   2945   2095    547    107    229       C
ATOM    163  CD2 LEU A 327      -9.398 -18.553  23.611  1.00 16.49           C
ANISOU  163  CD2 LEU A 327     1418   2819   2029    847    166    347       C
ATOM    164  N   TYR A 328     -10.874 -20.363  27.780  1.00 16.81           N
ANISOU  164  N   TYR A 328     1479   2855   2053    722    398    259       N
ATOM    165  CA  TYR A 328     -11.434 -21.078  28.920  1.00 17.98           C
ANISOU  165  CA  TYR A 328     1609   3044   2178    659    474    257       C
ATOM    166  C   TYR A 328     -11.820 -22.508  28.553  1.00 19.82           C
ANISOU  166  C   TYR A 328     1772   3340   2418    468    462    253       C
ATOM    167  O   TYR A 328     -12.035 -22.848  27.387  1.00 20.79           O
ANISOU  167  O   TYR A 328     1813   3535   2552    397    402    242       O
ATOM    168  CB  TYR A 328     -12.669 -20.346  29.456  1.00 19.86           C
ANISOU  168  CB  TYR A 328     1725   3426   2393    778    550    289       C
ATOM    169  CG  TYR A 328     -12.340 -19.092  30.176  1.00 25.85           C
ANISOU  169  CG  TYR A 328     2580   4093   3147    953    590    272       C
ATOM    170  CD1 TYR A 328     -11.897 -17.967  29.481  1.00 24.19           C
ANISOU  170  CD1 TYR A 328     2413   3805   2975   1077    545    277       C
ATOM    171  CD2 TYR A 328     -12.551 -18.998  31.567  1.00 25.21           C
ANISOU  171  CD2 TYR A 328     2544   4013   3021    995    681    250       C
ATOM    172  CE1 TYR A 328     -11.617 -16.791  30.170  1.00 30.65           C
ANISOU  172  CE1 TYR A 328     3343   4502   3801   1202    574    244       C
ATOM    173  CE2 TYR A 328     -12.271 -17.824  32.251  1.00 26.56           C
ANISOU  173  CE2 TYR A 328     2811   4098   3182   1152    721    208       C
ATOM    174  CZ  TYR A 328     -11.806 -16.748  31.547  1.00 28.32           C
ANISOU  174  CZ  TYR A 328     3100   4201   3460   1229    655    198       C
ATOM    175  OH  TYR A 328     -11.536 -15.633  32.271  1.00 35.29           O
ANISOU  175  OH  TYR A 328     4102   4961   4345   1310    671    141       O
ATOM    176  N   SER A 329     -11.957 -23.341  29.577  1.00 22.21           N
ANISOU  176  N   SER A 329     2107   3622   2711    382    525    261       N
ATOM    177  CA  SER A 329     -12.623 -24.619  29.394  1.00 23.29           C
ANISOU  177  CA  SER A 329     2156   3827   2864    199    539    267       C
ATOM    178  C   SER A 329     -14.151 -24.442  29.475  1.00 27.93           C
ANISOU  178  C   SER A 329     2541   4641   3431    200    593    304       C
ATOM    179  O   SER A 329     -14.664 -23.419  29.930  1.00 27.21           O
ANISOU  179  O   SER A 329     2393   4636   3308    355    639    330       O
ATOM    180  CB  SER A 329     -12.115 -25.618  30.435  1.00 24.72           C
ANISOU  180  CB  SER A 329     2459   3883   3051    104    588    286       C
ATOM    181  OG  SER A 329     -12.732 -26.854  30.233  1.00 25.79           O
ANISOU  181  OG  SER A 329     2525   4052   3221    -83    606    293       O
ATOM    182  N   GLU A 330     -14.904 -25.462  29.050  1.00 36.97           N
ANISOU  182  N   GLU A 330     3568   5884   4596     21    591    302       N
ATOM    183  CA  GLU A 330     -16.363 -25.300  29.000  1.00 35.85           C
ANISOU  183  CA  GLU A 330     3201   5987   4434     11    631    338       C
ATOM    184  C   GLU A 330     -16.999 -25.121  30.389  1.00 38.60           C
ANISOU  184  C   GLU A 330     3513   6405   4747     65    753    396       C
ATOM    185  O   GLU A 330     -16.559 -25.685  31.403  1.00 34.09           O
ANISOU  185  O   GLU A 330     3065   5718   4168     12    814    416       O
ATOM    186  CB  GLU A 330     -17.019 -26.485  28.288  1.00 51.62           C
ANISOU  186  CB  GLU A 330     5077   8076   6461   -224    601    313       C
ATOM    187  CG  GLU A 330     -17.342 -27.695  29.171  1.00 48.53           C
ANISOU  187  CG  GLU A 330     4699   7643   6098   -413    684    340       C
ATOM    188  CD  GLU A 330     -18.106 -28.781  28.409  1.00 60.78           C
ANISOU  188  CD  GLU A 330     6115   9290   7689   -659    655    303       C
ATOM    189  OE1 GLU A 330     -19.305 -28.977  28.702  1.00 60.83           O
ANISOU  189  OE1 GLU A 330     5932   9493   7688   -743    711    346       O
ATOM    190  OE2 GLU A 330     -17.513 -29.432  27.516  1.00 71.87           O
ANISOU  190  OE2 GLU A 330     7597  10580   9130   -772    578    222       O
ATOM    191  N   TYR A 331     -18.056 -24.321  30.435  1.00 32.10           N
ANISOU  191  N   TYR A 331     2514   5788   3896    183    794    429       N
ATOM    192  CA  TYR A 331     -18.836 -24.259  31.645  1.00 37.66           C
ANISOU  192  CA  TYR A 331     3171   6575   4563    213    906    469       C
ATOM    193  C   TYR A 331     -20.068 -25.181  31.586  1.00 43.88           C
ANISOU  193  C   TYR A 331     3795   7508   5368     25    925    495       C
ATOM    194  O   TYR A 331     -21.195 -24.731  31.367  1.00 48.33           O
ANISOU  194  O   TYR A 331     4219   8218   5926     77    914    503       O
ATOM    195  CB  TYR A 331     -19.245 -22.825  31.935  1.00 37.94           C
ANISOU  195  CB  TYR A 331     3209   6632   4573    453    917    461       C
ATOM    196  CG  TYR A 331     -18.149 -22.010  32.614  1.00 38.26           C
ANISOU  196  CG  TYR A 331     3443   6507   4589    615    942    430       C
ATOM    197  CD1 TYR A 331     -18.025 -21.972  34.006  1.00 39.45           C
ANISOU  197  CD1 TYR A 331     3687   6621   4683    652   1039    428       C
ATOM    198  CD2 TYR A 331     -17.261 -21.257  31.861  1.00 31.91           C
ANISOU  198  CD2 TYR A 331     2730   5584   3812    724    865    400       C
ATOM    199  CE1 TYR A 331     -17.020 -21.211  34.615  1.00 33.57           C
ANISOU  199  CE1 TYR A 331     3124   5725   3906    787   1048    382       C
ATOM    200  CE2 TYR A 331     -16.268 -20.486  32.471  1.00 30.76           C
ANISOU  200  CE2 TYR A 331     2765   5272   3650    856    880    361       C
ATOM    201  CZ  TYR A 331     -16.162 -20.450  33.846  1.00 32.78           C
ANISOU  201  CZ  TYR A 331     3112   5497   3847    886    967    344       C
ATOM    202  OH  TYR A 331     -15.140 -19.690  34.426  1.00 31.37           O
ANISOU  202  OH  TYR A 331     3118   5154   3645    997    966    287       O
ATOM    203  N   PHE A 337     -16.965 -31.231  35.894  1.00 55.68           N
ANISOU  203  N   PHE A 337     6049   8171   6936   -748   1216    794       N
ATOM    204  CA  PHE A 337     -15.593 -31.726  35.836  1.00 52.33           C
ANISOU  204  CA  PHE A 337     5846   7484   6555   -740   1152    785       C
ATOM    205  C   PHE A 337     -15.454 -33.030  36.620  1.00 46.87           C
ANISOU  205  C   PHE A 337     5250   6659   5899   -895   1225    906       C
ATOM    206  O   PHE A 337     -16.085 -33.197  37.661  1.00 55.45           O
ANISOU  206  O   PHE A 337     6289   7857   6922   -928   1335   1018       O
ATOM    207  CB  PHE A 337     -14.593 -30.694  36.397  1.00 52.15           C
ANISOU  207  CB  PHE A 337     5954   7421   6441   -510   1122    764       C
ATOM    208  CG  PHE A 337     -13.162 -31.203  36.438  1.00 54.72           C
ANISOU  208  CG  PHE A 337     6486   7504   6801   -494   1058    769       C
ATOM    209  CD1 PHE A 337     -12.355 -31.138  35.298  1.00 41.41           C
ANISOU  209  CD1 PHE A 337     4858   5688   5189   -474    949    671       C
ATOM    210  CD2 PHE A 337     -12.648 -31.798  37.597  1.00 49.86           C
ANISOU  210  CD2 PHE A 337     5996   6808   6141   -501   1112    884       C
ATOM    211  CE1 PHE A 337     -11.061 -31.631  35.317  1.00 40.72           C
ANISOU  211  CE1 PHE A 337     4940   5394   5138   -452    898    678       C
ATOM    212  CE2 PHE A 337     -11.360 -32.295  37.621  1.00 43.84           C
ANISOU  212  CE2 PHE A 337     5404   5839   5416   -476   1052    901       C
ATOM    213  CZ  PHE A 337     -10.563 -32.205  36.478  1.00 39.72           C
ANISOU  213  CZ  PHE A 337     4928   5188   4975   -448    947    793       C
ATOM    214  N   SER A 338     -14.601 -33.928  36.116  1.00 48.50           N
ANISOU  214  N   SER A 338     5595   6624   6207   -977   1168    889       N
ATOM    215  CA  SER A 338     -14.284 -35.196  36.775  1.00 41.42           C
ANISOU  215  CA  SER A 338     4822   5545   5368  -1103   1228   1012       C
ATOM    216  C   SER A 338     -12.981 -35.722  36.178  1.00 47.54           C
ANISOU  216  C   SER A 338     5776   6054   6234  -1078   1141    961       C
ATOM    217  O   SER A 338     -12.493 -35.220  35.161  1.00 43.29           O
ANISOU  217  O   SER A 338     5240   5490   5718  -1006   1044    825       O
ATOM    218  CB  SER A 338     -15.383 -36.248  36.569  1.00 43.90           C
ANISOU  218  CB  SER A 338     5030   5871   5779  -1363   1298   1053       C
ATOM    219  OG  SER A 338     -15.374 -36.623  35.192  1.00 42.65           O
ANISOU  219  OG  SER A 338     4848   5623   5735  -1473   1214    910       O
ATOM    220  N   GLU A 339     -12.446 -36.779  36.796  1.00 43.43           N
ANISOU  220  N   GLU A 339     5398   5337   5768  -1137   1185   1080       N
ATOM    221  CA  GLU A 339     -11.206 -37.358  36.290  1.00 45.63           C
ANISOU  221  CA  GLU A 339     5840   5358   6140  -1099   1116   1042       C
ATOM    222  C   GLU A 339     -11.414 -37.941  34.895  1.00 43.66           C
ANISOU  222  C   GLU A 339     5561   5002   6028  -1244   1069    895       C
ATOM    223  O   GLU A 339     -10.539 -37.805  34.027  1.00 42.38           O
ANISOU  223  O   GLU A 339     5464   4736   5902  -1166    983    778       O
ATOM    224  CB  GLU A 339     -10.672 -38.416  37.267  1.00 50.77           C
ANISOU  224  CB  GLU A 339     6642   5820   6830  -1124   1180   1221       C
ATOM    225  N   ALA A 340     -12.597 -38.540  34.650  1.00 41.37           N
ANISOU  225  N   ALA A 340     5159   4761   5800  -1462   1125    891       N
ATOM    226  CA  ALA A 340     -12.894 -39.207  33.379  1.00 41.83           C
ANISOU  226  CA  ALA A 340     5186   4726   5981  -1636   1085    742       C
ATOM    227  C   ALA A 340     -13.009 -38.246  32.183  1.00 43.48           C
ANISOU  227  C   ALA A 340     5278   5104   6137  -1571    982    564       C
ATOM    228  O   ALA A 340     -12.704 -38.633  31.047  1.00 42.17           O
ANISOU  228  O   ALA A 340     5143   4837   6044  -1633    919    418       O
ATOM    229  CB  ALA A 340     -14.184 -40.001  33.521  1.00 38.74           C
ANISOU  229  CB  ALA A 340     4683   4380   5655  -1894   1167    789       C
ATOM    230  N   SER A 341     -13.474 -37.014  32.389  1.00 37.70           N
ANISOU  230  N   SER A 341     4413   4630   5280  -1446    969    572       N
ATOM    231  CA  SER A 341     -13.618 -36.071  31.277  1.00 34.78           C
ANISOU  231  CA  SER A 341     3931   4423   4860  -1373    875    432       C
ATOM    232  C   SER A 341     -12.392 -35.175  31.105  1.00 31.93           C
ANISOU  232  C   SER A 341     3676   4014   4444  -1140    802    395       C
ATOM    233  O   SER A 341     -12.318 -34.380  30.167  1.00 31.97           O
ANISOU  233  O   SER A 341     3615   4123   4410  -1063    723    294       O
ATOM    234  CB  SER A 341     -14.939 -35.303  31.473  1.00 37.30           C
ANISOU  234  CB  SER A 341     4030   5043   5099  -1382    907    461       C
ATOM    235  OG  SER A 341     -14.846 -34.343  32.509  1.00 41.64           O
ANISOU  235  OG  SER A 341     4582   5696   5544  -1192    948    554       O
ATOM    236  N   MET A 342     -11.390 -35.331  31.957  1.00 28.02           N
ANISOU  236  N   MET A 342     3339   3362   3944  -1036    823    480       N
ATOM    237  CA  MET A 342     -10.202 -34.477  31.896  1.00 26.39           C
ANISOU  237  CA  MET A 342     3223   3119   3685   -829    755    451       C
ATOM    238  C   MET A 342      -9.492 -34.409  30.541  1.00 29.94           C
ANISOU  238  C   MET A 342     3701   3499   4176   -805    664    311       C
ATOM    239  O   MET A 342      -9.243 -33.313  29.995  1.00 27.83           O
ANISOU  239  O   MET A 342     3389   3341   3846   -681    601    252       O
ATOM    240  CB  MET A 342      -9.245 -34.912  32.975  1.00 34.24           C
ANISOU  240  CB  MET A 342     4376   3955   4680   -756    787    566       C
ATOM    241  CG  MET A 342      -7.979 -34.069  33.052  1.00 38.43           C
ANISOU  241  CG  MET A 342     4992   4458   5153   -558    718    546       C
ATOM    242  SD  MET A 342      -7.058 -34.693  34.450  1.00 44.30           S
ANISOU  242  SD  MET A 342     5889   5063   5881   -492    757    705       S
ATOM    243  CE  MET A 342      -5.572 -33.717  34.348  1.00 45.27           C
ANISOU  243  CE  MET A 342     6084   5172   5946   -290    660    654       C
ATOM    244  N   MET A 343      -9.162 -35.553  29.932  1.00 26.91           N
ANISOU  244  N   MET A 343     3393   2935   3897   -922    661    253       N
ATOM    245  CA  MET A 343      -8.492 -35.458  28.626  1.00 27.40           C
ANISOU  245  CA  MET A 343     3476   2956   3977   -892    583    110       C
ATOM    246  C   MET A 343      -9.362 -34.854  27.538  1.00 25.88           C
ANISOU  246  C   MET A 343     3123   2975   3735   -946    531      5       C
ATOM    247  O   MET A 343      -8.834 -34.170  26.648  1.00 25.44           O
ANISOU  247  O   MET A 343     3056   2975   3634   -851    461    -74       O
ATOM    248  CB  MET A 343      -7.914 -36.771  28.060  1.00 32.54           C
ANISOU  248  CB  MET A 343     4247   3370   4749   -990    591     36       C
ATOM    249  CG  MET A 343      -6.746 -37.466  28.773  1.00 37.60           C
ANISOU  249  CG  MET A 343     5061   3768   5458   -905    623    119       C
ATOM    250  SD  MET A 343      -5.425 -36.171  28.692  1.00 42.71           S
ANISOU  250  SD  MET A 343     5734   4486   6009   -653    545    116       S
ATOM    251  CE  MET A 343      -5.055 -36.135  26.941  1.00 33.76           C
ANISOU  251  CE  MET A 343     4575   3365   4887   -669    480    -80       C
ATOM    252  N   GLY A 344     -10.669 -35.142  27.562  1.00 29.01           N
ANISOU  252  N   GLY A 344     3390   3495   4136  -1102    564     10       N
ATOM    253  CA  GLY A 344     -11.575 -34.523  26.607  1.00 31.69           C
ANISOU  253  CA  GLY A 344     3552   4072   4415  -1142    509    -69       C
ATOM    254  C   GLY A 344     -11.541 -33.010  26.704  1.00 27.65           C
ANISOU  254  C   GLY A 344     2971   3735   3801   -938    475    -23       C
ATOM    255  O   GLY A 344     -11.496 -32.325  25.688  1.00 25.92           O
ANISOU  255  O   GLY A 344     2686   3633   3530   -879    403    -92       O
ATOM    256  N   LEU A 345     -11.573 -32.468  27.940  1.00 25.64           N
ANISOU  256  N   LEU A 345     2733   3496   3512   -829    532     95       N
ATOM    257  CA  LEU A 345     -11.521 -31.007  28.136  1.00 25.59           C
ANISOU  257  CA  LEU A 345     2680   3621   3420   -631    511    130       C
ATOM    258  C   LEU A 345     -10.192 -30.419  27.663  1.00 24.26           C
ANISOU  258  C   LEU A 345     2628   3349   3239   -489    445     90       C
ATOM    259  O   LEU A 345     -10.162 -29.372  26.990  1.00 21.54           O
ANISOU  259  O   LEU A 345     2226   3112   2847   -382    392     65       O
ATOM    260  CB  LEU A 345     -11.734 -30.685  29.620  1.00 24.38           C
ANISOU  260  CB  LEU A 345     2548   3486   3230   -557    592    242       C
ATOM    261  CG  LEU A 345     -13.092 -31.073  30.171  1.00 24.53           C
ANISOU  261  CG  LEU A 345     2429   3647   3246   -677    671    300       C
ATOM    262  CD1 LEU A 345     -13.067 -30.778  31.695  1.00 29.86           C
ANISOU  262  CD1 LEU A 345     3156   4324   3864   -586    758    408       C
ATOM    263  CD2 LEU A 345     -14.212 -30.302  29.494  1.00 28.69           C
ANISOU  263  CD2 LEU A 345     2748   4422   3730   -658    648    271       C
ATOM    264  N   LEU A 346      -9.076 -31.107  27.963  1.00 20.30           N
ANISOU  264  N   LEU A 346     2285   2640   2786   -488    449     92       N
ATOM    265  CA  LEU A 346      -7.765 -30.614  27.568  1.00 20.46           C
ANISOU  265  CA  LEU A 346     2405   2571   2798   -363    393     59       C
ATOM    266  C   LEU A 346      -7.618 -30.658  26.064  1.00 18.51           C
ANISOU  266  C   LEU A 346     2118   2360   2554   -401    329    -48       C
ATOM    267  O   LEU A 346      -7.017 -29.750  25.466  1.00 16.11           O
ANISOU  267  O   LEU A 346     1814   2096   2209   -289    277    -68       O
ATOM    268  CB  LEU A 346      -6.651 -31.445  28.241  1.00 22.21           C
ANISOU  268  CB  LEU A 346     2784   2581   3073   -352    414     94       C
ATOM    269  CG  LEU A 346      -6.638 -31.212  29.755  1.00 21.93           C
ANISOU  269  CG  LEU A 346     2794   2539   3000   -288    466    209       C
ATOM    270  CD1 LEU A 346      -5.670 -32.169  30.476  1.00 21.50           C
ANISOU  270  CD1 LEU A 346     2880   2295   2993   -285    488    271       C
ATOM    271  CD2 LEU A 346      -6.196 -29.779  30.053  1.00 25.01           C
ANISOU  271  CD2 LEU A 346     3183   3008   3312   -125    433    219       C
ATOM    272  N   THR A 347      -8.202 -31.692  25.444  1.00 18.40           N
ANISOU  272  N   THR A 347     2066   2342   2584   -567    334   -119       N
ATOM    273  CA  THR A 347      -8.133 -31.813  24.008  1.00 19.22           C
ANISOU  273  CA  THR A 347     2129   2504   2671   -618    274   -237       C
ATOM    274  C   THR A 347      -8.925 -30.698  23.360  1.00 21.76           C
ANISOU  274  C   THR A 347     2295   3069   2904   -567    225   -231       C
ATOM    275  O   THR A 347      -8.447 -30.071  22.393  1.00 18.74           O
ANISOU  275  O   THR A 347     1899   2752   2469   -493    167   -270       O
ATOM    276  CB  THR A 347      -8.657 -33.190  23.576  1.00 25.61           C
ANISOU  276  CB  THR A 347     2936   3252   3545   -825    293   -331       C
ATOM    277  OG1 THR A 347      -7.721 -34.178  24.045  1.00 28.29           O
ANISOU  277  OG1 THR A 347     3440   3333   3975   -836    336   -333       O
ATOM    278  CG2 THR A 347      -8.766 -33.307  22.058  1.00 28.66           C
ANISOU  278  CG2 THR A 347     3260   3743   3887   -896    227   -474       C
ATOM    279  N   ASN A 348     -10.153 -30.477  23.860  1.00 21.07           N
ANISOU  279  N   ASN A 348     2081   3125   2800   -606    254   -174       N
ATOM    280  CA  ASN A 348     -11.009 -29.442  23.303  1.00 28.06           C
ANISOU  280  CA  ASN A 348     2802   4250   3609   -544    213   -151       C
ATOM    281  C   ASN A 348     -10.328 -28.085  23.416  1.00 21.80           C
ANISOU  281  C   ASN A 348     2052   3455   2776   -331    193    -87       C
ATOM    282  O   ASN A 348     -10.305 -27.319  22.446  1.00 20.21           O
ANISOU  282  O   ASN A 348     1789   3369   2520   -260    134    -94       O
ATOM    283  CB  ASN A 348     -12.348 -29.430  24.021  1.00 23.36           C
ANISOU  283  CB  ASN A 348     2067   3796   3012   -597    263    -88       C
ATOM    284  CG  ASN A 348     -13.313 -28.403  23.458  1.00 30.07           C
ANISOU  284  CG  ASN A 348     2728   4907   3790   -518    224    -54       C
ATOM    285  OD1 ASN A 348     -13.323 -27.244  23.883  1.00 25.19           O
ANISOU  285  OD1 ASN A 348     2096   4333   3144   -336    238     24       O
ATOM    286  ND2 ASN A 348     -14.217 -28.857  22.642  1.00 34.18           N
ANISOU  286  ND2 ASN A 348     3097   5602   4287   -658    183   -108       N
ATOM    287  N   LEU A 349      -9.720 -27.811  24.575  1.00 20.40           N
ANISOU  287  N   LEU A 349     1986   3140   2624   -239    241    -26       N
ATOM    288  CA  LEU A 349      -8.976 -26.573  24.785  1.00 21.11           C
ANISOU  288  CA  LEU A 349     2137   3196   2689    -59    227     20       C
ATOM    289  C   LEU A 349      -7.810 -26.450  23.795  1.00 19.75           C
ANISOU  289  C   LEU A 349     2039   2952   2512    -28    167    -28       C
ATOM    290  O   LEU A 349      -7.633 -25.405  23.147  1.00 14.84           O
ANISOU  290  O   LEU A 349     1386   2399   1853     75    127     -6       O
ATOM    291  CB  LEU A 349      -8.460 -26.525  26.230  1.00 17.76           C
ANISOU  291  CB  LEU A 349     1827   2639   2284     -1    283     71       C
ATOM    292  CG  LEU A 349      -7.551 -25.349  26.657  1.00 17.66           C
ANISOU  292  CG  LEU A 349     1901   2555   2253    159    271    100       C
ATOM    293  CD1 LEU A 349      -8.328 -24.046  26.548  1.00 15.16           C
ANISOU  293  CD1 LEU A 349     1490   2369   1902    277    274    135       C
ATOM    294  CD2 LEU A 349      -7.032 -25.582  28.116  1.00 17.24           C
ANISOU  294  CD2 LEU A 349     1960   2388   2202    181    319    135       C
ATOM    295  N   ALA A 350      -6.975 -27.496  23.684  1.00 17.29           N
ANISOU  295  N   ALA A 350     1829   2498   2243   -106    168    -86       N
ATOM    296  CA  ALA A 350      -5.840 -27.398  22.777  1.00 19.25           C
ANISOU  296  CA  ALA A 350     2140   2693   2483    -69    124   -133       C
ATOM    297  C   ALA A 350      -6.296 -27.151  21.327  1.00 16.79           C
ANISOU  297  C   ALA A 350     1722   2551   2108    -98     70   -180       C
ATOM    298  O   ALA A 350      -5.694 -26.337  20.599  1.00 17.31           O
ANISOU  298  O   ALA A 350     1789   2657   2131    -12     33   -164       O
ATOM    299  CB  ALA A 350      -4.984 -28.660  22.885  1.00 15.80           C
ANISOU  299  CB  ALA A 350     1815   2081   2106   -140    144   -193       C
ATOM    300  N   ASP A 351      -7.386 -27.804  20.908  1.00 18.40           N
ANISOU  300  N   ASP A 351     1824   2871   2296   -224     64   -230       N
ATOM    301  CA  ASP A 351      -7.876 -27.626  19.550  1.00 17.27           C
ANISOU  301  CA  ASP A 351     1568   2921   2073   -261      3   -278       C
ATOM    302  C   ASP A 351      -8.363 -26.202  19.288  1.00 20.97           C
ANISOU  302  C   ASP A 351     1935   3556   2479   -126    -28   -174       C
ATOM    303  O   ASP A 351      -8.053 -25.624  18.228  1.00 21.48           O
ANISOU  303  O   ASP A 351     1969   3718   2474    -73    -78   -166       O
ATOM    304  CB  ASP A 351      -8.984 -28.644  19.283  1.00 25.59           C
ANISOU  304  CB  ASP A 351     2526   4071   3126   -443      0   -358       C
ATOM    305  CG  ASP A 351      -8.422 -30.067  19.122  1.00 26.18           C
ANISOU  305  CG  ASP A 351     2711   3975   3260   -583     22   -486       C
ATOM    306  OD1 ASP A 351      -7.174 -30.231  19.019  1.00 32.99           O
ANISOU  306  OD1 ASP A 351     3705   4683   4148   -522     32   -515       O
ATOM    307  OD2 ASP A 351      -9.220 -30.982  19.067  1.00 28.45           O
ANISOU  307  OD2 ASP A 351     2949   4288   3573   -748     31   -556       O
ATOM    308  N   ARG A 352      -9.075 -25.594  20.256  1.00 16.93           N
ANISOU  308  N   ARG A 352     1375   3068   1991    -56      7    -86       N
ATOM    309  CA  ARG A 352      -9.469 -24.194  20.097  1.00 19.71           C
ANISOU  309  CA  ARG A 352     1650   3536   2305    100    -10     17       C
ATOM    310  C   ARG A 352      -8.255 -23.268  20.146  1.00 16.53           C
ANISOU  310  C   ARG A 352     1370   2995   1916    233    -12     65       C
ATOM    311  O   ARG A 352      -8.211 -22.268  19.418  1.00 17.33           O
ANISOU  311  O   ARG A 352     1432   3176   1977    334    -46    131       O
ATOM    312  CB  ARG A 352     -10.478 -23.803  21.180  1.00 17.42           C
ANISOU  312  CB  ARG A 352     1287   3290   2041    153     43     83       C
ATOM    313  CG  ARG A 352     -11.915 -24.217  20.767  1.00 19.41           C
ANISOU  313  CG  ARG A 352     1344   3775   2255     60     26     75       C
ATOM    314  CD  ARG A 352     -12.883 -23.767  21.862  1.00 24.57           C
ANISOU  314  CD  ARG A 352     1916   4486   2933    131     92    147       C
ATOM    315  NE  ARG A 352     -12.728 -24.529  23.096  1.00 21.13           N
ANISOU  315  NE  ARG A 352     1572   3904   2552     54    167    124       N
ATOM    316  CZ  ARG A 352     -12.401 -24.042  24.290  1.00 22.48           C
ANISOU  316  CZ  ARG A 352     1839   3953   2750    159    232    166       C
ATOM    317  NH1 ARG A 352     -12.164 -22.746  24.441  1.00 18.63           N
ANISOU  317  NH1 ARG A 352     1379   3444   2255    344    236    219       N
ATOM    318  NH2 ARG A 352     -12.314 -24.859  25.358  1.00 19.44           N
ANISOU  318  NH2 ARG A 352     1526   3465   2398     73    296    156       N
ATOM    319  N   GLU A 353      -7.229 -23.609  20.922  1.00 16.28           N
ANISOU  319  N   GLU A 353     1482   2764   1940    228     21     38       N
ATOM    320  CA  GLU A 353      -6.051 -22.738  21.005  1.00 16.05           C
ANISOU  320  CA  GLU A 353     1558   2613   1928    334     17     77       C
ATOM    321  C   GLU A 353      -5.225 -22.786  19.715  1.00 17.23           C
ANISOU  321  C   GLU A 353     1720   2792   2035    316    -28     51       C
ATOM    322  O   GLU A 353      -4.612 -21.783  19.316  1.00 14.74           O
ANISOU  322  O   GLU A 353     1429   2462   1709    406    -44    113       O
ATOM    323  CB  GLU A 353      -5.157 -23.182  22.152  1.00 14.38           C
ANISOU  323  CB  GLU A 353     1478   2212   1773    323     54     53       C
ATOM    324  CG  GLU A 353      -5.714 -22.882  23.584  1.00 16.14           C
ANISOU  324  CG  GLU A 353     1716   2396   2020    370    106     91       C
ATOM    325  CD  GLU A 353      -4.585 -23.149  24.542  1.00 21.53           C
ANISOU  325  CD  GLU A 353     2532   2911   2737    375    123     78       C
ATOM    326  OE1 GLU A 353      -4.518 -24.341  24.932  1.00 15.24           O
ANISOU  326  OE1 GLU A 353     1767   2062   1960    285    143     47       O
ATOM    327  OE2 GLU A 353      -3.775 -22.221  24.874  1.00 20.33           O
ANISOU  327  OE2 GLU A 353     2450   2682   2593    460    114    102       O
ATOM    328  N   LEU A 354      -5.282 -23.904  19.006  1.00 14.58           N
ANISOU  328  N   LEU A 354     1361   2508   1672    198    -45    -41       N
ATOM    329  CA  LEU A 354      -4.530 -24.005  17.761  1.00 14.16           C
ANISOU  329  CA  LEU A 354     1315   2504   1561    182    -79    -80       C
ATOM    330  C   LEU A 354      -4.982 -22.965  16.761  1.00 18.06           C
ANISOU  330  C   LEU A 354     1712   3180   1972    252   -122      2       C
ATOM    331  O   LEU A 354      -4.153 -22.374  16.073  1.00 20.51           O
ANISOU  331  O   LEU A 354     2050   3496   2247    306   -135     43       O
ATOM    332  CB  LEU A 354      -4.650 -25.421  17.174  1.00 18.77           C
ANISOU  332  CB  LEU A 354     1893   3115   2125     39    -84   -218       C
ATOM    333  CG  LEU A 354      -3.785 -25.658  15.926  1.00 16.21           C
ANISOU  333  CG  LEU A 354     1588   2839   1732     22   -105   -286       C
ATOM    334  CD1 LEU A 354      -2.317 -25.617  16.346  1.00 17.38           C
ANISOU  334  CD1 LEU A 354     1858   2806   1941     85    -72   -277       C
ATOM    335  CD2 LEU A 354      -4.136 -26.967  15.312  1.00 21.77           C
ANISOU  335  CD2 LEU A 354     2277   3586   2409   -120   -110   -439       C
ATOM    336  N   VAL A 355      -6.307 -22.726  16.657  1.00 17.87           N
ANISOU  336  N   VAL A 355     1561   3317   1912    254   -142     41       N
ATOM    337  CA  VAL A 355      -6.811 -21.719  15.733  1.00 18.02           C
ANISOU  337  CA  VAL A 355     1476   3520   1850    340   -187    144       C
ATOM    338  C   VAL A 355      -6.128 -20.384  15.990  1.00 15.94           C
ANISOU  338  C   VAL A 355     1283   3143   1629    488   -168    269       C
ATOM    339  O   VAL A 355      -5.728 -19.674  15.061  1.00 18.22           O
ANISOU  339  O   VAL A 355     1561   3499   1862    545   -194    347       O
ATOM    340  CB  VAL A 355      -8.341 -21.583  15.873  1.00 21.14           C
ANISOU  340  CB  VAL A 355     1719   4090   2225    348   -203    185       C
ATOM    341  CG1 VAL A 355      -8.803 -20.622  14.877  1.00 28.13           C
ANISOU  341  CG1 VAL A 355     2495   5170   3024    446   -253    301       C
ATOM    342  CG2 VAL A 355      -9.034 -22.941  15.698  1.00 24.68           C
ANISOU  342  CG2 VAL A 355     2095   4638   2645    171   -219     53       C
ATOM    343  N   HIS A 356      -6.119 -19.968  17.248  1.00 16.70           N
ANISOU  343  N   HIS A 356     1444   3083   1820    549   -121    295       N
ATOM    344  CA  HIS A 356      -5.516 -18.696  17.645  1.00 17.07           C
ANISOU  344  CA  HIS A 356     1570   2994   1924    675    -99    392       C
ATOM    345  C   HIS A 356      -4.012 -18.722  17.493  1.00 16.08           C
ANISOU  345  C   HIS A 356     1560   2732   1817    646    -95    368       C
ATOM    346  O   HIS A 356      -3.400 -17.671  17.259  1.00 16.30           O
ANISOU  346  O   HIS A 356     1631   2697   1865    721    -93    456       O
ATOM    347  CB  HIS A 356      -5.857 -18.350  19.109  1.00 14.48           C
ANISOU  347  CB  HIS A 356     1289   2535   1678    733    -47    392       C
ATOM    348  CG  HIS A 356      -7.300 -18.027  19.295  1.00 23.79           C
ANISOU  348  CG  HIS A 356     2346   3848   2847    799    -37    440       C
ATOM    349  ND1 HIS A 356      -7.819 -16.783  19.001  1.00 23.10           N
ANISOU  349  ND1 HIS A 356     2224   3789   2765    926    -34    548       N
ATOM    350  CD2 HIS A 356      -8.344 -18.794  19.693  1.00 23.66           C
ANISOU  350  CD2 HIS A 356     2234   3939   2816    739    -25    395       C
ATOM    351  CE1 HIS A 356      -9.132 -16.805  19.183  1.00 25.36           C
ANISOU  351  CE1 HIS A 356     2399   4202   3034    946    -22    561       C
ATOM    352  NE2 HIS A 356      -9.474 -18.003  19.635  1.00 22.46           N
ANISOU  352  NE2 HIS A 356     1963   3915   2656    855    -19    482       N
ATOM    353  N   MET A 357      -3.396 -19.897  17.641  1.00 15.06           N
ANISOU  353  N   MET A 357     1479   2551   1691    542    -89    256       N
ATOM    354  CA  MET A 357      -1.962 -20.001  17.390  1.00 15.98           C
ANISOU  354  CA  MET A 357     1681   2573   1820    521    -85    233       C
ATOM    355  C   MET A 357      -1.602 -19.661  15.941  1.00 17.60           C
ANISOU  355  C   MET A 357     1840   2909   1939    526   -112    279       C
ATOM    356  O   MET A 357      -0.614 -18.955  15.707  1.00 16.50           O
ANISOU  356  O   MET A 357     1747   2708   1814    561   -104    340       O
ATOM    357  CB  MET A 357      -1.430 -21.384  17.790  1.00 12.46           C
ANISOU  357  CB  MET A 357     1288   2049   1397    428    -70    110       C
ATOM    358  CG  MET A 357       0.102 -21.433  17.860  1.00 15.20           C
ANISOU  358  CG  MET A 357     1719   2279   1777    431    -58     95       C
ATOM    359  SD  MET A 357       0.606 -23.196  17.909  1.00 15.89           S
ANISOU  359  SD  MET A 357     1847   2311   1881    340    -39    -46       S
ATOM    360  CE  MET A 357      -0.060 -23.571  19.543  1.00 14.41           C
ANISOU  360  CE  MET A 357     1702   2005   1768    332    -17    -47       C
ATOM    361  N   ILE A 358      -2.412 -20.097  14.972  1.00 18.29           N
ANISOU  361  N   ILE A 358     1829   3191   1930    487   -144    256       N
ATOM    362  CA  ILE A 358      -2.136 -19.778  13.569  1.00 17.34           C
ANISOU  362  CA  ILE A 358     1659   3230   1700    494   -171    305       C
ATOM    363  C   ILE A 358      -2.207 -18.269  13.381  1.00 22.14           C
ANISOU  363  C   ILE A 358     2254   3840   2316    611   -174    484       C
ATOM    364  O   ILE A 358      -1.320 -17.654  12.770  1.00 20.64           O
ANISOU  364  O   ILE A 358     2094   3642   2105    636   -166    562       O
ATOM    365  CB  ILE A 358      -3.142 -20.491  12.646  1.00 21.52           C
ANISOU  365  CB  ILE A 358     2074   3992   2109    427   -215    242       C
ATOM    366  CG1 ILE A 358      -3.133 -22.012  12.837  1.00 33.75           C
ANISOU  366  CG1 ILE A 358     3647   5508   3667    299   -206     55       C
ATOM    367  CG2 ILE A 358      -3.172 -19.906  11.191  1.00 28.74           C
ANISOU  367  CG2 ILE A 358     2911   5129   2879    459   -254    333       C
ATOM    368  CD1 ILE A 358      -1.939 -22.641  12.589  1.00 27.05           C
ANISOU  368  CD1 ILE A 358     2880   4576   2822    260   -177    -34       C
ATOM    369  N   ASN A 359      -3.266 -17.644  13.925  1.00 21.27           N
ANISOU  369  N   ASN A 359     2101   3734   2247    687   -179    556       N
ATOM    370  CA  ASN A 359      -3.411 -16.183  13.816  1.00 20.31           C
ANISOU  370  CA  ASN A 359     1996   3558   2165    792   -162    709       C
ATOM    371  C   ASN A 359      -2.229 -15.443  14.404  1.00 22.72           C
ANISOU  371  C   ASN A 359     2426   3634   2572    811   -122    740       C
ATOM    372  O   ASN A 359      -1.757 -14.447  13.812  1.00 20.89           O
ANISOU  372  O   ASN A 359     2227   3359   2351    829   -105    835       O
ATOM    373  CB  ASN A 359      -4.675 -15.701  14.490  1.00 26.63           C
ANISOU  373  CB  ASN A 359     2763   4338   3018    849   -145    731       C
ATOM    374  CG  ASN A 359      -5.884 -16.047  13.717  1.00 40.94           C
ANISOU  374  CG  ASN A 359     4441   6382   4731    835   -180    738       C
ATOM    375  OD1 ASN A 359      -5.784 -16.608  12.610  1.00 34.56           O
ANISOU  375  OD1 ASN A 359     3572   5752   3809    773   -220    718       O
ATOM    376  ND2 ASN A 359      -7.062 -15.735  14.284  1.00 37.95           N
ANISOU  376  ND2 ASN A 359     4012   6019   4388    886   -165    757       N
ATOM    377  N   TRP A 360      -1.757 -15.898  15.569  1.00 19.93           N
ANISOU  377  N   TRP A 360     2141   3136   2295    797   -106    658       N
ATOM    378  CA  TRP A 360      -0.565 -15.324  16.198  1.00 22.65           C
ANISOU  378  CA  TRP A 360     2599   3278   2730    792    -77    664       C
ATOM    379  C   TRP A 360       0.669 -15.539  15.320  1.00 21.07           C
ANISOU  379  C   TRP A 360     2409   3111   2484    731    -80    672       C
ATOM    380  O   TRP A 360       1.463 -14.616  15.101  1.00 18.74           O
ANISOU  380  O   TRP A 360     2156   2737   2226    745    -65    762       O
ATOM    381  CB  TRP A 360      -0.348 -15.925  17.599  1.00 18.27           C
ANISOU  381  CB  TRP A 360     2112   2585   2244    758    -59    548       C
ATOM    382  CG  TRP A 360       1.070 -15.792  18.153  1.00 17.69           C
ANISOU  382  CG  TRP A 360     2133   2357   2232    716    -47    517       C
ATOM    383  CD1 TRP A 360       1.612 -14.707  18.784  1.00 16.49           C
ANISOU  383  CD1 TRP A 360     2058   2048   2160    732    -33    548       C
ATOM    384  CD2 TRP A 360       2.112 -16.775  18.089  1.00 15.39           C
ANISOU  384  CD2 TRP A 360     1859   2064   1927    635    -51    435       C
ATOM    385  NE1 TRP A 360       2.933 -14.958  19.129  1.00 16.49           N
ANISOU  385  NE1 TRP A 360     2108   1968   2190    678    -35    510       N
ATOM    386  CE2 TRP A 360       3.269 -16.214  18.704  1.00 17.98           C
ANISOU  386  CE2 TRP A 360     2258   2253   2323    621    -44    442       C
ATOM    387  CE3 TRP A 360       2.184 -18.091  17.570  1.00 15.92           C
ANISOU  387  CE3 TRP A 360     1887   2228   1934    576    -57    349       C
ATOM    388  CZ2 TRP A 360       4.500 -16.924  18.835  1.00 17.09           C
ANISOU  388  CZ2 TRP A 360     2162   2115   2217    562    -46    381       C
ATOM    389  CZ3 TRP A 360       3.415 -18.790  17.695  1.00 16.49           C
ANISOU  389  CZ3 TRP A 360     1994   2250   2022    528    -49    285       C
ATOM    390  CH2 TRP A 360       4.555 -18.192  18.303  1.00 14.70           C
ANISOU  390  CH2 TRP A 360     1820   1905   1859    528    -45    311       C
ATOM    391  N   ALA A 361       0.875 -16.757  14.831  1.00 17.36           N
ANISOU  391  N   ALA A 361     1905   2749   1941    655    -91    568       N
ATOM    392  CA  ALA A 361       2.106 -16.988  14.057  1.00 19.88           C
ANISOU  392  CA  ALA A 361     2233   3102   2218    606    -79    560       C
ATOM    393  C   ALA A 361       2.177 -16.072  12.828  1.00 21.39           C
ANISOU  393  C   ALA A 361     2378   3414   2334    641    -83    708       C
ATOM    394  O   ALA A 361       3.239 -15.512  12.531  1.00 19.62           O
ANISOU  394  O   ALA A 361     2182   3144   2127    629    -59    777       O
ATOM    395  CB  ALA A 361       2.229 -18.456  13.646  1.00 16.08           C
ANISOU  395  CB  ALA A 361     1725   2716   1668    533    -82    413       C
ATOM    396  N   LYS A 362       1.040 -15.853  12.148  1.00 18.29           N
ANISOU  396  N   LYS A 362     1909   3181   1860    686   -112    775       N
ATOM    397  CA  LYS A 362       0.983 -14.944  10.994  1.00 23.03           C
ANISOU  397  CA  LYS A 362     2470   3889   2393    715   -109    920       C
ATOM    398  C   LYS A 362       1.348 -13.513  11.343  1.00 25.61           C
ANISOU  398  C   LYS A 362     2868   4018   2843    747    -70   1032       C
ATOM    399  O   LYS A 362       1.641 -12.714  10.434  1.00 26.05           O
ANISOU  399  O   LYS A 362     2912   4114   2872    750    -52   1147       O
ATOM    400  CB  LYS A 362      -0.430 -14.998  10.397  1.00 22.27           C
ANISOU  400  CB  LYS A 362     2283   3962   2217    735   -138    928       C
ATOM    401  CG  LYS A 362      -0.728 -16.307   9.669  1.00 26.61           C
ANISOU  401  CG  LYS A 362     2750   4745   2614    672   -179    812       C
ATOM    402  CD  LYS A 362      -2.205 -16.278   9.258  1.00 35.11           C
ANISOU  402  CD  LYS A 362     3732   5971   3636    685   -209    822       C
ATOM    403  CE  LYS A 362      -2.631 -15.268   8.217  1.00 43.90           C
ANISOU  403  CE  LYS A 362     4797   7182   4700    730   -200    964       C
ATOM    404  NZ  LYS A 362      -2.066 -15.346   6.890  1.00 55.27           N
ANISOU  404  NZ  LYS A 362     6201   8790   6010    695   -199    990       N
ATOM    405  N   ARG A 363       1.320 -13.166  12.623  1.00 20.66           N
ANISOU  405  N   ARG A 363     2316   3185   2348    764    -58    992       N
ATOM    406  CA  ARG A 363       1.685 -11.828  13.076  1.00 25.32           C
ANISOU  406  CA  ARG A 363     2987   3574   3058    779    -28   1061       C
ATOM    407  C   ARG A 363       3.109 -11.780  13.649  1.00 24.68           C
ANISOU  407  C   ARG A 363     2977   3349   3049    721    -11   1038       C
ATOM    408  O   ARG A 363       3.541 -10.709  14.084  1.00 25.50           O
ANISOU  408  O   ARG A 363     3153   3282   3254    712      8   1077       O
ATOM    409  CB  ARG A 363       0.664 -11.353  14.125  1.00 23.70           C
ANISOU  409  CB  ARG A 363     2817   3250   2938    832    -26   1018       C
ATOM    410  CG  ARG A 363      -0.722 -11.137  13.459  1.00 31.15           C
ANISOU  410  CG  ARG A 363     3678   4339   3820    898    -36   1076       C
ATOM    411  CD  ARG A 363      -1.772 -10.631  14.439  1.00 37.48           C
ANISOU  411  CD  ARG A 363     4499   5045   4697    964    -25   1046       C
ATOM    412  NE  ARG A 363      -1.375  -9.324  14.926  1.00 45.04           N
ANISOU  412  NE  ARG A 363     5553   5794   5765    988      1   1084       N
ATOM    413  CZ  ARG A 363      -2.059  -8.634  15.828  1.00 49.17           C
ANISOU  413  CZ  ARG A 363     6116   6199   6366   1049     17   1056       C
ATOM    414  NH1 ARG A 363      -3.182  -9.155  16.343  1.00 43.56           N
ANISOU  414  NH1 ARG A 363     5349   5568   5634   1092     17   1001       N
ATOM    415  NH2 ARG A 363      -1.597  -7.448  16.238  1.00 42.42           N
ANISOU  415  NH2 ARG A 363     5356   5150   5611   1062     36   1078       N
ATOM    416  N   VAL A 364       3.833 -12.909  13.716  1.00 16.28           N
ANISOU  416  N   VAL A 364     1896   2349   1942    683    -20    971       N
ATOM    417  CA  VAL A 364       5.248 -12.897  14.127  1.00 14.96           C
ANISOU  417  CA  VAL A 364     1773   2076   1835    622     -3    956       C
ATOM    418  C   VAL A 364       6.072 -12.353  12.957  1.00 22.32           C
ANISOU  418  C   VAL A 364     2671   3089   2719    590     22   1087       C
ATOM    419  O   VAL A 364       6.010 -12.908  11.842  1.00 25.00           O
ANISOU  419  O   VAL A 364     2939   3633   2928    585     23   1101       O
ATOM    420  CB  VAL A 364       5.735 -14.308  14.541  1.00 13.84           C
ANISOU  420  CB  VAL A 364     1619   1972   1667    567    -11    786       C
ATOM    421  CG1 VAL A 364       7.264 -14.286  14.754  1.00 16.82           C
ANISOU  421  CG1 VAL A 364     2012   2285   2093    497      7    768       C
ATOM    422  CG2 VAL A 364       4.968 -14.819  15.841  1.00 15.45           C
ANISOU  422  CG2 VAL A 364     1864   2082   1925    589    -29    673       C
ATOM    423  N   PRO A 365       6.802 -11.247  13.132  1.00 23.80           N
ANISOU  423  N   PRO A 365     2909   3132   3003    555     47   1174       N
ATOM    424  CA  PRO A 365       7.449 -10.594  11.984  1.00 26.28           C
ANISOU  424  CA  PRO A 365     3189   3521   3277    517     80   1313       C
ATOM    425  C   PRO A 365       8.323 -11.587  11.240  1.00 28.64           C
ANISOU  425  C   PRO A 365     3412   4009   3460    470     95   1287       C
ATOM    426  O   PRO A 365       9.063 -12.364  11.851  1.00 24.68           O
ANISOU  426  O   PRO A 365     2909   3480   2987    421     94   1147       O
ATOM    427  CB  PRO A 365       8.264  -9.467  12.629  1.00 30.41           C
ANISOU  427  CB  PRO A 365     3786   3823   3946    456    100   1358       C
ATOM    428  CG  PRO A 365       7.491  -9.150  13.905  1.00 32.05           C
ANISOU  428  CG  PRO A 365     4077   3850   4252    496     75   1253       C
ATOM    429  CD  PRO A 365       6.978 -10.489  14.383  1.00 27.85           C
ANISOU  429  CD  PRO A 365     3514   3408   3661    536     46   1128       C
ATOM    430  N   GLY A 366       8.157 -11.625   9.912  1.00 24.81           N
ANISOU  430  N   GLY A 366     2861   3732   2835    488    110   1385       N
ATOM    431  CA  GLY A 366       8.903 -12.521   9.047  1.00 26.15           C
ANISOU  431  CA  GLY A 366     2957   4104   2877    444    138   1324       C
ATOM    432  C   GLY A 366       8.223 -13.835   8.702  1.00 22.79           C
ANISOU  432  C   GLY A 366     2488   3846   2324    471    111   1166       C
ATOM    433  O   GLY A 366       8.534 -14.429   7.658  1.00 24.47           O
ANISOU  433  O   GLY A 366     2638   4268   2391    456    135   1139       O
ATOM    434  N   PHE A 367       7.306 -14.300   9.549  1.00 20.85           N
ANISOU  434  N   PHE A 367     2275   3517   2129    504     68   1057       N
ATOM    435  CA  PHE A 367       6.674 -15.593   9.341  1.00 23.24           C
ANISOU  435  CA  PHE A 367     2545   3947   2337    506     44    893       C
ATOM    436  C   PHE A 367       5.909 -15.663   8.026  1.00 23.20           C
ANISOU  436  C   PHE A 367     2468   4192   2154    527     28    946       C
ATOM    437  O   PHE A 367       6.042 -16.651   7.294  1.00 22.79           O
ANISOU  437  O   PHE A 367     2374   4308   1976    497     36    827       O
ATOM    438  CB  PHE A 367       5.754 -15.921  10.517  1.00 19.31           C
ANISOU  438  CB  PHE A 367     2091   3312   1933    529      6    801       C
ATOM    439  CG  PHE A 367       5.263 -17.343  10.508  1.00 15.85           C
ANISOU  439  CG  PHE A 367     1633   2954   1435    504    -11    619       C
ATOM    440  CD1 PHE A 367       6.119 -18.373  10.888  1.00 19.62           C
ANISOU  440  CD1 PHE A 367     2134   3374   1946    466     14    474       C
ATOM    441  CD2 PHE A 367       3.982 -17.640  10.046  1.00 17.06           C
ANISOU  441  CD2 PHE A 367     1736   3247   1498    517    -49    599       C
ATOM    442  CE1 PHE A 367       5.697 -19.662  10.889  1.00 20.15           C
ANISOU  442  CE1 PHE A 367     2198   3480   1978    440      7    312       C
ATOM    443  CE2 PHE A 367       3.511 -18.987  10.023  1.00 17.94           C
ANISOU  443  CE2 PHE A 367     1832   3421   1563    470    -63    419       C
ATOM    444  CZ  PHE A 367       4.421 -20.001  10.443  1.00 15.22           C
ANISOU  444  CZ  PHE A 367     1533   2979   1269    431    -29    275       C
ATOM    445  N   VAL A 368       5.090 -14.638   7.687  1.00 22.59           N
ANISOU  445  N   VAL A 368     2376   4145   2065    581      5   1112       N
ATOM    446  CA  VAL A 368       4.334 -14.709   6.426  1.00 23.28           C
ANISOU  446  CA  VAL A 368     2382   4452   2012    585    -10   1125       C
ATOM    447  C   VAL A 368       5.178 -14.427   5.186  1.00 27.36           C
ANISOU  447  C   VAL A 368     2856   5113   2428    556     33   1201       C
ATOM    448  O   VAL A 368       4.660 -14.512   4.052  1.00 28.16           O
ANISOU  448  O   VAL A 368     2886   5413   2401    556     20   1210       O
ATOM    449  CB  VAL A 368       3.116 -13.763   6.361  1.00 30.90           C
ANISOU  449  CB  VAL A 368     3330   5381   3029    641    -33   1226       C
ATOM    450  CG1 VAL A 368       1.991 -14.308   7.261  1.00 35.48           C
ANISOU  450  CG1 VAL A 368     3912   5917   3653    664    -77   1122       C
ATOM    451  CG2 VAL A 368       3.515 -12.296   6.638  1.00 27.47           C
ANISOU  451  CG2 VAL A 368     2955   4747   2734    668      3   1387       C
ATOM    452  N   ASP A 369       6.477 -14.119   5.361  1.00 24.96           N
ANISOU  452  N   ASP A 369     2584   4725   2174    525     85   1256       N
ATOM    453  CA  ASP A 369       7.381 -14.041   4.228  1.00 28.61           C
ANISOU  453  CA  ASP A 369     2995   5342   2533    490    133   1304       C
ATOM    454  C   ASP A 369       7.735 -15.411   3.690  1.00 24.93           C
ANISOU  454  C   ASP A 369     2488   5067   1916    461    148   1121       C
ATOM    455  O   ASP A 369       8.215 -15.498   2.563  1.00 26.01           O
ANISOU  455  O   ASP A 369     2570   5375   1939    441    180   1127       O
ATOM    456  CB  ASP A 369       8.684 -13.323   4.599  1.00 31.14           C
ANISOU  456  CB  ASP A 369     3347   5524   2961    451    190   1411       C
ATOM    457  CG  ASP A 369       8.476 -11.884   5.007  1.00 31.66           C
ANISOU  457  CG  ASP A 369     3464   5382   3182    463    187   1575       C
ATOM    458  OD1 ASP A 369       7.535 -11.223   4.498  1.00 31.77           O
ANISOU  458  OD1 ASP A 369     3466   5419   3185    509    163   1658       O
ATOM    459  OD2 ASP A 369       9.271 -11.459   5.878  1.00 36.05           O
ANISOU  459  OD2 ASP A 369     4072   5751   3875    425    210   1607       O
ATOM    460  N   LEU A 370       7.571 -16.455   4.503  1.00 23.88           N
ANISOU  460  N   LEU A 370     2391   4892   1791    459    132    952       N
ATOM    461  CA  LEU A 370       7.930 -17.819   4.129  1.00 24.85           C
ANISOU  461  CA  LEU A 370     2497   5141   1806    432    158    736       C
ATOM    462  C   LEU A 370       6.866 -18.423   3.202  1.00 22.81           C
ANISOU  462  C   LEU A 370     2189   5062   1415    419    109    630       C
ATOM    463  O   LEU A 370       5.721 -17.958   3.145  1.00 23.93           O
ANISOU  463  O   LEU A 370     2309   5219   1563    436     49    702       O
ATOM    464  CB  LEU A 370       8.046 -18.658   5.407  1.00 24.66           C
ANISOU  464  CB  LEU A 370     2534   4885   1951    422    150    561       C
ATOM    465  CG  LEU A 370       9.084 -18.157   6.432  1.00 23.67           C
ANISOU  465  CG  LEU A 370     2449   4535   2009    419    180    620       C
ATOM    466  CD1 LEU A 370       8.912 -19.022   7.672  1.00 19.16           C
ANISOU  466  CD1 LEU A 370     1936   3769   1574    419    156    460       C
ATOM    467  CD2 LEU A 370      10.453 -18.280   5.807  1.00 23.87           C
ANISOU  467  CD2 LEU A 370     2428   4657   1983    403    256    622       C
ATOM    468  N   THR A 371       7.239 -19.478   2.472  1.00 23.90           N
ANISOU  468  N   THR A 371     2307   5328   1448    388    137    449       N
ATOM    469  CA  THR A 371       6.241 -20.238   1.721  1.00 24.66           C
ANISOU  469  CA  THR A 371     2366   5570   1435    354     88    307       C
ATOM    470  C   THR A 371       5.212 -20.879   2.660  1.00 23.56           C
ANISOU  470  C   THR A 371     2261   5335   1354    335     33    188       C
ATOM    471  O   THR A 371       5.460 -21.114   3.860  1.00 21.98           O
ANISOU  471  O   THR A 371     2127   4964   1260    349     46    149       O
ATOM    472  CB  THR A 371       6.912 -21.332   0.878  1.00 27.00           C
ANISOU  472  CB  THR A 371     2654   5970   1634    321    135    109       C
ATOM    473  OG1 THR A 371       7.534 -22.253   1.791  1.00 29.16           O
ANISOU  473  OG1 THR A 371     2997   6084   1999    322    180    -56       O
ATOM    474  CG2 THR A 371       7.951 -20.745  -0.082  1.00 29.42           C
ANISOU  474  CG2 THR A 371     2917   6391   1870    337    192    222       C
ATOM    475  N   LEU A 372       4.027 -21.186   2.146  1.00 24.54           N
ANISOU  475  N   LEU A 372     2333   5580   1409    300    -29    133       N
ATOM    476  CA  LEU A 372       3.038 -21.835   3.031  1.00 24.38           C
ANISOU  476  CA  LEU A 372     2339   5469   1454    269    -76     20       C
ATOM    477  C   LEU A 372       3.564 -23.196   3.482  1.00 23.13           C
ANISOU  477  C   LEU A 372     2251   5214   1325    219    -39   -230       C
ATOM    478  O   LEU A 372       3.337 -23.547   4.619  1.00 21.84           O
ANISOU  478  O   LEU A 372     2142   4869   1286    211    -47   -292       O
ATOM    479  CB  LEU A 372       1.710 -22.007   2.308  1.00 28.77           C
ANISOU  479  CB  LEU A 372     2816   6166   1949    232   -145     11       C
ATOM    480  CG  LEU A 372       1.065 -20.726   1.821  1.00 32.77           C
ANISOU  480  CG  LEU A 372     3242   6790   2417    283   -173    224       C
ATOM    481  CD1 LEU A 372      -0.357 -20.990   1.356  1.00 39.47           C
ANISOU  481  CD1 LEU A 372     4016   7771   3211    225   -235    132       C
ATOM    482  CD2 LEU A 372       1.083 -19.659   2.877  1.00 43.55           C
ANISOU  482  CD2 LEU A 372     4640   7987   3919    370   -168    436       C
ATOM    483  N   HIS A 373       4.198 -23.937   2.576  1.00 26.71           N
ANISOU  483  N   HIS A 373     2705   5737   1705    190      6   -371       N
ATOM    484  CA AHIS A 373       4.766 -25.223   2.971  0.51 27.94           C
ANISOU  484  CA AHIS A 373     2939   5753   1926    163     58   -599       C
ATOM    485  CA BHIS A 373       4.716 -25.226   3.008  0.49 27.94           C
ANISOU  485  CA BHIS A 373     2938   5749   1928    161     56   -600       C
ATOM    486  C   HIS A 373       5.683 -25.062   4.179  1.00 25.89           C
ANISOU  486  C   HIS A 373     2743   5287   1809    227    111   -556       C
ATOM    487  O   HIS A 373       5.615 -25.837   5.141  1.00 23.24           O
ANISOU  487  O   HIS A 373     2473   4728   1629    211    117   -662       O
ATOM    488  CB AHIS A 373       5.542 -25.847   1.808  0.51 29.88           C
ANISOU  488  CB AHIS A 373     3178   6090   2084    153    113   -718       C
ATOM    489  CB BHIS A 373       5.353 -25.975   1.837  0.49 30.04           C
ANISOU  489  CB BHIS A 373     3200   6106   2106    140    104   -741       C
ATOM    490  CG AHIS A 373       6.356 -27.034   2.215  0.51 30.73           C
ANISOU  490  CG AHIS A 373     3370   6019   2287    160    185   -915       C
ATOM    491  CG BHIS A 373       4.504 -27.102   1.330  0.49 37.22           C
ANISOU  491  CG BHIS A 373     4117   7049   2977     47     74   -949       C
ATOM    492  ND1AHIS A 373       7.613 -26.921   2.775  0.51 29.43           N
ANISOU  492  ND1AHIS A 373     3236   5736   2210    238    259   -877       N
ATOM    493  ND1BHIS A 373       4.991 -28.376   1.111  0.49 39.23           N
ANISOU  493  ND1BHIS A 373     4439   7204   3261     20    129  -1170       N
ATOM    494  CD2AHIS A 373       6.097 -28.361   2.134  0.51 30.99           C
ANISOU  494  CD2AHIS A 373     3460   5959   2356    103    197  -1141       C
ATOM    495  CD2BHIS A 373       3.190 -27.141   1.003  0.49 33.21           C
ANISOU  495  CD2BHIS A 373     3552   6656   2410    -27     -3   -962       C
ATOM    496  CE1AHIS A 373       8.082 -28.126   3.042  0.51 30.27           C
ANISOU  496  CE1AHIS A 373     3413   5682   2407    244    312  -1064       C
ATOM    497  CE1BHIS A 373       4.014 -29.144   0.658  0.49 37.16           C
ANISOU  497  CE1BHIS A 373     4171   6990   2958    -78     87  -1314       C
ATOM    498  NE2AHIS A 373       7.185 -29.017   2.658  0.51 30.73           N
ANISOU  498  NE2AHIS A 373     3498   5740   2439    162    278  -1225       N
ATOM    499  NE2BHIS A 373       2.912 -28.419   0.584  0.49 40.71           N
ANISOU  499  NE2BHIS A 373     4538   7581   3350   -112      6  -1194       N
ATOM    500  N   ASP A 374       6.541 -24.031   4.165  1.00 21.93           N
ANISOU  500  N   ASP A 374     2220   4791   1323    288    143   -367       N
ATOM    501  CA  ASP A 374       7.461 -23.846   5.295  1.00 23.49           C
ANISOU  501  CA  ASP A 374     2466   4742   1717    332    179   -308       C
ATOM    502  C   ASP A 374       6.744 -23.366   6.558  1.00 24.74           C
ANISOU  502  C   ASP A 374     2659   4708   2035    333    121   -214       C
ATOM    503  O   ASP A 374       7.079 -23.792   7.687  1.00 18.39           O
ANISOU  503  O   ASP A 374     1914   3683   1392    344    132   -259       O
ATOM    504  CB  ASP A 374       8.573 -22.874   4.908  1.00 25.25           C
ANISOU  504  CB  ASP A 374     2648   5034   1914    372    228   -141       C
ATOM    505  CG  ASP A 374       9.591 -23.517   3.976  1.00 34.76           C
ANISOU  505  CG  ASP A 374     3824   6379   3005    387    312   -255       C
ATOM    506  OD1 ASP A 374       9.518 -24.744   3.777  1.00 30.04           O
ANISOU  506  OD1 ASP A 374     3257   5776   2382    377    335   -475       O
ATOM    507  OD2 ASP A 374      10.433 -22.815   3.393  1.00 35.79           O
ANISOU  507  OD2 ASP A 374     3901   6626   3070    406    361   -129       O
ATOM    508  N   GLN A 375       5.723 -22.502   6.399  1.00 20.36           N
ANISOU  508  N   GLN A 375     2066   4241   1430    330     61    -82       N
ATOM    509  CA  GLN A 375       4.936 -22.100   7.557  1.00 19.64           C
ANISOU  509  CA  GLN A 375     2003   3985   1476    340     14    -13       C
ATOM    510  C   GLN A 375       4.283 -23.321   8.197  1.00 18.17           C
ANISOU  510  C   GLN A 375     1854   3696   1354    290      0   -193       C
ATOM    511  O   GLN A 375       4.270 -23.452   9.427  1.00 16.81           O
ANISOU  511  O   GLN A 375     1736   3317   1333    298      0   -194       O
ATOM    512  CB  GLN A 375       3.865 -21.081   7.136  1.00 20.78           C
ANISOU  512  CB  GLN A 375     2085   4267   1543    361    -42    144       C
ATOM    513  CG  GLN A 375       4.385 -19.719   6.632  1.00 21.70           C
ANISOU  513  CG  GLN A 375     2177   4443   1624    414    -27    365       C
ATOM    514  CD  GLN A 375       3.231 -18.756   6.220  1.00 26.55           C
ANISOU  514  CD  GLN A 375     2732   5187   2169    458    -84    533       C
ATOM    515  OE1 GLN A 375       2.161 -18.777   6.802  1.00 25.07           O
ANISOU  515  OE1 GLN A 375     2533   4959   2033    469   -129    523       O
ATOM    516  NE2 GLN A 375       3.451 -17.948   5.167  1.00 28.23           N
ANISOU  516  NE2 GLN A 375     2898   5537   2289    480    -70    680       N
ATOM    517  N   VAL A 376       3.738 -24.232   7.364  1.00 21.69           N
ANISOU  517  N   VAL A 376     2273   4288   1680    228    -12   -348       N
ATOM    518  CA  VAL A 376       3.154 -25.476   7.876  1.00 24.61           C
ANISOU  518  CA  VAL A 376     2684   4551   2116    159    -17   -529       C
ATOM    519  C   VAL A 376       4.205 -26.309   8.609  1.00 25.86           C
ANISOU  519  C   VAL A 376     2931   4484   2410    180     46   -624       C
ATOM    520  O   VAL A 376       3.967 -26.820   9.716  1.00 22.67           O
ANISOU  520  O   VAL A 376     2583   3884   2146    166     47   -654       O
ATOM    521  CB  VAL A 376       2.516 -26.279   6.730  1.00 28.97           C
ANISOU  521  CB  VAL A 376     3195   5306   2508     74    -38   -696       C
ATOM    522  CG1 VAL A 376       2.121 -27.681   7.236  1.00 26.75           C
ANISOU  522  CG1 VAL A 376     2975   4871   2317    -12    -26   -901       C
ATOM    523  CG2 VAL A 376       1.329 -25.521   6.170  1.00 25.54           C
ANISOU  523  CG2 VAL A 376     2658   5099   1948     56   -115   -591       C
ATOM    524  N   HIS A 377       5.369 -26.492   7.984  1.00 23.02           N
ANISOU  524  N   HIS A 377     2579   4164   2005    219    103   -667       N
ATOM    525  CA  HIS A 377       6.432 -27.274   8.610  1.00 22.30           C
ANISOU  525  CA  HIS A 377     2555   3881   2039    260    165   -746       C
ATOM    526  C   HIS A 377       6.800 -26.719   9.990  1.00 20.03           C
ANISOU  526  C   HIS A 377     2299   3400   1912    308    154   -607       C
ATOM    527  O   HIS A 377       6.972 -27.475  10.944  1.00 20.73           O
ANISOU  527  O   HIS A 377     2451   3297   2129    317    169   -661       O
ATOM    528  CB  HIS A 377       7.682 -27.276   7.739  1.00 24.93           C
ANISOU  528  CB  HIS A 377     2862   4318   2293    314    231   -771       C
ATOM    529  CG  HIS A 377       8.792 -28.132   8.284  1.00 28.46           C
ANISOU  529  CG  HIS A 377     3361   4592   2862    376    297   -856       C
ATOM    530  ND1 HIS A 377       8.740 -29.512   8.250  0.53 33.22           N
ANISOU  530  ND1 HIS A 377     4028   5090   3505    365    336  -1056       N
ATOM    531  CD2 HIS A 377       9.951 -27.816   8.914  1.00 30.33           C
ANISOU  531  CD2 HIS A 377     3590   4737   3196    450    328   -762       C
ATOM    532  CE1 HIS A 377       9.835 -30.009   8.796  0.46 34.78           C
ANISOU  532  CE1 HIS A 377     4256   5143   3817    449    392  -1072       C
ATOM    533  NE2 HIS A 377      10.590 -29.004   9.203  0.92 32.09           N
ANISOU  533  NE2 HIS A 377     3864   4822   3507    500    384   -897       N
ATOM    534  N   LEU A 378       7.000 -25.406  10.091  1.00 20.29           N
ANISOU  534  N   LEU A 378     2292   3479   1936    340    132   -429       N
ATOM    535  CA  LEU A 378       7.392 -24.811  11.370  1.00 17.32           C
ANISOU  535  CA  LEU A 378     1948   2933   1699    376    120   -315       C
ATOM    536  C   LEU A 378       6.328 -25.013  12.436  1.00 19.87           C
ANISOU  536  C   LEU A 378     2313   3132   2106    349     81   -319       C
ATOM    537  O   LEU A 378       6.646 -25.432  13.557  1.00 17.79           O
ANISOU  537  O   LEU A 378     2104   2698   1957    367     87   -330       O
ATOM    538  CB  LEU A 378       7.699 -23.329  11.165  1.00 17.92           C
ANISOU  538  CB  LEU A 378     1982   3078   1750    398    107   -137       C
ATOM    539  CG  LEU A 378       9.015 -22.936  10.468  1.00 21.23           C
ANISOU  539  CG  LEU A 378     2357   3583   2126    422    155    -86       C
ATOM    540  CD1 LEU A 378       9.049 -21.402  10.417  1.00 19.67           C
ANISOU  540  CD1 LEU A 378     2133   3412   1928    423    135    107       C
ATOM    541  CD2 LEU A 378      10.293 -23.472  11.188  1.00 16.96           C
ANISOU  541  CD2 LEU A 378     1834   2919   1692    457    192   -130       C
ATOM    542  N   LEU A 379       5.042 -24.732  12.115  1.00 16.09           N
ANISOU  542  N   LEU A 379     1800   2751   1562    310     40   -303       N
ATOM    543  CA  LEU A 379       3.991 -24.944  13.105  1.00 14.88           C
ANISOU  543  CA  LEU A 379     1670   2501   1482    283     12   -306       C
ATOM    544  C   LEU A 379       3.827 -26.427  13.457  1.00 19.54           C
ANISOU  544  C   LEU A 379     2313   2984   2127    231     36   -459       C
ATOM    545  O   LEU A 379       3.592 -26.765  14.629  1.00 16.99           O
ANISOU  545  O   LEU A 379     2039   2509   1908    226     38   -449       O
ATOM    546  CB  LEU A 379       2.662 -24.371  12.589  1.00 14.94           C
ANISOU  546  CB  LEU A 379     1607   2666   1404    258    -34   -256       C
ATOM    547  CG  LEU A 379       2.586 -22.880  12.916  1.00 16.95           C
ANISOU  547  CG  LEU A 379     1843   2920   1678    326    -53    -78       C
ATOM    548  CD1 LEU A 379       1.425 -22.343  12.056  1.00 15.43           C
ANISOU  548  CD1 LEU A 379     1561   2926   1375    324    -96    -20       C
ATOM    549  CD2 LEU A 379       2.316 -22.624  14.439  1.00 14.11           C
ANISOU  549  CD2 LEU A 379     1535   2382   1446    351    -53    -36       C
ATOM    550  N   GLU A 380       3.930 -27.319  12.468  1.00 17.56           N
ANISOU  550  N   GLU A 380     2058   2806   1807    189     57   -599       N
ATOM    551  CA  GLU A 380       3.819 -28.754  12.740  1.00 21.38           C
ANISOU  551  CA  GLU A 380     2606   3158   2359    136     88   -752       C
ATOM    552  C   GLU A 380       4.906 -29.223  13.705  1.00 21.70           C
ANISOU  552  C   GLU A 380     2722   2992   2530    205    131   -738       C
ATOM    553  O   GLU A 380       4.655 -30.047  14.598  1.00 21.14           O
ANISOU  553  O   GLU A 380     2715   2754   2563    183    145   -769       O
ATOM    554  CB  GLU A 380       3.861 -29.540  11.416  1.00 25.97           C
ANISOU  554  CB  GLU A 380     3177   3855   2835     86    109   -924       C
ATOM    555  CG  GLU A 380       3.595 -31.028  11.621  1.00 27.67           C
ANISOU  555  CG  GLU A 380     3468   3916   3129     15    143  -1097       C
ATOM    556  CD  GLU A 380       3.445 -31.816  10.354  1.00 46.35           C
ANISOU  556  CD  GLU A 380     5832   6392   5389    -55    160  -1297       C
ATOM    557  OE1 GLU A 380       3.724 -31.276   9.264  1.00 46.37           O
ANISOU  557  OE1 GLU A 380     5772   6604   5241    -33    153  -1304       O
ATOM    558  OE2 GLU A 380       2.996 -32.974  10.462  1.00 45.10           O
ANISOU  558  OE2 GLU A 380     5734   6109   5294   -142    181  -1447       O
ATOM    559  N   SER A 381       6.113 -28.664  13.589  1.00 17.98           N
ANISOU  559  N   SER A 381     2238   2539   2056    289    149   -673       N
ATOM    560  CA  SER A 381       7.187 -28.994  14.520  1.00 19.07           C
ANISOU  560  CA  SER A 381     2422   2515   2306    364    177   -641       C
ATOM    561  C   SER A 381       6.984 -28.359  15.907  1.00 18.84           C
ANISOU  561  C   SER A 381     2414   2390   2356    379    140   -508       C
ATOM    562  O   SER A 381       7.353 -28.950  16.924  1.00 18.42           O
ANISOU  562  O   SER A 381     2415   2187   2399    411    152   -496       O
ATOM    563  CB  SER A 381       8.517 -28.565  13.888  1.00 22.95           C
ANISOU  563  CB  SER A 381     2868   3092   2759    435    207   -616       C
ATOM    564  OG  SER A 381       9.595 -28.720  14.811  1.00 33.47           O
ANISOU  564  OG  SER A 381     4220   4302   4194    511    222   -563       O
ATOM    565  N   ALA A 382       6.449 -27.152  15.983  1.00 14.41           N
ANISOU  565  N   ALA A 382     1811   1911   1751    366     99   -406       N
ATOM    566  CA  ALA A 382       6.489 -26.347  17.202  1.00 14.97           C
ANISOU  566  CA  ALA A 382     1900   1906   1882    394     71   -291       C
ATOM    567  C   ALA A 382       5.199 -26.307  18.029  1.00 14.50           C
ANISOU  567  C   ALA A 382     1861   1805   1844    355     50   -268       C
ATOM    568  O   ALA A 382       5.251 -25.840  19.180  1.00 13.57           O
ANISOU  568  O   ALA A 382     1771   1610   1774    381     36   -195       O
ATOM    569  CB  ALA A 382       6.839 -24.892  16.846  1.00 17.95           C
ANISOU  569  CB  ALA A 382     2230   2374   2216    416     49   -186       C
ATOM    570  N   TRP A 383       4.043 -26.728  17.478  1.00 15.15           N
ANISOU  570  N   TRP A 383     1918   1954   1884    291     47   -328       N
ATOM    571  CA  TRP A 383       2.759 -26.400  18.097  1.00 12.47           C
ANISOU  571  CA  TRP A 383     1562   1629   1548    259     28   -285       C
ATOM    572  C   TRP A 383       2.686 -26.895  19.530  1.00 11.72           C
ANISOU  572  C   TRP A 383     1530   1386   1537    260     44   -262       C
ATOM    573  O   TRP A 383       2.168 -26.176  20.381  1.00 11.90           O
ANISOU  573  O   TRP A 383     1550   1403   1568    281     34   -188       O
ATOM    574  CB  TRP A 383       1.586 -26.953  17.259  1.00 15.35           C
ANISOU  574  CB  TRP A 383     1874   2105   1854    173     20   -365       C
ATOM    575  CG  TRP A 383       1.537 -28.450  17.312  1.00 17.62           C
ANISOU  575  CG  TRP A 383     2212   2293   2191    102     52   -485       C
ATOM    576  CD1 TRP A 383       2.177 -29.318  16.489  1.00 18.84           C
ANISOU  576  CD1 TRP A 383     2394   2430   2335     84     77   -602       C
ATOM    577  CD2 TRP A 383       0.775 -29.257  18.251  1.00 14.94           C
ANISOU  577  CD2 TRP A 383     1906   1846   1924     37     71   -499       C
ATOM    578  NE1 TRP A 383       1.886 -30.658  16.870  1.00 19.08           N
ANISOU  578  NE1 TRP A 383     2487   2319   2444     14    111   -695       N
ATOM    579  CE2 TRP A 383       1.033 -30.622  17.953  1.00 20.65           C
ANISOU  579  CE2 TRP A 383     2688   2463   2693    -21    107   -621       C
ATOM    580  CE3 TRP A 383      -0.085 -28.944  19.332  1.00 17.71           C
ANISOU  580  CE3 TRP A 383     2246   2179   2305     26     70   -416       C
ATOM    581  CZ2 TRP A 383       0.452 -31.670  18.673  1.00 20.28           C
ANISOU  581  CZ2 TRP A 383     2691   2283   2731   -101    138   -649       C
ATOM    582  CZ3 TRP A 383      -0.629 -29.998  20.060  1.00 18.23           C
ANISOU  582  CZ3 TRP A 383     2352   2135   2440    -52    103   -441       C
ATOM    583  CH2 TRP A 383      -0.390 -31.341  19.696  1.00 20.96           C
ANISOU  583  CH2 TRP A 383     2757   2369   2838   -122    135   -552       C
ATOM    584  N   LEU A 384       3.252 -28.086  19.839  1.00 12.29           N
ANISOU  584  N   LEU A 384     1663   1337   1669    251     74   -319       N
ATOM    585  CA  LEU A 384       3.084 -28.515  21.240  1.00 14.19           C
ANISOU  585  CA  LEU A 384     1961   1454   1976    254     88   -270       C
ATOM    586  C   LEU A 384       4.034 -27.770  22.181  1.00 12.47           C
ANISOU  586  C   LEU A 384     1769   1194   1774    337     70   -181       C
ATOM    587  O   LEU A 384       3.684 -27.496  23.339  1.00 13.23           O
ANISOU  587  O   LEU A 384     1890   1257   1879    346     67   -119       O
ATOM    588  CB  LEU A 384       3.281 -30.043  21.396  1.00 17.14           C
ANISOU  588  CB  LEU A 384     2400   1690   2422    222    129   -333       C
ATOM    589  CG  LEU A 384       2.966 -30.684  22.810  1.00 14.60           C
ANISOU  589  CG  LEU A 384     2141   1240   2164    210    152   -267       C
ATOM    590  CD1 LEU A 384       1.532 -30.293  23.365  1.00 14.28           C
ANISOU  590  CD1 LEU A 384     2063   1268   2095    142    152   -225       C
ATOM    591  CD2 LEU A 384       3.086 -32.213  22.824  1.00 15.64           C
ANISOU  591  CD2 LEU A 384     2345   1215   2381    174    200   -322       C
ATOM    592  N   GLU A 385       5.239 -27.441  21.718  1.00 14.06           N
ANISOU  592  N   GLU A 385     1960   1411   1971    390     60   -180       N
ATOM    593  CA  GLU A 385       6.128 -26.614  22.536  1.00 14.93           C
ANISOU  593  CA  GLU A 385     2079   1505   2090    447     32   -104       C
ATOM    594  C   GLU A 385       5.505 -25.261  22.804  1.00 14.32           C
ANISOU  594  C   GLU A 385     1981   1485   1976    444      7    -52       C
ATOM    595  O   GLU A 385       5.638 -24.718  23.906  1.00 13.05           O
ANISOU  595  O   GLU A 385     1849   1289   1822    466    -10     -5       O
ATOM    596  CB  GLU A 385       7.464 -26.396  21.829  1.00 14.09           C
ANISOU  596  CB  GLU A 385     1938   1433   1982    488     28   -110       C
ATOM    597  CG  GLU A 385       8.383 -27.622  21.732  1.00 16.69           C
ANISOU  597  CG  GLU A 385     2285   1696   2360    530     56   -152       C
ATOM    598  CD  GLU A 385       9.542 -27.364  20.785  1.00 24.33           C
ANISOU  598  CD  GLU A 385     3195   2738   3311    567     65   -169       C
ATOM    599  OE1 GLU A 385      10.597 -26.961  21.246  1.00 26.98           O
ANISOU  599  OE1 GLU A 385     3505   3082   3665    610     45   -115       O
ATOM    600  OE2 GLU A 385       9.374 -27.599  19.583  1.00 27.14           O
ANISOU  600  OE2 GLU A 385     3526   3156   3629    549     94   -239       O
ATOM    601  N   ILE A 386       4.834 -24.697  21.791  1.00 13.15           N
ANISOU  601  N   ILE A 386     1783   1427   1784    422      6    -61       N
ATOM    602  CA  ILE A 386       4.153 -23.417  21.956  1.00 14.63           C
ANISOU  602  CA  ILE A 386     1952   1658   1950    437    -10     -5       C
ATOM    603  C   ILE A 386       3.009 -23.507  22.985  1.00 12.85           C
ANISOU  603  C   ILE A 386     1744   1409   1728    429      2      5       C
ATOM    604  O   ILE A 386       2.867 -22.630  23.850  1.00 12.75           O
ANISOU  604  O   ILE A 386     1755   1371   1719    464     -3     45       O
ATOM    605  CB  ILE A 386       3.694 -22.891  20.582  1.00 16.64           C
ANISOU  605  CB  ILE A 386     2142   2029   2152    429    -15      2       C
ATOM    606  CG1 ILE A 386       4.963 -22.537  19.747  1.00 11.86           C
ANISOU  606  CG1 ILE A 386     1521   1451   1535    443    -19     16       C
ATOM    607  CG2 ILE A 386       2.815 -21.633  20.726  1.00 16.49           C
ANISOU  607  CG2 ILE A 386     2101   2045   2119    462    -25     71       C
ATOM    608  CD1 ILE A 386       4.667 -22.282  18.162  1.00 17.89           C
ANISOU  608  CD1 ILE A 386     2217   2361   2220    430    -19     21       C
ATOM    609  N   LEU A 387       2.144 -24.521  22.871  1.00 13.39           N
ANISOU  609  N   LEU A 387     1798   1494   1796    379     23    -35       N
ATOM    610  CA  LEU A 387       1.138 -24.767  23.917  1.00 14.69           C
ANISOU  610  CA  LEU A 387     1974   1642   1967    361     46    -18       C
ATOM    611  C   LEU A 387       1.768 -24.874  25.298  1.00 16.78           C
ANISOU  611  C   LEU A 387     2311   1814   2252    392     51     14       C
ATOM    612  O   LEU A 387       1.278 -24.260  26.260  1.00 13.70           O
ANISOU  612  O   LEU A 387     1932   1429   1842    418     61     47       O
ATOM    613  CB  LEU A 387       0.329 -26.049  23.620  1.00 13.60           C
ANISOU  613  CB  LEU A 387     1815   1511   1840    276     72    -69       C
ATOM    614  CG  LEU A 387      -0.715 -25.927  22.496  1.00 15.00           C
ANISOU  614  CG  LEU A 387     1901   1822   1976    229     62   -102       C
ATOM    615  CD1 LEU A 387      -1.549 -27.232  22.505  1.00 16.49           C
ANISOU  615  CD1 LEU A 387     2078   2001   2188    120     88   -158       C
ATOM    616  CD2 LEU A 387      -1.630 -24.691  22.620  1.00 14.48           C
ANISOU  616  CD2 LEU A 387     1770   1858   1873    280     53    -40       C
ATOM    617  N   MET A 388       2.868 -25.673  25.432  1.00 13.60           N
ANISOU  617  N   MET A 388     1952   1335   1881    397     46      5       N
ATOM    618  CA  MET A 388       3.476 -25.858  26.741  1.00 14.05           C
ANISOU  618  CA  MET A 388     2067   1327   1944    428     42     48       C
ATOM    619  C   MET A 388       4.106 -24.591  27.283  1.00 16.42           C
ANISOU  619  C   MET A 388     2377   1645   2216    475      6     71       C
ATOM    620  O   MET A 388       3.979 -24.323  28.491  1.00 14.60           O
ANISOU  620  O   MET A 388     2184   1408   1956    492      6     98       O
ATOM    621  CB  MET A 388       4.478 -27.048  26.786  1.00 11.73           C
ANISOU  621  CB  MET A 388     1809    952   1695    441     45     49       C
ATOM    622  CG  MET A 388       3.913 -28.340  26.202  1.00 14.65           C
ANISOU  622  CG  MET A 388     2187   1270   2109    386     86      7       C
ATOM    623  SD  MET A 388       5.050 -29.727  26.246  1.00 14.64           S
ANISOU  623  SD  MET A 388     2240   1142   2181    425    103      7       S
ATOM    624  CE  MET A 388       4.102 -31.121  26.912  1.00 21.18           C
ANISOU  624  CE  MET A 388     3131   1854   3064    359    160     33       C
ATOM    625  N   ILE A 389       4.806 -23.805  26.463  1.00 11.46           N
ANISOU  625  N   ILE A 389     1721   1040   1594    489    -21     60       N
ATOM    626  CA  ILE A 389       5.399 -22.600  27.047  1.00 15.36           C
ANISOU  626  CA  ILE A 389     2232   1530   2074    513    -53     76       C
ATOM    627  C   ILE A 389       4.307 -21.624  27.479  1.00 14.14           C
ANISOU  627  C   ILE A 389     2088   1391   1895    526    -36     77       C
ATOM    628  O   ILE A 389       4.409 -20.986  28.544  1.00 14.76           O
ANISOU  628  O   ILE A 389     2209   1448   1949    543    -46     72       O
ATOM    629  CB  ILE A 389       6.455 -21.942  26.125  1.00 17.35           C
ANISOU  629  CB  ILE A 389     2450   1796   2346    511    -80     77       C
ATOM    630  CG1 ILE A 389       7.300 -20.950  26.972  1.00 16.81           C
ANISOU  630  CG1 ILE A 389     2408   1705   2276    512   -119     84       C
ATOM    631  CG2 ILE A 389       5.865 -21.172  24.918  1.00 11.89           C
ANISOU  631  CG2 ILE A 389     1719   1147   1653    506    -66     85       C
ATOM    632  CD1 ILE A 389       8.446 -20.309  26.185  1.00 13.64           C
ANISOU  632  CD1 ILE A 389     1966   1316   1901    492   -143     96       C
ATOM    633  N   GLY A 390       3.222 -21.521  26.693  1.00 15.15           N
ANISOU  633  N   GLY A 390     2172   1562   2022    523    -10     77       N
ATOM    634  CA  GLY A 390       2.078 -20.762  27.140  1.00 13.37           C
ANISOU  634  CA  GLY A 390     1943   1360   1777    555     17     83       C
ATOM    635  C   GLY A 390       1.575 -21.224  28.495  1.00 12.22           C
ANISOU  635  C   GLY A 390     1833   1210   1600    556     45     80       C
ATOM    636  O   GLY A 390       1.252 -20.408  29.369  1.00 12.41           O
ANISOU  636  O   GLY A 390     1889   1229   1597    596     59     70       O
ATOM    637  N   LEU A 391       1.417 -22.546  28.652  1.00 11.09           N
ANISOU  637  N   LEU A 391     1687   1070   1457    513     61     88       N
ATOM    638  CA  LEU A 391       0.947 -23.110  29.909  1.00 11.31           C
ANISOU  638  CA  LEU A 391     1746   1100   1449    506     95    108       C
ATOM    639  C   LEU A 391       1.875 -22.754  31.068  1.00 14.72           C
ANISOU  639  C   LEU A 391     2247   1505   1842    537     68    111       C
ATOM    640  O   LEU A 391       1.424 -22.278  32.134  1.00 13.63           O
ANISOU  640  O   LEU A 391     2137   1396   1646    563     91    107       O
ATOM    641  CB  LEU A 391       0.831 -24.632  29.760  1.00 13.07           C
ANISOU  641  CB  LEU A 391     1968   1299   1701    447    115    127       C
ATOM    642  CG  LEU A 391       0.416 -25.340  31.056  1.00 17.41           C
ANISOU  642  CG  LEU A 391     2554   1845   2216    431    155    175       C
ATOM    643  CD1 LEU A 391      -0.966 -24.841  31.559  1.00 16.71           C
ANISOU  643  CD1 LEU A 391     2425   1842   2083    433    209    180       C
ATOM    644  CD2 LEU A 391       0.442 -26.857  30.808  1.00 12.60           C
ANISOU  644  CD2 LEU A 391     1957   1169   1660    369    177    200       C
ATOM    645  N   VAL A 392       3.169 -23.005  30.901  1.00 15.65           N
ANISOU  645  N   VAL A 392     2384   1583   1981    535     19    115       N
ATOM    646  CA AVAL A 392       4.137 -22.733  31.960  0.46 15.78           C
ANISOU  646  CA AVAL A 392     2447   1596   1953    554    -22    119       C
ATOM    647  CA BVAL A 392       4.068 -22.747  32.017  0.54 16.00           C
ANISOU  647  CA BVAL A 392     2476   1626   1977    554    -18    120       C
ATOM    648  C   VAL A 392       4.086 -21.262  32.355  1.00 15.96           C
ANISOU  648  C   VAL A 392     2492   1628   1944    574    -34     67       C
ATOM    649  O   VAL A 392       4.098 -20.904  33.554  1.00 15.56           O
ANISOU  649  O   VAL A 392     2488   1604   1822    587    -37     48       O
ATOM    650  CB AVAL A 392       5.530 -23.192  31.489  0.46 17.49           C
ANISOU  650  CB AVAL A 392     2650   1785   2209    552    -72    133       C
ATOM    651  CB BVAL A 392       5.476 -23.321  31.769  0.54 17.59           C
ANISOU  651  CB BVAL A 392     2672   1802   2209    554    -69    141       C
ATOM    652  CG1AVAL A 392       6.653 -22.594  32.323  0.46 16.15           C
ANISOU  652  CG1AVAL A 392     2501   1638   1998    562   -133    125       C
ATOM    653  CG1BVAL A 392       5.394 -24.819  31.513  0.54 14.60           C
ANISOU  653  CG1BVAL A 392     2291   1387   1870    548    -42    185       C
ATOM    654  CG2AVAL A 392       5.592 -24.713  31.551  0.46 14.75           C
ANISOU  654  CG2AVAL A 392     2309   1408   1886    552    -51    184       C
ATOM    655  CG2BVAL A 392       6.229 -22.581  30.674  0.54 14.91           C
ANISOU  655  CG2BVAL A 392     2295   1451   1919    548   -102    109       C
ATOM    656  N   TRP A 393       3.997 -20.386  31.346  1.00 16.81           N
ANISOU  656  N   TRP A 393     2573   1711   2102    577    -36     43       N
ATOM    657  CA  TRP A 393       3.842 -18.948  31.591  1.00 19.93           C
ANISOU  657  CA  TRP A 393     3000   2081   2493    600    -36     -4       C
ATOM    658  C   TRP A 393       2.583 -18.655  32.424  1.00 18.16           C
ANISOU  658  C   TRP A 393     2796   1887   2219    643     24    -26       C
ATOM    659  O   TRP A 393       2.647 -17.968  33.465  1.00 16.34           O
ANISOU  659  O   TRP A 393     2622   1651   1935    662     26    -79       O
ATOM    660  CB  TRP A 393       3.832 -18.214  30.242  1.00 15.10           C
ANISOU  660  CB  TRP A 393     2352   1436   1952    604    -37      8       C
ATOM    661  CG  TRP A 393       3.454 -16.781  30.334  1.00 18.56           C
ANISOU  661  CG  TRP A 393     2816   1826   2409    631    -20    -23       C
ATOM    662  CD1 TRP A 393       2.307 -16.188  29.842  1.00 18.17           C
ANISOU  662  CD1 TRP A 393     2729   1793   2383    667     25     -6       C
ATOM    663  CD2 TRP A 393       4.214 -15.727  30.960  1.00 15.19           C
ANISOU  663  CD2 TRP A 393     2461   1323   1988    624    -48    -79       C
ATOM    664  NE1 TRP A 393       2.308 -14.863  30.159  1.00 21.84           N
ANISOU  664  NE1 TRP A 393     3235   2189   2875    685     34    -42       N
ATOM    665  CE2 TRP A 393       3.466 -14.549  30.833  1.00 21.84           C
ANISOU  665  CE2 TRP A 393     3307   2124   2866    651     -7    -94       C
ATOM    666  CE3 TRP A 393       5.443 -15.684  31.632  1.00 21.29           C
ANISOU  666  CE3 TRP A 393     3267   2085   2738    568   -106   -117       C
ATOM    667  CZ2 TRP A 393       3.914 -13.324  31.326  1.00 23.71           C
ANISOU  667  CZ2 TRP A 393     3616   2264   3130    642    -14   -157       C
ATOM    668  CZ3 TRP A 393       5.881 -14.481  32.137  1.00 23.38           C
ANISOU  668  CZ3 TRP A 393     3594   2273   3015    545   -123   -188       C
ATOM    669  CH2 TRP A 393       5.117 -13.307  31.972  1.00 23.70           C
ANISOU  669  CH2 TRP A 393     3680   2221   3103    593    -75   -216       C
ATOM    670  N   ARG A 394       1.422 -19.193  32.005  1.00 16.43           N
ANISOU  670  N   ARG A 394     2524   1713   2008    655     75      8       N
ATOM    671  CA  ARG A 394       0.155 -18.959  32.718  1.00 19.99           C
ANISOU  671  CA  ARG A 394     2968   2215   2412    700    142     -3       C
ATOM    672  C   ARG A 394       0.209 -19.481  34.141  1.00 19.06           C
ANISOU  672  C   ARG A 394     2897   2140   2204    692    159     -8       C
ATOM    673  O   ARG A 394      -0.467 -18.940  35.024  1.00 16.68           O
ANISOU  673  O   ARG A 394     2618   1878   1841    737    209    -44       O
ATOM    674  CB  ARG A 394      -1.011 -19.667  32.000  1.00 16.48           C
ANISOU  674  CB  ARG A 394     2436   1836   1991    689    184     42       C
ATOM    675  CG  ARG A 394      -1.417 -19.130  30.699  1.00 24.08           C
ANISOU  675  CG  ARG A 394     3334   2802   3011    711    177     55       C
ATOM    676  CD  ARG A 394      -2.851 -19.598  30.413  1.00 24.97           C
ANISOU  676  CD  ARG A 394     3352   3019   3118    711    228     84       C
ATOM    677  NE  ARG A 394      -2.991 -21.032  30.112  1.00 18.42           N
ANISOU  677  NE  ARG A 394     2483   2223   2292    617    227    108       N
ATOM    678  CZ  ARG A 394      -2.537 -21.581  28.986  1.00 15.82           C
ANISOU  678  CZ  ARG A 394     2130   1879   2000    564    185    109       C
ATOM    679  NH1 ARG A 394      -1.841 -20.849  28.090  1.00 14.94           N
ANISOU  679  NH1 ARG A 394     2026   1736   1916    593    141    104       N
ATOM    680  NH2 ARG A 394      -2.752 -22.879  28.718  1.00 12.85           N
ANISOU  680  NH2 ARG A 394     1728   1517   1637    478    193    113       N
ATOM    681  N   SER A 395       0.999 -20.540  34.381  1.00 16.25           N
ANISOU  681  N   SER A 395     2557   1784   1834    643    123     35       N
ATOM    682  CA  SER A 395       1.062 -21.221  35.666  1.00 14.13           C
ANISOU  682  CA  SER A 395     2326   1568   1473    635    137     66       C
ATOM    683  C   SER A 395       2.084 -20.619  36.624  1.00 21.84           C
ANISOU  683  C   SER A 395     3369   2554   2375    645     82     19       C
ATOM    684  O   SER A 395       2.172 -21.055  37.782  1.00 18.12           O
ANISOU  684  O   SER A 395     2932   2150   1801    646     87     44       O
ATOM    685  CB  SER A 395       1.398 -22.704  35.439  1.00 17.27           C
ANISOU  685  CB  SER A 395     2710   1948   1902    589    127    151       C
ATOM    686  OG  SER A 395       0.403 -23.320  34.626  1.00 15.31           O
ANISOU  686  OG  SER A 395     2404   1698   1716    558    177    178       O
ATOM    687  N   MET A 396       2.840 -19.630  36.166  1.00 15.22           N
ANISOU  687  N   MET A 396     2545   1657   1579    645     30    -46       N
ATOM    688  CA  MET A 396       4.009 -19.164  36.923  1.00 24.91           C
ANISOU  688  CA  MET A 396     3820   2896   2748    625    -41    -94       C
ATOM    689  C   MET A 396       3.621 -18.691  38.312  1.00 23.49           C
ANISOU  689  C   MET A 396     3699   2787   2438    648    -16   -157       C
ATOM    690  O   MET A 396       4.380 -18.860  39.272  1.00 25.17           O
ANISOU  690  O   MET A 396     3942   3069   2551    629    -68   -165       O
ATOM    691  CB  MET A 396       4.687 -17.995  36.201  1.00 21.90           C
ANISOU  691  CB  MET A 396     3445   2431   2445    606    -85   -162       C
ATOM    692  CG  MET A 396       6.193 -17.858  36.353  1.00 33.22           C
ANISOU  692  CG  MET A 396     4880   3869   3874    553   -178   -179       C
ATOM    693  SD  MET A 396       6.736 -16.625  35.151  1.00 33.73           S
ANISOU  693  SD  MET A 396     4933   3819   4063    516   -201   -222       S
ATOM    694  CE  MET A 396       6.543 -15.075  35.990  1.00 32.22           C
ANISOU  694  CE  MET A 396     4833   3569   3840    508   -193   -360       C
ATOM    695  N   GLU A 397       2.447 -18.077  38.440  1.00 21.18           N
ANISOU  695  N   GLU A 397     3417   2496   2136    695     64   -205       N
ATOM    696  CA  GLU A 397       2.003 -17.552  39.731  1.00 26.01           C
ANISOU  696  CA  GLU A 397     4086   3180   2616    728    105   -285       C
ATOM    697  C   GLU A 397       1.123 -18.517  40.502  1.00 24.16           C
ANISOU  697  C   GLU A 397     3832   3064   2283    746    177   -208       C
ATOM    698  O   GLU A 397       0.448 -18.106  41.453  1.00 26.78           O
ANISOU  698  O   GLU A 397     4196   3475   2505    788    241   -267       O
ATOM    699  CB  GLU A 397       1.314 -16.200  39.529  1.00 33.57           C
ANISOU  699  CB  GLU A 397     5072   4065   3619    785    160   -395       C
ATOM    700  CG  GLU A 397       2.159 -15.309  38.621  1.00 34.73           C
ANISOU  700  CG  GLU A 397     5236   4075   3886    755     97   -440       C
ATOM    701  CD  GLU A 397       1.400 -14.154  38.060  1.00 50.31           C
ANISOU  701  CD  GLU A 397     7224   5944   5948    823    156   -496       C
ATOM    702  OE1 GLU A 397       0.266 -14.386  37.578  1.00 58.16           O
ANISOU  702  OE1 GLU A 397     8158   6964   6978    886    227   -436       O
ATOM    703  OE2 GLU A 397       1.924 -13.017  38.137  1.00 57.37           O
ANISOU  703  OE2 GLU A 397     8189   6733   6878    812    133   -597       O
ATOM    704  N   HIS A 398       1.178 -19.806  40.175  1.00 18.72           N
ANISOU  704  N   HIS A 398     3098   2390   1626    713    170    -79       N
ATOM    705  CA  HIS A 398       0.336 -20.818  40.793  1.00 20.48           C
ANISOU  705  CA  HIS A 398     3299   2704   1779    711    244     18       C
ATOM    706  C   HIS A 398       1.229 -21.974  41.160  1.00 19.08           C
ANISOU  706  C   HIS A 398     3135   2546   1568    674    187    130       C
ATOM    707  O   HIS A 398       1.255 -22.994  40.455  1.00 20.96           O
ANISOU  707  O   HIS A 398     3338   2724   1903    643    187    226       O
ATOM    708  CB  HIS A 398      -0.784 -21.226  39.834  1.00 21.73           C
ANISOU  708  CB  HIS A 398     3380   2832   2044    705    313     68       C
ATOM    709  CG  HIS A 398      -1.594 -20.052  39.369  1.00 28.35           C
ANISOU  709  CG  HIS A 398     4193   3652   2927    762    359    -24       C
ATOM    710  ND1 HIS A 398      -2.711 -19.615  40.049  1.00 32.39           N
ANISOU  710  ND1 HIS A 398     4688   4253   3364    817    454    -59       N
ATOM    711  CD2 HIS A 398      -1.427 -19.199  38.326  1.00 27.45           C
ANISOU  711  CD2 HIS A 398     4067   3444   2920    784    326    -80       C
ATOM    712  CE1 HIS A 398      -3.207 -18.556  39.436  1.00 32.08           C
ANISOU  712  CE1 HIS A 398     4628   4166   3394    881    477   -132       C
ATOM    713  NE2 HIS A 398      -2.439 -18.273  38.399  1.00 30.52           N
ANISOU  713  NE2 HIS A 398     4436   3853   3305    860    399   -141       N
ATOM    714  N   PRO A 399       1.991 -21.851  42.254  1.00 23.44           N
ANISOU  714  N   PRO A 399     3738   3183   1984    680    137    118       N
ATOM    715  CA  PRO A 399       2.978 -22.885  42.573  1.00 22.87           C
ANISOU  715  CA  PRO A 399     3671   3133   1886    664     69    236       C
ATOM    716  C   PRO A 399       2.312 -24.238  42.743  1.00 19.97           C
ANISOU  716  C   PRO A 399     3289   2774   1525    653    140    394       C
ATOM    717  O   PRO A 399       1.298 -24.363  43.444  1.00 21.41           O
ANISOU  717  O   PRO A 399     3476   3041   1618    655    229    424       O
ATOM    718  CB  PRO A 399       3.598 -22.394  43.898  1.00 28.73           C
ANISOU  718  CB  PRO A 399     4462   4014   2440    676     17    188       C
ATOM    719  CG  PRO A 399       3.407 -20.856  43.864  1.00 24.00           C
ANISOU  719  CG  PRO A 399     3892   3398   1830    681     20     -5       C
ATOM    720  CD  PRO A 399       2.058 -20.695  43.190  1.00 27.01           C
ANISOU  720  CD  PRO A 399     4244   3713   2304    704    131    -18       C
ATOM    721  N   GLY A 400       2.924 -25.263  42.131  1.00 25.22           N
ANISOU  721  N   GLY A 400     3938   3348   2295    641    105    497       N
ATOM    722  CA  GLY A 400       2.430 -26.620  42.241  1.00 23.27           C
ANISOU  722  CA  GLY A 400     3691   3069   2080    620    167    651       C
ATOM    723  C   GLY A 400       1.195 -26.874  41.399  1.00 25.22           C
ANISOU  723  C   GLY A 400     3897   3246   2439    573    257    641       C
ATOM    724  O   GLY A 400       0.617 -27.956  41.491  1.00 27.47           O
ANISOU  724  O   GLY A 400     4180   3499   2757    532    322    756       O
ATOM    725  N   LYS A 401       0.745 -25.906  40.604  1.00 17.61           N
ANISOU  725  N   LYS A 401     2896   2263   1532    572    264    513       N
ATOM    726  CA  LYS A 401      -0.455 -26.131  39.795  1.00 20.70           C
ANISOU  726  CA  LYS A 401     3229   2620   2016    528    339    506       C
ATOM    727  C   LYS A 401      -0.220 -25.734  38.353  1.00 18.22           C
ANISOU  727  C   LYS A 401     2877   2213   1834    522    295    423       C
ATOM    728  O   LYS A 401       0.629 -24.892  38.032  1.00 18.35           O
ANISOU  728  O   LYS A 401     2907   2206   1860    558    225    347       O
ATOM    729  CB  LYS A 401      -1.674 -25.379  40.346  1.00 21.47           C
ANISOU  729  CB  LYS A 401     3295   2833   2029    544    422    459       C
ATOM    730  CG  LYS A 401      -1.982 -25.789  41.823  1.00 27.94           C
ANISOU  730  CG  LYS A 401     4149   3776   2693    547    481    546       C
ATOM    731  CD  LYS A 401      -3.306 -25.259  42.277  1.00 42.66           C
ANISOU  731  CD  LYS A 401     5963   5760   4485    561    586    512       C
ATOM    732  CE  LYS A 401      -3.676 -25.810  43.627  1.00 45.51           C
ANISOU  732  CE  LYS A 401     6347   6251   4693    551    658    617       C
ATOM    733  NZ  LYS A 401      -2.655 -25.349  44.607  1.00 45.50           N
ANISOU  733  NZ  LYS A 401     6429   6317   4543    607    592    587       N
ATOM    734  N   LEU A 402      -1.026 -26.318  37.461  1.00 16.71           N
ANISOU  734  N   LEU A 402     2631   1979   1740    466    339    437       N
ATOM    735  CA  LEU A 402      -0.952 -25.936  36.058  1.00 14.15           C
ANISOU  735  CA  LEU A 402     2262   1597   1518    460    304    362       C
ATOM    736  C   LEU A 402      -2.281 -25.278  35.656  1.00 16.81           C
ANISOU  736  C   LEU A 402     2521   2007   1859    457    358    316       C
ATOM    737  O   LEU A 402      -3.361 -25.897  35.755  1.00 19.63           O
ANISOU  737  O   LEU A 402     2826   2411   2221    402    427    359       O
ATOM    738  CB  LEU A 402      -0.637 -27.112  35.148  1.00 14.79           C
ANISOU  738  CB  LEU A 402     2339   1575   1707    402    291    393       C
ATOM    739  CG  LEU A 402       0.770 -27.745  35.389  1.00 20.24           C
ANISOU  739  CG  LEU A 402     3093   2185   2412    431    236    441       C
ATOM    740  CD1 LEU A 402       0.880 -28.907  34.458  1.00 19.69           C
ANISOU  740  CD1 LEU A 402     3022   2004   2457    381    245    454       C
ATOM    741  CD2 LEU A 402       1.869 -26.739  35.055  1.00 15.24           C
ANISOU  741  CD2 LEU A 402     2463   1557   1772    489    157    372       C
ATOM    742  N   LEU A 403      -2.193 -24.032  35.218  1.00 13.50           N
ANISOU  742  N   LEU A 403     2088   1599   1444    517    330    237       N
ATOM    743  CA  LEU A 403      -3.355 -23.233  34.812  1.00 17.35           C
ANISOU  743  CA  LEU A 403     2499   2155   1938    548    374    199       C
ATOM    744  C   LEU A 403      -3.569 -23.457  33.309  1.00 15.60           C
ANISOU  744  C   LEU A 403     2206   1910   1809    508    346    190       C
ATOM    745  O   LEU A 403      -3.202 -22.645  32.447  1.00 14.03           O
ANISOU  745  O   LEU A 403     1999   1684   1648    548    301    149       O
ATOM    746  CB  LEU A 403      -3.152 -21.752  35.165  1.00 14.02           C
ANISOU  746  CB  LEU A 403     2112   1737   1476    643    364    127       C
ATOM    747  CG  LEU A 403      -4.365 -20.780  35.107  1.00 15.28           C
ANISOU  747  CG  LEU A 403     2208   1969   1629    718    427     93       C
ATOM    748  CD1 LEU A 403      -4.096 -19.453  35.856  1.00 28.11           C
ANISOU  748  CD1 LEU A 403     3905   3573   3204    812    435     12       C
ATOM    749  CD2 LEU A 403      -4.770 -20.429  33.745  1.00 24.41           C
ANISOU  749  CD2 LEU A 403     3286   3119   2870    729    406     93       C
ATOM    750  N   PHE A 404      -4.144 -24.623  32.997  1.00 14.66           N
ANISOU  750  N   PHE A 404     2041   1803   1724    418    374    229       N
ATOM    751  CA  PHE A 404      -4.520 -24.883  31.614  1.00 17.02           C
ANISOU  751  CA  PHE A 404     2264   2112   2090    367    351    204       C
ATOM    752  C   PHE A 404      -5.523 -23.828  31.131  1.00 15.65           C
ANISOU  752  C   PHE A 404     1993   2048   1907    426    366    184       C
ATOM    753  O   PHE A 404      -5.443 -23.358  29.977  1.00 16.58           O
ANISOU  753  O   PHE A 404     2069   2176   2056    444    321    158       O
ATOM    754  CB  PHE A 404      -5.094 -26.297  31.497  1.00 15.40           C
ANISOU  754  CB  PHE A 404     2027   1901   1921    244    386    235       C
ATOM    755  CG  PHE A 404      -4.056 -27.406  31.618  1.00 13.86           C
ANISOU  755  CG  PHE A 404     1927   1570   1768    198    367    257       C
ATOM    756  CD1 PHE A 404      -3.352 -27.849  30.476  1.00 18.31           C
ANISOU  756  CD1 PHE A 404     2505   2056   2395    170    318    208       C
ATOM    757  CD2 PHE A 404      -3.861 -28.070  32.848  1.00 17.41           C
ANISOU  757  CD2 PHE A 404     2445   1980   2190    186    406    333       C
ATOM    758  CE1 PHE A 404      -2.391 -28.875  30.562  1.00 17.40           C
ANISOU  758  CE1 PHE A 404     2473   1809   2328    149    309    226       C
ATOM    759  CE2 PHE A 404      -2.946 -29.106  32.940  1.00 16.78           C
ANISOU  759  CE2 PHE A 404     2447   1770   2157    162    391    370       C
ATOM    760  CZ  PHE A 404      -2.221 -29.530  31.778  1.00 14.02           C
ANISOU  760  CZ  PHE A 404     2111   1328   1887    147    344    312       C
ATOM    761  N   ALA A 405      -6.455 -23.438  31.989  1.00 15.92           N
ANISOU  761  N   ALA A 405     1987   2171   1892    466    431    201       N
ATOM    762  CA  ALA A 405      -7.379 -22.338  31.723  1.00 17.05           C
ANISOU  762  CA  ALA A 405     2041   2412   2025    557    456    189       C
ATOM    763  C   ALA A 405      -7.729 -21.727  33.062  1.00 15.37           C
ANISOU  763  C   ALA A 405     1858   2239   1745    640    526    185       C
ATOM    764  O   ALA A 405      -7.558 -22.373  34.095  1.00 17.46           O
ANISOU  764  O   ALA A 405     2178   2499   1959    597    561    208       O
ATOM    765  CB  ALA A 405      -8.673 -22.810  31.022  1.00 16.20           C
ANISOU  765  CB  ALA A 405     1778   2440   1936    495    479    212       C
ATOM    766  N   PRO A 406      -8.379 -20.546  33.069  1.00 18.17           N
ANISOU  766  N   PRO A 406     2165   2649   2090    762    558    163       N
ATOM    767  CA  PRO A 406      -8.708 -19.929  34.365  1.00 16.85           C
ANISOU  767  CA  PRO A 406     2034   2519   1850    851    635    136       C
ATOM    768  C   PRO A 406      -9.689 -20.746  35.154  1.00 22.47           C
ANISOU  768  C   PRO A 406     2669   3364   2504    796    722    183       C
ATOM    769  O   PRO A 406      -9.676 -20.693  36.392  1.00 23.75           O
ANISOU  769  O   PRO A 406     2888   3555   2579    823    782    172       O
ATOM    770  CB  PRO A 406      -9.271 -18.549  33.978  1.00 18.87           C
ANISOU  770  CB  PRO A 406     2244   2791   2135   1001    655    105       C
ATOM    771  CG  PRO A 406      -8.594 -18.248  32.698  1.00 17.18           C
ANISOU  771  CG  PRO A 406     2044   2485   1998    993    565    112       C
ATOM    772  CD  PRO A 406      -8.512 -19.574  31.962  1.00 16.61           C
ANISOU  772  CD  PRO A 406     1919   2446   1948    845    519    155       C
ATOM    773  N   ASN A 407     -10.548 -21.505  34.475  1.00 21.04           N
ANISOU  773  N   ASN A 407     2356   3276   2363    709    732    233       N
ATOM    774  CA  ASN A 407     -11.461 -22.425  35.122  1.00 23.75           C
ANISOU  774  CA  ASN A 407     2616   3741   2668    619    814    291       C
ATOM    775  C   ASN A 407     -10.989 -23.880  35.038  1.00 21.22           C
ANISOU  775  C   ASN A 407     2340   3346   2376    447    786    340       C
ATOM    776  O   ASN A 407     -11.815 -24.806  35.163  1.00 22.99           O
ANISOU  776  O   ASN A 407     2474   3653   2606    329    839    396       O
ATOM    777  CB  ASN A 407     -12.864 -22.273  34.527  1.00 21.42           C
ANISOU  777  CB  ASN A 407     2123   3617   2397    629    854    314       C
ATOM    778  CG  ASN A 407     -12.954 -22.704  33.035  1.00 21.59           C
ANISOU  778  CG  ASN A 407     2062   3641   2500    539    767    317       C
ATOM    779  OD1 ASN A 407     -11.983 -22.613  32.264  1.00 22.60           O
ANISOU  779  OD1 ASN A 407     2277   3641   2669    535    679    286       O
ATOM    780  ND2 ASN A 407     -14.177 -23.145  32.629  1.00 26.02           N
ANISOU  780  ND2 ASN A 407     2440   4373   3074    465    797    352       N
ATOM    781  N   LEU A 408      -9.683 -24.106  34.822  1.00 22.60           N
ANISOU  781  N   LEU A 408     2647   3362   2577    429    708    321       N
ATOM    782  CA  LEU A 408      -9.164 -25.469  34.739  1.00 21.25           C
ANISOU  782  CA  LEU A 408     2532   3096   2447    291    686    366       C
ATOM    783  C   LEU A 408      -7.735 -25.465  35.285  1.00 18.23           C
ANISOU  783  C   LEU A 408     2306   2582   2039    333    637    362       C
ATOM    784  O   LEU A 408      -6.769 -25.530  34.520  1.00 18.32           O
ANISOU  784  O   LEU A 408     2372   2482   2106    330    558    330       O
ATOM    785  CB  LEU A 408      -9.214 -26.004  33.309  1.00 18.26           C
ANISOU  785  CB  LEU A 408     2095   2682   2162    201    626    339       C
ATOM    786  CG  LEU A 408      -9.063 -27.521  33.225  1.00 22.45           C
ANISOU  786  CG  LEU A 408     2659   3123   2748     44    632    377       C
ATOM    787  CD1 LEU A 408     -10.095 -28.241  34.043  1.00 25.38           C
ANISOU  787  CD1 LEU A 408     2967   3578   3099    -52    727    453       C
ATOM    788  CD2 LEU A 408      -9.123 -27.948  31.775  1.00 21.79           C
ANISOU  788  CD2 LEU A 408     2521   3015   2742    -41    573    319       C
ATOM    789  N   LEU A 409      -7.655 -25.353  36.602  1.00 20.10           N
ANISOU  789  N   LEU A 409     2600   2857   2180    373    686    395       N
ATOM    790  CA  LEU A 409      -6.400 -25.318  37.332  1.00 19.91           C
ANISOU  790  CA  LEU A 409     2708   2754   2103    414    642    400       C
ATOM    791  C   LEU A 409      -6.204 -26.680  37.974  1.00 23.38           C
ANISOU  791  C   LEU A 409     3194   3158   2533    323    669    510       C
ATOM    792  O   LEU A 409      -6.952 -27.050  38.881  1.00 24.59           O
ANISOU  792  O   LEU A 409     3323   3405   2615    293    755    581       O
ATOM    793  CB  LEU A 409      -6.442 -24.199  38.374  1.00 25.04           C
ANISOU  793  CB  LEU A 409     3393   3487   2635    524    674    350       C
ATOM    794  CG  LEU A 409      -5.160 -23.965  39.195  1.00 24.83           C
ANISOU  794  CG  LEU A 409     3491   3414   2530    566    617    334       C
ATOM    795  CD1 LEU A 409      -4.182 -23.186  38.358  1.00 25.03           C
ANISOU  795  CD1 LEU A 409     3553   3333   2623    607    521    251       C
ATOM    796  CD2 LEU A 409      -5.528 -23.216  40.495  1.00 33.73           C
ANISOU  796  CD2 LEU A 409     4645   4662   3508    641    681    296       C
ATOM    797  N   LEU A 410      -5.195 -27.419  37.499  1.00 19.04           N
ANISOU  797  N   LEU A 410     2710   2470   2054    287    603    532       N
ATOM    798  CA  LEU A 410      -5.002 -28.815  37.860  1.00 24.68           C
ANISOU  798  CA  LEU A 410     3471   3107   2799    203    627    644       C
ATOM    799  C   LEU A 410      -3.764 -28.990  38.740  1.00 28.88           C
ANISOU  799  C   LEU A 410     4112   3596   3266    265    582    703       C
ATOM    800  O   LEU A 410      -2.768 -28.296  38.549  1.00 19.62           O
ANISOU  800  O   LEU A 410     2977   2397   2081    340    502    636       O
ATOM    801  CB  LEU A 410      -4.881 -29.658  36.584  1.00 23.34           C
ANISOU  801  CB  LEU A 410     3287   2807   2775    118    597    622       C
ATOM    802  CG  LEU A 410      -6.150 -29.568  35.737  1.00 25.18           C
ANISOU  802  CG  LEU A 410     3397   3112   3057     42    633    570       C
ATOM    803  CD1 LEU A 410      -6.035 -30.544  34.572  1.00 24.87           C
ANISOU  803  CD1 LEU A 410     3354   2950   3144    -62    606    539       C
ATOM    804  CD2 LEU A 410      -7.320 -29.923  36.564  1.00 26.33           C
ANISOU  804  CD2 LEU A 410     3483   3365   3156    -25    732    649       C
ATOM    805  N   ASP A 411      -3.821 -29.923  39.695  1.00 30.02           N
ANISOU  805  N   ASP A 411     4301   3740   3365    229    633    837       N
ATOM    806  CA  ASP A 411      -2.655 -30.234  40.507  1.00 29.51           C
ANISOU  806  CA  ASP A 411     4329   3647   3237    289    584    918       C
ATOM    807  C   ASP A 411      -2.096 -31.571  40.048  1.00 33.43           C
ANISOU  807  C   ASP A 411     4874   3967   3863    244    571   1007       C
ATOM    808  O   ASP A 411      -2.700 -32.277  39.240  1.00 32.47           O
ANISOU  808  O   ASP A 411     4723   3748   3865    151    610   1002       O
ATOM    809  CB  ASP A 411      -2.981 -30.216  42.022  1.00 30.83           C
ANISOU  809  CB  ASP A 411     4521   3960   3232    310    643   1018       C
ATOM    810  CG  ASP A 411      -3.993 -31.285  42.459  1.00 31.57           C
ANISOU  810  CG  ASP A 411     4597   4060   3338    209    755   1162       C
ATOM    811  OD1 ASP A 411      -4.129 -32.333  41.783  1.00 36.85           O
ANISOU  811  OD1 ASP A 411     5268   4578   4154    122    773   1217       O
ATOM    812  OD2 ASP A 411      -4.711 -31.069  43.467  1.00 41.60           O
ANISOU  812  OD2 ASP A 411     5847   5489   4471    208    834   1214       O
ATOM    813  N   ARG A 412      -0.924 -31.899  40.586  1.00 32.79           N
ANISOU  813  N   ARG A 412     4864   3847   3748    316    514   1085       N
ATOM    814  CA  ARG A 412      -0.235 -33.152  40.301  1.00 36.89           C
ANISOU  814  CA  ARG A 412     5440   4191   4384    311    503   1183       C
ATOM    815  C   ARG A 412      -1.140 -34.382  40.456  1.00 40.19           C
ANISOU  815  C   ARG A 412     5877   4515   4878    202    605   1307       C
ATOM    816  O   ARG A 412      -1.112 -35.291  39.617  1.00 42.62           O
ANISOU  816  O   ARG A 412     6206   4642   5345    144    620   1303       O
ATOM    817  CB  ARG A 412       0.964 -33.245  41.245  1.00 40.14           C
ANISOU  817  CB  ARG A 412     5903   4644   4704    413    435   1277       C
ATOM    818  CG  ARG A 412       1.705 -34.466  41.149  1.00 35.88           C
ANISOU  818  CG  ARG A 412     5384   3967   4280    413    398   1339       C
ATOM    819  CD  ARG A 412       3.086 -34.269  41.728  1.00 30.66           C
ANISOU  819  CD  ARG A 412     4722   3376   3552    513    291   1355       C
ATOM    820  NE  ARG A 412       3.936 -35.239  41.064  1.00 35.69           N
ANISOU  820  NE  ARG A 412     5363   3858   4341    534    252   1355       N
ATOM    821  CZ  ARG A 412       3.977 -36.531  41.361  1.00 37.57           C
ANISOU  821  CZ  ARG A 412     5639   3985   4651    516    274   1461       C
ATOM    822  NH1 ARG A 412       3.257 -36.999  42.365  1.00 35.63           N
ANISOU  822  NH1 ARG A 412     5426   3776   4336    470    330   1589       N
ATOM    823  NH2 ARG A 412       4.760 -37.331  40.664  1.00 32.78           N
ANISOU  823  NH2 ARG A 412     5039   3238   4179    549    242   1438       N
ATOM    824  N   ASN A 413      -1.924 -34.440  41.542  1.00 38.14           N
ANISOU  824  N   ASN A 413     5613   4376   4504    166    680   1415       N
ATOM    825  CA  ASN A 413      -2.755 -35.617  41.800  1.00 36.87           C
ANISOU  825  CA  ASN A 413     5454   4142   4414     42    762   1523       C
ATOM    826  C   ASN A 413      -3.772 -35.838  40.687  1.00 40.58           C
ANISOU  826  C   ASN A 413     5870   4529   5019    -87    830   1451       C
ATOM    827  O   ASN A 413      -4.010 -36.980  40.275  1.00 42.28           O
ANISOU  827  O   ASN A 413     6110   4579   5377   -192    858   1482       O
ATOM    828  CB  ASN A 413      -3.466 -35.488  43.137  1.00 39.87           C
ANISOU  828  CB  ASN A 413     5814   4704   4630     21    824   1623       C
ATOM    829  CG  ASN A 413      -2.564 -35.788  44.294  1.00 40.50           C
ANISOU  829  CG  ASN A 413     5951   4831   4605    100    761   1721       C
ATOM    830  OD1 ASN A 413      -1.463 -36.302  44.114  1.00 45.27           O
ANISOU  830  OD1 ASN A 413     6602   5317   5280    158    678   1736       O
ATOM    831  ND2 ASN A 413      -3.040 -35.513  45.500  1.00 44.98           N
ANISOU  831  ND2 ASN A 413     6507   5582   5002    100    803   1786       N
ATOM    832  N   GLN A 414      -4.391 -34.756  40.195  1.00 34.46           N
ANISOU  832  N   GLN A 414     4998   3892   4203    -91    818   1298       N
ATOM    833  CA  GLN A 414      -5.255 -34.853  39.019  1.00 39.91           C
ANISOU  833  CA  GLN A 414     5606   4547   5011   -206    836   1183       C
ATOM    834  C   GLN A 414      -4.497 -35.328  37.777  1.00 38.88           C
ANISOU  834  C   GLN A 414     5516   4226   5030   -211    771   1090       C
ATOM    835  O   GLN A 414      -5.093 -35.939  36.884  1.00 45.11           O
ANISOU  835  O   GLN A 414     6272   4929   5937   -336    795   1030       O
ATOM    836  CB  GLN A 414      -5.908 -33.507  38.766  1.00 35.41           C
ANISOU  836  CB  GLN A 414     4927   4169   4358   -167    824   1054       C
ATOM    837  CG  GLN A 414      -6.991 -33.224  39.751  1.00 34.78           C
ANISOU  837  CG  GLN A 414     4781   4272   4164   -195    918   1124       C
ATOM    838  CD  GLN A 414      -7.422 -31.783  39.712  1.00 40.98           C
ANISOU  838  CD  GLN A 414     5481   5236   4852   -105    906   1005       C
ATOM    839  OE1 GLN A 414      -6.591 -30.887  39.841  1.00 31.82           O
ANISOU  839  OE1 GLN A 414     4368   4096   3627     21    838    937       O
ATOM    840  NE2 GLN A 414      -8.724 -31.542  39.556  1.00 40.44           N
ANISOU  840  NE2 GLN A 414     5286   5300   4781   -168    976    981       N
ATOM    841  N   GLY A 415      -3.195 -35.080  37.698  1.00 37.00           N
ANISOU  841  N   GLY A 415     5342   3932   4783    -83    690   1070       N
ATOM    842  CA  GLY A 415      -2.430 -35.632  36.585  1.00 36.56           C
ANISOU  842  CA  GLY A 415     5327   3700   4864    -78    643    992       C
ATOM    843  C   GLY A 415      -2.205 -37.129  36.684  1.00 45.81           C
ANISOU  843  C   GLY A 415     6592   4653   6162   -131    692   1100       C
ATOM    844  O   GLY A 415      -2.106 -37.806  35.653  1.00 42.83           O
ANISOU  844  O   GLY A 415     6234   4121   5920   -188    690   1011       O
ATOM    845  N   LYS A 416      -2.092 -37.657  37.917  1.00 46.65           N
ANISOU  845  N   LYS A 416     6739   4777   6209   -110    706   1254       N
ATOM    846  CA  LYS A 416      -1.952 -39.101  38.133  1.00 50.56           C
ANISOU  846  CA  LYS A 416     7295   5114   6804   -161    711   1327       C
ATOM    847  C   LYS A 416      -2.993 -39.864  37.344  1.00 50.14           C
ANISOU  847  C   LYS A 416     7228   4941   6881   -340    778   1272       C
ATOM    848  O   LYS A 416      -2.699 -40.871  36.683  1.00 51.43           O
ANISOU  848  O   LYS A 416     7440   4925   7177   -376    760   1219       O
ATOM    849  CB  LYS A 416      -2.173 -39.466  39.602  1.00 47.02           C
ANISOU  849  CB  LYS A 416     6870   4741   6253   -162    741   1507       C
ATOM    850  CG  LYS A 416      -1.276 -38.930  40.647  1.00 49.44           C
ANISOU  850  CG  LYS A 416     7191   5180   6414    -18    680   1584       C
ATOM    851  CD  LYS A 416       0.114 -39.467  40.597  1.00 60.63           C
ANISOU  851  CD  LYS A 416     8655   6500   7881     96    591   1591       C
ATOM    852  CE  LYS A 416       0.814 -38.794  41.730  1.00 47.62           C
ANISOU  852  CE  LYS A 416     7000   5029   6063    209    536   1664       C
ATOM    853  NZ  LYS A 416       0.182 -39.318  42.986  1.00 54.64           N
ANISOU  853  NZ  LYS A 416     7918   5979   6865    157    593   1829       N
ATOM    854  N   SER A 417      -4.236 -39.399  37.459  1.00 46.50           N
ANISOU  854  N   SER A 417     6693   4598   6378   -455    855   1281       N
ATOM    855  CA  SER A 417      -5.392 -40.145  37.012  1.00 48.32           C
ANISOU  855  CA  SER A 417     6886   4765   6709   -656    921   1256       C
ATOM    856  C   SER A 417      -5.314 -40.474  35.534  1.00 50.46           C
ANISOU  856  C   SER A 417     7156   4901   7117   -723    892   1075       C
ATOM    857  O   SER A 417      -5.859 -41.494  35.102  1.00 47.90           O
ANISOU  857  O   SER A 417     6842   4455   6904   -871    912   1039       O
ATOM    858  CB  SER A 417      -6.657 -39.348  37.321  1.00 54.18           C
ANISOU  858  CB  SER A 417     7509   5715   7363   -746   1003   1278       C
ATOM    859  OG  SER A 417      -6.822 -38.303  36.374  1.00 52.10           O
ANISOU  859  OG  SER A 417     7149   5579   7069   -717    949   1102       O
ATOM    860  N   VAL A 418      -4.635 -39.656  34.738  1.00 48.34           N
ANISOU  860  N   VAL A 418     6878   4653   6835   -620    840    953       N
ATOM    861  CA  VAL A 418      -4.450 -39.999  33.334  1.00 46.01           C
ANISOU  861  CA  VAL A 418     6588   4246   6650   -671    805    771       C
ATOM    862  C   VAL A 418      -3.132 -40.765  33.205  1.00 43.97           C
ANISOU  862  C   VAL A 418     6428   3834   6446   -541    739    763       C
ATOM    863  O   VAL A 418      -2.061 -40.206  33.439  1.00 40.00           O
ANISOU  863  O   VAL A 418     5942   3375   5880   -370    683    785       O
ATOM    864  CB  VAL A 418      -4.483 -38.757  32.448  1.00 44.70           C
ANISOU  864  CB  VAL A 418     6320   4257   6405   -624    741    618       C
ATOM    865  CG1 VAL A 418      -4.161 -39.144  31.017  1.00 47.31           C
ANISOU  865  CG1 VAL A 418     6665   4482   6828   -664    706    437       C
ATOM    866  N   GLU A 419      -3.209 -42.064  32.886  1.00 42.58           N
ANISOU  866  N   GLU A 419     6307   3487   6384   -623    746    737       N
ATOM    867  CA  GLU A 419      -2.015 -42.875  32.625  1.00 45.23           C
ANISOU  867  CA  GLU A 419     6728   3673   6785   -505    696    714       C
ATOM    868  C   GLU A 419      -1.026 -42.174  31.687  1.00 40.47           C
ANISOU  868  C   GLU A 419     6104   3118   6157   -374    635    576       C
ATOM    869  O   GLU A 419      -1.416 -41.658  30.637  1.00 39.47           O
ANISOU  869  O   GLU A 419     5925   3041   6030   -439    634    423       O
ATOM    870  CB  GLU A 419      -2.397 -44.218  31.993  1.00 51.21           C
ANISOU  870  CB  GLU A 419     7541   4239   7678   -633    719    640       C
ATOM    871  CG  GLU A 419      -1.147 -45.075  31.761  1.00 48.63           C
ANISOU  871  CG  GLU A 419     7303   3755   7420   -495    679    624       C
ATOM    872  CD  GLU A 419      -1.406 -46.424  31.154  1.00 74.58           C
ANISOU  872  CD  GLU A 419    10664   6830  10843   -599    703    547       C
ATOM    873  OE1 GLU A 419      -2.581 -46.772  30.906  1.00 78.82           O
ANISOU  873  OE1 GLU A 419    11182   7339  11427   -796    742    504       O
ATOM    874  OE2 GLU A 419      -0.406 -47.105  30.836  1.00 87.11           O
ANISOU  874  OE2 GLU A 419    12322   8287  12491   -484    679    513       O
ATOM    875  N   GLY A 420       0.275 -42.213  32.045  1.00 39.48           N
ANISOU  875  N   GLY A 420     6011   2983   6008   -198    581    631       N
ATOM    876  CA  GLY A 420       1.334 -41.586  31.269  1.00 39.12           C
ANISOU  876  CA  GLY A 420     5935   2998   5933    -70    521    523       C
ATOM    877  C   GLY A 420       1.631 -40.104  31.555  1.00 36.32           C
ANISOU  877  C   GLY A 420     5511   2833   5456     15    483    543       C
ATOM    878  O   GLY A 420       2.648 -39.584  31.077  1.00 38.04           O
ANISOU  878  O   GLY A 420     5700   3111   5645    128    426    481       O
ATOM    879  N   MET A 421       0.811 -39.399  32.320  1.00 37.29           N
ANISOU  879  N   MET A 421     5606   3056   5505    -33    514    627       N
ATOM    880  CA  MET A 421       0.933 -37.939  32.319  1.00 36.57           C
ANISOU  880  CA  MET A 421     5458   3127   5311     31    485    605       C
ATOM    881  C   MET A 421       1.787 -37.306  33.431  1.00 35.86           C
ANISOU  881  C   MET A 421     5361   3151   5112    165    430    715       C
ATOM    882  O   MET A 421       2.354 -36.221  33.205  1.00 27.56           O
ANISOU  882  O   MET A 421     4268   2209   3994    244    378    664       O
ATOM    883  CB  MET A 421      -0.472 -37.323  32.305  1.00 39.08           C
ANISOU  883  CB  MET A 421     5730   3523   5596    -93    546    595       C
ATOM    884  CG  MET A 421      -0.434 -35.843  32.001  1.00 37.62           C
ANISOU  884  CG  MET A 421     5452   3546   5295    -33    480    515       C
ATOM    885  SD  MET A 421      -1.991 -34.950  32.016  1.00 43.98           S
ANISOU  885  SD  MET A 421     6140   4556   6016   -135    499    478       S
ATOM    886  CE  MET A 421      -3.129 -36.035  31.254  1.00 49.13           C
ANISOU  886  CE  MET A 421     6768   5125   6774   -330    557    414       C
ATOM    887  N   VAL A 422       1.909 -37.930  34.603  1.00 32.12           N
ANISOU  887  N   VAL A 422     4926   2662   4615    184    437    859       N
ATOM    888  CA  VAL A 422       2.420 -37.204  35.770  1.00 30.34           C
ANISOU  888  CA  VAL A 422     4688   2580   4259    277    395    958       C
ATOM    889  C   VAL A 422       3.873 -36.791  35.563  1.00 27.81           C
ANISOU  889  C   VAL A 422     4336   2311   3919    400    302    911       C
ATOM    890  O   VAL A 422       4.279 -35.694  35.955  1.00 25.81           O
ANISOU  890  O   VAL A 422     4047   2197   3562    459    254    907       O
ATOM    891  CB  VAL A 422       2.203 -38.033  37.061  1.00 38.24           C
ANISOU  891  CB  VAL A 422     5735   3565   5230    262    424   1127       C
ATOM    892  CG1 VAL A 422       3.027 -39.340  37.068  1.00 33.47           C
ANISOU  892  CG1 VAL A 422     5179   2815   4723    303    400   1172       C
ATOM    893  CG2 VAL A 422       2.427 -37.180  38.315  1.00 36.19           C
ANISOU  893  CG2 VAL A 422     5461   3486   4806    331    395   1219       C
ATOM    894  N   GLU A 423       4.666 -37.614  34.866  1.00 27.64           N
ANISOU  894  N   GLU A 423     4323   2182   3998    434    277    863       N
ATOM    895  CA  GLU A 423       6.069 -37.256  34.647  1.00 31.42           C
ANISOU  895  CA  GLU A 423     4755   2720   4462    542    199    825       C
ATOM    896  C   GLU A 423       6.158 -35.961  33.859  1.00 23.53           C
ANISOU  896  C   GLU A 423     3693   1825   3420    544    170    707       C
ATOM    897  O   GLU A 423       7.007 -35.112  34.139  1.00 24.36           O
ANISOU  897  O   GLU A 423     3751   2047   3459    607    107    706       O
ATOM    898  CB  GLU A 423       6.780 -38.386  33.885  1.00 32.93           C
ANISOU  898  CB  GLU A 423     4967   2772   4772    578    197    781       C
ATOM    899  CG  GLU A 423       6.572 -39.794  34.556  1.00 41.89           C
ANISOU  899  CG  GLU A 423     6181   3762   5972    568    236    897       C
ATOM    900  CD  GLU A 423       5.191 -40.409  34.201  1.00 46.35           C
ANISOU  900  CD  GLU A 423     6801   4206   6605    431    317    873       C
ATOM    901  OE1 GLU A 423       4.567 -41.056  35.073  1.00 54.17           O
ANISOU  901  OE1 GLU A 423     7843   5139   7600    380    358    995       O
ATOM    902  OE2 GLU A 423       4.709 -40.193  33.064  1.00 65.90           O
ANISOU  902  OE2 GLU A 423     9261   6656   9122    366    340    733       O
ATOM    903  N   ILE A 424       5.261 -35.791  32.885  1.00 24.54           N
ANISOU  903  N   ILE A 424     3822   1914   3587    467    215    609       N
ATOM    904  CA  ILE A 424       5.253 -34.608  32.034  1.00 27.52           C
ANISOU  904  CA  ILE A 424     4147   2381   3930    468    192    502       C
ATOM    905  C   ILE A 424       4.755 -33.417  32.836  1.00 21.28           C
ANISOU  905  C   ILE A 424     3347   1710   3028    472    186    545       C
ATOM    906  O   ILE A 424       5.298 -32.312  32.802  1.00 19.34           O
ANISOU  906  O   ILE A 424     3060   1569   2720    516    133    508       O
ATOM    907  CB  ILE A 424       4.321 -34.795  30.826  1.00 29.03           C
ANISOU  907  CB  ILE A 424     4344   2501   4183    382    247    394       C
ATOM    908  CG1 ILE A 424       4.640 -36.010  29.950  1.00 36.23           C
ANISOU  908  CG1 ILE A 424     5281   3285   5198    365    264    325       C
ATOM    909  CG2 ILE A 424       4.518 -33.581  29.945  1.00 22.60           C
ANISOU  909  CG2 ILE A 424     3474   1788   3327    404    214    299       C
ATOM    910  CD1 ILE A 424       5.856 -36.020  29.345  1.00 37.88           C
ANISOU  910  CD1 ILE A 424     5458   3516   5421    447    217    271       C
ATOM    911  N   PHE A 425       3.691 -33.651  33.571  1.00 25.94           N
ANISOU  911  N   PHE A 425     3979   2283   3595    417    250    618       N
ATOM    912  CA  PHE A 425       3.118 -32.668  34.518  1.00 24.42           C
ANISOU  912  CA  PHE A 425     3781   2220   3279    428    249    663       C
ATOM    913  C   PHE A 425       4.225 -32.170  35.456  1.00 23.60           C
ANISOU  913  C   PHE A 425     3684   2206   3079    518    185    731       C
ATOM    914  O   PHE A 425       4.404 -30.997  35.641  1.00 16.03           O
ANISOU  914  O   PHE A 425     2699   1356   2036    550    140    679       O
ATOM    915  CB  PHE A 425       2.047 -33.416  35.287  1.00 31.47           C
ANISOU  915  CB  PHE A 425     4673   3117   4168    323    328    699       C
ATOM    916  CG  PHE A 425       0.897 -32.588  35.753  1.00 34.30           C
ANISOU  916  CG  PHE A 425     5012   3617   4403    316    347    741       C
ATOM    917  CD1 PHE A 425       1.098 -31.576  36.665  1.00 45.02           C
ANISOU  917  CD1 PHE A 425     6328   5116   5663    338    330    686       C
ATOM    918  CD2 PHE A 425      -0.370 -32.820  35.275  1.00 34.81           C
ANISOU  918  CD2 PHE A 425     5061   3644   4520    205    424    755       C
ATOM    919  CE1 PHE A 425       0.036 -30.817  37.111  1.00 30.19           C
ANISOU  919  CE1 PHE A 425     4426   3348   3694    306    388    717       C
ATOM    920  CE2 PHE A 425      -1.426 -32.058  35.714  1.00 45.73           C
ANISOU  920  CE2 PHE A 425     6396   5149   5831    148    480    773       C
ATOM    921  CZ  PHE A 425      -1.214 -31.061  36.629  1.00 48.05           C
ANISOU  921  CZ  PHE A 425     6665   5592   5999    211    464    754       C
ATOM    922  N   ASP A 426       4.985 -33.113  36.020  1.00 22.78           N
ANISOU  922  N   ASP A 426     3586   2067   3001    549    157    802       N
ATOM    923  CA  ASP A 426       6.125 -32.721  36.864  1.00 23.13           C
ANISOU  923  CA  ASP A 426     3611   2214   2964    625     79    846       C
ATOM    924  C   ASP A 426       7.168 -31.878  36.129  1.00 21.09           C
ANISOU  924  C   ASP A 426     3292   2005   2717    664      8    746       C
ATOM    925  O   ASP A 426       7.687 -30.906  36.698  1.00 19.71           O
ANISOU  925  O   ASP A 426     3100   1944   2443    700    -49    741       O
ATOM    926  CB  ASP A 426       6.756 -33.969  37.458  1.00 25.82           C
ANISOU  926  CB  ASP A 426     3969   2499   3344    656     67    954       C
ATOM    927  CG  ASP A 426       5.945 -34.496  38.621  1.00 32.03           C
ANISOU  927  CG  ASP A 426     4810   3298   4064    627    118   1085       C
ATOM    928  OD1 ASP A 426       5.136 -33.692  39.178  1.00 28.99           O
ANISOU  928  OD1 ASP A 426     4436   3014   3567    603    147   1093       O
ATOM    929  OD2 ASP A 426       6.086 -35.698  38.959  1.00 32.58           O
ANISOU  929  OD2 ASP A 426     4912   3277   4191    630    134   1178       O
ATOM    930  N   MET A 427       7.480 -32.193  34.857  1.00 20.80           N
ANISOU  930  N   MET A 427     3222   1891   2791    652     12    662       N
ATOM    931  CA  MET A 427       8.444 -31.368  34.126  1.00 20.25           C
ANISOU  931  CA  MET A 427     3086   1878   2729    678    -43    579       C
ATOM    932  C   MET A 427       7.880 -29.987  33.829  1.00 17.22           C
ANISOU  932  C   MET A 427     2696   1562   2286    651    -48    503       C
ATOM    933  O   MET A 427       8.594 -28.974  33.933  1.00 20.76           O
ANISOU  933  O   MET A 427     3112   2090   2684    674   -104    474       O
ATOM    934  CB  MET A 427       8.827 -32.068  32.822  1.00 20.39           C
ANISOU  934  CB  MET A 427     3076   1811   2862    675    -26    510       C
ATOM    935  CG  MET A 427       9.627 -33.413  33.050  1.00 21.10           C
ANISOU  935  CG  MET A 427     3176   1823   3019    728    -31    573       C
ATOM    936  SD  MET A 427       9.955 -34.100  31.380  1.00 32.26           S
ANISOU  936  SD  MET A 427     4568   3140   4547    731      0    456       S
ATOM    937  CE  MET A 427       8.417 -34.533  30.758  1.00 29.90           C
ANISOU  937  CE  MET A 427     4333   2744   4286    639     71    398       C
ATOM    938  N   LEU A 428       6.590 -29.921  33.477  1.00 15.92           N
ANISOU  938  N   LEU A 428     2563   1359   2128    603     11    475       N
ATOM    939  CA  LEU A 428       5.915 -28.622  33.308  1.00 19.12           C
ANISOU  939  CA  LEU A 428     2966   1823   2475    590     10    413       C
ATOM    940  C   LEU A 428       5.972 -27.763  34.578  1.00 19.60           C
ANISOU  940  C   LEU A 428     3042   1986   2418    608    -23    435       C
ATOM    941  O   LEU A 428       6.223 -26.547  34.501  1.00 16.53           O
ANISOU  941  O   LEU A 428     2633   1657   1992    607    -63    365       O
ATOM    942  CB  LEU A 428       4.445 -28.826  32.907  1.00 13.53           C
ANISOU  942  CB  LEU A 428     2254   1097   1789    517     79    385       C
ATOM    943  CG  LEU A 428       4.391 -29.333  31.454  1.00 16.91           C
ANISOU  943  CG  LEU A 428     2656   1456   2313    485     97    318       C
ATOM    944  CD1 LEU A 428       3.027 -29.928  31.166  1.00 19.31           C
ANISOU  944  CD1 LEU A 428     2955   1736   2647    399    160    306       C
ATOM    945  CD2 LEU A 428       4.700 -28.185  30.402  1.00 17.95           C
ANISOU  945  CD2 LEU A 428     2731   1648   2440    492     58    231       C
ATOM    946  N   LEU A 429       5.628 -28.357  35.726  1.00 14.16           N
ANISOU  946  N   LEU A 429     2396   1316   1667    614      2    526       N
ATOM    947  CA  LEU A 429       5.669 -27.638  37.009  1.00 17.65           C
ANISOU  947  CA  LEU A 429     2859   1875   1973    631    -26    540       C
ATOM    948  C   LEU A 429       7.069 -27.114  37.310  1.00 22.98           C
ANISOU  948  C   LEU A 429     3517   2610   2606    675   -121    528       C
ATOM    949  O   LEU A 429       7.224 -25.981  37.807  1.00 18.44           O
ANISOU  949  O   LEU A 429     2941   2120   1945    665   -161    457       O
ATOM    950  CB  LEU A 429       5.213 -28.560  38.143  1.00 21.10           C
ANISOU  950  CB  LEU A 429     3341   2332   2344    636     18    667       C
ATOM    951  CG  LEU A 429       3.705 -28.808  38.154  1.00 23.32           C
ANISOU  951  CG  LEU A 429     3627   2603   2631    574    115    674       C
ATOM    952  CD1 LEU A 429       3.370 -29.962  39.121  1.00 18.75           C
ANISOU  952  CD1 LEU A 429     3094   2016   2015    568    168    829       C
ATOM    953  CD2 LEU A 429       2.907 -27.531  38.484  1.00 20.56           C
ANISOU  953  CD2 LEU A 429     3261   2361   2192    563    135    580       C
ATOM    954  N   ALA A 430       8.099 -27.924  37.039  1.00 20.47           N
ANISOU  954  N   ALA A 430     3181   2249   2348    722   -156    591       N
ATOM    955  CA  ALA A 430       9.461 -27.468  37.315  1.00 19.32           C
ANISOU  955  CA  ALA A 430     2994   2185   2163    759   -251    587       C
ATOM    956  C   ALA A 430       9.850 -26.326  36.402  1.00 18.06           C
ANISOU  956  C   ALA A 430     2786   2030   2046    721   -284    465       C
ATOM    957  O   ALA A 430      10.608 -25.435  36.816  1.00 21.94           O
ANISOU  957  O   ALA A 430     3252   2610   2476    707   -356    421       O
ATOM    958  CB  ALA A 430      10.475 -28.630  37.143  1.00 22.12           C
ANISOU  958  CB  ALA A 430     3294   2508   2605    792   -265    662       C
ATOM    959  N   THR A 431       9.381 -26.331  35.148  1.00 20.73           N
ANISOU  959  N   THR A 431     3110   2280   2485    696   -234    412       N
ATOM    960  CA  THR A 431       9.685 -25.215  34.259  1.00 18.40           C
ANISOU  960  CA  THR A 431     2775   1991   2226    660   -257    317       C
ATOM    961  C   THR A 431       9.009 -23.951  34.765  1.00 18.82           C
ANISOU  961  C   THR A 431     2859   2082   2210    617   -257    246       C
ATOM    962  O   THR A 431       9.579 -22.859  34.735  1.00 22.04           O
ANISOU  962  O   THR A 431     3251   2518   2605    588   -305    183       O
ATOM    963  CB  THR A 431       9.224 -25.521  32.814  1.00 19.50           C
ANISOU  963  CB  THR A 431     2894   2051   2466    646   -201    285       C
ATOM    964  OG1 THR A 431       9.700 -26.811  32.447  1.00 21.95           O
ANISOU  964  OG1 THR A 431     3172   2323   2844    661   -178    326       O
ATOM    965  CG2 THR A 431       9.802 -24.535  31.781  1.00 18.51           C
ANISOU  965  CG2 THR A 431     2714   1938   2379    620   -226    221       C
ATOM    966  N   SER A 432       7.776 -24.076  35.208  1.00 17.06           N
ANISOU  966  N   SER A 432     2680   1852   1949    612   -198    251       N
ATOM    967  CA  SER A 432       7.083 -22.909  35.725  1.00 17.98           C
ANISOU  967  CA  SER A 432     2829   2002   2002    593   -185    177       C
ATOM    968  C   SER A 432       7.780 -22.389  36.976  1.00 22.04           C
ANISOU  968  C   SER A 432     3369   2602   2403    592   -247    155       C
ATOM    969  O   SER A 432       7.931 -21.170  37.146  1.00 21.09           O
ANISOU  969  O   SER A 432     3266   2491   2258    566   -273     61       O
ATOM    970  CB  SER A 432       5.612 -23.303  35.985  1.00 20.45           C
ANISOU  970  CB  SER A 432     3165   2314   2292    596    -99    199       C
ATOM    971  OG  SER A 432       4.877 -22.231  36.486  1.00 31.73           O
ANISOU  971  OG  SER A 432     4620   3777   3661    599    -72    128       O
ATOM    972  N   SER A 433       8.215 -23.297  37.868  1.00 19.84           N
ANISOU  972  N   SER A 433     3098   2387   2054    620   -273    241       N
ATOM    973  CA  SER A 433       9.008 -22.865  39.017  1.00 24.48           C
ANISOU  973  CA  SER A 433     3696   3088   2518    615   -350    223       C
ATOM    974  C   SER A 433      10.290 -22.162  38.590  1.00 23.31           C
ANISOU  974  C   SER A 433     3495   2952   2408    582   -438    166       C
ATOM    975  O   SER A 433      10.745 -21.236  39.273  1.00 23.43           O
ANISOU  975  O   SER A 433     3522   3038   2342    540   -497     83       O
ATOM    976  CB  SER A 433       9.363 -24.051  39.923  1.00 30.33           C
ANISOU  976  CB  SER A 433     4439   3904   3180    663   -371    357       C
ATOM    977  OG  SER A 433       8.216 -24.818  40.216  1.00 42.89           O
ANISOU  977  OG  SER A 433     6073   5470   4755    680   -281    430       O
ATOM    978  N   ARG A 434      10.926 -22.646  37.507  1.00 19.49           N
ANISOU  978  N   ARG A 434     2950   2411   2043    595   -446    208       N
ATOM    979  CA  ARG A 434      12.163 -22.052  36.998  1.00 21.02           C
ANISOU  979  CA  ARG A 434     3075   2629   2283    559   -518    170       C
ATOM    980  C   ARG A 434      11.914 -20.651  36.455  1.00 20.79           C
ANISOU  980  C   ARG A 434     3064   2539   2296    488   -507     55       C
ATOM    981  O   ARG A 434      12.669 -19.724  36.759  1.00 22.29           O
ANISOU  981  O   ARG A 434     3238   2770   2461    424   -573    -15       O
ATOM    982  CB  ARG A 434      12.746 -22.957  35.894  1.00 20.17           C
ANISOU  982  CB  ARG A 434     2899   2476   2290    602   -504    240       C
ATOM    983  CG  ARG A 434      13.966 -22.396  35.223  1.00 30.36           C
ANISOU  983  CG  ARG A 434     4101   3798   3635    566   -559    212       C
ATOM    984  CD  ARG A 434      15.136 -22.376  36.171  1.00 35.24           C
ANISOU  984  CD  ARG A 434     4660   4555   4176    563   -660    236       C
ATOM    985  NE  ARG A 434      16.358 -22.092  35.432  1.00 39.42           N
ANISOU  985  NE  ARG A 434     5078   5128   4773    536   -704    232       N
ATOM    986  CZ  ARG A 434      17.360 -21.353  35.889  1.00 42.24           C
ANISOU  986  CZ  ARG A 434     5366   5596   5088    465   -795    194       C
ATOM    987  NH1 ARG A 434      17.294 -20.820  37.099  1.00 39.63           N
ANISOU  987  NH1 ARG A 434     5077   5343   4638    417   -857    144       N
ATOM    988  NH2 ARG A 434      18.428 -21.152  35.126  1.00 42.81           N
ANISOU  988  NH2 ARG A 434     5323   5712   5232    437   -821    201       N
ATOM    989  N   PHE A 435      10.855 -20.478  35.649  1.00 18.74           N
ANISOU  989  N   PHE A 435     2835   2181   2103    495   -427     37       N
ATOM    990  CA  PHE A 435      10.434 -19.130  35.250  1.00 17.01           C
ANISOU  990  CA  PHE A 435     2648   1894   1920    449   -406    -54       C
ATOM    991  C   PHE A 435      10.163 -18.247  36.434  1.00 23.00           C
ANISOU  991  C   PHE A 435     3476   2679   2583    425   -422   -145       C
ATOM    992  O   PHE A 435      10.514 -17.057  36.405  1.00 21.04           O
ANISOU  992  O   PHE A 435     3249   2389   2356    365   -448   -233       O
ATOM    993  CB  PHE A 435       9.211 -19.125  34.331  1.00 20.28           C
ANISOU  993  CB  PHE A 435     3077   2227   2401    479   -320    -44       C
ATOM    994  CG  PHE A 435       9.466 -19.572  32.907  1.00 26.21           C
ANISOU  994  CG  PHE A 435     3766   2943   3250    483   -303      5       C
ATOM    995  CD1 PHE A 435      10.760 -19.647  32.422  1.00 19.72           C
ANISOU  995  CD1 PHE A 435     2880   2146   2466    458   -353     24       C
ATOM    996  CD2 PHE A 435       8.406 -19.703  32.007  1.00 25.98           C
ANISOU  996  CD2 PHE A 435     3735   2870   3267    505   -237     18       C
ATOM    997  CE1 PHE A 435      11.016 -19.946  31.062  1.00 27.25           C
ANISOU  997  CE1 PHE A 435     3776   3081   3497    462   -328     56       C
ATOM    998  CE2 PHE A 435       8.655 -20.044  30.666  1.00 25.59           C
ANISOU  998  CE2 PHE A 435     3629   2807   3286    502   -223     48       C
ATOM    999  CZ  PHE A 435       9.966 -20.170  30.217  1.00 27.24           C
ANISOU  999  CZ  PHE A 435     3784   3039   3526    484   -265     65       C
ATOM   1000  N   ARG A 436       9.504 -18.792  37.476  1.00 22.26           N
ANISOU 1000  N   ARG A 436     3425   2650   2382    466   -399   -128       N
ATOM   1001  CA  ARG A 436       9.195 -17.972  38.647  1.00 21.38           C
ANISOU 1001  CA  ARG A 436     3385   2582   2157    450   -404   -230       C
ATOM   1002  C   ARG A 436      10.482 -17.535  39.329  1.00 24.60           C
ANISOU 1002  C   ARG A 436     3777   3073   2498    383   -511   -286       C
ATOM   1003  O   ARG A 436      10.641 -16.359  39.688  1.00 28.65           O
ANISOU 1003  O   ARG A 436     4336   3560   2989    324   -534   -416       O
ATOM   1004  CB  ARG A 436       8.301 -18.753  39.627  1.00 21.27           C
ANISOU 1004  CB  ARG A 436     3406   2649   2025    506   -353   -182       C
ATOM   1005  CG  ARG A 436       7.870 -17.978  40.856  1.00 26.23           C
ANISOU 1005  CG  ARG A 436     4109   3344   2515    502   -342   -293       C
ATOM   1006  CD  ARG A 436       7.115 -18.918  41.840  1.00 29.61           C
ANISOU 1006  CD  ARG A 436     4556   3884   2810    554   -291   -213       C
ATOM   1007  NE  ARG A 436       6.291 -19.828  41.107  1.00 32.53           N
ANISOU 1007  NE  ARG A 436     4893   4196   3270    592   -214   -101       N
ATOM   1008  CZ  ARG A 436       6.307 -21.153  41.197  1.00 29.37           C
ANISOU 1008  CZ  ARG A 436     4467   3830   2863    612   -205     42       C
ATOM   1009  NH1 ARG A 436       7.060 -21.782  42.065  1.00 26.80           N
ANISOU 1009  NH1 ARG A 436     4141   3609   2434    619   -265    115       N
ATOM   1010  NH2 ARG A 436       5.520 -21.842  40.380  1.00 28.87           N
ANISOU 1010  NH2 ARG A 436     4377   3689   2903    625   -134    112       N
ATOM   1011  N   MET A 437      11.431 -18.468  39.500  1.00 21.98           N
ANISOU 1011  N   MET A 437     3376   2839   2137    392   -579   -191       N
ATOM   1012  CA  MET A 437      12.702 -18.115  40.122  1.00 23.31           C
ANISOU 1012  CA  MET A 437     3501   3119   2236    327   -693   -233       C
ATOM   1013  C   MET A 437      13.393 -16.984  39.360  1.00 27.34           C
ANISOU 1013  C   MET A 437     3985   3549   2853    230   -726   -323       C
ATOM   1014  O   MET A 437      13.893 -16.034  39.974  1.00 28.49           O
ANISOU 1014  O   MET A 437     4151   3729   2945    140   -788   -443       O
ATOM   1015  CB  MET A 437      13.613 -19.352  40.197  1.00 28.21           C
ANISOU 1015  CB  MET A 437     4030   3849   2840    376   -752    -92       C
ATOM   1016  N   MET A 438      13.442 -17.078  38.018  1.00 24.93           N
ANISOU 1016  N   MET A 438     3634   3140   2696    239   -684   -267       N
ATOM   1017  CA  MET A 438      14.080 -16.086  37.149  1.00 26.24           C
ANISOU 1017  CA  MET A 438     3769   3228   2975    149   -701   -317       C
ATOM   1018  C   MET A 438      13.282 -14.816  37.007  1.00 24.80           C
ANISOU 1018  C   MET A 438     3684   2900   2837    111   -646   -425       C
ATOM   1019  O   MET A 438      13.745 -13.892  36.341  1.00 27.25           O
ANISOU 1019  O   MET A 438     3986   3123   3245     30   -653   -461       O
ATOM   1020  CB  MET A 438      14.315 -16.672  35.744  1.00 18.75           C
ANISOU 1020  CB  MET A 438     2740   2235   2149    184   -663   -212       C
ATOM   1021  CG  MET A 438      15.047 -18.005  35.771  1.00 29.50           C
ANISOU 1021  CG  MET A 438     4009   3711   3489    248   -699   -104       C
ATOM   1022  SD  MET A 438      15.563 -18.397  34.081  1.00 31.80           S
ANISOU 1022  SD  MET A 438     4204   3958   3920    265   -657    -26       S
ATOM   1023  CE  MET A 438      16.483 -16.912  33.581  1.00 28.85           C
ANISOU 1023  CE  MET A 438     3784   3565   3614    121   -697    -93       C
ATOM   1024  N   ASN A 439      12.091 -14.752  37.589  1.00 26.28           N
ANISOU 1024  N   ASN A 439     3964   3058   2965    174   -584   -466       N
ATOM   1025  CA  ASN A 439      11.197 -13.596  37.430  1.00 27.40           C
ANISOU 1025  CA  ASN A 439     4199   3052   3158    175   -515   -559       C
ATOM   1026  C   ASN A 439      11.065 -13.213  35.939  1.00 25.32           C
ANISOU 1026  C   ASN A 439     3908   2658   3053    175   -467   -496       C
ATOM   1027  O   ASN A 439      11.162 -12.040  35.551  1.00 25.34           O
ANISOU 1027  O   ASN A 439     3953   2533   3141    120   -455   -554       O
ATOM   1028  CB  ASN A 439      11.677 -12.411  38.286  1.00 25.08           C
ANISOU 1028  CB  ASN A 439     3973   2733   2822     77   -564   -720       C
ATOM   1029  CG  ASN A 439      10.584 -11.332  38.470  1.00 32.62           C
ANISOU 1029  CG  ASN A 439     5050   3541   3804    113   -479   -832       C
ATOM   1030  OD1 ASN A 439       9.394 -11.588  38.264  1.00 33.31           O
ANISOU 1030  OD1 ASN A 439     5162   3596   3899    224   -390   -789       O
ATOM   1031  ND2 ASN A 439      11.001 -10.125  38.794  1.00 36.15           N
ANISOU 1031  ND2 ASN A 439     5566   3891   4277     19   -504   -974       N
ATOM   1032  N   LEU A 440      10.767 -14.221  35.120  1.00 20.97           N
ANISOU 1032  N   LEU A 440     3293   2137   2536    241   -433   -376       N
ATOM   1033  CA  LEU A 440      10.542 -14.026  33.665  1.00 21.97           C
ANISOU 1033  CA  LEU A 440     3387   2178   2782    255   -385   -306       C
ATOM   1034  C   LEU A 440       9.466 -12.955  33.421  1.00 23.77           C
ANISOU 1034  C   LEU A 440     3693   2275   3064    292   -315   -345       C
ATOM   1035  O   LEU A 440       8.425 -13.052  33.987  1.00 21.66           O
ANISOU 1035  O   LEU A 440     3475   2010   2746    367   -264   -376       O
ATOM   1036  CB  LEU A 440      10.087 -15.343  33.028  1.00 23.69           C
ANISOU 1036  CB  LEU A 440     3545   2455   2999    329   -351   -204       C
ATOM   1037  CG  LEU A 440      10.020 -15.320  31.503  1.00 18.96           C
ANISOU 1037  CG  LEU A 440     2898   1809   2497    338   -313   -133       C
ATOM   1038  CD1 LEU A 440      11.400 -15.379  30.929  1.00 17.15           C
ANISOU 1038  CD1 LEU A 440     2593   1622   2300    269   -368   -106       C
ATOM   1039  CD2 LEU A 440       9.130 -16.394  30.926  1.00 20.68           C
ANISOU 1039  CD2 LEU A 440     3083   2064   2709    408   -265    -70       C
ATOM   1040  N   GLN A 441       9.745 -12.022  32.520  1.00 23.57           N
ANISOU 1040  N   GLN A 441     3671   2141   3144    249   -305   -331       N
ATOM   1041  CA  GLN A 441       8.840 -10.933  32.175  1.00 23.59           C
ANISOU 1041  CA  GLN A 441     3745   2001   3217    293   -239   -348       C
ATOM   1042  C   GLN A 441       8.068 -11.257  30.894  1.00 22.31           C
ANISOU 1042  C   GLN A 441     3529   1841   3105    371   -185   -228       C
ATOM   1043  O   GLN A 441       8.529 -12.030  30.044  1.00 19.45           O
ANISOU 1043  O   GLN A 441     3082   1558   2749    354   -202   -145       O
ATOM   1044  CB  GLN A 441       9.631  -9.632  31.988  1.00 25.86           C
ANISOU 1044  CB  GLN A 441     4077   2150   3596    192   -259   -390       C
ATOM   1045  CG  GLN A 441      10.397  -9.217  33.242  1.00 27.73           C
ANISOU 1045  CG  GLN A 441     4366   2390   3780     94   -321   -530       C
ATOM   1046  CD  GLN A 441       9.443  -8.916  34.388  1.00 31.28           C
ANISOU 1046  CD  GLN A 441     4917   2812   4156    166   -284   -651       C
ATOM   1047  OE1 GLN A 441       8.676  -7.945  34.330  1.00 32.27           O
ANISOU 1047  OE1 GLN A 441     5131   2785   4346    219   -218   -697       O
ATOM   1048  NE2 GLN A 441       9.482  -9.747  35.438  1.00 26.04           N
ANISOU 1048  NE2 GLN A 441     4241   2301   3353    178   -319   -698       N
ATOM   1049  N   GLY A 442       6.887 -10.649  30.760  1.00 20.43           N
ANISOU 1049  N   GLY A 442     3330   1536   2897    457   -118   -225       N
ATOM   1050  CA  GLY A 442       6.046 -10.944  29.603  1.00 20.78           C
ANISOU 1050  CA  GLY A 442     3282   1646   2969    511    -68   -111       C
ATOM   1051  C   GLY A 442       6.743 -10.603  28.292  1.00 22.73           C
ANISOU 1051  C   GLY A 442     3492   1855   3288    469    -81    -17       C
ATOM   1052  O   GLY A 442       6.619 -11.326  27.311  1.00 19.25           O
ANISOU 1052  O   GLY A 442     2975   1504   2834    486    -79     66       O
ATOM   1053  N   GLU A 443       7.550  -9.540  28.280  1.00 20.41           N
ANISOU 1053  N   GLU A 443     3258   1429   3067    401    -96    -33       N
ATOM   1054  CA  GLU A 443       8.246  -9.199  27.034  1.00 21.43           C
ANISOU 1054  CA  GLU A 443     3358   1521   3263    353   -105     74       C
ATOM   1055  C   GLU A 443       9.265 -10.269  26.686  1.00 21.34           C
ANISOU 1055  C   GLU A 443     3252   1652   3205    286   -152     99       C
ATOM   1056  O   GLU A 443       9.533 -10.522  25.506  1.00 23.49           O
ANISOU 1056  O   GLU A 443     3452   1988   3485    278   -141    198       O
ATOM   1057  CB  GLU A 443       8.952  -7.864  27.147  1.00 27.64           C
ANISOU 1057  CB  GLU A 443     4214   2142   4146    263   -105     54       C
ATOM   1058  CG  GLU A 443       8.004  -6.691  27.324  1.00 27.83           C
ANISOU 1058  CG  GLU A 443     4273   2061   4240    322    -29     41       C
ATOM   1059  CD  GLU A 443       7.624  -6.439  28.792  1.00 42.71           C
ANISOU 1059  CD  GLU A 443     6224   3910   6094    336    -26   -118       C
ATOM   1060  OE1 GLU A 443       8.012  -7.223  29.701  1.00 31.28           O
ANISOU 1060  OE1 GLU A 443     4801   2534   4550    306    -77   -211       O
ATOM   1061  OE2 GLU A 443       6.896  -5.452  29.019  1.00 40.79           O
ANISOU 1061  OE2 GLU A 443     6005   3572   5922    386     14   -146       O
ATOM   1062  N   GLU A 444       9.859 -10.877  27.687  1.00 17.49           N
ANISOU 1062  N   GLU A 444     2759   1224   2663    243   -199     14       N
ATOM   1063  CA  GLU A 444      10.805 -11.954  27.428  1.00 17.78           C
ANISOU 1063  CA  GLU A 444     2699   1397   2659    204   -238     40       C
ATOM   1064  C   GLU A 444      10.060 -13.204  26.997  1.00 19.49           C
ANISOU 1064  C   GLU A 444     2869   1716   2819    293   -213     77       C
ATOM   1065  O   GLU A 444      10.473 -13.905  26.056  1.00 17.04           O
ANISOU 1065  O   GLU A 444     2481   1490   2503    292   -208    134       O
ATOM   1066  CB  GLU A 444      11.621 -12.227  28.684  1.00 20.52           C
ANISOU 1066  CB  GLU A 444     3051   1786   2960    146   -301    -49       C
ATOM   1067  CG  GLU A 444      12.673 -11.171  29.065  1.00 24.47           C
ANISOU 1067  CG  GLU A 444     3568   2221   3510     18   -345    -98       C
ATOM   1068  CD  GLU A 444      13.266 -11.438  30.449  1.00 25.57           C
ANISOU 1068  CD  GLU A 444     3715   2427   3574    -28   -417   -199       C
ATOM   1069  OE1 GLU A 444      12.516 -11.891  31.353  1.00 21.85           O
ANISOU 1069  OE1 GLU A 444     3295   1982   3024     44   -413   -252       O
ATOM   1070  OE2 GLU A 444      14.483 -11.220  30.650  1.00 25.28           O
ANISOU 1070  OE2 GLU A 444     3622   2436   3548   -139   -478   -219       O
ATOM   1071  N   PHE A 445       8.923 -13.474  27.643  1.00 18.06           N
ANISOU 1071  N   PHE A 445     2736   1529   2599    366   -189     39       N
ATOM   1072  CA  PHE A 445       8.103 -14.618  27.223  1.00 18.41           C
ANISOU 1072  CA  PHE A 445     2737   1659   2600    432   -162     71       C
ATOM   1073  C   PHE A 445       7.772 -14.565  25.729  1.00 17.96           C
ANISOU 1073  C   PHE A 445     2626   1632   2566    451   -132    151       C
ATOM   1074  O   PHE A 445       7.927 -15.559  25.006  1.00 14.52           O
ANISOU 1074  O   PHE A 445     2128   1285   2104    453   -130    175       O
ATOM   1075  CB  PHE A 445       6.823 -14.637  28.059  1.00 17.85           C
ANISOU 1075  CB  PHE A 445     2716   1573   2493    498   -130     30       C
ATOM   1076  CG  PHE A 445       5.766 -15.538  27.521  1.00 14.32           C
ANISOU 1076  CG  PHE A 445     2208   1215   2019    534    -92     65       C
ATOM   1077  CD1 PHE A 445       5.942 -16.921  27.515  1.00 13.17           C
ANISOU 1077  CD1 PHE A 445     2030   1136   1837    528   -102     68       C
ATOM   1078  CD2 PHE A 445       4.591 -14.984  27.014  1.00 14.11           C
ANISOU 1078  CD2 PHE A 445     2154   1201   2008    569    -51     93       C
ATOM   1079  CE1 PHE A 445       4.943 -17.746  27.005  1.00 14.57           C
ANISOU 1079  CE1 PHE A 445     2162   1377   1996    545    -69     86       C
ATOM   1080  CE2 PHE A 445       3.554 -15.815  26.514  1.00 16.68           C
ANISOU 1080  CE2 PHE A 445     2422   1613   2302    596    -28    116       C
ATOM   1081  CZ  PHE A 445       3.734 -17.182  26.513  1.00 15.22           C
ANISOU 1081  CZ  PHE A 445     2219   1480   2084    579    -37    107       C
ATOM   1082  N   VAL A 446       7.292 -13.422  25.240  1.00 14.28           N
ANISOU 1082  N   VAL A 446     2186   1095   2145    473   -106    195       N
ATOM   1083  CA  VAL A 446       6.842 -13.445  23.842  1.00 18.06           C
ANISOU 1083  CA  VAL A 446     2606   1635   2619    503    -81    284       C
ATOM   1084  C   VAL A 446       8.011 -13.666  22.898  1.00 18.29           C
ANISOU 1084  C   VAL A 446     2576   1725   2650    439    -94    331       C
ATOM   1085  O   VAL A 446       7.845 -14.243  21.811  1.00 16.71           O
ANISOU 1085  O   VAL A 446     2311   1629   2407    454    -80    374       O
ATOM   1086  CB  VAL A 446       6.036 -12.172  23.493  1.00 18.86           C
ANISOU 1086  CB  VAL A 446     2727   1673   2764    537    -59    333       C
ATOM   1087  CG1 VAL A 446       4.799 -12.108  24.377  1.00 18.73           C
ANISOU 1087  CG1 VAL A 446     2719   1662   2736    582    -42    270       C
ATOM   1088  CG2 VAL A 446       6.879 -10.870  23.627  1.00 14.64           C
ANISOU 1088  CG2 VAL A 446     2262    989   2312    491    -60    356       C
ATOM   1089  N   CYS A 447       9.204 -13.203  23.268  1.00 16.75           N
ANISOU 1089  N   CYS A 447     2392   1478   2495    364   -117    317       N
ATOM   1090  CA  CYS A 447      10.360 -13.422  22.408  1.00 15.65           C
ANISOU 1090  CA  CYS A 447     2178   1414   2356    304   -121    364       C
ATOM   1091  C   CYS A 447      10.690 -14.912  22.352  1.00 16.79           C
ANISOU 1091  C   CYS A 447     2262   1674   2443    323   -130    320       C
ATOM   1092  O   CYS A 447      11.037 -15.465  21.292  1.00 15.32           O
ANISOU 1092  O   CYS A 447     2008   1588   2226    325   -109    352       O
ATOM   1093  CB  CYS A 447      11.569 -12.664  22.972  1.00 17.34           C
ANISOU 1093  CB  CYS A 447     2402   1561   2627    207   -150    349       C
ATOM   1094  SG  CYS A 447      11.582 -10.839  22.725  1.00 24.23           S
ANISOU 1094  SG  CYS A 447     3342   2269   3597    149   -128    418       S
ATOM   1095  N   LEU A 448      10.634 -15.572  23.505  1.00 13.31           N
ANISOU 1095  N   LEU A 448     1851   1220   1988    338   -157    245       N
ATOM   1096  CA  LEU A 448      10.980 -16.996  23.580  1.00 10.54           C
ANISOU 1096  CA  LEU A 448     1458    947   1602    364   -162    211       C
ATOM   1097  C   LEU A 448       9.994 -17.830  22.792  1.00 11.61           C
ANISOU 1097  C   LEU A 448     1579   1134   1699    414   -126    210       C
ATOM   1098  O   LEU A 448      10.381 -18.780  22.101  1.00 14.53           O
ANISOU 1098  O   LEU A 448     1900   1574   2048    425   -110    199       O
ATOM   1099  CB  LEU A 448      10.987 -17.463  25.046  1.00 12.91           C
ANISOU 1099  CB  LEU A 448     1801   1215   1888    376   -197    155       C
ATOM   1100  CG  LEU A 448      12.203 -17.034  25.862  1.00 16.29           C
ANISOU 1100  CG  LEU A 448     2217   1640   2332    320   -249    139       C
ATOM   1101  CD1 LEU A 448      12.105 -17.652  27.306  1.00 16.17           C
ANISOU 1101  CD1 LEU A 448     2244   1627   2274    345   -284     93       C
ATOM   1102  CD2 LEU A 448      13.515 -17.463  25.239  1.00 19.47           C
ANISOU 1102  CD2 LEU A 448     2524   2126   2749    298   -258    167       C
ATOM   1103  N   LYS A 449       8.704 -17.466  22.864  1.00 12.89           N
ANISOU 1103  N   LYS A 449     1780   1267   1851    444   -111    215       N
ATOM   1104  CA  LYS A 449       7.703 -18.227  22.124  1.00 14.96           C
ANISOU 1104  CA  LYS A 449     2017   1597   2072    474    -85    208       C
ATOM   1105  C   LYS A 449       7.915 -18.041  20.613  1.00 16.09           C
ANISOU 1105  C   LYS A 449     2100   1827   2187    465    -68    256       C
ATOM   1106  O   LYS A 449       7.745 -18.986  19.843  1.00 14.60           O
ANISOU 1106  O   LYS A 449     1873   1722   1954    468    -52    225       O
ATOM   1107  CB  LYS A 449       6.297 -17.777  22.548  1.00 13.37           C
ANISOU 1107  CB  LYS A 449     1847   1369   1866    510    -75    213       C
ATOM   1108  CG  LYS A 449       5.183 -18.710  22.121  1.00 18.31           C
ANISOU 1108  CG  LYS A 449     2439   2069   2450    524    -57    190       C
ATOM   1109  CD  LYS A 449       3.875 -18.425  22.886  1.00 17.81           C
ANISOU 1109  CD  LYS A 449     2396   1988   2385    560    -44    187       C
ATOM   1110  CE  LYS A 449       3.487 -16.945  22.777  1.00 19.04           C
ANISOU 1110  CE  LYS A 449     2564   2105   2564    607    -38    247       C
ATOM   1111  NZ  LYS A 449       2.014 -16.801  23.107  1.00 19.53           N
ANISOU 1111  NZ  LYS A 449     2608   2200   2614    661    -14    251       N
ATOM   1112  N   SER A 450       8.302 -16.815  20.175  1.00 12.71           N
ANISOU 1112  N   SER A 450     1668   1380   1781    449    -66    332       N
ATOM   1113  CA  SER A 450       8.609 -16.583  18.769  1.00 14.13           C
ANISOU 1113  CA  SER A 450     1790   1658   1922    438    -45    397       C
ATOM   1114  C   SER A 450       9.864 -17.341  18.321  1.00 12.96           C
ANISOU 1114  C   SER A 450     1588   1581   1756    409    -34    368       C
ATOM   1115  O   SER A 450       9.897 -17.874  17.191  1.00 14.40           O
ANISOU 1115  O   SER A 450     1718   1883   1871    415     -8    366       O
ATOM   1116  CB  SER A 450       8.780 -15.078  18.540  1.00 17.63           C
ANISOU 1116  CB  SER A 450     2253   2039   2409    422    -40    502       C
ATOM   1117  OG  SER A 450       7.476 -14.541  18.413  1.00 26.21           O
ANISOU 1117  OG  SER A 450     3361   3110   3487    479    -36    546       O
ATOM   1118  N   ILE A 451      10.909 -17.394  19.178  1.00 15.47           N
ANISOU 1118  N   ILE A 451     1910   1843   2126    382    -52    342       N
ATOM   1119  CA  ILE A 451      12.072 -18.238  18.883  1.00 14.23           C
ANISOU 1119  CA  ILE A 451     1690   1759   1958    377    -40    310       C
ATOM   1120  C   ILE A 451      11.656 -19.685  18.614  1.00 14.10           C
ANISOU 1120  C   ILE A 451     1670   1788   1901    426    -21    227       C
ATOM   1121  O   ILE A 451      12.054 -20.280  17.591  1.00 16.60           O
ANISOU 1121  O   ILE A 451     1934   2203   2171    439     16    205       O
ATOM   1122  CB  ILE A 451      13.130 -18.122  19.992  1.00 12.57           C
ANISOU 1122  CB  ILE A 451     1475   1495   1806    350    -76    296       C
ATOM   1123  CG1 ILE A 451      13.851 -16.772  19.789  1.00 18.34           C
ANISOU 1123  CG1 ILE A 451     2182   2212   2575    274    -80    374       C
ATOM   1124  CG2 ILE A 451      14.222 -19.236  19.862  1.00 13.29           C
ANISOU 1124  CG2 ILE A 451     1494   1663   1892    379    -64    258       C
ATOM   1125  CD1 ILE A 451      14.608 -16.241  21.085  1.00 16.36           C
ANISOU 1125  CD1 ILE A 451     1946   1887   2383    216   -133    353       C
ATOM   1126  N   ILE A 452      10.842 -20.267  19.505  1.00 15.82           N
ANISOU 1126  N   ILE A 452     1945   1933   2133    449    -39    176       N
ATOM   1127  CA  ILE A 452      10.405 -21.657  19.332  1.00 15.10           C
ANISOU 1127  CA  ILE A 452     1863   1854   2021    478    -18     97       C
ATOM   1128  C   ILE A 452       9.742 -21.859  17.953  1.00 15.84           C
ANISOU 1128  C   ILE A 452     1926   2051   2042    471     12     76       C
ATOM   1129  O   ILE A 452      10.007 -22.849  17.259  1.00 14.76           O
ANISOU 1129  O   ILE A 452     1768   1965   1876    484     43      5       O
ATOM   1130  CB  ILE A 452       9.447 -22.072  20.472  1.00 17.98           C
ANISOU 1130  CB  ILE A 452     2293   2129   2409    486    -36     70       C
ATOM   1131  CG1 ILE A 452      10.189 -22.138  21.866  1.00 11.50           C
ANISOU 1131  CG1 ILE A 452     1501   1232   1635    499    -67     80       C
ATOM   1132  CG2 ILE A 452       8.760 -23.485  20.095  1.00 12.31           C
ANISOU 1132  CG2 ILE A 452     1588   1414   1675    491     -7    -10       C
ATOM   1133  CD1 ILE A 452       9.191 -22.341  23.038  1.00 14.68           C
ANISOU 1133  CD1 ILE A 452     1970   1565   2042    503    -78     71       C
ATOM   1134  N   LEU A 453       8.807 -20.963  17.575  1.00 12.61           N
ANISOU 1134  N   LEU A 453     1516   1676   1600    458      1    131       N
ATOM   1135  CA  LEU A 453       8.153 -21.053  16.277  1.00 16.91           C
ANISOU 1135  CA  LEU A 453     2020   2349   2057    450     16    125       C
ATOM   1136  C   LEU A 453       9.165 -21.117  15.148  1.00 19.51           C
ANISOU 1136  C   LEU A 453     2293   2789   2330    447     50    130       C
ATOM   1137  O   LEU A 453       9.083 -21.960  14.246  1.00 16.16           O
ANISOU 1137  O   LEU A 453     1843   2463   1834    446     75     50       O
ATOM   1138  CB  LEU A 453       7.214 -19.833  16.089  1.00 16.66           C
ANISOU 1138  CB  LEU A 453     1984   2341   2006    456     -4    225       C
ATOM   1139  CG  LEU A 453       6.576 -19.702  14.686  1.00 14.18           C
ANISOU 1139  CG  LEU A 453     1612   2194   1582    455      0    254       C
ATOM   1140  CD1 LEU A 453       5.643 -20.877  14.485  1.00 15.86           C
ANISOU 1140  CD1 LEU A 453     1813   2465   1747    436     -6    141       C
ATOM   1141  CD2 LEU A 453       5.797 -18.398  14.560  1.00 16.28           C
ANISOU 1141  CD2 LEU A 453     1871   2470   1846    485    -18    383       C
ATOM   1142  N   LEU A 454      10.163 -20.260  15.195  1.00 13.91           N
ANISOU 1142  N   LEU A 454     1563   2071   1652    440     55    213       N
ATOM   1143  CA  LEU A 454      11.031 -20.161  14.046  1.00 17.07           C
ANISOU 1143  CA  LEU A 454     1896   2602   1988    433     96    240       C
ATOM   1144  C   LEU A 454      12.156 -21.184  14.085  1.00 19.15           C
ANISOU 1144  C   LEU A 454     2130   2878   2268    456    130    154       C
ATOM   1145  O   LEU A 454      12.651 -21.587  13.013  1.00 18.01           O
ANISOU 1145  O   LEU A 454     1932   2864   2046    467    178    121       O
ATOM   1146  CB  LEU A 454      11.620 -18.756  13.944  1.00 16.71           C
ANISOU 1146  CB  LEU A 454     1829   2551   1969    400     96    381       C
ATOM   1147  CG  LEU A 454      10.627 -17.627  13.626  1.00 20.16           C
ANISOU 1147  CG  LEU A 454     2288   2986   2386    396     78    494       C
ATOM   1148  CD1 LEU A 454      11.384 -16.328  13.901  1.00 20.02           C
ANISOU 1148  CD1 LEU A 454     2275   2889   2444    354     81    615       C
ATOM   1149  CD2 LEU A 454      10.172 -17.697  12.203  1.00 20.73           C
ANISOU 1149  CD2 LEU A 454     2311   3240   2325    406    101    526       C
ATOM   1150  N   ASN A 455      12.486 -21.673  15.280  1.00 14.69           N
ANISOU 1150  N   ASN A 455     1598   2188   1793    475    108    113       N
ATOM   1151  CA  ASN A 455      13.642 -22.549  15.480  1.00 17.15           C
ANISOU 1151  CA  ASN A 455     1876   2500   2142    517    135     57       C
ATOM   1152  C   ASN A 455      13.316 -24.030  15.439  1.00 21.65           C
ANISOU 1152  C   ASN A 455     2482   3032   2710    566    160    -70       C
ATOM   1153  O   ASN A 455      14.179 -24.801  14.978  1.00 21.19           O
ANISOU 1153  O   ASN A 455     2384   3019   2648    617    209   -130       O
ATOM   1154  CB  ASN A 455      14.353 -22.254  16.823  1.00 17.28           C
ANISOU 1154  CB  ASN A 455     1897   2419   2252    517     91    100       C
ATOM   1155  CG  ASN A 455      15.635 -23.116  17.008  1.00 19.77           C
ANISOU 1155  CG  ASN A 455     2152   2757   2604    577    115     64       C
ATOM   1156  OD1 ASN A 455      16.618 -22.923  16.293  1.00 22.33           O
ANISOU 1156  OD1 ASN A 455     2385   3192   2906    581    154     88       O
ATOM   1157  ND2 ASN A 455      15.632 -24.014  17.996  1.00 17.58           N
ANISOU 1157  ND2 ASN A 455     1917   2380   2382    630     94     23       N
ATOM   1158  N   SER A 456      12.143 -24.477  15.965  1.00 22.66           N
ANISOU 1158  N   SER A 456     2686   3069   2855    554    134   -114       N
ATOM   1159  CA  SER A 456      12.014 -25.921  16.202  1.00 22.92           C
ANISOU 1159  CA  SER A 456     2765   3019   2925    591    159   -223       C
ATOM   1160  C   SER A 456      12.012 -26.718  14.923  1.00 28.11           C
ANISOU 1160  C   SER A 456     3407   3761   3514    601    216   -337       C
ATOM   1161  O   SER A 456      12.535 -27.840  14.932  1.00 25.84           O
ANISOU 1161  O   SER A 456     3138   3413   3269    658    258   -425       O
ATOM   1162  CB  SER A 456      10.781 -26.307  17.028  1.00 23.37           C
ANISOU 1162  CB  SER A 456     2898   2965   3016    561    129   -242       C
ATOM   1163  OG  SER A 456      10.947 -25.696  18.288  1.00 31.62           O
ANISOU 1163  OG  SER A 456     3961   3935   4117    566     85   -154       O
ATOM   1164  N   GLY A 457      11.450 -26.177  13.825  1.00 20.68           N
ANISOU 1164  N   GLY A 457     2434   2961   2464    555    219   -338       N
ATOM   1165  CA  GLY A 457      11.418 -26.941  12.600  1.00 23.42           C
ANISOU 1165  CA  GLY A 457     2768   3410   2723    557    270   -464       C
ATOM   1166  C   GLY A 457      12.532 -26.648  11.612  1.00 31.01           C
ANISOU 1166  C   GLY A 457     3649   4523   3609    593    325   -453       C
ATOM   1167  O   GLY A 457      12.567 -27.270  10.553  1.00 26.80           O
ANISOU 1167  O   GLY A 457     3104   4094   2984    601    375   -570       O
ATOM   1168  N   VAL A 458      13.462 -25.746  11.939  1.00 29.65           N
ANISOU 1168  N   VAL A 458     3421   4374   3471    608    320   -324       N
ATOM   1169  CA  VAL A 458      14.368 -25.218  10.920  1.00 25.04           C
ANISOU 1169  CA  VAL A 458     2746   3967   2801    617    372   -279       C
ATOM   1170  C   VAL A 458      15.440 -26.216  10.503  1.00 32.48           C
ANISOU 1170  C   VAL A 458     3650   4949   3743    699    453   -387       C
ATOM   1171  O   VAL A 458      16.043 -26.045   9.431  1.00 37.89           O
ANISOU 1171  O   VAL A 458     4261   5812   4325    710    516   -391       O
ATOM   1172  CB  VAL A 458      14.998 -23.898  11.422  1.00 22.31           C
ANISOU 1172  CB  VAL A 458     2350   3623   2505    585    343   -105       C
ATOM   1173  CG1 VAL A 458      16.107 -24.166  12.497  1.00 33.98           C
ANISOU 1173  CG1 VAL A 458     3801   5001   4107    631    338    -90       C
ATOM   1174  CG2 VAL A 458      15.442 -22.989  10.180  1.00 30.86           C
ANISOU 1174  CG2 VAL A 458     3348   4908   3469    551    387    -10       C
ATOM   1175  N   TYR A 459      15.676 -27.279  11.286  1.00 28.87           N
ANISOU 1175  N   TYR A 459     3239   4336   3394    765    461   -472       N
ATOM   1176  CA  TYR A 459      16.634 -28.330  10.907  1.00 36.73           C
ANISOU 1176  CA  TYR A 459     4206   5346   4405    868    545   -585       C
ATOM   1177  C   TYR A 459      16.019 -29.589  10.309  1.00 36.03           C
ANISOU 1177  C   TYR A 459     4198   5208   4283    890    592   -783       C
ATOM   1178  O   TYR A 459      16.758 -30.541  10.022  1.00 41.02           O
ANISOU 1178  O   TYR A 459     4835   5801   4951    964    661   -872       O
ATOM   1179  CB  TYR A 459      17.511 -28.707  12.101  1.00 33.29           C
ANISOU 1179  CB  TYR A 459     3756   4778   4115    951    533   -538       C
ATOM   1180  CG  TYR A 459      18.314 -27.495  12.466  1.00 38.80           C
ANISOU 1180  CG  TYR A 459     4353   5564   4826    919    499   -374       C
ATOM   1181  CD1 TYR A 459      19.035 -26.818  11.472  1.00 43.54           C
ANISOU 1181  CD1 TYR A 459     4844   6364   5335    902    551   -327       C
ATOM   1182  CD2 TYR A 459      18.281 -26.964  13.738  1.00 42.83           C
ANISOU 1182  CD2 TYR A 459     4880   5968   5425    888    416   -268       C
ATOM   1183  CE1 TYR A 459      19.739 -25.696  11.753  1.00 46.83           C
ANISOU 1183  CE1 TYR A 459     5171   6853   5771    849    524   -180       C
ATOM   1184  CE2 TYR A 459      18.997 -25.831  14.028  1.00 51.50           C
ANISOU 1184  CE2 TYR A 459     5891   7142   6534    837    383   -138       C
ATOM   1185  CZ  TYR A 459      19.715 -25.188  13.030  1.00 47.07           C
ANISOU 1185  CZ  TYR A 459     5223   6761   5901    811    437    -91       C
ATOM   1186  OH  TYR A 459      20.434 -24.047  13.309  1.00 64.82           O
ANISOU 1186  OH  TYR A 459     7385   9072   8172    739    408     40       O
ATOM   1187  N   THR A 460      14.711 -29.613  10.079  1.00 38.22           N
ANISOU 1187  N   THR A 460     4544   5472   4506    799    550   -834       N
ATOM   1188  CA  THR A 460      14.051 -30.753   9.446  1.00 37.64           C
ANISOU 1188  CA  THR A 460     4545   5363   4393    786    587  -1035       C
ATOM   1189  C   THR A 460      13.398 -30.399   8.110  1.00 46.21           C
ANISOU 1189  C   THR A 460     5606   6662   5292    703    587  -1089       C
ATOM   1190  O   THR A 460      12.461 -31.081   7.676  1.00 47.22           O
ANISOU 1190  O   THR A 460     5799   6762   5379    631    572  -1216       O
ATOM   1191  CB  THR A 460      13.047 -31.384  10.419  1.00 41.76           C
ANISOU 1191  CB  THR A 460     5173   5667   5028    740    536  -1067       C
ATOM   1192  OG1 THR A 460      12.244 -30.354  11.022  1.00 38.05           O
ANISOU 1192  OG1 THR A 460     4693   5208   4555    660    448   -919       O
ATOM   1193  N   PHE A 461      13.902 -29.370   7.428  1.00 44.06           N
ANISOU 1193  N   PHE A 461     5236   6602   4904    705    600   -982       N
ATOM   1194  CA  PHE A 461      13.517 -29.104   6.045  1.00 45.86           C
ANISOU 1194  CA  PHE A 461     5435   7043   4948    640    604  -1009       C
ATOM   1195  C   PHE A 461      14.273 -30.087   5.118  1.00 42.18           C
ANISOU 1195  C   PHE A 461     4984   6593   4451    676    682  -1142       C
ATOM   1196  O   PHE A 461      13.689 -30.992   4.533  1.00 53.35           O
ANISOU 1196  O   PHE A 461     6466   7981   5826    636    686  -1299       O
ATOM   1197  CB  PHE A 461      13.846 -27.651   5.651  1.00 39.69           C
ANISOU 1197  CB  PHE A 461     4552   6463   4064    627    598   -814       C
ATOM   1198  CG  PHE A 461      12.957 -26.596   6.284  1.00 40.12           C
ANISOU 1198  CG  PHE A 461     4613   6483   4149    565    506   -649       C
ATOM   1199  CD1 PHE A 461      11.588 -26.579   6.073  1.00 47.05           C
ANISOU 1199  CD1 PHE A 461     5525   7392   4959    496    441   -679       C
ATOM   1200  CD2 PHE A 461      13.515 -25.611   7.089  1.00 42.37           C
ANISOU 1200  CD2 PHE A 461     4867   6693   4539    572    482   -462       C
ATOM   1201  CE1 PHE A 461      10.786 -25.582   6.656  1.00 42.86           C
ANISOU 1201  CE1 PHE A 461     4997   6817   4470    454    360   -516       C
ATOM   1202  CE2 PHE A 461      12.729 -24.605   7.679  1.00 38.27           C
ANISOU 1202  CE2 PHE A 461     4366   6113   4063    521    402   -314       C
ATOM   1203  CZ  PHE A 461      11.363 -24.585   7.457  1.00 32.49           C
ANISOU 1203  CZ  PHE A 461     3667   5410   3266    473    345   -337       C
ATOM   1204  N   THR A 465      16.621 -26.780  -1.940  1.00 44.21           N
ANISOU 1204  N   THR A 465     4817   8187   3795    585    851   -772       N
ATOM   1205  CA  THR A 465      16.504 -25.946  -3.130  1.00 47.07           C
ANISOU 1205  CA  THR A 465     5114   8792   3980    542    840   -651       C
ATOM   1206  C   THR A 465      17.061 -24.558  -2.913  1.00 45.03           C
ANISOU 1206  C   THR A 465     4777   8587   3746    527    840   -386       C
ATOM   1207  O   THR A 465      17.336 -24.157  -1.792  1.00 36.95           O
ANISOU 1207  O   THR A 465     3753   7417   2870    536    831   -295       O
ATOM   1208  CB  THR A 465      15.047 -25.813  -3.577  1.00 45.10           C
ANISOU 1208  CB  THR A 465     4889   8622   3624    475    745   -664       C
ATOM   1209  OG1 THR A 465      14.295 -25.127  -2.563  1.00 44.05           O
ANISOU 1209  OG1 THR A 465     4773   8375   3588    449    667   -538       O
ATOM   1210  CG2 THR A 465      14.438 -27.176  -3.863  1.00 44.97           C
ANISOU 1210  CG2 THR A 465     4950   8557   3581    464    741   -930       C
ATOM   1211  N   LEU A 466      17.215 -23.800  -3.993  1.00 41.50           N
ANISOU 1211  N   LEU A 466     4265   8346   3156    500    850   -256       N
ATOM   1212  CA  LEU A 466      17.725 -22.453  -3.801  1.00 38.92           C
ANISOU 1212  CA  LEU A 466     3874   8045   2867    472    853      5       C
ATOM   1213  C   LEU A 466      16.700 -21.607  -3.025  1.00 39.94           C
ANISOU 1213  C   LEU A 466     4038   8069   3069    434    760    149       C
ATOM   1214  O   LEU A 466      17.074 -20.818  -2.149  1.00 32.65           O
ANISOU 1214  O   LEU A 466     3103   7030   2274    420    759    302       O
ATOM   1215  CB  LEU A 466      18.081 -21.888  -5.165  1.00 43.58           C
ANISOU 1215  CB  LEU A 466     4394   8872   3291    453    888    112       C
ATOM   1216  CG  LEU A 466      18.821 -20.603  -5.356  1.00 47.84           C
ANISOU 1216  CG  LEU A 466     4860   9475   3841    419    918    369       C
ATOM   1217  CD1 LEU A 466      20.195 -20.848  -4.745  1.00 44.15           C
ANISOU 1217  CD1 LEU A 466     4350   8930   3494    444   1001    345       C
ATOM   1218  CD2 LEU A 466      18.960 -20.479  -6.851  1.00 45.68           C
ANISOU 1218  CD2 LEU A 466     4534   9454   3370    413    953    396       C
ATOM   1219  N   LYS A 467      15.398 -21.812  -3.279  1.00 36.10           N
ANISOU 1219  N   LYS A 467     3592   7612   2511    416    683     90       N
ATOM   1220  CA  LYS A 467      14.368 -21.189  -2.452  1.00 39.45           C
ANISOU 1220  CA  LYS A 467     4052   7922   3014    395    600    195       C
ATOM   1221  C   LYS A 467      14.470 -21.626  -0.993  1.00 35.74           C
ANISOU 1221  C   LYS A 467     3637   7226   2715    416    600    119       C
ATOM   1222  O   LYS A 467      14.261 -20.817  -0.077  1.00 31.26           O
ANISOU 1222  O   LYS A 467     3084   6539   2255    406    569    265       O
ATOM   1223  CB  LYS A 467      12.973 -21.516  -3.011  1.00 43.97           C
ANISOU 1223  CB  LYS A 467     4643   8584   3479    374    520    116       C
ATOM   1224  CG  LYS A 467      11.818 -20.978  -2.130  1.00 46.11           C
ANISOU 1224  CG  LYS A 467     4948   8739   3834    362    435    207       C
ATOM   1225  CD  LYS A 467      10.553 -20.644  -2.928  1.00 52.52           C
ANISOU 1225  CD  LYS A 467     5726   9697   4530    342    357    259       C
ATOM   1226  CE  LYS A 467       9.856 -21.913  -3.370  1.00 47.85           C
ANISOU 1226  CE  LYS A 467     5152   9177   3854    314    329      8       C
ATOM   1227  NZ  LYS A 467       8.421 -21.774  -3.808  1.00 47.53           N
ANISOU 1227  NZ  LYS A 467     5077   9248   3736    284    239     24       N
ATOM   1228  N   SER A 468      14.762 -22.902  -0.741  1.00 34.30           N
ANISOU 1228  N   SER A 468     3492   6971   2569    448    636   -108       N
ATOM   1229  CA  SER A 468      14.815 -23.354   0.651  1.00 36.81           C
ANISOU 1229  CA  SER A 468     3860   7072   3053    476    633   -178       C
ATOM   1230  C   SER A 468      15.998 -22.719   1.366  1.00 30.39           C
ANISOU 1230  C   SER A 468     2998   6190   2360    494    683    -41       C
ATOM   1231  O   SER A 468      15.915 -22.366   2.562  1.00 32.08           O
ANISOU 1231  O   SER A 468     3228   6255   2704    497    659     25       O
ATOM   1232  CB  SER A 468      14.921 -24.878   0.705  1.00 43.30           C
ANISOU 1232  CB  SER A 468     4737   7809   3906    513    666   -440       C
ATOM   1233  OG  SER A 468      13.669 -25.466   0.423  1.00 57.90           O
ANISOU 1233  OG  SER A 468     6642   9666   5693    473    606   -569       O
ATOM   1234  N   LEU A 469      17.093 -22.520   0.617  1.00 33.51           N
ANISOU 1234  N   LEU A 469     3323   6704   2706    500    749      8       N
ATOM   1235  CA  LEU A 469      18.269 -21.848   1.160  1.00 33.86           C
ANISOU 1235  CA  LEU A 469     3299   6710   2856    496    793    148       C
ATOM   1236  C   LEU A 469      17.936 -20.409   1.535  1.00 35.00           C
ANISOU 1236  C   LEU A 469     3434   6825   3041    430    749    389       C
ATOM   1237  O   LEU A 469      18.332 -19.935   2.615  1.00 32.54           O
ANISOU 1237  O   LEU A 469     3108   6382   2872    414    746    475       O
ATOM   1238  CB  LEU A 469      19.393 -21.894   0.142  1.00 31.82           C
ANISOU 1238  CB  LEU A 469     2962   6609   2517    505    872    157       C
ATOM   1239  CG  LEU A 469      20.276 -23.129   0.231  1.00 50.44           C
ANISOU 1239  CG  LEU A 469     5309   8934   4922    585    940    -33       C
ATOM   1240  CD1 LEU A 469      21.280 -23.153  -0.921  1.00 40.10           C
ANISOU 1240  CD1 LEU A 469     3921   7809   3507    597   1024    -25       C
ATOM   1241  CD2 LEU A 469      20.945 -23.198   1.606  1.00 38.03           C
ANISOU 1241  CD2 LEU A 469     3715   7194   3542    614    941    -15       C
ATOM   1242  N   GLU A 470      17.199 -19.714   0.648  1.00 30.25           N
ANISOU 1242  N   GLU A 470     2839   6334   2321    394    714    500       N
ATOM   1243  CA  GLU A 470      16.712 -18.359   0.903  1.00 28.50           C
ANISOU 1243  CA  GLU A 470     2627   6058   2143    344    669    731       C
ATOM   1244  C   GLU A 470      15.840 -18.320   2.130  1.00 31.29           C
ANISOU 1244  C   GLU A 470     3049   6234   2604    351    611    723       C
ATOM   1245  O   GLU A 470      15.965 -17.403   2.950  1.00 31.08           O
ANISOU 1245  O   GLU A 470     3033   6076   2701    316    600    876       O
ATOM   1246  CB  GLU A 470      15.935 -17.841  -0.314  1.00 31.66           C
ANISOU 1246  CB  GLU A 470     3022   6609   2398    331    633    821       C
ATOM   1247  CG  GLU A 470      16.850 -17.549  -1.524  1.00 34.48           C
ANISOU 1247  CG  GLU A 470     3305   7146   2651    314    696    892       C
ATOM   1248  CD  GLU A 470      16.132 -17.327  -2.862  1.00 42.20           C
ANISOU 1248  CD  GLU A 470     4264   8314   3455    316    669    937       C
ATOM   1249  OE1 GLU A 470      14.888 -17.518  -2.950  1.00 39.48           O
ANISOU 1249  OE1 GLU A 470     3957   7982   3063    332    596    890       O
ATOM   1250  OE2 GLU A 470      16.828 -17.002  -3.866  1.00 41.73           O
ANISOU 1250  OE2 GLU A 470     4144   8411   3303    302    721   1015       O
ATOM   1251  N   GLU A 471      14.924 -19.300   2.257  1.00 27.11           N
ANISOU 1251  N   GLU A 471     2572   5696   2032    388    573    543       N
ATOM   1252  CA  GLU A 471      14.012 -19.352   3.395  1.00 30.48           C
ANISOU 1252  CA  GLU A 471     3065   5970   2545    399    520    523       C
ATOM   1253  C   GLU A 471      14.792 -19.489   4.701  1.00 26.47           C
ANISOU 1253  C   GLU A 471     2576   5232   2250    402    517    489       C
ATOM   1254  O   GLU A 471      14.537 -18.766   5.672  1.00 24.58           O
ANISOU 1254  O   GLU A 471     2382   4801   2155    377    459    584       O
ATOM   1255  CB  GLU A 471      13.024 -20.528   3.246  1.00 23.76           C
ANISOU 1255  CB  GLU A 471     2261   5141   1625    422    480    306       C
ATOM   1256  CG  GLU A 471      12.086 -20.451   2.074  1.00 33.47           C
ANISOU 1256  CG  GLU A 471     3481   6531   2706    402    429    309       C
ATOM   1257  CD  GLU A 471      10.833 -19.777   2.433  1.00 36.12           C
ANISOU 1257  CD  GLU A 471     3843   6826   3055    395    348    419       C
ATOM   1258  OE1 GLU A 471       9.847 -20.419   2.903  1.00 29.94           O
ANISOU 1258  OE1 GLU A 471     3100   5996   2278    394    297    296       O
ATOM   1259  OE2 GLU A 471      10.883 -18.543   2.285  1.00 40.65           O
ANISOU 1259  OE2 GLU A 471     4397   7396   3652    389    339    640       O
ATOM   1260  N   LYS A 472      15.750 -20.428   4.748  1.00 28.01           N
ANISOU 1260  N   LYS A 472     2733   5446   2462    439    578    349       N
ATOM   1261  CA  LYS A 472      16.492 -20.668   5.986  1.00 28.93           C
ANISOU 1261  CA  LYS A 472     2856   5368   2767    454    566    314       C
ATOM   1262  C   LYS A 472      17.307 -19.443   6.398  1.00 27.93           C
ANISOU 1262  C   LYS A 472     2679   5196   2736    392    567    507       C
ATOM   1263  O   LYS A 472      17.406 -19.125   7.589  1.00 23.21           O
ANISOU 1263  O   LYS A 472     2118   4406   2296    371    511    534       O
ATOM   1264  CB  LYS A 472      17.417 -21.850   5.809  1.00 34.06           C
ANISOU 1264  CB  LYS A 472     3459   6076   3407    525    641    152       C
ATOM   1265  CG  LYS A 472      16.792 -23.229   5.896  1.00 38.10           C
ANISOU 1265  CG  LYS A 472     4045   6523   3909    584    634    -70       C
ATOM   1266  CD  LYS A 472      18.008 -24.162   5.729  1.00 55.05           C
ANISOU 1266  CD  LYS A 472     6132   8713   6073    667    724   -187       C
ATOM   1267  CE  LYS A 472      17.690 -25.513   5.111  1.00 44.63           C
ANISOU 1267  CE  LYS A 472     4882   7375   4701    708    746   -405       C
ATOM   1268  NZ  LYS A 472      18.968 -26.128   4.620  1.00 57.18           N
ANISOU 1268  NZ  LYS A 472     6418   9006   6300    768    825   -466       N
ATOM   1269  N  AASP A 473      17.884 -18.738   5.426  0.97 24.23           N
ANISOU 1269  N  AASP A 473     2130   4906   2169    354    632    641       N
ATOM   1270  CA AASP A 473      18.625 -17.524   5.744  0.97 27.97           C
ANISOU 1270  CA AASP A 473     2559   5329   2739    271    638    831       C
ATOM   1271  C  AASP A 473      17.720 -16.487   6.378  0.97 27.72           C
ANISOU 1271  C  AASP A 473     2621   5110   2799    222    556    950       C
ATOM   1272  O  AASP A 473      18.076 -15.862   7.384  0.97 26.55           O
ANISOU 1272  O  AASP A 473     2492   4787   2808    169    517   1003       O
ATOM   1273  CB AASP A 473      19.250 -16.948   4.489  0.97 31.81           C
ANISOU 1273  CB AASP A 473     2958   6031   3099    231    719    964       C
ATOM   1274  CG AASP A 473      20.043 -15.703   4.778  0.97 41.34           C
ANISOU 1274  CG AASP A 473     4120   7171   4416    125    728   1158       C
ATOM   1275  OD1AASP A 473      21.219 -15.836   5.190  0.97 41.56           O
ANISOU 1275  OD1AASP A 473     4062   7202   4527     99    758   1137       O
ATOM   1276  OD2AASP A 473      19.481 -14.597   4.586  0.97 45.57           O
ANISOU 1276  OD2AASP A 473     4710   7642   4964     69    699   1325       O
ATOM   1277  N   HIS A 474      16.539 -16.295   5.786  1.00 26.94           N
ANISOU 1277  N   HIS A 474     2578   5058   2599    245    529    987       N
ATOM   1278  CA  HIS A 474      15.583 -15.344   6.314  1.00 23.93           C
ANISOU 1278  CA  HIS A 474     2283   4511   2299    226    459   1098       C
ATOM   1279  C   HIS A 474      15.199 -15.706   7.740  1.00 21.50           C
ANISOU 1279  C   HIS A 474     2052   3974   2144    244    387    976       C
ATOM   1280  O   HIS A 474      15.191 -14.851   8.623  1.00 22.44           O
ANISOU 1280  O   HIS A 474     2219   3906   2399    203    350   1050       O
ATOM   1281  CB  HIS A 474      14.357 -15.305   5.411  1.00 29.12           C
ANISOU 1281  CB  HIS A 474     2964   5297   2805    269    439   1136       C
ATOM   1282  CG  HIS A 474      13.298 -14.339   5.860  1.00 29.75           C
ANISOU 1282  CG  HIS A 474     3120   5224   2960    276    375   1259       C
ATOM   1283  ND1 HIS A 474      13.480 -12.970   5.806  1.00 32.91           N
ANISOU 1283  ND1 HIS A 474     3535   5541   3429    234    388   1477       N
ATOM   1284  CD2 HIS A 474      12.062 -14.537   6.388  1.00 32.85           C
ANISOU 1284  CD2 HIS A 474     3575   5526   3379    325    305   1194       C
ATOM   1285  CE1 HIS A 474      12.387 -12.369   6.242  1.00 26.57           C
ANISOU 1285  CE1 HIS A 474     2805   4602   2688    273    331   1538       C
ATOM   1286  NE2 HIS A 474      11.517 -13.294   6.618  1.00 30.03           N
ANISOU 1286  NE2 HIS A 474     3267   5045   3100    328    280   1370       N
ATOM   1287  N   ILE A 475      14.872 -16.974   7.990  1.00 22.67           N
ANISOU 1287  N   ILE A 475     2217   4128   2267    301    371    786       N
ATOM   1288  CA  ILE A 475      14.514 -17.405   9.353  1.00 17.98           C
ANISOU 1288  CA  ILE A 475     1695   3332   1805    320    310    680       C
ATOM   1289  C   ILE A 475      15.619 -17.046  10.351  1.00 25.98           C
ANISOU 1289  C   ILE A 475     2689   4222   2959    278    304    703       C
ATOM   1290  O   ILE A 475      15.355 -16.536  11.461  1.00 22.49           O
ANISOU 1290  O   ILE A 475     2311   3601   2634    255    248    719       O
ATOM   1291  CB  ILE A 475      14.217 -18.909   9.366  1.00 21.28           C
ANISOU 1291  CB  ILE A 475     2126   3781   2180    379    312    483       C
ATOM   1292  CG1 ILE A 475      12.914 -19.192   8.592  1.00 22.43           C
ANISOU 1292  CG1 ILE A 475     2298   4026   2200    397    293    447       C
ATOM   1293  CG2 ILE A 475      14.036 -19.389  10.868  1.00 22.24           C
ANISOU 1293  CG2 ILE A 475     2314   3693   2443    396    257    395       C
ATOM   1294  CD1 ILE A 475      12.650 -20.702   8.306  1.00 24.55           C
ANISOU 1294  CD1 ILE A 475     2576   4349   2404    433    309    240       C
ATOM   1295  N   HIS A 476      16.873 -17.304   9.970  1.00 22.12           N
ANISOU 1295  N   HIS A 476     2105   3845   2454    266    361    701       N
ATOM   1296  CA  HIS A 476      17.986 -17.036  10.887  1.00 27.45           C
ANISOU 1296  CA  HIS A 476     2738   4440   3254    220    349    718       C
ATOM   1297  C   HIS A 476      18.182 -15.542  11.105  1.00 24.66           C
ANISOU 1297  C   HIS A 476     2393   4000   2975    115    333    878       C
ATOM   1298  O   HIS A 476      18.540 -15.116  12.214  1.00 21.52           O
ANISOU 1298  O   HIS A 476     2017   3461   2700     64    283    875       O
ATOM   1299  CB  HIS A 476      19.279 -17.686  10.364  1.00 26.14           C
ANISOU 1299  CB  HIS A 476     2444   4439   3048    242    420    682       C
ATOM   1300  CG  HIS A 476      19.282 -19.174  10.545  1.00 29.61           C
ANISOU 1300  CG  HIS A 476     2888   4892   3472    349    430    508       C
ATOM   1301  ND1 HIS A 476      19.012 -19.769  11.764  1.00 34.11           N
ANISOU 1301  ND1 HIS A 476     3523   5300   4137    389    366    419       N
ATOM   1302  CD2 HIS A 476      19.475 -20.184   9.664  1.00 32.52           C
ANISOU 1302  CD2 HIS A 476     3215   5401   3739    427    500    406       C
ATOM   1303  CE1 HIS A 476      19.061 -21.084  11.625  1.00 33.26           C
ANISOU 1303  CE1 HIS A 476     3416   5219   4003    485    397    283       C
ATOM   1304  NE2 HIS A 476      19.321 -21.359  10.361  1.00 32.09           N
ANISOU 1304  NE2 HIS A 476     3209   5245   3740    510    479    261       N
ATOM   1305  N   ARG A 477      17.962 -14.738  10.051  1.00 22.39           N
ANISOU 1305  N   ARG A 477     2094   3796   2616     81    376   1019       N
ATOM   1306  CA  ARG A 477      17.998 -13.297  10.224  1.00 25.14           C
ANISOU 1306  CA  ARG A 477     2477   4025   3051    -14    366   1179       C
ATOM   1307  C   ARG A 477      16.929 -12.847  11.201  1.00 23.96           C
ANISOU 1307  C   ARG A 477     2456   3656   2991      4    292   1157       C
ATOM   1308  O   ARG A 477      17.193 -11.981  12.049  1.00 22.51           O
ANISOU 1308  O   ARG A 477     2316   3303   2936    -72    261   1193       O
ATOM   1309  CB  ARG A 477      17.836 -12.601   8.860  1.00 28.23           C
ANISOU 1309  CB  ARG A 477     2841   4549   3337    -34    429   1353       C
ATOM   1310  CG  ARG A 477      19.047 -12.706   7.957  1.00 33.47           C
ANISOU 1310  CG  ARG A 477     3371   5422   3925    -81    516   1414       C
ATOM   1311  CD  ARG A 477      18.920 -11.721   6.756  1.00 41.29           C
ANISOU 1311  CD  ARG A 477     4346   6514   4830   -125    576   1635       C
ATOM   1312  NE  ARG A 477      20.119 -11.639   5.915  1.00 54.91           N
ANISOU 1312  NE  ARG A 477     5949   8418   6496   -183    656   1698       N
ATOM   1313  N   VAL A 478      15.712 -13.435  11.115  1.00 20.67           N
ANISOU 1313  N   VAL A 478     2099   3246   2508     98    265   1087       N
ATOM   1314  CA  VAL A 478      14.650 -13.050  12.037  1.00 25.18           C
ANISOU 1314  CA  VAL A 478     2779   3631   3157    127    205   1063       C
ATOM   1315  C   VAL A 478      14.981 -13.538  13.440  1.00 23.88           C
ANISOU 1315  C   VAL A 478     2643   3343   3088    119    156    927       C
ATOM   1316  O   VAL A 478      14.832 -12.788  14.408  1.00 21.96           O
ANISOU 1316  O   VAL A 478     2470   2926   2949     84    119    933       O
ATOM   1317  CB  VAL A 478      13.259 -13.538  11.560  1.00 23.64           C
ANISOU 1317  CB  VAL A 478     2617   3501   2864    219    189   1033       C
ATOM   1318  CG1 VAL A 478      12.198 -13.172  12.611  1.00 23.40           C
ANISOU 1318  CG1 VAL A 478     2683   3287   2919    255    135   1004       C
ATOM   1319  CG2 VAL A 478      12.887 -12.887  10.218  1.00 25.23           C
ANISOU 1319  CG2 VAL A 478     2790   3834   2961    228    225   1195       C
ATOM   1320  N   LEU A 479      15.524 -14.765  13.568  1.00 20.64           N
ANISOU 1320  N   LEU A 479     2177   3021   2643    152    160    807       N
ATOM   1321  CA  LEU A 479      15.974 -15.234  14.880  1.00 17.83           C
ANISOU 1321  CA  LEU A 479     1835   2570   2368    149    114    704       C
ATOM   1322  C   LEU A 479      17.020 -14.280  15.481  1.00 25.74           C
ANISOU 1322  C   LEU A 479     2810   3502   3467     43     97    760       C
ATOM   1323  O   LEU A 479      16.938 -13.936  16.675  1.00 19.78           O
ANISOU 1323  O   LEU A 479     2117   2609   2791     15     41    716       O
ATOM   1324  CB  LEU A 479      16.500 -16.689  14.750  1.00 21.69           C
ANISOU 1324  CB  LEU A 479     2260   3170   2809    214    133    593       C
ATOM   1325  CG  LEU A 479      15.358 -17.762  14.732  1.00 17.33           C
ANISOU 1325  CG  LEU A 479     1770   2611   2203    300    125    489       C
ATOM   1326  CD1 LEU A 479      15.888 -19.079  14.224  1.00 23.17           C
ANISOU 1326  CD1 LEU A 479     2452   3461   2891    361    168    393       C
ATOM   1327  CD2 LEU A 479      14.724 -18.015  16.131  1.00 19.57           C
ANISOU 1327  CD2 LEU A 479     2140   2741   2556    320     65    422       C
ATOM   1328  N   ASP A 480      17.969 -13.797  14.661  1.00 18.33           N
ANISOU 1328  N   ASP A 480     1781   2665   2520    -26    146    856       N
ATOM   1329  CA  ASP A 480      18.978 -12.853  15.128  1.00 18.38           C
ANISOU 1329  CA  ASP A 480     1748   2614   2620   -153    133    915       C
ATOM   1330  C   ASP A 480      18.344 -11.563  15.661  1.00 22.67           C
ANISOU 1330  C   ASP A 480     2409   2951   3252   -217    103    968       C
ATOM   1331  O   ASP A 480      18.768 -11.043  16.700  1.00 24.95           O
ANISOU 1331  O   ASP A 480     2724   3122   3633   -299     54    927       O
ATOM   1332  CB  ASP A 480      19.942 -12.532  13.997  1.00 25.07           C
ANISOU 1332  CB  ASP A 480     2476   3616   3433   -219    207   1030       C
ATOM   1333  CG  ASP A 480      20.953 -13.650  13.746  1.00 29.15           C
ANISOU 1333  CG  ASP A 480     2855   4324   3897   -175    238    964       C
ATOM   1334  OD1 ASP A 480      21.072 -14.587  14.568  1.00 27.23           O
ANISOU 1334  OD1 ASP A 480     2607   4072   3668   -106    194    841       O
ATOM   1335  OD2 ASP A 480      21.608 -13.610  12.709  1.00 25.17           O
ANISOU 1335  OD2 ASP A 480     2247   3982   3334   -197    313   1041       O
ATOM   1336  N   LYS A 481      17.335 -11.023  14.952  1.00 23.25           N
ANISOU 1336  N   LYS A 481     2554   2983   3298   -176    132   1058       N
ATOM   1337  CA  LYS A 481      16.627  -9.840  15.442  1.00 26.43           C
ANISOU 1337  CA  LYS A 481     3078   3173   3792   -204    112   1107       C
ATOM   1338  C   LYS A 481      15.974 -10.098  16.801  1.00 24.70           C
ANISOU 1338  C   LYS A 481     2950   2822   3615   -156     48    964       C
ATOM   1339  O   LYS A 481      15.928  -9.194  17.647  1.00 21.78           O
ANISOU 1339  O   LYS A 481     2662   2271   3342   -216     21    946       O
ATOM   1340  CB  LYS A 481      15.571  -9.357  14.427  1.00 22.52           C
ANISOU 1340  CB  LYS A 481     2629   2681   3247   -133    151   1237       C
ATOM   1341  CG  LYS A 481      16.119  -8.864  13.097  1.00 32.65           C
ANISOU 1341  CG  LYS A 481     3839   4081   4484   -185    219   1411       C
ATOM   1342  N   ILE A 482      15.415 -11.299  17.022  1.00 20.37           N
ANISOU 1342  N   ILE A 482     2396   2353   2991    -52     28    861       N
ATOM   1343  CA  ILE A 482      14.758 -11.546  18.312  1.00 17.83           C
ANISOU 1343  CA  ILE A 482     2158   1919   2697     -8    -24    742       C
ATOM   1344  C   ILE A 482      15.796 -11.646  19.423  1.00 21.96           C
ANISOU 1344  C   ILE A 482     2657   2416   3269    -86    -73    657       C
ATOM   1345  O   ILE A 482      15.571 -11.161  20.548  1.00 24.49           O
ANISOU 1345  O   ILE A 482     3060   2605   3641   -111   -115    590       O
ATOM   1346  CB  ILE A 482      13.858 -12.796  18.232  1.00 16.39           C
ANISOU 1346  CB  ILE A 482     1976   1822   2429    108    -27    670       C
ATOM   1347  CG1 ILE A 482      12.759 -12.558  17.197  1.00 20.55           C
ANISOU 1347  CG1 ILE A 482     2520   2386   2903    172      7    753       C
ATOM   1348  CG2 ILE A 482      13.201 -13.049  19.629  1.00 18.07           C
ANISOU 1348  CG2 ILE A 482     2271   1928   2666    146    -73    561       C
ATOM   1349  CD1 ILE A 482      11.902 -13.768  16.908  1.00 21.69           C
ANISOU 1349  CD1 ILE A 482     2649   2635   2958    259      7    684       C
ATOM   1350  N   THR A 483      16.973 -12.233  19.116  1.00 20.92           N
ANISOU 1350  N   THR A 483     2407   2424   3116   -123    -68    659       N
ATOM   1351  CA  THR A 483      18.093 -12.178  20.055  1.00 20.98           C
ANISOU 1351  CA  THR A 483     2365   2437   3169   -210   -120    604       C
ATOM   1352  C   THR A 483      18.441 -10.729  20.419  1.00 21.60           C
ANISOU 1352  C   THR A 483     2489   2376   3343   -352   -135    636       C
ATOM   1353  O   THR A 483      18.538 -10.389  21.613  1.00 21.89           O
ANISOU 1353  O   THR A 483     2579   2320   3419   -404   -196    547       O
ATOM   1354  CB  THR A 483      19.308 -12.922  19.487  1.00 21.64           C
ANISOU 1354  CB  THR A 483     2293   2707   3221   -219    -99    624       C
ATOM   1355  OG1 THR A 483      18.984 -14.303  19.211  1.00 20.38           O
ANISOU 1355  OG1 THR A 483     2109   2647   2986    -85    -81    574       O
ATOM   1356  CG2 THR A 483      20.493 -12.887  20.486  1.00 22.60           C
ANISOU 1356  CG2 THR A 483     2337   2865   3385   -306   -164    575       C
ATOM   1357  N   ASP A 484      18.614  -9.855  19.408  1.00 20.54           N
ANISOU 1357  N   ASP A 484     2340   2219   3244   -419    -79    761       N
ATOM   1358  CA  ASP A 484      18.907  -8.445  19.690  1.00 26.18           C
ANISOU 1358  CA  ASP A 484     3113   2767   4069   -562    -83    799       C
ATOM   1359  C   ASP A 484      17.852  -7.859  20.628  1.00 24.08           C
ANISOU 1359  C   ASP A 484     3010   2292   3848   -525   -112    720       C
ATOM   1360  O   ASP A 484      18.182  -7.099  21.548  1.00 26.42           O
ANISOU 1360  O   ASP A 484     3363   2456   4219   -632   -152    647       O
ATOM   1361  CB  ASP A 484      18.918  -7.592  18.401  1.00 25.44           C
ANISOU 1361  CB  ASP A 484     3012   2650   4005   -609     -5    974       C
ATOM   1362  CG  ASP A 484      19.988  -7.980  17.399  1.00 31.25           C
ANISOU 1362  CG  ASP A 484     3586   3594   4694   -660     41   1066       C
ATOM   1363  OD1 ASP A 484      20.899  -8.795  17.669  1.00 30.67           O
ANISOU 1363  OD1 ASP A 484     3391   3678   4585   -674     16    999       O
ATOM   1364  OD2 ASP A 484      19.893  -7.464  16.273  1.00 30.83           O
ANISOU 1364  OD2 ASP A 484     3522   3560   4630   -674    111   1218       O
ATOM   1365  N   THR A 485      16.572  -8.193  20.376  1.00 22.82           N
ANISOU 1365  N   THR A 485     2919   2112   3638   -375    -89    729       N
ATOM   1366  CA  THR A 485      15.443  -7.693  21.161  1.00 27.34           C
ANISOU 1366  CA  THR A 485     3634   2510   4245   -310   -100    664       C
ATOM   1367  C   THR A 485      15.497  -8.191  22.608  1.00 26.40           C
ANISOU 1367  C   THR A 485     3544   2386   4101   -308   -167    498       C
ATOM   1368  O   THR A 485      15.249  -7.422  23.547  1.00 23.06           O
ANISOU 1368  O   THR A 485     3224   1804   3731   -344   -187    414       O
ATOM   1369  CB  THR A 485      14.124  -8.136  20.484  1.00 26.02           C
ANISOU 1369  CB  THR A 485     3490   2384   4012   -150    -63    718       C
ATOM   1370  OG1 THR A 485      14.097  -7.649  19.138  1.00 28.56           O
ANISOU 1370  OG1 THR A 485     3781   2735   4336   -151     -7    883       O
ATOM   1371  CG2 THR A 485      12.864  -7.640  21.216  1.00 25.82           C
ANISOU 1371  CG2 THR A 485     3592   2202   4018    -60    -62    664       C
ATOM   1372  N   LEU A 486      15.764  -9.485  22.807  1.00 23.73           N
ANISOU 1372  N   LEU A 486     3124   2216   3677   -256   -196    448       N
ATOM   1373  CA  LEU A 486      15.911  -9.990  24.176  1.00 23.63           C
ANISOU 1373  CA  LEU A 486     3129   2219   3629   -255   -261    316       C
ATOM   1374  C   LEU A 486      16.993  -9.223  24.930  1.00 24.99           C
ANISOU 1374  C   LEU A 486     3292   2348   3856   -413   -315    257       C
ATOM   1375  O   LEU A 486      16.787  -8.816  26.079  1.00 25.36           O
ANISOU 1375  O   LEU A 486     3424   2305   3905   -441   -356    146       O
ATOM   1376  CB  LEU A 486      16.239 -11.486  24.168  1.00 25.84           C
ANISOU 1376  CB  LEU A 486     3312   2680   3825   -182   -280    300       C
ATOM   1377  CG  LEU A 486      15.021 -12.404  24.088  1.00 26.41           C
ANISOU 1377  CG  LEU A 486     3425   2774   3834    -38   -254    288       C
ATOM   1378  CD1 LEU A 486      15.568 -13.777  23.772  1.00 24.16           C
ANISOU 1378  CD1 LEU A 486     3040   2645   3496     14   -256    292       C
ATOM   1379  CD2 LEU A 486      14.171 -12.411  25.386  1.00 21.81           C
ANISOU 1379  CD2 LEU A 486     2946   2113   3228      6   -282    192       C
ATOM   1380  N   ILE A 487      18.159  -9.032  24.299  1.00 21.00           N
ANISOU 1380  N   ILE A 487     2675   1918   3386   -523   -313    325       N
ATOM   1381  CA  ILE A 487      19.282  -8.371  24.962  1.00 28.09           C
ANISOU 1381  CA  ILE A 487     3534   2804   4334   -695   -371    270       C
ATOM   1382  C   ILE A 487      18.917  -6.930  25.293  1.00 27.38           C
ANISOU 1382  C   ILE A 487     3584   2477   4342   -793   -360    234       C
ATOM   1383  O   ILE A 487      19.195  -6.439  26.388  1.00 28.79           O
ANISOU 1383  O   ILE A 487     3814   2589   4536   -888   -420    108       O
ATOM   1384  CB  ILE A 487      20.550  -8.440  24.085  1.00 24.66           C
ANISOU 1384  CB  ILE A 487     2936   2512   3924   -794   -355    369       C
ATOM   1385  CG1 ILE A 487      21.193  -9.834  24.103  1.00 28.83           C
ANISOU 1385  CG1 ILE A 487     3317   3272   4365   -712   -383    364       C
ATOM   1386  CG2 ILE A 487      21.558  -7.367  24.506  1.00 29.17           C
ANISOU 1386  CG2 ILE A 487     3480   3024   4581  -1011   -396    339       C
ATOM   1387  CD1 ILE A 487      21.667 -10.272  25.476  1.00 26.10           C
ANISOU 1387  CD1 ILE A 487     2944   2998   3974   -729   -482    248       C
ATOM   1388  N   HIS A 488      18.277  -6.241  24.351  1.00 28.15           N
ANISOU 1388  N   HIS A 488     3748   2444   4503   -764   -282    343       N
ATOM   1389  CA  HIS A 488      17.808  -4.876  24.590  1.00 30.67           C
ANISOU 1389  CA  HIS A 488     4218   2505   4933   -824   -256    322       C
ATOM   1390  C   HIS A 488      16.894  -4.813  25.809  1.00 29.49           C
ANISOU 1390  C   HIS A 488     4201   2251   4754   -743   -283    165       C
ATOM   1391  O   HIS A 488      17.034  -3.931  26.654  1.00 29.62           O
ANISOU 1391  O   HIS A 488     4313   2110   4831   -844   -307     49       O
ATOM   1392  CB  HIS A 488      17.094  -4.380  23.342  1.00 33.29           C
ANISOU 1392  CB  HIS A 488     4590   2745   5313   -749   -167    491       C
ATOM   1393  CG  HIS A 488      16.402  -3.068  23.512  1.00 35.57           C
ANISOU 1393  CG  HIS A 488     5044   2750   5720   -755   -126    491       C
ATOM   1394  ND1 HIS A 488      15.059  -2.973  23.807  1.00 46.53           N
ANISOU 1394  ND1 HIS A 488     6546   4056   7077   -582    -92    449       N
ATOM   1395  CD2 HIS A 488      16.839  -1.799  23.337  1.00 43.71           C
ANISOU 1395  CD2 HIS A 488     6141   3631   6837   -877    -79    515       C
ATOM   1396  CE1 HIS A 488      14.711  -1.700  23.860  1.00 40.52           C
ANISOU 1396  CE1 HIS A 488     5918   3118   6360   -587    -31    438       C
ATOM   1397  NE2 HIS A 488      15.771  -0.967  23.572  1.00 45.28           N
ANISOU 1397  NE2 HIS A 488     6505   3662   7039   -765    -21    477       N
ATOM   1398  N   LEU A 489      15.944  -5.748  25.913  1.00 29.39           N
ANISOU 1398  N   LEU A 489     4195   2326   4646   -566   -274    155       N
ATOM   1399  CA  LEU A 489      15.058  -5.779  27.076  1.00 32.20           C
ANISOU 1399  CA  LEU A 489     4661   2615   4957   -482   -291     15       C
ATOM   1400  C   LEU A 489      15.851  -5.890  28.363  1.00 34.08           C
ANISOU 1400  C   LEU A 489     4890   2911   5147   -590   -377   -141       C
ATOM   1401  O   LEU A 489      15.598  -5.165  29.333  1.00 35.76           O
ANISOU 1401  O   LEU A 489     5219   2993   5375   -627   -391   -277       O
ATOM   1402  CB  LEU A 489      14.078  -6.948  26.970  1.00 31.03           C
ANISOU 1402  CB  LEU A 489     4488   2595   4707   -302   -273     39       C
ATOM   1403  CG  LEU A 489      12.989  -6.789  25.917  1.00 28.78           C
ANISOU 1403  CG  LEU A 489     4228   2258   4449   -176   -197    162       C
ATOM   1404  CD1 LEU A 489      12.298  -8.116  25.705  1.00 21.12           C
ANISOU 1404  CD1 LEU A 489     3197   1455   3374    -45   -192    183       C
ATOM   1405  CD2 LEU A 489      12.024  -5.698  26.334  1.00 34.10           C
ANISOU 1405  CD2 LEU A 489     5045   2719   5192   -121   -155    119       C
ATOM   1406  N   MET A 490      16.836  -6.779  28.379  1.00 28.29           N
ANISOU 1406  N   MET A 490     4016   2381   4351   -637   -434   -124       N
ATOM   1407  CA  MET A 490      17.577  -7.008  29.603  1.00 31.54           C
ANISOU 1407  CA  MET A 490     4398   2891   4694   -722   -527   -254       C
ATOM   1408  C   MET A 490      18.442  -5.812  29.950  1.00 30.96           C
ANISOU 1408  C   MET A 490     4349   2710   4704   -930   -565   -332       C
ATOM   1409  O   MET A 490      18.566  -5.468  31.131  1.00 36.68           O
ANISOU 1409  O   MET A 490     5135   3415   5388  -1000   -625   -490       O
ATOM   1410  CB  MET A 490      18.430  -8.271  29.478  1.00 28.98           C
ANISOU 1410  CB  MET A 490     3907   2814   4292   -700   -576   -196       C
ATOM   1411  CG  MET A 490      17.585  -9.546  29.363  1.00 27.76           C
ANISOU 1411  CG  MET A 490     3744   2752   4051   -508   -547   -150       C
ATOM   1412  SD  MET A 490      18.611 -10.900  28.816  1.00 28.03           S
ANISOU 1412  SD  MET A 490     3589   3020   4039   -470   -572    -56       S
ATOM   1413  CE  MET A 490      17.360 -12.196  28.583  1.00 24.44           C
ANISOU 1413  CE  MET A 490     3174   2595   3516   -262   -517    -16       C
ATOM   1414  N   ALA A 491      19.058  -5.166  28.940  1.00 33.08           N
ANISOU 1414  N   ALA A 491     4568   2916   5086  -1042   -529   -226       N
ATOM   1415  CA  ALA A 491      19.797  -3.916  29.179  1.00 32.62           C
ANISOU 1415  CA  ALA A 491     4547   2712   5134  -1261   -551   -293       C
ATOM   1416  C   ALA A 491      18.874  -2.826  29.705  1.00 41.81           C
ANISOU 1416  C   ALA A 491     5919   3598   6367  -1253   -511   -403       C
ATOM   1417  O   ALA A 491      19.248  -2.053  30.595  1.00 39.25           O
ANISOU 1417  O   ALA A 491     5653   3204   6057  -1381   -536   -562       O
ATOM   1418  CB  ALA A 491      20.485  -3.414  27.901  1.00 28.57           C
ANISOU 1418  CB  ALA A 491     3952   2167   4736  -1372   -498   -128       C
ATOM   1419  N   LYS A 492      17.673  -2.724  29.129  1.00 37.86           N
ANISOU 1419  N   LYS A 492     5515   2973   5898  -1081   -422   -322       N
ATOM   1420  CA  LYS A 492      16.701  -1.745  29.598  1.00 38.71           C
ANISOU 1420  CA  LYS A 492     5786   2885   6037  -1003   -331   -414       C
ATOM   1421  C   LYS A 492      16.326  -1.991  31.063  1.00 40.74           C
ANISOU 1421  C   LYS A 492     6106   3187   6188   -963   -380   -620       C
ATOM   1422  O   LYS A 492      16.111  -1.045  31.822  1.00 41.20           O
ANISOU 1422  O   LYS A 492     6253   3121   6279   -993   -334   -765       O
ATOM   1423  CB  LYS A 492      15.476  -1.805  28.687  1.00 41.87           C
ANISOU 1423  CB  LYS A 492     6231   3226   6453   -800   -231   -269       C
ATOM   1424  CG  LYS A 492      14.333  -0.919  29.076  1.00 49.74           C
ANISOU 1424  CG  LYS A 492     7366   4058   7475   -680   -121   -335       C
ATOM   1425  CD  LYS A 492      13.164  -1.125  28.117  1.00 48.74           C
ANISOU 1425  CD  LYS A 492     7257   3934   7328   -480    -42   -173       C
ATOM   1426  CE  LYS A 492      12.597   0.218  27.671  1.00 48.60           C
ANISOU 1426  CE  LYS A 492     7392   3745   7329   -435     21   -106       C
ATOM   1427  NZ  LYS A 492      11.190   0.067  27.219  1.00 57.27           N
ANISOU 1427  NZ  LYS A 492     8508   4880   8374   -211    -35    -13       N
ATOM   1428  N   ALA A 493      16.241  -3.258  31.475  1.00 38.74           N
ANISOU 1428  N   ALA A 493     5799   3111   5808   -892   -469   -634       N
ATOM   1429  CA  ALA A 493      15.995  -3.684  32.856  1.00 41.14           C
ANISOU 1429  CA  ALA A 493     6144   3514   5971   -855   -525   -805       C
ATOM   1430  C   ALA A 493      17.180  -3.440  33.789  1.00 46.19           C
ANISOU 1430  C   ALA A 493     6741   4246   6564  -1053   -627   -949       C
ATOM   1431  O   ALA A 493      17.070  -3.710  34.999  1.00 45.05           O
ANISOU 1431  O   ALA A 493     6627   4204   6286  -1039   -678  -1095       O
ATOM   1432  CB  ALA A 493      15.636  -5.175  32.886  1.00 37.99           C
ANISOU 1432  CB  ALA A 493     5647   3352   5436   -698   -539   -725       C
ATOM   1433  N   GLY A 494      18.308  -2.972  33.267  1.00 36.74           N
ANISOU 1433  N   GLY A 494     5456   3046   5458  -1233   -653   -904       N
ATOM   1434  CA  GLY A 494      19.423  -2.557  34.100  1.00 37.00           C
ANISOU 1434  CA  GLY A 494     5428   3169   5463  -1428   -733  -1044       C
ATOM   1435  C   GLY A 494      20.508  -3.601  34.292  1.00 48.36           C
ANISOU 1435  C   GLY A 494     6693   4885   6797  -1508   -873  -1007       C
ATOM   1436  O   GLY A 494      21.488  -3.335  35.008  1.00 39.59           O
ANISOU 1436  O   GLY A 494     5499   3897   5647  -1660   -949  -1115       O
ATOM   1437  N   LEU A 495      20.366  -4.776  33.681  1.00 38.59           N
ANISOU 1437  N   LEU A 495     5346   3808   5508  -1350   -855   -845       N
ATOM   1438  CA  LEU A 495      21.364  -5.826  33.827  1.00 37.65           C
ANISOU 1438  CA  LEU A 495     5031   3980   5293  -1360   -942   -787       C
ATOM   1439  C   LEU A 495      22.700  -5.382  33.233  1.00 40.71           C
ANISOU 1439  C   LEU A 495     5271   4422   5775  -1563   -978   -733       C
ATOM   1440  O   LEU A 495      22.750  -4.687  32.212  1.00 35.90           O
ANISOU 1440  O   LEU A 495     4676   3658   5307  -1631   -903   -646       O
ATOM   1441  CB  LEU A 495      20.868  -7.115  33.163  1.00 36.52           C
ANISOU 1441  CB  LEU A 495     4823   3949   5103  -1142   -890   -628       C
ATOM   1442  CG  LEU A 495      19.978  -8.027  34.015  1.00 36.29           C
ANISOU 1442  CG  LEU A 495     4857   3998   4933   -964   -898   -666       C
ATOM   1443  CD1 LEU A 495      18.748  -7.272  34.461  1.00 38.32           C
ANISOU 1443  CD1 LEU A 495     5312   4049   5199   -916   -837   -774       C
ATOM   1444  CD2 LEU A 495      19.554  -9.297  33.233  1.00 30.91           C
ANISOU 1444  CD2 LEU A 495     4108   3405   4232   -776   -842   -509       C
ATOM   1445  N   THR A 496      23.790  -5.748  33.907  1.00 40.59           N
ANISOU 1445  N   THR A 496     5106   4639   5676  -1666  -1096   -780       N
ATOM   1446  CA  THR A 496      25.113  -5.551  33.341  1.00 35.98           C
ANISOU 1446  CA  THR A 496     4334   4172   5165  -1840  -1133   -710       C
ATOM   1447  C   THR A 496      25.259  -6.405  32.098  1.00 39.26           C
ANISOU 1447  C   THR A 496     4620   4684   5614  -1705  -1058   -503       C
ATOM   1448  O   THR A 496      24.464  -7.306  31.838  1.00 33.64           O
ANISOU 1448  O   THR A 496     3946   3988   4848  -1485  -1005   -432       O
ATOM   1449  CB  THR A 496      26.203  -5.948  34.334  1.00 44.60           C
ANISOU 1449  CB  THR A 496     5263   5543   6140  -1926  -1272   -786       C
ATOM   1450  OG1 THR A 496      26.262  -7.379  34.435  1.00 37.00           O
ANISOU 1450  OG1 THR A 496     4185   4814   5059  -1733  -1306   -684       O
ATOM   1451  CG2 THR A 496      25.913  -5.356  35.706  1.00 46.27           C
ANISOU 1451  CG2 THR A 496     5601   5707   6270  -1958  -1321   -999       C
ATOM   1452  N   LEU A 497      26.306  -6.140  31.323  1.00 40.34           N
ANISOU 1452  N   LEU A 497     4596   4895   5835  -1846  -1052   -413       N
ATOM   1453  CA  LEU A 497      26.473  -6.917  30.096  1.00 42.52           C
ANISOU 1453  CA  LEU A 497     4749   5271   6134  -1719   -970   -229       C
ATOM   1454  C   LEU A 497      26.669  -8.405  30.397  1.00 36.53           C
ANISOU 1454  C   LEU A 497     3868   4761   5250  -1525  -1014   -187       C
ATOM   1455  O   LEU A 497      26.039  -9.272  29.774  1.00 36.26           O
ANISOU 1455  O   LEU A 497     3855   4730   5192  -1323   -940    -98       O
ATOM   1456  CB  LEU A 497      27.628  -6.353  29.278  1.00 38.47           C
ANISOU 1456  CB  LEU A 497     4072   4822   5723  -1913   -952   -141       C
ATOM   1457  CG  LEU A 497      27.655  -6.845  27.836  1.00 43.21           C
ANISOU 1457  CG  LEU A 497     4586   5473   6360  -1802   -836     43       C
ATOM   1458  CD1 LEU A 497      26.693  -6.044  26.962  1.00 46.43           C
ANISOU 1458  CD1 LEU A 497     5170   5611   6860  -1792   -721    108       C
ATOM   1459  CD2 LEU A 497      29.087  -6.734  27.310  1.00 49.25           C
ANISOU 1459  CD2 LEU A 497     5108   6436   7170  -1963   -845    126       C
ATOM   1460  N   GLN A 498      27.539  -8.712  31.352  1.00 37.26           N
ANISOU 1460  N   GLN A 498     3833   5061   5263  -1586  -1136   -250       N
ATOM   1461  CA  GLN A 498      27.729 -10.096  31.760  1.00 38.04           C
ANISOU 1461  CA  GLN A 498     3826   5380   5247  -1395  -1183   -203       C
ATOM   1462  C   GLN A 498      26.404 -10.756  32.139  1.00 35.60           C
ANISOU 1462  C   GLN A 498     3698   4964   4865  -1186  -1146   -222       C
ATOM   1463  O   GLN A 498      26.115 -11.876  31.701  1.00 30.00           O
ANISOU 1463  O   GLN A 498     2960   4311   4128   -988  -1096   -127       O
ATOM   1464  CB  GLN A 498      28.707 -10.145  32.933  1.00 40.49           C
ANISOU 1464  CB  GLN A 498     4003   5915   5467  -1500  -1336   -281       C
ATOM   1465  CG  GLN A 498      29.120 -11.548  33.264  1.00 43.46           C
ANISOU 1465  CG  GLN A 498     4236   6534   5742  -1304  -1385   -197       C
ATOM   1466  CD  GLN A 498      30.133 -11.571  34.365  1.00 46.79           C
ANISOU 1466  CD  GLN A 498     4537   7163   6077  -1357  -1505   -260       C
ATOM   1467  OE1 GLN A 498      30.801 -12.581  34.604  1.00 47.47           O
ANISOU 1467  OE1 GLN A 498     4485   7446   6106  -1205  -1536   -179       O
ATOM   1468  NE2 GLN A 498      30.230 -10.461  35.082  1.00 49.23           N
ANISOU 1468  NE2 GLN A 498     4927   7395   6384  -1541  -1556   -409       N
ATOM   1469  N   GLN A 499      25.577 -10.071  32.946  1.00 32.90           N
ANISOU 1469  N   GLN A 499     3543   4464   4493  -1232  -1164   -352       N
ATOM   1470  CA  GLN A 499      24.254 -10.579  33.308  1.00 38.87           C
ANISOU 1470  CA  GLN A 499     4469   5116   5183  -1052  -1118   -372       C
ATOM   1471  C   GLN A 499      23.336 -10.725  32.098  1.00 30.93           C
ANISOU 1471  C   GLN A 499     3542   3951   4259   -932   -984   -276       C
ATOM   1472  O   GLN A 499      22.518 -11.651  32.047  1.00 30.08           O
ANISOU 1472  O   GLN A 499     3486   3840   4102   -749   -941   -232       O
ATOM   1473  CB  GLN A 499      23.619  -9.655  34.352  1.00 33.82           C
ANISOU 1473  CB  GLN A 499     4003   4343   4503  -1139  -1152   -540       C
ATOM   1474  CG  GLN A 499      24.198  -9.808  35.725  1.00 38.39           C
ANISOU 1474  CG  GLN A 499     4533   5110   4943  -1199  -1286   -643       C
ATOM   1475  CD  GLN A 499      23.771  -8.682  36.659  1.00 46.80           C
ANISOU 1475  CD  GLN A 499     5761   6043   5977  -1331  -1317   -840       C
ATOM   1476  OE1 GLN A 499      23.448  -7.569  36.222  1.00 42.60           O
ANISOU 1476  OE1 GLN A 499     5341   5279   5566  -1437  -1255   -901       O
ATOM   1477  NE2 GLN A 499      23.749  -8.974  37.950  1.00 47.93           N
ANISOU 1477  NE2 GLN A 499     5925   6330   5955  -1315  -1408   -938       N
ATOM   1478  N   GLN A 500      23.459  -9.842  31.105  1.00 32.77           N
ANISOU 1478  N   GLN A 500     3780   4059   4613  -1037   -920   -236       N
ATOM   1479  CA  GLN A 500      22.642  -9.979  29.901  1.00 28.12           C
ANISOU 1479  CA  GLN A 500     3248   3351   4083   -924   -801   -134       C
ATOM   1480  C   GLN A 500      22.960 -11.276  29.150  1.00 29.90           C
ANISOU 1480  C   GLN A 500     3340   3743   4279   -781   -768    -18       C
ATOM   1481  O   GLN A 500      22.062 -12.052  28.819  1.00 26.92           O
ANISOU 1481  O   GLN A 500     3023   3336   3870   -616   -711     19       O
ATOM   1482  CB  GLN A 500      22.871  -8.771  28.990  1.00 26.21           C
ANISOU 1482  CB  GLN A 500     3021   2969   3969  -1074   -743    -90       C
ATOM   1483  CG  GLN A 500      22.286  -7.468  29.476  1.00 31.60           C
ANISOU 1483  CG  GLN A 500     3879   3416   4714  -1179   -738   -193       C
ATOM   1484  CD  GLN A 500      22.739  -6.316  28.605  1.00 35.69           C
ANISOU 1484  CD  GLN A 500     4391   3801   5369  -1346   -687   -128       C
ATOM   1485  OE1 GLN A 500      22.842  -6.457  27.389  1.00 31.44           O
ANISOU 1485  OE1 GLN A 500     3786   3288   4874  -1313   -612     18       O
ATOM   1486  NE2 GLN A 500      23.013  -5.173  29.223  1.00 35.89           N
ANISOU 1486  NE2 GLN A 500     4492   3685   5460  -1531   -724   -239       N
ATOM   1487  N   HIS A 501      24.243 -11.526  28.877  1.00 26.70           N
ANISOU 1487  N   HIS A 501     2746   3514   3884   -843   -801     34       N
ATOM   1488  CA  HIS A 501      24.651 -12.751  28.199  1.00 28.40           C
ANISOU 1488  CA  HIS A 501     2828   3887   4075   -700   -765    129       C
ATOM   1489  C   HIS A 501      24.220 -13.973  28.990  1.00 24.43           C
ANISOU 1489  C   HIS A 501     2356   3446   3481   -524   -801    110       C
ATOM   1490  O   HIS A 501      23.715 -14.941  28.410  1.00 26.50           O
ANISOU 1490  O   HIS A 501     2633   3706   3731   -365   -734    163       O
ATOM   1491  CB  HIS A 501      26.164 -12.762  28.029  1.00 27.90           C
ANISOU 1491  CB  HIS A 501     2543   4024   4032   -796   -807    173       C
ATOM   1492  CG  HIS A 501      26.674 -11.709  27.105  1.00 44.89           C
ANISOU 1492  CG  HIS A 501     4642   6137   6278   -967   -755    222       C
ATOM   1493  ND1 HIS A 501      25.885 -11.127  26.130  1.00 39.03           N
ANISOU 1493  ND1 HIS A 501     4015   5222   5592   -972   -654    271       N
ATOM   1494  CD2 HIS A 501      27.864 -11.060  27.069  1.00 41.38           C
ANISOU 1494  CD2 HIS A 501     4043   5797   5881  -1154   -793    236       C
ATOM   1495  CE1 HIS A 501      26.591 -10.214  25.485  1.00 41.76           C
ANISOU 1495  CE1 HIS A 501     4284   5566   6016  -1144   -623    327       C
ATOM   1496  NE2 HIS A 501      27.790 -10.143  26.046  1.00 38.03           N
ANISOU 1496  NE2 HIS A 501     3648   5255   5545  -1267   -705    302       N
ATOM   1497  N   GLN A 502      24.412 -13.931  30.321  1.00 28.47           N
ANISOU 1497  N   GLN A 502     2879   4015   3924   -561   -904     35       N
ATOM   1498  CA  GLN A 502      24.139 -15.093  31.156  1.00 27.08           C
ANISOU 1498  CA  GLN A 502     2718   3918   3654   -404   -944     41       C
ATOM   1499  C   GLN A 502      22.663 -15.417  31.154  1.00 26.08           C
ANISOU 1499  C   GLN A 502     2772   3630   3507   -287   -875     26       C
ATOM   1500  O   GLN A 502      22.288 -16.598  31.074  1.00 22.23           O
ANISOU 1500  O   GLN A 502     2291   3165   2991   -127   -842     80       O
ATOM   1501  CB  GLN A 502      24.598 -14.868  32.581  1.00 23.34           C
ANISOU 1501  CB  GLN A 502     2225   3553   3090   -478  -1071    -34       C
ATOM   1502  CG  GLN A 502      26.160 -14.902  32.747  1.00 28.47           C
ANISOU 1502  CG  GLN A 502     2650   4433   3735   -561  -1162     -3       C
ATOM   1503  CD  GLN A 502      26.614 -14.598  34.157  1.00 30.23           C
ANISOU 1503  CD  GLN A 502     2848   4786   3852   -655  -1301    -87       C
ATOM   1504  OE1 GLN A 502      25.800 -14.416  35.064  1.00 29.81           O
ANISOU 1504  OE1 GLN A 502     2948   4660   3717   -649  -1327   -170       O
ATOM   1505  NE2 GLN A 502      27.931 -14.537  34.352  1.00 35.41           N
ANISOU 1505  NE2 GLN A 502     3300   5658   4498   -744  -1392    -68       N
ATOM   1506  N   ARG A 503      21.817 -14.372  31.252  1.00 20.93           N
ANISOU 1506  N   ARG A 503     2264   2810   2876   -367   -850    -47       N
ATOM   1507  CA  ARG A 503      20.367 -14.581  31.255  1.00 20.32           C
ANISOU 1507  CA  ARG A 503     2344   2593   2781   -262   -782    -61       C
ATOM   1508  C   ARG A 503      19.879 -15.052  29.886  1.00 21.23           C
ANISOU 1508  C   ARG A 503     2454   2656   2956   -173   -681     22       C
ATOM   1509  O   ARG A 503      19.022 -15.941  29.797  1.00 19.05           O
ANISOU 1509  O   ARG A 503     2233   2354   2651    -45   -636     44       O
ATOM   1510  CB  ARG A 503      19.634 -13.288  31.669  1.00 24.72           C
ANISOU 1510  CB  ARG A 503     3046   2990   3356   -356   -775   -160       C
ATOM   1511  CG  ARG A 503      18.109 -13.511  31.905  1.00 24.01           C
ANISOU 1511  CG  ARG A 503     3104   2787   3232   -239   -713   -182       C
ATOM   1512  CD  ARG A 503      17.384 -12.242  32.442  1.00 22.13           C
ANISOU 1512  CD  ARG A 503     3009   2393   3006   -306   -701   -291       C
ATOM   1513  NE  ARG A 503      15.930 -12.436  32.554  1.00 20.85           N
ANISOU 1513  NE  ARG A 503     2961   2141   2818   -186   -631   -300       N
ATOM   1514  CZ  ARG A 503      15.327 -12.874  33.665  1.00 22.46           C
ANISOU 1514  CZ  ARG A 503     3228   2388   2918   -122   -645   -355       C
ATOM   1515  NH1 ARG A 503      16.055 -13.198  34.747  1.00 24.27           N
ANISOU 1515  NH1 ARG A 503     3421   2753   3049   -159   -733   -399       N
ATOM   1516  NH2 ARG A 503      14.006 -13.006  33.679  1.00 25.90           N
ANISOU 1516  NH2 ARG A 503     3750   2751   3339    -22   -573   -355       N
ATOM   1517  N   LEU A 504      20.406 -14.474  28.800  1.00 19.60           N
ANISOU 1517  N   LEU A 504     2181   2441   2826   -248   -642     67       N
ATOM   1518  CA  LEU A 504      20.057 -14.980  27.470  1.00 24.84           C
ANISOU 1518  CA  LEU A 504     2823   3095   3521   -164   -551    143       C
ATOM   1519  C   LEU A 504      20.309 -16.485  27.388  1.00 17.98           C
ANISOU 1519  C   LEU A 504     1880   2339   2612    -24   -544    179       C
ATOM   1520  O   LEU A 504      19.437 -17.263  26.979  1.00 16.81           O
ANISOU 1520  O   LEU A 504     1790   2147   2449     86   -487    190       O
ATOM   1521  CB  LEU A 504      20.856 -14.228  26.393  1.00 18.84           C
ANISOU 1521  CB  LEU A 504     1971   2360   2829   -269   -516    202       C
ATOM   1522  CG  LEU A 504      20.666 -14.666  24.947  1.00 20.71           C
ANISOU 1522  CG  LEU A 504     2168   2624   3077   -198   -423    280       C
ATOM   1523  CD1 LEU A 504      19.214 -14.426  24.536  1.00 16.51           C
ANISOU 1523  CD1 LEU A 504     1777   1955   2542   -142   -368    281       C
ATOM   1524  CD2 LEU A 504      21.650 -13.945  24.028  1.00 22.04           C
ANISOU 1524  CD2 LEU A 504     2223   2853   3296   -313   -392    350       C
ATOM   1525  N   ALA A 505      21.490 -16.903  27.801  1.00 17.15           N
ANISOU 1525  N   ALA A 505     1646   2375   2495    -29   -601    194       N
ATOM   1526  CA  ALA A 505      21.866 -18.314  27.780  1.00 18.99           C
ANISOU 1526  CA  ALA A 505     1805   2706   2705    116   -594    235       C
ATOM   1527  C   ALA A 505      20.935 -19.165  28.639  1.00 20.63           C
ANISOU 1527  C   ALA A 505     2126   2853   2861    224   -604    218       C
ATOM   1528  O   ALA A 505      20.498 -20.250  28.198  1.00 17.02           O
ANISOU 1528  O   ALA A 505     1691   2368   2409    347   -546    243       O
ATOM   1529  CB  ALA A 505      23.304 -18.463  28.265  1.00 18.53           C
ANISOU 1529  CB  ALA A 505     1579   2821   2640     92   -669    261       C
ATOM   1530  N   GLN A 506      20.626 -18.696  29.868  1.00 16.53           N
ANISOU 1530  N   GLN A 506     1680   2314   2288    174   -673    172       N
ATOM   1531  CA  GLN A 506      19.752 -19.461  30.762  1.00 19.40           C
ANISOU 1531  CA  GLN A 506     2145   2636   2589    267   -679    168       C
ATOM   1532  C   GLN A 506      18.359 -19.636  30.134  1.00 21.01           C
ANISOU 1532  C   GLN A 506     2469   2701   2815    313   -588    157       C
ATOM   1533  O   GLN A 506      17.765 -20.740  30.170  1.00 17.51           O
ANISOU 1533  O   GLN A 506     2066   2227   2360    418   -550    186       O
ATOM   1534  CB  GLN A 506      19.656 -18.765  32.154  1.00 17.59           C
ANISOU 1534  CB  GLN A 506     1974   2429   2280    191   -762    106       C
ATOM   1535  CG  GLN A 506      20.914 -18.761  33.039  1.00 23.55           C
ANISOU 1535  CG  GLN A 506     2613   3355   2980    151   -873    113       C
ATOM   1536  CD  GLN A 506      20.934 -17.552  34.043  1.00 33.97           C
ANISOU 1536  CD  GLN A 506     3986   4685   4238      8   -950      8       C
ATOM   1537  OE1 GLN A 506      19.949 -16.810  34.161  1.00 30.11           O
ANISOU 1537  OE1 GLN A 506     3631   4061   3747    -36   -912    -67       O
ATOM   1538  NE2 GLN A 506      22.046 -17.375  34.756  1.00 29.60           N
ANISOU 1538  NE2 GLN A 506     3321   4294   3630    -61  -1058     -4       N
ATOM   1539  N   LEU A 507      17.838 -18.571  29.502  1.00 18.08           N
ANISOU 1539  N   LEU A 507     2146   2245   2480    234   -551    123       N
ATOM   1540  CA  LEU A 507      16.533 -18.657  28.868  1.00 17.04           C
ANISOU 1540  CA  LEU A 507     2104   2008   2362    277   -474    118       C
ATOM   1541  C   LEU A 507      16.571 -19.620  27.680  1.00 16.02           C
ANISOU 1541  C   LEU A 507     1923   1899   2264    351   -411    160       C
ATOM   1542  O   LEU A 507      15.625 -20.394  27.471  1.00 16.07           O
ANISOU 1542  O   LEU A 507     1986   1857   2262    419   -364    159       O
ATOM   1543  CB  LEU A 507      16.053 -17.269  28.411  1.00 13.45           C
ANISOU 1543  CB  LEU A 507     1702   1464   1943    192   -451     92       C
ATOM   1544  CG  LEU A 507      15.713 -16.336  29.615  1.00 16.74           C
ANISOU 1544  CG  LEU A 507     2207   1824   2328    133   -495     21       C
ATOM   1545  CD1 LEU A 507      15.116 -14.986  29.171  1.00 18.50           C
ANISOU 1545  CD1 LEU A 507     2502   1922   2606     72   -459     -3       C
ATOM   1546  CD2 LEU A 507      14.753 -17.060  30.600  1.00 23.58           C
ANISOU 1546  CD2 LEU A 507     3153   2685   3123    214   -492     -2       C
ATOM   1547  N   LEU A 508      17.613 -19.548  26.856  1.00 18.76           N
ANISOU 1547  N   LEU A 508     2162   2320   2646    331   -403    189       N
ATOM   1548  CA  LEU A 508      17.609 -20.400  25.669  1.00 16.51           C
ANISOU 1548  CA  LEU A 508     1836   2059   2379    402   -333    208       C
ATOM   1549  C   LEU A 508      17.836 -21.861  26.037  1.00 16.18           C
ANISOU 1549  C   LEU A 508     1778   2036   2332    517   -330    216       C
ATOM   1550  O   LEU A 508      17.291 -22.743  25.360  1.00 20.43           O
ANISOU 1550  O   LEU A 508     2345   2536   2879    585   -268    202       O
ATOM   1551  CB  LEU A 508      18.638 -19.939  24.640  1.00 16.87           C
ANISOU 1551  CB  LEU A 508     1765   2192   2452    356   -309    239       C
ATOM   1552  CG  LEU A 508      18.431 -18.544  24.055  1.00 17.82           C
ANISOU 1552  CG  LEU A 508     1903   2276   2590    245   -295    256       C
ATOM   1553  CD1 LEU A 508      19.561 -18.254  23.073  1.00 19.90           C
ANISOU 1553  CD1 LEU A 508     2037   2649   2876    200   -264    304       C
ATOM   1554  CD2 LEU A 508      17.058 -18.449  23.416  1.00 18.37           C
ANISOU 1554  CD2 LEU A 508     2071   2265   2646    271   -243    249       C
ATOM   1555  N   LEU A 509      18.595 -22.136  27.104  1.00 16.99           N
ANISOU 1555  N   LEU A 509     1839   2194   2421    540   -396    239       N
ATOM   1556  CA  LEU A 509      18.750 -23.528  27.546  1.00 20.39           C
ANISOU 1556  CA  LEU A 509     2269   2624   2855    664   -391    269       C
ATOM   1557  C   LEU A 509      17.431 -24.120  28.047  1.00 19.14           C
ANISOU 1557  C   LEU A 509     2244   2351   2677    697   -367    259       C
ATOM   1558  O   LEU A 509      17.200 -25.322  27.903  1.00 20.12           O
ANISOU 1558  O   LEU A 509     2397   2422   2827    788   -322    273       O
ATOM   1559  CB  LEU A 509      19.827 -23.660  28.614  1.00 18.31           C
ANISOU 1559  CB  LEU A 509     1924   2466   2568    689   -476    316       C
ATOM   1560  CG  LEU A 509      21.237 -23.425  28.071  1.00 19.17           C
ANISOU 1560  CG  LEU A 509     1868   2709   2706    681   -491    339       C
ATOM   1561  CD1 LEU A 509      22.275 -23.372  29.208  1.00 25.52           C
ANISOU 1561  CD1 LEU A 509     2574   3648   3474    683   -595    383       C
ATOM   1562  CD2 LEU A 509      21.662 -24.461  26.972  1.00 22.18           C
ANISOU 1562  CD2 LEU A 509     2185   3100   3141    801   -406    351       C
ATOM   1563  N   ILE A 510      16.540 -23.290  28.591  1.00 20.51           N
ANISOU 1563  N   ILE A 510     2501   2482   2812    623   -385    231       N
ATOM   1564  CA  ILE A 510      15.211 -23.754  28.973  1.00 19.20           C
ANISOU 1564  CA  ILE A 510     2444   2224   2625    643   -351    222       C
ATOM   1565  C   ILE A 510      14.450 -24.245  27.748  1.00 20.69           C
ANISOU 1565  C   ILE A 510     2656   2351   2854    658   -271    193       C
ATOM   1566  O   ILE A 510      13.720 -25.245  27.828  1.00 15.26           O
ANISOU 1566  O   ILE A 510     2025   1596   2176    699   -231    196       O
ATOM   1567  CB  ILE A 510      14.475 -22.619  29.730  1.00 18.82           C
ANISOU 1567  CB  ILE A 510     2465   2160   2527    567   -379    188       C
ATOM   1568  CG1 ILE A 510      15.173 -22.363  31.061  1.00 22.86           C
ANISOU 1568  CG1 ILE A 510     2963   2744   2978    555   -461    201       C
ATOM   1569  CG2 ILE A 510      12.992 -22.992  29.967  1.00 17.67           C
ANISOU 1569  CG2 ILE A 510     2414   1939   2362    582   -328    178       C
ATOM   1570  CD1 ILE A 510      14.510 -21.227  31.900  1.00 25.49           C
ANISOU 1570  CD1 ILE A 510     3373   3061   3253    484   -485    143       C
ATOM   1571  N   LEU A 511      14.661 -23.609  26.582  1.00 16.33           N
ANISOU 1571  N   LEU A 511     2056   1829   2321    619   -247    169       N
ATOM   1572  CA  LEU A 511      14.055 -24.078  25.336  1.00 17.67           C
ANISOU 1572  CA  LEU A 511     2233   1974   2506    631   -178    136       C
ATOM   1573  C   LEU A 511      14.426 -25.529  25.021  1.00 17.20           C
ANISOU 1573  C   LEU A 511     2162   1893   2482    716   -139    126       C
ATOM   1574  O   LEU A 511      13.613 -26.233  24.424  1.00 18.31           O
ANISOU 1574  O   LEU A 511     2347   1980   2632    724    -87     83       O
ATOM   1575  CB  LEU A 511      14.470 -23.160  24.173  1.00 14.88           C
ANISOU 1575  CB  LEU A 511     1815   1687   2153    583   -162    133       C
ATOM   1576  CG  LEU A 511      13.901 -21.727  24.298  1.00 18.12           C
ANISOU 1576  CG  LEU A 511     2257   2079   2547    505   -184    144       C
ATOM   1577  CD1 LEU A 511      14.077 -20.950  22.957  1.00 16.00           C
ANISOU 1577  CD1 LEU A 511     1939   1863   2277    464   -152    162       C
ATOM   1578  CD2 LEU A 511      12.439 -21.723  24.748  1.00 19.76           C
ANISOU 1578  CD2 LEU A 511     2555   2218   2734    505   -175    125       C
ATOM   1579  N   SER A 512      15.638 -26.002  25.378  1.00 15.01           N
ANISOU 1579  N   SER A 512     1821   1654   2228    782   -159    161       N
ATOM   1580  CA  SER A 512      15.961 -27.439  25.218  1.00 15.14           C
ANISOU 1580  CA  SER A 512     1837   1623   2293    853   -114    152       C
ATOM   1581  C   SER A 512      15.092 -28.323  26.080  0.85 16.18           C
ANISOU 1581  C   SER A 512     2057   1653   2439    832   -106    165       C
ATOM   1582  O   SER A 512      14.720 -29.442  25.668  1.00 14.11           O
ANISOU 1582  O   SER A 512     1831   1309   2220    846    -55    128       O
ATOM   1583  CB  SER A 512      17.435 -27.803  25.500  1.00 22.87           C
ANISOU 1583  CB  SER A 512     2720   2670   3300    925   -138    197       C
ATOM   1584  OG  SER A 512      18.424 -27.267  24.592  1.00 29.19           O
ANISOU 1584  OG  SER A 512     3405   3585   4100    952   -126    189       O
ATOM   1585  N   HIS A 513      14.806 -27.870  27.298  1.00 14.80           N
ANISOU 1585  N   HIS A 513     1914   1486   2224    805   -157    217       N
ATOM   1586  CA  HIS A 513      13.896 -28.620  28.171  1.00 17.17           C
ANISOU 1586  CA  HIS A 513     2290   1709   2523    784   -145    242       C
ATOM   1587  C   HIS A 513      12.463 -28.628  27.633  1.00 16.81           C
ANISOU 1587  C   HIS A 513     2305   1607   2475    721    -97    187       C
ATOM   1588  O   HIS A 513      11.766 -29.647  27.750  1.00 16.61           O
ANISOU 1588  O   HIS A 513     2329   1500   2481    712    -63    183       O
ATOM   1589  CB  HIS A 513      13.912 -28.040  29.588  1.00 17.74           C
ANISOU 1589  CB  HIS A 513     2382   1830   2529    779   -207    305       C
ATOM   1590  CG  HIS A 513      13.073 -28.829  30.560  1.00 29.55           C
ANISOU 1590  CG  HIS A 513     3949   3266   4012    771   -191    349       C
ATOM   1591  ND1 HIS A 513      11.979 -28.288  31.212  1.00 39.72           N
ANISOU 1591  ND1 HIS A 513     5300   4555   5238    727   -189    350       N
ATOM   1592  CD2 HIS A 513      13.171 -30.111  30.995  1.00 29.95           C
ANISOU 1592  CD2 HIS A 513     4022   3254   4103    808   -177    400       C
ATOM   1593  CE1 HIS A 513      11.447 -29.201  32.013  1.00 32.68           C
ANISOU 1593  CE1 HIS A 513     4459   3616   4343    734   -169    407       C
ATOM   1594  NE2 HIS A 513      12.150 -30.317  31.898  1.00 36.57           N
ANISOU 1594  NE2 HIS A 513     4932   4063   4900    780   -164    441       N
ATOM   1595  N   ILE A 514      11.995 -27.505  27.076  1.00 13.64           N
ANISOU 1595  N   ILE A 514     1900   1246   2036    680   -100    150       N
ATOM   1596  CA  ILE A 514      10.663 -27.462  26.465  1.00 13.70           C
ANISOU 1596  CA  ILE A 514     1948   1222   2036    632    -62    101       C
ATOM   1597  C   ILE A 514      10.598 -28.400  25.248  1.00 17.61           C
ANISOU 1597  C   ILE A 514     2442   1676   2573    649    -10     37       C
ATOM   1598  O   ILE A 514       9.590 -29.106  25.051  1.00 13.05           O
ANISOU 1598  O   ILE A 514     1913   1034   2012    621     27      2       O
ATOM   1599  CB  ILE A 514      10.293 -26.006  26.138  1.00 12.76           C
ANISOU 1599  CB  ILE A 514     1819   1157   1871    602    -84     88       C
ATOM   1600  CG1 ILE A 514      10.061 -25.259  27.479  1.00 16.82           C
ANISOU 1600  CG1 ILE A 514     2364   1682   2344    585   -123    126       C
ATOM   1601  CG2 ILE A 514       9.015 -25.925  25.264  1.00 14.88           C
ANISOU 1601  CG2 ILE A 514     2109   1417   2128    575    -49     43       C
ATOM   1602  CD1 ILE A 514       9.869 -23.783  27.294  1.00 16.90           C
ANISOU 1602  CD1 ILE A 514     2374   1720   2329    563   -149    112       C
ATOM   1603  N   ARG A 515      11.676 -28.473  24.441  1.00 15.68           N
ANISOU 1603  N   ARG A 515     2145   1467   2346    698     -1     14       N
ATOM   1604  CA  ARG A 515      11.708 -29.469  23.366  1.00 14.42           C
ANISOU 1604  CA  ARG A 515     1991   1266   2221    725     57    -64       C
ATOM   1605  C   ARG A 515      11.549 -30.865  23.947  1.00 15.08           C
ANISOU 1605  C   ARG A 515     2123   1237   2371    731     76    -63       C
ATOM   1606  O   ARG A 515      10.768 -31.691  23.443  1.00 15.40           O
ANISOU 1606  O   ARG A 515     2216   1199   2437    705    117   -134       O
ATOM   1607  CB  ARG A 515      13.022 -29.409  22.568  1.00 14.45           C
ANISOU 1607  CB  ARG A 515     1921   1339   2231    794     73    -83       C
ATOM   1608  CG  ARG A 515      13.111 -30.444  21.333  1.00 20.18           C
ANISOU 1608  CG  ARG A 515     2653   2035   2980    830    147   -193       C
ATOM   1609  CD  ARG A 515      12.153 -30.119  20.212  1.00 23.34           C
ANISOU 1609  CD  ARG A 515     3067   2486   3316    768    171   -281       C
ATOM   1610  NE  ARG A 515      12.558 -28.796  19.717  1.00 31.54           N
ANISOU 1610  NE  ARG A 515     4025   3673   4287    741    143   -238       N
ATOM   1611  CZ  ARG A 515      13.497 -28.587  18.795  1.00 34.08           C
ANISOU 1611  CZ  ARG A 515     4271   4098   4580    775    173   -258       C
ATOM   1612  NH1 ARG A 515      14.005 -29.607  18.113  1.00 34.04           N
ANISOU 1612  NH1 ARG A 515     4262   4080   4593    841    236   -346       N
ATOM   1613  NH2 ARG A 515      13.853 -27.348  18.465  1.00 30.88           N
ANISOU 1613  NH2 ARG A 515     3797   3811   4125    737    149   -196       N
ATOM   1614  N   HIS A 516      12.311 -31.160  24.997  1.00 14.61           N
ANISOU 1614  N   HIS A 516     2048   1167   2336    768     40     16       N
ATOM   1615  CA  HIS A 516      12.260 -32.464  25.646  1.00 17.75           C
ANISOU 1615  CA  HIS A 516     2495   1459   2790    791     45     41       C
ATOM   1616  C   HIS A 516      10.826 -32.821  26.075  1.00 18.14           C
ANISOU 1616  C   HIS A 516     2625   1433   2835    719     61     43       C
ATOM   1617  O   HIS A 516      10.334 -33.931  25.799  1.00 16.19           O
ANISOU 1617  O   HIS A 516     2439   1076   2637    707     98      2       O
ATOM   1618  CB  HIS A 516      13.242 -32.432  26.835  1.00 17.31           C
ANISOU 1618  CB  HIS A 516     2407   1439   2730    845     -7    146       C
ATOM   1619  CG  HIS A 516      13.317 -33.712  27.617  1.00 19.51           C
ANISOU 1619  CG  HIS A 516     2737   1619   3057    886     -7    201       C
ATOM   1620  ND1 HIS A 516      14.069 -34.796  27.225  1.00 29.01           N
ANISOU 1620  ND1 HIS A 516     3940   2753   4330    965     15    181       N
ATOM   1621  CD2 HIS A 516      12.648 -34.108  28.727  1.00 24.33           C
ANISOU 1621  CD2 HIS A 516     3410   2179   3654    862    -17    277       C
ATOM   1622  CE1 HIS A 516      13.908 -35.785  28.089  1.00 28.07           C
ANISOU 1622  CE1 HIS A 516     3882   2540   4243    989     12    252       C
ATOM   1623  NE2 HIS A 516      13.055 -35.390  29.016  1.00 25.51           N
ANISOU 1623  NE2 HIS A 516     3596   2231   3867    925     -6    316       N
ATOM   1624  N   MET A 517      10.147 -31.882  26.759  1.00 13.71           N
ANISOU 1624  N   MET A 517     2068    927   2213    672     38     90       N
ATOM   1625  CA  MET A 517       8.772 -32.103  27.221  1.00 15.23           C
ANISOU 1625  CA  MET A 517     2326   1067   2396    609     63    103       C
ATOM   1626  C   MET A 517       7.815 -32.293  26.049  1.00 18.23           C
ANISOU 1626  C   MET A 517     2731   1405   2789    556    113      3       C
ATOM   1627  O   MET A 517       6.911 -33.137  26.099  1.00 16.23           O
ANISOU 1627  O   MET A 517     2537   1057   2574    502    156    -12       O
ATOM   1628  CB  MET A 517       8.279 -30.916  28.052  1.00 15.73           C
ANISOU 1628  CB  MET A 517     2382   1212   2381    585     35    154       C
ATOM   1629  CG  MET A 517       8.993 -30.744  29.316  1.00 17.03           C
ANISOU 1629  CG  MET A 517     2540   1417   2514    623     -8    242       C
ATOM   1630  SD  MET A 517       8.184 -29.512  30.380  1.00 19.33           S
ANISOU 1630  SD  MET A 517     2857   1784   2705    599    -27    280       S
ATOM   1631  CE  MET A 517       8.532 -27.969  29.561  1.00 15.48           C
ANISOU 1631  CE  MET A 517     2314   1382   2186    589    -60    213       C
ATOM   1632  N   SER A 518       7.967 -31.490  24.991  1.00 14.41           N
ANISOU 1632  N   SER A 518     2206    997   2274    561    113    -64       N
ATOM   1633  CA  SER A 518       7.142 -31.702  23.806  1.00 17.04           C
ANISOU 1633  CA  SER A 518     2553   1316   2606    507    159   -172       C
ATOM   1634  C   SER A 518       7.319 -33.113  23.243  1.00 20.40           C
ANISOU 1634  C   SER A 518     3023   1625   3103    505    206   -253       C
ATOM   1635  O   SER A 518       6.319 -33.771  22.911  1.00 16.60           O
ANISOU 1635  O   SER A 518     2582   1073   2651    418    247   -323       O
ATOM   1636  CB  SER A 518       7.460 -30.642  22.746  1.00 19.08           C
ANISOU 1636  CB  SER A 518     2735   1719   2796    509    134   -215       C
ATOM   1637  OG  SER A 518       6.807 -30.912  21.511  1.00 21.65           O
ANISOU 1637  OG  SER A 518     3042   2088   3094    443    157   -324       O
ATOM   1638  N   ASN A 519       8.571 -33.631  23.169  1.00 17.36           N
ANISOU 1638  N   ASN A 519     2620   1229   2748    587    192   -248       N
ATOM   1639  CA  ASN A 519       8.724 -34.980  22.616  1.00 16.34           C
ANISOU 1639  CA  ASN A 519     2541    992   2675    594    229   -330       C
ATOM   1640  C   ASN A 519       8.105 -36.047  23.516  1.00 18.11           C
ANISOU 1640  C   ASN A 519     2842   1078   2963    550    240   -277       C
ATOM   1641  O   ASN A 519       7.500 -36.999  23.028  1.00 18.85           O
ANISOU 1641  O   ASN A 519     2994   1067   3100    488    282   -359       O
ATOM   1642  CB  ASN A 519      10.192 -35.365  22.306  1.00 18.96           C
ANISOU 1642  CB  ASN A 519     2837   1335   3033    707    224   -341       C
ATOM   1643  CG  ASN A 519      10.771 -34.495  21.222  1.00 25.38           C
ANISOU 1643  CG  ASN A 519     3575   2277   3790    740    237   -408       C
ATOM   1644  OD1 ASN A 519      10.274 -34.541  20.137  1.00 29.47           O
ANISOU 1644  OD1 ASN A 519     4112   2816   4268    701    281   -523       O
ATOM   1645  ND2 ASN A 519      11.982 -33.912  21.455  1.00 26.12           N
ANISOU 1645  ND2 ASN A 519     3582   2454   3889    813    215   -341       N
ATOM   1646  N   LYS A 520       8.286 -35.937  24.822  1.00 17.31           N
ANISOU 1646  N   LYS A 520     2737    974   2864    577    205   -142       N
ATOM   1647  CA  LYS A 520       7.612 -36.846  25.753  1.00 19.03           C
ANISOU 1647  CA  LYS A 520     3027   1074   3132    531    225    -69       C
ATOM   1648  C   LYS A 520       6.106 -36.692  25.619  1.00 18.77           C
ANISOU 1648  C   LYS A 520     3021   1019   3092    403    266   -104       C
ATOM   1649  O   LYS A 520       5.368 -37.678  25.618  1.00 23.52           O
ANISOU 1649  O   LYS A 520     3682   1500   3756    322    309   -127       O
ATOM   1650  CB  LYS A 520       8.037 -36.617  27.193  1.00 25.45           C
ANISOU 1650  CB  LYS A 520     3827   1920   3921    581    184     82       C
ATOM   1651  CG  LYS A 520       9.533 -36.870  27.503  1.00 27.73           C
ANISOU 1651  CG  LYS A 520     4080   2228   4228    699    144    131       C
ATOM   1652  CD  LYS A 520       9.735 -38.387  27.281  1.00 36.34           C
ANISOU 1652  CD  LYS A 520     5239   3156   5412    730    180    111       C
ATOM   1653  CE  LYS A 520      11.116 -38.939  27.642  1.00 45.43           C
ANISOU 1653  CE  LYS A 520     6368   4290   6602    857    154    169       C
ATOM   1654  NZ  LYS A 520      11.218 -40.483  27.328  1.00 52.17           N
ANISOU 1654  NZ  LYS A 520     7304   4956   7560    894    200    138       N
ATOM   1655  N   GLY A 521       5.645 -35.471  25.463  1.00 19.06           N
ANISOU 1655  N   GLY A 521     3011   1169   3063    377    256   -114       N
ATOM   1656  CA  GLY A 521       4.211 -35.267  25.333  1.00 19.34           C
ANISOU 1656  CA  GLY A 521     3056   1193   3099    256    301   -151       C
ATOM   1657  C   GLY A 521       3.650 -35.941  24.097  1.00 23.54           C
ANISOU 1657  C   GLY A 521     3599   1673   3672    157    340   -310       C
ATOM   1658  O   GLY A 521       2.601 -36.585  24.159  1.00 26.14           O
ANISOU 1658  O   GLY A 521     3951   1942   4040     30    373   -337       O
ATOM   1659  N  AMET A 522       4.348 -35.819  22.961  0.62 21.65           N
ANISOU 1659  N  AMET A 522     3332   1486   3407    202    329   -419       N
ATOM   1660  N  BMET A 522       4.346 -35.789  22.960  0.38 21.71           N
ANISOU 1660  N  BMET A 522     3339   1497   3414    203    329   -418       N
ATOM   1661  CA AMET A 522       3.854 -36.396  21.723  0.62 25.96           C
ANISOU 1661  CA AMET A 522     3881   2021   3961    106    357   -592       C
ATOM   1662  CA BMET A 522       3.919 -36.388  21.705  0.38 25.95           C
ANISOU 1662  CA BMET A 522     3879   2021   3958    112    356   -592       C
ATOM   1663  C  AMET A 522       3.782 -37.917  21.816  0.62 27.04           C
ANISOU 1663  C  AMET A 522     4098   1995   4180     64    383   -615       C
ATOM   1664  C  BMET A 522       3.787 -37.900  21.834  0.38 27.06           C
ANISOU 1664  C  BMET A 522     4100   1999   4182     66    382   -613       C
ATOM   1665  O  AMET A 522       2.834 -38.528  21.309  0.62 30.80           O
ANISOU 1665  O  AMET A 522     4590   2433   4680    -77    407   -721       O
ATOM   1666  O  BMET A 522       2.804 -38.487  21.367  0.38 30.78           O
ANISOU 1666  O  BMET A 522     4586   2432   4677    -78    406   -714       O
ATOM   1667  CB AMET A 522       4.746 -35.945  20.568  0.62 24.37           C
ANISOU 1667  CB AMET A 522     3634   1929   3697    182    345   -686       C
ATOM   1668  CB BMET A 522       4.925 -36.022  20.610  0.38 24.32           C
ANISOU 1668  CB BMET A 522     3633   1910   3696    200    345   -678       C
ATOM   1669  CG AMET A 522       4.429 -34.548  20.142  0.62 25.32           C
ANISOU 1669  CG AMET A 522     3649   2281   3691    169    285   -660       C
ATOM   1670  CG BMET A 522       4.278 -35.775  19.282  0.38 26.91           C
ANISOU 1670  CG BMET A 522     3905   2380   3939    103    335   -826       C
ATOM   1671  SD AMET A 522       5.305 -34.078  18.645  0.62 34.11           S
ANISOU 1671  SD AMET A 522     4704   3541   4715    227    281   -765       S
ATOM   1672  SD BMET A 522       3.339 -34.239  19.333  0.38 24.83           S
ANISOU 1672  SD BMET A 522     3527   2358   3551     53    263   -738       S
ATOM   1673  CE AMET A 522       4.690 -32.415  18.403  0.62 30.99           C
ANISOU 1673  CE AMET A 522     4200   3382   4191    202    212   -682       C
ATOM   1674  CE BMET A 522       4.574 -33.088  18.733  0.38 28.74           C
ANISOU 1674  CE BMET A 522     3960   2998   3963    183    234   -701       C
ATOM   1675  N   GLU A 523       4.780 -38.544  22.459  1.00 25.96           N
ANISOU 1675  N   GLU A 523     4006   1770   4089    181    373   -521       N
ATOM   1676  CA  GLU A 523       4.713 -39.982  22.732  1.00 30.89           C
ANISOU 1676  CA  GLU A 523     4713   2217   4806    156    400   -518       C
ATOM   1677  C   GLU A 523       3.458 -40.303  23.526  1.00 34.17           C
ANISOU 1677  C   GLU A 523     5156   2562   5265     19    425   -453       C
ATOM   1678  O   GLU A 523       2.734 -41.256  23.235  1.00 30.07           O
ANISOU 1678  O   GLU A 523     4683   1934   4808   -100    457   -525       O
ATOM   1679  CB  GLU A 523       5.931 -40.418  23.566  1.00 27.52           C
ANISOU 1679  CB  GLU A 523     4310   1729   4416    308    378   -394       C
ATOM   1680  CG  GLU A 523       7.235 -40.509  22.884  1.00 33.71           C
ANISOU 1680  CG  GLU A 523     5076   2540   5191    442    365   -451       C
ATOM   1681  CD  GLU A 523       8.229 -41.305  23.748  1.00 47.28           C
ANISOU 1681  CD  GLU A 523     6826   4160   6978    564    352   -340       C
ATOM   1682  OE1 GLU A 523       8.968 -40.701  24.574  1.00 40.38           O
ANISOU 1682  OE1 GLU A 523     5896   3372   6073    651    308   -218       O
ATOM   1683  OE2 GLU A 523       8.251 -42.548  23.602  1.00 40.39           O
ANISOU 1683  OE2 GLU A 523     6033   3123   6192    566    385   -378       O
ATOM   1684  N   HIS A 524       3.212 -39.520  24.572  1.00 26.93           N
ANISOU 1684  N   HIS A 524     4208   1710   4314     33    413   -315       N
ATOM   1685  CA  HIS A 524       2.052 -39.751  25.408  1.00 34.32           C
ANISOU 1685  CA  HIS A 524     5162   2598   5281    -90    448   -235       C
ATOM   1686  C   HIS A 524       0.775 -39.589  24.593  1.00 34.58           C
ANISOU 1686  C   HIS A 524     5154   2675   5310   -270    474   -369       C
ATOM   1687  O   HIS A 524      -0.079 -40.480  24.583  1.00 36.25           O
ANISOU 1687  O   HIS A 524     5393   2798   5583   -412    507   -399       O
ATOM   1688  CB  HIS A 524       2.118 -38.787  26.599  1.00 35.39           C
ANISOU 1688  CB  HIS A 524     5267   2825   5354    -22    431    -75       C
ATOM   1689  CG  HIS A 524       0.974 -38.889  27.550  1.00 38.37           C
ANISOU 1689  CG  HIS A 524     5654   3180   5743   -133    476     27       C
ATOM   1690  ND1 HIS A 524       0.319 -37.767  28.015  1.00 34.33           N
ANISOU 1690  ND1 HIS A 524     5089   2795   5159   -156    483     80       N
ATOM   1691  CD2 HIS A 524       0.344 -39.955  28.101  1.00 40.62           C
ANISOU 1691  CD2 HIS A 524     5990   3349   6097   -229    519     88       C
ATOM   1692  CE1 HIS A 524      -0.647 -38.138  28.840  1.00 44.50           C
ANISOU 1692  CE1 HIS A 524     6383   4066   6460   -258    530    174       C
ATOM   1693  NE2 HIS A 524      -0.658 -39.459  28.905  1.00 42.20           N
ANISOU 1693  NE2 HIS A 524     6159   3613   6262   -312    558    184       N
ATOM   1694  N   LEU A 525       0.685 -38.501  23.816  1.00 24.19           N
ANISOU 1694  N   LEU A 525     3767   1506   3921   -271    454   -461       N
ATOM   1695  CA  LEU A 525      -0.526 -38.228  23.046  1.00 30.58           C
ANISOU 1695  CA  LEU A 525     4490   2453   4677   -432    438   -573       C
ATOM   1696  C   LEU A 525      -0.768 -39.317  22.010  1.00 40.18           C
ANISOU 1696  C   LEU A 525     5746   3571   5949   -551    462   -754       C
ATOM   1697  O   LEU A 525      -1.922 -39.717  21.775  1.00 39.25           O
ANISOU 1697  O   LEU A 525     5594   3475   5845   -735    471   -821       O
ATOM   1698  CB  LEU A 525      -0.404 -36.869  22.361  1.00 28.87           C
ANISOU 1698  CB  LEU A 525     4163   2485   4322   -364    369   -599       C
ATOM   1699  CG  LEU A 525      -0.528 -35.649  23.263  1.00 28.22           C
ANISOU 1699  CG  LEU A 525     4018   2539   4164   -284    335   -446       C
ATOM   1700  CD1 LEU A 525      -0.437 -34.332  22.436  1.00 26.63           C
ANISOU 1700  CD1 LEU A 525     3718   2556   3846   -226    273   -477       C
ATOM   1701  CD2 LEU A 525      -1.808 -35.686  24.115  1.00 24.95           C
ANISOU 1701  CD2 LEU A 525     3565   2163   3753   -392    357   -366       C
ATOM   1702  N   TYR A 526       0.307 -39.824  21.393  1.00 34.37           N
ANISOU 1702  N   TYR A 526     5062   2778   5219   -438    453   -813       N
ATOM   1703  CA  TYR A 526       0.148 -40.928  20.452  1.00 40.17           C
ANISOU 1703  CA  TYR A 526     5838   3442   5983   -521    461   -965       C
ATOM   1704  C   TYR A 526      -0.320 -42.211  21.142  1.00 44.52           C
ANISOU 1704  C   TYR A 526     6469   3796   6649   -604    495   -909       C
ATOM   1705  O   TYR A 526      -1.038 -43.000  20.522  1.00 47.76           O
ANISOU 1705  O   TYR A 526     6893   4167   7088   -751    502  -1032       O
ATOM   1706  CB  TYR A 526       1.445 -41.184  19.695  1.00 33.15           C
ANISOU 1706  CB  TYR A 526     4988   2531   5075   -370    456  -1035       C
ATOM   1707  CG  TYR A 526       1.345 -42.276  18.647  1.00 45.92           C
ANISOU 1707  CG  TYR A 526     6657   4079   6713   -441    469  -1208       C
ATOM   1708  CD1 TYR A 526       0.894 -41.978  17.364  1.00 52.12           C
ANISOU 1708  CD1 TYR A 526     7381   5026   7397   -532    449  -1383       C
ATOM   1709  CD2 TYR A 526       1.725 -43.593  18.924  1.00 48.18           C
ANISOU 1709  CD2 TYR A 526     7051   4146   7110   -411    499  -1198       C
ATOM   1710  CE1 TYR A 526       0.814 -42.960  16.386  1.00 50.65           C
ANISOU 1710  CE1 TYR A 526     7244   4787   7215   -596    459  -1550       C
ATOM   1711  CE2 TYR A 526       1.644 -44.589  17.948  1.00 53.96           C
ANISOU 1711  CE2 TYR A 526     7840   4798   7863   -473    514  -1371       C
ATOM   1712  CZ  TYR A 526       1.191 -44.268  16.681  1.00 56.79           C
ANISOU 1712  CZ  TYR A 526     8140   5322   8115   -567    495  -1550       C
ATOM   1713  OH  TYR A 526       1.111 -45.261  15.715  1.00 60.01           O
ANISOU 1713  OH  TYR A 526     8609   5659   8535   -630    509  -1728       O
ATOM   1714  N   SER A 527       0.047 -42.443  22.414  1.00 46.11           N
ANISOU 1714  N   SER A 527     6722   3887   6912   -520    512   -725       N
ATOM   1715  CA  SER A 527      -0.443 -43.648  23.095  1.00 44.98           C
ANISOU 1715  CA  SER A 527     6653   3562   6877   -607    546   -657       C
ATOM   1716  C   SER A 527      -1.960 -43.646  23.293  1.00 58.88           C
ANISOU 1716  C   SER A 527     8359   5368   8646   -825    565   -661       C
ATOM   1717  O   SER A 527      -2.527 -44.694  23.634  1.00 56.49           O
ANISOU 1717  O   SER A 527     8108   4924   8432   -936    593   -635       O
ATOM   1718  CB  SER A 527       0.202 -43.824  24.470  1.00 44.63           C
ANISOU 1718  CB  SER A 527     6659   3427   6871   -477    554   -444       C
ATOM   1719  OG  SER A 527      -0.204 -42.793  25.361  1.00 41.82           O
ANISOU 1719  OG  SER A 527     6241   3195   6454   -477    553   -313       O
ATOM   1720  N   MET A 528      -2.620 -42.498  23.125  1.00 51.30           N
ANISOU 1720  N   MET A 528     7289   4604   7598   -888    550   -684       N
ATOM   1721  CA  MET A 528      -4.076 -42.418  23.224  1.00 48.93           C
ANISOU 1721  CA  MET A 528     6905   4395   7293  -1099    561   -697       C
ATOM   1722  C   MET A 528      -4.707 -41.823  21.959  1.00 48.91           C
ANISOU 1722  C   MET A 528     6788   4599   7197  -1209    516   -883       C
ATOM   1723  O   MET A 528      -5.628 -41.005  22.038  1.00 53.72           O
ANISOU 1723  O   MET A 528     7273   5394   7744  -1309    503   -872       O
ATOM   1724  CB  MET A 528      -4.462 -41.623  24.489  1.00 41.58           C
ANISOU 1724  CB  MET A 528     5928   3530   6340  -1085    591   -509       C
ATOM   1725  CG  MET A 528      -3.939 -40.212  24.608  1.00 42.50           C
ANISOU 1725  CG  MET A 528     5994   3789   6365   -946    567   -468       C
ATOM   1726  SD  MET A 528      -3.917 -39.795  26.354  1.00 74.65           S
ANISOU 1726  SD  MET A 528    10079   7870  10416   -847    597   -208       S
ATOM   1727  CE  MET A 528      -2.709 -38.495  26.338  1.00 47.40           C
ANISOU 1727  CE  MET A 528     6606   4552   6852   -604    527   -176       C
ATOM   1728  N   LEU A 536      -2.485 -33.611  10.560  1.00 46.79           N
ANISOU 1728  N   LEU A 536     5710   6648   5420   -698    -25  -1567       N
ATOM   1729  CA  LEU A 536      -2.260 -32.287  11.167  1.00 33.84           C
ANISOU 1729  CA  LEU A 536     4025   5052   3783   -552    -43  -1333       C
ATOM   1730  C   LEU A 536      -1.704 -31.334  10.071  1.00 37.90           C
ANISOU 1730  C   LEU A 536     4479   5790   4133   -457    -71  -1287       C
ATOM   1731  O   LEU A 536      -2.079 -30.150  10.002  1.00 37.71           O
ANISOU 1731  O   LEU A 536     4363   5928   4039   -392   -119  -1125       O
ATOM   1732  CB  LEU A 536      -1.308 -32.363  12.385  1.00 36.34           C
ANISOU 1732  CB  LEU A 536     4452   5095   4259   -443     19  -1237       C
ATOM   1733  CG  LEU A 536      -1.017 -31.008  13.033  1.00 35.35           C
ANISOU 1733  CG  LEU A 536     4293   5000   4139   -307      2  -1022       C
ATOM   1734  CD1 LEU A 536      -2.310 -30.305  13.413  1.00 39.15           C
ANISOU 1734  CD1 LEU A 536     4671   5609   4596   -340    -48   -915       C
ATOM   1735  CD2 LEU A 536      -0.006 -31.023  14.234  1.00 31.70           C
ANISOU 1735  CD2 LEU A 536     3931   4302   3813   -203     51   -931       C
ATOM   1736  N   SER A 537      -0.861 -31.881   9.208  1.00 40.10           N
ANISOU 1736  N   SER A 537     4811   6072   4352   -447    -34  -1429       N
ATOM   1737  CA  SER A 537      -0.319 -31.128   8.051  1.00 41.83           C
ANISOU 1737  CA  SER A 537     4971   6524   4397   -379    -50  -1402       C
ATOM   1738  C   SER A 537      -1.456 -30.491   7.257  1.00 38.64           C
ANISOU 1738  C   SER A 537     4430   6428   3825   -438   -138  -1360       C
ATOM   1739  O   SER A 537      -1.383 -29.317   6.999  1.00 35.07           O
ANISOU 1739  O   SER A 537     3904   6136   3286   -345   -171  -1181       O
ATOM   1740  CB  SER A 537       0.433 -32.048   7.156  1.00 39.05           C
ANISOU 1740  CB  SER A 537     4686   6153   4000   -391      6  -1591       C
ATOM   1741  OG  SER A 537       1.799 -32.025   7.465  1.00 62.57           O
ANISOU 1741  OG  SER A 537     7758   8934   7081   -281     84  -1594       O
ATOM   1742  N   ASP A 538      -2.479 -31.271   6.906  1.00 40.21           N
ANISOU 1742  N   ASP A 538     4590   6679   4007   -580   -169  -1481       N
ATOM   1743  CA  ASP A 538      -3.562 -30.729   6.082  1.00 37.59           C
ANISOU 1743  CA  ASP A 538     4117   6626   3541   -620   -243  -1411       C
ATOM   1744  C   ASP A 538      -4.378 -29.706   6.858  1.00 35.91           C
ANISOU 1744  C   ASP A 538     3808   6495   3342   -578   -300  -1226       C
ATOM   1745  O   ASP A 538      -4.784 -28.674   6.304  1.00 35.13           O
ANISOU 1745  O   ASP A 538     3603   6606   3137   -506   -346  -1068       O
ATOM   1746  CB  ASP A 538      -4.454 -31.852   5.551  1.00 49.90           C
ANISOU 1746  CB  ASP A 538     5656   8208   5095   -783   -255  -1577       C
ATOM   1747  N   LEU A 539      -4.612 -29.964   8.151  1.00 33.44           N
ANISOU 1747  N   LEU A 539     3536   5987   3182   -604   -284  -1216       N
ATOM   1748  CA  LEU A 539      -5.354 -29.015   8.970  1.00 36.10           C
ANISOU 1748  CA  LEU A 539     3793   6348   3576   -535   -311  -1013       C
ATOM   1749  C   LEU A 539      -4.636 -27.670   9.065  1.00 33.51           C
ANISOU 1749  C   LEU A 539     3474   6020   3238   -350   -302   -806       C
ATOM   1750  O   LEU A 539      -5.278 -26.612   9.003  1.00 33.10           O
ANISOU 1750  O   LEU A 539     3320   6120   3136   -275   -347   -642       O
ATOM   1751  CB  LEU A 539      -5.586 -29.615  10.363  1.00 32.11           C
ANISOU 1751  CB  LEU A 539     3356   5581   3263   -579   -262  -1017       C
ATOM   1752  CG  LEU A 539      -6.372 -28.789  11.360  1.00 40.64           C
ANISOU 1752  CG  LEU A 539     4366   6663   4412   -515   -272   -838       C
ATOM   1753  CD1 LEU A 539      -7.806 -28.532  10.858  1.00 41.54           C
ANISOU 1753  CD1 LEU A 539     4297   7063   4423   -585   -348   -818       C
ATOM   1754  CD2 LEU A 539      -6.361 -29.431  12.767  1.00 42.35           C
ANISOU 1754  CD2 LEU A 539     4674   6611   4806   -549   -208   -840       C
ATOM   1755  N   LEU A 540      -3.299 -27.683   9.248  1.00 35.10           N
ANISOU 1755  N   LEU A 540     3796   6043   3499   -274   -240   -806       N
ATOM   1756  CA  LEU A 540      -2.536 -26.426   9.332  1.00 27.63           C
ANISOU 1756  CA  LEU A 540     2862   5083   2554   -123   -227   -618       C
ATOM   1757  C   LEU A 540      -2.574 -25.662   8.006  1.00 31.69           C
ANISOU 1757  C   LEU A 540     3287   5874   2880    -84   -271   -547       C
ATOM   1758  O   LEU A 540      -2.773 -24.434   7.981  1.00 28.59           O
ANISOU 1758  O   LEU A 540     2840   5558   2463     16   -295   -352       O
ATOM   1759  CB  LEU A 540      -1.056 -26.726   9.721  1.00 27.69           C
ANISOU 1759  CB  LEU A 540     2997   4871   2654    -70   -155   -651       C
ATOM   1760  CG  LEU A 540      -0.832 -27.315  11.103  1.00 21.26           C
ANISOU 1760  CG  LEU A 540     2276   3782   2020    -75   -111   -674       C
ATOM   1761  CD1 LEU A 540       0.645 -27.737  11.298  1.00 24.40           C
ANISOU 1761  CD1 LEU A 540     2778   4007   2487    -22    -48   -719       C
ATOM   1762  CD2 LEU A 540      -1.220 -26.263  12.132  1.00 23.34           C
ANISOU 1762  CD2 LEU A 540     2522   3985   2361      2   -124   -496       C
ATOM   1763  N   LEU A 541      -2.376 -26.373   6.898  1.00 30.01           N
ANISOU 1763  N   LEU A 541     3064   5810   2530   -159   -277   -702       N
ATOM   1764  CA  LEU A 541      -2.513 -25.747   5.580  1.00 36.07           C
ANISOU 1764  CA  LEU A 541     3742   6839   3122   -131   -309   -627       C
ATOM   1765  C   LEU A 541      -3.869 -25.061   5.449  1.00 49.62           C
ANISOU 1765  C   LEU A 541     5335   8706   4814   -121   -368   -490       C
ATOM   1766  O   LEU A 541      -3.955 -23.881   5.072  1.00 40.88           O
ANISOU 1766  O   LEU A 541     4175   7686   3669    -17   -376   -289       O
ATOM   1767  CB  LEU A 541      -2.315 -26.787   4.472  1.00 38.34           C
ANISOU 1767  CB  LEU A 541     4041   7198   3327   -226   -286   -822       C
ATOM   1768  N   GLU A 542      -4.945 -25.767   5.808  1.00 39.05           N
ANISOU 1768  N   GLU A 542     3949   7378   3511   -225   -399   -589       N
ATOM   1769  CA  GLU A 542      -6.271 -25.174   5.664  1.00 39.43           C
ANISOU 1769  CA  GLU A 542     3870   7581   3532   -211   -445   -467       C
ATOM   1770  C   GLU A 542      -6.371 -23.863   6.431  1.00 39.57           C
ANISOU 1770  C   GLU A 542     3873   7537   3625    -59   -444   -237       C
ATOM   1771  O   GLU A 542      -6.848 -22.852   5.903  1.00 40.62           O
ANISOU 1771  O   GLU A 542     3937   7784   3711     31   -453    -68       O
ATOM   1772  CB  GLU A 542      -7.336 -26.180   6.108  1.00 38.89           C
ANISOU 1772  CB  GLU A 542     3757   7510   3510   -356   -467   -609       C
ATOM   1773  CG  GLU A 542      -8.744 -25.715   5.966  1.00 48.53           C
ANISOU 1773  CG  GLU A 542     4840   8902   4698   -351   -508   -505       C
ATOM   1774  CD  GLU A 542      -9.204 -25.746   4.542  1.00 56.21           C
ANISOU 1774  CD  GLU A 542     5729  10112   5515   -389   -534   -524       C
ATOM   1775  OE1 GLU A 542      -8.870 -26.711   3.827  1.00 53.08           O
ANISOU 1775  OE1 GLU A 542     5369   9741   5058   -501   -529   -708       O
ATOM   1776  OE2 GLU A 542      -9.930 -24.817   4.146  1.00 65.22           O
ANISOU 1776  OE2 GLU A 542     6770  11412   6597   -303   -558   -360       O
ATOM   1777  N   MET A 543      -5.900 -23.842   7.673  1.00 33.40           N
ANISOU 1777  N   MET A 543     3164   6560   2968    -24   -428   -228       N
ATOM   1778  CA  MET A 543      -6.065 -22.624   8.448  1.00 26.83           C
ANISOU 1778  CA  MET A 543     2324   5645   2226    120   -420    -22       C
ATOM   1779  C   MET A 543      -5.092 -21.546   7.989  1.00 33.45           C
ANISOU 1779  C   MET A 543     3219   6443   3046    240   -389    131       C
ATOM   1780  O   MET A 543      -5.390 -20.341   8.079  1.00 33.11           O
ANISOU 1780  O   MET A 543     3162   6371   3048    355   -374    315       O
ATOM   1781  CB  MET A 543      -5.810 -22.915   9.946  1.00 29.28           C
ANISOU 1781  CB  MET A 543     2728   5681   2718    121   -371    -56       C
ATOM   1782  CG  MET A 543      -6.932 -23.600  10.666  1.00 40.94           C
ANISOU 1782  CG  MET A 543     4143   7159   4254     33   -380   -131       C
ATOM   1783  SD  MET A 543      -6.386 -23.967  12.352  1.00 58.83           S
ANISOU 1783  SD  MET A 543     6554   9074   6723     39   -296   -158       S
ATOM   1784  CE  MET A 543      -5.704 -25.613  12.117  1.00 28.32           C
ANISOU 1784  CE  MET A 543     2787   5102   2871   -121   -270   -386       C
ATOM   1785  N   LEU A 544      -3.891 -21.968   7.587  1.00 30.95           N
ANISOU 1785  N   LEU A 544     2978   6099   2682    212   -368     50       N
ATOM   1786  CA  LEU A 544      -2.848 -21.033   7.171  1.00 30.50           C
ANISOU 1786  CA  LEU A 544     2973   6002   2615    303   -330    189       C
ATOM   1787  C   LEU A 544      -3.114 -20.503   5.766  1.00 36.04           C
ANISOU 1787  C   LEU A 544     3601   6894   3197    315   -329    273       C
ATOM   1788  O   LEU A 544      -2.840 -19.331   5.486  1.00 37.13           O
ANISOU 1788  O   LEU A 544     3744   7009   3354    406   -305    456       O
ATOM   1789  CB  LEU A 544      -1.476 -21.724   7.200  1.00 28.86           C
ANISOU 1789  CB  LEU A 544     2868   5673   2424    263   -276     66       C
ATOM   1790  CG  LEU A 544      -0.815 -21.908   8.544  1.00 31.27           C
ANISOU 1790  CG  LEU A 544     3283   5672   2925    276   -222     35       C
ATOM   1791  CD1 LEU A 544       0.324 -22.963   8.447  1.00 26.96           C
ANISOU 1791  CD1 LEU A 544     2817   5031   2394    221   -169   -133       C
ATOM   1792  CD2 LEU A 544      -0.305 -20.540   9.007  1.00 24.27           C
ANISOU 1792  CD2 LEU A 544     2431   4668   2123    384   -201    235       C
ATOM   1793  N   ASP A 545      -3.669 -21.355   4.889  1.00 32.02           N
ANISOU 1793  N   ASP A 545     3026   6567   2572    218   -356    136       N
ATOM   1794  CA  ASP A 545      -3.862 -21.038   3.472  1.00 33.53           C
ANISOU 1794  CA  ASP A 545     3142   6971   2628    218   -361    189       C
ATOM   1795  C   ASP A 545      -5.176 -20.290   3.327  1.00 36.69           C
ANISOU 1795  C   ASP A 545     3442   7476   3021    268   -393    325       C
ATOM   1796  O   ASP A 545      -6.179 -20.798   2.843  1.00 32.78           O
ANISOU 1796  O   ASP A 545     2856   7150   2447    200   -432    252       O
ATOM   1797  CB  ASP A 545      -3.809 -22.305   2.625  1.00 32.40           C
ANISOU 1797  CB  ASP A 545     2982   6960   2370     93   -370    -33       C
ATOM   1798  CG  ASP A 545      -3.894 -22.024   1.111  1.00 31.99           C
ANISOU 1798  CG  ASP A 545     2850   7143   2160     93   -377     12       C
ATOM   1799  OD1 ASP A 545      -3.585 -20.867   0.694  1.00 30.11           O
ANISOU 1799  OD1 ASP A 545     2595   6939   1906    192   -359    215       O
ATOM   1800  OD2 ASP A 545      -4.203 -23.013   0.369  1.00 31.30           O
ANISOU 1800  OD2 ASP A 545     2727   7191   1973    -13   -395   -168       O
ATOM   1801  N   ALA A 546      -5.162 -19.057   3.789  1.00 34.90           N
ANISOU 1801  N   ALA A 546     3237   7137   2886    387   -371    523       N
ATOM   1802  CA  ALA A 546      -6.404 -18.323   3.667  1.00 36.21           C
ANISOU 1802  CA  ALA A 546     3315   7393   3051    449   -391    650       C
ATOM   1803  C   ALA A 546      -6.528 -17.719   2.274  1.00 45.59           C
ANISOU 1803  C   ALA A 546     4429   8784   4110    481   -396    763       C
ATOM   1804  O   ALA A 546      -5.542 -17.587   1.541  1.00 39.88           O
ANISOU 1804  O   ALA A 546     3737   8090   3326    478   -372    784       O
ATOM   1805  CB  ALA A 546      -6.491 -17.237   4.738  1.00 32.27           C
ANISOU 1805  CB  ALA A 546     2872   6676   2712    567   -361    800       C
ATOM   1806  N   HIS A 547      -7.776 -17.398   1.883  1.00 36.54           N
ANISOU 1806  N   HIS A 547     3174   7800   2910    508   -428    833       N
ATOM   1807  CA  HIS A 547      -7.951 -16.577   0.692  1.00 39.75           C
ANISOU 1807  CA  HIS A 547     3509   8381   3211    570   -431    987       C
ATOM   1808  C   HIS A 547      -7.824 -15.099   1.082  1.00 45.16           C
ANISOU 1808  C   HIS A 547     4243   8897   4017    715   -391   1211       C
ATOM   1809  O   HIS A 547      -7.656 -14.753   2.260  1.00 37.87           O
ANISOU 1809  O   HIS A 547     3405   7731   3251    761   -362   1229       O
ATOM   1810  CB  HIS A 547      -9.272 -16.913   0.004  1.00 36.46           C
ANISOU 1810  CB  HIS A 547     2949   8234   2669    533   -487    962       C
ATOM   1811  CG  HIS A 547     -10.464 -16.767   0.906  1.00 49.97           C
ANISOU 1811  CG  HIS A 547     4614   9908   4466    570   -504    987       C
ATOM   1812  ND1 HIS A 547     -10.703 -15.631   1.654  1.00 48.98           N
ANISOU 1812  ND1 HIS A 547     4523   9614   4474    707   -471   1154       N
ATOM   1813  CD2 HIS A 547     -11.495 -17.607   1.164  1.00 47.61           C
ANISOU 1813  CD2 HIS A 547     4233   9719   4138    485   -546    864       C
ATOM   1814  CE1 HIS A 547     -11.812 -15.791   2.354  1.00 47.98           C
ANISOU 1814  CE1 HIS A 547     4336   9502   4393    714   -491   1131       C
ATOM   1815  NE2 HIS A 547     -12.321 -16.975   2.062  1.00 44.76           N
ANISOU 1815  NE2 HIS A 547     3850   9269   3886    578   -537    964       N
ATOM   1816  N   ARG A 548      -7.836 -14.224   0.075  1.00 41.54           N
ANISOU 1816  N   ARG A 548     3739   8558   3486    782   -385   1376       N
ATOM   1817  CA  ARG A 548      -7.697 -12.792   0.299  1.00 42.80           C
ANISOU 1817  CA  ARG A 548     3949   8555   3759    912   -345   1589       C
ATOM   1818  C   ARG A 548      -9.031 -12.087   0.267  1.00 49.78           C
ANISOU 1818  C   ARG A 548     4745   9521   4648   1010   -364   1715       C
ATOM   1819  O   ARG A 548      -9.074 -10.874   0.029  1.00 57.22           O
ANISOU 1819  O   ARG A 548     5699  10406   5638   1123   -339   1908       O
ATOM   1820  CB  ARG A 548      -6.754 -12.175  -0.735  1.00 48.64           C
ANISOU 1820  CB  ARG A 548     4705   9343   4434    930   -318   1713       C
ATOM   1821  N   LEU A 549     -10.126 -12.825   0.477  1.00 45.28           N
ANISOU 1821  N   LEU A 549     4083   9090   4030    970   -409   1611       N
ATOM   1822  CA  LEU A 549     -11.455 -12.326   0.116  1.00 50.40           C
ANISOU 1822  CA  LEU A 549     4608   9915   4628   1049   -439   1724       C
ATOM   1823  C   LEU A 549     -12.080 -11.531   1.249  1.00 60.18           C
ANISOU 1823  C   LEU A 549     5880  10952   6032   1166   -410   1806       C
ATOM   1824  O   LEU A 549     -12.103 -10.304   1.176  1.00 55.90           O
ANISOU 1824  O   LEU A 549     5366  10315   5559   1296   -379   1987       O
ATOM   1825  CB  LEU A 549     -12.389 -13.472  -0.319  1.00 47.13           C
ANISOU 1825  CB  LEU A 549     4060   9779   4067    940   -503   1580       C
ATOM   1826  CG  LEU A 549     -12.059 -14.108  -1.678  1.00 43.28           C
ANISOU 1826  CG  LEU A 549     3507   9551   3385    842   -537   1515       C
ATOM   1827  CD1 LEU A 549     -12.998 -15.272  -1.956  1.00 44.37           C
ANISOU 1827  CD1 LEU A 549     3527   9928   3402    716   -600   1344       C
ATOM   1828  CD2 LEU A 549     -12.050 -13.065  -2.824  1.00 45.75           C
ANISOU 1828  CD2 LEU A 549     3764  10012   3608    943   -535   1730       C
TER    1829      LEU A 549
HETATM 1830  C1  RAL A 601      -3.501 -28.347  26.415  1.00 14.32           C
HETATM 1831  C2  RAL A 601      -3.569 -26.991  26.273  1.00 17.07           C
HETATM 1832  C3  RAL A 601      -2.475 -26.192  26.587  1.00 15.01           C
HETATM 1833  O3  RAL A 601      -2.602 -24.851  26.454  1.00 15.20           O
HETATM 1834  C4  RAL A 601      -1.298 -26.762  27.025  1.00 14.37           C
HETATM 1835  C5  RAL A 601      -1.219 -28.140  27.137  1.00 11.59           C
HETATM 1836  S6  RAL A 601       0.143 -29.081  27.660  1.00 16.96           S
HETATM 1837  C7  RAL A 601      -0.732 -30.565  27.496  1.00 16.07           C
HETATM 1838  C8  RAL A 601      -0.102 -31.848  27.852  1.00 27.02           C
HETATM 1839  C9  RAL A 601       0.545 -32.016  29.063  1.00 28.33           C
HETATM 1840  C10 RAL A 601       1.084 -33.234  29.433  1.00 30.53           C
HETATM 1841  C11 RAL A 601       0.979 -34.324  28.587  1.00 36.09           C
HETATM 1842  O11 RAL A 601       1.504 -35.520  28.952  1.00 48.24           O
HETATM 1843  C12 RAL A 601       0.342 -34.179  27.372  1.00 29.05           C
HETATM 1844  C13 RAL A 601      -0.216 -32.958  27.028  1.00 30.43           C
HETATM 1845  C14 RAL A 601      -2.321 -28.948  26.842  1.00 13.28           C
HETATM 1846  C15 RAL A 601      -1.991 -30.354  27.038  1.00 14.49           C
HETATM 1847  C16 RAL A 601      -2.891 -31.455  26.680  1.00 16.58           C
HETATM 1848  O16 RAL A 601      -3.389 -32.098  27.552  1.00 22.27           O
HETATM 1849  C17 RAL A 601      -3.171 -31.819  25.260  1.00 16.68           C
HETATM 1850  C18 RAL A 601      -4.214 -32.634  24.866  1.00 18.41           C
HETATM 1851  C19 RAL A 601      -4.449 -32.908  23.534  1.00 20.81           C
HETATM 1852  C20 RAL A 601      -3.626 -32.386  22.560  1.00 22.00           C
HETATM 1853  C21 RAL A 601      -2.580 -31.577  22.941  1.00 21.27           C
HETATM 1854  C22 RAL A 601      -2.382 -31.284  24.265  1.00 18.81           C
HETATM 1855  O23 RAL A 601      -3.793 -32.677  21.240  1.00 25.07           O
HETATM 1856  C24 RAL A 601      -5.129 -32.804  20.784  1.00 27.57           C
HETATM 1857  C25 RAL A 601      -5.099 -33.191  19.342  1.00 36.36           C
HETATM 1858  N26 RAL A 601      -5.085 -32.025  18.478  1.00 36.98           N
HETATM 1859  C27 RAL A 601      -4.692 -32.408  17.135  1.00 49.29           C
HETATM 1860  C28 RAL A 601      -4.642 -31.221  16.215  1.00 43.02           C
HETATM 1861  C29 RAL A 601      -3.681 -30.201  16.773  1.00 46.33           C
HETATM 1862  C30 RAL A 601      -4.117 -29.813  18.162  1.00 36.98           C
HETATM 1863  C31 RAL A 601      -4.176 -31.033  19.019  1.00 34.48           C
HETATM 1864  O   HOH A 701       0.769 -30.159  41.976  1.00 38.22           O
HETATM 1865  O   HOH A 702       4.681 -30.014   7.640  1.00 41.97           O
HETATM 1866  O   HOH A 703     -11.412 -25.419   2.481  1.00 36.81           O
HETATM 1867  O   HOH A 704      13.248  -9.608  38.931  1.00 45.47           O
HETATM 1868  O   HOH A 705      22.264 -13.829   5.911  1.00 58.87           O
HETATM 1869  O   HOH A 706      -0.020  -8.607  24.830  1.00 35.74           O
HETATM 1870  O   HOH A 707     -11.530 -30.638  19.741  1.00 33.72           O
HETATM 1871  O   HOH A 708      -6.555 -18.925  12.660  1.00 31.01           O
HETATM 1872  O   HOH A 709      -2.776 -12.930  17.419  1.00 26.20           O
HETATM 1873  O   HOH A 710     -14.885 -17.247  34.093  1.00 27.58           O
HETATM 1874  O   HOH A 711      -3.160 -13.097  12.230  1.00 29.33           O
HETATM 1875  O   HOH A 712      10.472 -38.934  23.613  1.00 37.70           O
HETATM 1876  O   HOH A 713      -4.824 -39.098  41.402  1.00 47.18           O
HETATM 1877  O   HOH A 714       9.643 -29.796  18.347  1.00 28.56           O
HETATM 1878  O   HOH A 715     -13.751 -26.375  34.696  1.00 30.67           O
HETATM 1879  O   HOH A 716     -15.478 -29.250  26.004  1.00 41.29           O
HETATM 1880  O   HOH A 717      12.932 -26.005  21.581  1.00 25.46           O
HETATM 1881  O   HOH A 718      -3.059 -20.210  23.462  1.00 23.32           O
HETATM 1882  O   HOH A 719      21.523 -11.616  11.097  1.00 29.25           O
HETATM 1883  O   HOH A 720     -11.941 -37.483  28.878  1.00 33.15           O
HETATM 1884  O   HOH A 721      20.912 -15.213  17.069  1.00 22.37           O
HETATM 1885  O   HOH A 722       5.945 -31.910  40.879  1.00 28.23           O
HETATM 1886  O   HOH A 723     -14.597 -27.210  32.149  1.00 29.77           O
HETATM 1887  O   HOH A 724      -0.076 -11.367   9.024  1.00 35.51           O
HETATM 1888  O   HOH A 725       9.324 -24.752  14.338  1.00 15.93           O
HETATM 1889  O   HOH A 726       1.634  -7.562  15.930  1.00 32.49           O
HETATM 1890  O   HOH A 727      -4.934 -11.496  19.843  1.00 38.10           O
HETATM 1891  O   HOH A 728     -15.136 -20.063  37.041  1.00 37.96           O
HETATM 1892  O   HOH A 729      19.092 -23.916   9.735  1.00 39.80           O
HETATM 1893  O   HOH A 730       3.485 -12.863  20.948  1.00 21.23           O
HETATM 1894  O   HOH A 731      18.537 -22.079  32.327  1.00 27.03           O
HETATM 1895  O   HOH A 732     -12.318 -33.219  23.324  1.00 28.83           O
HETATM 1896  O   HOH A 733      20.117  -5.299  21.232  1.00 38.85           O
HETATM 1897  O   HOH A 734      -8.781 -33.540  18.475  1.00 36.76           O
HETATM 1898  O   HOH A 735       7.446  -9.823  37.840  1.00 39.26           O
HETATM 1899  O   HOH A 736      -8.103 -26.712  15.791  1.00 31.20           O
HETATM 1900  O   HOH A 737      21.642  -2.295  31.781  1.00 39.38           O
HETATM 1901  O   HOH A 738      18.371 -24.735  23.731  1.00 23.83           O
HETATM 1902  O   HOH A 739      19.249 -23.662  15.677  1.00 33.36           O
HETATM 1903  O   HOH A 740      21.977 -12.622  34.481  1.00 28.44           O
HETATM 1904  O   HOH A 741       1.120 -17.843  20.804  1.00 19.60           O
HETATM 1905  O   HOH A 742       2.401 -15.703   3.221  1.00 40.59           O
HETATM 1906  O   HOH A 743      11.370 -24.088   0.211  1.00 44.04           O
HETATM 1907  O   HOH A 744       7.185  -3.555  27.124  1.00 44.29           O
HETATM 1908  O   HOH A 745       5.191 -24.517  40.165  1.00 21.58           O
HETATM 1909  O   HOH A 746       5.941 -39.891  27.064  1.00 34.10           O
HETATM 1910  O   HOH A 747       4.271 -12.557   9.799  1.00 22.67           O
HETATM 1911  O   HOH A 748      20.465 -20.908   3.983  1.00 36.37           O
HETATM 1912  O   HOH A 749       4.889 -28.453   5.092  1.00 34.10           O
HETATM 1913  O   HOH A 750      -0.266 -17.693   6.245  1.00 36.56           O
HETATM 1914  O   HOH A 751      17.234 -16.206  18.365  1.00 22.78           O
HETATM 1915  O   HOH A 752      18.423  -5.184  16.007  1.00 42.79           O
HETATM 1916  O   HOH A 753      -6.110 -20.975  28.833  1.00 20.01           O
HETATM 1917  O   HOH A 754       8.561 -24.404   0.453  1.00 31.01           O
HETATM 1918  O   HOH A 755      -1.155 -22.479  25.625  1.00 15.71           O
HETATM 1919  O   HOH A 756       9.034 -14.341  40.605  1.00 42.20           O
HETATM 1920  O   HOH A 757       5.678  -2.911  15.852  1.00 35.09           O
HETATM 1921  O   HOH A 758      10.020 -31.440  14.793  1.00 37.39           O
HETATM 1922  O   HOH A 759      -6.628 -14.641  17.745  1.00 33.12           O
HETATM 1923  O   HOH A 760      -6.454 -27.629  41.529  1.00 42.40           O
HETATM 1924  O   HOH A 761       1.125 -16.637  36.237  1.00 29.40           O
HETATM 1925  O   HOH A 762      13.893 -29.214  12.917  1.00 29.90           O
HETATM 1926  O   HOH A 763       3.092 -23.674  38.284  1.00 16.36           O
HETATM 1927  O   HOH A 764      12.783 -25.740  38.487  1.00 33.11           O
HETATM 1928  O   HOH A 765      -5.157 -20.377  26.394  1.00 18.49           O
HETATM 1929  O   HOH A 766      -1.428 -15.057  25.701  1.00 37.17           O
HETATM 1930  O   HOH A 767      23.170 -14.547  35.901  1.00 32.80           O
HETATM 1931  O   HOH A 768       8.105 -30.557  39.417  1.00 26.47           O
HETATM 1932  O   HOH A 769       1.078 -35.208  44.330  1.00 48.50           O
HETATM 1933  O   HOH A 770       0.556 -21.093  23.851  1.00 13.59           O
HETATM 1934  O   HOH A 771       5.628  -9.366  32.875  1.00 35.12           O
HETATM 1935  O   HOH A 772      19.796  -8.099  13.567  1.00 34.32           O
HETATM 1936  O   HOH A 773       8.347 -32.305  19.659  1.00 27.72           O
HETATM 1937  O   HOH A 774      -4.791 -16.957  37.698  1.00 38.19           O
HETATM 1938  O   HOH A 775       0.903 -18.626  24.898  1.00 21.93           O
HETATM 1939  O  AHOH A 776     -12.201 -27.502  27.339  0.59 18.67           O
HETATM 1940  O  BHOH A 776     -14.326 -27.247  26.868  0.41 22.35           O
HETATM 1941  O   HOH A 777       6.023 -29.071  19.376  1.00 15.68           O
HETATM 1942  O   HOH A 778       6.578 -31.219   8.708  1.00 37.67           O
HETATM 1943  O   HOH A 779     -11.948 -19.283  19.847  1.00 18.22           O
HETATM 1944  O   HOH A 780      -9.217 -14.358  28.587  1.00 32.67           O
HETATM 1945  O   HOH A 781       9.293 -35.756  35.644  1.00 33.38           O
HETATM 1946  O   HOH A 782       5.626 -32.563  15.409  1.00 37.51           O
HETATM 1947  O   HOH A 783     -11.779 -24.194   6.180  1.00 40.67           O
HETATM 1948  O   HOH A 784       8.074  -1.767  22.919  1.00 38.08           O
HETATM 1949  O   HOH A 785      16.870 -14.797   2.341  1.00 34.22           O
HETATM 1950  O   HOH A 786      14.174   0.262  20.146  1.00 38.72           O
HETATM 1951  O   HOH A 787      19.080  -9.902  11.686  1.00 34.20           O
HETATM 1952  O   HOH A 788      14.545 -22.641  -5.853  1.00 37.88           O
HETATM 1953  O   HOH A 789      13.412 -10.328  35.854  1.00 36.48           O
HETATM 1954  O   HOH A 790      -3.389 -18.248  25.419  1.00 21.55           O
HETATM 1955  O   HOH A 791       4.196 -16.868   0.999  1.00 40.94           O
HETATM 1956  O   HOH A 792       7.825 -37.634  37.776  1.00 41.65           O
HETATM 1957  O   HOH A 793      15.327  -8.631  31.533  1.00 35.22           O
HETATM 1958  O   HOH A 794      -5.548 -18.953  22.442  1.00 25.09           O
HETATM 1959  O   HOH A 795      -3.095 -19.864  20.819  1.00 20.83           O
HETATM 1960  O   HOH A 796      -4.124 -15.009  18.061  1.00 23.87           O
HETATM 1961  O   HOH A 797      -5.802 -44.366  35.010  1.00 47.55           O
HETATM 1962  O   HOH A 798      10.515 -20.675  42.090  1.00 30.06           O
HETATM 1963  O   HOH A 799      23.340  -4.624  25.219  1.00 35.65           O
HETATM 1964  O   HOH A 800       2.962 -32.905  15.390  1.00 32.90           O
HETATM 1965  O   HOH A 801      -9.773 -38.131  31.109  1.00 37.42           O
HETATM 1966  O   HOH A 802     -10.820 -21.356  18.538  1.00 19.52           O
HETATM 1967  O   HOH A 803       0.297 -40.286  35.165  1.00 38.67           O
HETATM 1968  O   HOH A 804       2.818 -15.175  34.262  1.00 28.90           O
HETATM 1969  O   HOH A 805       6.119 -11.839  35.293  1.00 29.12           O
HETATM 1970  O   HOH A 806      10.641   3.823  12.860  1.00 51.49           O
HETATM 1971  O   HOH A 807      21.997 -15.519  10.522  1.00 30.86           O
HETATM 1972  O   HOH A 808      29.141  -6.640  32.664  1.00 38.69           O
HETATM 1973  O   HOH A 809      11.650   2.432  18.296  1.00 45.00           O
HETATM 1974  O   HOH A 810     -10.160 -25.160  38.121  1.00 26.98           O
HETATM 1975  O   HOH A 811      13.236 -24.214  19.696  1.00 27.73           O
HETATM 1976  O   HOH A 812      26.286 -12.661  37.389  1.00 44.67           O
HETATM 1977  O   HOH A 813     -15.966 -21.717  27.894  1.00 19.13           O
HETATM 1978  O   HOH A 814      -2.409 -15.199  36.616  1.00 44.44           O
HETATM 1979  O   HOH A 815       4.371 -41.001  29.135  1.00 47.47           O
HETATM 1980  O   HOH A 816      16.497 -17.870  -6.686  1.00 32.46           O
HETATM 1981  O   HOH A 817      -0.841 -22.304  43.735  1.00 40.20           O
HETATM 1982  O   HOH A 818       2.399 -34.291  13.072  1.00 38.25           O
HETATM 1983  O   HOH A 819       1.715 -37.821  18.634  1.00 40.45           O
HETATM 1984  O   HOH A 820     -22.111 -27.342  32.504  1.00 51.28           O
HETATM 1985  O   HOH A 821     -15.846 -24.819  34.494  1.00 33.84           O
HETATM 1986  O   HOH A 822      16.881 -24.543  -6.893  1.00 34.36           O
HETATM 1987  O   HOH A 823      18.955 -13.887  35.188  1.00 28.82           O
HETATM 1988  O   HOH A 824      -6.936 -36.218  21.969  1.00 42.20           O
HETATM 1989  O   HOH A 825     -14.718 -34.163  28.329  1.00 34.91           O
HETATM 1990  O  AHOH A 826      -9.635 -17.532   4.293  0.62 29.81           O
HETATM 1991  O  BHOH A 826     -10.279 -15.653   5.195  0.38 27.24           O
HETATM 1992  O   HOH A 827     -18.450 -22.573  27.942  1.00 33.92           O
HETATM 1993  O   HOH A 828       6.305 -26.992  41.247  1.00 32.06           O
HETATM 1994  O   HOH A 829      -6.562 -12.844  27.408  1.00 29.47           O
HETATM 1995  O  AHOH A 830      20.425 -19.478  36.848  0.43 28.48           O
HETATM 1996  O  BHOH A 830      22.867 -18.412  37.820  0.57 33.93           O
HETATM 1997  O   HOH A 831      20.103 -17.475  13.615  1.00 32.39           O
HETATM 1998  O   HOH A 832      -2.084 -16.280  34.488  1.00 39.26           O
HETATM 1999  O   HOH A 833      10.692 -44.371  24.437  1.00 45.65           O
HETATM 2000  O   HOH A 834      16.266 -12.153   4.546  1.00 42.47           O
HETATM 2001  O   HOH A 835      15.974 -27.258  15.887  1.00 36.25           O
HETATM 2002  O   HOH A 836      21.115 -15.496   8.419  1.00 37.81           O
HETATM 2003  O   HOH A 837      -6.726 -24.627   1.705  1.00 44.98           O
HETATM 2004  O   HOH A 838       1.118 -12.116  27.835  1.00 38.05           O
HETATM 2005  O   HOH A 839      16.542 -33.645   8.794  1.00 42.20           O
HETATM 2006  O   HOH A 840       5.576 -26.819  -1.813  1.00 40.37           O
HETATM 2007  O   HOH A 841       0.472 -15.074  33.047  1.00 32.79           O
HETATM 2008  O   HOH A 842      19.726 -19.077  15.112  1.00 32.31           O
HETATM 2009  O   HOH A 843       6.548 -39.510  30.150  1.00 43.21           O
HETATM 2010  O   HOH A 844      -5.050 -22.772  44.380  1.00 39.33           O
HETATM 2011  O   HOH A 845     -14.982 -32.569  26.407  1.00 41.73           O
HETATM 2012  O   HOH A 846      -0.724 -15.774  28.513  1.00 32.75           O
HETATM 2013  O   HOH A 847       8.607 -28.492  40.527  1.00 38.37           O
HETATM 2014  O   HOH A 848      21.296 -23.445   5.110  1.00 36.33           O
HETATM 2015  O   HOH A 849       6.308 -39.385  19.302  1.00 37.19           O
HETATM 2016  O   HOH A 850      30.683  -7.022  30.766  1.00 51.11           O
HETATM 2017  O   HOH A 851      16.935  -0.584  19.292  1.00 52.35           O
HETATM 2018  O   HOH A 852      23.337 -20.884  31.055  1.00 26.93           O
HETATM 2019  O   HOH A 853      20.712 -20.682   6.781  1.00 31.58           O
HETATM 2020  O   HOH A 854      -1.079 -17.669  26.271  1.00 29.74           O
HETATM 2021  O   HOH A 855      -9.965 -37.376  24.596  1.00 37.96           O
HETATM 2022  O   HOH A 856      10.744 -18.641  43.287  1.00 30.72           O
HETATM 2023  O   HOH A 857      15.530  -9.202  34.629  1.00 37.14           O
HETATM 2024  O   HOH A 858     -20.350 -31.912  31.223  1.00 50.14           O
HETATM 2025  O   HOH A 859      21.175  -3.564  23.474  1.00 44.26           O
HETATM 2026  O   HOH A 860      -3.844 -11.757   7.574  1.00 42.66           O
HETATM 2027  O   HOH A 861      -0.888 -38.055  17.923  1.00 41.80           O
HETATM 2028  O   HOH A 862     -11.303 -35.679  22.807  1.00 38.83           O
HETATM 2029  O  AHOH A 863      -4.237 -14.908  39.985  0.54 36.60           O
HETATM 2030  O  BHOH A 863      -2.973 -14.451  40.853  0.46 39.41           O
HETATM 2031  O   HOH A 864       3.089  -9.797  32.249  1.00 36.73           O
HETATM 2032  O   HOH A 865      -2.392 -11.423  10.059  1.00 28.63           O
HETATM 2033  O   HOH A 866      18.497  -3.748  18.880  1.00 46.15           O
HETATM 2034  O   HOH A 867      -0.957 -10.266  26.380  1.00 49.41           O
HETATM 2035  O   HOH A 868       5.057  -3.882  13.586  1.00 45.82           O
HETATM 2036  O   HOH A 869      -0.371 -20.333  21.154  1.00 16.33           O
HETATM 2037  O   HOH A 870      19.184  -8.330   9.268  1.00 46.79           O
HETATM 2038  O   HOH A 871      -7.800 -35.701  19.498  1.00 50.74           O
HETATM 2039  O   HOH A 872      -6.635 -17.106  35.837  1.00 31.44           O
HETATM 2040  O   HOH A 873      -3.626 -13.446  34.750  1.00 40.07           O
HETATM 2041  O   HOH A 874      -1.347 -11.170  29.796  1.00 47.69           O
HETATM 2042  O   HOH A 875     -23.807 -29.292  33.338  1.00 45.44           O
HETATM 2043  O   HOH A 876     -18.857 -34.919  26.803  1.00 47.87           O
HETATM 2044  O   HOH A 877      -2.210 -11.889  32.373  1.00 45.70           O
HETATM 2045  O   HOH A 878      -1.451 -38.711  15.553  1.00 60.51           O
CONECT 1830 1831 1845
CONECT 1840 1839 1841
CONECT 1841 1840 1842 1843
CONECT 1843 1841 1844
CONECT 1844 1843 1838
CONECT 1845 1835 1830 1846
CONECT 1846 1837 1845 1847
CONECT 1847 1848 1849 1846
CONECT 1849 1854 1850 1847
CONECT 1850 1849 1851
CONECT 1851 1852 1850
CONECT 1831 1832 1830
CONECT 1852 1851 1853 1855
CONECT 1853 1854 1852
CONECT 1854 1849 1853
CONECT 1856 1857 1855
CONECT 1857 1858 1856
CONECT 1859 1858 1860
CONECT 1860 1861 1859
CONECT 1861 1860 1862
CONECT 1832 1831 1834 1833
CONECT 1862 1861 1863
CONECT 1863 1858 1862
CONECT 1834 1832 1835
CONECT 1835 1834 1845 1836
CONECT 1837 1836 1838 1846
CONECT 1838 1837 1839 1844
CONECT 1839 1840 1838
CONECT 1858 1857 1859 1863
CONECT 1842 1841
CONECT 1848 1847
CONECT 1855 1852 1856
CONECT 1833 1832
CONECT 1836 1837 1835
END



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