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***  HYDROLASE/HYDROLASE INHIBITOR 07-JUL-17 5WE9  ***

elNémo ID: 21062219191652538

Job options:

ID        	=	 21062219191652538
JOBID     	=	 HYDROLASE/HYDROLASE INHIBITOR 07-JUL-17 5WE9
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    HYDROLASE/HYDROLASE INHIBITOR           07-JUL-17   5WE9              
TITLE     CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS PA ENDONUCLEASE IN COMPLEX   
TITLE    2 WITH INHIBITOR 7B (SRI-29731)                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYMERASE ACIDIC PROTEIN;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;                              
SOURCE   3 ORGANISM_TAXID: 641501;                                              
SOURCE   4 STRAIN: SWL A/CALIFORNIA/04/2009 H1N1;                               
SOURCE   5 GENE: PA;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET52B                                    
KEYWDS    VIRUS, NUCLEASE, TRANSCRIPTION, CAP-SNATCHING, HYDROLASE, HYDROLASE-  
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.KUMAR,S.W.WHITE                                                     
REVDAT   2   11-DEC-19 5WE9    1       REMARK                                   
REVDAT   1   27-DEC-17 5WE9    0                                                
JRNL        AUTH   D.BEYLKIN,G.KUMAR,W.ZHOU,J.PARK,T.JEEVAN,C.LAGISETTI,        
JRNL        AUTH 2 R.HARFOOT,R.J.WEBBY,S.W.WHITE,T.R.WEBB                       
JRNL        TITL   PROTEIN-STRUCTURE ASSISTED OPTIMIZATION OF                   
JRNL        TITL 2 4,5-DIHYDROXYPYRIMIDINE-6-CARBOXAMIDE INHIBITORS OF          
JRNL        TITL 3 INFLUENZA VIRUS ENDONUCLEASE.                                
JRNL        REF    SCI REP                       V.   7 17139 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29215062                                                     
JRNL        DOI    10.1038/S41598-017-17419-6                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18640                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 917                             
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 35.5810 -  3.4496    1.00     2884   165  0.1799 0.1842        
REMARK   3     2  3.4496 -  2.7384    1.00     2724   128  0.1915 0.2554        
REMARK   3     3  2.7384 -  2.3923    1.00     2661   157  0.1935 0.2685        
REMARK   3     4  2.3923 -  2.1736    1.00     2636   140  0.1865 0.2435        
REMARK   3     5  2.1736 -  2.0178    1.00     2654   125  0.1872 0.2222        
REMARK   3     6  2.0178 -  1.8989    0.95     2481   126  0.2042 0.2339        
REMARK   3     7  1.8989 -  1.8038    0.64     1683    76  0.2405 0.2957        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           1552                                  
REMARK   3   ANGLE     :  0.914           2091                                  
REMARK   3   CHIRALITY :  0.056            216                                  
REMARK   3   PLANARITY :  0.006            267                                  
REMARK   3   DIHEDRAL  :  5.152            955                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND ( RESID 1:178 OR RESID 477:477 ) )       
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.425   75.618   14.074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.0470                                     
REMARK   3      T33:   0.2071 T12:   0.0173                                     
REMARK   3      T13:   0.1065 T23:  -0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1207 L22:   3.0081                                     
REMARK   3      L33:   2.5165 L12:  -0.1380                                     
REMARK   3      L13:   0.0953 L23:   0.8169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1001 S12:   0.1097 S13:  -0.4800                       
REMARK   3      S21:  -0.1138 S22:  -0.1192 S23:  -0.1298                       
REMARK   3      S31:   0.4554 S32:   0.1217 S33:   0.1105                       
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 5WE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228882.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19618                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 17.70                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 30% PEG 4000, 0.2 M   
REMARK 280  MGCL2, 2 MM MNCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.56467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       85.12933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       42.56467            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.12933            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.56467            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       85.12933            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       42.56467            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       85.12933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000     -111.12150            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       64.15603            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       42.56467            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   198                                                      
REMARK 465     ALA A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     LEU A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     LEU A   203                                                      
REMARK 465     VAL A   204                                                      
REMARK 465     PRO A   205                                                      
REMARK 465     ARG A   206                                                      
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     GLU A 101    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     LYS A 139    CG   CD   CE   NZ                                   
REMARK 470     SER A 140    OG                                                  
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 166    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   436     O    HOH A   512              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 125     -120.61    -95.13                                   
REMARK 500    LYS A 139       46.51     31.51                                   
REMARK 500    GLU A 141      -45.36     64.73                                   
REMARK 500    THR A 162      -58.09     66.33                                   
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 526        DISTANCE =  6.38 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  41   NE2                                                    
REMARK 620 2 ASP A 108   OD2  94.5                                              
REMARK 620 3 GLU A 119   OE2 176.9  88.5                                        
REMARK 620 4 ILE A 120   O    93.2  88.7  87.3                                  
REMARK 620 5 GY7 A 303   O4   91.9 172.6  85.0  94.7                            
REMARK 620 6 GY7 A 303   O4   82.7 177.1  94.3  92.3   9.7                      
REMARK 620 7 GY7 A 303   O3   87.7 100.9  91.3 170.3  75.6  78.2                
REMARK 620 8 GY7 A 303   O3   86.9 103.3  91.9 168.0  73.3  75.8   2.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE1                                                    
REMARK 620 2 ASP A 108   OD1  89.1                                              
REMARK 620 3 GY7 A 303   O3   98.5  94.2                                        
REMARK 620 4 GY7 A 303   O3   97.6  93.9   1.0                                  
REMARK 620 5 HOH A 407   O   173.6  86.9  86.8  87.7                            
REMARK 620 6 HOH A 458   O    87.6  91.6 171.6 172.5  87.5                      
REMARK 620 7 GY7 A 303   O2   89.0 178.0  86.8  87.0  94.9  87.6                
REMARK 620 8 GY7 A 303   O2   85.9 173.9  83.1  83.3  98.4  91.7   5.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GY7 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5W3I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W44   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W7U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W92   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W9G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WA6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WA7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WAP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WB3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WDW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WCS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WCT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WDN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WE7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5WDC   RELATED DB: PDB                                   
DBREF  5WE9 A    1    50  UNP    C3W5S0   C3W5S0_I09A0     1     50             
DBREF  5WE9 A   73   196  UNP    C3W5S0   C3W5S0_I09A0    73    196             
SEQADV 5WE9 GLY A   51  UNP  C3W5S0              LINKER                         
SEQADV 5WE9 GLY A   52  UNP  C3W5S0              LINKER                         
SEQADV 5WE9 SER A   53  UNP  C3W5S0              LINKER                         
SEQADV 5WE9 ALA A  197  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 ALA A  198  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 ALA A  199  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 GLU A  200  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 LEU A  201  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 ALA A  202  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 LEU A  203  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 VAL A  204  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 PRO A  205  UNP  C3W5S0              EXPRESSION TAG                 
SEQADV 5WE9 ARG A  206  UNP  C3W5S0              EXPRESSION TAG                 
SEQRES   1 A  187  MET GLU ASP PHE VAL ARG GLN CYS PHE ASN PRO MET ILE          
SEQRES   2 A  187  VAL GLU LEU ALA GLU LYS ALA MET LYS GLU TYR GLY GLU          
SEQRES   3 A  187  ASP PRO LYS ILE GLU THR ASN LYS PHE ALA ALA ILE CYS          
SEQRES   4 A  187  THR HIS LEU GLU VAL CYS PHE MET TYR SER ASP GLY GLY          
SEQRES   5 A  187  SER LYS HIS ARG PHE GLU ILE ILE GLU GLY ARG ASP ARG          
SEQRES   6 A  187  ILE MET ALA TRP THR VAL VAL ASN SER ILE CYS ASN THR          
SEQRES   7 A  187  THR GLY VAL GLU LYS PRO LYS PHE LEU PRO ASP LEU TYR          
SEQRES   8 A  187  ASP TYR LYS GLU ASN ARG PHE ILE GLU ILE GLY VAL THR          
SEQRES   9 A  187  ARG ARG GLU VAL HIS ILE TYR TYR LEU GLU LYS ALA ASN          
SEQRES  10 A  187  LYS ILE LYS SER GLU LYS THR HIS ILE HIS ILE PHE SER          
SEQRES  11 A  187  PHE THR GLY GLU GLU MET ALA THR LYS ALA ASP TYR THR          
SEQRES  12 A  187  LEU ASP GLU GLU SER ARG ALA ARG ILE LYS THR ARG LEU          
SEQRES  13 A  187  PHE THR ILE ARG GLN GLU MET ALA SER ARG SER LEU TRP          
SEQRES  14 A  187  ASP SER PHE ARG GLN SER GLU ARG ALA ALA ALA GLU LEU          
SEQRES  15 A  187  ALA LEU VAL PRO ARG                                          
HET     MN  A 301       1                                                       
HET     MG  A 302       1                                                       
HET    GY7  A 303      68                                                       
HET    EDO  A 304       4                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GY7 2-[(2S)-1-(2,6-DIFLUOROBENZENE-1-CARBONYL)PYRROLIDIN-2-          
HETNAM   2 GY7  YL]-5-HYDROXY-6-OXO-N-(2-PHENYLETHYL)-1,6-                      
HETNAM   3 GY7  DIHYDROPYRIMIDINE-4-CARBOXAMIDE                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GY7 SRI-29731                                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   MN    MN 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GY7    C24 H22 F2 N4 O4                                             
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6  HOH   *126(H2 O)                                                    
HELIX    1 AA1 MET A    1  PHE A    9  1                                   9    
HELIX    2 AA2 ASN A   10  GLU A   23  1                                  14    
HELIX    3 AA3 GLU A   31  ASP A   50  1                                  20    
HELIX    4 AA4 ASP A   83  GLY A   99  1                                  17    
HELIX    5 AA5 GLU A  126  LYS A  139  1                                  14    
HELIX    6 AA6 LYS A  158  ASP A  160  5                                   3    
HELIX    7 AA7 ASP A  164  ARG A  185  1                                  22    
HELIX    8 AA8 LEU A  187  GLN A  193  1                                   7    
SHEET    1 AA1 5 PHE A  76  ILE A  78  0                                        
SHEET    2 AA1 5 LEU A 109  ASP A 111 -1  O  TYR A 110   N  GLU A  77           
SHEET    3 AA1 5 ARG A 116  THR A 123 -1  O  ARG A 116   N  ASP A 111           
SHEET    4 AA1 5 HIS A 144  SER A 149  1  O  HIS A 144   N  GLU A 119           
SHEET    5 AA1 5 GLU A 154  ALA A 156 -1  O  MET A 155   N  ILE A 147           
LINK         NE2 HIS A  41                MN    MN A 301     1555   1555  2.44  
LINK         OE1 GLU A  80                MG    MG A 302     1555   1555  2.07  
LINK         OD1 ASP A 108                MG    MG A 302     1555   1555  2.11  
LINK         OD2 ASP A 108                MN    MN A 301     1555   1555  2.16  
LINK         OE2 GLU A 119                MN    MN A 301     1555   1555  2.23  
LINK         O   ILE A 120                MN    MN A 301     1555   1555  2.17  
LINK        MN    MN A 301                 O4 AGY7 A 303     1555   1555  2.06  
LINK        MN    MN A 301                 O4 BGY7 A 303     1555   1555  2.16  
LINK        MN    MN A 301                 O3 AGY7 A 303     1555   1555  2.27  
LINK        MN    MN A 301                 O3 BGY7 A 303     1555   1555  2.21  
LINK        MG    MG A 302                 O3 AGY7 A 303     1555   1555  1.98  
LINK        MG    MG A 302                 O3 BGY7 A 303     1555   1555  2.09  
LINK        MG    MG A 302                 O   HOH A 407     1555   1555  2.10  
LINK        MG    MG A 302                 O   HOH A 458     1555   1555  2.19  
LINK        MG    MG A 302                 O2 AGY7 A 303     1555   1555  2.03  
LINK        MG    MG A 302                 O2 BGY7 A 303     1555   1555  1.97  
SITE     1 AC1  6 HIS A  41  ASP A 108  GLU A 119  ILE A 120                    
SITE     2 AC1  6  MG A 302  GY7 A 303                                          
SITE     1 AC2  6 GLU A  80  ASP A 108   MN A 301  GY7 A 303                    
SITE     2 AC2  6 HOH A 407  HOH A 458                                          
SITE     1 AC3 20 ALA A  20  TYR A  24  GLU A  26  LYS A  34                    
SITE     2 AC3 20 ILE A  38  HIS A  41  GLU A  80  ASP A 108                    
SITE     3 AC3 20 GLU A 119  ILE A 120  LYS A 134  LYS A 137                    
SITE     4 AC3 20  MN A 301   MG A 302  HOH A 407  HOH A 415                    
SITE     5 AC3 20 HOH A 416  HOH A 439  HOH A 458  HOH A 500                    
SITE     1 AC4  7 PRO A 103  PHE A 105  LEU A 106  PRO A 107                    
SITE     2 AC4  7 GLU A 119  ILE A 138  THR A 143                               
CRYST1   74.081   74.081  127.694  90.00  90.00 120.00 P 64 2 2     12          
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      0.013499  0.007793  0.000000        0.00000                         
SCALE2      0.000000  0.015587  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007831        0.00000                         
ATOM      1  N   MET A   1     -14.024  84.679  -4.536  1.00 28.59           N  
ANISOU    1  N   MET A   1     5461   3551   1852     96    770   -785       N  
ATOM      2  CA  MET A   1     -14.127  84.057  -3.214  1.00 31.42           C  
ANISOU    2  CA  MET A   1     5603   3877   2460    101    740   -823       C  
ATOM      3  C   MET A   1     -14.961  84.886  -2.239  1.00 27.81           C  
ANISOU    3  C   MET A   1     5106   3363   2097     89    589   -772       C  
ATOM      4  O   MET A   1     -15.732  84.320  -1.477  1.00 28.13           O  
ANISOU    4  O   MET A   1     4991   3404   2294    105    484   -847       O  
ATOM      5  CB  MET A   1     -12.748  83.792  -2.598  1.00 29.98           C  
ANISOU    5  CB  MET A   1     5319   3679   2394     77    930   -767       C  
ATOM      6  CG  MET A   1     -12.843  83.255  -1.151  1.00 24.14           C  
ANISOU    6  CG  MET A   1     4382   2896   1894     85    882   -779       C  
ATOM      7  SD  MET A   1     -13.564  81.613  -1.060  1.00 27.22           S  
ANISOU    7  SD  MET A   1     4649   3301   2394    147    793   -934       S  
ATOM      8  CE  MET A   1     -12.028  80.777  -1.303  1.00 29.35           C  
ANISOU    8  CE  MET A   1     4882   3581   2688    172   1003   -939       C  
ATOM      9  N   GLU A   2     -14.834  86.221  -2.252  1.00 27.24           N  
ANISOU    9  N   GLU A   2     5174   3241   1935     60    578   -648       N  
ATOM     10  CA  GLU A   2     -15.723  87.019  -1.401  1.00 23.02           C  
ANISOU   10  CA  GLU A   2     4613   2652   1480     67    415   -618       C  
ATOM     11  C   GLU A   2     -17.183  86.767  -1.753  1.00 24.34           C  
ANISOU   11  C   GLU A   2     4756   2856   1636    118    218   -723       C  
ATOM     12  O   GLU A   2     -18.030  86.625  -0.861  1.00 24.10           O  
ANISOU   12  O   GLU A   2     4564   2826   1766    125    112   -777       O  
ATOM     13  CB  GLU A   2     -15.403  88.511  -1.514  1.00 23.63           C  
ANISOU   13  CB  GLU A   2     4884   2651   1442     36    416   -474       C  
ATOM     14  CG  GLU A   2     -16.158  89.341  -0.478  1.00 26.60           C  
ANISOU   14  CG  GLU A   2     5222   2960   1925     51    260   -448       C  
ATOM     15  CD  GLU A   2     -16.089  90.841  -0.729  1.00 36.19           C  
ANISOU   15  CD  GLU A   2     6664   4075   3011     38    209   -319       C  
ATOM     16  OE1 GLU A   2     -15.274  91.279  -1.581  1.00 32.35           O  
ANISOU   16  OE1 GLU A   2     6348   3574   2371    -10    333   -227       O  
ATOM     17  OE2 GLU A   2     -16.868  91.577  -0.077  1.00 37.47           O  
ANISOU   17  OE2 GLU A   2     6823   4175   3237     77     44   -311       O  
ATOM     18  N   ASP A   3     -17.487  86.665  -3.057  1.00 25.60           N  
ANISOU   18  N   ASP A   3     5060   3057   1609    145    180   -761       N  
ATOM     19  CA  ASP A   3     -18.843  86.360  -3.495  1.00 29.98           C  
ANISOU   19  CA  ASP A   3     5589   3655   2148    183      0   -877       C  
ATOM     20  C   ASP A   3     -19.254  84.961  -3.072  1.00 29.69           C  
ANISOU   20  C   ASP A   3     5326   3672   2283    158     18  -1035       C  
ATOM     21  O   ASP A   3     -20.404  84.738  -2.679  1.00 26.36           O  
ANISOU   21  O   ASP A   3     4781   3263   1971    146    -99  -1121       O  
ATOM     22  CB  ASP A   3     -18.951  86.474  -5.017  1.00 38.65           C  
ANISOU   22  CB  ASP A   3     6902   4792   2990    215    -35   -887       C  
ATOM     23  CG  ASP A   3     -19.063  87.903  -5.489  1.00 52.07           C  
ANISOU   23  CG  ASP A   3     8834   6426   4523    252   -129   -746       C  
ATOM     24  OD1 ASP A   3     -19.471  88.767  -4.684  1.00 56.95           O  
ANISOU   24  OD1 ASP A   3     9432   6970   5238    271   -231   -680       O  
ATOM     25  OD2 ASP A   3     -18.761  88.158  -6.674  1.00 57.73           O  
ANISOU   25  OD2 ASP A   3     9760   7162   5011    265   -103   -702       O  
ATOM     26  N   PHE A   4     -18.342  83.995  -3.183  1.00 25.63           N  
ANISOU   26  N   PHE A   4     4763   3181   1793    147    169  -1075       N  
ATOM     27  CA  PHE A   4     -18.663  82.664  -2.691  1.00 24.92           C  
ANISOU   27  CA  PHE A   4     4472   3114   1882    134    180  -1214       C  
ATOM     28  C   PHE A   4     -19.058  82.715  -1.220  1.00 22.59           C  
ANISOU   28  C   PHE A   4     3987   2783   1813    112    144  -1193       C  
ATOM     29  O   PHE A   4     -20.089  82.158  -0.819  1.00 25.21           O  
ANISOU   29  O   PHE A   4     4189   3122   2267     75     82  -1300       O  
ATOM     30  CB  PHE A   4     -17.486  81.713  -2.885  1.00 28.75           C  
ANISOU   30  CB  PHE A   4     4948   3602   2375    159    336  -1230       C  
ATOM     31  CG  PHE A   4     -17.676  80.407  -2.175  1.00 24.49           C  
ANISOU   31  CG  PHE A   4     4227   3044   2033    178    328  -1333       C  
ATOM     32  CD1 PHE A   4     -17.025  80.143  -0.977  1.00 22.96           C  
ANISOU   32  CD1 PHE A   4     3941   2786   1996    191    386  -1245       C  
ATOM     33  CD2 PHE A   4     -18.560  79.461  -2.680  1.00 29.90           C  
ANISOU   33  CD2 PHE A   4     4886   3746   2730    176    260  -1507       C  
ATOM     34  CE1 PHE A   4     -17.221  78.936  -0.317  1.00 23.83           C  
ANISOU   34  CE1 PHE A   4     3976   2830   2247    217    373  -1298       C  
ATOM     35  CE2 PHE A   4     -18.766  78.271  -2.022  1.00 33.28           C  
ANISOU   35  CE2 PHE A   4     5219   4101   3323    207    241  -1561       C  
ATOM     36  CZ  PHE A   4     -18.096  78.010  -0.833  1.00 26.01           C  
ANISOU   36  CZ  PHE A   4     4255   3100   2528    238    293  -1453       C  
ATOM     37  N   VAL A   5     -18.252  83.392  -0.401  1.00 23.69           N  
ANISOU   37  N   VAL A   5     4127   2875   1998    116    202  -1055       N  
ATOM     38  CA  VAL A   5     -18.493  83.411   1.041  1.00 20.93           C  
ANISOU   38  CA  VAL A   5     3606   2499   1847    103    175  -1030       C  
ATOM     39  C   VAL A   5     -19.851  84.030   1.339  1.00 18.87           C  
ANISOU   39  C   VAL A   5     3290   2250   1630     69     55  -1069       C  
ATOM     40  O   VAL A   5     -20.644  83.490   2.113  1.00 20.77           O  
ANISOU   40  O   VAL A   5     3405   2480   2008     32     39  -1136       O  
ATOM     41  CB  VAL A   5     -17.357  84.153   1.768  1.00 19.91           C  
ANISOU   41  CB  VAL A   5     3516   2318   1730     95    262   -880       C  
ATOM     42  CG1 VAL A   5     -17.744  84.466   3.237  1.00 19.85           C  
ANISOU   42  CG1 VAL A   5     3361   2291   1890     85    204   -848       C  
ATOM     43  CG2 VAL A   5     -16.070  83.319   1.733  1.00 18.25           C  
ANISOU   43  CG2 VAL A   5     3306   2095   1533    101    414   -853       C  
ATOM     44  N   ARG A   6     -20.152  85.160   0.703  1.00 21.94           N  
ANISOU   44  N   ARG A   6     3845   2622   1870     90    -27  -1008       N  
ATOM     45  CA  ARG A   6     -21.387  85.854   1.040  1.00 25.72           C  
ANISOU   45  CA  ARG A   6     4298   3090   2386     89   -159  -1016       C  
ATOM     46  C   ARG A   6     -22.615  85.076   0.598  1.00 34.42           C  
ANISOU   46  C   ARG A   6     5354   4224   3502     49   -218  -1144       C  
ATOM     47  O   ARG A   6     -23.685  85.229   1.196  1.00 26.86           O  
ANISOU   47  O   ARG A   6     4336   3243   2625     42   -299  -1160       O  
ATOM     48  CB  ARG A   6     -21.370  87.260   0.444  1.00 20.70           C  
ANISOU   48  CB  ARG A   6     3870   2404   1589    165   -275   -912       C  
ATOM     49  CG  ARG A   6     -20.286  88.131   1.101  1.00 20.68           C  
ANISOU   49  CG  ARG A   6     3932   2335   1591    163   -203   -777       C  
ATOM     50  CD  ARG A   6     -20.367  89.618   0.684  1.00 26.67           C  
ANISOU   50  CD  ARG A   6     4914   3008   2212    222   -319   -670       C  
ATOM     51  NE  ARG A   6     -19.163  90.331   1.100  1.00 24.45           N  
ANISOU   51  NE  ARG A   6     4737   2649   1902    181   -210   -548       N  
ATOM     52  CZ  ARG A   6     -18.945  90.804   2.324  1.00 25.43           C  
ANISOU   52  CZ  ARG A   6     4768   2733   2161    157   -199   -512       C  
ATOM     53  NH1 ARG A   6     -19.862  90.674   3.276  1.00 24.92           N  
ANISOU   53  NH1 ARG A   6     4497   2706   2267    176   -279   -579       N  
ATOM     54  NH2 ARG A   6     -17.803  91.404   2.598  1.00 29.27           N  
ANISOU   54  NH2 ARG A   6     5366   3148   2607     98    -89   -414       N  
ATOM     55  N   GLN A   7     -22.495  84.221  -0.415  1.00 29.80           N  
ANISOU   55  N   GLN A   7     4821   3674   2826     36   -189  -1232       N  
ATOM     56  CA  GLN A   7     -23.673  83.468  -0.811  1.00 27.37           C  
ANISOU   56  CA  GLN A   7     4514   3366   2519     -5   -260  -1350       C  
ATOM     57  C   GLN A   7     -23.773  82.090  -0.166  1.00 29.95           C  
ANISOU   57  C   GLN A   7     4762   3639   2978   -103   -135  -1423       C  
ATOM     58  O   GLN A   7     -24.883  81.556  -0.075  1.00 42.68           O  
ANISOU   58  O   GLN A   7     6393   5203   4621   -136   -209  -1473       O  
ATOM     59  CB  GLN A   7     -23.759  83.357  -2.344  1.00 42.89           C  
ANISOU   59  CB  GLN A   7     6621   5388   4289     28   -331  -1417       C  
ATOM     60  CG  GLN A   7     -22.677  82.568  -3.054  1.00 45.21           C  
ANISOU   60  CG  GLN A   7     6957   5717   4503     23   -198  -1467       C  
ATOM     61  CD  GLN A   7     -22.874  82.568  -4.575  1.00 58.43           C  
ANISOU   61  CD  GLN A   7     8815   7441   5944     67   -285  -1525       C  
ATOM     62  OE1 GLN A   7     -22.070  83.130  -5.327  1.00 58.82           O  
ANISOU   62  OE1 GLN A   7     9031   7508   5811    133   -264  -1445       O  
ATOM     63  NE2 GLN A   7     -23.954  81.939  -5.029  1.00 61.56           N  
ANISOU   63  NE2 GLN A   7     9208   7849   6332     20   -376  -1654       N  
ATOM     64  N   CYS A   8     -22.683  81.506   0.333  1.00 28.30           N  
ANISOU   64  N   CYS A   8     4450   3427   2874   -100      4  -1382       N  
ATOM     65  CA  CYS A   8     -22.788  80.149   0.872  1.00 22.03           C  
ANISOU   65  CA  CYS A   8     3630   2546   2194   -180    115  -1380       C  
ATOM     66  C   CYS A   8     -22.909  80.111   2.405  1.00 27.81           C  
ANISOU   66  C   CYS A   8     4517   3093   2958   -145    101  -1159       C  
ATOM     67  O   CYS A   8     -23.256  79.058   2.961  1.00 24.07           O  
ANISOU   67  O   CYS A   8     4061   2542   2543     -5    -36  -1176       O  
ATOM     68  CB  CYS A   8     -21.588  79.308   0.416  1.00 24.86           C  
ANISOU   68  CB  CYS A   8     3823   3005   2616     32     55  -1489       C  
ATOM     69  SG  CYS A   8     -22.019  77.508   0.122  1.00 37.47           S  
ANISOU   69  SG  CYS A   8     5697   4391   4149    275   -165  -1478       S  
ATOM     70  N   PHE A   9     -22.652  81.217   3.107  1.00 22.63           N  
ANISOU   70  N   PHE A   9     3680   2531   2387   -169    133  -1136       N  
ATOM     71  CA  PHE A   9     -22.713  81.245   4.568  1.00 17.59           C  
ANISOU   71  CA  PHE A   9     3123   1779   1779    -28     14   -980       C  
ATOM     72  C   PHE A   9     -23.790  82.201   5.069  1.00 21.31           C  
ANISOU   72  C   PHE A   9     3475   2313   2309    -94    -24  -1039       C  
ATOM     73  O   PHE A   9     -24.005  83.280   4.500  1.00 19.26           O  
ANISOU   73  O   PHE A   9     3180   2128   2011   -104    -67  -1092       O  
ATOM     74  CB  PHE A   9     -21.357  81.645   5.187  1.00 17.34           C  
ANISOU   74  CB  PHE A   9     2847   1869   1871    172    -84   -984       C  
ATOM     75  CG  PHE A   9     -20.290  80.617   4.964  1.00 16.24           C  
ANISOU   75  CG  PHE A   9     2705   1722   1742    153     42  -1019       C  
ATOM     76  CD1 PHE A   9     -20.255  79.454   5.730  1.00 16.81           C  
ANISOU   76  CD1 PHE A   9     2795   1715   1878    119    112  -1009       C  
ATOM     77  CD2 PHE A   9     -19.351  80.792   3.971  1.00 16.85           C  
ANISOU   77  CD2 PHE A   9     2800   1853   1747    153    117  -1062       C  
ATOM     78  CE1 PHE A   9     -19.271  78.476   5.508  1.00 18.08           C  
ANISOU   78  CE1 PHE A   9     2955   1855   2059    111    225  -1012       C  
ATOM     79  CE2 PHE A   9     -18.373  79.810   3.724  1.00 19.40           C  
ANISOU   79  CE2 PHE A   9     3174   2141   2057    161    229  -1058       C  
ATOM     80  CZ  PHE A   9     -18.342  78.654   4.497  1.00 19.91           C  
ANISOU   80  CZ  PHE A   9     3223   2129   2212    145    275  -1036       C  
ATOM     81  N   ASN A  10     -24.428  81.794   6.160  1.00 16.71           N  
ANISOU   81  N   ASN A  10     2808   1712   1828    -70    -69  -1057       N  
ATOM     82  CA  ASN A  10     -25.459  82.579   6.827  1.00 21.23           C  
ANISOU   82  CA  ASN A  10     3230   2350   2487    -67   -137  -1084       C  
ATOM     83  C   ASN A  10     -24.938  83.991   7.142  1.00 17.82           C  
ANISOU   83  C   ASN A  10     2808   1938   2026    -47   -135  -1004       C  
ATOM     84  O   ASN A  10     -23.768  84.150   7.508  1.00 16.67           O  
ANISOU   84  O   ASN A  10     2726   1757   1850    -57    -48   -910       O  
ATOM     85  CB  ASN A  10     -25.866  81.823   8.100  1.00 25.65           C  
ANISOU   85  CB  ASN A  10     3644   2917   3185    -84    -97  -1091       C  
ATOM     86  CG  ASN A  10     -26.870  82.543   8.928  1.00 42.43           C  
ANISOU   86  CG  ASN A  10     5614   5105   5402    -77   -139  -1125       C  
ATOM     87  OD1 ASN A  10     -26.610  83.614   9.438  1.00 44.50           O  
ANISOU   87  OD1 ASN A  10     5870   5384   5653    -44   -151  -1064       O  
ATOM     88  ND2 ASN A  10     -28.049  81.946   9.075  1.00 50.96           N  
ANISOU   88  ND2 ASN A  10     6562   6219   6581   -108   -156  -1237       N  
ATOM     89  N   PRO A  11     -25.759  85.032   6.979  1.00 16.05           N  
ANISOU   89  N   PRO A  11     2516   1765   1816      0   -249  -1044       N  
ATOM     90  CA  PRO A  11     -25.280  86.399   7.259  1.00 15.30           C  
ANISOU   90  CA  PRO A  11     2431   1678   1705     39   -272   -975       C  
ATOM     91  C   PRO A  11     -24.774  86.602   8.667  1.00 13.90           C  
ANISOU   91  C   PRO A  11     2205   1484   1592     22   -195   -898       C  
ATOM     92  O   PRO A  11     -23.952  87.495   8.873  1.00 13.20           O  
ANISOU   92  O   PRO A  11     2148   1385   1481     25   -173   -834       O  
ATOM     93  CB  PRO A  11     -26.517  87.267   6.993  1.00 16.37           C  
ANISOU   93  CB  PRO A  11     2503   1849   1867    131   -441  -1040       C  
ATOM     94  CG  PRO A  11     -27.297  86.474   5.984  1.00 17.91           C  
ANISOU   94  CG  PRO A  11     2702   2067   2036    131   -507  -1143       C  
ATOM     95  CD  PRO A  11     -27.028  85.027   6.225  1.00 19.40           C  
ANISOU   95  CD  PRO A  11     2887   2233   2251     41   -385  -1158       C  
ATOM     96  N   MET A  12     -25.300  85.875   9.660  1.00 13.67           N  
ANISOU   96  N   MET A  12     2080   1465   1649     11   -170   -915       N  
ATOM     97  CA  MET A  12     -24.765  86.011  11.013  1.00 12.52           C  
ANISOU   97  CA  MET A  12     1896   1315   1546      2   -107   -844       C  
ATOM     98  C   MET A  12     -23.320  85.537  11.065  1.00 11.69           C  
ANISOU   98  C   MET A  12     1899   1158   1384    -14    -29   -753       C  
ATOM     99  O   MET A  12     -22.464  86.159  11.703  1.00 10.84           O  
ANISOU   99  O   MET A  12     1819   1037   1263     -6     -7   -681       O  
ATOM    100  CB  MET A  12     -25.600  85.192  12.000  1.00 15.80           C  
ANISOU  100  CB  MET A  12     2171   1768   2066    -21    -75   -898       C  
ATOM    101  CG  MET A  12     -26.991  85.737  12.238  1.00 37.81           C  
ANISOU  101  CG  MET A  12     4821   4614   4931      7   -142   -997       C  
ATOM    102  SD  MET A  12     -28.126  85.644  10.825  1.00 53.68           S  
ANISOU  102  SD  MET A  12     6803   6647   6946     44   -260  -1121       S  
ATOM    103  CE  MET A  12     -29.120  84.194  11.215  1.00 50.02           C  
ANISOU  103  CE  MET A  12     6195   6213   6598    -30   -193  -1233       C  
ATOM    104  N   ILE A  13     -23.044  84.415  10.408  1.00 12.09           N  
ANISOU  104  N   ILE A  13     1998   1183   1413    -13     -8   -770       N  
ATOM    105  CA  ILE A  13     -21.674  83.906  10.331  1.00 11.58           C  
ANISOU  105  CA  ILE A  13     1964   1102   1334     32     17   -716       C  
ATOM    106  C   ILE A  13     -20.775  84.901   9.608  1.00 15.35           C  
ANISOU  106  C   ILE A  13     2463   1606   1765     99    -44   -674       C  
ATOM    107  O   ILE A  13     -19.645  85.186  10.045  1.00 10.70           O  
ANISOU  107  O   ILE A  13     1784   1050   1229     89      6   -666       O  
ATOM    108  CB  ILE A  13     -21.681  82.538   9.626  1.00 12.40           C  
ANISOU  108  CB  ILE A  13     2072   1191   1447     27     47   -778       C  
ATOM    109  CG1 ILE A  13     -22.304  81.495  10.555  1.00 16.25           C  
ANISOU  109  CG1 ILE A  13     2452   1684   2039    -41    115   -803       C  
ATOM    110  CG2 ILE A  13     -20.237  82.132   9.173  1.00 12.25           C  
ANISOU  110  CG2 ILE A  13     2047   1184   1425     58    101   -761       C  
ATOM    111  CD1 ILE A  13     -22.406  80.113   9.910  1.00 22.13           C  
ANISOU  111  CD1 ILE A  13     3213   2393   2804    -64    154   -867       C  
ATOM    112  N   VAL A  14     -21.244  85.417   8.467  1.00 12.26           N  
ANISOU  112  N   VAL A  14     2023   1264   1373    -95    123   -764       N  
ATOM    113  CA  VAL A  14     -20.435  86.358   7.692  1.00 12.38           C  
ANISOU  113  CA  VAL A  14     2032   1319   1351     -1     30   -800       C  
ATOM    114  C   VAL A  14     -20.110  87.595   8.523  1.00 11.58           C  
ANISOU  114  C   VAL A  14     1943   1192   1264      2      9   -736       C  
ATOM    115  O   VAL A  14     -18.971  88.087   8.526  1.00 11.43           O  
ANISOU  115  O   VAL A  14     1976   1151   1215     26     17   -666       O  
ATOM    116  CB  VAL A  14     -21.166  86.720   6.395  1.00 13.67           C  
ANISOU  116  CB  VAL A  14     2322   1479   1393     -4    -26   -853       C  
ATOM    117  CG1 VAL A  14     -20.437  87.863   5.702  1.00 13.92           C  
ANISOU  117  CG1 VAL A  14     2479   1494   1317     46    -76   -774       C  
ATOM    118  CG2 VAL A  14     -21.279  85.465   5.491  1.00 14.66           C  
ANISOU  118  CG2 VAL A  14     2449   1629   1493    -19      8   -933       C  
ATOM    119  N   GLU A  15     -21.095  88.115   9.250  1.00 11.48           N  
ANISOU  119  N   GLU A  15     1933   1160   1269    -24    -11   -725       N  
ATOM    120  CA  GLU A  15     -20.842  89.297  10.076  1.00 10.93           C  
ANISOU  120  CA  GLU A  15     1860   1071   1221     -3    -50   -671       C  
ATOM    121  C   GLU A  15     -19.806  89.013  11.170  1.00  9.93           C  
ANISOU  121  C   GLU A  15     1642    960   1172    -21     15   -629       C  
ATOM    122  O   GLU A  15     -18.928  89.848  11.432  1.00  9.64           O  
ANISOU  122  O   GLU A  15     1632    895   1134     -6     -8   -592       O  
ATOM    123  CB  GLU A  15     -22.160  89.797  10.684  1.00 11.23           C  
ANISOU  123  CB  GLU A  15     1884   1106   1278     34   -135   -682       C  
ATOM    124  CG  GLU A  15     -22.005  91.040  11.545  1.00 14.30           C  
ANISOU  124  CG  GLU A  15     2262   1477   1696     64   -183   -643       C  
ATOM    125  CD  GLU A  15     -21.692  92.304  10.735  1.00 28.02           C  
ANISOU  125  CD  GLU A  15     4098   3165   3383    113   -276   -611       C  
ATOM    126  OE1 GLU A  15     -22.099  92.403   9.556  1.00 24.19           O  
ANISOU  126  OE1 GLU A  15     3690   2667   2834    154   -348   -627       O  
ATOM    127  OE2 GLU A  15     -21.035  93.204  11.311  1.00 31.04           O  
ANISOU  127  OE2 GLU A  15     4502   3511   3782    107   -280   -565       O  
ATOM    128  N   LEU A  16     -19.895  87.856  11.830  1.00  9.61           N  
ANISOU  128  N   LEU A  16     1482    965   1204     -4     25   -639       N  
ATOM    129  CA  LEU A  16     -18.924  87.538  12.880  1.00  8.86           C  
ANISOU  129  CA  LEU A  16     1477    820   1069     65    -23   -542       C  
ATOM    130  C   LEU A  16     -17.530  87.406  12.304  1.00  8.76           C  
ANISOU  130  C   LEU A  16     1487    794   1047     35     58   -526       C  
ATOM    131  O   LEU A  16     -16.546  87.840  12.914  1.00  9.13           O  
ANISOU  131  O   LEU A  16     1533    829   1107     12     90   -475       O  
ATOM    132  CB  LEU A  16     -19.313  86.241  13.600  1.00  9.19           C  
ANISOU  132  CB  LEU A  16     1527    847   1117     38     42   -538       C  
ATOM    133  CG  LEU A  16     -20.509  86.303  14.543  1.00 18.74           C  
ANISOU  133  CG  LEU A  16     2709   2066   2344     11     47   -554       C  
ATOM    134  CD1 LEU A  16     -20.999  84.873  14.841  1.00 19.76           C  
ANISOU  134  CD1 LEU A  16     2771   2209   2527    -30    118   -584       C  
ATOM    135  CD2 LEU A  16     -20.070  87.018  15.812  1.00 15.98           C  
ANISOU  135  CD2 LEU A  16     2336   1728   2008      8     47   -519       C  
ATOM    136  N   ALA A  17     -17.433  86.797  11.128  1.00  9.33           N  
ANISOU  136  N   ALA A  17     1598    868   1079     36     94   -549       N  
ATOM    137  CA  ALA A  17     -16.134  86.616  10.487  1.00 10.80           C  
ANISOU  137  CA  ALA A  17     1836   1041   1228     16    189   -508       C  
ATOM    138  C   ALA A  17     -15.536  87.953  10.068  1.00 14.47           C  
ANISOU  138  C   ALA A  17     2403   1462   1632    -22    215   -472       C  
ATOM    139  O   ALA A  17     -14.331  88.170  10.246  1.00 10.82           O  
ANISOU  139  O   ALA A  17     1987    960   1162    -67    320   -426       O  
ATOM    140  CB  ALA A  17     -16.281  85.680   9.287  1.00 10.35           C  
ANISOU  140  CB  ALA A  17     1819    992   1122     31    224   -553       C  
ATOM    141  N   GLU A  18     -16.347  88.862   9.503  1.00 10.32           N  
ANISOU  141  N   GLU A  18     1933    927   1060    -13    134   -494       N  
ATOM    142  CA  GLU A  18     -15.824  90.193   9.189  1.00 10.94           C  
ANISOU  142  CA  GLU A  18     2172    926   1057    -50    140   -435       C  
ATOM    143  C   GLU A  18     -15.292  90.873  10.431  1.00 10.30           C  
ANISOU  143  C   GLU A  18     2037    819   1058    -82    130   -404       C  
ATOM    144  O   GLU A  18     -14.238  91.527  10.404  1.00 10.80           O  
ANISOU  144  O   GLU A  18     2203    808   1093   -151    200   -355       O  
ATOM    145  CB  GLU A  18     -16.905  91.081   8.569  1.00 14.98           C  
ANISOU  145  CB  GLU A  18     2768   1415   1508    -13     18   -448       C  
ATOM    146  CG  GLU A  18     -17.347  90.699   7.191  1.00 18.62           C  
ANISOU  146  CG  GLU A  18     3339   1885   1851     15      4   -473       C  
ATOM    147  CD  GLU A  18     -18.486  91.609   6.708  1.00 32.73           C  
ANISOU  147  CD  GLU A  18     5213   3641   3582     73   -149   -482       C  
ATOM    148  OE1 GLU A  18     -19.065  92.357   7.546  1.00 43.51           O  
ANISOU  148  OE1 GLU A  18     6506   4994   5032     94   -231   -485       O  
ATOM    149  OE2 GLU A  18     -18.799  91.595   5.514  1.00 31.84           O  
ANISOU  149  OE2 GLU A  18     5243   3515   3340    106   -193   -487       O  
ATOM    150  N   LYS A  19     -16.030  90.763  11.531  1.00  9.43           N  
ANISOU  150  N   LYS A  19     1764    766   1052    -46     55   -442       N  
ATOM    151  CA  LYS A  19     -15.619  91.448  12.738  1.00  9.02           C  
ANISOU  151  CA  LYS A  19     1661    699   1066    -65     29   -425       C  
ATOM    152  C   LYS A  19     -14.311  90.870  13.264  1.00  8.86           C  
ANISOU  152  C   LYS A  19     1638    665   1065   -107    118   -391       C  
ATOM    153  O   LYS A  19     -13.424  91.616  13.683  1.00 11.01           O  
ANISOU  153  O   LYS A  19     1938    883   1361   -168    133   -365       O  
ATOM    154  CB  LYS A  19     -16.729  91.335  13.780  1.00 11.61           C  
ANISOU  154  CB  LYS A  19     1845   1093   1473    -32    -19   -485       C  
ATOM    155  CG  LYS A  19     -16.356  91.969  15.082  1.00 18.71           C  
ANISOU  155  CG  LYS A  19     2700   1989   2419    -50    -33   -476       C  
ATOM    156  CD  LYS A  19     -17.489  91.840  16.090  1.00 25.18           C  
ANISOU  156  CD  LYS A  19     3480   2858   3232    -66      4   -492       C  
ATOM    157  CE  LYS A  19     -17.155  92.577  17.365  1.00 31.52           C  
ANISOU  157  CE  LYS A  19     4302   3648   4026    -91     -2   -478       C  
ATOM    158  NZ  LYS A  19     -18.346  93.328  17.843  1.00 46.95           N  
ANISOU  158  NZ  LYS A  19     6300   5587   5951    -62    -58   -508       N  
ATOM    159  N   ALA A  20     -14.171  89.540  13.221  1.00 10.22           N  
ANISOU  159  N   ALA A  20     1765    876   1241    -86    184   -397       N  
ATOM    160  CA  ALA A  20     -12.944  88.908  13.687  1.00  9.62           C  
ANISOU  160  CA  ALA A  20     1665    784   1206   -117    297   -381       C  
ATOM    161  C   ALA A  20     -11.749  89.385  12.880  1.00 14.59           C  
ANISOU  161  C   ALA A  20     2374   1344   1826   -190    432   -371       C  
ATOM    162  O   ALA A  20     -10.693  89.690  13.443  1.00 15.55           O  
ANISOU  162  O   ALA A  20     2423   1457   2027   -238    467   -341       O  
ATOM    163  CB  ALA A  20     -13.074  87.388  13.604  1.00 10.31           C  
ANISOU  163  CB  ALA A  20     1703    909   1304    -72    345   -387       C  
ATOM    164  N   MET A  21     -11.898  89.477  11.561  1.00 10.35           N  
ANISOU  164  N   MET A  21     1947    791   1195   -199    487   -369       N  
ATOM    165  CA  MET A  21     -10.787  89.943  10.731  1.00 15.05           C  
ANISOU  165  CA  MET A  21     2582   1371   1764   -270    616   -311       C  
ATOM    166  C   MET A  21     -10.460  91.402  10.992  1.00 18.74           C  
ANISOU  166  C   MET A  21     3073   1791   2258   -357    550   -240       C  
ATOM    167  O   MET A  21      -9.283  91.780  11.047  1.00 15.08           O  
ANISOU  167  O   MET A  21     2524   1343   1864   -438    629   -176       O  
ATOM    168  CB  MET A  21     -11.117  89.730   9.261  1.00 14.33           C  
ANISOU  168  CB  MET A  21     2641   1279   1524   -255    686   -323       C  
ATOM    169  CG  MET A  21     -11.206  88.217   8.943  1.00 15.76           C  
ANISOU  169  CG  MET A  21     2760   1515   1713   -181    746   -378       C  
ATOM    170  SD  MET A  21     -11.425  87.928   7.224  1.00 18.06           S  
ANISOU  170  SD  MET A  21     3181   1830   1852   -166    792   -379       S  
ATOM    171  CE  MET A  21      -9.785  88.345   6.564  1.00 16.87           C  
ANISOU  171  CE  MET A  21     3049   1700   1663   -245   1037   -316       C  
ATOM    172  N   LYS A  22     -11.479  92.249  11.105  1.00 11.73           N  
ANISOU  172  N   LYS A  22     2296    837   1325   -344    406   -258       N  
ATOM    173  CA  LYS A  22     -11.212  93.673  11.274  1.00 12.44           C  
ANISOU  173  CA  LYS A  22     2438    848   1441   -424    339   -194       C  
ATOM    174  C   LYS A  22     -10.576  93.962  12.629  1.00 12.12           C  
ANISOU  174  C   LYS A  22     2247    819   1541   -468    292   -202       C  
ATOM    175  O   LYS A  22      -9.858  94.965  12.783  1.00 13.07           O  
ANISOU  175  O   LYS A  22     2360    887   1720   -569    282   -147       O  
ATOM    176  CB  LYS A  22     -12.515  94.454  11.073  1.00 12.36           C  
ANISOU  176  CB  LYS A  22     2555    782   1358   -357    180   -217       C  
ATOM    177  CG  LYS A  22     -12.942  94.437   9.582  1.00 14.50           C  
ANISOU  177  CG  LYS A  22     3033   1007   1468   -341    210   -194       C  
ATOM    178  CD  LYS A  22     -14.358  94.960   9.375  1.00 21.00           C  
ANISOU  178  CD  LYS A  22     3910   1831   2236   -230     30   -222       C  
ATOM    179  CE  LYS A  22     -14.468  96.423   9.734  1.00 30.36           C  
ANISOU  179  CE  LYS A  22     5145   2928   3461   -246    -81   -172       C  
ATOM    180  NZ  LYS A  22     -15.914  96.851   9.698  1.00 44.59           N  
ANISOU  180  NZ  LYS A  22     6948   4747   5246   -119   -247   -216       N  
ATOM    181  N   GLU A  23     -10.833  93.108  13.628  1.00 11.03           N  
ANISOU  181  N   GLU A  23     1998    741   1451   -399    257   -270       N  
ATOM    182  CA  GLU A  23     -10.213  93.294  14.942  1.00 10.93           C  
ANISOU  182  CA  GLU A  23     1856    754   1544   -428    198   -280       C  
ATOM    183  C   GLU A  23      -8.711  93.037  14.912  1.00 11.89           C  
ANISOU  183  C   GLU A  23     1832    932   1754   -492    298   -224       C  
ATOM    184  O   GLU A  23      -8.014  93.418  15.865  1.00 12.30           O  
ANISOU  184  O   GLU A  23     1774   1003   1899   -537    233   -227       O  
ATOM    185  CB  GLU A  23     -10.871  92.363  15.965  1.00 10.56           C  
ANISOU  185  CB  GLU A  23     1753    764   1497   -332    149   -346       C  
ATOM    186  CG  GLU A  23     -12.262  92.829  16.347  1.00 11.62           C  
ANISOU  186  CG  GLU A  23     1893    934   1587   -236     16   -372       C  
ATOM    187  CD  GLU A  23     -12.954  91.875  17.330  1.00 18.40           C  
ANISOU  187  CD  GLU A  23     2684   1867   2438   -153    -15   -403       C  
ATOM    188  OE1 GLU A  23     -13.948  92.291  17.954  1.00 20.39           O  
ANISOU  188  OE1 GLU A  23     2878   2169   2701   -101    -81   -434       O  
ATOM    189  OE2 GLU A  23     -12.517  90.712  17.449  1.00 19.15           O  
ANISOU  189  OE2 GLU A  23     2763   1980   2533   -151     69   -397       O  
ATOM    190  N   TYR A  24      -8.202  92.447  13.829  1.00 14.09           N  
ANISOU  190  N   TYR A  24     2104   1244   2008   -497    450   -186       N  
ATOM    191  CA  TYR A  24      -6.768  92.247  13.635  1.00 13.77           C  
ANISOU  191  CA  TYR A  24     1907   1264   2062   -557    571   -143       C  
ATOM    192  C   TYR A  24      -6.236  93.044  12.450  1.00 19.84           C  
ANISOU  192  C   TYR A  24     2741   1998   2798   -675    694    -73       C  
ATOM    193  O   TYR A  24      -5.125  92.791  11.965  1.00 21.45           O  
ANISOU  193  O   TYR A  24     2825   2263   3062   -727    847    -42       O  
ATOM    194  CB  TYR A  24      -6.486  90.744  13.510  1.00 17.59           C  
ANISOU  194  CB  TYR A  24     2299   1824   2560   -450    669   -170       C  
ATOM    195  CG  TYR A  24      -6.666  90.097  14.859  1.00 19.44           C  
ANISOU  195  CG  TYR A  24     2451   2084   2850   -363    552   -209       C  
ATOM    196  CD1 TYR A  24      -5.611  90.029  15.768  1.00 32.18           C  
ANISOU  196  CD1 TYR A  24     3884   3755   4587   -367    507   -199       C  
ATOM    197  CD2 TYR A  24      -7.914  89.637  15.267  1.00 17.31           C  
ANISOU  197  CD2 TYR A  24     2288   1784   2505   -286    478   -254       C  
ATOM    198  CE1 TYR A  24      -5.788  89.491  17.020  1.00 31.12           C  
ANISOU  198  CE1 TYR A  24     3710   3643   4471   -285    389   -220       C  
ATOM    199  CE2 TYR A  24      -8.102  89.089  16.515  1.00 26.84           C  
ANISOU  199  CE2 TYR A  24     3447   3010   3739   -221    388   -275       C  
ATOM    200  CZ  TYR A  24      -7.039  89.020  17.395  1.00 40.30           C  
ANISOU  200  CZ  TYR A  24     5005   4768   5540   -216    340   -251       C  
ATOM    201  OH  TYR A  24      -7.235  88.485  18.659  1.00 43.63           O  
ANISOU  201  OH  TYR A  24     5412   5209   5958   -145    242   -258       O  
ATOM    202  N   GLY A  25      -6.992  94.040  11.997  1.00 15.32           N  
ANISOU  202  N   GLY A  25     2360   1325   2135   -718    633    -43       N  
ATOM    203  CA  GLY A  25      -6.538  94.875  10.908  1.00 16.99           C  
ANISOU  203  CA  GLY A  25     2677   1482   2295   -839    745     46       C  
ATOM    204  C   GLY A  25      -6.555  94.217   9.550  1.00 17.63           C  
ANISOU  204  C   GLY A  25     2856   1605   2237   -808    912     72       C  
ATOM    205  O   GLY A  25      -5.878  94.706   8.653  1.00 21.17           O  
ANISOU  205  O   GLY A  25     3351   2049   2645   -907   1049    149       O  
ATOM    206  N   GLU A  26      -7.305  93.115   9.372  1.00 16.45           N  
ANISOU  206  N   GLU A  26     2739   1503   2009   -670    900      0       N  
ATOM    207  CA  GLU A  26      -7.400  92.420   8.096  1.00 20.86           C  
ANISOU  207  CA  GLU A  26     3404   2102   2421   -629   1042     -3       C  
ATOM    208  C   GLU A  26      -8.694  92.775   7.377  1.00 22.40           C  
ANISOU  208  C   GLU A  26     3847   2227   2435   -578    933     -6       C  
ATOM    209  O   GLU A  26      -9.748  92.926   7.997  1.00 21.76           O  
ANISOU  209  O   GLU A  26     3801   2102   2365   -509    750    -58       O  
ATOM    210  CB  GLU A  26      -7.317  90.905   8.296  1.00 26.24           C  
ANISOU  210  CB  GLU A  26     3959   2868   3144   -514   1101    -95       C  
ATOM    211  CG  GLU A  26      -5.994  90.452   8.895  1.00 32.54           C  
ANISOU  211  CG  GLU A  26     4508   3741   4117   -533   1203    -95       C  
ATOM    212  CD  GLU A  26      -6.071  89.081   9.564  1.00 42.24           C  
ANISOU  212  CD  GLU A  26     5616   5010   5423   -399   1181   -176       C  
ATOM    213  OE1 GLU A  26      -5.015  88.576   9.987  1.00 41.22           O  
ANISOU  213  OE1 GLU A  26     5288   4942   5432   -380   1252   -182       O  
ATOM    214  OE2 GLU A  26      -7.180  88.510   9.676  1.00 43.10           O  
ANISOU  214  OE2 GLU A  26     5826   5084   5465   -314   1090   -234       O  
ATOM    215  N   ASP A  27      -8.610  92.897   6.059  1.00 22.81           N  
ANISOU  215  N   ASP A  27     4068   2280   2318   -605   1047     45       N  
ATOM    216  CA  ASP A  27      -9.753  93.280   5.242  1.00 19.46           C  
ANISOU  216  CA  ASP A  27     3895   1796   1702   -549    932     52       C  
ATOM    217  C   ASP A  27     -10.350  92.035   4.611  1.00 19.59           C  
ANISOU  217  C   ASP A  27     3953   1885   1606   -437    952    -57       C  
ATOM    218  O   ASP A  27      -9.661  91.352   3.830  1.00 22.53           O  
ANISOU  218  O   ASP A  27     4289   2328   1942   -437   1108    -68       O  
ATOM    219  CB  ASP A  27      -9.331  94.264   4.157  1.00 25.29           C  
ANISOU  219  CB  ASP A  27     4818   2485   2307   -641   1010    179       C  
ATOM    220  CG  ASP A  27     -10.517  94.861   3.393  1.00 40.79           C  
ANISOU  220  CG  ASP A  27     7055   4367   4078   -571    844    204       C  
ATOM    221  OD1 ASP A  27     -11.625  94.280   3.389  1.00 30.65           O  
ANISOU  221  OD1 ASP A  27     5826   3098   2721   -450    709    107       O  
ATOM    222  OD2 ASP A  27     -10.337  95.931   2.772  1.00 40.67           O  
ANISOU  222  OD2 ASP A  27     7168   4280   4003   -625    828    307       O  
ATOM    223  N   PRO A  28     -11.614  91.717   4.896  1.00 22.09           N  
ANISOU  223  N   PRO A  28     4299   2185   1910   -334    767   -153       N  
ATOM    224  CA  PRO A  28     -12.216  90.497   4.323  1.00 22.41           C  
ANISOU  224  CA  PRO A  28     4311   2287   1917   -239    743   -254       C  
ATOM    225  C   PRO A  28     -12.280  90.494   2.807  1.00 23.34           C  
ANISOU  225  C   PRO A  28     4582   2426   1860   -226    770   -225       C  
ATOM    226  O   PRO A  28     -12.333  89.413   2.206  1.00 23.07           O  
ANISOU  226  O   PRO A  28     4483   2460   1823   -175    799   -292       O  
ATOM    227  CB  PRO A  28     -13.626  90.489   4.929  1.00 23.92           C  
ANISOU  227  CB  PRO A  28     4445   2465   2180   -159    509   -318       C  
ATOM    228  CG  PRO A  28     -13.517  91.313   6.177  1.00 29.57           C  
ANISOU  228  CG  PRO A  28     5121   3117   2997   -197    459   -302       C  
ATOM    229  CD  PRO A  28     -12.498  92.380   5.868  1.00 25.80           C  
ANISOU  229  CD  PRO A  28     4741   2587   2475   -301    556   -174       C  
ATOM    230  N   LYS A  29     -12.295  91.663   2.168  1.00 21.45           N  
ANISOU  230  N   LYS A  29     4549   2126   1475   -268    749   -125       N  
ATOM    231  CA  LYS A  29     -12.319  91.739   0.712  1.00 24.01           C  
ANISOU  231  CA  LYS A  29     5031   2470   1622   -255    773    -89       C  
ATOM    232  C   LYS A  29     -10.961  91.467   0.086  1.00 30.55           C  
ANISOU  232  C   LYS A  29     5809   3362   2438   -328   1014    -44       C  
ATOM    233  O   LYS A  29     -10.890  91.261  -1.132  1.00 34.68           O  
ANISOU  233  O   LYS A  29     6436   3929   2812   -311   1062    -39       O  
ATOM    234  CB  LYS A  29     -12.817  93.116   0.274  1.00 28.53           C  
ANISOU  234  CB  LYS A  29     5837   2942   2063   -265    647     17       C  
ATOM    235  CG  LYS A  29     -14.046  93.572   1.033  1.00 34.15           C  
ANISOU  235  CG  LYS A  29     6573   3581   2820   -186    401    -25       C  
ATOM    236  CD  LYS A  29     -14.482  94.967   0.613  1.00 47.25           C  
ANISOU  236  CD  LYS A  29     8460   5120   4373   -177    259     85       C  
ATOM    237  CE  LYS A  29     -15.965  94.994   0.276  1.00 51.18           C  
ANISOU  237  CE  LYS A  29     9013   5603   4830    -29      1      9       C  
ATOM    238  NZ  LYS A  29     -16.288  94.070  -0.856  1.00 51.01           N  
ANISOU  238  NZ  LYS A  29     8992   5685   4705     26     12    -56       N  
ATOM    239  N   ILE A  30      -9.890  91.440   0.877  1.00 24.42           N  
ANISOU  239  N   ILE A  30     4858   2604   1818   -402   1157    -20       N  
ATOM    240  CA  ILE A  30      -8.537  91.200   0.383  1.00 28.80           C  
ANISOU  240  CA  ILE A  30     5306   3232   2403   -464   1375     12       C  
ATOM    241  C   ILE A  30      -8.034  89.812   0.775  1.00 27.11           C  
ANISOU  241  C   ILE A  30     4871   3100   2329   -402   1454    -96       C  
ATOM    242  O   ILE A  30      -7.581  89.034  -0.070  1.00 26.37           O  
ANISOU  242  O   ILE A  30     4754   3080   2185   -367   1558   -141       O  
ATOM    243  CB  ILE A  30      -7.578  92.300   0.887  1.00 29.62           C  
ANISOU  243  CB  ILE A  30     5342   3303   2609   -596   1459    127       C  
ATOM    244  CG1 ILE A  30      -7.998  93.649   0.302  1.00 32.46           C  
ANISOU  244  CG1 ILE A  30     5939   3567   2829   -652   1381    246       C  
ATOM    245  CG2 ILE A  30      -6.139  91.943   0.545  1.00 34.68           C  
ANISOU  245  CG2 ILE A  30     5808   4041   3326   -651   1674    137       C  
ATOM    246  CD1 ILE A  30      -7.627  94.841   1.157  1.00 43.56           C  
ANISOU  246  CD1 ILE A  30     7298   4886   4366   -761   1344    340       C  
ATOM    247  N   GLU A  31      -8.101  89.489   2.062  1.00 23.95           N  
ANISOU  247  N   GLU A  31     4316   2684   2102   -382   1400   -138       N  
ATOM    248  CA  GLU A  31      -7.706  88.176   2.558  1.00 23.64           C  
ANISOU  248  CA  GLU A  31     4077   2697   2208   -308   1437   -228       C  
ATOM    249  C   GLU A  31      -8.918  87.247   2.519  1.00 20.45           C  
ANISOU  249  C   GLU A  31     3713   2280   1777   -208   1286   -324       C  
ATOM    250  O   GLU A  31      -9.469  86.823   3.530  1.00 18.70           O  
ANISOU  250  O   GLU A  31     3402   2032   1670   -169   1177   -366       O  
ATOM    251  CB  GLU A  31      -7.122  88.312   3.956  1.00 21.31           C  
ANISOU  251  CB  GLU A  31     3593   2394   2111   -337   1445   -212       C  
ATOM    252  CG  GLU A  31      -6.126  89.478   4.036  1.00 33.16           C  
ANISOU  252  CG  GLU A  31     5046   3900   3653   -464   1542   -108       C  
ATOM    253  CD  GLU A  31      -5.079  89.278   5.110  1.00 50.11           C  
ANISOU  253  CD  GLU A  31     6931   6089   6018   -481   1588   -109       C  
ATOM    254  OE1 GLU A  31      -4.536  88.155   5.210  1.00 56.98           O  
ANISOU  254  OE1 GLU A  31     7656   7018   6976   -394   1637   -174       O  
ATOM    255  OE2 GLU A  31      -4.808  90.244   5.859  1.00 55.14           O  
ANISOU  255  OE2 GLU A  31     7510   6696   6744   -577   1552    -46       O  
ATOM    256  N   THR A  32      -9.338  86.937   1.302  1.00 22.56           N  
ANISOU  256  N   THR A  32     4105   2575   1892   -175   1276   -357       N  
ATOM    257  CA  THR A  32     -10.603  86.239   1.163  1.00 21.00           C  
ANISOU  257  CA  THR A  32     3936   2375   1668   -100   1109   -443       C  
ATOM    258  C   THR A  32     -10.498  84.775   1.573  1.00 21.52           C  
ANISOU  258  C   THR A  32     3839   2467   1872    -36   1108   -531       C  
ATOM    259  O   THR A  32     -11.496  84.195   1.989  1.00 19.31           O  
ANISOU  259  O   THR A  32     3511   2176   1650      5    964   -589       O  
ATOM    260  CB  THR A  32     -11.111  86.375  -0.262  1.00 27.17           C  
ANISOU  260  CB  THR A  32     4898   3184   2240    -83   1082   -459       C  
ATOM    261  OG1 THR A  32     -10.111  85.887  -1.165  1.00 26.55           O  
ANISOU  261  OG1 THR A  32     4823   3170   2096    -86   1258   -471       O  
ATOM    262  CG2 THR A  32     -11.377  87.845  -0.563  1.00 27.56           C  
ANISOU  262  CG2 THR A  32     5136   3182   2154   -135   1037   -355       C  
ATOM    263  N   ASN A  33      -9.318  84.153   1.479  1.00 24.12           N  
ANISOU  263  N   ASN A  33     4074   2830   2260    -24   1261   -539       N  
ATOM    264  CA  ASN A  33      -9.219  82.763   1.933  1.00 24.29           C  
ANISOU  264  CA  ASN A  33     3966   2853   2410     46   1245   -612       C  
ATOM    265  C   ASN A  33      -9.372  82.679   3.450  1.00 18.99           C  
ANISOU  265  C   ASN A  33     3173   2134   1907     48   1161   -582       C  
ATOM    266  O   ASN A  33     -10.011  81.756   3.978  1.00 19.55           O  
ANISOU  266  O   ASN A  33     3192   2182   2054     90   1060   -626       O  
ATOM    267  CB  ASN A  33      -7.884  82.134   1.501  1.00 22.70           C  
ANISOU  267  CB  ASN A  33     3688   2699   2237     77   1419   -632       C  
ATOM    268  CG  ASN A  33      -7.813  81.836   0.005  1.00 29.97           C  
ANISOU  268  CG  ASN A  33     4722   3678   2989     97   1499   -691       C  
ATOM    269  OD1 ASN A  33      -6.748  81.969  -0.615  1.00 32.65           O  
ANISOU  269  OD1 ASN A  33     5045   4077   3286     86   1667   -678       O  
ATOM    270  ND2 ASN A  33      -8.933  81.439  -0.582  1.00 24.95           N  
ANISOU  270  ND2 ASN A  33     4187   3037   2257    125   1381   -763       N  
ATOM    271  N   LYS A  34      -8.781  83.628   4.169  1.00 18.45           N  
ANISOU  271  N   LYS A  34     3061   2054   1894     -4   1206   -508       N  
ATOM    272  CA  LYS A  34      -8.958  83.685   5.617  1.00 21.92           C  
ANISOU  272  CA  LYS A  34     3404   2457   2470     -5   1124   -483       C  
ATOM    273  C   LYS A  34     -10.421  83.902   5.979  1.00 17.86           C  
ANISOU  273  C   LYS A  34     2944   1915   1928     -8    949   -496       C  
ATOM    274  O   LYS A  34     -10.943  83.264   6.903  1.00 14.28           O  
ANISOU  274  O   LYS A  34     2414   1448   1565     20    854   -507       O  
ATOM    275  CB  LYS A  34      -8.089  84.805   6.199  1.00 20.65           C  
ANISOU  275  CB  LYS A  34     3191   2296   2359    -69   1206   -416       C  
ATOM    276  CG  LYS A  34      -8.050  84.847   7.727  1.00 34.92           C  
ANISOU  276  CG  LYS A  34     4884   4077   4306    -61   1140   -400       C  
ATOM    277  CD  LYS A  34      -6.939  85.755   8.230  1.00 40.67           C  
ANISOU  277  CD  LYS A  34     5508   4831   5114   -123   1240   -348       C  
ATOM    278  CE  LYS A  34      -5.649  85.561   7.428  1.00 40.70           C  
ANISOU  278  CE  LYS A  34     5424   4901   5138   -129   1392   -333       C  
ATOM    279  NZ  LYS A  34      -4.506  86.333   8.003  1.00 46.65           N  
ANISOU  279  NZ  LYS A  34     6010   5700   6014   -200   1460   -278       N  
ATOM    280  N   PHE A  35     -11.081  84.810   5.261  1.00 16.56           N  
ANISOU  280  N   PHE A  35     2909   1748   1636    -39    904   -489       N  
ATOM    281  CA  PHE A  35     -12.513  85.067   5.408  1.00 17.68           C  
ANISOU  281  CA  PHE A  35     3080   1884   1752    -25    727   -515       C  
ATOM    282  C   PHE A  35     -13.299  83.768   5.312  1.00 14.65           C  
ANISOU  282  C   PHE A  35     2625   1527   1412     29    645   -592       C  
ATOM    283  O   PHE A  35     -14.097  83.445   6.205  1.00 15.72           O  
ANISOU  283  O   PHE A  35     2672   1664   1638     44    536   -606       O  
ATOM    284  CB  PHE A  35     -12.917  86.062   4.309  1.00 15.87           C  
ANISOU  284  CB  PHE A  35     3025   1649   1355    -45    705   -502       C  
ATOM    285  CG  PHE A  35     -14.295  86.671   4.426  1.00 15.22           C  
ANISOU  285  CG  PHE A  35     2971   1561   1251    -24    520   -523       C  
ATOM    286  CD1 PHE A  35     -15.000  86.715   5.617  1.00 13.92           C  
ANISOU  286  CD1 PHE A  35     2673   1400   1218    -11    407   -536       C  
ATOM    287  CD2 PHE A  35     -14.865  87.263   3.299  1.00 25.89           C  
ANISOU  287  CD2 PHE A  35     4483   2909   2443    -12    460   -527       C  
ATOM    288  CE1 PHE A  35     -16.245  87.336   5.672  1.00 16.05           C  
ANISOU  288  CE1 PHE A  35     2935   1677   1486     13    255   -568       C  
ATOM    289  CE2 PHE A  35     -16.115  87.857   3.350  1.00 26.51           C  
ANISOU  289  CE2 PHE A  35     4575   2983   2513     20    285   -552       C  
ATOM    290  CZ  PHE A  35     -16.807  87.891   4.548  1.00 20.97           C  
ANISOU  290  CZ  PHE A  35     3705   2293   1971     30    192   -579       C  
ATOM    291  N   ALA A  36     -13.067  83.002   4.233  1.00 16.01           N  
ANISOU  291  N   ALA A  36     2843   1722   1518     56    706   -647       N  
ATOM    292  CA  ALA A  36     -13.730  81.708   4.043  1.00 16.28           C  
ANISOU  292  CA  ALA A  36     2831   1766   1589    102    643   -735       C  
ATOM    293  C   ALA A  36     -13.428  80.741   5.182  1.00 15.48           C  
ANISOU  293  C   ALA A  36     2624   1629   1631    118    654   -716       C  
ATOM    294  O   ALA A  36     -14.325  80.025   5.656  1.00 17.05           O  
ANISOU  294  O   ALA A  36     2792   1800   1888    122    578   -750       O  
ATOM    295  CB  ALA A  36     -13.303  81.087   2.703  1.00 18.16           C  
ANISOU  295  CB  ALA A  36     3147   2030   1724    130    729   -803       C  
ATOM    296  N   ALA A  37     -12.170  80.681   5.628  1.00 15.57           N  
ANISOU  296  N   ALA A  37     2597   1623   1695    116    771   -663       N  
ATOM    297  CA  ALA A  37     -11.820  79.709   6.663  1.00 16.70           C  
ANISOU  297  CA  ALA A  37     2659   1727   1960    142    780   -646       C  
ATOM    298  C   ALA A  37     -12.495  80.040   7.989  1.00 15.89           C  
ANISOU  298  C   ALA A  37     2506   1611   1921    114    682   -596       C  
ATOM    299  O   ALA A  37     -12.962  79.145   8.707  1.00 15.31           O  
ANISOU  299  O   ALA A  37     2408   1499   1911    120    650   -600       O  
ATOM    300  CB  ALA A  37     -10.303  79.666   6.838  1.00 17.72           C  
ANISOU  300  CB  ALA A  37     2738   1853   2141    166    916   -613       C  
ATOM    301  N   ILE A  38     -12.531  81.316   8.351  1.00 13.38           N  
ANISOU  301  N   ILE A  38     2188   1311   1585     77    657   -550       N  
ATOM    302  CA  ILE A  38     -13.192  81.698   9.597  1.00 12.55           C  
ANISOU  302  CA  ILE A  38     2035   1205   1528     58    564   -513       C  
ATOM    303  C   ILE A  38     -14.677  81.342   9.547  1.00 11.49           C  
ANISOU  303  C   ILE A  38     1913   1071   1384     50    474   -558       C  
ATOM    304  O   ILE A  38     -15.239  80.830  10.526  1.00 11.13           O  
ANISOU  304  O   ILE A  38     1832   1004   1393     34    454   -547       O  
ATOM    305  CB  ILE A  38     -12.975  83.196   9.877  1.00 11.29           C  
ANISOU  305  CB  ILE A  38     1888   1055   1346     22    556   -474       C  
ATOM    306  CG1 ILE A  38     -11.491  83.460  10.137  1.00 11.46           C  
ANISOU  306  CG1 ILE A  38     1887   1057   1411     13    684   -440       C  
ATOM    307  CG2 ILE A  38     -13.847  83.667  11.053  1.00 12.39           C  
ANISOU  307  CG2 ILE A  38     1983   1207   1519     14    443   -456       C  
ATOM    308  CD1 ILE A  38     -11.146  84.936  10.109  1.00 14.83           C  
ANISOU  308  CD1 ILE A  38     2356   1474   1805    -40    714   -416       C  
ATOM    309  N   CYS A  39     -15.332  81.617   8.410  1.00 12.12           N  
ANISOU  309  N   CYS A  39     2045   1169   1390     58    432   -617       N  
ATOM    310  CA  CYS A  39     -16.747  81.272   8.261  1.00 12.44           C  
ANISOU  310  CA  CYS A  39     2091   1206   1428     59    347   -683       C  
ATOM    311  C   CYS A  39     -16.957  79.775   8.399  1.00 13.08           C  
ANISOU  311  C   CYS A  39     2169   1241   1562     52    390   -717       C  
ATOM    312  O   CYS A  39     -17.945  79.323   8.992  1.00 13.06           O  
ANISOU  312  O   CYS A  39     2142   1217   1603     25    358   -737       O  
ATOM    313  CB  CYS A  39     -17.269  81.722   6.902  1.00 13.34           C  
ANISOU  313  CB  CYS A  39     2265   1354   1452     86    287   -761       C  
ATOM    314  SG  CYS A  39     -17.536  83.501   6.743  1.00 14.23           S  
ANISOU  314  SG  CYS A  39     2385   1508   1514     83    212   -744       S  
ATOM    315  N   THR A  40     -16.068  78.993   7.798  1.00 13.90           N  
ANISOU  315  N   THR A  40     2300   1322   1658     74    471   -735       N  
ATOM    316  CA  THR A  40     -16.248  77.546   7.814  1.00 14.80           C  
ANISOU  316  CA  THR A  40     2426   1375   1823     74    510   -782       C  
ATOM    317  C   THR A  40     -16.133  77.009   9.241  1.00 14.18           C  
ANISOU  317  C   THR A  40     2299   1252   1839     48    545   -717       C  
ATOM    318  O   THR A  40     -16.930  76.168   9.669  1.00 14.58           O  
ANISOU  318  O   THR A  40     2348   1253   1938     16    545   -745       O  
ATOM    319  CB  THR A  40     -15.208  76.903   6.890  1.00 16.81           C  
ANISOU  319  CB  THR A  40     2721   1617   2051    122    592   -820       C  
ATOM    320  OG1 THR A  40     -15.441  77.305   5.530  1.00 16.84           O  
ANISOU  320  OG1 THR A  40     2785   1668   1947    143    564   -894       O  
ATOM    321  CG2 THR A  40     -15.323  75.382   6.933  1.00 19.97           C  
ANISOU  321  CG2 THR A  40     3141   1933   2512    132    631   -875       C  
ATOM    322  N   HIS A  41     -15.145  77.498   9.996  1.00 13.39           N  
ANISOU  322  N   HIS A  41     2162   1165   1760     63    576   -637       N  
ATOM    323  CA  HIS A  41     -14.963  77.038  11.358  1.00 12.98           C  
ANISOU  323  CA  HIS A  41     2080   1073   1778     58    597   -579       C  
ATOM    324  C   HIS A  41     -16.161  77.418  12.217  1.00 12.29           C  
ANISOU  324  C   HIS A  41     1969   1002   1697      1    548   -568       C  
ATOM    325  O   HIS A  41     -16.652  76.603  12.995  1.00 12.57           O  
ANISOU  325  O   HIS A  41     2009    989   1780    -25    575   -564       O  
ATOM    326  CB  HIS A  41     -13.654  77.609  11.904  1.00 12.85           C  
ANISOU  326  CB  HIS A  41     2028   1078   1776     99    618   -515       C  
ATOM    327  CG  HIS A  41     -13.512  77.543  13.397  1.00 15.03           C  
ANISOU  327  CG  HIS A  41     2280   1333   2097    105    606   -455       C  
ATOM    328  ND1 HIS A  41     -13.974  78.522  14.244  1.00 18.20           N  
ANISOU  328  ND1 HIS A  41     2697   1657   2560    150    654   -434       N  
ATOM    329  CD2 HIS A  41     -12.982  76.581  14.176  1.00 10.90           C  
ANISOU  329  CD2 HIS A  41     1733    847   1562     78    557   -417       C  
ATOM    330  CE1 HIS A  41     -13.734  78.165  15.507  1.00 12.26           C  
ANISOU  330  CE1 HIS A  41     1942    890   1827    149    646   -379       C  
ATOM    331  NE2 HIS A  41     -13.130  76.992  15.477  1.00 13.89           N  
ANISOU  331  NE2 HIS A  41     2122   1169   1986    102    589   -375       N  
ATOM    332  N   LEU A  42     -16.666  78.642  12.056  1.00 11.95           N  
ANISOU  332  N   LEU A  42     1908   1022   1609    -14    482   -569       N  
ATOM    333  CA  LEU A  42     -17.890  79.036  12.759  1.00 11.20           C  
ANISOU  333  CA  LEU A  42     1782    950   1524    -55    437   -578       C  
ATOM    334  C   LEU A  42     -19.051  78.101  12.417  1.00 12.19           C  
ANISOU  334  C   LEU A  42     1913   1044   1676    -92    443   -653       C  
ATOM    335  O   LEU A  42     -19.780  77.633  13.304  1.00 13.26           O  
ANISOU  335  O   LEU A  42     2020   1158   1857   -140    475   -657       O  
ATOM    336  CB  LEU A  42     -18.246  80.482  12.398  1.00 10.66           C  
ANISOU  336  CB  LEU A  42     1706    940   1404    -41    353   -584       C  
ATOM    337  CG  LEU A  42     -17.488  81.582  13.120  1.00 24.78           C  
ANISOU  337  CG  LEU A  42     3475   2756   3182    -29    337   -520       C  
ATOM    338  CD1 LEU A  42     -17.697  82.949  12.426  1.00 20.70           C  
ANISOU  338  CD1 LEU A  42     2978   2273   2613     -5    257   -535       C  
ATOM    339  CD2 LEU A  42     -17.946  81.631  14.576  1.00 32.87           C  
ANISOU  339  CD2 LEU A  42     4463   3786   4240    -54    339   -495       C  
ATOM    340  N   GLU A  43     -19.260  77.823  11.130  1.00 12.99           N  
ANISOU  340  N   GLU A  43     2052   1138   1745    -75    416   -723       N  
ATOM    341  CA  GLU A  43     -20.402  76.981  10.796  1.00 14.07           C  
ANISOU  341  CA  GLU A  43     2192   1242   1913   -115    410   -810       C  
ATOM    342  C   GLU A  43     -20.254  75.597  11.413  1.00 14.74           C  
ANISOU  342  C   GLU A  43     2284   1244   2071   -151    503   -807       C  
ATOM    343  O   GLU A  43     -21.225  75.048  11.934  1.00 15.28           O  
ANISOU  343  O   GLU A  43     2325   1284   2196   -215    529   -843       O  
ATOM    344  CB  GLU A  43     -20.599  76.873   9.291  1.00 25.02           C  
ANISOU  344  CB  GLU A  43     3641   2627   3237    -80    353   -897       C  
ATOM    345  CG  GLU A  43     -21.989  76.280   9.007  1.00 33.17           C  
ANISOU  345  CG  GLU A  43     4666   3637   4302   -132    318   -999       C  
ATOM    346  CD  GLU A  43     -22.351  76.186   7.540  1.00 35.75           C  
ANISOU  346  CD  GLU A  43     5077   3956   4551    -98    239  -1098       C  
ATOM    347  OE1 GLU A  43     -21.847  76.979   6.724  1.00 42.73           O  
ANISOU  347  OE1 GLU A  43     6028   4874   5332    -26    185  -1089       O  
ATOM    348  OE2 GLU A  43     -23.157  75.293   7.206  1.00 47.41           O  
ANISOU  348  OE2 GLU A  43     6559   5389   6064   -146    233  -1194       O  
ATOM    349  N   VAL A  44     -19.034  75.043  11.405  1.00 14.86           N  
ANISOU  349  N   VAL A  44     2339   1214   2092   -108    558   -764       N  
ATOM    350  CA  VAL A  44     -18.811  73.726  12.011  1.00 15.69           C  
ANISOU  350  CA  VAL A  44     2476   1218   2267   -120    637   -753       C  
ATOM    351  C   VAL A  44     -19.087  73.772  13.509  1.00 15.12           C  
ANISOU  351  C   VAL A  44     2381   1134   2229   -159    673   -684       C  
ATOM    352  O   VAL A  44     -19.732  72.874  14.060  1.00 15.97           O  
ANISOU  352  O   VAL A  44     2509   1168   2391   -212    726   -700       O  
ATOM    353  CB  VAL A  44     -17.386  73.214  11.721  1.00 16.09           C  
ANISOU  353  CB  VAL A  44     2568   1223   2322    -41    678   -725       C  
ATOM    354  CG1 VAL A  44     -17.115  71.936  12.556  1.00 17.95           C  
ANISOU  354  CG1 VAL A  44     2849   1338   2634    -33    744   -697       C  
ATOM    355  CG2 VAL A  44     -17.222  72.916  10.238  1.00 17.11           C  
ANISOU  355  CG2 VAL A  44     2737   1350   2415     -7    667   -816       C  
ATOM    356  N   CYS A  45     -18.623  74.824  14.197  1.00 13.84           N  
ANISOU  356  N   CYS A  45     2189   1038   2033   -136    647   -612       N  
ATOM    357  CA  CYS A  45     -18.920  74.936  15.633  1.00 15.53           C  
ANISOU  357  CA  CYS A  45     2397   1245   2261   -166    676   -557       C  
ATOM    358  C   CYS A  45     -20.422  74.932  15.896  1.00 14.11           C  
ANISOU  358  C   CYS A  45     2177   1081   2102   -251    692   -616       C  
ATOM    359  O   CYS A  45     -20.909  74.244  16.807  1.00 14.40           O  
ANISOU  359  O   CYS A  45     2239   1059   2174   -301    765   -607       O  
ATOM    360  CB  CYS A  45     -18.307  76.210  16.211  1.00 12.14           C  
ANISOU  360  CB  CYS A  45     1938    890   1786   -130    626   -497       C  
ATOM    361  SG  CYS A  45     -16.519  76.134  16.373  1.00 13.32           S  
ANISOU  361  SG  CYS A  45     2115   1012   1935    -35    625   -428       S  
ATOM    362  N   PHE A  46     -21.180  75.708  15.107  1.00 13.59           N  
ANISOU  362  N   PHE A  46     2053   1091   2019   -265    625   -681       N  
ATOM    363  CA  PHE A  46     -22.627  75.768  15.306  1.00 18.68           C  
ANISOU  363  CA  PHE A  46     2634   1762   2700   -337    633   -755       C  
ATOM    364  C   PHE A  46     -23.294  74.428  14.976  1.00 22.69           C  
ANISOU  364  C   PHE A  46     3158   2188   3274   -400    692   -830       C  
ATOM    365  O   PHE A  46     -24.184  73.970  15.707  1.00 20.59           O  
ANISOU  365  O   PHE A  46     2866   1897   3062   -478    766   -862       O  
ATOM    366  CB  PHE A  46     -23.223  76.898  14.469  1.00 17.26           C  
ANISOU  366  CB  PHE A  46     2398   1670   2490   -312    526   -810       C  
ATOM    367  CG  PHE A  46     -22.735  78.293  14.861  1.00 16.61           C  
ANISOU  367  CG  PHE A  46     2303   1654   2354   -260    467   -746       C  
ATOM    368  CD1 PHE A  46     -22.033  78.512  16.026  1.00 29.77           C  
ANISOU  368  CD1 PHE A  46     3986   3316   4009   -253    506   -665       C  
ATOM    369  CD2 PHE A  46     -22.986  79.379  14.036  1.00 29.06           C  
ANISOU  369  CD2 PHE A  46     3869   3284   3887   -214    364   -774       C  
ATOM    370  CE1 PHE A  46     -21.602  79.800  16.381  1.00 36.45           C  
ANISOU  370  CE1 PHE A  46     4823   4216   4811   -210    445   -621       C  
ATOM    371  CE2 PHE A  46     -22.563  80.656  14.376  1.00 30.33           C  
ANISOU  371  CE2 PHE A  46     4032   3487   4006   -170    311   -721       C  
ATOM    372  CZ  PHE A  46     -21.865  80.864  15.549  1.00 33.17           C  
ANISOU  372  CZ  PHE A  46     4392   3846   4364   -172    351   -648       C  
ATOM    373  N   MET A  47     -22.876  73.776  13.885  1.00 19.04           N  
ANISOU  373  N   MET A  47     2745   1678   2810   -372    669   -866       N  
ATOM    374  CA  MET A  47     -23.380  72.449  13.561  1.00 18.05           C  
ANISOU  374  CA  MET A  47     2652   1454   2752   -429    719   -940       C  
ATOM    375  C   MET A  47     -23.092  71.449  14.668  1.00 26.45           C  
ANISOU  375  C   MET A  47     3779   2407   3864   -461    829   -876       C  
ATOM    376  O   MET A  47     -23.935  70.595  14.968  1.00 25.84           O  
ANISOU  376  O   MET A  47     3706   2256   3856   -549    894   -926       O  
ATOM    377  CB  MET A  47     -22.767  71.932  12.252  1.00 18.77           C  
ANISOU  377  CB  MET A  47     2808   1503   2820   -375    676   -988       C  
ATOM    378  CG  MET A  47     -23.281  72.630  11.009  1.00 25.25           C  
ANISOU  378  CG  MET A  47     3607   2401   3587   -353    567  -1075       C  
ATOM    379  SD  MET A  47     -22.559  71.860   9.535  1.00 29.40           S  
ANISOU  379  SD  MET A  47     4238   2864   4070   -290    538  -1145       S  
ATOM    380  CE  MET A  47     -23.452  70.316   9.428  1.00 33.45           C  
ANISOU  380  CE  MET A  47     4775   3250   4684   -383    581  -1258       C  
ATOM    381  N   TYR A  48     -21.874  71.488  15.220  1.00 17.89           N  
ANISOU  381  N   TYR A  48     2754   1298   2747   -388    844   -770       N  
ATOM    382  CA  TYR A  48     -21.489  70.570  16.285  1.00 18.80           C  
ANISOU  382  CA  TYR A  48     2955   1287   2900   -402    951   -700       C  
ATOM    383  C   TYR A  48     -22.406  70.728  17.485  1.00 19.13           C  
ANISOU  383  C   TYR A  48     2985   1328   2955   -498   1052   -691       C  
ATOM    384  O   TYR A  48     -22.898  69.738  18.040  1.00 27.09           O  
ANISOU  384  O   TYR A  48     4056   2218   4018   -576   1162   -696       O  
ATOM    385  CB  TYR A  48     -20.039  70.836  16.668  1.00 19.49           C  
ANISOU  385  CB  TYR A  48     3089   1368   2947   -295    934   -598       C  
ATOM    386  CG  TYR A  48     -19.270  69.709  17.313  1.00 20.49           C  
ANISOU  386  CG  TYR A  48     3332   1337   3117   -254   1006   -527       C  
ATOM    387  CD1 TYR A  48     -19.520  69.347  18.630  1.00 20.16           C  
ANISOU  387  CD1 TYR A  48     3369   1210   3081   -296   1099   -454       C  
ATOM    388  CD2 TYR A  48     -18.265  69.041  16.623  1.00 20.00           C  
ANISOU  388  CD2 TYR A  48     3309   1207   3083   -162    978   -528       C  
ATOM    389  CE1 TYR A  48     -18.814  68.343  19.244  1.00 21.63           C  
ANISOU  389  CE1 TYR A  48     3680   1239   3300   -242   1141   -368       C  
ATOM    390  CE2 TYR A  48     -17.528  68.044  17.236  1.00 23.15           C  
ANISOU  390  CE2 TYR A  48     3812   1453   3531   -102   1023   -457       C  
ATOM    391  CZ  TYR A  48     -17.820  67.696  18.556  1.00 22.26           C  
ANISOU  391  CZ  TYR A  48     3786   1249   3423   -140   1095   -368       C  
ATOM    392  OH  TYR A  48     -17.113  66.695  19.195  1.00 25.86           O  
ANISOU  392  OH  TYR A  48     4364   1538   3924    -69   1120   -277       O  
ATOM    393  N   SER A  49     -22.653  71.970  17.892  1.00 17.78           N  
ANISOU  393  N   SER A  49     2741   1280   2733   -497   1020   -682       N  
ATOM    394  CA  SER A  49     -23.513  72.234  19.039  1.00 21.84           C  
ANISOU  394  CA  SER A  49     3242   1807   3251   -584   1128   -692       C  
ATOM    395  C   SER A  49     -24.943  71.773  18.809  1.00 31.21           C  
ANISOU  395  C   SER A  49     4356   2988   4515   -701   1192   -814       C  
ATOM    396  O   SER A  49     -25.653  71.496  19.783  1.00 42.29           O  
ANISOU  396  O   SER A  49     5777   4352   5940   -795   1331   -833       O  
ATOM    397  CB  SER A  49     -23.470  73.718  19.372  1.00 30.64           C  
ANISOU  397  CB  SER A  49     4284   3055   4303   -550   1061   -677       C  
ATOM    398  OG  SER A  49     -24.130  74.481  18.384  1.00 38.29           O  
ANISOU  398  OG  SER A  49     5131   4133   5283   -540    943   -757       O  
ATOM    399  N   ASP A  50     -25.380  71.672  17.553  1.00 31.52           N  
ANISOU  399  N   ASP A  50     4323   3061   4593   -699   1095   -903       N  
ATOM    400  CA  ASP A  50     -26.699  71.139  17.221  1.00 35.66           C  
ANISOU  400  CA  ASP A  50     4772   3572   5207   -808   1139  -1034       C  
ATOM    401  C   ASP A  50     -26.742  69.617  17.146  1.00 43.29           C  
ANISOU  401  C   ASP A  50     5831   4372   6245   -875   1221  -1047       C  
ATOM    402  O   ASP A  50     -27.829  69.057  16.977  1.00 50.67           O  
ANISOU  402  O   ASP A  50     6709   5275   7267   -986   1271  -1157       O  
ATOM    403  CB  ASP A  50     -27.177  71.708  15.880  1.00 35.49           C  
ANISOU  403  CB  ASP A  50     4653   3647   5185   -768    979  -1128       C  
ATOM    404  CG  ASP A  50     -27.716  73.116  16.006  1.00 46.10           C  
ANISOU  404  CG  ASP A  50     5878   5137   6501   -738    912  -1155       C  
ATOM    405  OD1 ASP A  50     -28.191  73.462  17.104  1.00 55.37           O  
ANISOU  405  OD1 ASP A  50     7002   6342   7695   -795   1021  -1164       O  
ATOM    406  OD2 ASP A  50     -27.660  73.879  15.015  1.00 54.45           O  
ANISOU  406  OD2 ASP A  50     6910   6269   7509   -656    756  -1169       O  
ATOM    407  N   GLY A  51     -25.606  68.937  17.279  1.00 40.72           N  
ANISOU  407  N   GLY A  51     5642   3935   5896   -812   1232   -945       N  
ATOM    408  CA  GLY A  51     -25.525  67.521  16.985  1.00 38.93           C  
ANISOU  408  CA  GLY A  51     5510   3539   5741   -850   1273   -959       C  
ATOM    409  C   GLY A  51     -25.943  66.584  18.094  1.00 42.93           C  
ANISOU  409  C   GLY A  51     6107   3900   6303   -959   1432   -916       C  
ATOM    410  O   GLY A  51     -25.978  65.372  17.871  1.00 55.34           O  
ANISOU  410  O   GLY A  51     7763   5312   7950  -1005   1465   -928       O  
ATOM    411  N   GLY A  52     -26.258  67.090  19.277  1.00 48.44           N  
ANISOU  411  N   GLY A  52     6807   4636   6962  -1003   1531   -866       N  
ATOM    412  CA  GLY A  52     -26.668  66.181  20.328  1.00 51.58           C  
ANISOU  412  CA  GLY A  52     7314   4888   7395  -1111   1683   -811       C  
ATOM    413  C   GLY A  52     -28.069  66.451  20.831  1.00 49.19           C  
ANISOU  413  C   GLY A  52     6908   4648   7133  -1260   1793   -909       C  
ATOM    414  O   GLY A  52     -28.907  66.999  20.108  1.00 54.19           O  
ANISOU  414  O   GLY A  52     7372   5406   7814  -1294   1744  -1055       O  
ATOM    415  N   SER A  53     -28.336  66.069  22.073  1.00 49.62           N  
ANISOU  415  N   SER A  53     7066   4619   7167  -1345   1937   -828       N  
ATOM    416  CA  SER A  53     -29.594  66.441  22.690  1.00 44.20           C  
ANISOU  416  CA  SER A  53     6280   4008   6506  -1479   2056   -919       C  
ATOM    417  C   SER A  53     -29.654  67.953  22.871  1.00 50.68           C  
ANISOU  417  C   SER A  53     6986   5021   7248  -1408   2009   -972       C  
ATOM    418  O   SER A  53     -28.628  68.636  22.948  1.00 50.29           O  
ANISOU  418  O   SER A  53     6989   5019   7102  -1274   1924   -887       O  
ATOM    419  CB  SER A  53     -29.754  65.749  24.040  1.00 46.74           C  
ANISOU  419  CB  SER A  53     6761   4203   6794  -1580   2216   -792       C  
ATOM    420  OG  SER A  53     -29.178  66.531  25.070  1.00 50.95           O  
ANISOU  420  OG  SER A  53     7379   4793   7185  -1506   2228   -680       O  
ATOM    421  N   LYS A  73     -30.874  68.478  22.921  1.00 48.55           N  
ANISOU  421  N   LYS A  73     6552   4860   7033  -1499   2062  -1124       N  
ATOM    422  CA  LYS A  73     -31.044  69.868  23.302  1.00 43.02           C  
ANISOU  422  CA  LYS A  73     5758   4319   6267  -1446   2040  -1181       C  
ATOM    423  C   LYS A  73     -30.405  70.078  24.667  1.00 46.24           C  
ANISOU  423  C   LYS A  73     6341   4684   6544  -1428   2113  -1031       C  
ATOM    424  O   LYS A  73     -30.528  69.236  25.560  1.00 57.62           O  
ANISOU  424  O   LYS A  73     7915   6011   7967  -1519   2238   -931       O  
ATOM    425  CB  LYS A  73     -32.528  70.244  23.334  1.00 55.46           C  
ANISOU  425  CB  LYS A  73     7140   5996   7938  -1555   2104  -1371       C  
ATOM    426  CG  LYS A  73     -32.796  71.703  23.692  1.00 49.56           C  
ANISOU  426  CG  LYS A  73     6284   5406   7141  -1496   2071  -1458       C  
ATOM    427  CD  LYS A  73     -34.275  72.054  23.582  1.00 53.68           C  
ANISOU  427  CD  LYS A  73     6587   6029   7779  -1583   2109  -1667       C  
ATOM    428  CE  LYS A  73     -35.104  71.359  24.653  1.00 50.77           C  
ANISOU  428  CE  LYS A  73     6250   5596   7443  -1757   2301  -1664       C  
ATOM    429  NZ  LYS A  73     -36.505  71.887  24.706  1.00 50.41           N  
ANISOU  429  NZ  LYS A  73     5976   5670   7505  -1832   2339  -1871       N  
ATOM    430  N   HIS A  74     -29.676  71.179  24.803  1.00 44.76           N  
ANISOU  430  N   HIS A  74     6161   4585   6260  -1310   2025  -1000       N  
ATOM    431  CA  HIS A  74     -28.958  71.575  26.010  1.00 42.10           C  
ANISOU  431  CA  HIS A  74     5981   4227   5786  -1270   2049   -860       C  
ATOM    432  C   HIS A  74     -27.674  70.787  26.229  1.00 34.36           C  
ANISOU  432  C   HIS A  74     5199   3115   4741  -1189   2016   -661       C  
ATOM    433  O   HIS A  74     -27.063  70.954  27.279  1.00 32.80           O  
ANISOU  433  O   HIS A  74     5145   2894   4424  -1153   2029   -522       O  
ATOM    434  CB  HIS A  74     -29.800  71.447  27.288  1.00 42.95           C  
ANISOU  434  CB  HIS A  74     6130   4331   5859  -1398   2200   -845       C  
ATOM    435  CG  HIS A  74     -31.167  72.050  27.188  1.00 53.91           C  
ANISOU  435  CG  HIS A  74     7314   5836   7333  -1490   2247  -1045       C  
ATOM    436  ND1 HIS A  74     -31.403  73.275  26.599  1.00 54.16           N  
ANISOU  436  ND1 HIS A  74     7180   6002   7396  -1423   2138  -1198       N  
ATOM    437  CD2 HIS A  74     -32.370  71.602  27.617  1.00 53.66           C  
ANISOU  437  CD2 HIS A  74     7211   5808   7369  -1639   2389  -1118       C  
ATOM    438  CE1 HIS A  74     -32.693  73.551  26.664  1.00 54.40           C  
ANISOU  438  CE1 HIS A  74     7042   6113   7514  -1515   2196  -1362       C  
ATOM    439  NE2 HIS A  74     -33.302  72.553  27.278  1.00 58.72           N  
ANISOU  439  NE2 HIS A  74     7635   6589   8086  -1650   2355  -1319       N  
ATOM    440  N   ARG A  75     -27.244  69.925  25.300  1.00 27.45           N  
ANISOU  440  N   ARG A  75     4336   2156   3938  -1153   1962   -639       N  
ATOM    441  CA  ARG A  75     -26.002  69.195  25.543  1.00 27.64           C  
ANISOU  441  CA  ARG A  75     4538   2050   3913  -1061   1919   -460       C  
ATOM    442  C   ARG A  75     -24.783  70.124  25.529  1.00 32.85           C  
ANISOU  442  C   ARG A  75     5219   2778   4485   -906   1792   -392       C  
ATOM    443  O   ARG A  75     -23.843  69.940  26.320  1.00 25.63           O  
ANISOU  443  O   ARG A  75     4458   1796   3483   -830   1769   -233       O  
ATOM    444  CB  ARG A  75     -25.827  68.088  24.515  1.00 28.38           C  
ANISOU  444  CB  ARG A  75     4632   2036   4115  -1056   1882   -474       C  
ATOM    445  CG  ARG A  75     -24.388  67.595  24.431  1.00 39.87           C  
ANISOU  445  CG  ARG A  75     6218   3391   5541   -914   1789   -331       C  
ATOM    446  CD  ARG A  75     -24.269  66.102  24.496  1.00 40.15           C  
ANISOU  446  CD  ARG A  75     6387   3227   5641   -947   1835   -252       C  
ATOM    447  NE  ARG A  75     -22.891  65.662  24.704  1.00 32.99           N  
ANISOU  447  NE  ARG A  75     5616   2218   4701   -800   1752   -102       N  
ATOM    448  CZ  ARG A  75     -22.384  64.553  24.179  1.00 38.42           C  
ANISOU  448  CZ  ARG A  75     6374   2752   5472   -756   1718    -72       C  
ATOM    449  NH1 ARG A  75     -23.149  63.781  23.415  1.00 40.37           N  
ANISOU  449  NH1 ARG A  75     6581   2928   5832   -860   1758   -179       N  
ATOM    450  NH2 ARG A  75     -21.121  64.206  24.421  1.00 33.21           N  
ANISOU  450  NH2 ARG A  75     5823   2005   4791   -607   1636     57       N  
ATOM    451  N   PHE A  76     -24.770  71.117  24.640  1.00 23.22           N  
ANISOU  451  N   PHE A  76     3845   1694   3285   -857   1698   -499       N  
ATOM    452  CA  PHE A  76     -23.598  71.965  24.461  1.00 21.20           C  
ANISOU  452  CA  PHE A  76     3591   1498   2966   -723   1571   -438       C  
ATOM    453  C   PHE A  76     -23.885  73.422  24.780  1.00 21.10           C  
ANISOU  453  C   PHE A  76     3496   1626   2896   -727   1553   -505       C  
ATOM    454  O   PHE A  76     -25.003  73.915  24.599  1.00 23.71           O  
ANISOU  454  O   PHE A  76     3696   2047   3266   -807   1595   -641       O  
ATOM    455  CB  PHE A  76     -23.065  71.889  23.026  1.00 20.05           C  
ANISOU  455  CB  PHE A  76     3347   1387   2886   -646   1443   -469       C  
ATOM    456  CG  PHE A  76     -22.642  70.523  22.624  1.00 21.39           C  
ANISOU  456  CG  PHE A  76     3599   1414   3116   -627   1448   -421       C  
ATOM    457  CD1 PHE A  76     -21.460  69.985  23.100  1.00 21.87           C  
ANISOU  457  CD1 PHE A  76     3796   1366   3148   -528   1421   -284       C  
ATOM    458  CD2 PHE A  76     -23.420  69.772  21.768  1.00 24.53           C  
ANISOU  458  CD2 PHE A  76     3935   1778   3606   -701   1467   -517       C  
ATOM    459  CE1 PHE A  76     -21.057  68.704  22.733  1.00 23.35           C  
ANISOU  459  CE1 PHE A  76     4060   1409   3403   -502   1421   -245       C  
ATOM    460  CE2 PHE A  76     -23.024  68.480  21.395  1.00 26.76           C  
ANISOU  460  CE2 PHE A  76     4306   1910   3951   -687   1471   -482       C  
ATOM    461  CZ  PHE A  76     -21.842  67.950  21.888  1.00 28.48           C  
ANISOU  461  CZ  PHE A  76     4662   2015   4144   -586   1451   -346       C  
ATOM    462  N   GLU A  77     -22.846  74.104  25.253  1.00 18.76           N  
ANISOU  462  N   GLU A  77     3272   1342   2513   -636   1481   -414       N  
ATOM    463  CA  GLU A  77     -22.813  75.556  25.284  1.00 17.19           C  
ANISOU  463  CA  GLU A  77     2987   1272   2272   -619   1417   -465       C  
ATOM    464  C   GLU A  77     -21.821  76.019  24.232  1.00 15.52           C  
ANISOU  464  C   GLU A  77     2687   1120   2091   -505   1233   -427       C  
ATOM    465  O   GLU A  77     -20.740  75.439  24.106  1.00 16.62           O  
ANISOU  465  O   GLU A  77     2907   1181   2226   -416   1190   -338       O  
ATOM    466  CB  GLU A  77     -22.392  76.077  26.649  1.00 17.51           C  
ANISOU  466  CB  GLU A  77     3181   1284   2189   -609   1445   -391       C  
ATOM    467  CG  GLU A  77     -22.756  77.537  26.802  1.00 27.45           C  
ANISOU  467  CG  GLU A  77     4328   2668   3435   -636   1375   -470       C  
ATOM    468  CD  GLU A  77     -24.208  77.652  27.177  1.00 31.68           C  
ANISOU  468  CD  GLU A  77     4769   3254   4013   -752   1446   -586       C  
ATOM    469  OE1 GLU A  77     -24.946  78.298  26.423  1.00 41.56           O  
ANISOU  469  OE1 GLU A  77     5818   4608   5366   -784   1372   -682       O  
ATOM    470  OE2 GLU A  77     -24.615  77.037  28.177  1.00 37.02           O  
ANISOU  470  OE2 GLU A  77     5543   3906   4617   -799   1562   -542       O  
ATOM    471  N   ILE A  78     -22.195  77.041  23.461  1.00 14.28           N  
ANISOU  471  N   ILE A  78     2360   1096   1968   -497   1107   -494       N  
ATOM    472  CA  ILE A  78     -21.330  77.566  22.406  1.00 12.91           C  
ANISOU  472  CA  ILE A  78     2116    983   1806   -391    930   -469       C  
ATOM    473  C   ILE A  78     -20.533  78.698  23.025  1.00 12.55           C  
ANISOU  473  C   ILE A  78     2090    985   1692   -325    843   -430       C  
ATOM    474  O   ILE A  78     -21.116  79.585  23.646  1.00 15.91           O  
ANISOU  474  O   ILE A  78     2482   1478   2088   -351    827   -470       O  
ATOM    475  CB  ILE A  78     -22.147  78.088  21.209  1.00 27.60           C  
ANISOU  475  CB  ILE A  78     3830   2943   3713   -393    823   -547       C  
ATOM    476  CG1 ILE A  78     -23.142  77.034  20.730  1.00 36.50           C  
ANISOU  476  CG1 ILE A  78     4928   4029   4909   -473    914   -619       C  
ATOM    477  CG2 ILE A  78     -21.211  78.506  20.055  1.00 21.30           C  
ANISOU  477  CG2 ILE A  78     3010   2183   2901   -294    678   -515       C  
ATOM    478  CD1 ILE A  78     -23.838  77.387  19.448  1.00 37.32           C  
ANISOU  478  CD1 ILE A  78     4925   4207   5049   -454    799   -693       C  
ATOM    479  N   ILE A  79     -19.213  78.648  22.887  1.00 12.28           N  
ANISOU  479  N   ILE A  79     2105    918   1642   -237    789   -365       N  
ATOM    480  CA  ILE A  79     -18.332  79.714  23.336  1.00 10.96           C  
ANISOU  480  CA  ILE A  79     1946    796   1424   -171    699   -344       C  
ATOM    481  C   ILE A  79     -17.816  80.525  22.158  1.00  9.86           C  
ANISOU  481  C   ILE A  79     1694    738   1314   -121    567   -359       C  
ATOM    482  O   ILE A  79     -17.710  81.759  22.231  1.00  9.18           O  
ANISOU  482  O   ILE A  79     1561    725   1202   -101    475   -380       O  
ATOM    483  CB  ILE A  79     -17.170  79.105  24.152  1.00 13.80           C  
ANISOU  483  CB  ILE A  79     2458   1038   1749    -99    746   -259       C  
ATOM    484  CG1 ILE A  79     -17.729  78.309  25.349  1.00 20.48           C  
ANISOU  484  CG1 ILE A  79     3479   1770   2533   -147    888   -217       C  
ATOM    485  CG2 ILE A  79     -16.203  80.182  24.662  1.00 11.33           C  
ANISOU  485  CG2 ILE A  79     2162    762   1382    -26    652   -254       C  
ATOM    486  CD1 ILE A  79     -16.751  77.311  25.868  1.00 20.67           C  
ANISOU  486  CD1 ILE A  79     3633   1674   2545    -61    890    -66       C  
ATOM    487  N   GLU A  80     -17.499  79.862  21.059  1.00  9.86           N  
ANISOU  487  N   GLU A  80     1669    717   1358   -104    564   -352       N  
ATOM    488  CA  GLU A  80     -17.033  80.552  19.861  1.00 11.76           C  
ANISOU  488  CA  GLU A  80     1843   1019   1606    -68    472   -363       C  
ATOM    489  C   GLU A  80     -18.157  81.439  19.318  1.00  9.18           C  
ANISOU  489  C   GLU A  80     1458    767   1265    -93    405   -410       C  
ATOM    490  O   GLU A  80     -19.337  81.162  19.518  1.00 14.12           O  
ANISOU  490  O   GLU A  80     2066   1396   1903   -140    438   -448       O  
ATOM    491  CB  GLU A  80     -16.560  79.487  18.844  1.00 11.01           C  
ANISOU  491  CB  GLU A  80     1759    878   1547    -48    508   -359       C  
ATOM    492  CG  GLU A  80     -15.991  80.005  17.504  1.00 15.91           C  
ANISOU  492  CG  GLU A  80     2344   1542   2160    -18    455   -373       C  
ATOM    493  CD  GLU A  80     -14.707  80.781  17.714  1.00 11.82           C  
ANISOU  493  CD  GLU A  80     1818   1030   1643     21    446   -345       C  
ATOM    494  OE1 GLU A  80     -13.587  80.187  17.771  1.00 10.75           O  
ANISOU  494  OE1 GLU A  80     1695    842   1549     71    501   -321       O  
ATOM    495  OE2 GLU A  80     -14.826  82.026  17.865  1.00 15.56           O  
ANISOU  495  OE2 GLU A  80     2270   1553   2088     10    385   -352       O  
ATOM    496  N   GLY A  81     -17.791  82.536  18.667  1.00  9.08           N  
ANISOU  496  N   GLY A  81     1423    793   1235    -68    337   -413       N  
ATOM    497  CA  GLY A  81     -18.796  83.430  18.114  1.00  9.20           C  
ANISOU  497  CA  GLY A  81     1408    848   1239    -77    284   -456       C  
ATOM    498  C   GLY A  81     -19.328  84.482  19.079  1.00 21.04           C  
ANISOU  498  C   GLY A  81     2893   2380   2721    -73    242   -472       C  
ATOM    499  O   GLY A  81     -20.191  85.279  18.689  1.00 22.53           O  
ANISOU  499  O   GLY A  81     3063   2592   2907    -65    194   -510       O  
ATOM    500  N   ARG A  82     -18.892  84.475  20.329  1.00 11.48           N  
ANISOU  500  N   ARG A  82     1701   1166   1494    -70    256   -452       N  
ATOM    501  CA  ARG A  82     -19.294  85.473  21.310  1.00  8.67           C  
ANISOU  501  CA  ARG A  82     1344    840   1110    -60    217   -476       C  
ATOM    502  C   ARG A  82     -18.204  86.516  21.425  1.00 12.33           C  
ANISOU  502  C   ARG A  82     1830   1302   1552    -22    140   -456       C  
ATOM    503  O   ARG A  82     -17.034  86.229  21.155  1.00 11.75           O  
ANISOU  503  O   ARG A  82     1767   1208   1490    -10    138   -425       O  
ATOM    504  CB  ARG A  82     -19.525  84.818  22.675  1.00 11.50           C  
ANISOU  504  CB  ARG A  82     1730   1196   1445    -80    279   -481       C  
ATOM    505  CG  ARG A  82     -20.597  83.724  22.660  1.00 14.84           C  
ANISOU  505  CG  ARG A  82     2138   1601   1899   -144    381   -506       C  
ATOM    506  CD  ARG A  82     -20.831  83.231  24.064  1.00 13.70           C  
ANISOU  506  CD  ARG A  82     2056   1434   1716   -200    499   -520       C  
ATOM    507  NE  ARG A  82     -21.814  82.148  24.136  1.00 11.27           N  
ANISOU  507  NE  ARG A  82     1749   1085   1449   -292    635   -550       N  
ATOM    508  CZ  ARG A  82     -23.115  82.334  24.297  1.00 27.06           C  
ANISOU  508  CZ  ARG A  82     3674   3126   3481   -347    675   -628       C  
ATOM    509  NH1 ARG A  82     -23.613  83.568  24.392  1.00 21.80           N  
ANISOU  509  NH1 ARG A  82     2939   2540   2806   -297    582   -672       N  
ATOM    510  NH2 ARG A  82     -23.915  81.274  24.373  1.00 22.97           N  
ANISOU  510  NH2 ARG A  82     3155   2557   3014   -456    823   -668       N  
ATOM    511  N   ASP A  83     -18.584  87.737  21.808  1.00  8.13           N  
ANISOU  511  N   ASP A  83     1309    783    998     -8     83   -480       N  
ATOM    512  CA  ASP A  83     -17.544  88.707  22.099  1.00  7.89           C  
ANISOU  512  CA  ASP A  83     1316    733    948      9     12   -467       C  
ATOM    513  C   ASP A  83     -16.729  88.211  23.282  1.00  7.76           C  
ANISOU  513  C   ASP A  83     1307    725    916     12     22   -481       C  
ATOM    514  O   ASP A  83     -17.171  87.343  24.043  1.00 10.28           O  
ANISOU  514  O   ASP A  83     1634   1059   1211     -4     97   -496       O  
ATOM    515  CB  ASP A  83     -18.125  90.094  22.374  1.00 13.56           C  
ANISOU  515  CB  ASP A  83     2068   1445   1638     -6    -17   -480       C  
ATOM    516  CG  ASP A  83     -19.001  90.149  23.624  1.00 34.33           C  
ANISOU  516  CG  ASP A  83     4704   4103   4238      1      2   -533       C  
ATOM    517  OD1 ASP A  83     -18.479  90.171  24.779  1.00 15.72           O  
ANISOU  517  OD1 ASP A  83     2379   1756   1836      8    -13   -534       O  
ATOM    518  OD2 ASP A  83     -20.245  90.215  23.455  1.00 41.79           O  
ANISOU  518  OD2 ASP A  83     5598   5072   5208     -1     31   -576       O  
ATOM    519  N   ARG A  84     -15.510  88.753  23.429  1.00  7.92           N  
ANISOU  519  N   ARG A  84     1337    725    946     -4    -17   -486       N  
ATOM    520  CA  ARG A  84     -14.583  88.186  24.419  1.00  8.76           C  
ANISOU  520  CA  ARG A  84     1485    821   1023    -27     15   -517       C  
ATOM    521  C   ARG A  84     -15.134  88.244  25.841  1.00  9.20           C  
ANISOU  521  C   ARG A  84     1588    926    980    -27     13   -553       C  
ATOM    522  O   ARG A  84     -14.949  87.301  26.630  1.00  9.84           O  
ANISOU  522  O   ARG A  84     1780    991    969    -19     63   -520       O  
ATOM    523  CB  ARG A  84     -13.256  88.934  24.364  1.00  8.97           C  
ANISOU  523  CB  ARG A  84     1508    824   1075    -56    -68   -520       C  
ATOM    524  CG  ARG A  84     -12.555  88.745  23.015  1.00  9.70           C  
ANISOU  524  CG  ARG A  84     1542    881   1262    -66    -24   -473       C  
ATOM    525  CD  ARG A  84     -11.380  89.744  22.930  1.00 15.52           C  
ANISOU  525  CD  ARG A  84     2210   1629   2059   -108   -113   -455       C  
ATOM    526  NE  ARG A  84     -10.631  89.533  21.679  1.00 23.75           N  
ANISOU  526  NE  ARG A  84     3192   2651   3182   -124    -41   -405       N  
ATOM    527  CZ  ARG A  84     -11.082  89.884  20.473  1.00 27.51           C  
ANISOU  527  CZ  ARG A  84     3708   3079   3664   -154     16   -423       C  
ATOM    528  NH1 ARG A  84     -12.257  90.491  20.359  1.00 19.79           N  
ANISOU  528  NH1 ARG A  84     2802   2095   2621   -141    -28   -446       N  
ATOM    529  NH2 ARG A  84     -10.343  89.652  19.386  1.00 27.97           N  
ANISOU  529  NH2 ARG A  84     3725   3132   3772   -170     99   -377       N  
ATOM    530  N   ILE A  85     -15.757  89.360  26.218  1.00  9.29           N  
ANISOU  530  N   ILE A  85     1536    993   1000    -17    -46   -595       N  
ATOM    531  CA  ILE A  85     -16.249  89.456  27.599  1.00 10.17           C  
ANISOU  531  CA  ILE A  85     1693   1162   1007    -18    -34   -645       C  
ATOM    532  C   ILE A  85     -17.313  88.383  27.867  1.00 10.39           C  
ANISOU  532  C   ILE A  85     1775   1188    985     -6     73   -624       C  
ATOM    533  O   ILE A  85     -17.290  87.698  28.900  1.00 11.32           O  
ANISOU  533  O   ILE A  85     1996   1325    980    -29    144   -610       O  
ATOM    534  CB  ILE A  85     -16.775  90.870  27.888  1.00 10.40           C  
ANISOU  534  CB  ILE A  85     1782   1162   1008   -108     -8   -617       C  
ATOM    535  CG1 ILE A  85     -15.581  91.839  27.927  1.00 10.66           C  
ANISOU  535  CG1 ILE A  85     1777   1208   1065   -123   -119   -658       C  
ATOM    536  CG2 ILE A  85     -17.453  90.878  29.263  1.00 12.15           C  
ANISOU  536  CG2 ILE A  85     2120   1390   1106    -36    -34   -638       C  
ATOM    537  CD1 ILE A  85     -15.962  93.291  28.277  1.00 11.61           C  
ANISOU  537  CD1 ILE A  85     1912   1317   1183   -145   -150   -687       C  
ATOM    538  N   MET A  86     -18.253  88.216  26.939  1.00  9.79           N  
ANISOU  538  N   MET A  86     1645   1087    987      4    101   -602       N  
ATOM    539  CA  MET A  86     -19.310  87.215  27.139  1.00 10.22           C  
ANISOU  539  CA  MET A  86     1701   1150   1034    -38    229   -600       C  
ATOM    540  C   MET A  86     -18.752  85.801  27.078  1.00 10.41           C  
ANISOU  540  C   MET A  86     1794   1117   1044    -84    334   -544       C  
ATOM    541  O   MET A  86     -19.185  84.915  27.836  1.00 11.41           O  
ANISOU  541  O   MET A  86     2004   1227   1103   -129    458   -528       O  
ATOM    542  CB  MET A  86     -20.406  87.391  26.087  1.00  9.74           C  
ANISOU  542  CB  MET A  86     1563   1082   1058    -34    218   -602       C  
ATOM    543  CG  MET A  86     -21.242  88.654  26.339  1.00 14.51           C  
ANISOU  543  CG  MET A  86     2154   1705   1654     -8    175   -652       C  
ATOM    544  SD  MET A  86     -21.996  88.684  27.991  1.00 25.59           S  
ANISOU  544  SD  MET A  86     3585   3168   2968    -13    253   -722       S  
ATOM    545  CE  MET A  86     -22.770  87.040  28.023  1.00 14.81           C  
ANISOU  545  CE  MET A  86     2187   1811   1629   -117    430   -728       C  
ATOM    546  N   ALA A  87     -17.791  85.559  26.176  1.00  9.74           N  
ANISOU  546  N   ALA A  87     1703    983   1016    -67    300   -503       N  
ATOM    547  CA  ALA A  87     -17.179  84.241  26.088  1.00 10.10           C  
ANISOU  547  CA  ALA A  87     1844    938   1055    -72    396   -441       C  
ATOM    548  C   ALA A  87     -16.542  83.845  27.418  1.00 12.77           C  
ANISOU  548  C   ALA A  87     2334   1263   1253    -45    412   -380       C  
ATOM    549  O   ALA A  87     -16.755  82.731  27.909  1.00 12.16           O  
ANISOU  549  O   ALA A  87     2346   1138   1136    -54    507   -300       O  
ATOM    550  CB  ALA A  87     -16.138  84.215  24.961  1.00  9.44           C  
ANISOU  550  CB  ALA A  87     1716    813   1057    -35    347   -413       C  
ATOM    551  N   TRP A  88     -15.779  84.764  28.038  1.00 11.44           N  
ANISOU  551  N   TRP A  88     2158   1162   1024     -9    276   -377       N  
ATOM    552  CA  TRP A  88     -15.132  84.430  29.305  1.00 12.77           C  
ANISOU  552  CA  TRP A  88     2422   1365   1063     36    219   -279       C  
ATOM    553  C   TRP A  88     -16.141  84.386  30.441  1.00 14.57           C  
ANISOU  553  C   TRP A  88     2761   1641   1136     -4    309   -306       C  
ATOM    554  O   TRP A  88     -15.931  83.672  31.426  1.00 15.18           O  
ANISOU  554  O   TRP A  88     2966   1719   1083     19    325   -199       O  
ATOM    555  CB  TRP A  88     -14.005  85.448  29.623  1.00 12.93           C  
ANISOU  555  CB  TRP A  88     2390   1452   1072     76     31   -290       C  
ATOM    556  CG  TRP A  88     -12.732  85.117  28.885  1.00 12.78           C  
ANISOU  556  CG  TRP A  88     2278   1399   1179    129    -41   -216       C  
ATOM    557  CD1 TRP A  88     -12.165  85.810  27.845  1.00 11.92           C  
ANISOU  557  CD1 TRP A  88     2043   1285   1203    112    -87   -260       C  
ATOM    558  CD2 TRP A  88     -11.878  83.986  29.127  1.00 13.79           C  
ANISOU  558  CD2 TRP A  88     2433   1493   1314    211    -63    -85       C  
ATOM    559  NE1 TRP A  88     -11.008  85.161  27.420  1.00 13.31           N  
ANISOU  559  NE1 TRP A  88     2146   1440   1472    173   -118   -176       N  
ATOM    560  CE2 TRP A  88     -10.817  84.043  28.195  1.00 15.64           C  
ANISOU  560  CE2 TRP A  88     2528   1715   1700    246   -115    -73       C  
ATOM    561  CE3 TRP A  88     -11.910  82.934  30.054  1.00 15.17           C  
ANISOU  561  CE3 TRP A  88     2745   1640   1378    265    -42     28       C  
ATOM    562  CZ2 TRP A  88      -9.792  83.088  28.166  1.00 17.57           C  
ANISOU  562  CZ2 TRP A  88     2742   1928   2007    347   -151     30       C  
ATOM    563  CZ3 TRP A  88     -10.899  81.974  30.017  1.00 21.06           C  
ANISOU  563  CZ3 TRP A  88     3487   2335   2181    369    -94    146       C  
ATOM    564  CH2 TRP A  88      -9.851  82.066  29.085  1.00 21.59           C  
ANISOU  564  CH2 TRP A  88     3389   2399   2417    417   -152    137       C  
ATOM    565  N   THR A  89     -17.221  85.163  30.342  1.00 13.34           N  
ANISOU  565  N   THR A  89     2562   1524    983    -58    368   -448       N  
ATOM    566  CA  THR A  89     -18.269  85.048  31.351  1.00 14.52           C  
ANISOU  566  CA  THR A  89     2750   1732   1035    -99    472   -466       C  
ATOM    567  C   THR A  89     -18.860  83.646  31.340  1.00 15.22           C  
ANISOU  567  C   THR A  89     2918   1744   1119   -156    654   -387       C  
ATOM    568  O   THR A  89     -19.097  83.058  32.414  1.00 16.82           O  
ANISOU  568  O   THR A  89     3253   1960   1177   -179    741   -311       O  
ATOM    569  CB  THR A  89     -19.356  86.096  31.114  1.00 14.07           C  
ANISOU  569  CB  THR A  89     2515   1740   1090   -106    449   -585       C  
ATOM    570  OG1 THR A  89     -18.761  87.402  31.130  1.00 13.63           O  
ANISOU  570  OG1 THR A  89     2402   1728   1049    -49    287   -647       O  
ATOM    571  CG2 THR A  89     -20.386  86.039  32.226  1.00 15.59           C  
ANISOU  571  CG2 THR A  89     2739   2000   1184   -135    557   -614       C  
ATOM    572  N   VAL A  90     -19.080  83.084  30.146  1.00 14.27           N  
ANISOU  572  N   VAL A  90     2720   1539   1161   -183    704   -395       N  
ATOM    573  CA  VAL A  90     -19.617  81.722  30.042  1.00 15.06           C  
ANISOU  573  CA  VAL A  90     2893   1541   1287   -249    875   -333       C  
ATOM    574  C   VAL A  90     -18.613  80.708  30.580  1.00 16.26           C  
ANISOU  574  C   VAL A  90     3207   1614   1358   -193    862   -147       C  
ATOM    575  O   VAL A  90     -18.967  79.803  31.352  1.00 17.72           O  
ANISOU  575  O   VAL A  90     3533   1748   1450   -238    986    -48       O  
ATOM    576  CB  VAL A  90     -20.023  81.417  28.589  1.00 13.93           C  
ANISOU  576  CB  VAL A  90     2611   1332   1350   -281    882   -391       C  
ATOM    577  CG1 VAL A  90     -20.514  79.985  28.462  1.00 20.58           C  
ANISOU  577  CG1 VAL A  90     3539   2049   2231   -359   1060   -346       C  
ATOM    578  CG2 VAL A  90     -21.107  82.372  28.166  1.00 15.33           C  
ANISOU  578  CG2 VAL A  90     2592   1607   1626   -309    815   -501       C  
ATOM    579  N   VAL A  91     -17.347  80.845  30.186  1.00 15.47           N  
ANISOU  579  N   VAL A  91     3073   1499   1305    -91    701    -89       N  
ATOM    580  CA  VAL A  91     -16.323  79.906  30.639  1.00 17.75           C  
ANISOU  580  CA  VAL A  91     3478   1714   1552     -4    646     84       C  
ATOM    581  C   VAL A  91     -16.189  79.937  32.156  1.00 18.39           C  
ANISOU  581  C   VAL A  91     3720   1857   1410     20    615    176       C  
ATOM    582  O   VAL A  91     -16.172  78.883  32.815  1.00 20.09           O  
ANISOU  582  O   VAL A  91     4107   1989   1537     30    681    322       O  
ATOM    583  CB  VAL A  91     -14.975  80.205  29.958  1.00 18.70           C  
ANISOU  583  CB  VAL A  91     3488   1839   1777    104    476    101       C  
ATOM    584  CG1 VAL A  91     -13.836  79.439  30.684  1.00 17.44           C  
ANISOU  584  CG1 VAL A  91     3432   1638   1557    225    373    268       C  
ATOM    585  CG2 VAL A  91     -15.029  79.825  28.484  1.00 14.65           C  
ANISOU  585  CG2 VAL A  91     2870   1242   1454     90    535     46       C  
ATOM    586  N   ASN A  92     -16.029  81.138  32.733  1.00 18.23           N  
ANISOU  586  N   ASN A  92     3667   1974   1286     36    503     96       N  
ATOM    587  CA  ASN A  92     -15.842  81.231  34.184  1.00 20.09           C  
ANISOU  587  CA  ASN A  92     4069   2284   1282     67    453    167       C  
ATOM    588  C   ASN A  92     -17.080  80.753  34.927  1.00 21.45           C  
ANISOU  588  C   ASN A  92     4384   2454   1314    -36    674    182       C  
ATOM    589  O   ASN A  92     -16.969  80.148  36.006  1.00 23.54           O  
ANISOU  589  O   ASN A  92     4802   2714   1429    -17    680    308       O  
ATOM    590  CB  ASN A  92     -15.494  82.673  34.602  1.00 19.76           C  
ANISOU  590  CB  ASN A  92     3960   2382   1166     92    292     43       C  
ATOM    591  CG  ASN A  92     -14.093  83.109  34.161  1.00 31.84           C  
ANISOU  591  CG  ASN A  92     5370   3924   2802    184     64     55       C  
ATOM    592  OD1 ASN A  92     -13.167  82.307  34.119  1.00 35.53           O  
ANISOU  592  OD1 ASN A  92     5860   4336   3305    270    -16    187       O  
ATOM    593  ND2 ASN A  92     -13.938  84.406  33.838  1.00 31.18           N  
ANISOU  593  ND2 ASN A  92     5156   3910   2782    165    -36    -89       N  
ATOM    594  N   SER A  93     -18.274  81.006  34.370  1.00 20.57           N  
ANISOU  594  N   SER A  93     4143   2349   1322   -143    825     42       N  
ATOM    595  CA  SER A  93     -19.502  80.516  34.993  1.00 22.05           C  
ANISOU  595  CA  SER A  93     4342   2539   1498   -248   1003     35       C  
ATOM    596  C   SER A  93     -19.532  78.995  35.047  1.00 24.74           C  
ANISOU  596  C   SER A  93     4814   2727   1858   -281   1114    195       C  
ATOM    597  O   SER A  93     -19.958  78.394  36.050  1.00 25.62           O  
ANISOU  597  O   SER A  93     5040   2832   1860   -323   1202    277       O  
ATOM    598  CB  SER A  93     -20.711  81.041  34.221  1.00 32.26           C  
ANISOU  598  CB  SER A  93     5426   3862   2968   -333   1090   -145       C  
ATOM    599  OG  SER A  93     -21.917  80.528  34.763  1.00 32.35           O  
ANISOU  599  OG  SER A  93     5435   3875   2981   -437   1262   -157       O  
ATOM    600  N   ILE A  94     -19.118  78.354  33.959  1.00 22.33           N  
ANISOU  600  N   ILE A  94     4491   2293   1702   -263   1114    233       N  
ATOM    601  CA  ILE A  94     -19.113  76.899  33.921  1.00 26.77           C  
ANISOU  601  CA  ILE A  94     5159   2688   2323   -281   1195    366       C  
ATOM    602  C   ILE A  94     -18.087  76.359  34.904  1.00 26.83           C  
ANISOU  602  C   ILE A  94     5352   2667   2177   -165   1079    558       C  
ATOM    603  O   ILE A  94     -18.365  75.410  35.657  1.00 27.81           O  
ANISOU  603  O   ILE A  94     5605   2722   2240   -197   1153    666       O  
ATOM    604  CB  ILE A  94     -18.839  76.420  32.481  1.00 25.43           C  
ANISOU  604  CB  ILE A  94     4905   2392   2366   -269   1198    340       C  
ATOM    605  CG1 ILE A  94     -20.050  76.707  31.582  1.00 21.04           C  
ANISOU  605  CG1 ILE A  94     4175   1856   1965   -397   1316    151       C  
ATOM    606  CG2 ILE A  94     -18.482  74.940  32.479  1.00 23.76           C  
ANISOU  606  CG2 ILE A  94     4805   2007   2217   -235   1218    478       C  
ATOM    607  CD1 ILE A  94     -19.727  76.608  30.060  1.00 20.17           C  
ANISOU  607  CD1 ILE A  94     3956   1666   2043   -377   1288     85       C  
ATOM    608  N   CYS A  95     -16.885  76.951  34.916  1.00 27.66           N  
ANISOU  608  N   CYS A  95     5465   2825   2219    -27    881    598       N  
ATOM    609  CA  CYS A  95     -15.847  76.493  35.838  1.00 31.21           C  
ANISOU  609  CA  CYS A  95     6058   3264   2537    104    723    764       C  
ATOM    610  C   CYS A  95     -16.321  76.576  37.282  1.00 40.15           C  
ANISOU  610  C   CYS A  95     7313   4491   3453     60    758    799       C  
ATOM    611  O   CYS A  95     -16.146  75.628  38.064  1.00 33.53           O  
ANISOU  611  O   CYS A  95     6625   3583   2530     88    759    948       O  
ATOM    612  CB  CYS A  95     -14.572  77.308  35.643  1.00 29.94           C  
ANISOU  612  CB  CYS A  95     5838   3181   2357    250    482    761       C  
ATOM    613  SG  CYS A  95     -13.752  77.014  34.068  1.00 32.09           S  
ANISOU  613  SG  CYS A  95     5930   3344   2918    333    414    738       S  
ATOM    614  N   ASN A  96     -16.961  77.687  37.645  1.00 35.97           N  
ANISOU  614  N   ASN A  96     6715   4114   2837     -8    793    658       N  
ATOM    615  CA  ASN A  96     -17.456  77.827  39.011  1.00 41.01           C  
ANISOU  615  CA  ASN A  96     7457   4854   3271    -48    841    676       C  
ATOM    616  C   ASN A  96     -18.546  76.805  39.316  1.00 42.55           C  
ANISOU  616  C   ASN A  96     7724   4961   3482   -173   1072    732       C  
ATOM    617  O   ASN A  96     -18.599  76.257  40.424  1.00 50.03           O  
ANISOU  617  O   ASN A  96     8836   5912   4263   -176   1103    853       O  
ATOM    618  CB  ASN A  96     -17.967  79.248  39.233  1.00 35.54           C  
ANISOU  618  CB  ASN A  96     6642   4336   2524    -86    836    486       C  
ATOM    619  CG  ASN A  96     -16.872  80.275  39.098  1.00 53.11           C  
ANISOU  619  CG  ASN A  96     8809   6650   4720     25    593    426       C  
ATOM    620  OD1 ASN A  96     -15.691  79.950  39.224  1.00 60.11           O  
ANISOU  620  OD1 ASN A  96     9766   7505   5568    141    410    542       O  
ATOM    621  ND2 ASN A  96     -17.250  81.526  38.832  1.00 55.45           N  
ANISOU  621  ND2 ASN A  96     8956   7052   5059     -5    576    236       N  
ATOM    622  N   THR A  97     -19.401  76.513  38.337  1.00 36.02           N  
ANISOU  622  N   THR A  97     6777   4053   2856   -279   1228    645       N  
ATOM    623  CA  THR A  97     -20.573  75.678  38.576  1.00 38.91           C  
ANISOU  623  CA  THR A  97     7172   4351   3259   -420   1448    657       C  
ATOM    624  C   THR A  97     -20.234  74.188  38.568  1.00 42.97           C  
ANISOU  624  C   THR A  97     7836   4675   3814   -410   1475    833       C  
ATOM    625  O   THR A  97     -20.799  73.416  39.355  1.00 41.13           O  
ANISOU  625  O   THR A  97     7730   4398   3500   -488   1604    925       O  
ATOM    626  CB  THR A  97     -21.650  75.995  37.534  1.00 42.24           C  
ANISOU  626  CB  THR A  97     7382   4775   3892   -536   1574    470       C  
ATOM    627  OG1 THR A  97     -22.240  77.263  37.846  1.00 42.84           O  
ANISOU  627  OG1 THR A  97     7333   5029   3916   -557   1581    315       O  
ATOM    628  CG2 THR A  97     -22.739  74.932  37.527  1.00 44.67           C  
ANISOU  628  CG2 THR A  97     7703   4978   4291   -681   1779    481       C  
ATOM    629  N   THR A  98     -19.324  73.758  37.695  1.00 33.46           N  
ANISOU  629  N   THR A  98     6619   3356   2738   -312   1357    882       N  
ATOM    630  CA  THR A  98     -18.995  72.345  37.574  1.00 38.12           C  
ANISOU  630  CA  THR A  98     7328   3756   3400   -288   1371   1027       C  
ATOM    631  C   THR A  98     -17.660  71.987  38.197  1.00 39.69           C  
ANISOU  631  C   THR A  98     7674   3924   3483   -113   1172   1204       C  
ATOM    632  O   THR A  98     -17.374  70.797  38.361  1.00 49.87           O  
ANISOU  632  O   THR A  98     9089   5060   4798    -81   1172   1345       O  
ATOM    633  CB  THR A  98     -18.959  71.918  36.100  1.00 36.32           C  
ANISOU  633  CB  THR A  98     6968   3404   3427   -294   1386    946       C  
ATOM    634  OG1 THR A  98     -17.837  72.538  35.471  1.00 38.27           O  
ANISOU  634  OG1 THR A  98     7137   3686   3718   -148   1202    930       O  
ATOM    635  CG2 THR A  98     -20.252  72.302  35.361  1.00 34.24           C  
ANISOU  635  CG2 THR A  98     6533   3179   3298   -454   1548    751       C  
ATOM    636  N   GLY A  99     -16.829  72.970  38.526  1.00 41.18           N  
ANISOU  636  N   GLY A  99     7840   4251   3556      3    989   1193       N  
ATOM    637  CA  GLY A  99     -15.524  72.709  39.085  1.00 40.09           C  
ANISOU  637  CA  GLY A  99     7803   4104   3325    180    766   1338       C  
ATOM    638  C   GLY A  99     -14.433  72.350  38.095  1.00 47.84           C  
ANISOU  638  C   GLY A  99     8696   4986   4496    322    617   1362       C  
ATOM    639  O   GLY A  99     -13.299  72.101  38.524  1.00 48.59           O  
ANISOU  639  O   GLY A  99     8841   5076   4546    483    416   1473       O  
ATOM    640  N   VAL A 100     -14.716  72.325  36.784  1.00 47.45           N  
ANISOU  640  N   VAL A 100     8500   4864   4663    275    703   1252       N  
ATOM    641  CA  VAL A 100     -13.674  71.929  35.841  1.00 34.26           C  
ANISOU  641  CA  VAL A 100     6738   3102   3179    414    577   1269       C  
ATOM    642  C   VAL A 100     -12.594  73.009  35.782  1.00 40.36           C  
ANISOU  642  C   VAL A 100     7401   4011   3921    551    358   1235       C  
ATOM    643  O   VAL A 100     -12.811  74.176  36.134  1.00 43.32           O  
ANISOU  643  O   VAL A 100     7746   4544   4169    511    327   1155       O  
ATOM    644  CB  VAL A 100     -14.254  71.636  34.446  1.00 42.22           C  
ANISOU  644  CB  VAL A 100     7616   4011   4414    326    722   1147       C  
ATOM    645  CG1 VAL A 100     -15.420  70.657  34.540  1.00 42.50           C  
ANISOU  645  CG1 VAL A 100     7737   3932   4480    170    929   1153       C  
ATOM    646  CG2 VAL A 100     -14.680  72.920  33.760  1.00 37.73           C  
ANISOU  646  CG2 VAL A 100     6896   3564   3875    255    759    981       C  
ATOM    647  N   GLU A 101     -11.400  72.598  35.358  1.00 37.35           N  
ANISOU  647  N   GLU A 101     6949   3573   3668    717    198   1285       N  
ATOM    648  CA  GLU A 101     -10.270  73.516  35.287  1.00 41.57           C  
ANISOU  648  CA  GLU A 101     7349   4236   4208    854    -27   1251       C  
ATOM    649  C   GLU A 101     -10.538  74.631  34.276  1.00 41.41           C  
ANISOU  649  C   GLU A 101     7171   4288   4274    792     18   1095       C  
ATOM    650  O   GLU A 101     -11.063  74.387  33.186  1.00 39.26           O  
ANISOU  650  O   GLU A 101     6831   3922   4163    719    173   1022       O  
ATOM    651  CB  GLU A 101      -8.999  72.751  34.907  1.00 43.39           C  
ANISOU  651  CB  GLU A 101     7491   4386   4608   1037   -177   1316       C  
ATOM    652  N   LYS A 102     -10.172  75.871  34.652  1.00 35.54           N  
ANISOU  652  N   LYS A 102     6368   3714   3420    816   -131   1036       N  
ATOM    653  CA  LYS A 102     -10.360  77.027  33.777  1.00 35.82           C  
ANISOU  653  CA  LYS A 102     6183   3857   3569    727   -111    848       C  
ATOM    654  C   LYS A 102      -9.293  77.042  32.688  1.00 43.27           C  
ANISOU  654  C   LYS A 102     6897   4789   4755    824   -203    798       C  
ATOM    655  O   LYS A 102      -8.099  76.989  32.998  1.00 44.88           O  
ANISOU  655  O   LYS A 102     7039   5032   4981    973   -401    853       O  
ATOM    656  CB  LYS A 102     -10.307  78.326  34.572  1.00 37.17           C  
ANISOU  656  CB  LYS A 102     6323   4219   3579    692   -240    763       C  
ATOM    657  CG  LYS A 102     -10.244  79.567  33.707  1.00 38.78           C  
ANISOU  657  CG  LYS A 102     6285   4524   3926    618   -265    577       C  
ATOM    658  CD  LYS A 102     -10.230  80.836  34.549  1.00 42.99           C  
ANISOU  658  CD  LYS A 102     6812   5219   4304    581   -392    482       C  
ATOM    659  CE  LYS A 102      -9.792  82.026  33.702  1.00 40.54           C  
ANISOU  659  CE  LYS A 102     6262   4982   4161    537   -469    328       C  
ATOM    660  NZ  LYS A 102     -10.217  83.327  34.285  1.00 42.97           N  
ANISOU  660  NZ  LYS A 102     6574   5404   4347    456   -520    196       N  
ATOM    661  N   PRO A 103      -9.677  77.112  31.418  1.00 30.25           N  
ANISOU  661  N   PRO A 103     5114   3097   3284    745    -65    689       N  
ATOM    662  CA  PRO A 103      -8.689  77.037  30.339  1.00 28.87           C  
ANISOU  662  CA  PRO A 103     4737   2907   3324    832   -114    644       C  
ATOM    663  C   PRO A 103      -7.885  78.318  30.199  1.00 22.77           C  
ANISOU  663  C   PRO A 103     3753   2303   2595    831   -264    545       C  
ATOM    664  O   PRO A 103      -8.334  79.411  30.550  1.00 26.68           O  
ANISOU  664  O   PRO A 103     4235   2909   2995    727   -291    464       O  
ATOM    665  CB  PRO A 103      -9.549  76.791  29.093  1.00 29.07           C  
ANISOU  665  CB  PRO A 103     4728   2846   3473    724     92    550       C  
ATOM    666  CG  PRO A 103     -10.875  77.404  29.441  1.00 27.98           C  
ANISOU  666  CG  PRO A 103     4666   2757   3208    560    191    485       C  
ATOM    667  CD  PRO A 103     -11.058  77.106  30.907  1.00 32.93           C  
ANISOU  667  CD  PRO A 103     5493   3387   3631    582    150    608       C  
ATOM    668  N   LYS A 104      -6.670  78.169  29.657  1.00 24.30           N  
ANISOU  668  N   LYS A 104     3773   2508   2951    946   -353    544       N  
ATOM    669  CA  LYS A 104      -5.832  79.341  29.399  1.00 30.02           C  
ANISOU  669  CA  LYS A 104     4273   3380   3754    924   -474    448       C  
ATOM    670  C   LYS A 104      -6.325  80.161  28.204  1.00 32.16           C  
ANISOU  670  C   LYS A 104     4433   3673   4116    778   -338    317       C  
ATOM    671  O   LYS A 104      -6.136  81.385  28.178  1.00 33.83           O  
ANISOU  671  O   LYS A 104     4535   3990   4329    694   -408    233       O  
ATOM    672  CB  LYS A 104      -4.377  78.908  29.182  1.00 35.83           C  
ANISOU  672  CB  LYS A 104     4832   4131   4651   1086   -594    479       C  
ATOM    673  N   PHE A 105      -6.931  79.521  27.203  1.00 32.28           N  
ANISOU  673  N   PHE A 105     4483   3581   4203    750   -156    297       N  
ATOM    674  CA  PHE A 105      -7.465  80.195  26.021  1.00 25.01           C  
ANISOU  674  CA  PHE A 105     3487   2672   3344    628    -34    183       C  
ATOM    675  C   PHE A 105      -8.948  79.865  25.873  1.00 19.87           C  
ANISOU  675  C   PHE A 105     2994   1941   2617    534    109    158       C  
ATOM    676  O   PHE A 105      -9.419  78.850  26.382  1.00 23.21           O  
ANISOU  676  O   PHE A 105     3564   2268   2988    566    161    231       O  
ATOM    677  CB  PHE A 105      -6.754  79.749  24.745  1.00 34.65           C  
ANISOU  677  CB  PHE A 105     4578   3855   4731    681     51    153       C  
ATOM    678  CG  PHE A 105      -5.267  79.883  24.794  1.00 40.34           C  
ANISOU  678  CG  PHE A 105     5111   4652   5565    781    -61    170       C  
ATOM    679  CD1 PHE A 105      -4.670  81.136  24.835  1.00 43.71           C  
ANISOU  679  CD1 PHE A 105     5384   5204   6018    710   -154    118       C  
ATOM    680  CD2 PHE A 105      -4.460  78.752  24.788  1.00 40.15           C  
ANISOU  680  CD2 PHE A 105     5052   4565   5638    947    -72    230       C  
ATOM    681  CE1 PHE A 105      -3.284  81.262  24.873  1.00 47.50           C  
ANISOU  681  CE1 PHE A 105     5657   5764   6625    787   -254    119       C  
ATOM    682  CE2 PHE A 105      -3.079  78.869  24.831  1.00 46.61           C  
ANISOU  682  CE2 PHE A 105     5661   5466   6582   1050   -179    230       C  
ATOM    683  CZ  PHE A 105      -2.492  80.128  24.869  1.00 43.78           C  
ANISOU  683  CZ  PHE A 105     5128   5250   6255    961   -267    171       C  
ATOM    684  N   LEU A 106      -9.680  80.692  25.143  1.00 15.40           N  
ANISOU  684  N   LEU A 106     2393   1405   2053    419    173     54       N  
ATOM    685  CA  LEU A 106     -11.100  80.400  24.942  1.00 12.86           C  
ANISOU  685  CA  LEU A 106     2182   1022   1683    332    298      8       C  
ATOM    686  C   LEU A 106     -11.266  79.138  24.115  1.00 13.14           C  
ANISOU  686  C   LEU A 106     2259    929   1805    362    423     15       C  
ATOM    687  O   LEU A 106     -10.745  79.083  22.994  1.00 15.21           O  
ANISOU  687  O   LEU A 106     2433   1180   2166    388    457    -29       O  
ATOM    688  CB  LEU A 106     -11.802  81.552  24.229  1.00 11.42           C  
ANISOU  688  CB  LEU A 106     1943    896   1499    229    315   -111       C  
ATOM    689  CG  LEU A 106     -12.086  82.739  25.116  1.00 14.56           C  
ANISOU  689  CG  LEU A 106     2345   1387   1801    181    221   -145       C  
ATOM    690  CD1 LEU A 106     -12.623  83.869  24.241  1.00 12.82           C  
ANISOU  690  CD1 LEU A 106     2067   1196   1609    106    225   -254       C  
ATOM    691  CD2 LEU A 106     -13.061  82.391  26.236  1.00 12.13           C  
ANISOU  691  CD2 LEU A 106     2164   1074   1371    154    262   -129       C  
ATOM    692  N   PRO A 107     -11.988  78.112  24.595  1.00 13.87           N  
ANISOU  692  N   PRO A 107     2492    916   1863    350    503     63       N  
ATOM    693  CA  PRO A 107     -12.313  76.987  23.716  1.00 14.16           C  
ANISOU  693  CA  PRO A 107     2566    825   1989    347    621     38       C  
ATOM    694  C   PRO A 107     -13.532  77.286  22.860  1.00 13.02           C  
ANISOU  694  C   PRO A 107     2354    760   1832    202    668    -82       C  
ATOM    695  O   PRO A 107     -13.998  78.429  22.831  1.00 11.95           O  
ANISOU  695  O   PRO A 107     2169    719   1654    141    633   -146       O  
ATOM    696  CB  PRO A 107     -12.554  75.829  24.696  1.00 19.23           C  
ANISOU  696  CB  PRO A 107     3368   1350   2589    369    658    154       C  
ATOM    697  CG  PRO A 107     -13.004  76.491  25.941  1.00 24.25           C  
ANISOU  697  CG  PRO A 107     4076   2058   3080    322    620    199       C  
ATOM    698  CD  PRO A 107     -12.507  77.917  25.955  1.00 18.95           C  
ANISOU  698  CD  PRO A 107     3267   1555   2376    327    495    142       C  
ATOM    699  N   ASP A 108     -14.074  76.278  22.185  1.00 13.44           N  
ANISOU  699  N   ASP A 108     2403    781   1921    156    724   -107       N  
ATOM    700  CA  ASP A 108     -15.164  76.501  21.245  1.00 12.63           C  
ANISOU  700  CA  ASP A 108     2221    762   1814     51    730   -200       C  
ATOM    701  C   ASP A 108     -16.522  76.092  21.785  1.00 14.33           C  
ANISOU  701  C   ASP A 108     2488    950   2005    -48    810   -220       C  
ATOM    702  O   ASP A 108     -17.517  76.787  21.525  1.00 12.63           O  
ANISOU  702  O   ASP A 108     2199    826   1773   -124    792   -287       O  
ATOM    703  CB  ASP A 108     -14.894  75.747  19.937  1.00 12.93           C  
ANISOU  703  CB  ASP A 108     2215    791   1908     69    729   -236       C  
ATOM    704  CG  ASP A 108     -13.754  76.362  19.147  1.00 12.46           C  
ANISOU  704  CG  ASP A 108     2082    787   1864    136    675   -246       C  
ATOM    705  OD1 ASP A 108     -13.632  77.603  19.168  1.00 15.12           O  
ANISOU  705  OD1 ASP A 108     2369   1208   2168    123    622   -257       O  
ATOM    706  OD2 ASP A 108     -12.965  75.600  18.551  1.00 13.90           O  
ANISOU  706  OD2 ASP A 108     2263    921   2096    201    695   -245       O  
ATOM    707  N   LEU A 109     -16.583  74.988  22.531  1.00 14.51           N  
ANISOU  707  N   LEU A 109     2633    846   2033    -46    896   -158       N  
ATOM    708  CA  LEU A 109     -17.826  74.518  23.141  1.00 15.36           C  
ANISOU  708  CA  LEU A 109     2804    911   2121   -154   1007   -175       C  
ATOM    709  C   LEU A 109     -17.551  74.028  24.552  1.00 16.75           C  
ANISOU  709  C   LEU A 109     3156    973   2235   -130   1065    -53       C  
ATOM    710  O   LEU A 109     -16.406  73.745  24.923  1.00 17.31           O  
ANISOU  710  O   LEU A 109     3295    984   2299    -13   1003     56       O  
ATOM    711  CB  LEU A 109     -18.458  73.373  22.347  1.00 16.27           C  
ANISOU  711  CB  LEU A 109     2901    972   2310   -208   1060   -224       C  
ATOM    712  CG  LEU A 109     -18.783  73.608  20.873  1.00 26.49           C  
ANISOU  712  CG  LEU A 109     4056   2360   3648   -226    989   -323       C  
ATOM    713  CD1 LEU A 109     -19.106  72.286  20.221  1.00 30.99           C  
ANISOU  713  CD1 LEU A 109     4654   2834   4287   -254   1035   -358       C  
ATOM    714  CD2 LEU A 109     -19.931  74.555  20.697  1.00 27.77           C  
ANISOU  714  CD2 LEU A 109     4115   2642   3795   -306    970   -404       C  
ATOM    715  N   TYR A 110     -18.619  73.907  25.333  1.00 17.57           N  
ANISOU  715  N   TYR A 110     3327   1058   2290   -239   1175    -62       N  
ATOM    716  CA  TYR A 110     -18.574  73.087  26.535  1.00 19.50           C  
ANISOU  716  CA  TYR A 110     3747   1196   2465   -242   1237     73       C  
ATOM    717  C   TYR A 110     -19.614  71.987  26.409  1.00 20.99           C  
ANISOU  717  C   TYR A 110     3953   1310   2712   -355   1357     33       C  
ATOM    718  O   TYR A 110     -20.733  72.242  25.963  1.00 20.63           O  
ANISOU  718  O   TYR A 110     3803   1325   2709   -465   1425   -103       O  
ATOM    719  CB  TYR A 110     -18.818  73.901  27.802  1.00 22.10           C  
ANISOU  719  CB  TYR A 110     4164   1583   2648   -277   1262    126       C  
ATOM    720  CG  TYR A 110     -18.675  73.067  29.067  1.00 26.39           C  
ANISOU  720  CG  TYR A 110     4890   2055   3083   -265   1294    290       C  
ATOM    721  CD1 TYR A 110     -17.420  72.795  29.607  1.00 22.76           C  
ANISOU  721  CD1 TYR A 110     4535   1553   2560   -117   1174    449       C  
ATOM    722  CD2 TYR A 110     -19.801  72.548  29.722  1.00 24.89           C  
ANISOU  722  CD2 TYR A 110     4756   1846   2856   -396   1433    283       C  
ATOM    723  CE1 TYR A 110     -17.290  72.031  30.787  1.00 25.13           C  
ANISOU  723  CE1 TYR A 110     5009   1796   2745    -97   1181    605       C  
ATOM    724  CE2 TYR A 110     -19.675  71.778  30.903  1.00 26.01           C  
ANISOU  724  CE2 TYR A 110     5075   1924   2884   -389   1460    444       C  
ATOM    725  CZ  TYR A 110     -18.419  71.536  31.423  1.00 26.73           C  
ANISOU  725  CZ  TYR A 110     5283   1976   2898   -237   1329    607       C  
ATOM    726  OH  TYR A 110     -18.277  70.779  32.574  1.00 29.33           O  
ANISOU  726  OH  TYR A 110     5794   2245   3106   -221   1338    770       O  
ATOM    727  N   ASP A 111     -19.219  70.763  26.781  1.00 22.88           N  
ANISOU  727  N   ASP A 111     4318   1412   2962   -320   1371    150       N  
ATOM    728  CA  ASP A 111     -20.061  69.569  26.705  1.00 24.75           C  
ANISOU  728  CA  ASP A 111     4599   1541   3264   -424   1479    134       C  
ATOM    729  C   ASP A 111     -20.563  69.274  28.119  1.00 27.93           C  
ANISOU  729  C   ASP A 111     5153   1901   3559   -499   1575    244       C  
ATOM    730  O   ASP A 111     -19.776  68.868  28.974  1.00 28.05           O  
ANISOU  730  O   ASP A 111     5319   1847   3493   -414   1529    412       O  
ATOM    731  CB  ASP A 111     -19.248  68.398  26.146  1.00 25.82           C  
ANISOU  731  CB  ASP A 111     4783   1538   3489   -335   1426    192       C  
ATOM    732  CG  ASP A 111     -20.079  67.127  25.921  1.00 27.89           C  
ANISOU  732  CG  ASP A 111     5093   1667   3837   -447   1527    166       C  
ATOM    733  OD1 ASP A 111     -21.193  67.009  26.467  1.00 28.98           O  
ANISOU  733  OD1 ASP A 111     5255   1802   3955   -590   1647    144       O  
ATOM    734  OD2 ASP A 111     -19.609  66.234  25.179  1.00 28.62           O  
ANISOU  734  OD2 ASP A 111     5196   1653   4026   -394   1486    160       O  
ATOM    735  N   TYR A 112     -21.860  69.514  28.369  1.00 27.17           N  
ANISOU  735  N   TYR A 112     5007   1860   3457   -651   1698    149       N  
ATOM    736  CA  TYR A 112     -22.441  69.294  29.701  1.00 29.28           C  
ANISOU  736  CA  TYR A 112     5401   2113   3613   -739   1805    241       C  
ATOM    737  C   TYR A 112     -22.539  67.814  30.055  1.00 32.63           C  
ANISOU  737  C   TYR A 112     5972   2361   4066   -785   1878    357       C  
ATOM    738  O   TYR A 112     -22.572  67.463  31.247  1.00 34.27           O  
ANISOU  738  O   TYR A 112     6340   2529   4154   -810   1932    502       O  
ATOM    739  CB  TYR A 112     -23.838  69.920  29.795  1.00 31.30           C  
ANISOU  739  CB  TYR A 112     5532   2478   3883   -890   1922     86       C  
ATOM    740  CG  TYR A 112     -23.823  71.429  29.871  1.00 31.50           C  
ANISOU  740  CG  TYR A 112     5454   2669   3844   -856   1863      1       C  
ATOM    741  CD1 TYR A 112     -24.274  72.204  28.806  1.00 25.18           C  
ANISOU  741  CD1 TYR A 112     4462   1956   3148   -872   1829   -186       C  
ATOM    742  CD2 TYR A 112     -23.330  72.083  30.997  1.00 29.28           C  
ANISOU  742  CD2 TYR A 112     5273   2460   3393   -803   1828    110       C  
ATOM    743  CE1 TYR A 112     -24.241  73.603  28.864  1.00 28.71           C  
ANISOU  743  CE1 TYR A 112     4823   2539   3547   -841   1766   -261       C  
ATOM    744  CE2 TYR A 112     -23.295  73.483  31.064  1.00 28.57           C  
ANISOU  744  CE2 TYR A 112     5089   2521   3246   -772   1764     28       C  
ATOM    745  CZ  TYR A 112     -23.751  74.228  29.991  1.00 27.75           C  
ANISOU  745  CZ  TYR A 112     4797   2482   3266   -795   1735   -155       C  
ATOM    746  OH  TYR A 112     -23.717  75.601  30.031  1.00 29.05           O  
ANISOU  746  OH  TYR A 112     4867   2785   3387   -764   1661   -233       O  
ATOM    747  N   LYS A 113     -22.633  66.942  29.045  1.00 32.47           N  
ANISOU  747  N   LYS A 113     5907   2234   4196   -803   1880    296       N  
ATOM    748  CA  LYS A 113     -22.752  65.508  29.303  1.00 35.38           C  
ANISOU  748  CA  LYS A 113     6418   2412   4612   -855   1947    398       C  
ATOM    749  C   LYS A 113     -21.418  64.921  29.755  1.00 38.43           C  
ANISOU  749  C   LYS A 113     6974   2681   4948   -694   1836    590       C  
ATOM    750  O   LYS A 113     -21.364  64.159  30.728  1.00 41.35           O  
ANISOU  750  O   LYS A 113     7528   2935   5247   -711   1880    754       O  
ATOM    751  CB  LYS A 113     -23.265  64.795  28.049  1.00 35.56           C  
ANISOU  751  CB  LYS A 113     6337   2361   4811   -924   1970    258       C  
ATOM    752  CG  LYS A 113     -23.724  63.350  28.280  1.00 38.88           C  
ANISOU  752  CG  LYS A 113     6889   2579   5304  -1032   2070    328       C  
ATOM    753  CD  LYS A 113     -23.950  62.638  26.955  1.00 39.00           C  
ANISOU  753  CD  LYS A 113     6816   2512   5491  -1063   2048    195       C  
ATOM    754  CE  LYS A 113     -23.441  61.189  26.975  1.00 49.72           C  
ANISOU  754  CE  LYS A 113     8347   3622   6921  -1037   2038    312       C  
ATOM    755  NZ  LYS A 113     -23.507  60.551  25.622  1.00 48.90           N  
ANISOU  755  NZ  LYS A 113     8163   3442   6975  -1044   1992    173       N  
ATOM    756  N   GLU A 114     -20.331  65.253  29.056  1.00 34.48           N  
ANISOU  756  N   GLU A 114     6408   2207   4484   -532   1689    574       N  
ATOM    757  CA  GLU A 114     -19.004  64.776  29.421  1.00 35.43           C  
ANISOU  757  CA  GLU A 114     6652   2231   4578   -357   1562    736       C  
ATOM    758  C   GLU A 114     -18.274  65.705  30.377  1.00 39.24           C  
ANISOU  758  C   GLU A 114     7183   2830   4898   -249   1468    844       C  
ATOM    759  O   GLU A 114     -17.210  65.331  30.881  1.00 35.98           O  
ANISOU  759  O   GLU A 114     6877   2348   4444   -100   1351    993       O  
ATOM    760  CB  GLU A 114     -18.134  64.566  28.174  1.00 34.22           C  
ANISOU  760  CB  GLU A 114     6395   2044   4563   -231   1452    659       C  
ATOM    761  CG  GLU A 114     -18.678  63.544  27.169  1.00 35.18           C  
ANISOU  761  CG  GLU A 114     6487   2040   4841   -312   1513    555       C  
ATOM    762  CD  GLU A 114     -18.590  62.087  27.651  1.00 53.26           C  
ANISOU  762  CD  GLU A 114     8968   4093   7176   -317   1542    688       C  
ATOM    763  OE1 GLU A 114     -17.899  61.813  28.664  1.00 52.22           O  
ANISOU  763  OE1 GLU A 114     8989   3890   6962   -221   1487    872       O  
ATOM    764  OE2 GLU A 114     -19.226  61.218  27.010  1.00 43.27           O  
ANISOU  764  OE2 GLU A 114     7703   2709   6028   -418   1611    610       O  
ATOM    765  N   ASN A 115     -18.810  66.895  30.627  1.00 33.06           N  
ANISOU  765  N   ASN A 115     6318   2217   4025   -314   1504    766       N  
ATOM    766  CA  ASN A 115     -18.184  67.907  31.473  1.00 37.37           C  
ANISOU  766  CA  ASN A 115     6898   2891   4410   -223   1408    842       C  
ATOM    767  C   ASN A 115     -16.751  68.194  31.021  1.00 35.08           C  
ANISOU  767  C   ASN A 115     6556   2613   4160    -26   1224    875       C  
ATOM    768  O   ASN A 115     -15.776  68.005  31.750  1.00 32.44           O  
ANISOU  768  O   ASN A 115     6326   2254   3747    112   1101   1024       O  
ATOM    769  CB  ASN A 115     -18.250  67.511  32.950  1.00 43.10           C  
ANISOU  769  CB  ASN A 115     7828   3587   4961   -236   1434   1019       C  
ATOM    770  CG  ASN A 115     -19.582  67.876  33.573  1.00 45.56           C  
ANISOU  770  CG  ASN A 115     8145   3981   5185   -419   1604    963       C  
ATOM    771  OD1 ASN A 115     -19.940  69.065  33.668  1.00 36.53           O  
ANISOU  771  OD1 ASN A 115     6901   3001   3977   -454   1613    861       O  
ATOM    772  ND2 ASN A 115     -20.347  66.863  33.965  1.00 43.02           N  
ANISOU  772  ND2 ASN A 115     7928   3544   4875   -541   1742   1018       N  
ATOM    773  N   ARG A 116     -16.641  68.686  29.788  1.00 28.83           N  
ANISOU  773  N   ARG A 116     5588   1872   3494    -13   1201    726       N  
ATOM    774  CA  ARG A 116     -15.335  69.083  29.292  1.00 27.70           C  
ANISOU  774  CA  ARG A 116     5363   1762   3401    159   1045    735       C  
ATOM    775  C   ARG A 116     -15.519  70.144  28.218  1.00 24.93           C  
ANISOU  775  C   ARG A 116     4823   1532   3117    124   1046    564       C  
ATOM    776  O   ARG A 116     -16.511  70.140  27.483  1.00 24.14           O  
ANISOU  776  O   ARG A 116     4641   1450   3082     -3   1147    430       O  
ATOM    777  CB  ARG A 116     -14.533  67.918  28.719  1.00 29.03           C  
ANISOU  777  CB  ARG A 116     5540   1785   3704    269    987    772       C  
ATOM    778  CG  ARG A 116     -15.147  67.260  27.499  1.00 28.72           C  
ANISOU  778  CG  ARG A 116     5422   1680   3813    182   1078    634       C  
ATOM    779  CD  ARG A 116     -14.624  65.828  27.327  1.00 31.08           C  
ANISOU  779  CD  ARG A 116     5808   1787   4213    260   1053    701       C  
ATOM    780  NE  ARG A 116     -15.241  65.178  26.177  1.00 31.03           N  
ANISOU  780  NE  ARG A 116     5739   1719   4332    172   1130    563       N  
ATOM    781  CZ  ARG A 116     -15.117  63.888  25.881  1.00 35.44           C  
ANISOU  781  CZ  ARG A 116     6378   2096   4993    194   1140    583       C  
ATOM    782  NH1 ARG A 116     -14.387  63.093  26.654  1.00 35.53           N  
ANISOU  782  NH1 ARG A 116     6533   1962   5004    307   1076    741       N  
ATOM    783  NH2 ARG A 116     -15.734  63.397  24.818  1.00 33.08           N  
ANISOU  783  NH2 ARG A 116     6019   1758   4793    107   1201    443       N  
ATOM    784  N   PHE A 117     -14.555  71.050  28.159  1.00 23.72           N  
ANISOU  784  N   PHE A 117     4601   1466   2946    241    922    575       N  
ATOM    785  CA  PHE A 117     -14.480  71.994  27.045  1.00 21.72           C  
ANISOU  785  CA  PHE A 117     4170   1312   2771    233    902    429       C  
ATOM    786  C   PHE A 117     -14.020  71.262  25.788  1.00 21.97           C  
ANISOU  786  C   PHE A 117     4100   1293   2953    281    891    358       C  
ATOM    787  O   PHE A 117     -13.379  70.205  25.853  1.00 23.06           O  
ANISOU  787  O   PHE A 117     4297   1318   3146    372    859    432       O  
ATOM    788  CB  PHE A 117     -13.533  73.146  27.379  1.00 20.49           C  
ANISOU  788  CB  PHE A 117     3973   1251   2559    341    772    466       C  
ATOM    789  CG  PHE A 117     -14.065  74.072  28.438  1.00 21.06           C  
ANISOU  789  CG  PHE A 117     4135   1403   2463    279    778    502       C  
ATOM    790  CD1 PHE A 117     -13.596  73.993  29.746  1.00 21.85           C  
ANISOU  790  CD1 PHE A 117     4376   1518   2407    354    693    653       C  
ATOM    791  CD2 PHE A 117     -15.054  75.003  28.134  1.00 18.72           C  
ANISOU  791  CD2 PHE A 117     3771   1190   2152    145    854    371       C  
ATOM    792  CE1 PHE A 117     -14.088  74.839  30.728  1.00 25.12           C  
ANISOU  792  CE1 PHE A 117     4861   2050   2635    290    691    665       C  
ATOM    793  CE2 PHE A 117     -15.554  75.854  29.109  1.00 18.72           C  
ANISOU  793  CE2 PHE A 117     3794   1326   1992     84    842    362       C  
ATOM    794  CZ  PHE A 117     -15.082  75.762  30.416  1.00 20.29           C  
ANISOU  794  CZ  PHE A 117     4138   1551   2021    150    771    505       C  
ATOM    795  N   ILE A 118     -14.376  71.819  24.628  1.00 19.69           N  
ANISOU  795  N   ILE A 118     3665   1093   2721    220    910    210       N  
ATOM    796  CA  ILE A 118     -14.039  71.229  23.336  1.00 19.67           C  
ANISOU  796  CA  ILE A 118     3571   1075   2827    248    901    128       C  
ATOM    797  C   ILE A 118     -13.377  72.301  22.478  1.00 18.01           C  
ANISOU  797  C   ILE A 118     3210    997   2636    291    832     53       C  
ATOM    798  O   ILE A 118     -13.884  73.421  22.384  1.00 16.51           O  
ANISOU  798  O   ILE A 118     2956    920   2396    220    824     -4       O  
ATOM    799  CB  ILE A 118     -15.275  70.680  22.596  1.00 19.73           C  
ANISOU  799  CB  ILE A 118     3560   1071   2865    112    988     24       C  
ATOM    800  CG1 ILE A 118     -15.922  69.536  23.363  1.00 21.71           C  
ANISOU  800  CG1 ILE A 118     3956   1177   3117     54   1073     91       C  
ATOM    801  CG2 ILE A 118     -14.887  70.137  21.228  1.00 21.75           C  
ANISOU  801  CG2 ILE A 118     3741   1320   3205    148    964    -60       C  
ATOM    802  CD1 ILE A 118     -17.302  69.182  22.825  1.00 23.25           C  
ANISOU  802  CD1 ILE A 118     4118   1374   3341    -98   1164    -18       C  
ATOM    803  N   GLU A 119     -12.246  71.963  21.881  1.00 18.52           N  
ANISOU  803  N   GLU A 119     3219   1043   2775    406    784     52       N  
ATOM    804  CA  GLU A 119     -11.637  72.815  20.871  1.00 18.67           C  
ANISOU  804  CA  GLU A 119     3097   1180   2817    429    747    -28       C  
ATOM    805  C   GLU A 119     -11.864  72.156  19.515  1.00 17.55           C  
ANISOU  805  C   GLU A 119     2919   1035   2713    394    784   -125       C  
ATOM    806  O   GLU A 119     -11.490  70.991  19.324  1.00 19.65           O  
ANISOU  806  O   GLU A 119     3233   1191   3044    459    802   -118       O  
ATOM    807  CB  GLU A 119     -10.144  73.016  21.149  1.00 18.65           C  
ANISOU  807  CB  GLU A 119     3038   1178   2870    588    679     29       C  
ATOM    808  CG  GLU A 119      -9.431  73.654  19.944  1.00 17.32           C  
ANISOU  808  CG  GLU A 119     2726   1116   2740    606    678    -60       C  
ATOM    809  CD  GLU A 119      -9.943  75.070  19.672  1.00 15.48           C  
ANISOU  809  CD  GLU A 119     2435   1008   2439    500    670   -109       C  
ATOM    810  OE1 GLU A 119     -10.424  75.768  20.617  1.00 16.09           O  
ANISOU  810  OE1 GLU A 119     2552   1101   2461    462    642    -71       O  
ATOM    811  OE2 GLU A 119      -9.908  75.482  18.493  1.00 16.99           O  
ANISOU  811  OE2 GLU A 119     2557   1276   2621    454    689   -184       O  
ATOM    812  N   ILE A 120     -12.512  72.874  18.590  1.00 16.23           N  
ANISOU  812  N   ILE A 120     2683    980   2503    299    781   -210       N  
ATOM    813  CA  ILE A 120     -12.829  72.366  17.256  1.00 16.49           C  
ANISOU  813  CA  ILE A 120     2696   1022   2546    267    797   -299       C  
ATOM    814  C   ILE A 120     -11.831  72.949  16.275  1.00 17.15           C  
ANISOU  814  C   ILE A 120     2700   1187   2630    325    778   -337       C  
ATOM    815  O   ILE A 120     -11.545  74.152  16.305  1.00 15.08           O  
ANISOU  815  O   ILE A 120     2376   1022   2332    315    748   -325       O  
ATOM    816  CB  ILE A 120     -14.272  72.718  16.841  1.00 16.90           C  
ANISOU  816  CB  ILE A 120     2734   1139   2547    139    789   -358       C  
ATOM    817  CG1 ILE A 120     -15.272  71.847  17.588  1.00 33.33           C  
ANISOU  817  CG1 ILE A 120     4892   3123   4650     73    847   -345       C  
ATOM    818  CG2 ILE A 120     -14.491  72.530  15.334  1.00 17.85           C  
ANISOU  818  CG2 ILE A 120     2828   1296   2659    125    772   -449       C  
ATOM    819  CD1 ILE A 120     -16.618  72.461  17.676  1.00 33.06           C  
ANISOU  819  CD1 ILE A 120     4820   3165   4576    -39    844   -386       C  
ATOM    820  N   GLY A 121     -11.251  72.128  15.431  1.00 17.40           N  
ANISOU  820  N   GLY A 121     2735   1171   2703    389    808   -384       N  
ATOM    821  CA  GLY A 121     -10.373  72.598  14.368  1.00 17.46           C  
ANISOU  821  CA  GLY A 121     2675   1257   2702    435    822   -431       C  
ATOM    822  C   GLY A 121     -10.889  72.121  13.023  1.00 18.99           C  
ANISOU  822  C   GLY A 121     2899   1454   2861    400    838   -526       C  
ATOM    823  O   GLY A 121     -11.446  71.034  12.932  1.00 18.93           O  
ANISOU  823  O   GLY A 121     2957   1353   2883    392    849   -561       O  
ATOM    824  N   VAL A 122     -10.749  72.964  11.996  1.00 17.45           N  
ANISOU  824  N   VAL A 122     2667   1362   2601    378    839   -566       N  
ATOM    825  CA  VAL A 122     -11.078  72.613  10.616  1.00 18.19           C  
ANISOU  825  CA  VAL A 122     2795   1469   2646    369    852   -660       C  
ATOM    826  C   VAL A 122      -9.829  72.916   9.795  1.00 19.01           C  
ANISOU  826  C   VAL A 122     2857   1627   2740    440    922   -687       C  
ATOM    827  O   VAL A 122      -9.331  74.043   9.839  1.00 18.24           O  
ANISOU  827  O   VAL A 122     2705   1610   2617    425    934   -645       O  
ATOM    828  CB  VAL A 122     -12.281  73.419  10.076  1.00 18.14           C  
ANISOU  828  CB  VAL A 122     2809   1527   2558    267    806   -683       C  
ATOM    829  CG1 VAL A 122     -12.544  73.018   8.628  1.00 18.45           C  
ANISOU  829  CG1 VAL A 122     2900   1566   2544    273    827   -787       C  
ATOM    830  CG2 VAL A 122     -13.528  73.196  10.928  1.00 16.67           C  
ANISOU  830  CG2 VAL A 122     2641   1300   2393    191    764   -662       C  
ATOM    831  N   THR A 123      -9.301  71.925   9.087  1.00 20.77           N  
ANISOU  831  N   THR A 123     3101   1801   2988    519    979   -762       N  
ATOM    832  CA  THR A 123      -7.999  72.095   8.452  1.00 25.84           C  
ANISOU  832  CA  THR A 123     3683   2497   3637    602   1069   -791       C  
ATOM    833  C   THR A 123      -8.042  71.825   6.949  1.00 25.10           C  
ANISOU  833  C   THR A 123     3639   2437   3461    614   1120   -900       C  
ATOM    834  O   THR A 123      -8.730  70.911   6.490  1.00 24.02           O  
ANISOU  834  O   THR A 123     3580   2233   3313    616   1095   -976       O  
ATOM    835  CB  THR A 123      -6.933  71.199   9.121  1.00 24.72           C  
ANISOU  835  CB  THR A 123     3493   2281   3620    733   1104   -782       C  
ATOM    836  OG1 THR A 123      -5.657  71.459   8.520  1.00 30.92           O  
ANISOU  836  OG1 THR A 123     4185   3143   4420    815   1198   -815       O  
ATOM    837  CG2 THR A 123      -7.257  69.701   8.962  1.00 24.95           C  
ANISOU  837  CG2 THR A 123     3606   2176   3696    789   1099   -852       C  
ATOM    838  N   ARG A 124      -7.294  72.653   6.197  1.00 23.61           N  
ANISOU  838  N   ARG A 124     3407   2352   3214    619   1200   -908       N  
ATOM    839  CA  ARG A 124      -7.028  72.466   4.776  1.00 25.28           C  
ANISOU  839  CA  ARG A 124     3658   2612   3335    649   1281  -1008       C  
ATOM    840  C   ARG A 124      -5.832  71.556   4.546  1.00 30.96           C  
ANISOU  840  C   ARG A 124     4322   3313   4127    781   1385  -1073       C  
ATOM    841  O   ARG A 124      -5.607  71.114   3.413  1.00 32.83           O  
ANISOU  841  O   ARG A 124     4600   3576   4297    828   1459  -1179       O  
ATOM    842  CB  ARG A 124      -6.783  73.830   4.084  1.00 26.08           C  
ANISOU  842  CB  ARG A 124     3749   2832   3328    584   1338   -977       C  
ATOM    843  CG  ARG A 124      -7.969  74.860   4.197  1.00 27.46           C  
ANISOU  843  CG  ARG A 124     3983   3027   3424    471   1230   -922       C  
ATOM    844  CD  ARG A 124      -7.533  76.337   4.300  1.00 32.03           C  
ANISOU  844  CD  ARG A 124     4524   3678   3967    407   1270   -837       C  
ATOM    845  NE  ARG A 124      -7.583  76.823   5.681  1.00 30.80           N  
ANISOU  845  NE  ARG A 124     4302   3495   3907    377   1203   -745       N  
ATOM    846  CZ  ARG A 124      -7.191  78.024   6.088  1.00 34.05           C  
ANISOU  846  CZ  ARG A 124     4668   3945   4326    325   1224   -672       C  
ATOM    847  NH1 ARG A 124      -6.714  78.906   5.218  1.00 42.60           N  
ANISOU  847  NH1 ARG A 124     5769   5091   5325    286   1319   -665       N  
ATOM    848  NH2 ARG A 124      -7.270  78.342   7.378  1.00 38.12           N  
ANISOU  848  NH2 ARG A 124     5126   4431   4925    311   1157   -607       N  
ATOM    849  N   ARG A 125      -5.073  71.257   5.598  1.00 30.02           N  
ANISOU  849  N   ARG A 125     4112   3153   4141    855   1386  -1021       N  
ATOM    850  CA  ARG A 125      -3.955  70.334   5.483  1.00 33.55           C  
ANISOU  850  CA  ARG A 125     4494   3576   4679   1006   1464  -1086       C  
ATOM    851  C   ARG A 125      -4.408  68.932   5.885  1.00 42.26           C  
ANISOU  851  C   ARG A 125     5680   4518   5860   1075   1399  -1131       C  
ATOM    852  O   ARG A 125      -5.342  68.385   5.293  1.00 56.56           O  
ANISOU  852  O   ARG A 125     7608   6271   7610   1032   1366  -1201       O  
ATOM    853  CB  ARG A 125      -2.778  70.830   6.330  1.00 33.35           C  
ANISOU  853  CB  ARG A 125     4305   3605   4761   1070   1495  -1013       C  
ATOM    854  CG  ARG A 125      -2.240  72.201   5.898  1.00 31.37           C  
ANISOU  854  CG  ARG A 125     3965   3505   4451    993   1579   -973       C  
ATOM    855  CD  ARG A 125      -1.158  72.693   6.844  1.00 33.71           C  
ANISOU  855  CD  ARG A 125     4080   3854   4873   1045   1588   -903       C  
ATOM    856  NE  ARG A 125      -1.736  73.175   8.098  1.00 34.11           N  
ANISOU  856  NE  ARG A 125     4142   3856   4962    986   1463   -800       N  
ATOM    857  CZ  ARG A 125      -1.085  73.212   9.254  1.00 31.45           C  
ANISOU  857  CZ  ARG A 125     3685   3513   4750   1061   1409   -740       C  
ATOM    858  NH1 ARG A 125       0.174  72.789   9.318  1.00 36.83           N  
ANISOU  858  NH1 ARG A 125     4211   4239   5543   1203   1458   -773       N  
ATOM    859  NH2 ARG A 125      -1.693  73.657  10.344  1.00 31.61           N  
ANISOU  859  NH2 ARG A 125     3736   3491   4783   1006   1300   -654       N  
ATOM    860  N   GLU A 126      -3.780  68.355   6.900  1.00 39.63           N  
ANISOU  860  N   GLU A 126     5288   4106   5662   1183   1371  -1091       N  
ATOM    861  CA  GLU A 126      -4.037  66.983   7.316  1.00 32.72           C  
ANISOU  861  CA  GLU A 126     4498   3057   4877   1265   1320  -1127       C  
ATOM    862  C   GLU A 126      -4.372  66.994   8.799  1.00 31.43           C  
ANISOU  862  C   GLU A 126     4344   2809   4790   1242   1221  -1000       C  
ATOM    863  O   GLU A 126      -3.850  67.832   9.546  1.00 30.48           O  
ANISOU  863  O   GLU A 126     4122   2764   4696   1246   1204   -909       O  
ATOM    864  CB  GLU A 126      -2.818  66.100   7.009  1.00 40.62           C  
ANISOU  864  CB  GLU A 126     5437   4027   5971   1462   1387  -1216       C  
ATOM    865  CG  GLU A 126      -3.097  64.617   7.105  1.00 46.90           C  
ANISOU  865  CG  GLU A 126     6348   4625   6847   1553   1346  -1285       C  
ATOM    866  CD  GLU A 126      -2.713  64.067   8.453  1.00 53.52           C  
ANISOU  866  CD  GLU A 126     7171   5333   7830   1659   1262  -1196       C  
ATOM    867  OE1 GLU A 126      -2.973  62.875   8.710  1.00 56.42           O  
ANISOU  867  OE1 GLU A 126     7648   5510   8278   1725   1216  -1227       O  
ATOM    868  OE2 GLU A 126      -2.128  64.834   9.247  1.00 56.19           O  
ANISOU  868  OE2 GLU A 126     7393   5754   8203   1679   1237  -1097       O  
ATOM    869  N   VAL A 127      -5.279  66.108   9.224  1.00 31.52           N  
ANISOU  869  N   VAL A 127     4480   2666   4832   1209   1159   -994       N  
ATOM    870  CA  VAL A 127      -5.817  66.246  10.577  1.00 30.19           C  
ANISOU  870  CA  VAL A 127     4341   2430   4698   1152   1079   -866       C  
ATOM    871  C   VAL A 127      -4.756  65.965  11.635  1.00 35.53           C  
ANISOU  871  C   VAL A 127     4954   3050   5497   1308   1043   -794       C  
ATOM    872  O   VAL A 127      -4.793  66.543  12.728  1.00 30.15           O  
ANISOU  872  O   VAL A 127     4247   2383   4825   1284    985   -679       O  
ATOM    873  CB  VAL A 127      -7.050  65.344  10.777  1.00 30.83           C  
ANISOU  873  CB  VAL A 127     4567   2360   4787   1068   1042   -873       C  
ATOM    874  CG1 VAL A 127      -8.186  65.752   9.827  1.00 29.17           C  
ANISOU  874  CG1 VAL A 127     4398   2226   4460    916   1048   -939       C  
ATOM    875  CG2 VAL A 127      -6.682  63.871  10.582  1.00 33.13           C  
ANISOU  875  CG2 VAL A 127     4934   2473   5181   1197   1051   -948       C  
ATOM    876  N   HIS A 128      -3.799  65.074  11.353  1.00 33.87           N  
ANISOU  876  N   HIS A 128     4718   2772   5380   1485   1063   -865       N  
ATOM    877  CA  HIS A 128      -2.827  64.739  12.388  1.00 35.30           C  
ANISOU  877  CA  HIS A 128     4837   2888   5685   1655    996   -797       C  
ATOM    878  C   HIS A 128      -1.874  65.895  12.659  1.00 34.63           C  
ANISOU  878  C   HIS A 128     4569   2985   5604   1697    999   -753       C  
ATOM    879  O   HIS A 128      -1.580  66.194  13.820  1.00 34.37           O  
ANISOU  879  O   HIS A 128     4495   2943   5622   1744    909   -646       O  
ATOM    880  CB  HIS A 128      -2.080  63.464  12.007  1.00 38.45           C  
ANISOU  880  CB  HIS A 128     5253   3163   6194   1850   1003   -894       C  
ATOM    881  CG  HIS A 128      -2.996  62.301  11.839  1.00 39.38           C  
ANISOU  881  CG  HIS A 128     5554   3079   6329   1808    991   -933       C  
ATOM    882  ND1 HIS A 128      -3.699  62.075  10.676  1.00 42.50           N  
ANISOU  882  ND1 HIS A 128     6020   3483   6644   1710   1062  -1049       N  
ATOM    883  CD2 HIS A 128      -3.377  61.335  12.706  1.00 54.93           C  
ANISOU  883  CD2 HIS A 128     7654   4829   8386   1837    915   -865       C  
ATOM    884  CE1 HIS A 128      -4.441  60.991  10.817  1.00 52.78           C  
ANISOU  884  CE1 HIS A 128     7477   4583   7996   1685   1031  -1065       C  
ATOM    885  NE2 HIS A 128      -4.261  60.520  12.039  1.00 58.82           N  
ANISOU  885  NE2 HIS A 128     8285   5202   8864   1755    950   -949       N  
ATOM    886  N   ILE A 129      -1.389  66.554  11.606  1.00 34.57           N  
ANISOU  886  N   ILE A 129     4453   3141   5542   1677   1101   -832       N  
ATOM    887  CA  ILE A 129      -0.578  67.755  11.785  1.00 34.46           C  
ANISOU  887  CA  ILE A 129     4259   3305   5530   1676   1122   -790       C  
ATOM    888  C   ILE A 129      -1.338  68.774  12.610  1.00 32.12           C  
ANISOU  888  C   ILE A 129     3990   3041   5174   1525   1058   -675       C  
ATOM    889  O   ILE A 129      -0.838  69.315  13.609  1.00 31.03           O  
ANISOU  889  O   ILE A 129     3756   2943   5092   1571    985   -591       O  
ATOM    890  CB  ILE A 129      -0.192  68.349  10.418  1.00 34.46           C  
ANISOU  890  CB  ILE A 129     4178   3461   5455   1625   1264   -881       C  
ATOM    891  CG1 ILE A 129       0.055  67.234   9.397  1.00 54.13           C  
ANISOU  891  CG1 ILE A 129     6717   5895   7953   1731   1339  -1016       C  
ATOM    892  CG2 ILE A 129       1.022  69.262  10.566  1.00 42.42           C  
ANISOU  892  CG2 ILE A 129     4961   4636   6518   1675   1305   -857       C  
ATOM    893  CD1 ILE A 129       0.367  67.738   7.987  1.00 54.74           C  
ANISOU  893  CD1 ILE A 129     6744   6120   7933   1681   1488  -1108       C  
ATOM    894  N   TYR A 130      -2.574  69.045  12.205  1.00 29.38           N  
ANISOU  894  N   TYR A 130     3769   2681   4712   1351   1073   -676       N  
ATOM    895  CA  TYR A 130      -3.365  70.078  12.862  1.00 26.92           C  
ANISOU  895  CA  TYR A 130     3483   2413   4332   1206   1024   -586       C  
ATOM    896  C   TYR A 130      -3.659  69.706  14.312  1.00 26.77           C  
ANISOU  896  C   TYR A 130     3525   2279   4366   1243    918   -483       C  
ATOM    897  O   TYR A 130      -3.602  70.567  15.199  1.00 25.67           O  
ANISOU  897  O   TYR A 130     3336   2193   4224   1220    862   -399       O  
ATOM    898  CB  TYR A 130      -4.661  70.301  12.072  1.00 25.39           C  
ANISOU  898  CB  TYR A 130     3406   2228   4013   1036   1047   -623       C  
ATOM    899  CG  TYR A 130      -5.309  71.667  12.295  1.00 25.76           C  
ANISOU  899  CG  TYR A 130     3443   2371   3973    891   1022   -566       C  
ATOM    900  CD1 TYR A 130      -4.820  72.795  11.667  1.00 32.06           C  
ANISOU  900  CD1 TYR A 130     4151   3300   4729    848   1075   -577       C  
ATOM    901  CD2 TYR A 130      -6.409  71.804  13.105  1.00 29.49           C  
ANISOU  901  CD2 TYR A 130     3999   2797   4409    798    953   -506       C  
ATOM    902  CE1 TYR A 130      -5.409  74.047  11.866  1.00 38.44           C  
ANISOU  902  CE1 TYR A 130     4964   4176   5467    725   1045   -529       C  
ATOM    903  CE2 TYR A 130      -7.007  73.045  13.305  1.00 30.11           C  
ANISOU  903  CE2 TYR A 130     4068   2960   4414    682    924   -468       C  
ATOM    904  CZ  TYR A 130      -6.498  74.161  12.685  1.00 32.77           C  
ANISOU  904  CZ  TYR A 130     4325   3411   4716    650    963   -480       C  
ATOM    905  OH  TYR A 130      -7.084  75.400  12.889  1.00 41.52           O  
ANISOU  905  OH  TYR A 130     5434   4582   5759    544    927   -446       O  
ATOM    906  N   TYR A 131      -3.967  68.430  14.571  1.00 28.08           N  
ANISOU  906  N   TYR A 131     3807   2282   4579   1302    889   -485       N  
ATOM    907  CA  TYR A 131      -4.206  67.995  15.944  1.00 28.38           C  
ANISOU  907  CA  TYR A 131     3927   2195   4661   1341    795   -371       C  
ATOM    908  C   TYR A 131      -3.000  68.291  16.831  1.00 29.43           C  
ANISOU  908  C   TYR A 131     3936   2364   4881   1502    709   -304       C  
ATOM    909  O   TYR A 131      -3.141  68.857  17.922  1.00 29.19           O  
ANISOU  909  O   TYR A 131     3912   2345   4833   1486    630   -196       O  
ATOM    910  CB  TYR A 131      -4.533  66.502  15.990  1.00 30.24           C  
ANISOU  910  CB  TYR A 131     4302   2232   4955   1393    785   -384       C  
ATOM    911  CG  TYR A 131      -4.825  66.036  17.399  1.00 30.82           C  
ANISOU  911  CG  TYR A 131     4486   2165   5060   1418    698   -245       C  
ATOM    912  CD1 TYR A 131      -3.794  65.711  18.281  1.00 32.67           C  
ANISOU  912  CD1 TYR A 131     4682   2339   5392   1603    595   -168       C  
ATOM    913  CD2 TYR A 131      -6.134  65.938  17.857  1.00 33.27           C  
ANISOU  913  CD2 TYR A 131     4934   2411   5296   1259    716   -188       C  
ATOM    914  CE1 TYR A 131      -4.066  65.309  19.582  1.00 35.51           C  
ANISOU  914  CE1 TYR A 131     5163   2570   5759   1622    507    -18       C  
ATOM    915  CE2 TYR A 131      -6.412  65.526  19.146  1.00 30.54           C  
ANISOU  915  CE2 TYR A 131     4705   1943   4956   1271    658    -48       C  
ATOM    916  CZ  TYR A 131      -5.376  65.218  20.004  1.00 40.32           C  
ANISOU  916  CZ  TYR A 131     5928   3117   6275   1450    551     45       C  
ATOM    917  OH  TYR A 131      -5.659  64.816  21.287  1.00 49.91           O  
ANISOU  917  OH  TYR A 131     7278   4213   7470   1459    487    204       O  
ATOM    918  N   LEU A 132      -1.803  67.905  16.379  1.00 31.47           N  
ANISOU  918  N   LEU A 132     4073   2650   5233   1667    717   -372       N  
ATOM    919  CA  LEU A 132      -0.597  68.141  17.166  1.00 32.87           C  
ANISOU  919  CA  LEU A 132     4101   2882   5507   1838    617   -324       C  
ATOM    920  C   LEU A 132      -0.386  69.629  17.409  1.00 40.04           C  
ANISOU  920  C   LEU A 132     4867   3974   6373   1758    613   -286       C  
ATOM    921  O   LEU A 132      -0.098  70.053  18.536  1.00 38.78           O  
ANISOU  921  O   LEU A 132     4662   3834   6239   1812    488   -190       O  
ATOM    922  CB  LEU A 132       0.613  67.529  16.457  1.00 35.48           C  
ANISOU  922  CB  LEU A 132     4301   3245   5937   2023    650   -430       C  
ATOM    923  CG  LEU A 132       0.865  66.045  16.697  1.00 38.15           C  
ANISOU  923  CG  LEU A 132     4735   3384   6375   2196    579   -445       C  
ATOM    924  CD1 LEU A 132       2.042  65.586  15.875  1.00 40.70           C  
ANISOU  924  CD1 LEU A 132     4915   3772   6779   2382    635   -572       C  
ATOM    925  CD2 LEU A 132       1.112  65.807  18.184  1.00 40.80           C  
ANISOU  925  CD2 LEU A 132     5101   3617   6783   2306    389   -310       C  
ATOM    926  N   GLU A 133      -0.533  70.441  16.359  1.00 31.51           N  
ANISOU  926  N   GLU A 133     3722   3022   5227   1626    740   -357       N  
ATOM    927  CA  GLU A 133      -0.412  71.885  16.529  1.00 31.27           C  
ANISOU  927  CA  GLU A 133     3569   3143   5167   1526    745   -322       C  
ATOM    928  C   GLU A 133      -1.382  72.409  17.576  1.00 31.08           C  
ANISOU  928  C   GLU A 133     3659   3073   5078   1431    659   -222       C  
ATOM    929  O   GLU A 133      -1.009  73.227  18.425  1.00 36.81           O  
ANISOU  929  O   GLU A 133     4284   3871   5830   1451    572   -156       O  
ATOM    930  CB  GLU A 133      -0.623  72.585  15.187  1.00 34.90           C  
ANISOU  930  CB  GLU A 133     4002   3707   5551   1380    892   -402       C  
ATOM    931  CG  GLU A 133       0.543  72.358  14.241  1.00 36.54           C  
ANISOU  931  CG  GLU A 133     4056   4005   5821   1471    990   -490       C  
ATOM    932  CD  GLU A 133       0.460  73.171  12.946  1.00 41.29           C  
ANISOU  932  CD  GLU A 133     4633   4719   6338   1326   1134   -549       C  
ATOM    933  OE1 GLU A 133      -0.554  73.871  12.729  1.00 46.09           O  
ANISOU  933  OE1 GLU A 133     5353   5323   6834   1164   1143   -527       O  
ATOM    934  OE2 GLU A 133       1.415  73.090  12.144  1.00 46.23           O  
ANISOU  934  OE2 GLU A 133     5130   5433   7001   1383   1237   -617       O  
ATOM    935  N   LYS A 134      -2.629  71.931  17.551  1.00 32.66           N  
ANISOU  935  N   LYS A 134     4059   3160   5192   1329    678   -212       N  
ATOM    936  CA  LYS A 134      -3.625  72.390  18.515  1.00 32.02           C  
ANISOU  936  CA  LYS A 134     4090   3041   5033   1233    621   -125       C  
ATOM    937  C   LYS A 134      -3.314  71.892  19.923  1.00 33.68           C  
ANISOU  937  C   LYS A 134     4347   3163   5288   1362    486     -7       C  
ATOM    938  O   LYS A 134      -3.514  72.619  20.905  1.00 42.58           O  
ANISOU  938  O   LYS A 134     5485   4321   6371   1343    408     80       O  
ATOM    939  CB  LYS A 134      -5.013  71.921  18.080  1.00 35.06           C  
ANISOU  939  CB  LYS A 134     4647   3348   5325   1088    683   -155       C  
ATOM    940  CG  LYS A 134      -6.128  72.766  18.610  1.00 44.70           C  
ANISOU  940  CG  LYS A 134     5941   4599   6445    943    671   -115       C  
ATOM    941  CD  LYS A 134      -6.123  74.130  17.961  1.00 40.13           C  
ANISOU  941  CD  LYS A 134     5263   4163   5822    850    704   -165       C  
ATOM    942  CE  LYS A 134      -7.182  74.270  16.876  1.00 33.40           C  
ANISOU  942  CE  LYS A 134     4472   3341   4877    701    761   -242       C  
ATOM    943  NZ  LYS A 134      -7.495  75.732  16.734  1.00 28.10           N  
ANISOU  943  NZ  LYS A 134     3757   2776   4142    600    753   -251       N  
ATOM    944  N   ALA A 135      -2.843  70.652  20.044  1.00 33.17           N  
ANISOU  944  N   ALA A 135     4323   2980   5300   1496    448      2       N  
ATOM    945  CA  ALA A 135      -2.480  70.131  21.358  1.00 35.52           C  
ANISOU  945  CA  ALA A 135     4676   3184   5636   1626    298    129       C  
ATOM    946  C   ALA A 135      -1.285  70.884  21.928  1.00 51.57           C  
ANISOU  946  C   ALA A 135     6510   5348   7736   1755    167    159       C  
ATOM    947  O   ALA A 135      -1.250  71.184  23.128  1.00 53.71           O  
ANISOU  947  O   ALA A 135     6811   5621   7974   1790     28    282       O  
ATOM    948  CB  ALA A 135      -2.179  68.635  21.266  1.00 39.06           C  
ANISOU  948  CB  ALA A 135     5204   3462   6174   1748    279    125       C  
ATOM    949  N   ASN A 136      -0.297  71.195  21.080  1.00 44.47           N  
ANISOU  949  N   ASN A 136     5402   4577   6917   1821    211     50       N  
ATOM    950  CA  ASN A 136       0.869  71.949  21.529  1.00 46.78           C  
ANISOU  950  CA  ASN A 136     5467   5033   7275   1929     97     59       C  
ATOM    951  C   ASN A 136       0.469  73.331  22.014  1.00 51.55           C  
ANISOU  951  C   ASN A 136     6024   5753   7809   1798     68    112       C  
ATOM    952  O   ASN A 136       0.926  73.782  23.071  1.00 57.78           O  
ANISOU  952  O   ASN A 136     6744   6611   8599   1870   -109    191       O  
ATOM    953  CB  ASN A 136       1.894  72.076  20.399  1.00 48.78           C  
ANISOU  953  CB  ASN A 136     5501   5425   7606   1978    213    -61       C  
ATOM    954  CG  ASN A 136       2.496  70.739  19.986  1.00 52.67           C  
ANISOU  954  CG  ASN A 136     6011   5826   8175   2156    222   -123       C  
ATOM    955  OD1 ASN A 136       3.268  70.672  19.028  1.00 66.33           O  
ANISOU  955  OD1 ASN A 136     7590   7655   9958   2204    337   -220       O  
ATOM    956  ND2 ASN A 136       2.149  69.671  20.704  1.00 58.11           N  
ANISOU  956  ND2 ASN A 136     6883   6314   8884   2242    105    -64       N  
ATOM    957  N   LYS A 137      -0.388  74.016  21.250  1.00 45.80           N  
ANISOU  957  N   LYS A 137     5338   5049   7014   1610    221     64       N  
ATOM    958  CA  LYS A 137      -0.757  75.390  21.566  1.00 45.40           C  
ANISOU  958  CA  LYS A 137     5230   5098   6923   1482    203     91       C  
ATOM    959  C   LYS A 137      -1.583  75.454  22.839  1.00 57.42           C  
ANISOU  959  C   LYS A 137     6933   6547   8335   1478     86    214       C  
ATOM    960  O   LYS A 137      -1.166  76.053  23.837  1.00 64.55           O  
ANISOU  960  O   LYS A 137     7768   7544   9213   1504    -91    275       O  
ATOM    961  CB  LYS A 137      -1.529  76.006  20.399  1.00 38.44           C  
ANISOU  961  CB  LYS A 137     4383   4238   5984   1296    384      4       C  
ATOM    962  CG  LYS A 137      -1.972  77.441  20.627  1.00 45.41           C  
ANISOU  962  CG  LYS A 137     5222   5204   6829   1153    365     12       C  
ATOM    963  CD  LYS A 137      -2.422  78.086  19.321  1.00 51.57           C  
ANISOU  963  CD  LYS A 137     6003   6019   7574    999    534    -81       C  
ATOM    964  CE  LYS A 137      -2.328  79.612  19.377  1.00 51.55           C  
ANISOU  964  CE  LYS A 137     5905   6148   7535    839    481    -95       C  
ATOM    965  NZ  LYS A 137      -2.612  80.248  18.050  1.00 50.92           N  
ANISOU  965  NZ  LYS A 137     5829   6095   7424    710    643   -167       N  
ATOM    966  N   ILE A 138      -2.761  74.831  22.827  1.00 56.06           N  
ANISOU  966  N   ILE A 138     7005   6241   8057   1402    166    233       N  
ATOM    967  CA  ILE A 138      -3.679  75.012  23.943  1.00 58.68           C  
ANISOU  967  CA  ILE A 138     7530   6527   8240   1360    103    338       C  
ATOM    968  C   ILE A 138      -3.136  74.354  25.202  1.00 57.63           C  
ANISOU  968  C   ILE A 138     7464   6356   8076   1507    -79    466       C  
ATOM    969  O   ILE A 138      -3.369  74.853  26.310  1.00 66.24           O  
ANISOU  969  O   ILE A 138     8640   7504   9024   1489   -207    544       O  
ATOM    970  CB  ILE A 138      -5.085  74.498  23.574  1.00 48.01           C  
ANISOU  970  CB  ILE A 138     6385   5059   6797   1209    246    307       C  
ATOM    971  CG1 ILE A 138      -5.196  72.984  23.761  1.00 43.11           C  
ANISOU  971  CG1 ILE A 138     5900   4285   6193   1260    252    353       C  
ATOM    972  CG2 ILE A 138      -5.440  74.897  22.140  1.00 47.85           C  
ANISOU  972  CG2 ILE A 138     6287   5086   6806   1081    390    164       C  
ATOM    973  CD1 ILE A 138      -6.544  72.432  23.373  1.00 40.97           C  
ANISOU  973  CD1 ILE A 138     5787   3925   5856   1102    383    314       C  
ATOM    974  N   LYS A 139      -2.382  73.257  25.054  1.00 60.66           N  
ANISOU  974  N   LYS A 139     7810   6659   8579   1629   -112    470       N  
ATOM    975  CA  LYS A 139      -1.786  72.488  26.148  1.00 59.95           C  
ANISOU  975  CA  LYS A 139     7776   6512   8492   1769   -282    597       C  
ATOM    976  C   LYS A 139      -2.634  72.519  27.417  1.00 66.88           C  
ANISOU  976  C   LYS A 139     8897   7360   9153   1714   -347    733       C  
ATOM    977  O   LYS A 139      -2.119  72.757  28.515  1.00 74.77           O  
ANISOU  977  O   LYS A 139     9899   8438  10071   1790   -534    825       O  
ATOM    978  CB  LYS A 139      -0.370  72.995  26.442  1.00 61.02           C  
ANISOU  978  CB  LYS A 139     7645   6796   8745   1901   -451    597       C  
ATOM    979  N   SER A 140      -3.941  72.299  27.268  1.00 62.33           N  
ANISOU  979  N   SER A 140     8520   6691   8473   1566   -191    731       N  
ATOM    980  CA  SER A 140      -4.860  72.358  28.395  1.00 57.16           C  
ANISOU  980  CA  SER A 140     8097   6017   7606   1484   -208    838       C  
ATOM    981  C   SER A 140      -5.017  71.024  29.107  1.00 58.53           C  
ANISOU  981  C   SER A 140     8462   6035   7741   1523   -219    965       C  
ATOM    982  O   SER A 140      -5.526  70.999  30.234  1.00 61.82           O  
ANISOU  982  O   SER A 140     9064   6452   7973   1482   -257   1075       O  
ATOM    983  CB  SER A 140      -6.235  72.845  27.927  1.00 54.02           C  
ANISOU  983  CB  SER A 140     7788   5608   7129   1288    -24    764       C  
ATOM    984  N   GLU A 141      -4.612  69.923  28.471  1.00 51.73           N  
ANISOU  984  N   GLU A 141     7569   5040   7044   1596   -181    946       N  
ATOM    985  CA  GLU A 141      -4.723  68.576  29.022  1.00 54.62           C  
ANISOU  985  CA  GLU A 141     8115   5231   7406   1640   -189   1062       C  
ATOM    986  C   GLU A 141      -6.177  68.152  29.210  1.00 56.29           C  
ANISOU  986  C   GLU A 141     8547   5343   7496   1455    -22   1089       C  
ATOM    987  O   GLU A 141      -6.543  67.027  28.854  1.00 59.60           O  
ANISOU  987  O   GLU A 141     9058   5596   7990   1427     67   1089       O  
ATOM    988  CB  GLU A 141      -3.959  68.461  30.347  1.00 55.47           C  
ANISOU  988  CB  GLU A 141     8277   5373   7426   1779   -393   1221       C  
ATOM    989  N   LYS A 142      -7.016  69.028  29.768  1.00 51.94           N  
ANISOU  989  N   LYS A 142     8074   4894   6768   1324     21   1100       N  
ATOM    990  CA  LYS A 142      -8.415  68.684  29.993  1.00 49.32           C  
ANISOU  990  CA  LYS A 142     7918   4488   6332   1138    190   1113       C  
ATOM    991  C   LYS A 142      -9.321  69.052  28.826  1.00 35.89           C  
ANISOU  991  C   LYS A 142     6130   2808   4700    981    360    946       C  
ATOM    992  O   LYS A 142     -10.413  68.490  28.713  1.00 51.14           O  
ANISOU  992  O   LYS A 142     8158   4657   6616    836    505    923       O  
ATOM    993  CB  LYS A 142      -8.932  69.356  31.270  1.00 47.44           C  
ANISOU  993  CB  LYS A 142     7817   4348   5859   1072    164   1203       C  
ATOM    994  N   THR A 143      -8.902  69.964  27.956  1.00 37.58           N  
ANISOU  994  N   THR A 143     6155   3133   4990   1003    341    826       N  
ATOM    995  CA  THR A 143      -9.730  70.350  26.819  1.00 31.97           C  
ANISOU  995  CA  THR A 143     5358   2457   4333    858    481    667       C  
ATOM    996  C   THR A 143      -9.692  69.254  25.762  1.00 36.09           C  
ANISOU  996  C   THR A 143     5846   2869   4998    862    546    588       C  
ATOM    997  O   THR A 143      -8.617  68.771  25.394  1.00 35.69           O  
ANISOU  997  O   THR A 143     5723   2778   5059   1008    472    587       O  
ATOM    998  CB  THR A 143      -9.255  71.681  26.241  1.00 34.85           C  
ANISOU  998  CB  THR A 143     5546   2973   4722    879    437    575       C  
ATOM    999  OG1 THR A 143      -9.362  72.687  27.252  1.00 40.51           O  
ANISOU  999  OG1 THR A 143     6315   3783   5295    874    367    641       O  
ATOM   1000  CG2 THR A 143     -10.116  72.105  25.034  1.00 23.28           C  
ANISOU 1000  CG2 THR A 143     3993   1556   3297    729    562    412       C  
ATOM   1001  N   HIS A 144     -10.869  68.832  25.309  1.00 25.63           N  
ANISOU 1001  N   HIS A 144     4571   1498   3669    705    676    517       N  
ATOM   1002  CA  HIS A 144     -10.964  67.839  24.251  1.00 26.29           C  
ANISOU 1002  CA  HIS A 144     4633   1489   3869    693    732    427       C  
ATOM   1003  C   HIS A 144     -10.772  68.515  22.900  1.00 24.46           C  
ANISOU 1003  C   HIS A 144     4225   1380   3688    676    744    270       C  
ATOM   1004  O   HIS A 144     -11.248  69.628  22.686  1.00 22.81           O  
ANISOU 1004  O   HIS A 144     3941   1307   3419    587    763    209       O  
ATOM   1005  CB  HIS A 144     -12.326  67.156  24.304  1.00 26.82           C  
ANISOU 1005  CB  HIS A 144     4807   1472   3910    527    852    408       C  
ATOM   1006  CG  HIS A 144     -12.293  65.711  23.946  1.00 35.06           C  
ANISOU 1006  CG  HIS A 144     5931   2335   5054    551    876    409       C  
ATOM   1007  ND1 HIS A 144     -12.766  65.231  22.742  1.00 32.94           N  
ANISOU 1007  ND1 HIS A 144     5611   2043   4862    483    935    268       N  
ATOM   1008  CD2 HIS A 144     -11.833  64.635  24.629  1.00 31.58           C  
ANISOU 1008  CD2 HIS A 144     5630   1722   4649    642    838    534       C  
ATOM   1009  CE1 HIS A 144     -12.597  63.921  22.703  1.00 31.19           C  
ANISOU 1009  CE1 HIS A 144     5492   1631   4725    528    938    298       C  
ATOM   1010  NE2 HIS A 144     -12.036  63.537  23.834  1.00 32.91           N  
ANISOU 1010  NE2 HIS A 144     5827   1751   4926    625    881    461       N  
ATOM   1011  N   ILE A 145     -10.049  67.859  21.994  1.00 29.29           N  
ANISOU 1011  N   ILE A 145     4780   1945   4405    766    730    205       N  
ATOM   1012  CA  ILE A 145      -9.770  68.418  20.673  1.00 24.02           C  
ANISOU 1012  CA  ILE A 145     3965   1397   3765    756    747     66       C  
ATOM   1013  C   ILE A 145     -10.453  67.543  19.634  1.00 24.53           C  
ANISOU 1013  C   ILE A 145     4060   1398   3862    680    816    -39       C  
ATOM   1014  O   ILE A 145     -10.346  66.320  19.686  1.00 26.53           O  
ANISOU 1014  O   ILE A 145     4404   1491   4184    732    823    -22       O  
ATOM   1015  CB  ILE A 145      -8.260  68.512  20.405  1.00 24.81           C  
ANISOU 1015  CB  ILE A 145     3954   1526   3947    933    680     59       C  
ATOM   1016  CG1 ILE A 145      -7.603  69.508  21.360  1.00 24.31           C  
ANISOU 1016  CG1 ILE A 145     3833   1549   3857   1005    595    150       C  
ATOM   1017  CG2 ILE A 145      -7.975  68.888  18.962  1.00 24.00           C  
ANISOU 1017  CG2 ILE A 145     3728   1532   3860    917    726    -81       C  
ATOM   1018  CD1 ILE A 145      -6.080  69.308  21.425  1.00 26.42           C  
ANISOU 1018  CD1 ILE A 145     3991   1815   4232   1208    505    169       C  
ATOM   1019  N   HIS A 146     -11.163  68.170  18.698  1.00 22.93           N  
ANISOU 1019  N   HIS A 146     3788   1315   3609    563    851   -144       N  
ATOM   1020  CA  HIS A 146     -11.835  67.448  17.622  1.00 23.44           C  
ANISOU 1020  CA  HIS A 146     3872   1341   3694    494    894   -252       C  
ATOM   1021  C   HIS A 146     -11.540  68.179  16.319  1.00 22.33           C  
ANISOU 1021  C   HIS A 146     3620   1346   3519    492    884   -356       C  
ATOM   1022  O   HIS A 146     -11.863  69.362  16.191  1.00 20.53           O  
ANISOU 1022  O   HIS A 146     3321   1261   3218    423    866   -363       O  
ATOM   1023  CB  HIS A 146     -13.342  67.359  17.882  1.00 23.07           C  
ANISOU 1023  CB  HIS A 146     3878   1282   3607    332    939   -263       C  
ATOM   1024  CG  HIS A 146     -14.041  66.339  17.037  1.00 24.31           C  
ANISOU 1024  CG  HIS A 146     4079   1348   3810    272    974   -358       C  
ATOM   1025  ND1 HIS A 146     -15.135  65.628  17.482  1.00 25.33           N  
ANISOU 1025  ND1 HIS A 146     4292   1373   3961    161   1028   -351       N  
ATOM   1026  CD2 HIS A 146     -13.775  65.877  15.790  1.00 29.62           C  
ANISOU 1026  CD2 HIS A 146     4733   2011   4513    309    964   -465       C  
ATOM   1027  CE1 HIS A 146     -15.541  64.803  16.532  1.00 27.45           C  
ANISOU 1027  CE1 HIS A 146     4581   1568   4279    129   1040   -455       C  
ATOM   1028  NE2 HIS A 146     -14.730  64.927  15.496  1.00 26.31           N  
ANISOU 1028  NE2 HIS A 146     4383   1479   4134    223    998   -527       N  
ATOM   1029  N   ILE A 147     -10.907  67.484  15.367  1.00 23.62           N  
ANISOU 1029  N   ILE A 147     3778   1465   3731    574    896   -432       N  
ATOM   1030  CA  ILE A 147     -10.436  68.078  14.118  1.00 23.09           C  
ANISOU 1030  CA  ILE A 147     3625   1523   3624    593    902   -521       C  
ATOM   1031  C   ILE A 147     -11.219  67.481  12.961  1.00 24.13           C  
ANISOU 1031  C   ILE A 147     3803   1632   3735    531    919   -635       C  
ATOM   1032  O   ILE A 147     -11.417  66.259  12.910  1.00 25.77           O  
ANISOU 1032  O   ILE A 147     4093   1690   4007    553    936   -671       O  
ATOM   1033  CB  ILE A 147      -8.928  67.819  13.890  1.00 24.44           C  
ANISOU 1033  CB  ILE A 147     3742   1681   3862    759    914   -534       C  
ATOM   1034  CG1 ILE A 147      -8.087  68.196  15.117  1.00 24.42           C  
ANISOU 1034  CG1 ILE A 147     3696   1677   3908    851    875   -423       C  
ATOM   1035  CG2 ILE A 147      -8.446  68.542  12.631  1.00 24.01           C  
ANISOU 1035  CG2 ILE A 147     3603   1769   3751    763    947   -617       C  
ATOM   1036  CD1 ILE A 147      -8.143  69.648  15.451  1.00 22.40           C  
ANISOU 1036  CD1 ILE A 147     3361   1567   3583    783    854   -378       C  
ATOM   1037  N   PHE A 148     -11.608  68.327  12.002  1.00 22.55           N  
ANISOU 1037  N   PHE A 148     3554   1566   3447    466    905   -694       N  
ATOM   1038  CA  PHE A 148     -12.197  67.904  10.737  1.00 23.35           C  
ANISOU 1038  CA  PHE A 148     3694   1663   3514    432    912   -812       C  
ATOM   1039  C   PHE A 148     -11.375  68.425   9.560  1.00 23.57           C  
ANISOU 1039  C   PHE A 148     3679   1792   3483    493    940   -875       C  
ATOM   1040  O   PHE A 148     -10.810  69.508   9.616  1.00 22.38           O  
ANISOU 1040  O   PHE A 148     3456   1758   3290    502    936   -825       O  
ATOM   1041  CB  PHE A 148     -13.638  68.404  10.555  1.00 22.37           C  
ANISOU 1041  CB  PHE A 148     3576   1591   3333    294    882   -834       C  
ATOM   1042  CG  PHE A 148     -14.599  67.946  11.620  1.00 23.57           C  
ANISOU 1042  CG  PHE A 148     3762   1661   3534    212    878   -788       C  
ATOM   1043  CD1 PHE A 148     -14.768  68.684  12.776  1.00 22.54           C  
ANISOU 1043  CD1 PHE A 148     3593   1581   3389    177    861   -686       C  
ATOM   1044  CD2 PHE A 148     -15.362  66.808  11.445  1.00 26.99           C  
ANISOU 1044  CD2 PHE A 148     4267   1965   4022    166    898   -855       C  
ATOM   1045  CE1 PHE A 148     -15.665  68.295  13.751  1.00 24.94           C  
ANISOU 1045  CE1 PHE A 148     3933   1816   3727     98    880   -647       C  
ATOM   1046  CE2 PHE A 148     -16.271  66.402  12.424  1.00 24.11           C  
ANISOU 1046  CE2 PHE A 148     3934   1525   3703     76    913   -812       C  
ATOM   1047  CZ  PHE A 148     -16.423  67.159  13.583  1.00 22.67           C  
ANISOU 1047  CZ  PHE A 148     3714   1404   3498     43    911   -706       C  
ATOM   1048  N   SER A 149     -11.334  67.660   8.476  1.00 25.27           N  
ANISOU 1048  N   SER A 149     3946   1961   3693    532    973   -991       N  
ATOM   1049  CA  SER A 149     -10.768  68.127   7.211  1.00 25.76           C  
ANISOU 1049  CA  SER A 149     3989   2124   3674    574   1012  -1067       C  
ATOM   1050  C   SER A 149     -11.898  68.330   6.200  1.00 25.82           C  
ANISOU 1050  C   SER A 149     4054   2167   3588    488    980  -1154       C  
ATOM   1051  O   SER A 149     -13.068  68.042   6.471  1.00 25.82           O  
ANISOU 1051  O   SER A 149     4092   2113   3605    402    929  -1165       O  
ATOM   1052  CB  SER A 149      -9.734  67.130   6.682  1.00 28.02           C  
ANISOU 1052  CB  SER A 149     4292   2345   4011    711   1077  -1151       C  
ATOM   1053  OG  SER A 149     -10.389  66.030   6.082  1.00 29.72           O  
ANISOU 1053  OG  SER A 149     4607   2445   4241    706   1075  -1265       O  
ATOM   1054  N   PHE A 150     -11.556  68.835   5.024  1.00 26.31           N  
ANISOU 1054  N   PHE A 150     4121   2326   3550    515   1008  -1220       N  
ATOM   1055  CA  PHE A 150     -12.543  68.995   3.959  1.00 26.99           C  
ANISOU 1055  CA  PHE A 150     4274   2448   3535    463    961  -1319       C  
ATOM   1056  C   PHE A 150     -12.720  67.728   3.128  1.00 34.65           C  
ANISOU 1056  C   PHE A 150     5334   3321   4511    510    976  -1469       C  
ATOM   1057  O   PHE A 150     -13.568  67.703   2.225  1.00 31.43           O  
ANISOU 1057  O   PHE A 150     4993   2930   4020    478    922  -1574       O  
ATOM   1058  CB  PHE A 150     -12.160  70.153   3.037  1.00 26.46           C  
ANISOU 1058  CB  PHE A 150     4194   2526   3335    472    980  -1323       C  
ATOM   1059  CG  PHE A 150     -12.330  71.508   3.662  1.00 25.02           C  
ANISOU 1059  CG  PHE A 150     3949   2429   3129    406    937  -1200       C  
ATOM   1060  CD1 PHE A 150     -11.354  72.026   4.498  1.00 27.27           C  
ANISOU 1060  CD1 PHE A 150     4150   2742   3468    425    982  -1091       C  
ATOM   1061  CD2 PHE A 150     -13.471  72.268   3.412  1.00 23.42           C  
ANISOU 1061  CD2 PHE A 150     3770   2276   2855    337    842  -1206       C  
ATOM   1062  CE1 PHE A 150     -11.508  73.280   5.079  1.00 21.84           C  
ANISOU 1062  CE1 PHE A 150     3415   2122   2762    367    938   -990       C  
ATOM   1063  CE2 PHE A 150     -13.640  73.513   3.984  1.00 21.60           C  
ANISOU 1063  CE2 PHE A 150     3488   2111   2608    288    800  -1104       C  
ATOM   1064  CZ  PHE A 150     -12.655  74.031   4.820  1.00 21.85           C  
ANISOU 1064  CZ  PHE A 150     3448   2164   2691    297    851   -995       C  
ATOM   1065  N   THR A 151     -11.949  66.679   3.412  1.00 30.54           N  
ANISOU 1065  N   THR A 151     4824   2694   4087    595   1036  -1492       N  
ATOM   1066  CA  THR A 151     -12.006  65.445   2.632  1.00 33.08           C  
ANISOU 1066  CA  THR A 151     5238   2908   4423    654   1054  -1646       C  
ATOM   1067  C   THR A 151     -12.456  64.253   3.473  1.00 34.25           C  
ANISOU 1067  C   THR A 151     5435   2866   4713    636   1031  -1644       C  
ATOM   1068  O   THR A 151     -12.127  63.105   3.150  1.00 40.09           O  
ANISOU 1068  O   THR A 151     6243   3478   5511    715   1061  -1745       O  
ATOM   1069  CB  THR A 151     -10.648  65.184   1.989  1.00 34.79           C  
ANISOU 1069  CB  THR A 151     5440   3157   4623    793   1155  -1708       C  
ATOM   1070  OG1 THR A 151      -9.622  65.324   2.976  1.00 39.90           O  
ANISOU 1070  OG1 THR A 151     5991   3803   5365    856   1197  -1592       O  
ATOM   1071  CG2 THR A 151     -10.401  66.199   0.880  1.00 35.90           C  
ANISOU 1071  CG2 THR A 151     5569   3472   4600    794   1190  -1746       C  
ATOM   1072  N   GLY A 152     -13.192  64.498   4.549  1.00 32.27           N  
ANISOU 1072  N   GLY A 152     5155   2589   4516    535    985  -1533       N  
ATOM   1073  CA  GLY A 152     -13.843  63.444   5.296  1.00 35.94           C  
ANISOU 1073  CA  GLY A 152     5678   2879   5099    485    967  -1530       C  
ATOM   1074  C   GLY A 152     -13.056  62.846   6.439  1.00 41.08           C  
ANISOU 1074  C   GLY A 152     6323   3416   5871    557   1000  -1430       C  
ATOM   1075  O   GLY A 152     -13.526  61.876   7.045  1.00 42.06           O  
ANISOU 1075  O   GLY A 152     6517   3370   6095    524    993  -1424       O  
ATOM   1076  N   GLU A 153     -11.880  63.374   6.757  1.00 35.98           N  
ANISOU 1076  N   GLU A 153     5602   2848   5222    657   1029  -1353       N  
ATOM   1077  CA  GLU A 153     -11.121  62.825   7.869  1.00 33.70           C  
ANISOU 1077  CA  GLU A 153     5309   2450   5047    745   1034  -1261       C  
ATOM   1078  C   GLU A 153     -11.423  63.579   9.148  1.00 31.01           C  
ANISOU 1078  C   GLU A 153     4916   2158   4708    669   1000  -1104       C  
ATOM   1079  O   GLU A 153     -11.713  64.777   9.140  1.00 28.96           O  
ANISOU 1079  O   GLU A 153     4586   2055   4361    594    986  -1058       O  
ATOM   1080  CB  GLU A 153      -9.618  62.862   7.600  1.00 34.03           C  
ANISOU 1080  CB  GLU A 153     5286   2537   5105    916   1074  -1279       C  
ATOM   1081  CG  GLU A 153      -9.214  62.107   6.365  1.00 42.72           C  
ANISOU 1081  CG  GLU A 153     6437   3598   6199   1011   1122  -1444       C  
ATOM   1082  CD  GLU A 153      -8.409  62.962   5.428  1.00 54.41           C  
ANISOU 1082  CD  GLU A 153     7832   5265   7578   1067   1182  -1492       C  
ATOM   1083  OE1 GLU A 153      -8.782  64.145   5.247  1.00 53.17           O  
ANISOU 1083  OE1 GLU A 153     7626   5261   7317    965   1174  -1441       O  
ATOM   1084  OE2 GLU A 153      -7.413  62.455   4.865  1.00 57.27           O  
ANISOU 1084  OE2 GLU A 153     8179   5617   7965   1215   1241  -1583       O  
ATOM   1085  N   GLU A 154     -11.338  62.862  10.259  1.00 31.86           N  
ANISOU 1085  N   GLU A 154     5073   2116   4915    695    991  -1021       N  
ATOM   1086  CA  GLU A 154     -11.466  63.503  11.556  1.00 30.19           C  
ANISOU 1086  CA  GLU A 154     4829   1936   4704    647    976   -872       C  
ATOM   1087  C   GLU A 154     -10.505  62.814  12.508  1.00 36.34           C  
ANISOU 1087  C   GLU A 154     5643   2574   5589    783    975   -788       C  
ATOM   1088  O   GLU A 154     -10.040  61.691  12.260  1.00 39.04           O  
ANISOU 1088  O   GLU A 154     6053   2760   6021    888    980   -843       O  
ATOM   1089  CB  GLU A 154     -12.920  63.478  12.063  1.00 29.52           C  
ANISOU 1089  CB  GLU A 154     4791   1820   4605    479    970   -842       C  
ATOM   1090  CG  GLU A 154     -13.457  62.141  12.501  1.00 48.98           C  
ANISOU 1090  CG  GLU A 154     7379   4063   7169    447    990   -843       C  
ATOM   1091  CD  GLU A 154     -14.964  62.189  12.733  1.00 44.07           C  
ANISOU 1091  CD  GLU A 154     6776   3441   6529    265   1002   -851       C  
ATOM   1092  OE1 GLU A 154     -15.688  61.387  12.108  1.00 47.04           O  
ANISOU 1092  OE1 GLU A 154     7210   3719   6944    201   1005   -955       O  
ATOM   1093  OE2 GLU A 154     -15.428  63.038  13.527  1.00 34.88           O  
ANISOU 1093  OE2 GLU A 154     5563   2376   5316    189   1007   -764       O  
ATOM   1094  N   MET A 155     -10.176  63.528  13.571  1.00 30.47           N  
ANISOU 1094  N   MET A 155     4855   1886   4835    795    954   -659       N  
ATOM   1095  CA  MET A 155      -9.214  63.087  14.569  1.00 36.70           C  
ANISOU 1095  CA  MET A 155     5664   2566   5713    939    923   -560       C  
ATOM   1096  C   MET A 155      -9.617  63.752  15.876  1.00 36.57           C  
ANISOU 1096  C   MET A 155     5659   2581   5655    869    899   -414       C  
ATOM   1097  O   MET A 155      -9.713  64.979  15.935  1.00 30.91           O  
ANISOU 1097  O   MET A 155     4852   2037   4855    809    894   -396       O  
ATOM   1098  CB  MET A 155      -7.799  63.486  14.153  1.00 32.65           C  
ANISOU 1098  CB  MET A 155     5032   2150   5225   1102    914   -596       C  
ATOM   1099  CG  MET A 155      -6.722  63.139  15.149  1.00 52.02           C  
ANISOU 1099  CG  MET A 155     7473   4514   7778   1276    854   -501       C  
ATOM   1100  SD  MET A 155      -6.248  61.413  15.083  1.00 77.66           S  
ANISOU 1100  SD  MET A 155    10831   7504  11174   1437    831   -543       S  
ATOM   1101  CE  MET A 155      -5.351  61.249  16.625  1.00 70.17           C  
ANISOU 1101  CE  MET A 155     9886   6458  10318   1600    718   -371       C  
ATOM   1102  N   ALA A 156      -9.897  62.960  16.904  1.00 33.71           N  
ANISOU 1102  N   ALA A 156     5419   2048   5342    871    887   -312       N  
ATOM   1103  CA  ALA A 156     -10.308  63.508  18.185  1.00 30.87           C  
ANISOU 1103  CA  ALA A 156     5094   1709   4925    808    874   -171       C  
ATOM   1104  C   ALA A 156      -9.507  62.868  19.308  1.00 32.89           C  
ANISOU 1104  C   ALA A 156     5434   1817   5247    952    809    -31       C  
ATOM   1105  O   ALA A 156      -9.003  61.746  19.174  1.00 35.31           O  
ANISOU 1105  O   ALA A 156     5806   1951   5658   1063    786    -38       O  
ATOM   1106  CB  ALA A 156     -11.807  63.295  18.429  1.00 30.58           C  
ANISOU 1106  CB  ALA A 156     5144   1632   4844    616    938   -167       C  
ATOM   1107  N   THR A 157      -9.401  63.597  20.413  1.00 32.09           N  
ANISOU 1107  N   THR A 157     5334   1777   5080    956    769     97       N  
ATOM   1108  CA  THR A 157      -8.697  63.124  21.597  1.00 35.09           C  
ANISOU 1108  CA  THR A 157     5800   2040   5495   1091    683    256       C  
ATOM   1109  C   THR A 157      -9.208  61.745  22.022  1.00 36.61           C  
ANISOU 1109  C   THR A 157     6181   1994   5736   1066    707    326       C  
ATOM   1110  O   THR A 157     -10.415  61.538  22.189  1.00 36.41           O  
ANISOU 1110  O   THR A 157     6249   1928   5657    892    796    334       O  
ATOM   1111  CB  THR A 157      -8.874  64.155  22.721  1.00 32.70           C  
ANISOU 1111  CB  THR A 157     5503   1851   5072   1050    650    377       C  
ATOM   1112  OG1 THR A 157      -8.319  65.413  22.310  1.00 30.62           O  
ANISOU 1112  OG1 THR A 157     5065   1787   4784   1080    620    311       O  
ATOM   1113  CG2 THR A 157      -8.187  63.720  23.997  1.00 34.89           C  
ANISOU 1113  CG2 THR A 157     5880   2026   5351   1187    541    558       C  
ATOM   1114  N   LYS A 158      -8.282  60.790  22.133  1.00 42.91           N  
ANISOU 1114  N   LYS A 158     7021   2630   6651   1242    630    366       N  
ATOM   1115  CA  LYS A 158      -8.567  59.434  22.615  1.00 44.75           C  
ANISOU 1115  CA  LYS A 158     7445   2606   6951   1249    632    456       C  
ATOM   1116  C   LYS A 158      -9.550  58.690  21.709  1.00 43.87           C  
ANISOU 1116  C   LYS A 158     7395   2394   6882   1106    741    328       C  
ATOM   1117  O   LYS A 158     -10.251  57.779  22.158  1.00 46.73           O  
ANISOU 1117  O   LYS A 158     7923   2568   7264   1020    784    400       O  
ATOM   1118  CB  LYS A 158      -9.079  59.456  24.064  1.00 42.93           C  
ANISOU 1118  CB  LYS A 158     7369   2331   6612   1180    627    660       C  
ATOM   1119  CG  LYS A 158      -8.076  59.963  25.122  1.00 46.90           C  
ANISOU 1119  CG  LYS A 158     7852   2898   7071   1342    489    815       C  
ATOM   1120  CD  LYS A 158      -6.612  59.752  24.711  1.00 60.03           C  
ANISOU 1120  CD  LYS A 158     9382   4543   8883   1586    361    771       C  
ATOM   1121  CE  LYS A 158      -5.952  61.060  24.233  1.00 62.90           C  
ANISOU 1121  CE  LYS A 158     9516   5157   9228   1634    326    668       C  
ATOM   1122  NZ  LYS A 158      -4.651  60.865  23.534  1.00 63.56           N  
ANISOU 1122  NZ  LYS A 158     9433   5245   9473   1840    247    566       N  
ATOM   1123  N   ALA A 159      -9.602  59.070  20.429  1.00 40.99           N  
ANISOU 1123  N   ALA A 159     6898   2152   6525   1076    781    141       N  
ATOM   1124  CA  ALA A 159     -10.578  58.538  19.475  1.00 42.22           C  
ANISOU 1124  CA  ALA A 159     7087   2254   6702    933    868      3       C  
ATOM   1125  C   ALA A 159     -11.993  58.550  20.059  1.00 49.43           C  
ANISOU 1125  C   ALA A 159     8091   3146   7542    712    953     61       C  
ATOM   1126  O   ALA A 159     -12.807  57.662  19.802  1.00 42.29           O  
ANISOU 1126  O   ALA A 159     7283   2092   6692    603   1010     18       O  
ATOM   1127  CB  ALA A 159     -10.182  57.138  19.004  1.00 44.27           C  
ANISOU 1127  CB  ALA A 159     7443   2271   7107   1039    846    -53       C  
ATOM   1128  N   ASP A 160     -12.280  59.573  20.865  1.00 38.83           N  
ANISOU 1128  N   ASP A 160     6713   1957   6083    647    963    153       N  
ATOM   1129  CA  ASP A 160     -13.602  59.810  21.436  1.00 40.52           C  
ANISOU 1129  CA  ASP A 160     6979   2200   6217    443   1055    191       C  
ATOM   1130  C   ASP A 160     -14.219  60.952  20.638  1.00 40.77           C  
ANISOU 1130  C   ASP A 160     6847   2466   6178    336   1089     52       C  
ATOM   1131  O   ASP A 160     -13.827  62.112  20.803  1.00 33.13           O  
ANISOU 1131  O   ASP A 160     5776   1679   5132    376   1052     68       O  
ATOM   1132  CB  ASP A 160     -13.494  60.161  22.920  1.00 40.51           C  
ANISOU 1132  CB  ASP A 160     7065   2204   6121    457   1041    384       C  
ATOM   1133  CG  ASP A 160     -14.846  60.447  23.564  1.00 41.56           C  
ANISOU 1133  CG  ASP A 160     7249   2381   6163    249   1153    415       C  
ATOM   1134  OD1 ASP A 160     -15.860  60.535  22.842  1.00 37.28           O  
ANISOU 1134  OD1 ASP A 160     6637   1890   5637     98   1232    279       O  
ATOM   1135  OD2 ASP A 160     -14.898  60.569  24.809  1.00 42.92           O  
ANISOU 1135  OD2 ASP A 160     7528   2537   6244    241   1161    573       O  
ATOM   1136  N   TYR A 161     -15.172  60.628  19.763  1.00 35.34           N  
ANISOU 1136  N   TYR A 161     6135   1769   5522    206   1145    -82       N  
ATOM   1137  CA  TYR A 161     -15.645  61.602  18.786  1.00 42.36           C  
ANISOU 1137  CA  TYR A 161     6868   2869   6358    136   1145   -222       C  
ATOM   1138  C   TYR A 161     -16.862  62.377  19.256  1.00 31.56           C  
ANISOU 1138  C   TYR A 161     5456   1622   4915    -30   1207   -222       C  
ATOM   1139  O   TYR A 161     -17.433  63.133  18.463  1.00 29.88           O  
ANISOU 1139  O   TYR A 161     5119   1569   4665    -97   1198   -335       O  
ATOM   1140  CB  TYR A 161     -15.940  60.900  17.460  1.00 36.64           C  
ANISOU 1140  CB  TYR A 161     6131   2088   5703    111   1143   -382       C  
ATOM   1141  CG  TYR A 161     -14.682  60.383  16.797  1.00 34.90           C  
ANISOU 1141  CG  TYR A 161     5920   1798   5543    291   1085   -422       C  
ATOM   1142  CD1 TYR A 161     -13.734  61.255  16.276  1.00 39.99           C  
ANISOU 1142  CD1 TYR A 161     6447   2607   6141    406   1036   -454       C  
ATOM   1143  CD2 TYR A 161     -14.436  59.018  16.708  1.00 46.36           C  
ANISOU 1143  CD2 TYR A 161     7496   3011   7106    346   1085   -432       C  
ATOM   1144  CE1 TYR A 161     -12.576  60.780  15.671  1.00 43.89           C  
ANISOU 1144  CE1 TYR A 161     6934   3046   6695    574    999   -504       C  
ATOM   1145  CE2 TYR A 161     -13.284  58.536  16.109  1.00 50.25           C  
ANISOU 1145  CE2 TYR A 161     7990   3439   7664    526   1035   -485       C  
ATOM   1146  CZ  TYR A 161     -12.360  59.422  15.595  1.00 54.99           C  
ANISOU 1146  CZ  TYR A 161     8459   4222   8213    640    998   -525       C  
ATOM   1147  OH  TYR A 161     -11.219  58.938  14.997  1.00 59.02           O  
ANISOU 1147  OH  TYR A 161     8957   4677   8791    822    965   -592       O  
ATOM   1148  N   THR A 162     -17.280  62.172  20.511  1.00 32.54           N  
ANISOU 1148  N   THR A 162     5683   1669   5013    -93   1267    -97       N  
ATOM   1149  CA  THR A 162     -18.319  62.926  21.203  1.00 34.73           C  
ANISOU 1149  CA  THR A 162     5929   2056   5211   -231   1339    -84       C  
ATOM   1150  C   THR A 162     -19.712  62.740  20.612  1.00 34.58           C  
ANISOU 1150  C   THR A 162     5850   2055   5235   -406   1409   -218       C  
ATOM   1151  O   THR A 162     -20.638  62.337  21.323  1.00 36.55           O  
ANISOU 1151  O   THR A 162     6162   2233   5494   -539   1509   -188       O  
ATOM   1152  CB  THR A 162     -17.957  64.410  21.231  1.00 30.26           C  
ANISOU 1152  CB  THR A 162     5239   1707   4550   -178   1285    -92       C  
ATOM   1153  OG1 THR A 162     -16.745  64.570  21.968  1.00 29.36           O  
ANISOU 1153  OG1 THR A 162     5184   1569   4401    -30   1221     41       O  
ATOM   1154  CG2 THR A 162     -19.044  65.213  21.903  1.00 31.64           C  
ANISOU 1154  CG2 THR A 162     5378   1992   4652   -310   1358   -100       C  
ATOM   1155  N   LEU A 163     -19.882  63.055  19.336  1.00 30.78           N  
ANISOU 1155  N   LEU A 163     5244   1675   4775   -407   1355   -365       N  
ATOM   1156  CA  LEU A 163     -21.177  62.947  18.688  1.00 31.19           C  
ANISOU 1156  CA  LEU A 163     5221   1758   4870   -557   1391   -502       C  
ATOM   1157  C   LEU A 163     -21.352  61.562  18.076  1.00 33.72           C  
ANISOU 1157  C   LEU A 163     5626   1882   5303   -593   1401   -564       C  
ATOM   1158  O   LEU A 163     -20.403  60.785  17.962  1.00 36.23           O  
ANISOU 1158  O   LEU A 163     6045   2058   5663   -483   1368   -519       O  
ATOM   1159  CB  LEU A 163     -21.330  63.997  17.596  1.00 29.00           C  
ANISOU 1159  CB  LEU A 163     4785   1685   4548   -536   1304   -620       C  
ATOM   1160  CG  LEU A 163     -21.056  65.436  18.010  1.00 26.50           C  
ANISOU 1160  CG  LEU A 163     4381   1558   4130   -488   1270   -572       C  
ATOM   1161  CD1 LEU A 163     -20.938  66.286  16.773  1.00 24.81           C  
ANISOU 1161  CD1 LEU A 163     4046   1503   3876   -440   1162   -666       C  
ATOM   1162  CD2 LEU A 163     -22.187  65.889  18.901  1.00 28.82           C  
ANISOU 1162  CD2 LEU A 163     4641   1905   4405   -615   1359   -572       C  
ATOM   1163  N   ASP A 164     -22.573  61.279  17.628  1.00 34.72           N  
ANISOU 1163  N   ASP A 164     5702   2003   5487   -743   1438   -683       N  
ATOM   1164  CA  ASP A 164     -22.819  60.015  16.943  1.00 37.24           C  
ANISOU 1164  CA  ASP A 164     6096   2136   5918   -792   1436   -767       C  
ATOM   1165  C   ASP A 164     -22.437  60.119  15.462  1.00 39.84           C  
ANISOU 1165  C   ASP A 164     6366   2530   6240   -704   1320   -905       C  
ATOM   1166  O   ASP A 164     -22.264  61.212  14.912  1.00 34.22           O  
ANISOU 1166  O   ASP A 164     5540   2020   5441   -643   1249   -944       O  
ATOM   1167  CB  ASP A 164     -24.280  59.574  17.118  1.00 40.04           C  
ANISOU 1167  CB  ASP A 164     6425   2438   6351  -1001   1525   -842       C  
ATOM   1168  CG  ASP A 164     -25.290  60.589  16.591  1.00 49.37           C  
ANISOU 1168  CG  ASP A 164     7419   3838   7502  -1080   1498   -972       C  
ATOM   1169  OD1 ASP A 164     -26.468  60.508  17.005  1.00 57.16           O  
ANISOU 1169  OD1 ASP A 164     8350   4826   8541  -1244   1586  -1017       O  
ATOM   1170  OD2 ASP A 164     -24.932  61.456  15.765  1.00 55.32           O  
ANISOU 1170  OD2 ASP A 164     8079   4755   8185   -980   1389  -1028       O  
ATOM   1171  N   GLU A 165     -22.305  58.949  14.817  1.00 38.85           N  
ANISOU 1171  N   GLU A 165     6337   2221   6205   -698   1302   -978       N  
ATOM   1172  CA  GLU A 165     -21.789  58.902  13.449  1.00 38.66           C  
ANISOU 1172  CA  GLU A 165     6296   2231   6163   -594   1201  -1105       C  
ATOM   1173  C   GLU A 165     -22.634  59.750  12.502  1.00 38.39           C  
ANISOU 1173  C   GLU A 165     6127   2392   6068   -655   1133  -1239       C  
ATOM   1174  O   GLU A 165     -22.097  60.368  11.576  1.00 41.78           O  
ANISOU 1174  O   GLU A 165     6511   2950   6413   -549   1050  -1294       O  
ATOM   1175  CB  GLU A 165     -21.709  57.451  12.953  1.00 41.78           C  
ANISOU 1175  CB  GLU A 165     6826   2378   6672   -598   1198  -1185       C  
ATOM   1176  N   GLU A 166     -23.957  59.796  12.716  1.00 38.05           N  
ANISOU 1176  N   GLU A 166     6019   2370   6069   -825   1170  -1294       N  
ATOM   1177  CA  GLU A 166     -24.823  60.578  11.837  1.00 38.26           C  
ANISOU 1177  CA  GLU A 166     5916   2570   6049   -874   1088  -1423       C  
ATOM   1178  C   GLU A 166     -24.524  62.071  11.933  1.00 39.91           C  
ANISOU 1178  C   GLU A 166     6017   3012   6135   -791   1042  -1358       C  
ATOM   1179  O   GLU A 166     -24.481  62.769  10.913  1.00 38.99           O  
ANISOU 1179  O   GLU A 166     5847   3025   5943   -736    954  -1438       O  
ATOM   1180  CB  GLU A 166     -26.290  60.319  12.167  1.00 43.99           C  
ANISOU 1180  CB  GLU A 166     6574   3272   6869  -1071   1146  -1497       C  
ATOM   1181  N   SER A 167     -24.344  62.589  13.148  1.00 35.40           N  
ANISOU 1181  N   SER A 167     5424   2484   5543   -794   1120  -1223       N  
ATOM   1182  CA  SER A 167     -24.028  64.007  13.289  1.00 31.71           C  
ANISOU 1182  CA  SER A 167     4863   2220   4967   -718   1073  -1163       C  
ATOM   1183  C   SER A 167     -22.680  64.333  12.653  1.00 28.88           C  
ANISOU 1183  C   SER A 167     4539   1903   4530   -555   1002  -1128       C  
ATOM   1184  O   SER A 167     -22.551  65.326  11.931  1.00 29.83           O  
ANISOU 1184  O   SER A 167     4590   2174   4569   -503    931  -1161       O  
ATOM   1185  CB  SER A 167     -24.049  64.415  14.760  1.00 36.65           C  
ANISOU 1185  CB  SER A 167     5482   2862   5582   -752   1176  -1035       C  
ATOM   1186  OG  SER A 167     -25.353  64.269  15.300  1.00 45.65           O  
ANISOU 1186  OG  SER A 167     6569   3991   6785   -909   1261  -1085       O  
ATOM   1187  N   ARG A 168     -21.665  63.504  12.906  1.00 29.74           N  
ANISOU 1187  N   ARG A 168     4756   1873   4673   -474   1033  -1066       N  
ATOM   1188  CA  ARG A 168     -20.350  63.754  12.323  1.00 28.98           C  
ANISOU 1188  CA  ARG A 168     4677   1814   4521   -322    990  -1047       C  
ATOM   1189  C   ARG A 168     -20.392  63.655  10.804  1.00 30.36           C  
ANISOU 1189  C   ARG A 168     4854   2015   4668   -294    933  -1195       C  
ATOM   1190  O   ARG A 168     -19.750  64.450  10.107  1.00 28.55           O  
ANISOU 1190  O   ARG A 168     4586   1909   4351   -209    889  -1205       O  
ATOM   1191  CB  ARG A 168     -19.321  62.781  12.900  1.00 33.70           C  
ANISOU 1191  CB  ARG A 168     5384   2240   5181   -233   1031   -968       C  
ATOM   1192  CG  ARG A 168     -18.951  63.080  14.346  1.00 37.06           C  
ANISOU 1192  CG  ARG A 168     5825   2654   5602   -220   1086   -808       C  
ATOM   1193  CD  ARG A 168     -18.869  61.811  15.164  1.00 39.36           C  
ANISOU 1193  CD  ARG A 168     6253   2712   5988   -232   1154   -740       C  
ATOM   1194  NE  ARG A 168     -17.925  60.866  14.583  1.00 43.11           N  
ANISOU 1194  NE  ARG A 168     6809   3044   6525   -110   1125   -774       N  
ATOM   1195  CZ  ARG A 168     -17.848  59.588  14.937  1.00 49.66           C  
ANISOU 1195  CZ  ARG A 168     7773   3639   7457   -106   1159   -747       C  
ATOM   1196  NH1 ARG A 168     -18.654  59.105  15.879  1.00 52.63           N  
ANISOU 1196  NH1 ARG A 168     8223   3898   7875   -231   1230   -674       N  
ATOM   1197  NH2 ARG A 168     -16.959  58.802  14.358  1.00 45.86           N  
ANISOU 1197  NH2 ARG A 168     7354   3034   7034     25   1125   -794       N  
ATOM   1198  N   ALA A 169     -21.129  62.674  10.271  1.00 31.89           N  
ANISOU 1198  N   ALA A 169     5102   2086   4929   -369    932  -1314       N  
ATOM   1199  CA  ALA A 169     -21.292  62.587   8.823  1.00 32.84           C  
ANISOU 1199  CA  ALA A 169     5238   2232   5007   -348    865  -1469       C  
ATOM   1200  C   ALA A 169     -21.908  63.861   8.253  1.00 31.29           C  
ANISOU 1200  C   ALA A 169     4945   2234   4711   -372    790  -1507       C  
ATOM   1201  O   ALA A 169     -21.524  64.312   7.167  1.00 31.12           O  
ANISOU 1201  O   ALA A 169     4936   2293   4593   -294    730  -1571       O  
ATOM   1202  CB  ALA A 169     -22.136  61.358   8.458  1.00 35.59           C  
ANISOU 1202  CB  ALA A 169     5659   2411   5453   -447    865  -1597       C  
ATOM   1203  N   ARG A 170     -22.849  64.474   8.976  1.00 30.33           N  
ANISOU 1203  N   ARG A 170     4731   2189   4605   -471    794  -1467       N  
ATOM   1204  CA  ARG A 170     -23.466  65.691   8.451  1.00 29.10           C  
ANISOU 1204  CA  ARG A 170     4486   2206   4365   -480    709  -1504       C  
ATOM   1205  C   ARG A 170     -22.456  66.840   8.378  1.00 26.95           C  
ANISOU 1205  C   ARG A 170     4191   2063   3985   -365    686  -1407       C  
ATOM   1206  O   ARG A 170     -22.458  67.619   7.418  1.00 26.53           O  
ANISOU 1206  O   ARG A 170     4134   2112   3834   -317    604  -1455       O  
ATOM   1207  CB  ARG A 170     -24.666  66.093   9.302  1.00 41.28           C  
ANISOU 1207  CB  ARG A 170     5921   3801   5961   -599    727  -1492       C  
ATOM   1208  CG  ARG A 170     -25.544  67.140   8.638  1.00 46.88           C  
ANISOU 1208  CG  ARG A 170     6542   4657   6611   -614    621  -1568       C  
ATOM   1209  CD  ARG A 170     -26.159  68.096   9.655  1.00 50.20           C  
ANISOU 1209  CD  ARG A 170     6841   5186   7047   -657    644  -1500       C  
ATOM   1210  NE  ARG A 170     -26.600  69.347   9.037  1.00 56.43           N  
ANISOU 1210  NE  ARG A 170     7563   6121   7757   -617    531  -1535       N  
ATOM   1211  CZ  ARG A 170     -26.871  70.466   9.707  1.00 57.88           C  
ANISOU 1211  CZ  ARG A 170     7654   6416   7923   -608    523  -1473       C  
ATOM   1212  NH1 ARG A 170     -26.745  70.504  11.028  1.00 59.00           N  
ANISOU 1212  NH1 ARG A 170     7760   6550   8107   -640    626  -1377       N  
ATOM   1213  NH2 ARG A 170     -27.264  71.554   9.052  1.00 62.09           N  
ANISOU 1213  NH2 ARG A 170     8147   7058   8388   -562    409  -1509       N  
ATOM   1214  N   ILE A 171     -21.583  66.951   9.380  1.00 25.79           N  
ANISOU 1214  N   ILE A 171     4042   1906   3852   -322    753  -1272       N  
ATOM   1215  CA  ILE A 171     -20.510  67.947   9.336  1.00 24.05           C  
ANISOU 1215  CA  ILE A 171     3799   1792   3548   -223    737  -1185       C  
ATOM   1216  C   ILE A 171     -19.542  67.646   8.192  1.00 30.06           C  
ANISOU 1216  C   ILE A 171     4625   2536   4260   -121    727  -1244       C  
ATOM   1217  O   ILE A 171     -19.214  68.524   7.386  1.00 24.21           O  
ANISOU 1217  O   ILE A 171     3873   1903   3422    -68    680  -1259       O  
ATOM   1218  CB  ILE A 171     -19.785  67.995  10.689  1.00 25.98           C  
ANISOU 1218  CB  ILE A 171     4035   2012   3826   -199    802  -1043       C  
ATOM   1219  CG1 ILE A 171     -20.691  68.629  11.749  1.00 28.65           C  
ANISOU 1219  CG1 ILE A 171     4304   2409   4175   -285    811   -989       C  
ATOM   1220  CG2 ILE A 171     -18.484  68.787  10.587  1.00 21.77           C  
ANISOU 1220  CG2 ILE A 171     3484   1559   3228    -94    791   -969       C  
ATOM   1221  CD1 ILE A 171     -20.142  68.510  13.162  1.00 22.44           C  
ANISOU 1221  CD1 ILE A 171     3538   1576   3413   -270    872   -861       C  
ATOM   1222  N   LYS A 172     -19.062  66.400   8.110  1.00 26.55           N  
ANISOU 1222  N   LYS A 172     4258   1950   3881    -87    776  -1281       N  
ATOM   1223  CA  LYS A 172     -18.115  66.044   7.053  1.00 27.62           C  
ANISOU 1223  CA  LYS A 172     4453   2068   3976     20    783  -1353       C  
ATOM   1224  C   LYS A 172     -18.715  66.276   5.668  1.00 28.46           C  
ANISOU 1224  C   LYS A 172     4592   2233   3991     14    710  -1491       C  
ATOM   1225  O   LYS A 172     -18.017  66.721   4.747  1.00 28.52           O  
ANISOU 1225  O   LYS A 172     4618   2317   3902     99    703  -1527       O  
ATOM   1226  CB  LYS A 172     -17.665  64.590   7.219  1.00 30.93           C  
ANISOU 1226  CB  LYS A 172     4955   2302   4495     59    837  -1387       C  
ATOM   1227  CG  LYS A 172     -16.917  64.343   8.513  1.00 29.13           C  
ANISOU 1227  CG  LYS A 172     4720   2007   4343     99    891  -1249       C  
ATOM   1228  CD  LYS A 172     -16.395  62.916   8.594  1.00 32.76           C  
ANISOU 1228  CD  LYS A 172     5277   2267   4904    164    929  -1284       C  
ATOM   1229  CE  LYS A 172     -17.245  62.084   9.513  1.00 41.89           C  
ANISOU 1229  CE  LYS A 172     6487   3270   6161     62    949  -1250       C  
ATOM   1230  NZ  LYS A 172     -16.595  60.764   9.814  1.00 40.67           N  
ANISOU 1230  NZ  LYS A 172     6439   2900   6114    142    978  -1246       N  
ATOM   1231  N   THR A 173     -20.010  65.993   5.508  1.00 29.31           N  
ANISOU 1231  N   THR A 173     4708   2307   4123    -85    657  -1575       N  
ATOM   1232  CA  THR A 173     -20.670  66.216   4.230  1.00 30.33           C  
ANISOU 1232  CA  THR A 173     4883   2486   4157    -86    564  -1711       C  
ATOM   1233  C   THR A 173     -20.757  67.693   3.898  1.00 28.67           C  
ANISOU 1233  C   THR A 173     4627   2441   3825    -58    496  -1665       C  
ATOM   1234  O   THR A 173     -20.560  68.098   2.750  1.00 29.24           O  
ANISOU 1234  O   THR A 173     4762   2575   3772     12    441  -1736       O  
ATOM   1235  CB  THR A 173     -22.058  65.586   4.251  1.00 39.18           C  
ANISOU 1235  CB  THR A 173     6008   3530   5349   -211    518  -1810       C  
ATOM   1236  OG1 THR A 173     -21.912  64.162   4.207  1.00 36.43           O  
ANISOU 1236  OG1 THR A 173     5740   3008   5094   -223    566  -1885       O  
ATOM   1237  CG2 THR A 173     -22.877  66.039   3.048  1.00 39.37           C  
ANISOU 1237  CG2 THR A 173     6074   3623   5261   -218    394  -1937       C  
ATOM   1238  N   ARG A 174     -21.053  68.524   4.887  1.00 26.79           N  
ANISOU 1238  N   ARG A 174     4293   2271   3617   -106    498  -1550       N  
ATOM   1239  CA  ARG A 174     -21.068  69.954   4.639  1.00 25.30           C  
ANISOU 1239  CA  ARG A 174     4071   2219   3324    -71    432  -1499       C  
ATOM   1240  C   ARG A 174     -19.700  70.450   4.181  1.00 24.73           C  
ANISOU 1240  C   ARG A 174     4020   2205   3171     34    472  -1451       C  
ATOM   1241  O   ARG A 174     -19.606  71.235   3.234  1.00 24.80           O  
ANISOU 1241  O   ARG A 174     4067   2298   3058     89    414  -1486       O  
ATOM   1242  CB  ARG A 174     -21.517  70.673   5.908  1.00 23.55           C  
ANISOU 1242  CB  ARG A 174     3741   2045   3161   -134    442  -1388       C  
ATOM   1243  CG  ARG A 174     -21.535  72.183   5.792  1.00 22.06           C  
ANISOU 1243  CG  ARG A 174     3522   1978   2881    -98    373  -1329       C  
ATOM   1244  CD  ARG A 174     -22.406  72.750   4.661  1.00 22.91           C  
ANISOU 1244  CD  ARG A 174     3690   2129   2885    -83    248  -1424       C  
ATOM   1245  NE  ARG A 174     -22.350  74.218   4.723  1.00 21.49           N  
ANISOU 1245  NE  ARG A 174     3495   2041   2629    -43    191  -1347       N  
ATOM   1246  CZ  ARG A 174     -22.418  75.042   3.678  1.00 30.14           C  
ANISOU 1246  CZ  ARG A 174     4689   3179   3585     21     98  -1377       C  
ATOM   1247  NH1 ARG A 174     -22.597  74.571   2.447  1.00 27.91           N  
ANISOU 1247  NH1 ARG A 174     4531   2867   3205     53     47  -1487       N  
ATOM   1248  NH2 ARG A 174     -22.354  76.356   3.868  1.00 27.57           N  
ANISOU 1248  NH2 ARG A 174     4357   2912   3205     53     53  -1299       N  
ATOM   1249  N   LEU A 175     -18.625  69.982   4.826  1.00 24.41           N  
ANISOU 1249  N   LEU A 175     3958   2120   3197     63    575  -1377       N  
ATOM   1250  CA  LEU A 175     -17.299  70.467   4.447  1.00 24.03           C  
ANISOU 1250  CA  LEU A 175     3908   2134   3090    149    629  -1335       C  
ATOM   1251  C   LEU A 175     -16.938  70.007   3.045  1.00 25.93           C  
ANISOU 1251  C   LEU A 175     4233   2374   3244    220    637  -1465       C  
ATOM   1252  O   LEU A 175     -16.365  70.760   2.250  1.00 25.93           O  
ANISOU 1252  O   LEU A 175     4243   2472   3136    272    647  -1474       O  
ATOM   1253  CB  LEU A 175     -16.263  69.991   5.458  1.00 23.62           C  
ANISOU 1253  CB  LEU A 175     3818   2022   3133    176    722  -1239       C  
ATOM   1254  CG  LEU A 175     -16.355  70.589   6.856  1.00 21.78           C  
ANISOU 1254  CG  LEU A 175     3510   1810   2956    127    721  -1104       C  
ATOM   1255  CD1 LEU A 175     -15.548  69.817   7.877  1.00 21.94           C  
ANISOU 1255  CD1 LEU A 175     3524   1740   3074    162    790  -1034       C  
ATOM   1256  CD2 LEU A 175     -15.888  72.042   6.803  1.00 20.26           C  
ANISOU 1256  CD2 LEU A 175     3267   1741   2688    142    700  -1032       C  
ATOM   1257  N   PHE A 176     -17.272  68.763   2.721  1.00 27.76           N  
ANISOU 1257  N   PHE A 176     4532   2495   3521    220    640  -1575       N  
ATOM   1258  CA  PHE A 176     -17.041  68.286   1.365  1.00 29.84           C  
ANISOU 1258  CA  PHE A 176     4889   2758   3693    290    638  -1722       C  
ATOM   1259  C   PHE A 176     -17.821  69.117   0.350  1.00 30.11           C  
ANISOU 1259  C   PHE A 176     4969   2893   3580    292    526  -1798       C  
ATOM   1260  O   PHE A 176     -17.303  69.461  -0.717  1.00 31.03           O  
ANISOU 1260  O   PHE A 176     5128   3094   3567    364    538  -1865       O  
ATOM   1261  CB  PHE A 176     -17.434  66.821   1.287  1.00 31.86           C  
ANISOU 1261  CB  PHE A 176     5217   2857   4033    276    642  -1833       C  
ATOM   1262  CG  PHE A 176     -17.126  66.191  -0.026  1.00 34.28           C  
ANISOU 1262  CG  PHE A 176     5628   3145   4252    358    647  -1999       C  
ATOM   1263  CD1 PHE A 176     -15.814  65.935  -0.395  1.00 35.10           C  
ANISOU 1263  CD1 PHE A 176     5735   3265   4337    464    755  -2015       C  
ATOM   1264  CD2 PHE A 176     -18.149  65.851  -0.888  1.00 35.95           C  
ANISOU 1264  CD2 PHE A 176     5938   3326   4397    333    543  -2147       C  
ATOM   1265  CE1 PHE A 176     -15.531  65.329  -1.621  1.00 41.04           C  
ANISOU 1265  CE1 PHE A 176     6584   4008   4999    546    772  -2184       C  
ATOM   1266  CE2 PHE A 176     -17.873  65.237  -2.112  1.00 38.44           C  
ANISOU 1266  CE2 PHE A 176     6365   3625   4617    416    542  -2316       C  
ATOM   1267  CZ  PHE A 176     -16.568  64.991  -2.471  1.00 39.23           C  
ANISOU 1267  CZ  PHE A 176     6460   3749   4694    523    662  -2336       C  
ATOM   1268  N   THR A 177     -19.057  69.486   0.689  1.00 29.47           N  
ANISOU 1268  N   THR A 177     4878   2808   3511    217    420  -1787       N  
ATOM   1269  CA  THR A 177     -19.856  70.316  -0.202  1.00 29.84           C  
ANISOU 1269  CA  THR A 177     4986   2935   3419    234    288  -1851       C  
ATOM   1270  C   THR A 177     -19.202  71.677  -0.412  1.00 37.37           C  
ANISOU 1270  C   THR A 177     5887   4034   4279    287    296  -1775       C  
ATOM   1271  O   THR A 177     -19.173  72.196  -1.533  1.00 29.52           O  
ANISOU 1271  O   THR A 177     4925   3141   3150    335    251  -1839       O  
ATOM   1272  CB  THR A 177     -21.264  70.475   0.370  1.00 30.86           C  
ANISOU 1272  CB  THR A 177     5105   3023   3599    131    194  -1835       C  
ATOM   1273  OG1 THR A 177     -21.896  69.190   0.436  1.00 35.32           O  
ANISOU 1273  OG1 THR A 177     5701   3463   4255     55    200  -1931       O  
ATOM   1274  CG2 THR A 177     -22.092  71.384  -0.508  1.00 33.16           C  
ANISOU 1274  CG2 THR A 177     5479   3380   3740    139     60  -1861       C  
ATOM   1275  N   ILE A 178     -18.660  72.269   0.656  1.00 26.46           N  
ANISOU 1275  N   ILE A 178     4402   2676   2975    256    365  -1622       N  
ATOM   1276  CA  ILE A 178     -17.964  73.549   0.508  1.00 25.34           C  
ANISOU 1276  CA  ILE A 178     4214   2654   2758    280    393  -1544       C  
ATOM   1277  C   ILE A 178     -16.773  73.400  -0.433  1.00 26.58           C  
ANISOU 1277  C   ILE A 178     4409   2864   2828    334    508  -1586       C  
ATOM   1278  O   ILE A 178     -16.579  74.196  -1.361  1.00 27.16           O  
ANISOU 1278  O   ILE A 178     4510   3046   2763    351    510  -1618       O  
ATOM   1279  CB  ILE A 178     -17.532  74.083   1.883  1.00 23.16           C  
ANISOU 1279  CB  ILE A 178     3843   2371   2586    234    448  -1379       C  
ATOM   1280  CG1 ILE A 178     -18.756  74.553   2.681  1.00 22.05           C  
ANISOU 1280  CG1 ILE A 178     3666   2217   2495    181    340  -1341       C  
ATOM   1281  CG2 ILE A 178     -16.522  75.227   1.704  1.00 22.36           C  
ANISOU 1281  CG2 ILE A 178     3715   2363   2416    249    512  -1295       C  
ATOM   1282  CD1 ILE A 178     -18.477  74.825   4.183  1.00 20.21           C  
ANISOU 1282  CD1 ILE A 178     3338   1968   2373    129    395  -1201       C  
ATOM   1283  N   ARG A 179     -15.973  72.352  -0.222  1.00 27.28           N  
ANISOU 1283  N   ARG A 179     4501   2876   2989    358    616  -1593       N  
ATOM   1284  CA  ARG A 179     -14.809  72.106  -1.067  1.00 28.75           C  
ANISOU 1284  CA  ARG A 179     4721   3103   3100    422    740  -1639       C  
ATOM   1285  C   ARG A 179     -15.212  71.974  -2.533  1.00 34.52           C  
ANISOU 1285  C   ARG A 179     5548   3897   3672    459    699  -1804       C  
ATOM   1286  O   ARG A 179     -14.623  72.617  -3.415  1.00 31.74           O  
ANISOU 1286  O   ARG A 179     5226   3658   3176    478    767  -1816       O  
ATOM   1287  CB  ARG A 179     -14.084  70.850  -0.572  1.00 29.49           C  
ANISOU 1287  CB  ARG A 179     4801   3085   3317    460    833  -1649       C  
ATOM   1288  CG  ARG A 179     -12.837  70.415  -1.407  1.00 31.40           C  
ANISOU 1288  CG  ARG A 179     5069   3359   3502    548    972  -1717       C  
ATOM   1289  CD  ARG A 179     -12.937  68.962  -1.835  1.00 54.01           C  
ANISOU 1289  CD  ARG A 179     8004   6114   6403    606    981  -1867       C  
ATOM   1290  NE  ARG A 179     -11.629  68.370  -2.136  1.00 51.41           N  
ANISOU 1290  NE  ARG A 179     7664   5780   6088    703   1124  -1907       N  
ATOM   1291  CZ  ARG A 179     -11.078  68.317  -3.346  1.00 56.84           C  
ANISOU 1291  CZ  ARG A 179     8405   6551   6641    769   1206  -2020       C  
ATOM   1292  NH1 ARG A 179     -11.716  68.807  -4.408  1.00 60.67           N  
ANISOU 1292  NH1 ARG A 179     8969   7131   6952    747   1152  -2105       N  
ATOM   1293  NH2 ARG A 179      -9.877  67.769  -3.494  1.00 53.55           N  
ANISOU 1293  NH2 ARG A 179     7958   6130   6258    866   1342  -2054       N  
ATOM   1294  N   GLN A 180     -16.248  71.175  -2.805  1.00 32.07           N  
ANISOU 1294  N   GLN A 180     5295   3516   3375    463    586  -1932       N  
ATOM   1295  CA  GLN A 180     -16.693  70.960  -4.181  1.00 38.61           C  
ANISOU 1295  CA  GLN A 180     6212   4404   4055    501    525  -2111       C  
ATOM   1296  C   GLN A 180     -17.206  72.250  -4.812  1.00 36.59           C  
ANISOU 1296  C   GLN A 180     5933   4301   3667    460    450  -2101       C  
ATOM   1297  O   GLN A 180     -17.001  72.489  -6.009  1.00 36.02           O  
ANISOU 1297  O   GLN A 180     5916   4343   3428    468    485  -2197       O  
ATOM   1298  CB  GLN A 180     -17.775  69.883  -4.213  1.00 37.72           C  
ANISOU 1298  CB  GLN A 180     6166   4160   4006    489    403  -2211       C  
ATOM   1299  CG  GLN A 180     -17.263  68.526  -3.823  1.00 36.59           C  
ANISOU 1299  CG  GLN A 180     6064   3863   3976    517    492  -2259       C  
ATOM   1300  CD  GLN A 180     -16.083  68.119  -4.689  1.00 42.16           C  
ANISOU 1300  CD  GLN A 180     6804   4617   4600    606    628  -2349       C  
ATOM   1301  OE1 GLN A 180     -16.238  67.837  -5.876  1.00 47.39           O  
ANISOU 1301  OE1 GLN A 180     7545   5327   5132    644    601  -2501       O  
ATOM   1302  NE2 GLN A 180     -14.892  68.125  -4.108  1.00 45.86           N  
ANISOU 1302  NE2 GLN A 180     7201   5083   5142    626    778  -2236       N  
ATOM   1303  N   GLU A 181     -17.875  73.088  -4.023  1.00 32.21           N  
ANISOU 1303  N   GLU A 181     5304   3753   3180    408    361  -1993       N  
ATOM   1304  CA  GLU A 181     -18.342  74.379  -4.520  1.00 31.99           C  
ANISOU 1304  CA  GLU A 181     5242   3865   3047    350    309  -1982       C  
ATOM   1305  C   GLU A 181     -17.178  75.304  -4.853  1.00 42.73           C  
ANISOU 1305  C   GLU A 181     6656   5313   4266    352    452  -1898       C  
ATOM   1306  O   GLU A 181     -17.157  75.918  -5.928  1.00 33.14           O  
ANISOU 1306  O   GLU A 181     5529   4206   2858    328    471  -1936       O  
ATOM   1307  CB  GLU A 181     -19.259  75.038  -3.493  1.00 29.99           C  
ANISOU 1307  CB  GLU A 181     4888   3589   2919    305    194  -1888       C  
ATOM   1308  CG  GLU A 181     -20.687  74.587  -3.594  1.00 44.48           C  
ANISOU 1308  CG  GLU A 181     6683   5399   4820    300     22  -1986       C  
ATOM   1309  CD  GLU A 181     -21.314  74.969  -4.927  1.00 57.29           C  
ANISOU 1309  CD  GLU A 181     8263   7180   6325    103     94  -2161       C  
ATOM   1310  OE1 GLU A 181     -20.893  75.996  -5.520  1.00 60.94           O  
ANISOU 1310  OE1 GLU A 181     8848   7714   6595     73    146  -2101       O  
ATOM   1311  OE2 GLU A 181     -22.217  74.232  -5.381  1.00 56.06           O  
ANISOU 1311  OE2 GLU A 181     8114   6996   6189    -91    157  -2294       O  
ATOM   1312  N   MET A 182     -16.205  75.439  -3.936  1.00 30.08           N  
ANISOU 1312  N   MET A 182     5015   3656   2757    364    557  -1743       N  
ATOM   1313  CA  MET A 182     -15.026  76.233  -4.268  1.00 30.14           C  
ANISOU 1313  CA  MET A 182     5066   3729   2658    359    701  -1630       C  
ATOM   1314  C   MET A 182     -14.339  75.723  -5.527  1.00 32.76           C  
ANISOU 1314  C   MET A 182     5493   4122   2834    403    814  -1729       C  
ATOM   1315  O   MET A 182     -13.920  76.510  -6.380  1.00 33.99           O  
ANISOU 1315  O   MET A 182     5754   4359   2800    383    892  -1689       O  
ATOM   1316  CB  MET A 182     -14.028  76.258  -3.114  1.00 28.42           C  
ANISOU 1316  CB  MET A 182     4762   3449   2588    359    802  -1485       C  
ATOM   1317  CG  MET A 182     -14.602  76.812  -1.789  1.00 25.92           C  
ANISOU 1317  CG  MET A 182     4357   3080   2413    314    707  -1378       C  
ATOM   1318  SD  MET A 182     -13.255  76.659  -0.609  1.00 26.28           S  
ANISOU 1318  SD  MET A 182     4308   3071   2606    317    840  -1243       S  
ATOM   1319  CE  MET A 182     -12.178  77.599  -1.631  1.00 45.49           C  
ANISOU 1319  CE  MET A 182     6822   5594   4869    307    991  -1199       C  
ATOM   1320  N   ALA A 183     -14.191  74.406  -5.648  1.00 33.99           N  
ANISOU 1320  N   ALA A 183     5647   4216   3052    460    842  -1850       N  
ATOM   1321  CA  ALA A 183     -13.491  73.856  -6.801  1.00 36.68           C  
ANISOU 1321  CA  ALA A 183     6072   4615   3250    514    960  -1961       C  
ATOM   1322  C   ALA A 183     -14.205  74.211  -8.100  1.00 38.70           C  
ANISOU 1322  C   ALA A 183     6441   4982   3282    493    893  -2078       C  
ATOM   1323  O   ALA A 183     -13.560  74.593  -9.082  1.00 40.76           O  
ANISOU 1323  O   ALA A 183     6809   5338   3342    497   1011  -2076       O  
ATOM   1324  CB  ALA A 183     -13.349  72.343  -6.643  1.00 37.74           C  
ANISOU 1324  CB  ALA A 183     6193   4640   3506    585    979  -2083       C  
ATOM   1325  N   SER A 184     -15.539  74.119  -8.116  1.00 38.60           N  
ANISOU 1325  N   SER A 184     6414   4959   3293    456    714  -2179       N  
ATOM   1326  CA  SER A 184     -16.306  74.481  -9.306  1.00 40.65           C  
ANISOU 1326  CA  SER A 184     6772   5331   3344    410    638  -2296       C  
ATOM   1327  C   SER A 184     -16.137  75.944  -9.691  1.00 43.08           C  
ANISOU 1327  C   SER A 184     7188   5720   3462    359    663  -2132       C  
ATOM   1328  O   SER A 184     -16.489  76.319 -10.815  1.00 47.18           O  
ANISOU 1328  O   SER A 184     7861   6324   3743    334    632  -2181       O  
ATOM   1329  CB  SER A 184     -17.788  74.184  -9.098  1.00 40.49           C  
ANISOU 1329  CB  SER A 184     6677   5269   3440    338    455  -2391       C  
ATOM   1330  OG  SER A 184     -18.429  75.259  -8.428  1.00 53.69           O  
ANISOU 1330  OG  SER A 184     8294   6947   5159    265    373  -2267       O  
ATOM   1331  N   ARG A 185     -15.628  76.779  -8.786  1.00 38.26           N  
ANISOU 1331  N   ARG A 185     6536   5064   2937    346    711  -1931       N  
ATOM   1332  CA  ARG A 185     -15.321  78.172  -9.074  1.00 38.34           C  
ANISOU 1332  CA  ARG A 185     6681   5108   2777    310    750  -1755       C  
ATOM   1333  C   ARG A 185     -13.825  78.413  -9.211  1.00 38.93           C  
ANISOU 1333  C   ARG A 185     6803   5195   2794    327    974  -1640       C  
ATOM   1334  O   ARG A 185     -13.398  79.571  -9.250  1.00 38.88           O  
ANISOU 1334  O   ARG A 185     6886   5193   2691    289   1034  -1474       O  
ATOM   1335  CB  ARG A 185     -15.901  79.072  -7.979  1.00 35.63           C  
ANISOU 1335  CB  ARG A 185     6261   4706   2571    268    639  -1625       C  
ATOM   1336  CG  ARG A 185     -17.402  78.919  -7.796  1.00 35.19           C  
ANISOU 1336  CG  ARG A 185     6132   4649   2590    234    437  -1737       C  
ATOM   1337  CD  ARG A 185     -17.921  79.772  -6.662  1.00 32.67           C  
ANISOU 1337  CD  ARG A 185     5722   4275   2414    200    348  -1619       C  
ATOM   1338  NE  ARG A 185     -19.319  79.479  -6.360  1.00 44.07           N  
ANISOU 1338  NE  ARG A 185     7055   5718   3971    147    198  -1738       N  
ATOM   1339  CZ  ARG A 185     -20.238  80.398  -6.068  1.00 48.69           C  
ANISOU 1339  CZ  ARG A 185     7653   6290   4557    110     73  -1676       C  
ATOM   1340  NH1 ARG A 185     -19.919  81.695  -6.027  1.00 36.98           N  
ANISOU 1340  NH1 ARG A 185     6292   4789   2971    144     50  -1501       N  
ATOM   1341  NH2 ARG A 185     -21.483  80.016  -5.811  1.00 52.28           N  
ANISOU 1341  NH2 ARG A 185     8017   6733   5114     32    -21  -1784       N  
ATOM   1342  N   SER A 186     -13.019  77.347  -9.276  1.00 39.77           N  
ANISOU 1342  N   SER A 186     6845   5300   2967    381   1104  -1728       N  
ATOM   1343  CA  SER A 186     -11.558  77.447  -9.313  1.00 40.48           C  
ANISOU 1343  CA  SER A 186     6928   5408   3046    395   1333  -1642       C  
ATOM   1344  C   SER A 186     -10.998  78.192  -8.104  1.00 37.95           C  
ANISOU 1344  C   SER A 186     6500   5023   2895    351   1379  -1461       C  
ATOM   1345  O   SER A 186      -9.937  78.813  -8.187  1.00 38.56           O  
ANISOU 1345  O   SER A 186     6590   5130   2932    323   1550  -1349       O  
ATOM   1346  CB  SER A 186     -11.063  78.108 -10.608  1.00 43.37           C  
ANISOU 1346  CB  SER A 186     7478   5879   3123    376   1460  -1607       C  
ATOM   1347  OG  SER A 186     -11.233  77.251 -11.710  1.00 46.14           O  
ANISOU 1347  OG  SER A 186     7913   6300   3319    428   1470  -1790       O  
ATOM   1348  N   LEU A 187     -11.694  78.142  -6.965  1.00 39.01           N  
ANISOU 1348  N   LEU A 187     6522   5076   3224    339   1232  -1436       N  
ATOM   1349  CA  LEU A 187     -11.206  78.780  -5.751  1.00 32.97           C  
ANISOU 1349  CA  LEU A 187     5653   4252   2621    300   1264  -1284       C  
ATOM   1350  C   LEU A 187     -10.463  77.826  -4.830  1.00 32.09           C  
ANISOU 1350  C   LEU A 187     5381   4085   2726    344   1332  -1297       C  
ATOM   1351  O   LEU A 187      -9.778  78.291  -3.909  1.00 30.71           O  
ANISOU 1351  O   LEU A 187     5115   3880   2674    316   1392  -1181       O  
ATOM   1352  CB  LEU A 187     -12.368  79.408  -4.965  1.00 30.71           C  
ANISOU 1352  CB  LEU A 187     5343   3918   2410    261   1071  -1236       C  
ATOM   1353  CG  LEU A 187     -13.269  80.344  -5.755  1.00 33.83           C  
ANISOU 1353  CG  LEU A 187     5891   4351   2611    231    960  -1224       C  
ATOM   1354  CD1 LEU A 187     -14.495  80.742  -4.925  1.00 29.51           C  
ANISOU 1354  CD1 LEU A 187     5277   3762   2175    211    763  -1215       C  
ATOM   1355  CD2 LEU A 187     -12.469  81.552  -6.190  1.00 35.72           C  
ANISOU 1355  CD2 LEU A 187     6263   4609   2699    186   1085  -1074       C  
ATOM   1356  N   TRP A 188     -10.588  76.510  -5.046  1.00 33.04           N  
ANISOU 1356  N   TRP A 188     5475   4185   2894    414   1315  -1438       N  
ATOM   1357  CA  TRP A 188     -10.147  75.558  -4.034  1.00 32.09           C  
ANISOU 1357  CA  TRP A 188     5224   3982   2987    460   1329  -1442       C  
ATOM   1358  C   TRP A 188      -8.630  75.496  -3.943  1.00 40.36           C  
ANISOU 1358  C   TRP A 188     6200   5054   4079    491   1527  -1397       C  
ATOM   1359  O   TRP A 188      -8.075  75.408  -2.837  1.00 31.72           O  
ANISOU 1359  O   TRP A 188     4985   3909   3158    497   1546  -1320       O  
ATOM   1360  CB  TRP A 188     -10.710  74.169  -4.333  1.00 40.11           C  
ANISOU 1360  CB  TRP A 188     6256   4947   4037    528   1257  -1605       C  
ATOM   1361  CG  TRP A 188     -10.083  73.116  -3.480  1.00 37.84           C  
ANISOU 1361  CG  TRP A 188     5877   4563   3937    585   1304  -1608       C  
ATOM   1362  CD1 TRP A 188      -9.177  72.165  -3.873  1.00 40.47           C  
ANISOU 1362  CD1 TRP A 188     6202   4885   4289    674   1428  -1697       C  
ATOM   1363  CD2 TRP A 188     -10.276  72.931  -2.076  1.00 34.43           C  
ANISOU 1363  CD2 TRP A 188     5358   4031   3693    561   1238  -1516       C  
ATOM   1364  NE1 TRP A 188      -8.816  71.386  -2.798  1.00 34.34           N  
ANISOU 1364  NE1 TRP A 188     5341   3999   3706    711   1429  -1665       N  
ATOM   1365  CE2 TRP A 188      -9.472  71.839  -1.683  1.00 39.56           C  
ANISOU 1365  CE2 TRP A 188     5958   4608   4467    638   1316  -1550       C  
ATOM   1366  CE3 TRP A 188     -11.062  73.573  -1.113  1.00 31.86           C  
ANISOU 1366  CE3 TRP A 188     4995   3674   3435    488   1120  -1415       C  
ATOM   1367  CZ2 TRP A 188      -9.437  71.376  -0.369  1.00 30.48           C  
ANISOU 1367  CZ2 TRP A 188     4732   3354   3493    638   1277  -1476       C  
ATOM   1368  CZ3 TRP A 188     -11.022  73.119   0.188  1.00 31.14           C  
ANISOU 1368  CZ3 TRP A 188     4827   3490   3515    482   1094  -1344       C  
ATOM   1369  CH2 TRP A 188     -10.216  72.034   0.552  1.00 30.19           C  
ANISOU 1369  CH2 TRP A 188     4668   3298   3504    554   1170  -1371       C  
ATOM   1370  N   ASP A 189      -7.946  75.526  -5.097  1.00 35.59           N  
ANISOU 1370  N   ASP A 189     5663   4539   3320    515   1676  -1450       N  
ATOM   1371  CA  ASP A 189      -6.491  75.395  -5.103  1.00 41.71           C  
ANISOU 1371  CA  ASP A 189     6346   5358   4145    555   1875  -1431       C  
ATOM   1372  C   ASP A 189      -5.833  76.466  -4.251  1.00 35.84           C  
ANISOU 1372  C   ASP A 189     5504   4622   3493    486   1929  -1268       C  
ATOM   1373  O   ASP A 189      -4.920  76.176  -3.466  1.00 35.31           O  
ANISOU 1373  O   ASP A 189     5286   4538   3593    523   1997  -1239       O  
ATOM   1374  CB  ASP A 189      -5.945  75.470  -6.530  1.00 46.97           C  
ANISOU 1374  CB  ASP A 189     7108   6139   4600    573   2037  -1501       C  
ATOM   1375  CG  ASP A 189      -4.417  75.562  -6.566  1.00 61.01           C  
ANISOU 1375  CG  ASP A 189     8768   7989   6426    599   2261  -1467       C  
ATOM   1376  OD1 ASP A 189      -3.755  74.626  -6.062  1.00 61.11           O  
ANISOU 1376  OD1 ASP A 189     8651   7966   6601    693   2304  -1526       O  
ATOM   1377  OD2 ASP A 189      -3.876  76.574  -7.080  1.00 64.95           O  
ANISOU 1377  OD2 ASP A 189     9297   8577   6805    527   2393  -1381       O  
ATOM   1378  N   SER A 190      -6.266  77.714  -4.407  1.00 34.75           N  
ANISOU 1378  N   SER A 190     5450   4506   3246    390   1896  -1168       N  
ATOM   1379  CA  SER A 190      -5.700  78.767  -3.580  1.00 34.47           C  
ANISOU 1379  CA  SER A 190     5330   4466   3302    317   1937  -1024       C  
ATOM   1380  C   SER A 190      -6.094  78.594  -2.109  1.00 35.52           C  
ANISOU 1380  C   SER A 190     5354   4503   3638    320   1795   -982       C  
ATOM   1381  O   SER A 190      -5.256  78.744  -1.210  1.00 30.10           O  
ANISOU 1381  O   SER A 190     4525   3809   3104    319   1847   -920       O  
ATOM   1382  CB  SER A 190      -6.144  80.128  -4.103  1.00 34.59           C  
ANISOU 1382  CB  SER A 190     5490   4505   3147    218   1924   -930       C  
ATOM   1383  OG  SER A 190      -5.718  81.138  -3.216  1.00 33.95           O  
ANISOU 1383  OG  SER A 190     5333   4399   3169    143   1942   -801       O  
ATOM   1384  N   PHE A 191      -7.355  78.264  -1.839  1.00 29.22           N  
ANISOU 1384  N   PHE A 191     4612   3643   2845    325   1615  -1018       N  
ATOM   1385  CA  PHE A 191      -7.783  78.106  -0.450  1.00 26.83           C  
ANISOU 1385  CA  PHE A 191     4218   3259   2717    321   1489   -972       C  
ATOM   1386  C   PHE A 191      -7.037  76.973   0.235  1.00 27.11           C  
ANISOU 1386  C   PHE A 191     4129   3254   2915    401   1530  -1005       C  
ATOM   1387  O   PHE A 191      -6.580  77.123   1.376  1.00 25.93           O  
ANISOU 1387  O   PHE A 191     3870   3075   2908    398   1522   -932       O  
ATOM   1388  CB  PHE A 191      -9.282  77.840  -0.415  1.00 25.74           C  
ANISOU 1388  CB  PHE A 191     4148   3079   2553    313   1304  -1021       C  
ATOM   1389  CG  PHE A 191      -9.856  77.657   0.963  1.00 23.54           C  
ANISOU 1389  CG  PHE A 191     3786   2728   2431    302   1179   -974       C  
ATOM   1390  CD1 PHE A 191     -10.046  78.742   1.803  1.00 21.80           C  
ANISOU 1390  CD1 PHE A 191     3538   2499   2247    240   1128   -870       C  
ATOM   1391  CD2 PHE A 191     -10.259  76.395   1.392  1.00 30.51           C  
ANISOU 1391  CD2 PHE A 191     4635   3546   3411    349   1114  -1037       C  
ATOM   1392  CE1 PHE A 191     -10.590  78.570   3.066  1.00 20.02           C  
ANISOU 1392  CE1 PHE A 191     3240   2220   2146    230   1021   -831       C  
ATOM   1393  CE2 PHE A 191     -10.792  76.216   2.654  1.00 21.73           C  
ANISOU 1393  CE2 PHE A 191     3460   2372   2422    330   1014   -983       C  
ATOM   1394  CZ  PHE A 191     -10.967  77.301   3.486  1.00 20.01           C  
ANISOU 1394  CZ  PHE A 191     3207   2165   2232    272    968   -883       C  
ATOM   1395  N   ARG A 192      -6.905  75.834  -0.451  1.00 28.86           N  
ANISOU 1395  N   ARG A 192     4377   3474   3116    480   1571  -1122       N  
ATOM   1396  CA  ARG A 192      -6.304  74.655   0.159  1.00 29.42           C  
ANISOU 1396  CA  ARG A 192     4355   3485   3337    572   1594  -1163       C  
ATOM   1397  C   ARG A 192      -4.851  74.893   0.552  1.00 36.66           C  
ANISOU 1397  C   ARG A 192     5133   4450   4348    609   1732  -1114       C  
ATOM   1398  O   ARG A 192      -4.342  74.232   1.465  1.00 33.77           O  
ANISOU 1398  O   ARG A 192     4664   4030   4136    678   1720  -1105       O  
ATOM   1399  CB  ARG A 192      -6.404  73.470  -0.798  1.00 35.28           C  
ANISOU 1399  CB  ARG A 192     5167   4213   4022    654   1623  -1313       C  
ATOM   1400  CG  ARG A 192      -5.981  72.151  -0.184  1.00 43.80           C  
ANISOU 1400  CG  ARG A 192     6186   5199   5256    758   1624  -1366       C  
ATOM   1401  CD  ARG A 192      -4.926  71.478  -1.024  1.00 51.00           C  
ANISOU 1401  CD  ARG A 192     7075   6156   6146    867   1778  -1474       C  
ATOM   1402  NE  ARG A 192      -5.118  71.747  -2.442  1.00 52.28           N  
ANISOU 1402  NE  ARG A 192     7344   6410   6111    849   1845  -1558       N  
ATOM   1403  CZ  ARG A 192      -4.133  71.770  -3.333  1.00 57.64           C  
ANISOU 1403  CZ  ARG A 192     8003   7189   6710    901   2020  -1617       C  
ATOM   1404  NH1 ARG A 192      -2.881  71.547  -2.942  1.00 58.54           N  
ANISOU 1404  NH1 ARG A 192     7972   7327   6943    980   2140  -1605       N  
ATOM   1405  NH2 ARG A 192      -4.399  72.020  -4.612  1.00 60.37           N  
ANISOU 1405  NH2 ARG A 192     8468   7618   6851    879   2074  -1691       N  
ATOM   1406  N   GLN A 193      -4.164  75.815  -0.127  1.00 31.28           N  
ANISOU 1406  N   GLN A 193     4438   3870   3576    565   1864  -1082       N  
ATOM   1407  CA  GLN A 193      -2.757  76.081   0.135  1.00 32.47           C  
ANISOU 1407  CA  GLN A 193     4429   4088   3820    591   2006  -1045       C  
ATOM   1408  C   GLN A 193      -2.546  77.315   0.989  1.00 30.88           C  
ANISOU 1408  C   GLN A 193     4150   3901   3682    497   1986   -916       C  
ATOM   1409  O   GLN A 193      -1.420  77.807   1.087  1.00 34.24           O  
ANISOU 1409  O   GLN A 193     4437   4402   4169    487   2107   -879       O  
ATOM   1410  CB  GLN A 193      -1.997  76.229  -1.180  1.00 35.27           C  
ANISOU 1410  CB  GLN A 193     4798   4556   4045    599   2195  -1099       C  
ATOM   1411  CG  GLN A 193      -2.043  75.004  -2.035  1.00 39.46           C  
ANISOU 1411  CG  GLN A 193     5394   5084   4517    706   2234  -1245       C  
ATOM   1412  CD  GLN A 193      -0.959  75.018  -3.079  1.00 47.89           C  
ANISOU 1412  CD  GLN A 193     6418   6277   5500    741   2451  -1302       C  
ATOM   1413  OE1 GLN A 193      -1.223  75.296  -4.249  1.00 50.08           O  
ANISOU 1413  OE1 GLN A 193     6831   6620   5578    703   2521  -1340       O  
ATOM   1414  NE2 GLN A 193       0.274  74.715  -2.667  1.00 48.37           N  
ANISOU 1414  NE2 GLN A 193     6287   6382   5709    820   2560  -1312       N  
ATOM   1415  N   SER A 194      -3.602  77.822   1.614  1.00 30.05           N  
ANISOU 1415  N   SER A 194     4120   3729   3570    429   1837   -856       N  
ATOM   1416  CA  SER A 194      -3.541  79.097   2.304  1.00 27.15           C  
ANISOU 1416  CA  SER A 194     3712   3369   3235    333   1815   -747       C  
ATOM   1417  C   SER A 194      -3.371  78.930   3.805  1.00 33.06           C  
ANISOU 1417  C   SER A 194     4334   4065   4161    364   1724   -702       C  
ATOM   1418  O   SER A 194      -3.222  79.927   4.524  1.00 30.49           O  
ANISOU 1418  O   SER A 194     3951   3747   3887    295   1704   -624       O  
ATOM   1419  CB  SER A 194      -4.801  79.913   1.984  1.00 33.17           C  
ANISOU 1419  CB  SER A 194     4643   4100   3860    246   1715   -714       C  
ATOM   1420  OG  SER A 194      -5.960  79.347   2.599  1.00 39.63           O  
ANISOU 1420  OG  SER A 194     5508   4838   4710    268   1545   -736       O  
ATOM   1421  N   GLU A 195      -3.403  77.700   4.306  1.00 27.85           N  
ANISOU 1421  N   GLU A 195     3641   3349   3591    465   1668   -751       N  
ATOM   1422  CA  GLU A 195      -3.265  77.473   5.735  1.00 31.03           C  
ANISOU 1422  CA  GLU A 195     3946   3700   4143    505   1579   -704       C  
ATOM   1423  C   GLU A 195      -1.786  77.347   6.073  1.00 37.96           C  
ANISOU 1423  C   GLU A 195     4629   4641   5152    582   1673   -703       C  
ATOM   1424  O   GLU A 195      -1.027  76.694   5.348  1.00 39.94           O  
ANISOU 1424  O   GLU A 195     4830   4936   5410    661   1781   -772       O  
ATOM   1425  CB  GLU A 195      -4.027  76.211   6.146  1.00 34.18           C  
ANISOU 1425  CB  GLU A 195     4417   3998   4571    572   1474   -744       C  
ATOM   1426  CG  GLU A 195      -4.086  75.961   7.643  1.00 30.09           C  
ANISOU 1426  CG  GLU A 195     3843   3415   4175    607   1372   -684       C  
ATOM   1427  CD  GLU A 195      -4.927  74.730   7.957  1.00 34.31           C  
ANISOU 1427  CD  GLU A 195     4472   3842   4724    647   1286   -716       C  
ATOM   1428  OE1 GLU A 195      -6.151  74.820   7.755  1.00 36.10           O  
ANISOU 1428  OE1 GLU A 195     4808   4041   4868    566   1212   -721       O  
ATOM   1429  OE2 GLU A 195      -4.368  73.679   8.371  1.00 29.57           O  
ANISOU 1429  OE2 GLU A 195     3832   3183   4221    762   1291   -739       O  
ATOM   1430  N   ARG A 196      -1.374  77.987   7.163  1.00 45.18           N  
ANISOU 1430  N   ARG A 196     5422   5570   6176    565   1629   -632       N  
ATOM   1431  CA  ARG A 196       0.030  78.029   7.542  1.00 45.47           C  
ANISOU 1431  CA  ARG A 196     5237   5687   6353    629   1696   -628       C  
ATOM   1432  C   ARG A 196       0.225  77.395   8.914  1.00 43.01           C  
ANISOU 1432  C   ARG A 196     4838   5320   6184    740   1575   -604       C  
ATOM   1433  O   ARG A 196      -0.671  77.421   9.761  1.00 46.31           O  
ANISOU 1433  O   ARG A 196     5347   5655   6593    719   1451   -559       O  
ATOM   1434  CB  ARG A 196       0.562  79.471   7.540  1.00 47.95           C  
ANISOU 1434  CB  ARG A 196     5447   6091   6681    501   1757   -568       C  
ATOM   1435  CG  ARG A 196       0.707  80.086   6.142  1.00 48.33           C  
ANISOU 1435  CG  ARG A 196     5560   6207   6595    404   1907   -580       C  
ATOM   1436  CD  ARG A 196       1.715  79.320   5.271  1.00 51.81           C  
ANISOU 1436  CD  ARG A 196     5908   6728   7049    493   2054   -656       C  
ATOM   1437  NE  ARG A 196       1.869  79.917   3.942  1.00 49.81           N  
ANISOU 1437  NE  ARG A 196     5726   6547   6652    399   2209   -661       N  
ATOM   1438  CZ  ARG A 196       1.153  79.570   2.874  1.00 51.44           C  
ANISOU 1438  CZ  ARG A 196     6128   6729   6687    400   2241   -708       C  
ATOM   1439  NH1 ARG A 196       0.231  78.623   2.976  1.00 49.21           N  
ANISOU 1439  NH1 ARG A 196     5974   6352   6373    478   2128   -760       N  
ATOM   1440  NH2 ARG A 196       1.357  80.167   1.703  1.00 53.71           N  
ANISOU 1440  NH2 ARG A 196     6484   7089   6833    318   2384   -702       N  
ATOM   1441  N   ALA A 197       1.404  76.815   9.121  1.00 45.81           N  
ANISOU 1441  N   ALA A 197     5016   5725   6667    868   1610   -634       N  
ATOM   1442  CA  ALA A 197       1.709  76.134  10.375  1.00 45.00           C  
ANISOU 1442  CA  ALA A 197     4831   5570   6697   1006   1486   -610       C  
ATOM   1443  C   ALA A 197       1.982  77.138  11.491  1.00 46.23           C  
ANISOU 1443  C   ALA A 197     4851   5773   6941    956   1395   -531       C  
ATOM   1444  O   ALA A 197       1.488  76.979  12.610  1.00 50.20           O  
ANISOU 1444  O   ALA A 197     5399   6199   7474    995   1256   -479       O  
ATOM   1445  CB  ALA A 197       2.895  75.197  10.193  1.00 47.19           C  
ANISOU 1445  CB  ALA A 197     4958   5889   7083   1180   1537   -675       C  
TER    1446      ALA A 197                                                      
HETATM 1447 MN    MN A 301     -11.491  76.179  17.089  1.00 13.17          MN  
HETATM 1448 MG    MG A 302     -12.270  79.214  19.043  1.00 11.01          MG  
HETATM 1449  C1 AGY7 A 303     -10.301  82.028  13.862  0.44 27.40           C  
HETATM 1450  C1 BGY7 A 303      -8.251  84.904  12.163  0.56 30.84           C  
HETATM 1451  C10AGY7 A 303      -7.801  84.423  18.854  0.44 39.40           C  
HETATM 1452  C10BGY7 A 303      -7.679  84.155  18.501  0.56 39.55           C  
HETATM 1453  C11AGY7 A 303      -6.709  83.607  19.116  0.44 37.49           C  
HETATM 1454  C11BGY7 A 303      -6.581  83.310  18.438  0.56 38.75           C  
HETATM 1455  C12AGY7 A 303      -5.489  83.832  18.499  0.44 39.45           C  
HETATM 1456  C12BGY7 A 303      -5.513  83.591  17.599  0.56 39.24           C  
HETATM 1457  C13AGY7 A 303      -5.346  84.873  17.611  0.44 40.74           C  
HETATM 1458  C13BGY7 A 303      -5.532  84.720  16.813  0.56 42.76           C  
HETATM 1459  C14AGY7 A 303      -6.417  85.691  17.340  0.44 42.02           C  
HETATM 1460  C14BGY7 A 303      -6.613  85.569  16.863  0.56 42.38           C  
HETATM 1461  C15AGY7 A 303      -7.639  85.468  17.957  0.44 41.96           C  
HETATM 1462  C15BGY7 A 303      -7.681  85.290  17.703  0.56 41.94           C  
HETATM 1463  C16AGY7 A 303     -10.094  78.830  16.982  0.44  9.17           C  
HETATM 1464  C16BGY7 A 303     -10.270  78.866  16.685  0.56  9.69           C  
HETATM 1465  C17AGY7 A 303      -9.523  77.946  16.066  0.44 10.91           C  
HETATM 1466  C17BGY7 A 303      -9.800  78.029  15.671  0.56 12.55           C  
HETATM 1467  C18AGY7 A 303      -5.465  80.095  15.344  0.44 27.35           C  
HETATM 1468  C18BGY7 A 303      -6.193  80.263  14.050  0.56 27.51           C  
HETATM 1469  C19AGY7 A 303      -5.420  81.390  16.138  0.44 26.61           C  
HETATM 1470  C19BGY7 A 303      -5.841  81.399  15.000  0.56 26.89           C  
HETATM 1471  C2 AGY7 A 303      -9.117  81.561  13.311  0.44 25.15           C  
HETATM 1472  C2 BGY7 A 303      -8.687  84.214  13.286  0.56 27.25           C  
HETATM 1473  C20AGY7 A 303      -5.893  82.396  15.113  0.44 29.11           C  
HETATM 1474  C20BGY7 A 303      -6.470  82.590  14.305  0.56 26.37           C  
HETATM 1475  C21AGY7 A 303      -9.211  80.434  12.509  0.44 27.52           C  
HETATM 1476  C21BGY7 A 303      -9.069  84.988  14.374  0.56 22.17           C  
HETATM 1477  C22AGY7 A 303     -10.399  79.781  12.282  0.44 30.10           C  
HETATM 1478  C22BGY7 A 303      -9.023  86.363  14.367  0.56 14.71           C  
HETATM 1479  C23AGY7 A 303     -11.540  80.276  12.870  0.44 17.37           C  
HETATM 1480  C23BGY7 A 303      -8.577  86.996  13.223  0.56 25.50           C  
HETATM 1481  C24AGY7 A 303     -11.509  81.402  13.666  0.44 25.72           C  
HETATM 1482  C24BGY7 A 303      -8.186  86.280  12.111  0.56 26.97           C  
HETATM 1483  C3 AGY7 A 303      -7.802  82.244  13.549  0.44 22.96           C  
HETATM 1484  C3 BGY7 A 303      -8.767  82.714  13.313  0.56 21.39           C  
HETATM 1485  C4 AGY7 A 303      -6.838  80.197  14.664  0.44 20.29           C  
HETATM 1486  C4 BGY7 A 303      -7.680  80.535  13.774  0.56 19.91           C  
HETATM 1487  C5 AGY7 A 303      -7.997  79.684  15.490  0.44 12.31           C  
HETATM 1488  C5 BGY7 A 303      -8.611  79.921  14.800  0.56 13.54           C  
HETATM 1489  C6 AGY7 A 303      -9.586  80.091  17.116  0.44  7.60           C  
HETATM 1490  C6 BGY7 A 303      -9.883  80.175  16.719  0.56  9.72           C  
HETATM 1491  C7 AGY7 A 303     -10.138  81.100  18.088  0.44 14.19           C  
HETATM 1492  C7 BGY7 A 303     -10.329  81.112  17.810  0.56 13.53           C  
HETATM 1493  C8 AGY7 A 303     -10.139  83.492  18.641  0.44 24.55           C  
HETATM 1494  C8 BGY7 A 303     -10.080  83.385  18.698  0.56 24.52           C  
HETATM 1495  C9 AGY7 A 303      -9.130  84.178  19.533  0.44 32.85           C  
HETATM 1496  C9 BGY7 A 303      -8.838  83.848  19.424  0.56 33.09           C  
HETATM 1497  F1 AGY7 A 303     -10.283  83.132  14.642  0.44 32.68           F  
HETATM 1498  F1 BGY7 A 303      -7.867  84.208  11.068  0.56 29.46           F  
HETATM 1499  F2 AGY7 A 303      -8.091  79.934  11.940  0.44 34.37           F  
HETATM 1500  F2 BGY7 A 303      -9.503  84.377  15.499  0.56 33.19           F  
HETATM 1501  N1 AGY7 A 303      -6.919  81.646  14.366  0.44 25.37           N  
HETATM 1502  N1 BGY7 A 303      -7.712  82.019  13.759  0.56 24.20           N  
HETATM 1503  N2 AGY7 A 303      -8.554  80.518  16.368  0.44  9.19           N  
HETATM 1504  N2 BGY7 A 303      -9.058  80.697  15.789  0.56  8.62           N  
HETATM 1505  N3 AGY7 A 303      -9.587  82.313  17.981  0.44 15.23           N  
HETATM 1506  N3 BGY7 A 303      -9.795  82.333  17.727  0.56 17.29           N  
HETATM 1507  N4 AGY7 A 303      -8.465  78.421  15.322  0.44  9.16           N  
HETATM 1508  N4 BGY7 A 303      -8.959  78.601  14.740  0.56 11.76           N  
HETATM 1509  O1 AGY7 A 303      -7.581  83.352  13.071  0.44 26.13           O  
HETATM 1510  O1 BGY7 A 303      -9.787  82.141  12.937  0.56 23.28           O  
HETATM 1511  O2 AGY7 A 303     -11.018  80.802  18.902  0.44 10.49           O  
HETATM 1512  O2 BGY7 A 303     -11.065  80.737  18.729  0.56 14.13           O  
HETATM 1513  O3 AGY7 A 303     -11.133  78.339  17.675  0.44 11.37           O  
HETATM 1514  O3 BGY7 A 303     -11.097  78.297  17.577  0.56  7.35           O  
HETATM 1515  O4 AGY7 A 303      -9.918  76.779  15.898  0.44  8.64           O  
HETATM 1516  O4 BGY7 A 303     -10.094  76.819  15.578  0.56 15.55           O  
HETATM 1517  C1  EDO A 304      -8.941  75.598  23.586  0.71 24.39           C  
HETATM 1518  O1  EDO A 304      -8.594  76.411  22.472  0.71 32.73           O  
HETATM 1519  C2  EDO A 304      -8.392  76.242  24.847  0.71 21.75           C  
HETATM 1520  O2  EDO A 304      -8.772  75.427  25.946  0.71 30.69           O  
HETATM 1521  O   HOH A 401     -22.344  69.391  33.509  1.00 51.33           O  
HETATM 1522  O   HOH A 402      -1.985  75.749  13.398  1.00 43.97           O  
HETATM 1523  O   HOH A 403     -24.750  78.293  23.976  1.00 30.61           O  
HETATM 1524  O   HOH A 404      -7.867  78.551  -6.804  1.00 37.08           O  
HETATM 1525  O   HOH A 405      -8.524  69.487   4.417  1.00 40.43           O  
HETATM 1526  O   HOH A 406     -24.370  85.698   3.587  1.00 24.85           O  
HETATM 1527  O   HOH A 407     -11.119  78.204  20.475  1.00 12.91           O  
HETATM 1528  O   HOH A 408      -9.351  60.177  16.233  1.00 35.13           O  
HETATM 1529  O   HOH A 409       2.675  74.837  -3.560  1.00 38.85           O  
HETATM 1530  O   HOH A 410      -6.123  81.190   6.276  1.00 45.30           O  
HETATM 1531  O   HOH A 411     -14.678  64.579  20.393  1.00 26.07           O  
HETATM 1532  O   HOH A 412       3.396  81.946   4.509  1.00 56.92           O  
HETATM 1533  O   HOH A 413     -12.864  75.666  38.267  1.00 47.40           O  
HETATM 1534  O   HOH A 414     -21.420  87.527  19.213  1.00 36.33           O  
HETATM 1535  O   HOH A 415      -9.682  75.756  13.144  1.00 14.88           O  
HETATM 1536  O   HOH A 416     -14.392  80.941  13.208  1.00 21.61           O  
HETATM 1537  O   HOH A 417      -9.422  80.898  -3.150  1.00 28.02           O  
HETATM 1538  O   HOH A 418     -15.882  83.549  21.451  1.00 14.11           O  
HETATM 1539  O   HOH A 419     -13.052  90.455  -2.822  1.00 30.20           O  
HETATM 1540  O   HOH A 420       1.985  72.620   7.348  1.00 49.80           O  
HETATM 1541  O   HOH A 421     -21.438  88.114  22.291  1.00 15.98           O  
HETATM 1542  O   HOH A 422     -15.916  87.836  -4.891  1.00 48.49           O  
HETATM 1543  O   HOH A 423      -2.893  91.638  12.915  1.00 37.25           O  
HETATM 1544  O   HOH A 424     -13.962  88.446  17.141  1.00 32.97           O  
HETATM 1545  O   HOH A 425     -10.078  97.374  11.555  1.00 13.86           O  
HETATM 1546  O   HOH A 426     -24.780  92.512   9.104  1.00 29.16           O  
HETATM 1547  O   HOH A 427     -20.299  61.467  24.520  1.00 34.90           O  
HETATM 1548  O   HOH A 428     -17.003  66.236  24.384  1.00 31.71           O  
HETATM 1549  O   HOH A 429       0.911  72.497  -1.214  1.00 37.76           O  
HETATM 1550  O   HOH A 430     -15.107  66.358   5.132  1.00 28.14           O  
HETATM 1551  O   HOH A 431      -6.213  92.878   4.712  1.00 33.58           O  
HETATM 1552  O   HOH A 432      -9.506  75.526   7.513  1.00 25.19           O  
HETATM 1553  O   HOH A 433     -23.702  89.441   6.923  1.00 17.53           O  
HETATM 1554  O   HOH A 434     -10.458  60.124  10.012  1.00 38.85           O  
HETATM 1555  O   HOH A 435     -14.956  86.850  32.997  1.00 36.92           O  
HETATM 1556  O   HOH A 436      -6.241  83.967  27.155  1.00 34.67           O  
HETATM 1557  O   HOH A 437      -2.988  76.682  11.113  1.00 45.44           O  
HETATM 1558  O   HOH A 438      -3.037  93.255  10.176  1.00 43.90           O  
HETATM 1559  O   HOH A 439      -9.643  81.086  21.320  1.00 22.95           O  
HETATM 1560  O   HOH A 440     -18.872  85.965  -8.419  1.00 48.70           O  
HETATM 1561  O   HOH A 441     -24.619  68.261   5.736  1.00 37.26           O  
HETATM 1562  O   HOH A 442     -14.607  91.058  21.803  1.00 14.43           O  
HETATM 1563  O   HOH A 443     -16.233  87.884  15.718  1.00 23.04           O  
HETATM 1564  O   HOH A 444     -19.115  59.762  10.623  1.00 41.17           O  
HETATM 1565  O   HOH A 445      -7.229  76.376   9.867  1.00 30.29           O  
HETATM 1566  O   HOH A 446     -20.313  93.101  14.059  1.00 26.00           O  
HETATM 1567  O   HOH A 447      -8.594  82.956  23.809  1.00 27.97           O  
HETATM 1568  O   HOH A 448     -10.482  86.881  -3.811  1.00 31.89           O  
HETATM 1569  O   HOH A 449     -18.992  83.233  37.353  1.00 31.42           O  
HETATM 1570  O   HOH A 450     -10.850  72.231  31.317  1.00 54.68           O  
HETATM 1571  O   HOH A 451      -6.466  64.678   7.040  1.00 39.30           O  
HETATM 1572  O   HOH A 452      -8.239  87.949  21.540  1.00 45.87           O  
HETATM 1573  O   HOH A 453     -20.408  93.921   4.963  1.00 38.28           O  
HETATM 1574  O   HOH A 454     -22.685  90.139   3.027  1.00 32.27           O  
HETATM 1575  O   HOH A 455     -25.256  78.055   4.782  1.00 52.44           O  
HETATM 1576  O   HOH A 456     -11.462  76.685   8.886  1.00 21.22           O  
HETATM 1577  O   HOH A 457     -17.037  59.438  26.385  1.00 48.43           O  
HETATM 1578  O   HOH A 458     -13.251  80.250  20.704  1.00 10.36           O  
HETATM 1579  O   HOH A 459      -4.920  61.351  20.687  1.00 48.59           O  
HETATM 1580  O   HOH A 460     -26.678  64.006  23.276  1.00 39.51           O  
HETATM 1581  O   HOH A 461     -24.184  79.047   7.103  1.00 26.20           O  
HETATM 1582  O   HOH A 462      -5.574  93.414  17.465  1.00 22.97           O  
HETATM 1583  O   HOH A 463     -12.333  70.436  29.973  1.00 28.68           O  
HETATM 1584  O   HOH A 464     -36.201  72.366  27.720  1.00 61.21           O  
HETATM 1585  O   HOH A 465     -16.773  58.167  19.582  1.00 40.15           O  
HETATM 1586  O   HOH A 466     -18.792  84.412  35.010  1.00 19.60           O  
HETATM 1587  O   HOH A 467     -21.757  91.264   6.860  1.00 34.60           O  
HETATM 1588  O   HOH A 468     -26.859  71.756  22.459  1.00 28.71           O  
HETATM 1589  O   HOH A 469     -23.011  86.373  23.700  1.00 11.46           O  
HETATM 1590  O   HOH A 470     -24.320  72.189   2.109  1.00 33.89           O  
HETATM 1591  O   HOH A 471     -18.720  59.974  23.400  1.00 44.64           O  
HETATM 1592  O   HOH A 472      -9.576  95.892   7.924  1.00 34.47           O  
HETATM 1593  O   HOH A 473     -19.799  76.984 -10.459  1.00 51.97           O  
HETATM 1594  O   HOH A 474     -28.249  62.401  15.501  1.00 49.34           O  
HETATM 1595  O   HOH A 475     -12.569  56.581  23.686  1.00 48.95           O  
HETATM 1596  O   HOH A 476     -12.818  68.522  32.136  1.00 34.30           O  
HETATM 1597  O   HOH A 477     -13.508  82.871  20.459  1.00 18.36           O  
ANISOU 1597  O   HOH A 477     2671   1855   2452     54    383   -324       O  
HETATM 1598  O   HOH A 478     -22.490  86.843  -3.343  1.00 50.13           O  
HETATM 1599  O   HOH A 479     -25.850  74.171   8.074  1.00 60.14           O  
HETATM 1600  O   HOH A 480      -7.025  59.524  18.493  1.00 58.03           O  
HETATM 1601  O   HOH A 481     -12.979  88.047  -3.868  1.00 30.27           O  
HETATM 1602  O   HOH A 482     -14.427  87.322  19.918  1.00 37.23           O  
HETATM 1603  O   HOH A 483     -22.743  62.857   1.534  1.00 52.13           O  
HETATM 1604  O   HOH A 484     -19.734  58.181  27.270  1.00 52.96           O  
HETATM 1605  O   HOH A 485     -26.393  75.632  12.803  1.00 51.21           O  
HETATM 1606  O   HOH A 486      -3.131  71.311   1.568  1.00 40.57           O  
HETATM 1607  O   HOH A 487      -5.360  95.291   5.649  1.00 44.63           O  
HETATM 1608  O   HOH A 488      -9.606  74.960  -7.762  1.00 28.00           O  
HETATM 1609  O   HOH A 489      -6.354  85.125   2.727  1.00 23.15           O  
HETATM 1610  O   HOH A 490     -11.907  60.427  25.926  1.00 43.68           O  
HETATM 1611  O   HOH A 491      -4.058  82.999   0.798  1.00 48.21           O  
HETATM 1612  O   HOH A 492     -12.703  59.676   9.255  1.00 48.29           O  
HETATM 1613  O   HOH A 493      -8.623  68.369   2.530  1.00 50.70           O  
HETATM 1614  O   HOH A 494     -24.692  63.589   5.767  1.00 48.74           O  
HETATM 1615  O   HOH A 495     -23.256  91.260  24.092  1.00 39.02           O  
HETATM 1616  O   HOH A 496     -14.484  83.257  14.862  1.00 33.09           O  
HETATM 1617  O   HOH A 497     -10.840  84.820  -5.250  1.00 34.22           O  
HETATM 1618  O   HOH A 498     -18.975  63.918  34.374  1.00 51.69           O  
HETATM 1619  O   HOH A 499     -17.034  56.002  16.274  1.00 57.75           O  
HETATM 1620  O   HOH A 500      -9.955  77.200  10.933  1.00 32.18           O  
HETATM 1621  O   HOH A 501     -29.684  69.208  12.429  1.00 56.30           O  
HETATM 1622  O   HOH A 502     -21.041  76.418  42.945  1.00 51.35           O  
HETATM 1623  O   HOH A 503     -30.635  81.257   6.645  1.00 59.45           O  
HETATM 1624  O   HOH A 504      -4.684  83.237   4.241  1.00 50.98           O  
HETATM 1625  O   HOH A 505      -7.259  68.713  -0.857  1.00 40.79           O  
HETATM 1626  O   HOH A 506     -18.443  94.966  13.196  1.00 45.44           O  
HETATM 1627  O   HOH A 507     -16.047  84.894  15.911  1.00 33.36           O  
HETATM 1628  O   HOH A 508     -17.490  88.478  18.273  1.00 35.25           O  
HETATM 1629  O   HOH A 509      -8.796  89.162  -3.558  1.00 55.06           O  
HETATM 1630  O   HOH A 510     -24.326  69.455   3.324  1.00 41.91           O  
HETATM 1631  O   HOH A 511     -18.573  95.068   2.280  1.00 42.78           O  
HETATM 1632  O   HOH A 512      -7.602  84.795  25.684  1.00 38.60           O  
HETATM 1633  O   HOH A 513     -10.900  64.752  27.358  1.00 41.79           O  
HETATM 1634  O   HOH A 514     -10.647  61.780  27.363  1.00 51.26           O  
HETATM 1635  O   HOH A 515      -9.940  85.643  22.525  1.00 26.91           O  
HETATM 1636  O   HOH A 516     -27.386  77.978  15.637  1.00 61.74           O  
HETATM 1637  O   HOH A 517     -24.118  88.301   4.252  1.00 22.07           O  
HETATM 1638  O   HOH A 518     -12.998  86.020  18.086  1.00 44.23           O  
HETATM 1639  O   HOH A 519     -19.164  87.304  35.522  1.00 30.53           O  
HETATM 1640  O   HOH A 520      -7.093  59.704   8.619  1.00 49.56           O  
HETATM 1641  O   HOH A 521     -26.016  65.983   4.949  1.00 42.28           O  
HETATM 1642  O   HOH A 522     -12.348  85.409  20.783  1.00 22.22           O  
HETATM 1643  O   HOH A 523     -27.262  85.369  -1.802  1.00 58.95           O  
HETATM 1644  O   HOH A 524      -7.536  98.585   0.064  1.00 53.53           O  
HETATM 1645  O   HOH A 525     -24.252  90.372   0.520  1.00 61.05           O  
HETATM 1646  O   HOH A 526     -18.473  54.365  20.141  1.00 56.79           O  
CONECT  331 1447                                                                
CONECT  494 1448                                                                
CONECT  705 1448                                                                
CONECT  706 1447                                                                
CONECT  811 1447                                                                
CONECT  815 1447                                                                
CONECT 1447  331  706  811  815                                                 
CONECT 1447 1513 1514 1515 1516                                                 
CONECT 1448  494  705 1511 1512                                                 
CONECT 1448 1513 1514 1527 1578                                                 
CONECT 1449 1471 1481 1497                                                      
CONECT 1450 1472 1482 1498                                                      
CONECT 1451 1453 1461 1495                                                      
CONECT 1452 1454 1462 1496                                                      
CONECT 1453 1451 1455                                                           
CONECT 1454 1452 1456                                                           
CONECT 1455 1453 1457                                                           
CONECT 1456 1454 1458                                                           
CONECT 1457 1455 1459                                                           
CONECT 1458 1456 1460                                                           
CONECT 1459 1457 1461                                                           
CONECT 1460 1458 1462                                                           
CONECT 1461 1451 1459                                                           
CONECT 1462 1452 1460                                                           
CONECT 1463 1465 1489 1513                                                      
CONECT 1464 1466 1490 1514                                                      
CONECT 1465 1463 1507 1515                                                      
CONECT 1466 1464 1508 1516                                                      
CONECT 1467 1469 1485                                                           
CONECT 1468 1470 1486                                                           
CONECT 1469 1467 1473                                                           
CONECT 1470 1468 1474                                                           
CONECT 1471 1449 1475 1483                                                      
CONECT 1472 1450 1476 1484                                                      
CONECT 1473 1469 1501                                                           
CONECT 1474 1470 1502                                                           
CONECT 1475 1471 1477 1499                                                      
CONECT 1476 1472 1478 1500                                                      
CONECT 1477 1475 1479                                                           
CONECT 1478 1476 1480                                                           
CONECT 1479 1477 1481                                                           
CONECT 1480 1478 1482                                                           
CONECT 1481 1449 1479                                                           
CONECT 1482 1450 1480                                                           
CONECT 1483 1471 1501 1509                                                      
CONECT 1484 1472 1502 1510                                                      
CONECT 1485 1467 1487 1501                                                      
CONECT 1486 1468 1488 1502                                                      
CONECT 1487 1485 1503 1507                                                      
CONECT 1488 1486 1504 1508                                                      
CONECT 1489 1463 1491 1503                                                      
CONECT 1490 1464 1492 1504                                                      
CONECT 1491 1489 1505 1511                                                      
CONECT 1492 1490 1506 1512                                                      
CONECT 1493 1495 1505                                                           
CONECT 1494 1496 1506                                                           
CONECT 1495 1451 1493                                                           
CONECT 1496 1452 1494                                                           
CONECT 1497 1449                                                                
CONECT 1498 1450                                                                
CONECT 1499 1475                                                                
CONECT 1500 1476                                                                
CONECT 1501 1473 1483 1485                                                      
CONECT 1502 1474 1484 1486                                                      
CONECT 1503 1487 1489                                                           
CONECT 1504 1488 1490                                                           
CONECT 1505 1491 1493                                                           
CONECT 1506 1492 1494                                                           
CONECT 1507 1465 1487                                                           
CONECT 1508 1466 1488                                                           
CONECT 1509 1483                                                                
CONECT 1510 1484                                                                
CONECT 1511 1448 1491                                                           
CONECT 1512 1448 1492                                                           
CONECT 1513 1447 1448 1463                                                      
CONECT 1514 1447 1448 1464                                                      
CONECT 1515 1447 1465                                                           
CONECT 1516 1447 1466                                                           
CONECT 1517 1518 1519                                                           
CONECT 1518 1517                                                                
CONECT 1519 1517 1520                                                           
CONECT 1520 1519                                                                
CONECT 1527 1448                                                                
CONECT 1578 1448                                                                
MASTER      394    0    4    8    5    0   11    6 1611    1   84   15          
END                                                                             



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