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***  HYDROLASE/HYDROLASE INHIBITOR 07-APR-21 7MEQ  ***

elNémo ID: 21100610522125101

Job options:

ID        	=	 21100610522125101
JOBID     	=	 HYDROLASE/HYDROLASE INHIBITOR 07-APR-21 7MEQ
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
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-APR-21   7MEQ              
TITLE     CRYSTAL STRUCTURE OF HUMAN TMPRSS2 IN COMPLEX WITH NAFAMOSTAT         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SERINE PROTEASE 10;                                         
COMPND   5 EC: 3.4.21.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TMPRSS2, PRSS10;                                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    COVID19, PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.FRASER,S.BELDAR,A.HUTCHINSON,Y.LI,A.SEITOVA,A.M.EDWARDS,F.BENARD,   
AUTHOR   2 C.H.ARROWSMITH,L.HALABELIAN,STRUCTURAL GENOMICS CONSORTIUM (SGC)     
REVDAT   1   21-APR-21 7MEQ    0                                                
JRNL        AUTH   B.FRASER,S.BELDAR,A.HUTCHINSON,Y.LI,A.SEITOVA,A.M.EDWARDS,   
JRNL        AUTH 2 F.BENARD,C.H.ARROWSMITH,L.HALABELIAN,                        
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TMPRSS2 IN COMPLEX WITH           
JRNL        TITL 2 NAFAMOSTAT                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27797                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.193                          
REMARK   3   R VALUE            (WORKING SET)  : 0.192                          
REMARK   3   FREE R VALUE                      : 0.225                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.760                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1322                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.95                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.96                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.30                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 556                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2232                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 533                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2226                   
REMARK   3   BIN FREE R VALUE                        : 0.2431                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.14                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 23                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2482                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 118                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -19.42080                                            
REMARK   3    B22 (A**2) : 5.04720                                              
REMARK   3    B33 (A**2) : 14.37360                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -7.66000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.320               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.147               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.135               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.147               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.136               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2598   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3550   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 825    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 442    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2598   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 338    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2909   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.29                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.06                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    7.3127   -8.3286   13.8778           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1856 T22:   -0.2074                                    
REMARK   3     T33:   -0.1874 T12:    0.0184                                    
REMARK   3     T13:    0.0754 T23:   -0.0142                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8045 L22:    1.1951                                    
REMARK   3     L33:    2.1824 L12:    0.0343                                    
REMARK   3     L13:   -0.1650 L23:   -0.1946                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0120 S12:    0.0613 S13:   -0.0408                     
REMARK   3     S21:   -0.0716 S22:    0.0310 S23:   -0.0976                     
REMARK   3     S31:    0.0925 S32:    0.1445 S33:   -0.0190                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7MEQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-21.                  
REMARK 100 THE DEPOSITION ID IS D_1000255490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27823                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81100                            
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: 1Z8G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30.0% (W/V) JEFFAMINE ED-2001 7.0, 0.1   
REMARK 280  M HEPES PH7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.71250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   109                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     CYS A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     ASN A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     ILE A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     CYS A   120                                                      
REMARK 465     ASP A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     ILE A   127                                                      
REMARK 465     ASN A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     SER A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     TRP A   132                                                      
REMARK 465     CYS A   133                                                      
REMARK 465     ASP A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     VAL A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     HIS A   138                                                      
REMARK 465     CYS A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     GLY A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     GLU A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     ASN A   146                                                      
REMARK 465     ARG A   147                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     ARG A   165                                                      
REMARK 465     LYS A   166                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     GLY A   205                                                      
REMARK 465     SER A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     ASN A   218                                                      
REMARK 465     VAL A   219                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     ASP A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     GLY A   492                                                      
REMARK 465     GLU A   493                                                      
REMARK 465     PHE A   494                                                      
REMARK 465     VAL A   495                                                      
REMARK 465     GLU A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     HIS A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     HIS A   504                                                      
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     SER A 162    OG                                                  
REMARK 470     SER A 163    OG                                                  
REMARK 470     SER A 167    OG                                                  
REMARK 470     ASN A 179    CG   OD1  ND2                                       
REMARK 470     LYS A 191    CG   CD   CE   NZ                                   
REMARK 470     ILE A 200    CG1  CG2  CD1                                       
REMARK 470     SER A 208    OG                                                  
REMARK 470     ILE A 221    CG1  CG2  CD1                                       
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     HIS A 227    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 229    CG   OD1  OD2                                       
REMARK 470     LYS A 234    CE   NZ                                             
REMARK 470     LEU A 248    CG   CD1  CD2                                       
REMARK 470     LYS A 340    CD   CE   NZ                                        
REMARK 470     LYS A 353    CG   CD   CE   NZ                                   
REMARK 470     LYS A 390    CE   NZ                                             
REMARK 470     LYS A 392    CG   CD   CE   NZ                                   
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 438    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 486    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 489    CG   CD   NE   CZ   NH1  NH2                        
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   OG   SER A   441     O    GBS A   601              2.05            
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    ASP A 175        6.54     58.58                                   
REMARK 500    LYS A 191     -103.39     47.94                                   
REMARK 500    TYR A 195      -60.78   -121.91                                   
REMARK 500    VAL A 415     -101.33   -107.09                                   
REMARK 500    ASP A 417       77.70     31.58                                   
REMARK 500    ASN A 433      -33.55     77.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 IN THIS CONSTRUCT SER250 IS DELETED AND RESIDUES 251-255 ARE         
REMARK 999 REPLACED WITH 251-DDDDK-255 TO MODIFY AUTOPROTEOLYTIC ACTIVITY. THE  
REMARK 999 PROTEIN IS EXPRESSED AS A ZYMOGEN AND ACTIVATED THROUGH              
REMARK 999 AUTOPROTEOLYTIC CLEAVAGE OF LOOP REGION RESIDUES 255-256. THE        
REMARK 999 CLEAVED I256 ADOPTS A CATALYTICALLY ACTIVE MODE BY FORMING A SALT    
REMARK 999 BRIDGE WITH ASP440. A SIMILAR ACTIVATION MECHANISM HAS BEEN          
REMARK 999 OBSERVED FOR OTHER PROTEASES SUCH AS PDB ID 6KD5.                    
DBREF  7MEQ A  109   492  UNP    O15393   TMPS2_HUMAN    109    492             
SEQADV 7MEQ ASP A  251  UNP  O15393    SER   250 CONFLICT                       
SEQADV 7MEQ ASP A  252  UNP  O15393    SER   251 CONFLICT                       
SEQADV 7MEQ     A       UNP  O15393    ARG   252 DELETION                       
SEQADV 7MEQ ASP A  253  UNP  O15393    GLN   253 CONFLICT                       
SEQADV 7MEQ ASP A  254  UNP  O15393    SER   254 CONFLICT                       
SEQADV 7MEQ LYS A  255  UNP  O15393    ARG   255 CONFLICT                       
SEQADV 7MEQ GLU A  493  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ PHE A  494  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ VAL A  495  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ GLU A  496  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  497  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  498  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  499  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  500  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  501  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  502  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  503  UNP  O15393              EXPRESSION TAG                 
SEQADV 7MEQ HIS A  504  UNP  O15393              EXPRESSION TAG                 
SEQRES   1 A  395  MET GLY SER LYS CYS SER ASN SER GLY ILE GLU CYS ASP          
SEQRES   2 A  395  SER SER GLY THR CYS ILE ASN PRO SER ASN TRP CYS ASP          
SEQRES   3 A  395  GLY VAL SER HIS CYS PRO GLY GLY GLU ASP GLU ASN ARG          
SEQRES   4 A  395  CYS VAL ARG LEU TYR GLY PRO ASN PHE ILE LEU GLN VAL          
SEQRES   5 A  395  TYR SER SER GLN ARG LYS SER TRP HIS PRO VAL CYS GLN          
SEQRES   6 A  395  ASP ASP TRP ASN GLU ASN TYR GLY ARG ALA ALA CYS ARG          
SEQRES   7 A  395  ASP MET GLY TYR LYS ASN ASN PHE TYR SER SER GLN GLY          
SEQRES   8 A  395  ILE VAL ASP ASP SER GLY SER THR SER PHE MET LYS LEU          
SEQRES   9 A  395  ASN THR SER ALA GLY ASN VAL ASP ILE TYR LYS LYS LEU          
SEQRES  10 A  395  TYR HIS SER ASP ALA CYS SER SER LYS ALA VAL VAL SER          
SEQRES  11 A  395  LEU ARG CYS ILE ALA CYS GLY VAL ASN LEU ASN ASP ASP          
SEQRES  12 A  395  ASP ASP LYS ILE VAL GLY GLY GLU SER ALA LEU PRO GLY          
SEQRES  13 A  395  ALA TRP PRO TRP GLN VAL SER LEU HIS VAL GLN ASN VAL          
SEQRES  14 A  395  HIS VAL CYS GLY GLY SER ILE ILE THR PRO GLU TRP ILE          
SEQRES  15 A  395  VAL THR ALA ALA HIS CYS VAL GLU LYS PRO LEU ASN ASN          
SEQRES  16 A  395  PRO TRP HIS TRP THR ALA PHE ALA GLY ILE LEU ARG GLN          
SEQRES  17 A  395  SER PHE MET PHE TYR GLY ALA GLY TYR GLN VAL GLU LYS          
SEQRES  18 A  395  VAL ILE SER HIS PRO ASN TYR ASP SER LYS THR LYS ASN          
SEQRES  19 A  395  ASN ASP ILE ALA LEU MET LYS LEU GLN LYS PRO LEU THR          
SEQRES  20 A  395  PHE ASN ASP LEU VAL LYS PRO VAL CYS LEU PRO ASN PRO          
SEQRES  21 A  395  GLY MET MET LEU GLN PRO GLU GLN LEU CYS TRP ILE SER          
SEQRES  22 A  395  GLY TRP GLY ALA THR GLU GLU LYS GLY LYS THR SER GLU          
SEQRES  23 A  395  VAL LEU ASN ALA ALA LYS VAL LEU LEU ILE GLU THR GLN          
SEQRES  24 A  395  ARG CYS ASN SER ARG TYR VAL TYR ASP ASN LEU ILE THR          
SEQRES  25 A  395  PRO ALA MET ILE CYS ALA GLY PHE LEU GLN GLY ASN VAL          
SEQRES  26 A  395  ASP SER CYS GLN GLY ASP SER GLY GLY PRO LEU VAL THR          
SEQRES  27 A  395  SER LYS ASN ASN ILE TRP TRP LEU ILE GLY ASP THR SER          
SEQRES  28 A  395  TRP GLY SER GLY CYS ALA LYS ALA TYR ARG PRO GLY VAL          
SEQRES  29 A  395  TYR GLY ASN VAL MET VAL PHE THR ASP TRP ILE TYR ARG          
SEQRES  30 A  395  GLN MET ARG ALA ASP GLY GLU PHE VAL GLU HIS HIS HIS          
SEQRES  31 A  395  HIS HIS HIS HIS HIS                                          
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    GBS  A 601      12                                                       
HET    UNX  A 602       1                                                       
HET    UNX  A 603       1                                                       
HET    UNX  A 604       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GBS 4-CARBAMIMIDAMIDOBENZOIC ACID                                    
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     GBS NAFAMOSTAT, BOUND FORM                                           
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3  GBS    C8 H9 N3 O2                                                  
FORMUL   4  UNX    3(X)                                                         
FORMUL   7  HOH   *118(H2 O)                                                    
HELIX    1 AA1 ASN A  177  MET A  188  1                                  12    
HELIX    2 AA2 ALA A  294  GLU A  299  5                                   6    
HELIX    3 AA3 ASN A  304  TRP A  306  5                                   3    
HELIX    4 AA4 ARG A  316  MET A  320  5                                   5    
HELIX    5 AA5 GLU A  406  ASN A  411  1                                   6    
HELIX    6 AA6 VAL A  477  ASP A  491  1                                  15    
SHEET    1 AA1 3 VAL A 149  TYR A 152  0                                        
SHEET    2 AA1 3 ILE A 157  TYR A 161 -1  O  GLN A 159   N  ARG A 150           
SHEET    3 AA1 3 TRP A 168  PRO A 170 -1  O  HIS A 169   N  VAL A 160           
SHEET    1 AA2 2 SER A 196  ILE A 200  0                                        
SHEET    2 AA2 2 VAL A 236  ARG A 240 -1  O  ARG A 240   N  SER A 196           
SHEET    1 AA3 2 PHE A 209  LEU A 212  0                                        
SHEET    2 AA3 2 LEU A 225  SER A 228 -1  O  TYR A 226   N  LYS A 211           
SHEET    1 AA4 8 GLU A 260  SER A 261  0                                        
SHEET    2 AA4 8 ASN A 398  ILE A 405 -1  O  ALA A 399   N  GLU A 260           
SHEET    3 AA4 8 MET A 424  GLY A 428 -1  O  CYS A 426   N  ILE A 405           
SHEET    4 AA4 8 GLY A 472  ASN A 476 -1  O  TYR A 474   N  ILE A 425           
SHEET    5 AA4 8 ILE A 452  TRP A 461 -1  N  TRP A 461   O  VAL A 473           
SHEET    6 AA4 8 PRO A 444  LYS A 449 -1  N  THR A 447   O  TRP A 454           
SHEET    7 AA4 8 LEU A 378  GLY A 383 -1  N  TRP A 380   O  VAL A 446           
SHEET    8 AA4 8 ASN A 398  ILE A 405 -1  O  VAL A 402   N  CYS A 379           
SHEET    1 AA5 7 GLN A 270  VAL A 275  0                                        
SHEET    2 AA5 7 VAL A 278  ILE A 285 -1  O  CYS A 281   N  LEU A 273           
SHEET    3 AA5 7 TRP A 290  THR A 293 -1  O  VAL A 292   N  SER A 284           
SHEET    4 AA5 7 ALA A 347  LEU A 351 -1  O  ALA A 347   N  THR A 293           
SHEET    5 AA5 7 TYR A 326  SER A 333 -1  N  GLU A 329   O  LYS A 350           
SHEET    6 AA5 7 TRP A 308  ALA A 312 -1  N  ALA A 310   O  TYR A 326           
SHEET    7 AA5 7 GLN A 270  VAL A 275 -1  N  HIS A 274   O  THR A 309           
SSBOND   1 CYS A  172    CYS A  231                          1555   1555  2.04  
SSBOND   2 CYS A  185    CYS A  241                          1555   1555  2.04  
SSBOND   3 CYS A  244    CYS A  365                          1555   1555  2.04  
SSBOND   4 CYS A  281    CYS A  297                          1555   1555  2.04  
SSBOND   5 CYS A  410    CYS A  426                          1555   1555  2.04  
SSBOND   6 CYS A  437    CYS A  465                          1555   1555  2.05  
LINK         ND2 ASN A 213                 C1  NAG B   1     1555   1555  1.44  
LINK         OG  SER A 441                 C6  GBS A 601     1555   1555  1.47  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.43  
CISPEP   1 LYS A  300    PRO A  301          0         7.04                     
CRYST1   59.445   51.425   64.353  90.00  91.53  90.00 P 1 21 1      2          
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      0.016822  0.000000  0.000449        0.00000                         
SCALE2      0.000000  0.019446  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015545        0.00000                         
ATOM      1  N   CYS A 148      16.314 -18.520  -1.196  1.00-1.274           N  
ANISOU    1  N   CYS A 148    14056   9461   8944   1065   1729   -733       N  
ATOM      2  CA  CYS A 148      16.431 -19.802  -0.489  1.00-1.274           C  
ANISOU    2  CA  CYS A 148    14094   9313   8938   1185   1723   -762       C  
ATOM      3  C   CYS A 148      17.461 -19.766   0.680  1.00-1.274           C  
ANISOU    3  C   CYS A 148    13817   9286   8940   1297   1730   -710       C  
ATOM      4  O   CYS A 148      18.045 -20.794   1.041  1.00-1.274           O  
ANISOU    4  O   CYS A 148    13753   9135   8857   1451   1768   -729       O  
ATOM      5  CB  CYS A 148      16.707 -20.942  -1.468  1.00-1.274           C  
ANISOU    5  CB  CYS A 148    14387   9353   8965   1296   1816   -844       C  
ATOM      6  SG  CYS A 148      17.767 -20.486  -2.866  1.00-1.274           S  
ANISOU    6  SG  CYS A 148    14881  10031   9420   1354   1965   -869       S  
ATOM      7  N   VAL A 149      17.636 -18.568   1.283  1.00-0.663           N  
ANISOU    7  N   VAL A 149    12738   8499   8105   1214   1688   -643       N  
ATOM      8  CA  VAL A 149      18.550 -18.284   2.399  1.00-0.663           C  
ANISOU    8  CA  VAL A 149    12247   8288   7891   1279   1675   -589       C  
ATOM      9  C   VAL A 149      17.707 -17.792   3.590  1.00-0.663           C  
ANISOU    9  C   VAL A 149    11929   7959   7665   1170   1550   -542       C  
ATOM     10  O   VAL A 149      16.896 -16.879   3.422  1.00-0.663           O  
ANISOU   10  O   VAL A 149    11781   7811   7504   1023   1500   -525       O  
ATOM     11  CB  VAL A 149      19.634 -17.242   1.971  1.00-0.663           C  
ANISOU   11  CB  VAL A 149    12588   8997   8426   1264   1748   -558       C  
ATOM     12  CG1 VAL A 149      20.538 -16.850   3.135  1.00-0.663           C  
ANISOU   12  CG1 VAL A 149    12346   9068   8476   1305   1721   -502       C  
ATOM     13  CG2 VAL A 149      20.471 -17.755   0.799  1.00-0.663           C  
ANISOU   13  CG2 VAL A 149    12611   9042   8353   1375   1886   -603       C  
ATOM     14  N   ARG A 150      17.897 -18.397   4.784  1.00-1.011           N  
ANISOU   14  N   ARG A 150    11065   7083   6884   1251   1502   -520       N  
ATOM     15  CA  ARG A 150      17.151 -18.018   5.993  1.00-1.011           C  
ANISOU   15  CA  ARG A 150    10800   6803   6695   1163   1393   -477       C  
ATOM     16  C   ARG A 150      18.011 -17.975   7.269  1.00-1.011           C  
ANISOU   16  C   ARG A 150    10665   6884   6774   1242   1360   -429       C  
ATOM     17  O   ARG A 150      19.111 -18.539   7.304  1.00-1.011           O  
ANISOU   17  O   ARG A 150    10485   6823   6668   1391   1413   -430       O  
ATOM     18  CB  ARG A 150      15.947 -18.970   6.195  1.00-1.011           C  
ANISOU   18  CB  ARG A 150    10713   6357   6396   1138   1341   -503       C  
ATOM     19  CG  ARG A 150      16.296 -20.282   6.884  1.00-1.011           C  
ANISOU   19  CG  ARG A 150    10668   6147   6293   1282   1343   -507       C  
ATOM     20  CD  ARG A 150      15.103 -21.182   7.021  1.00-1.011           C  
ANISOU   20  CD  ARG A 150    10045   5160   5450   1231   1298   -531       C  
ATOM     21  NE  ARG A 150      15.408 -22.388   7.796  1.00-1.011           N  
ANISOU   21  NE  ARG A 150    11048   5977   6385   1363   1296   -525       N  
ATOM     22  CZ  ARG A 150      14.497 -23.309   8.091  1.00-1.011           C  
ANISOU   22  CZ  ARG A 150    12719   7314   7862   1328   1261   -538       C  
ATOM     23  NH1 ARG A 150      13.238 -23.154   7.701  1.00-1.011           N  
ANISOU   23  NH1 ARG A 150    12286   6735   7312   1163   1220   -559       N  
ATOM     24  NH2 ARG A 150      14.832 -24.383   8.796  1.00-1.011           N  
ANISOU   24  NH2 ARG A 150    10006   4415   5074   1454   1263   -525       N  
ATOM     25  N   LEU A 151      17.467 -17.340   8.327  1.00-0.265           N  
ANISOU   25  N   LEU A 151     9838   6101   6034   1147   1269   -387       N  
ATOM     26  CA  LEU A 151      18.064 -17.305   9.666  1.00-0.265           C  
ANISOU   26  CA  LEU A 151     9547   5975   5909   1200   1215   -342       C  
ATOM     27  C   LEU A 151      17.232 -18.230  10.554  1.00-0.265           C  
ANISOU   27  C   LEU A 151     9880   6035   6114   1223   1153   -334       C  
ATOM     28  O   LEU A 151      16.008 -18.154  10.519  1.00-0.265           O  
ANISOU   28  O   LEU A 151     9905   5862   6017   1115   1116   -343       O  
ATOM     29  CB  LEU A 151      18.127 -15.877  10.233  1.00-0.265           C  
ANISOU   29  CB  LEU A 151     9369   6036   5902   1072   1164   -304       C  
ATOM     30  CG  LEU A 151      19.036 -14.891   9.480  1.00-0.265           C  
ANISOU   30  CG  LEU A 151     9728   6679   6400   1031   1224   -301       C  
ATOM     31  CD1 LEU A 151      18.946 -13.509  10.082  1.00-0.265           C  
ANISOU   31  CD1 LEU A 151     9555   6666   6349    889   1168   -268       C  
ATOM     32  CD2 LEU A 151      20.492 -15.385   9.408  1.00-0.265           C  
ANISOU   32  CD2 LEU A 151     9722   6915   6534   1176   1282   -297       C  
ATOM     33  N   TYR A 152      17.874 -19.153  11.276  1.00 0.020           N  
ANISOU   33  N   TYR A 152     9379   5516   5628   1369   1146   -316       N  
ATOM     34  CA  TYR A 152      17.156 -20.138  12.086  1.00 0.020           C  
ANISOU   34  CA  TYR A 152     9483   5332   5585   1399   1098   -304       C  
ATOM     35  C   TYR A 152      17.370 -20.007  13.599  1.00 0.020           C  
ANISOU   35  C   TYR A 152     9664   5622   5875   1420   1018   -246       C  
ATOM     36  O   TYR A 152      18.514 -19.959  14.058  1.00 0.020           O  
ANISOU   36  O   TYR A 152     9488   5686   5852   1526   1014   -217       O  
ATOM     37  CB  TYR A 152      17.501 -21.569  11.608  1.00 0.020           C  
ANISOU   37  CB  TYR A 152     9759   5367   5696   1560   1158   -335       C  
ATOM     38  CG  TYR A 152      16.845 -22.680  12.408  1.00 0.020           C  
ANISOU   38  CG  TYR A 152    10259   5535   6020   1596   1118   -319       C  
ATOM     39  CD1 TYR A 152      15.615 -23.211  12.026  1.00 0.020           C  
ANISOU   39  CD1 TYR A 152    10705   5641   6246   1496   1114   -353       C  
ATOM     40  CD2 TYR A 152      17.475 -23.232  13.521  1.00 0.020           C  
ANISOU   40  CD2 TYR A 152    10344   5645   6151   1727   1083   -268       C  
ATOM     41  CE1 TYR A 152      15.010 -24.237  12.755  1.00 0.020           C  
ANISOU   41  CE1 TYR A 152    10806   5427   6176   1511   1082   -335       C  
ATOM     42  CE2 TYR A 152      16.859 -24.222  14.285  1.00 0.020           C  
ANISOU   42  CE2 TYR A 152    10663   5642   6292   1751   1048   -245       C  
ATOM     43  CZ  TYR A 152      15.635 -24.737  13.887  1.00 0.020           C  
ANISOU   43  CZ  TYR A 152    11856   6488   7265   1640   1053   -280       C  
ATOM     44  OH  TYR A 152      15.041 -25.735  14.628  1.00 0.020           O  
ANISOU   44  OH  TYR A 152    12365   6669   7590   1651   1026   -254       O  
ATOM     45  N   GLY A 153      16.259 -20.067  14.346  1.00 0.346           N  
ANISOU   45  N   GLY A 153     9074   4844   5189   1326    959   -228       N  
ATOM     46  CA  GLY A 153      16.219 -20.047  15.804  1.00 0.346           C  
ANISOU   46  CA  GLY A 153     8882   4682   5038   1333    884   -174       C  
ATOM     47  C   GLY A 153      16.631 -18.753  16.488  1.00 0.346           C  
ANISOU   47  C   GLY A 153     8959   5073   5310   1262    833   -146       C  
ATOM     48  O   GLY A 153      16.897 -17.748  15.818  1.00 0.346           O  
ANISOU   48  O   GLY A 153     8575   4886   5037   1189    857   -166       O  
ATOM     49  N   PRO A 154      16.695 -18.760  17.852  1.00 0.767           N  
ANISOU   49  N   PRO A 154     8611   4759   4986   1276    763   -100       N  
ATOM     50  CA  PRO A 154      17.079 -17.542  18.586  1.00 0.767           C  
ANISOU   50  CA  PRO A 154     8446   4867   4979   1200    708    -79       C  
ATOM     51  C   PRO A 154      18.560 -17.157  18.486  1.00 0.767           C  
ANISOU   51  C   PRO A 154     8825   5589   5557   1271    710    -71       C  
ATOM     52  O   PRO A 154      18.937 -16.081  18.959  1.00 0.767           O  
ANISOU   52  O   PRO A 154     8689   5684   5551   1186    667    -62       O  
ATOM     53  CB  PRO A 154      16.670 -17.846  20.047  1.00 0.767           C  
ANISOU   53  CB  PRO A 154     8747   5063   5204   1205    636    -35       C  
ATOM     54  CG  PRO A 154      16.017 -19.176  20.044  1.00 0.767           C  
ANISOU   54  CG  PRO A 154     9444   5432   5710   1270    657    -28       C  
ATOM     55  CD  PRO A 154      16.419 -19.874  18.783  1.00 0.767           C  
ANISOU   55  CD  PRO A 154     8957   4878   5194   1357    730    -64       C  
ATOM     56  N   ASN A 155      19.401 -18.029  17.909  1.00-0.488           N  
ANISOU   56  N   ASN A 155     8413   5214   5168   1423    759    -76       N  
ATOM     57  CA  ASN A 155      20.824 -17.740  17.728  1.00-0.488           C  
ANISOU   57  CA  ASN A 155     8318   5480   5282   1500    772    -67       C  
ATOM     58  C   ASN A 155      21.191 -17.303  16.283  1.00-0.488           C  
ANISOU   58  C   ASN A 155     8757   6042   5791   1472    866   -108       C  
ATOM     59  O   ASN A 155      22.378 -17.188  15.964  1.00-0.488           O  
ANISOU   59  O   ASN A 155     8501   6087   5707   1545    897   -103       O  
ATOM     60  CB  ASN A 155      21.689 -18.901  18.212  1.00-0.488           C  
ANISOU   60  CB  ASN A 155     8648   5841   5625   1710    761    -32       C  
ATOM     61  CG  ASN A 155      21.933 -18.789  19.687  1.00-0.488           C  
ANISOU   61  CG  ASN A 155    10671   7968   7693   1720    654     22       C  
ATOM     62  OD1 ASN A 155      22.482 -17.795  20.180  1.00-0.488           O  
ANISOU   62  OD1 ASN A 155     9743   7345   6932   1639    599     35       O  
ATOM     63  ND2 ASN A 155      21.496 -19.783  20.427  1.00-0.488           N  
ANISOU   63  ND2 ASN A 155     9785   6815   6640   1808    621     53       N  
ATOM     64  N   PHE A 156      20.168 -17.012  15.441  1.00-0.311           N  
ANISOU   64  N   PHE A 156     8391   5465   5296   1360    906   -146       N  
ATOM     65  CA  PHE A 156      20.299 -16.521  14.057  1.00-0.311           C  
ANISOU   65  CA  PHE A 156     8265   5405   5190   1309    991   -184       C  
ATOM     66  C   PHE A 156      21.271 -17.353  13.208  1.00-0.311           C  
ANISOU   66  C   PHE A 156     8822   6038   5772   1472   1079   -202       C  
ATOM     67  O   PHE A 156      22.155 -16.783  12.556  1.00-0.311           O  
ANISOU   67  O   PHE A 156     8480   5975   5578   1468   1134   -207       O  
ATOM     68  CB  PHE A 156      20.734 -15.033  14.036  1.00-0.311           C  
ANISOU   68  CB  PHE A 156     8240   5674   5338   1169    978   -174       C  
ATOM     69  CG  PHE A 156      19.916 -14.063  14.843  1.00-0.311           C  
ANISOU   69  CG  PHE A 156     8333   5714   5412   1016    902   -161       C  
ATOM     70  CD1 PHE A 156      20.155 -13.889  16.203  1.00-0.311           C  
ANISOU   70  CD1 PHE A 156     8581   6059   5728   1012    815   -128       C  
ATOM     71  CD2 PHE A 156      18.942 -13.281  14.238  1.00-0.311           C  
ANISOU   71  CD2 PHE A 156     8588   5830   5578    881    918   -180       C  
ATOM     72  CE1 PHE A 156      19.402 -12.979  16.951  1.00-0.311           C  
ANISOU   72  CE1 PHE A 156     8648   6061   5759    877    754   -121       C  
ATOM     73  CE2 PHE A 156      18.207 -12.352  14.983  1.00-0.311           C  
ANISOU   73  CE2 PHE A 156     8843   6037   5815    756    856   -167       C  
ATOM     74  CZ  PHE A 156      18.454 -12.198  16.328  1.00-0.311           C  
ANISOU   74  CZ  PHE A 156     8554   5829   5583    755    779   -142       C  
ATOM     75  N   ILE A 157      21.140 -18.700  13.257  1.00 0.521           N  
ANISOU   75  N   ILE A 157     8744   5711   5546   1620   1095   -209       N  
ATOM     76  CA  ILE A 157      21.994 -19.614  12.493  1.00 0.521           C  
ANISOU   76  CA  ILE A 157     8749   5733   5539   1801   1185   -230       C  
ATOM     77  C   ILE A 157      21.638 -19.510  11.015  1.00 0.521           C  
ANISOU   77  C   ILE A 157     9387   6251   6059   1748   1278   -287       C  
ATOM     78  O   ILE A 157      20.488 -19.760  10.636  1.00 0.521           O  
ANISOU   78  O   ILE A 157     9417   5955   5880   1668   1274   -319       O  
ATOM     79  CB  ILE A 157      21.939 -21.079  13.012  1.00 0.521           C  
ANISOU   79  CB  ILE A 157     9294   5998   5927   1976   1176   -220       C  
ATOM     80  CG1 ILE A 157      22.280 -21.138  14.513  1.00 0.521           C  
ANISOU   80  CG1 ILE A 157     9323   6143   6056   2025   1075   -155       C  
ATOM     81  CG2 ILE A 157      22.876 -22.002  12.180  1.00 0.521           C  
ANISOU   81  CG2 ILE A 157     9267   5984   5881   2186   1279   -245       C  
ATOM     82  CD1 ILE A 157      21.721 -22.370  15.258  1.00 0.521           C  
ANISOU   82  CD1 ILE A 157    10899   7343   7419   2121   1039   -135       C  
ATOM     83  N   LEU A 158      22.624 -19.114  10.191  1.00-1.220           N  
ANISOU   83  N   LEU A 158     8900   6045   5707   1785   1360   -298       N  
ATOM     84  CA  LEU A 158      22.447 -18.986   8.749  1.00-1.220           C  
ANISOU   84  CA  LEU A 158     9003   6067   5698   1746   1458   -349       C  
ATOM     85  C   LEU A 158      22.249 -20.353   8.110  1.00-1.220           C  
ANISOU   85  C   LEU A 158    10070   6798   6527   1891   1524   -398       C  
ATOM     86  O   LEU A 158      23.083 -21.254   8.278  1.00-1.220           O  
ANISOU   86  O   LEU A 158    10002   6760   6482   2090   1564   -394       O  
ATOM     87  CB  LEU A 158      23.641 -18.252   8.120  1.00-1.220           C  
ANISOU   87  CB  LEU A 158     8775   6243   5681   1755   1537   -342       C  
ATOM     88  CG  LEU A 158      23.554 -17.952   6.620  1.00-1.220           C  
ANISOU   88  CG  LEU A 158     9355   6782   6154   1703   1644   -386       C  
ATOM     89  CD1 LEU A 158      22.508 -16.873   6.327  1.00-1.220           C  
ANISOU   89  CD1 LEU A 158     9475   6800   6198   1482   1600   -387       C  
ATOM     90  CD2 LEU A 158      24.886 -17.521   6.100  1.00-1.220           C  
ANISOU   90  CD2 LEU A 158     9155   6985   6163   1756   1737   -374       C  
ATOM     91  N   GLN A 159      21.126 -20.507   7.396  1.00-1.006           N  
ANISOU   91  N   GLN A 159    10151   6552   6370   1792   1531   -444       N  
ATOM     92  CA  GLN A 159      20.787 -21.748   6.702  1.00-1.006           C  
ANISOU   92  CA  GLN A 159    10524   6553   6472   1891   1589   -502       C  
ATOM     93  C   GLN A 159      20.498 -21.530   5.201  1.00-1.006           C  
ANISOU   93  C   GLN A 159    11510   7445   7301   1823   1670   -562       C  
ATOM     94  O   GLN A 159      19.988 -20.482   4.807  1.00-1.006           O  
ANISOU   94  O   GLN A 159    11297   7320   7116   1653   1647   -557       O  
ATOM     95  CB  GLN A 159      19.632 -22.487   7.399  1.00-1.006           C  
ANISOU   95  CB  GLN A 159    10829   6480   6587   1847   1506   -503       C  
ATOM     96  CG  GLN A 159      20.003 -23.071   8.764  1.00-1.006           C  
ANISOU   96  CG  GLN A 159    11053   6709   6889   1963   1447   -450       C  
ATOM     97  CD  GLN A 159      18.935 -23.957   9.354  1.00-1.006           C  
ANISOU   97  CD  GLN A 159    11796   7045   7412   1929   1386   -451       C  
ATOM     98  OE1 GLN A 159      17.739 -23.823   9.080  1.00-1.006           O  
ANISOU   98  OE1 GLN A 159    11582   6626   7059   1766   1353   -475       O  
ATOM     99  NE2 GLN A 159      19.342 -24.875  10.204  1.00-1.006           N  
ANISOU   99  NE2 GLN A 159    10517   5654   6102   2080   1369   -418       N  
ATOM    100  N   VAL A 160      20.868 -22.521   4.369  1.00-0.237           N  
ANISOU  100  N   VAL A 160    11700   7452   7314   1967   1768   -618       N  
ATOM    101  CA  VAL A 160      20.650 -22.513   2.911  1.00-0.237           C  
ANISOU  101  CA  VAL A 160    11915   7534   7330   1927   1853   -684       C  
ATOM    102  C   VAL A 160      19.882 -23.796   2.564  1.00-0.237           C  
ANISOU  102  C   VAL A 160    12747   7873   7823   1967   1857   -750       C  
ATOM    103  O   VAL A 160      20.215 -24.859   3.086  1.00-0.237           O  
ANISOU  103  O   VAL A 160    12718   7673   7730   2128   1870   -754       O  
ATOM    104  CB  VAL A 160      21.968 -22.316   2.095  1.00-0.237           C  
ANISOU  104  CB  VAL A 160    12293   8204   7817   2049   1987   -695       C  
ATOM    105  CG1 VAL A 160      21.764 -22.596   0.609  1.00-0.237           C  
ANISOU  105  CG1 VAL A 160    12501   8206   7758   2040   2085   -771       C  
ATOM    106  CG2 VAL A 160      22.527 -20.906   2.281  1.00-0.237           C  
ANISOU  106  CG2 VAL A 160    11989   8360   7818   1948   1977   -634       C  
ATOM    107  N   TYR A 161      18.817 -23.680   1.747  1.00 0.384           N  
ANISOU  107  N   TYR A 161    12669   7558   7524   1813   1836   -796       N  
ATOM    108  CA  TYR A 161      17.988 -24.830   1.374  1.00 0.384           C  
ANISOU  108  CA  TYR A 161    13043   7459   7564   1809   1828   -863       C  
ATOM    109  C   TYR A 161      18.587 -25.686   0.244  1.00 0.384           C  
ANISOU  109  C   TYR A 161    13940   8155   8223   1956   1956   -945       C  
ATOM    110  O   TYR A 161      19.147 -25.147  -0.717  1.00 0.384           O  
ANISOU  110  O   TYR A 161    13757   8159   8059   1970   2043   -965       O  
ATOM    111  CB  TYR A 161      16.564 -24.383   0.994  1.00 0.384           C  
ANISOU  111  CB  TYR A 161    13265   7532   7651   1578   1742   -879       C  
ATOM    112  CG  TYR A 161      15.609 -25.524   0.695  1.00 0.384           C  
ANISOU  112  CG  TYR A 161    13708   7504   7761   1533   1715   -946       C  
ATOM    113  CD1 TYR A 161      15.065 -26.291   1.721  1.00 0.384           C  
ANISOU  113  CD1 TYR A 161    13991   7556   7995   1528   1646   -927       C  
ATOM    114  CD2 TYR A 161      15.239 -25.826  -0.614  1.00 0.384           C  
ANISOU  114  CD2 TYR A 161    13968   7540   7739   1485   1759  -1027       C  
ATOM    115  CE1 TYR A 161      14.162 -27.319   1.455  1.00 0.384           C  
ANISOU  115  CE1 TYR A 161    14307   7433   8002   1461   1620   -987       C  
ATOM    116  CE2 TYR A 161      14.341 -26.855  -0.893  1.00 0.384           C  
ANISOU  116  CE2 TYR A 161    14341   7476   7797   1420   1726  -1093       C  
ATOM    117  CZ  TYR A 161      13.791 -27.589   0.147  1.00 0.384           C  
ANISOU  117  CZ  TYR A 161    15575   8489   8999   1401   1657  -1071       C  
ATOM    118  OH  TYR A 161      12.916 -28.617  -0.118  1.00 0.384           O  
ANISOU  118  OH  TYR A 161    16267   8742   9375   1320   1626  -1135       O  
ATOM    119  N   SER A 162      18.396 -27.019   0.369  1.00-0.284           N  
ANISOU  119  N   SER A 162    13929   7734   7964   2054   1968   -991       N  
ATOM    120  CA  SER A 162      18.774 -28.076  -0.568  1.00-0.284           C  
ANISOU  120  CA  SER A 162    14315   7803   8052   2198   2080  -1079       C  
ATOM    121  C   SER A 162      17.534 -28.963  -0.811  1.00-0.284           C  
ANISOU  121  C   SER A 162    15323   8288   8696   2078   2024  -1146       C  
ATOM    122  O   SER A 162      16.915 -29.449   0.150  1.00-0.284           O  
ANISOU  122  O   SER A 162    15379   8145   8725   2033   1937  -1117       O  
ATOM    123  CB  SER A 162      19.925 -28.910  -0.009  1.00-0.284           C  
ANISOU  123  CB  SER A 162    14867   8357   8666   2470   2155  -1063       C  
ATOM    124  N   SER A 163      17.163 -29.128  -2.101  1.00 1.658           N  
ANISOU  124  N   SER A 163    15064   7820   8156   2012   2071  -1234       N  
ATOM    125  CA  SER A 163      16.002 -29.888  -2.588  1.00 1.658           C  
ANISOU  125  CA  SER A 163    19252  11535  11976   1871   2020  -1311       C  
ATOM    126  C   SER A 163      15.952 -31.334  -2.103  1.00 1.658           C  
ANISOU  126  C   SER A 163    22125  13931  14598   1982   2035  -1350       C  
ATOM    127  O   SER A 163      14.866 -31.898  -1.984  1.00 1.658           O  
ANISOU  127  O   SER A 163    16903   8359   9160   1830   1954  -1379       O  
ATOM    128  CB  SER A 163      15.941 -29.848  -4.113  1.00 1.658           C  
ANISOU  128  CB  SER A 163    19812  11987  12275   1828   2090  -1401       C  
ATOM    129  N   SER A 167      16.889 -31.103   3.087  1.00 0.590           N  
ANISOU  129  N   SER A 167    14656   7034   8039   2169   1807   -997       N  
ATOM    130  CA  SER A 167      16.360 -30.184   4.093  1.00 0.590           C  
ANISOU  130  CA  SER A 167    14392   7081   8065   2049   1700   -906       C  
ATOM    131  C   SER A 167      17.101 -28.823   4.036  1.00 0.590           C  
ANISOU  131  C   SER A 167    14471   7719   8491   2060   1715   -861       C  
ATOM    132  O   SER A 167      17.507 -28.394   2.947  1.00 0.590           O  
ANISOU  132  O   SER A 167    14558   7935   8567   2072   1790   -908       O  
ATOM    133  CB  SER A 167      16.455 -30.824   5.478  1.00 0.590           C  
ANISOU  133  CB  SER A 167    14847   7422   8554   2168   1664   -838       C  
ATOM    134  N   TRP A 168      17.233 -28.131   5.195  1.00-0.728           N  
ANISOU  134  N   TRP A 168    13477   7039   7786   2039   1643   -773       N  
ATOM    135  CA  TRP A 168      17.973 -26.871   5.354  1.00-0.728           C  
ANISOU  135  CA  TRP A 168    12937   7016   7581   2042   1646   -724       C  
ATOM    136  C   TRP A 168      19.240 -27.213   6.144  1.00-0.728           C  
ANISOU  136  C   TRP A 168    13415   7684   8234   2268   1674   -672       C  
ATOM    137  O   TRP A 168      19.164 -27.917   7.159  1.00-0.728           O  
ANISOU  137  O   TRP A 168    13488   7590   8269   2341   1626   -633       O  
ATOM    138  CB  TRP A 168      17.172 -25.824   6.157  1.00-0.728           C  
ANISOU  138  CB  TRP A 168    12411   6694   7239   1845   1534   -664       C  
ATOM    139  CG  TRP A 168      15.955 -25.265   5.483  1.00-0.728           C  
ANISOU  139  CG  TRP A 168    12383   6577   7106   1626   1494   -696       C  
ATOM    140  CD1 TRP A 168      14.684 -25.754   5.564  1.00-0.728           C  
ANISOU  140  CD1 TRP A 168    12895   6771   7420   1492   1433   -716       C  
ATOM    141  CD2 TRP A 168      15.862 -24.023   4.774  1.00-0.728           C  
ANISOU  141  CD2 TRP A 168    12131   6595   6970   1507   1498   -697       C  
ATOM    142  NE1 TRP A 168      13.809 -24.908   4.925  1.00-0.728           N  
ANISOU  142  NE1 TRP A 168    12711   6663   7233   1309   1397   -730       N  
ATOM    143  CE2 TRP A 168      14.509 -23.852   4.404  1.00-0.728           C  
ANISOU  143  CE2 TRP A 168    12653   6942   7350   1321   1437   -719       C  
ATOM    144  CE3 TRP A 168      16.793 -23.042   4.400  1.00-0.728           C  
ANISOU  144  CE3 TRP A 168    12033   6868   7079   1538   1548   -677       C  
ATOM    145  CZ2 TRP A 168      14.073 -22.768   3.644  1.00-0.728           C  
ANISOU  145  CZ2 TRP A 168    12418   6872   7155   1185   1424   -722       C  
ATOM    146  CZ3 TRP A 168      16.359 -21.964   3.649  1.00-0.728           C  
ANISOU  146  CZ3 TRP A 168    12150   7123   7222   1390   1542   -680       C  
ATOM    147  CH2 TRP A 168      15.015 -21.839   3.269  1.00-0.728           C  
ANISOU  147  CH2 TRP A 168    12335   7112   7249   1226   1479   -702       C  
ATOM    148  N   HIS A 169      20.395 -26.714   5.691  1.00 0.338           N  
ANISOU  148  N   HIS A 169    12733   7362   7743   2377   1751   -668       N  
ATOM    149  CA  HIS A 169      21.664 -26.991   6.359  1.00 0.338           C  
ANISOU  149  CA  HIS A 169    12503   7380   7710   2598   1779   -618       C  
ATOM    150  C   HIS A 169      22.380 -25.702   6.789  1.00 0.338           C  
ANISOU  150  C   HIS A 169    12115   7549   7693   2548   1750   -556       C  
ATOM    151  O   HIS A 169      22.289 -24.694   6.080  1.00 0.338           O  
ANISOU  151  O   HIS A 169    11791   7430   7451   2408   1772   -572       O  
ATOM    152  CB  HIS A 169      22.562 -27.858   5.463  1.00 0.338           C  
ANISOU  152  CB  HIS A 169    12799   7577   7880   2826   1915   -672       C  
ATOM    153  CG  HIS A 169      21.858 -29.059   4.910  1.00 0.338           C  
ANISOU  153  CG  HIS A 169    13690   7890   8372   2853   1950   -746       C  
ATOM    154  ND1 HIS A 169      21.573 -30.159   5.700  1.00 0.338           N  
ANISOU  154  ND1 HIS A 169    14168   7998   8675   2951   1913   -730       N  
ATOM    155  CD2 HIS A 169      21.369 -29.275   3.666  1.00 0.338           C  
ANISOU  155  CD2 HIS A 169    14202   8135   8621   2777   2012   -834       C  
ATOM    156  CE1 HIS A 169      20.939 -31.010   4.912  1.00 0.338           C  
ANISOU  156  CE1 HIS A 169    14429   7774   8577   2927   1956   -812       C  
ATOM    157  NE2 HIS A 169      20.791 -30.520   3.679  1.00 0.338           N  
ANISOU  157  NE2 HIS A 169    14483   7876   8565   2823   2012   -879       N  
ATOM    158  N   PRO A 170      23.097 -25.704   7.941  1.00-0.219           N  
ANISOU  158  N   PRO A 170    11303   6980   7096   2656   1697   -485       N  
ATOM    159  CA  PRO A 170      23.809 -24.482   8.352  1.00-0.219           C  
ANISOU  159  CA  PRO A 170    10955   7159   7093   2593   1665   -431       C  
ATOM    160  C   PRO A 170      25.070 -24.208   7.528  1.00-0.219           C  
ANISOU  160  C   PRO A 170    11401   7972   7713   2710   1780   -442       C  
ATOM    161  O   PRO A 170      25.683 -25.138   7.025  1.00-0.219           O  
ANISOU  161  O   PRO A 170    11465   7943   7687   2919   1875   -471       O  
ATOM    162  CB  PRO A 170      24.108 -24.718   9.832  1.00-0.219           C  
ANISOU  162  CB  PRO A 170    11041   7340   7306   2672   1565   -357       C  
ATOM    163  CG  PRO A 170      24.141 -26.185   9.988  1.00-0.219           C  
ANISOU  163  CG  PRO A 170    11815   7743   7859   2874   1591   -365       C  
ATOM    164  CD  PRO A 170      23.310 -26.806   8.904  1.00-0.219           C  
ANISOU  164  CD  PRO A 170    11530   7009   7250   2834   1662   -448       C  
ATOM    165  N   VAL A 171      25.452 -22.931   7.399  1.00-0.888           N  
ANISOU  165  N   VAL A 171    10918   7898   7473   2575   1776   -419       N  
ATOM    166  CA  VAL A 171      26.620 -22.486   6.628  1.00-0.888           C  
ANISOU  166  CA  VAL A 171    10758   8139   7508   2641   1885   -421       C  
ATOM    167  C   VAL A 171      27.900 -22.536   7.480  1.00-0.888           C  
ANISOU  167  C   VAL A 171    11438   9251   8492   2799   1867   -357       C  
ATOM    168  O   VAL A 171      27.907 -22.019   8.597  1.00-0.888           O  
ANISOU  168  O   VAL A 171    11185   9176   8405   2721   1749   -301       O  
ATOM    169  CB  VAL A 171      26.368 -21.074   6.012  1.00-0.888           C  
ANISOU  169  CB  VAL A 171    11017   8599   7856   2401   1893   -425       C  
ATOM    170  CG1 VAL A 171      27.584 -20.554   5.244  1.00-0.888           C  
ANISOU  170  CG1 VAL A 171    10734   8750   7781   2445   2010   -420       C  
ATOM    171  CG2 VAL A 171      25.130 -21.075   5.116  1.00-0.888           C  
ANISOU  171  CG2 VAL A 171    11211   8387   7748   2265   1907   -484       C  
ATOM    172  N   CYS A 172      28.981 -23.134   6.936  1.00-1.296           N  
ANISOU  172  N   CYS A 172    11406   9399   8532   3021   1983   -367       N  
ATOM    173  CA  CYS A 172      30.298 -23.226   7.578  1.00-1.296           C  
ANISOU  173  CA  CYS A 172    11438   9894   8871   3195   1981   -306       C  
ATOM    174  C   CYS A 172      30.894 -21.842   7.790  1.00-1.296           C  
ANISOU  174  C   CYS A 172    11270  10266   9038   3018   1946   -262       C  
ATOM    175  O   CYS A 172      30.735 -20.965   6.935  1.00-1.296           O  
ANISOU  175  O   CYS A 172    11048  10124   8822   2844   2005   -289       O  
ATOM    176  CB  CYS A 172      31.249 -24.086   6.747  1.00-1.296           C  
ANISOU  176  CB  CYS A 172    11770  10307   9198   3461   2136   -333       C  
ATOM    177  SG  CYS A 172      31.036 -25.871   6.946  1.00-1.296           S  
ANISOU  177  SG  CYS A 172    12759  10763   9872   3756   2159   -358       S  
ATOM    178  N   GLN A 173      31.646 -21.669   8.892  1.00 0.197           N  
ANISOU  178  N   GLN A 173    10527   9895   8566   3068   1855   -194       N  
ATOM    179  CA  GLN A 173      32.351 -20.417   9.194  1.00 0.197           C  
ANISOU  179  CA  GLN A 173    10141  10047   8511   2907   1816   -150       C  
ATOM    180  C   GLN A 173      33.629 -20.330   8.324  1.00 0.197           C  
ANISOU  180  C   GLN A 173    10394  10762   8993   3018   1959   -149       C  
ATOM    181  O   GLN A 173      34.212 -19.252   8.189  1.00 0.197           O  
ANISOU  181  O   GLN A 173    10189  10990   9038   2860   1969   -125       O  
ATOM    182  CB  GLN A 173      32.652 -20.309  10.707  1.00 0.197           C  
ANISOU  182  CB  GLN A 173    10100  10222   8653   2914   1656    -82       C  
ATOM    183  CG  GLN A 173      33.311 -19.001  11.185  1.00 0.197           C  
ANISOU  183  CG  GLN A 173    10249  10895   9123   2721   1590    -40       C  
ATOM    184  CD  GLN A 173      32.511 -17.736  10.965  1.00 0.197           C  
ANISOU  184  CD  GLN A 173    12092  12632  10902   2408   1560    -62       C  
ATOM    185  OE1 GLN A 173      31.275 -17.724  10.945  1.00 0.197           O  
ANISOU  185  OE1 GLN A 173    11911  11990  10456   2307   1527    -94       O  
ATOM    186  NE2 GLN A 173      33.212 -16.627  10.814  1.00 0.197           N  
ANISOU  186  NE2 GLN A 173    10618  11594   9677   2248   1570    -43       N  
ATOM    187  N   ASP A 174      34.022 -21.460   7.701  1.00-0.612           N  
ANISOU  187  N   ASP A 174     9922  10174   8417   3283   2079   -176       N  
ATOM    188  CA  ASP A 174      35.176 -21.576   6.808  1.00-0.612           C  
ANISOU  188  CA  ASP A 174     9714  10354   8387   3432   2239   -182       C  
ATOM    189  C   ASP A 174      35.126 -20.517   5.694  1.00-0.612           C  
ANISOU  189  C   ASP A 174    10159  10932   8851   3210   2339   -212       C  
ATOM    190  O   ASP A 174      34.119 -20.412   4.983  1.00-0.612           O  
ANISOU  190  O   ASP A 174    10334  10676   8730   3086   2369   -268       O  
ATOM    191  CB  ASP A 174      35.224 -22.981   6.172  1.00-0.612           C  
ANISOU  191  CB  ASP A 174    10117  10414   8545   3728   2359   -229       C  
ATOM    192  CG  ASP A 174      35.385 -24.141   7.131  1.00-0.612           C  
ANISOU  192  CG  ASP A 174    11169  11301   9547   3986   2287   -196       C  
ATOM    193  OD1 ASP A 174      34.626 -24.207   8.121  1.00-0.612           O  
ANISOU  193  OD1 ASP A 174    11311  11194   9596   3901   2136   -171       O  
ATOM    194  OD2 ASP A 174      36.245 -25.000   6.873  1.00-0.612           O  
ANISOU  194  OD2 ASP A 174    11844  12073  10256   4279   2389   -196       O  
ATOM    195  N   ASP A 175      36.201 -19.701   5.602  1.00 0.199           N  
ANISOU  195  N   ASP A 175     9335  10716   8378   3148   2381   -170       N  
ATOM    196  CA  ASP A 175      36.437 -18.628   4.625  1.00 0.199           C  
ANISOU  196  CA  ASP A 175     9161  10780   8286   2943   2484   -180       C  
ATOM    197  C   ASP A 175      35.362 -17.510   4.610  1.00 0.199           C  
ANISOU  197  C   ASP A 175     9541  10902   8520   2615   2400   -190       C  
ATOM    198  O   ASP A 175      35.424 -16.611   3.759  1.00 0.199           O  
ANISOU  198  O   ASP A 175     9555  11031   8547   2436   2483   -197       O  
ATOM    199  CB  ASP A 175      36.647 -19.214   3.215  1.00 0.199           C  
ANISOU  199  CB  ASP A 175     9547  11052   8504   3091   2687   -236       C  
ATOM    200  CG  ASP A 175      37.647 -20.353   3.163  1.00 0.199           C  
ANISOU  200  CG  ASP A 175    11495  13211  10564   3438   2786   -232       C  
ATOM    201  OD1 ASP A 175      38.754 -20.202   3.733  1.00 0.199           O  
ANISOU  201  OD1 ASP A 175    11331  13622  10775   3513   2772   -170       O  
ATOM    202  OD2 ASP A 175      37.326 -21.395   2.548  1.00 0.199           O  
ANISOU  202  OD2 ASP A 175    12871  14178  11649   3635   2875   -290       O  
ATOM    203  N   TRP A 176      34.409 -17.551   5.563  1.00-1.099           N  
ANISOU  203  N   TRP A 176     8919   9942   7763   2542   2241   -186       N  
ATOM    204  CA  TRP A 176      33.342 -16.568   5.709  1.00-1.099           C  
ANISOU  204  CA  TRP A 176     8849   9616   7556   2263   2150   -193       C  
ATOM    205  C   TRP A 176      33.926 -15.274   6.294  1.00-1.099           C  
ANISOU  205  C   TRP A 176     9030  10243   8034   2050   2080   -140       C  
ATOM    206  O   TRP A 176      34.947 -15.310   6.989  1.00-1.099           O  
ANISOU  206  O   TRP A 176     8832  10490   8130   2122   2043    -95       O  
ATOM    207  CB  TRP A 176      32.212 -17.127   6.604  1.00-1.099           C  
ANISOU  207  CB  TRP A 176     8827   9126   7312   2280   2013   -203       C  
ATOM    208  CG  TRP A 176      30.941 -16.329   6.567  1.00-1.099           C  
ANISOU  208  CG  TRP A 176     9063   9018   7349   2037   1943   -221       C  
ATOM    209  CD1 TRP A 176      30.567 -15.349   7.437  1.00-1.099           C  
ANISOU  209  CD1 TRP A 176     9364   9369   7728   1836   1817   -190       C  
ATOM    210  CD2 TRP A 176      29.872 -16.452   5.617  1.00-1.099           C  
ANISOU  210  CD2 TRP A 176     9269   8781   7239   1980   1994   -275       C  
ATOM    211  NE1 TRP A 176      29.341 -14.839   7.079  1.00-1.099           N  
ANISOU  211  NE1 TRP A 176     9444   9075   7573   1669   1794   -217       N  
ATOM    212  CE2 TRP A 176      28.895 -15.492   5.959  1.00-1.099           C  
ANISOU  212  CE2 TRP A 176     9776   9115   7670   1748   1895   -266       C  
ATOM    213  CE3 TRP A 176      29.667 -17.245   4.475  1.00-1.099           C  
ANISOU  213  CE3 TRP A 176     9592   8843   7331   2098   2115   -330       C  
ATOM    214  CZ2 TRP A 176      27.715 -15.328   5.224  1.00-1.099           C  
ANISOU  214  CZ2 TRP A 176     9885   8829   7502   1641   1906   -305       C  
ATOM    215  CZ3 TRP A 176      28.493 -17.086   3.750  1.00-1.099           C  
ANISOU  215  CZ3 TRP A 176     9966   8812   7416   1976   2119   -373       C  
ATOM    216  CH2 TRP A 176      27.535 -16.135   4.124  1.00-1.099           C  
ANISOU  216  CH2 TRP A 176    10081   8794   7483   1753   2013   -357       C  
ATOM    217  N   ASN A 177      33.304 -14.134   5.961  1.00-0.282           N  
ANISOU  217  N   ASN A 177     8427   9523   7347   1788   2067   -145       N  
ATOM    218  CA  ASN A 177      33.687 -12.802   6.425  1.00-0.282           C  
ANISOU  218  CA  ASN A 177     8104   9518   7235   1546   2003   -103       C  
ATOM    219  C   ASN A 177      32.472 -11.879   6.415  1.00-0.282           C  
ANISOU  219  C   ASN A 177     8535   9568   7445   1311   1937   -117       C  
ATOM    220  O   ASN A 177      31.407 -12.285   5.945  1.00-0.282           O  
ANISOU  220  O   ASN A 177     8637   9216   7258   1338   1951   -156       O  
ATOM    221  CB  ASN A 177      34.864 -12.223   5.612  1.00-0.282           C  
ANISOU  221  CB  ASN A 177     7871   9774   7240   1491   2136    -81       C  
ATOM    222  CG  ASN A 177      34.666 -12.166   4.115  1.00-0.282           C  
ANISOU  222  CG  ASN A 177    10995  12741  10180   1477   2302   -114       C  
ATOM    223  OD1 ASN A 177      33.689 -11.615   3.598  1.00-0.282           O  
ANISOU  223  OD1 ASN A 177    10804  12180   9740   1326   2301   -135       O  
ATOM    224  ND2 ASN A 177      35.618 -12.711   3.380  1.00-0.282           N  
ANISOU  224  ND2 ASN A 177     9750  11793   9056   1638   2449   -116       N  
ATOM    225  N   GLU A 178      32.628 -10.643   6.935  1.00 1.334           N  
ANISOU  225  N   GLU A 178     7964   9178   7007   1081   1864    -85       N  
ATOM    226  CA  GLU A 178      31.559  -9.637   7.016  1.00 1.334           C  
ANISOU  226  CA  GLU A 178     8073   8960   6930    858   1798    -91       C  
ATOM    227  C   GLU A 178      30.939  -9.300   5.658  1.00 1.334           C  
ANISOU  227  C   GLU A 178     8428   9047   7057    786   1910   -114       C  
ATOM    228  O   GLU A 178      29.734  -9.050   5.599  1.00 1.334           O  
ANISOU  228  O   GLU A 178     8590   8801   6978    709   1860   -132       O  
ATOM    229  CB  GLU A 178      32.049  -8.363   7.720  1.00 1.334           C  
ANISOU  229  CB  GLU A 178     8129   9289   7174    631   1723    -55       C  
ATOM    230  CG  GLU A 178      32.058  -8.444   9.236  1.00 1.334           C  
ANISOU  230  CG  GLU A 178     9736  10960   8880    638   1562    -41       C  
ATOM    231  CD  GLU A 178      32.381  -7.127   9.912  1.00 1.334           C  
ANISOU  231  CD  GLU A 178    13338  14751  12608    390   1481    -17       C  
ATOM    232  OE1 GLU A 178      33.554  -6.693   9.844  1.00 1.334           O  
ANISOU  232  OE1 GLU A 178    12947  14818  12472    316   1515     10       O  
ATOM    233  OE2 GLU A 178      31.460  -6.526  10.510  1.00 1.334           O  
ANISOU  233  OE2 GLU A 178    13506  14607  12613    267   1386    -27       O  
ATOM    234  N   ASN A 179      31.752  -9.333   4.574  1.00-0.059           N  
ANISOU  234  N   ASN A 179     7655   8511   6355    820   2060   -112       N  
ATOM    235  CA  ASN A 179      31.316  -9.073   3.198  1.00-0.059           C  
ANISOU  235  CA  ASN A 179     7734   8376   6215    767   2180   -131       C  
ATOM    236  C   ASN A 179      30.354 -10.143   2.686  1.00-0.059           C  
ANISOU  236  C   ASN A 179     8174   8384   6365    928   2198   -183       C  
ATOM    237  O   ASN A 179      29.387  -9.801   2.005  1.00-0.059           O  
ANISOU  237  O   ASN A 179     8329   8195   6265    840   2207   -200       O  
ATOM    238  CB  ASN A 179      32.502  -8.863   2.251  1.00-0.059           C  
ANISOU  238  CB  ASN A 179     7815   8849   6454    765   2341   -113       C  
ATOM    239  N   TYR A 180      30.586 -11.427   3.035  1.00-0.102           N  
ANISOU  239  N   TYR A 180     7518   7729   5735   1158   2195   -206       N  
ATOM    240  CA  TYR A 180      29.650 -12.496   2.677  1.00-0.102           C  
ANISOU  240  CA  TYR A 180     7624   7394   5552   1299   2198   -259       C  
ATOM    241  C   TYR A 180      28.340 -12.317   3.492  1.00-0.102           C  
ANISOU  241  C   TYR A 180     7962   7365   5736   1203   2046   -262       C  
ATOM    242  O   TYR A 180      27.255 -12.473   2.936  1.00-0.102           O  
ANISOU  242  O   TYR A 180     8003   7022   5509   1173   2042   -295       O  
ATOM    243  CB  TYR A 180      30.269 -13.894   2.877  1.00-0.102           C  
ANISOU  243  CB  TYR A 180     7801   7641   5783   1570   2238   -279       C  
ATOM    244  CG  TYR A 180      31.352 -14.250   1.877  1.00-0.102           C  
ANISOU  244  CG  TYR A 180     8097   8208   6158   1702   2410   -291       C  
ATOM    245  CD1 TYR A 180      31.056 -14.417   0.527  1.00-0.102           C  
ANISOU  245  CD1 TYR A 180     8522   8410   6335   1720   2536   -336       C  
ATOM    246  CD2 TYR A 180      32.660 -14.479   2.290  1.00-0.102           C  
ANISOU  246  CD2 TYR A 180     8012   8604   6386   1823   2449   -257       C  
ATOM    247  CE1 TYR A 180      32.044 -14.758  -0.394  1.00-0.102           C  
ANISOU  247  CE1 TYR A 180     8786   8915   6654   1850   2706   -349       C  
ATOM    248  CE2 TYR A 180      33.657 -14.830   1.377  1.00-0.102           C  
ANISOU  248  CE2 TYR A 180     8042   8905   6500   1960   2618   -266       C  
ATOM    249  CZ  TYR A 180      33.343 -14.974   0.036  1.00-0.102           C  
ANISOU  249  CZ  TYR A 180     9484  10104   7680   1975   2752   -314       C  
ATOM    250  OH  TYR A 180      34.321 -15.327  -0.871  1.00-0.102           O  
ANISOU  250  OH  TYR A 180     9770  10651   8032   2116   2931   -327       O  
ATOM    251  N   GLY A 181      28.467 -11.915   4.767  1.00-0.514           N  
ANISOU  251  N   GLY A 181     7359   6908   5308   1143   1926   -226       N  
ATOM    252  CA  GLY A 181      27.349 -11.622   5.662  1.00-0.514           C  
ANISOU  252  CA  GLY A 181     7427   6692   5267   1046   1787   -223       C  
ATOM    253  C   GLY A 181      26.473 -10.475   5.178  1.00-0.514           C  
ANISOU  253  C   GLY A 181     7935   7001   5629    838   1775   -219       C  
ATOM    254  O   GLY A 181      25.242 -10.560   5.253  1.00-0.514           O  
ANISOU  254  O   GLY A 181     7773   6482   5262    806   1713   -236       O  
ATOM    255  N   ARG A 182      27.109  -9.395   4.648  1.00 0.293           N  
ANISOU  255  N   ARG A 182     7544   6846   5343    697   1837   -192       N  
ATOM    256  CA  ARG A 182      26.445  -8.225   4.047  1.00 0.293           C  
ANISOU  256  CA  ARG A 182     7639   6772   5298    506   1844   -179       C  
ATOM    257  C   ARG A 182      25.634  -8.662   2.824  1.00 0.293           C  
ANISOU  257  C   ARG A 182     8163   6983   5548    552   1912   -212       C  
ATOM    258  O   ARG A 182      24.479  -8.259   2.671  1.00 0.293           O  
ANISOU  258  O   ARG A 182     8206   6720   5398    470   1859   -215       O  
ATOM    259  CB  ARG A 182      27.480  -7.162   3.619  1.00 0.293           C  
ANISOU  259  CB  ARG A 182     7409   6873   5232    365   1920   -141       C  
ATOM    260  CG  ARG A 182      27.968  -6.320   4.785  1.00 0.293           C  
ANISOU  260  CG  ARG A 182     7706   7394   5737    236   1828   -108       C  
ATOM    261  CD  ARG A 182      28.942  -5.231   4.379  1.00 0.293           C  
ANISOU  261  CD  ARG A 182     7867   7861   6047     66   1899    -71       C  
ATOM    262  NE  ARG A 182      29.388  -4.502   5.567  1.00 0.293           N  
ANISOU  262  NE  ARG A 182     8439   8629   6803    -62   1797    -47       N  
ATOM    263  CZ  ARG A 182      30.480  -4.790   6.270  1.00 0.293           C  
ANISOU  263  CZ  ARG A 182    10107  10703   8745    -21   1773    -36       C  
ATOM    264  NH1 ARG A 182      31.304  -5.752   5.868  1.00 0.293           N  
ANISOU  264  NH1 ARG A 182     8094   8965   6873    153   1857    -40       N  
ATOM    265  NH2 ARG A 182      30.775  -4.094   7.363  1.00 0.293           N  
ANISOU  265  NH2 ARG A 182     8483   9218   7252   -153   1667    -19       N  
ATOM    266  N   ALA A 183      26.241  -9.509   1.977  1.00 1.185           N  
ANISOU  266  N   ALA A 183     7824   6728   5191    691   2027   -239       N  
ATOM    267  CA  ALA A 183      25.628 -10.069   0.769  1.00 1.185           C  
ANISOU  267  CA  ALA A 183     7925   6552   5022    751   2101   -280       C  
ATOM    268  C   ALA A 183      24.411 -10.948   1.136  1.00 1.185           C  
ANISOU  268  C   ALA A 183     8443   6691   5343    824   2008   -318       C  
ATOM    269  O   ALA A 183      23.356 -10.816   0.512  1.00 1.185           O  
ANISOU  269  O   ALA A 183     8407   6360   5074    763   1990   -335       O  
ATOM    270  CB  ALA A 183      26.654 -10.853  -0.018  1.00 1.185           C  
ANISOU  270  CB  ALA A 183     7946   6763   5082    903   2243   -304       C  
ATOM    271  N   ALA A 184      24.531 -11.770   2.206  1.00-0.353           N  
ANISOU  271  N   ALA A 184     8097   6363   5098    941   1941   -326       N  
ATOM    272  CA  ALA A 184      23.428 -12.604   2.704  1.00-0.353           C  
ANISOU  272  CA  ALA A 184     8263   6186   5097    997   1851   -355       C  
ATOM    273  C   ALA A 184      22.264 -11.726   3.197  1.00-0.353           C  
ANISOU  273  C   ALA A 184     8511   6257   5279    834   1740   -332       C  
ATOM    274  O   ALA A 184      21.112 -12.006   2.874  1.00-0.353           O  
ANISOU  274  O   ALA A 184     8568   6007   5125    812   1703   -356       O  
ATOM    275  CB  ALA A 184      23.912 -13.518   3.820  1.00-0.353           C  
ANISOU  275  CB  ALA A 184     8321   6326   5288   1143   1804   -353       C  
ATOM    276  N   CYS A 185      22.570 -10.641   3.925  1.00-1.293           N  
ANISOU  276  N   CYS A 185     7946   5890   4890    717   1690   -287       N  
ATOM    277  CA  CYS A 185      21.561  -9.698   4.423  1.00-1.293           C  
ANISOU  277  CA  CYS A 185     8006   5797   4895    572   1596   -264       C  
ATOM    278  C   CYS A 185      20.832  -8.968   3.289  1.00-1.293           C  
ANISOU  278  C   CYS A 185     8438   6058   5141    466   1630   -261       C  
ATOM    279  O   CYS A 185      19.610  -8.820   3.350  1.00-1.293           O  
ANISOU  279  O   CYS A 185     8450   5823   5009    419   1561   -263       O  
ATOM    280  CB  CYS A 185      22.157  -8.734   5.443  1.00-1.293           C  
ANISOU  280  CB  CYS A 185     7898   5924   4996    477   1542   -223       C  
ATOM    281  SG  CYS A 185      22.611  -9.524   7.005  1.00-1.293           S  
ANISOU  281  SG  CYS A 185     8351   6504   5617    585   1455   -220       S  
ATOM    282  N   ARG A 186      21.564  -8.561   2.239  1.00-0.234           N  
ANISOU  282  N   ARG A 186     8100   5858   4803    438   1736   -253       N  
ATOM    283  CA  ARG A 186      20.978  -7.935   1.050  1.00-0.234           C  
ANISOU  283  CA  ARG A 186     8245   5844   4751    352   1778   -246       C  
ATOM    284  C   ARG A 186      19.968  -8.885   0.390  1.00-0.234           C  
ANISOU  284  C   ARG A 186     8996   6302   5261    426   1767   -292       C  
ATOM    285  O   ARG A 186      18.876  -8.450   0.033  1.00-0.234           O  
ANISOU  285  O   ARG A 186     8917   6012   5018    353   1717   -283       O  
ATOM    286  CB  ARG A 186      22.059  -7.566   0.036  1.00-0.234           C  
ANISOU  286  CB  ARG A 186     8271   6079   4811    330   1910   -233       C  
ATOM    287  CG  ARG A 186      22.577  -6.156   0.171  1.00-0.234           C  
ANISOU  287  CG  ARG A 186     9645   7625   6305    172   1922   -177       C  
ATOM    288  CD  ARG A 186      23.486  -5.762  -1.001  1.00-0.234           C  
ANISOU  288  CD  ARG A 186    10928   9077   7578    132   2063   -159       C  
ATOM    289  NE  ARG A 186      24.769  -6.484  -1.036  1.00-0.234           N  
ANISOU  289  NE  ARG A 186    11243   9708   8079    239   2155   -176       N  
ATOM    290  CZ  ARG A 186      25.801  -6.249  -0.225  1.00-0.234           C  
ANISOU  290  CZ  ARG A 186    12417  11215   9530    217   2153   -153       C  
ATOM    291  NH1 ARG A 186      25.707  -5.333   0.734  1.00-0.234           N  
ANISOU  291  NH1 ARG A 186    11497  10331   8719     86   2059   -120       N  
ATOM    292  NH2 ARG A 186      26.924  -6.948  -0.347  1.00-0.234           N  
ANISOU  292  NH2 ARG A 186     9468   8566   6748    334   2241   -166       N  
ATOM    293  N   ASP A 187      20.323 -10.185   0.261  1.00-0.672           N  
ANISOU  293  N   ASP A 187     9030   6319   5270    572   1809   -340       N  
ATOM    294  CA  ASP A 187      19.444 -11.211  -0.323  1.00-0.672           C  
ANISOU  294  CA  ASP A 187     9401   6398   5402    639   1799   -393       C  
ATOM    295  C   ASP A 187      18.129 -11.344   0.465  1.00-0.672           C  
ANISOU  295  C   ASP A 187    10036   6813   5975    597   1669   -392       C  
ATOM    296  O   ASP A 187      17.072 -11.495  -0.147  1.00-0.672           O  
ANISOU  296  O   ASP A 187    10108   6657   5843    560   1636   -412       O  
ATOM    297  CB  ASP A 187      20.168 -12.561  -0.448  1.00-0.672           C  
ANISOU  297  CB  ASP A 187     9781   6788   5774    810   1869   -444       C  
ATOM    298  CG  ASP A 187      21.267 -12.625  -1.501  1.00-0.672           C  
ANISOU  298  CG  ASP A 187    11691   8863   7678    871   2015   -458       C  
ATOM    299  OD1 ASP A 187      21.423 -11.640  -2.267  1.00-0.672           O  
ANISOU  299  OD1 ASP A 187    11861   9116   7817    767   2067   -430       O  
ATOM    300  OD2 ASP A 187      21.975 -13.658  -1.557  1.00-0.672           O  
ANISOU  300  OD2 ASP A 187    12622   9835   8627   1027   2084   -495       O  
ATOM    301  N   MET A 188      18.186 -11.188   1.807  1.00-0.715           N  
ANISOU  301  N   MET A 188     9568   6433   5684    592   1594   -366       N  
ATOM    302  CA  MET A 188      17.018 -11.221   2.700  1.00-0.715           C  
ANISOU  302  CA  MET A 188     9634   6332   5722    550   1480   -357       C  
ATOM    303  C   MET A 188      16.196  -9.921   2.689  1.00-0.715           C  
ANISOU  303  C   MET A 188    10295   6958   6362    413   1425   -316       C  
ATOM    304  O   MET A 188      15.234  -9.807   3.447  1.00-0.715           O  
ANISOU  304  O   MET A 188    10555   7111   6616    377   1338   -303       O  
ATOM    305  CB  MET A 188      17.443 -11.549   4.140  1.00-0.715           C  
ANISOU  305  CB  MET A 188     9829   6632   6095    605   1428   -344       C  
ATOM    306  CG  MET A 188      17.913 -12.954   4.301  1.00-0.715           C  
ANISOU  306  CG  MET A 188    10327   7093   6581    754   1459   -379       C  
ATOM    307  SD  MET A 188      18.251 -13.335   6.016  1.00-0.715           S  
ANISOU  307  SD  MET A 188    10745   7598   7170    816   1380   -354       S  
ATOM    308  CE  MET A 188      19.711 -14.288   5.815  1.00-0.715           C  
ANISOU  308  CE  MET A 188    10230   7254   6745    993   1468   -371       C  
ATOM    309  N   GLY A 189      16.595  -8.950   1.864  1.00-1.110           N  
ANISOU  309  N   GLY A 189     9606   6356   5658    344   1483   -291       N  
ATOM    310  CA  GLY A 189      15.913  -7.668   1.727  1.00-1.110           C  
ANISOU  310  CA  GLY A 189     9416   6114   5425    227   1445   -246       C  
ATOM    311  C   GLY A 189      16.247  -6.626   2.771  1.00-1.110           C  
ANISOU  311  C   GLY A 189     9622   6444   5797    156   1408   -205       C  
ATOM    312  O   GLY A 189      15.500  -5.659   2.912  1.00-1.110           O  
ANISOU  312  O   GLY A 189     9779   6508   5909     76   1360   -171       O  
ATOM    313  N   TYR A 190      17.372  -6.781   3.501  1.00-0.414           N  
ANISOU  313  N   TYR A 190     8772   5804   5135    185   1428   -206       N  
ATOM    314  CA  TYR A 190      17.752  -5.809   4.529  1.00-0.414           C  
ANISOU  314  CA  TYR A 190     8637   5789   5149    105   1387   -174       C  
ATOM    315  C   TYR A 190      18.443  -4.575   3.973  1.00-0.414           C  
ANISOU  315  C   TYR A 190     9463   6726   6002     -9   1446   -137       C  
ATOM    316  O   TYR A 190      18.769  -3.670   4.743  1.00-0.414           O  
ANISOU  316  O   TYR A 190     9379   6719   6018    -96   1414   -113       O  
ATOM    317  CB  TYR A 190      18.569  -6.447   5.654  1.00-0.414           C  
ANISOU  317  CB  TYR A 190     8417   5750   5113    172   1361   -186       C  
ATOM    318  CG  TYR A 190      17.676  -7.072   6.700  1.00-0.414           C  
ANISOU  318  CG  TYR A 190     8495   5680   5165    223   1270   -199       C  
ATOM    319  CD1 TYR A 190      17.059  -6.290   7.676  1.00-0.414           C  
ANISOU  319  CD1 TYR A 190     8681   5800   5365    150   1193   -178       C  
ATOM    320  CD2 TYR A 190      17.400  -8.437   6.684  1.00-0.414           C  
ANISOU  320  CD2 TYR A 190     8495   5584   5108    341   1267   -231       C  
ATOM    321  CE1 TYR A 190      16.214  -6.857   8.626  1.00-0.414           C  
ANISOU  321  CE1 TYR A 190     8633   5624   5288    194   1119   -187       C  
ATOM    322  CE2 TYR A 190      16.566  -9.015   7.639  1.00-0.414           C  
ANISOU  322  CE2 TYR A 190     8613   5561   5194    375   1189   -237       C  
ATOM    323  CZ  TYR A 190      15.970  -8.219   8.603  1.00-0.414           C  
ANISOU  323  CZ  TYR A 190     8792   5704   5400    300   1117   -213       C  
ATOM    324  OH  TYR A 190      15.159  -8.779   9.557  1.00-0.414           O  
ANISOU  324  OH  TYR A 190     8292   5078   4868    331   1050   -216       O  
ATOM    325  N   LYS A 191      18.648  -4.535   2.641  1.00 0.724           N  
ANISOU  325  N   LYS A 191     9231   6486   5664    -15   1532   -134       N  
ATOM    326  CA  LYS A 191      19.260  -3.444   1.874  1.00 0.724           C  
ANISOU  326  CA  LYS A 191     9283   6614   5700   -124   1607    -95       C  
ATOM    327  C   LYS A 191      20.585  -2.929   2.490  1.00 0.724           C  
ANISOU  327  C   LYS A 191     9537   7155   6177   -192   1636    -78       C  
ATOM    328  O   LYS A 191      21.606  -3.601   2.376  1.00 0.724           O  
ANISOU  328  O   LYS A 191     9480   7334   6253   -129   1699    -94       O  
ATOM    329  CB  LYS A 191      18.241  -2.308   1.641  1.00 0.724           C  
ANISOU  329  CB  LYS A 191     9851   6951   6107   -220   1565    -56       C  
ATOM    330  N   ASN A 192      20.557  -1.773   3.158  1.00 0.352           N  
ANISOU  330  N   ASN A 192     8942   6538   5619   -317   1590    -46       N  
ATOM    331  CA  ASN A 192      21.735  -1.121   3.741  1.00 0.352           C  
ANISOU  331  CA  ASN A 192     8848   6699   5717   -418   1605    -28       C  
ATOM    332  C   ASN A 192      22.005  -1.497   5.210  1.00 0.352           C  
ANISOU  332  C   ASN A 192     9349   7328   6392   -385   1515    -49       C  
ATOM    333  O   ASN A 192      22.937  -0.966   5.825  1.00 0.352           O  
ANISOU  333  O   ASN A 192     9254   7451   6460   -476   1506    -38       O  
ATOM    334  CB  ASN A 192      21.616   0.413   3.567  1.00 0.352           C  
ANISOU  334  CB  ASN A 192     9455   7181   6233   -592   1612     17       C  
ATOM    335  CG  ASN A 192      20.371   1.025   4.190  1.00 0.352           C  
ANISOU  335  CG  ASN A 192    13402  10825  10041   -616   1517     24       C  
ATOM    336  OD1 ASN A 192      19.273   0.439   4.194  1.00 0.352           O  
ANISOU  336  OD1 ASN A 192    11623   8863   8156   -514   1468      7       O  
ATOM    337  ND2 ASN A 192      20.513   2.233   4.726  1.00 0.352           N  
ANISOU  337  ND2 ASN A 192    13280  10644   9913   -755   1493     48       N  
ATOM    338  N   ASN A 193      21.207  -2.425   5.764  1.00 0.334           N  
ANISOU  338  N   ASN A 193     8859   6708   5862   -262   1447    -79       N  
ATOM    339  CA  ASN A 193      21.345  -2.834   7.160  1.00 0.334           C  
ANISOU  339  CA  ASN A 193     8593   6527   5725   -221   1359    -95       C  
ATOM    340  C   ASN A 193      22.263  -4.034   7.325  1.00 0.334           C  
ANISOU  340  C   ASN A 193     8559   6744   5851    -91   1382   -114       C  
ATOM    341  O   ASN A 193      22.178  -4.998   6.568  1.00 0.334           O  
ANISOU  341  O   ASN A 193     8508   6660   5743     28   1437   -133       O  
ATOM    342  CB  ASN A 193      19.973  -3.093   7.792  1.00 0.334           C  
ANISOU  342  CB  ASN A 193     8557   6210   5557   -171   1273   -108       C  
ATOM    343  CG  ASN A 193      19.037  -1.915   7.679  1.00 0.334           C  
ANISOU  343  CG  ASN A 193    10193   7607   7042   -275   1250    -86       C  
ATOM    344  OD1 ASN A 193      19.153  -0.931   8.406  1.00 0.334           O  
ANISOU  344  OD1 ASN A 193     9282   6683   6153   -378   1211    -74       O  
ATOM    345  ND2 ASN A 193      18.090  -1.982   6.761  1.00 0.334           N  
ANISOU  345  ND2 ASN A 193     9186   6398   5868   -246   1271    -82       N  
ATOM    346  N   PHE A 194      23.159  -3.952   8.310  1.00 0.089           N  
ANISOU  346  N   PHE A 194     7838   6272   5322   -111   1339   -108       N  
ATOM    347  CA  PHE A 194      24.080  -5.020   8.711  1.00 0.089           C  
ANISOU  347  CA  PHE A 194     7654   6354   5313     22   1341   -118       C  
ATOM    348  C   PHE A 194      24.483  -4.809  10.172  1.00 0.089           C  
ANISOU  348  C   PHE A 194     8229   7076   6028    -13   1236   -111       C  
ATOM    349  O   PHE A 194      24.704  -3.674  10.582  1.00 0.089           O  
ANISOU  349  O   PHE A 194     8098   6999   5935   -174   1203    -97       O  
ATOM    350  CB  PHE A 194      25.306  -5.162   7.780  1.00 0.089           C  
ANISOU  350  CB  PHE A 194     7610   6620   5409     41   1455   -109       C  
ATOM    351  CG  PHE A 194      26.235  -6.273   8.219  1.00 0.089           C  
ANISOU  351  CG  PHE A 194     7531   6819   5514    203   1457   -115       C  
ATOM    352  CD1 PHE A 194      25.899  -7.609   8.008  1.00 0.089           C  
ANISOU  352  CD1 PHE A 194     7828   6982   5727    396   1476   -141       C  
ATOM    353  CD2 PHE A 194      27.426  -5.985   8.883  1.00 0.089           C  
ANISOU  353  CD2 PHE A 194     7522   7198   5756    162   1432    -94       C  
ATOM    354  CE1 PHE A 194      26.730  -8.640   8.467  1.00 0.089           C  
ANISOU  354  CE1 PHE A 194     7761   7142   5814    564   1475   -142       C  
ATOM    355  CE2 PHE A 194      28.270  -7.016   9.320  1.00 0.089           C  
ANISOU  355  CE2 PHE A 194     7691   7636   6100    331   1427    -92       C  
ATOM    356  CZ  PHE A 194      27.912  -8.337   9.115  1.00 0.089           C  
ANISOU  356  CZ  PHE A 194     7477   7261   5790    539   1450   -114       C  
ATOM    357  N   TYR A 195      24.567  -5.892  10.952  1.00-0.376           N  
ANISOU  357  N   TYR A 195     8005   6898   5860    133   1183   -120       N  
ATOM    358  CA  TYR A 195      24.949  -5.768  12.355  1.00-0.376           C  
ANISOU  358  CA  TYR A 195     8011   7044   5980    111   1077   -111       C  
ATOM    359  C   TYR A 195      26.191  -6.578  12.717  1.00-0.376           C  
ANISOU  359  C   TYR A 195     8458   7856   6646    230   1073    -99       C  
ATOM    360  O   TYR A 195      27.181  -5.994  13.153  1.00-0.376           O  
ANISOU  360  O   TYR A 195     8278   7994   6651    142   1045    -82       O  
ATOM    361  CB  TYR A 195      23.768  -6.088  13.297  1.00-0.376           C  
ANISOU  361  CB  TYR A 195     8316   7042   6128    150    987   -121       C  
ATOM    362  CG  TYR A 195      24.060  -5.849  14.764  1.00-0.376           C  
ANISOU  362  CG  TYR A 195     8616   7448   6504    113    875   -113       C  
ATOM    363  CD1 TYR A 195      24.579  -4.634  15.206  1.00-0.376           C  
ANISOU  363  CD1 TYR A 195     8812   7782   6771    -61    837   -108       C  
ATOM    364  CD2 TYR A 195      23.774  -6.821  15.719  1.00-0.376           C  
ANISOU  364  CD2 TYR A 195     8800   7564   6660    241    806   -112       C  
ATOM    365  CE1 TYR A 195      24.842  -4.407  16.556  1.00-0.376           C  
ANISOU  365  CE1 TYR A 195     8957   8013   6963   -102    729   -107       C  
ATOM    366  CE2 TYR A 195      24.020  -6.600  17.076  1.00-0.376           C  
ANISOU  366  CE2 TYR A 195     8847   7697   6750    207    700   -103       C  
ATOM    367  CZ  TYR A 195      24.557  -5.392  17.489  1.00-0.376           C  
ANISOU  367  CZ  TYR A 195     9798   8798   7773     35    660   -104       C  
ATOM    368  OH  TYR A 195      24.807  -5.163  18.822  1.00-0.376           O  
ANISOU  368  OH  TYR A 195    10059   9138   8058     -6    551   -101       O  
ATOM    369  N   SER A 196      26.141  -7.909  12.553  1.00 0.634           N  
ANISOU  369  N   SER A 196     8140   7493   6306    430   1098   -106       N  
ATOM    370  CA  SER A 196      27.239  -8.798  12.931  1.00 0.634           C  
ANISOU  370  CA  SER A 196     7956   7623   6311    584   1092    -91       C  
ATOM    371  C   SER A 196      27.185 -10.126  12.211  1.00 0.634           C  
ANISOU  371  C   SER A 196     8567   8134   6855    793   1171   -105       C  
ATOM    372  O   SER A 196      26.109 -10.579  11.817  1.00 0.634           O  
ANISOU  372  O   SER A 196     8680   7880   6749    830   1190   -129       O  
ATOM    373  CB  SER A 196      27.185  -9.074  14.434  1.00 0.634           C  
ANISOU  373  CB  SER A 196     8314   7987   6693    621    960    -76       C  
ATOM    374  OG  SER A 196      26.037  -9.847  14.749  1.00 0.634           O  
ANISOU  374  OG  SER A 196     9428   8721   7597    715    930    -88       O  
ATOM    375  N   SER A 197      28.352 -10.778  12.122  1.00 0.182           N  
ANISOU  375  N   SER A 197     8166   8064   6643    934   1211    -90       N  
ATOM    376  CA  SER A 197      28.564 -12.103  11.544  1.00 0.182           C  
ANISOU  376  CA  SER A 197     8289   8137   6725   1162   1290   -103       C  
ATOM    377  C   SER A 197      29.662 -12.758  12.383  1.00 0.182           C  
ANISOU  377  C   SER A 197     8958   9148   7610   1319   1243    -69       C  
ATOM    378  O   SER A 197      30.757 -12.197  12.505  1.00 0.182           O  
ANISOU  378  O   SER A 197     8878   9510   7784   1269   1244    -43       O  
ATOM    379  CB  SER A 197      28.982 -11.997  10.078  1.00 0.182           C  
ANISOU  379  CB  SER A 197     8597   8539   7042   1165   1438   -122       C  
ATOM    380  OG  SER A 197      28.884 -13.242   9.405  1.00 0.182           O  
ANISOU  380  OG  SER A 197     9689   9455   8008   1370   1521   -149       O  
ATOM    381  N   GLN A 198      29.352 -13.901  13.013  1.00-0.361           N  
ANISOU  381  N   GLN A 198     8686   8678   7238   1498   1194    -64       N  
ATOM    382  CA  GLN A 198      30.298 -14.626  13.877  1.00-0.361           C  
ANISOU  382  CA  GLN A 198     8629   8900   7354   1675   1138    -24       C  
ATOM    383  C   GLN A 198      30.059 -16.138  13.902  1.00-0.361           C  
ANISOU  383  C   GLN A 198     9433   9432   8002   1928   1161    -27       C  
ATOM    384  O   GLN A 198      28.936 -16.589  13.681  1.00-0.361           O  
ANISOU  384  O   GLN A 198     9485   9026   7789   1929   1173    -58       O  
ATOM    385  CB  GLN A 198      30.307 -14.042  15.309  1.00-0.361           C  
ANISOU  385  CB  GLN A 198     8762   9148   7564   1567    982     10       C  
ATOM    386  CG  GLN A 198      28.964 -14.111  16.034  1.00-0.361           C  
ANISOU  386  CG  GLN A 198    11275  11205   9820   1508    899     -1       C  
ATOM    387  CD  GLN A 198      29.009 -13.378  17.346  1.00-0.361           C  
ANISOU  387  CD  GLN A 198    14031  14082  12639   1382    760     25       C  
ATOM    388  OE1 GLN A 198      29.402 -13.933  18.378  1.00-0.361           O  
ANISOU  388  OE1 GLN A 198    13671  13841  12336   1494    670     62       O  
ATOM    389  NE2 GLN A 198      28.605 -12.113  17.331  1.00-0.361           N  
ANISOU  389  NE2 GLN A 198    12643  12651  11224   1150    739      6       N  
ATOM    390  N   GLY A 199      31.112 -16.894  14.204  1.00 0.117           N  
ANISOU  390  N   GLY A 199     9186   9471   7921   2137   1163      7       N  
ATOM    391  CA  GLY A 199      31.062 -18.349  14.269  1.00 0.117           C  
ANISOU  391  CA  GLY A 199     9423   9469   8019   2401   1188     12       C  
ATOM    392  C   GLY A 199      30.559 -18.908  15.583  1.00 0.117           C  
ANISOU  392  C   GLY A 199    10319  10133   8793   2458   1058     47       C  
ATOM    393  O   GLY A 199      31.263 -18.827  16.592  1.00 0.117           O  
ANISOU  393  O   GLY A 199    10250  10367   8898   2498    957     99       O  
ATOM    394  N   ILE A 200      29.349 -19.507  15.576  1.00 0.243           N  
ANISOU  394  N   ILE A 200    10279   9560   8447   2460   1059     20       N  
ATOM    395  CA  ILE A 200      28.736 -20.140  16.754  1.00 0.243           C  
ANISOU  395  CA  ILE A 200    10514   9505   8518   2512    952     53       C  
ATOM    396  C   ILE A 200      29.012 -21.657  16.770  1.00 0.243           C  
ANISOU  396  C   ILE A 200    11430  10220   9313   2797    989     72       C  
ATOM    397  O   ILE A 200      28.964 -22.297  15.718  1.00 0.243           O  
ANISOU  397  O   ILE A 200    11347   9950   9117   2901   1107     30       O  
ATOM    398  CB  ILE A 200      27.223 -19.831  16.832  1.00 0.243           C  
ANISOU  398  CB  ILE A 200    11110   9662   8865   2323    926     20       C  
ATOM    399  N   VAL A 201      29.313 -22.224  17.958  1.00 0.341           N  
ANISOU  399  N   VAL A 201    11451  10265   9342   2925    889    135       N  
ATOM    400  CA  VAL A 201      29.601 -23.660  18.118  1.00 0.341           C  
ANISOU  400  CA  VAL A 201    11776  10380   9539   3207    911    165       C  
ATOM    401  C   VAL A 201      28.283 -24.413  18.428  1.00 0.341           C  
ANISOU  401  C   VAL A 201    12891  10876  10295   3182    895    155       C  
ATOM    402  O   VAL A 201      27.992 -24.752  19.583  1.00 0.341           O  
ANISOU  402  O   VAL A 201    12918  10760  10226   3206    794    208       O  
ATOM    403  CB  VAL A 201      30.778 -23.963  19.110  1.00 0.341           C  
ANISOU  403  CB  VAL A 201    12141  11130  10110   3396    822    247       C  
ATOM    404  CG1 VAL A 201      31.062 -25.464  19.205  1.00 0.341           C  
ANISOU  404  CG1 VAL A 201    12252  10999  10074   3712    859    281       C  
ATOM    405  CG2 VAL A 201      32.052 -23.219  18.700  1.00 0.341           C  
ANISOU  405  CG2 VAL A 201    11790  11421  10131   3392    843    255       C  
ATOM    406  N   ASP A 202      27.479 -24.636  17.367  1.00 0.872           N  
ANISOU  406  N   ASP A 202    12756  10386   9960   3120    994     85       N  
ATOM    407  CA  ASP A 202      26.178 -25.307  17.424  1.00 0.872           C  
ANISOU  407  CA  ASP A 202    16263  13318  13134   3065    995     63       C  
ATOM    408  C   ASP A 202      26.190 -26.575  16.574  1.00 0.872           C  
ANISOU  408  C   ASP A 202    19046  15742  15698   3259   1103     28       C  
ATOM    409  O   ASP A 202      26.750 -26.580  15.479  1.00 0.872           O  
ANISOU  409  O   ASP A 202    13929  10749  10644   3331   1210    -18       O  
ATOM    410  CB  ASP A 202      25.070 -24.350  16.946  1.00 0.872           C  
ANISOU  410  CB  ASP A 202    16530  13471  13341   2785   1001      9       C  
ATOM    411  CG  ASP A 202      23.666 -24.780  17.318  1.00 0.872           C  
ANISOU  411  CG  ASP A 202    17916  14370  14444   2676    966      2       C  
ATOM    412  OD1 ASP A 202      23.095 -25.624  16.597  1.00 0.872           O  
ANISOU  412  OD1 ASP A 202    18150  14211  14442   2716   1036    -40       O  
ATOM    413  OD2 ASP A 202      23.130 -24.257  18.321  1.00 0.872           O  
ANISOU  413  OD2 ASP A 202    18644  15113  15182   2544    872     36       O  
ATOM    414  N   SER A 208      25.062 -32.308   8.158  1.00 0.456           N  
ANISOU  414  N   SER A 208    13735   7882   8579   3852   1970   -540       N  
ATOM    415  CA  SER A 208      25.540 -31.769   6.890  1.00 0.456           C  
ANISOU  415  CA  SER A 208    13590   7981   8508   3848   2083   -604       C  
ATOM    416  C   SER A 208      25.550 -30.244   6.911  1.00 0.456           C  
ANISOU  416  C   SER A 208    13713   8631   8960   3633   2032   -574       C  
ATOM    417  O   SER A 208      24.677 -29.626   7.534  1.00 0.456           O  
ANISOU  417  O   SER A 208    13678   8594   8967   3410   1916   -543       O  
ATOM    418  CB  SER A 208      24.697 -32.283   5.726  1.00 0.456           C  
ANISOU  418  CB  SER A 208    14337   8232   8874   3756   2153   -713       C  
ATOM    419  N   PHE A 209      26.538 -29.637   6.222  1.00-0.260           N  
ANISOU  419  N   PHE A 209    12879   8239   8351   3701   2124   -582       N  
ATOM    420  CA  PHE A 209      26.709 -28.184   6.175  1.00-0.260           C  
ANISOU  420  CA  PHE A 209    12497   8363   8279   3510   2091   -552       C  
ATOM    421  C   PHE A 209      26.927 -27.665   4.755  1.00-0.260           C  
ANISOU  421  C   PHE A 209    12999   8997   8765   3455   2215   -616       C  
ATOM    422  O   PHE A 209      27.283 -28.432   3.861  1.00-0.260           O  
ANISOU  422  O   PHE A 209    13094   8918   8683   3625   2343   -676       O  
ATOM    423  CB  PHE A 209      27.898 -27.750   7.052  1.00-0.260           C  
ANISOU  423  CB  PHE A 209    12338   8758   8509   3627   2056   -464       C  
ATOM    424  CG  PHE A 209      28.034 -28.431   8.390  1.00-0.260           C  
ANISOU  424  CG  PHE A 209    12480   8820   8673   3765   1957   -394       C  
ATOM    425  CD1 PHE A 209      27.328 -27.976   9.494  1.00-0.260           C  
ANISOU  425  CD1 PHE A 209    12799   9112   9035   3592   1810   -343       C  
ATOM    426  CD2 PHE A 209      28.893 -29.511   8.553  1.00-0.260           C  
ANISOU  426  CD2 PHE A 209    12810   9105   8976   4076   2015   -376       C  
ATOM    427  CE1 PHE A 209      27.459 -28.604  10.736  1.00-0.260           C  
ANISOU  427  CE1 PHE A 209    12973   9205   9209   3717   1720   -274       C  
ATOM    428  CE2 PHE A 209      29.025 -30.140   9.795  1.00-0.260           C  
ANISOU  428  CE2 PHE A 209    13201   9410   9371   4210   1919   -303       C  
ATOM    429  CZ  PHE A 209      28.309 -29.679  10.880  1.00-0.260           C  
ANISOU  429  CZ  PHE A 209    12936   9116   9138   4024   1772   -251       C  
ATOM    430  N   MET A 210      26.724 -26.349   4.558  1.00 0.413           N  
ANISOU  430  N   MET A 210    12380   8673   8318   3222   2180   -602       N  
ATOM    431  CA  MET A 210      26.966 -25.676   3.286  1.00 0.413           C  
ANISOU  431  CA  MET A 210    12267   8737   8216   3147   2290   -646       C  
ATOM    432  C   MET A 210      28.298 -24.944   3.424  1.00 0.413           C  
ANISOU  432  C   MET A 210    12358   9447   8695   3215   2336   -589       C  
ATOM    433  O   MET A 210      28.440 -24.076   4.288  1.00 0.413           O  
ANISOU  433  O   MET A 210    12066   9483   8671   3100   2237   -522       O  
ATOM    434  CB  MET A 210      25.821 -24.708   2.924  1.00 0.413           C  
ANISOU  434  CB  MET A 210    12642   9012   8508   2848   2224   -662       C  
ATOM    435  CG  MET A 210      24.494 -25.399   2.639  1.00 0.413           C  
ANISOU  435  CG  MET A 210    13467   9266   8958   2764   2184   -723       C  
ATOM    436  SD  MET A 210      24.522 -26.519   1.216  1.00 0.413           S  
ANISOU  436  SD  MET A 210    14313   9711   9424   2902   2334   -832       S  
ATOM    437  CE  MET A 210      24.365 -25.346  -0.133  1.00 0.413           C  
ANISOU  437  CE  MET A 210    13814   9397   8914   2706   2394   -863       C  
ATOM    438  N   LYS A 211      29.291 -25.342   2.623  1.00-0.181           N  
ANISOU  438  N   LYS A 211    11845   9095   8209   3408   2487   -616       N  
ATOM    439  CA  LYS A 211      30.632 -24.766   2.676  1.00-0.181           C  
ANISOU  439  CA  LYS A 211    11499   9364   8238   3490   2549   -564       C  
ATOM    440  C   LYS A 211      30.884 -23.816   1.505  1.00-0.181           C  
ANISOU  440  C   LYS A 211    12046  10156   8837   3350   2658   -588       C  
ATOM    441  O   LYS A 211      30.398 -24.061   0.401  1.00-0.181           O  
ANISOU  441  O   LYS A 211    12163   9956   8662   3325   2746   -661       O  
ATOM    442  CB  LYS A 211      31.679 -25.892   2.696  1.00-0.181           C  
ANISOU  442  CB  LYS A 211    11671   9605   8443   3832   2649   -565       C  
ATOM    443  CG  LYS A 211      32.971 -25.532   3.409  1.00-0.181           C  
ANISOU  443  CG  LYS A 211    12595  11163   9801   3947   2640   -482       C  
ATOM    444  CD  LYS A 211      33.986 -26.661   3.295  1.00-0.181           C  
ANISOU  444  CD  LYS A 211    13972  12628  11205   4304   2764   -486       C  
ATOM    445  CE  LYS A 211      35.316 -26.326   3.927  1.00-0.181           C  
ANISOU  445  CE  LYS A 211    14959  14292  12642   4430   2756   -401       C  
ATOM    446  NZ  LYS A 211      36.071 -25.302   3.157  1.00-0.181           N  
ANISOU  446  NZ  LYS A 211    15784  15672  13751   4291   2842   -389       N  
ATOM    447  N   LEU A 212      31.654 -22.739   1.749  1.00 0.048           N  
ANISOU  447  N   LEU A 212    11469  10135   8619   3252   2652   -526       N  
ATOM    448  CA  LEU A 212      32.023 -21.751   0.731  1.00 0.048           C  
ANISOU  448  CA  LEU A 212    11413  10363   8648   3112   2758   -533       C  
ATOM    449  C   LEU A 212      33.036 -22.320  -0.260  1.00 0.048           C  
ANISOU  449  C   LEU A 212    12157  11275   9393   3332   2955   -567       C  
ATOM    450  O   LEU A 212      34.017 -22.950   0.153  1.00 0.048           O  
ANISOU  450  O   LEU A 212    11947  11326   9373   3571   2997   -540       O  
ATOM    451  CB  LEU A 212      32.634 -20.500   1.384  1.00 0.048           C  
ANISOU  451  CB  LEU A 212    11096  10593   8720   2947   2693   -453       C  
ATOM    452  CG  LEU A 212      31.731 -19.298   1.631  1.00 0.048           C  
ANISOU  452  CG  LEU A 212    11719  11141   9328   2636   2576   -432       C  
ATOM    453  CD1 LEU A 212      32.484 -18.230   2.380  1.00 0.048           C  
ANISOU  453  CD1 LEU A 212    11464  11413   9452   2510   2515   -358       C  
ATOM    454  CD2 LEU A 212      31.203 -18.710   0.331  1.00 0.048           C  
ANISOU  454  CD2 LEU A 212    12105  11354   9499   2478   2663   -474       C  
ATOM    455  N   ASN A 213      32.811 -22.063  -1.568  1.00 0.071           N  
ANISOU  455  N   ASN A 213    12057  11044   9085   3255   3076   -621       N  
ATOM    456  CA  ASN A 213      33.715 -22.466  -2.635  1.00 0.071           C  
ANISOU  456  CA  ASN A 213    12065  11210   9069   3437   3280   -658       C  
ATOM    457  C   ASN A 213      34.646 -21.291  -2.933  1.00 0.071           C  
ANISOU  457  C   ASN A 213    12537  12295   9882   3318   3356   -600       C  
ATOM    458  O   ASN A 213      34.187 -20.243  -3.395  1.00 0.071           O  
ANISOU  458  O   ASN A 213    12507  12276   9813   3063   3344   -591       O  
ATOM    459  CB  ASN A 213      32.943 -22.912  -3.904  1.00 0.071           C  
ANISOU  459  CB  ASN A 213    12415  11049   8965   3423   3373   -754       C  
ATOM    460  CG  ASN A 213      33.784 -23.599  -4.970  1.00 0.071           C  
ANISOU  460  CG  ASN A 213    14106  12788  10550   3656   3589   -810       C  
ATOM    461  OD1 ASN A 213      34.986 -23.844  -4.789  1.00 0.071           O  
ANISOU  461  OD1 ASN A 213    13179  12285   9898   3859   3684   -776       O  
ATOM    462  ND2 ASN A 213      33.151 -23.928  -6.109  1.00 0.071           N  
ANISOU  462  ND2 ASN A 213    13229  11479   9265   3631   3671   -896       N  
ATOM    463  N   THR A 214      35.950 -21.457  -2.645  1.00 0.603           N  
ANISOU  463  N   THR A 214    12068  12339   9748   3501   3432   -556       N  
ATOM    464  CA  THR A 214      36.969 -20.431  -2.899  1.00 0.603           C  
ANISOU  464  CA  THR A 214    11834  12741   9870   3400   3515   -498       C  
ATOM    465  C   THR A 214      37.386 -20.471  -4.386  1.00 0.603           C  
ANISOU  465  C   THR A 214    12684  13628  10572   3450   3739   -546       C  
ATOM    466  O   THR A 214      38.559 -20.694  -4.724  1.00 0.603           O  
ANISOU  466  O   THR A 214    12431  13813  10536   3622   3892   -531       O  
ATOM    467  CB  THR A 214      38.125 -20.516  -1.881  1.00 0.603           C  
ANISOU  467  CB  THR A 214    12345  13824  10825   3547   3480   -425       C  
ATOM    468  OG1 THR A 214      38.545 -21.875  -1.732  1.00 0.603           O  
ANISOU  468  OG1 THR A 214    12443  13808  10859   3896   3537   -452       O  
ATOM    469  CG2 THR A 214      37.753 -19.927  -0.528  1.00 0.603           C  
ANISOU  469  CG2 THR A 214    11908  13470  10576   3377   3260   -363       C  
ATOM    470  N   SER A 215      36.380 -20.277  -5.270  1.00-0.211           N  
ANISOU  470  N   SER A 215    12759  13235  10265   3300   3755   -603       N  
ATOM    471  CA  SER A 215      36.478 -20.267  -6.734  1.00-0.211           C  
ANISOU  471  CA  SER A 215    12946  13327  10209   3304   3944   -657       C  
ATOM    472  C   SER A 215      35.355 -19.397  -7.320  1.00-0.211           C  
ANISOU  472  C   SER A 215    13784  13834  10781   3005   3880   -670       C  
ATOM    473  O   SER A 215      34.216 -19.457  -6.841  1.00-0.211           O  
ANISOU  473  O   SER A 215    13861  13492  10670   2904   3717   -686       O  
ATOM    474  CB  SER A 215      36.383 -21.686  -7.293  1.00-0.211           C  
ANISOU  474  CB  SER A 215    13688  13654  10614   3586   4050   -751       C  
ATOM    475  OG  SER A 215      37.479 -22.500  -6.903  1.00-0.211           O  
ANISOU  475  OG  SER A 215    14528  14799  11681   3891   4135   -739       O  
ATOM    476  N   ALA A 216      35.689 -18.602  -8.368  1.00 1.258           N  
ANISOU  476  N   ALA A 216    13439  13687  10419   2872   4014   -657       N  
ATOM    477  CA  ALA A 216      34.802 -17.678  -9.096  1.00 1.258           C  
ANISOU  477  CA  ALA A 216    17230  17233  13969   2601   3984   -656       C  
ATOM    478  C   ALA A 216      34.089 -16.677  -8.191  1.00 1.258           C  
ANISOU  478  C   ALA A 216    19275  19267  16146   2347   3780   -594       C  
ATOM    479  O   ALA A 216      34.701 -15.709  -7.748  1.00 1.258           O  
ANISOU  479  O   ALA A 216    13911  14324  11088   2194   3770   -517       O  
ATOM    480  CB  ALA A 216      33.796 -18.444  -9.949  1.00 1.258           C  
ANISOU  480  CB  ALA A 216    17697  17084  13932   2648   3999   -752       C  
ATOM    481  N   ILE A 221      26.322 -15.232  -3.633  1.00-0.050           N  
ANISOU  481  N   ILE A 221    14264  12248  10501   1510   2607   -557       N  
ATOM    482  CA  ILE A 221      26.548 -15.767  -2.290  1.00-0.050           C  
ANISOU  482  CA  ILE A 221    14153  12220  10590   1607   2517   -540       C  
ATOM    483  C   ILE A 221      26.026 -17.201  -2.153  1.00-0.050           C  
ANISOU  483  C   ILE A 221    14791  12491  11014   1772   2494   -602       C  
ATOM    484  O   ILE A 221      26.722 -18.051  -1.598  1.00-0.050           O  
ANISOU  484  O   ILE A 221    14660  12455  10996   1957   2516   -606       O  
ATOM    485  CB  ILE A 221      25.980 -14.829  -1.189  1.00-0.050           C  
ANISOU  485  CB  ILE A 221    14482  12591  11063   1434   2362   -483       C  
ATOM    486  N   TYR A 222      24.798 -17.461  -2.647  1.00-0.402           N  
ANISOU  486  N   TYR A 222    14569  11852  10481   1701   2446   -648       N  
ATOM    487  CA  TYR A 222      24.135 -18.768  -2.602  1.00-0.402           C  
ANISOU  487  CA  TYR A 222    14735  11611  10397   1813   2418   -712       C  
ATOM    488  C   TYR A 222      24.785 -19.785  -3.560  1.00-0.402           C  
ANISOU  488  C   TYR A 222    15009  11783  10493   2004   2570   -780       C  
ATOM    489  O   TYR A 222      25.055 -20.921  -3.157  1.00-0.402           O  
ANISOU  489  O   TYR A 222    14956  11592  10396   2187   2585   -810       O  
ATOM    490  CB  TYR A 222      22.611 -18.599  -2.837  1.00-0.402           C  
ANISOU  490  CB  TYR A 222    15187  11701  10598   1646   2312   -734       C  
ATOM    491  CG  TYR A 222      21.923 -19.729  -3.577  1.00-0.402           C  
ANISOU  491  CG  TYR A 222    15831  11909  10879   1704   2334   -819       C  
ATOM    492  CD1 TYR A 222      21.596 -19.608  -4.925  1.00-0.402           C  
ANISOU  492  CD1 TYR A 222    16290  12219  11078   1646   2399   -867       C  
ATOM    493  CD2 TYR A 222      21.556 -20.900  -2.919  1.00-0.402           C  
ANISOU  493  CD2 TYR A 222    16101  11898  11047   1804   2282   -852       C  
ATOM    494  CE1 TYR A 222      20.959 -20.642  -5.611  1.00-0.402           C  
ANISOU  494  CE1 TYR A 222    16789  12309  11225   1685   2411   -952       C  
ATOM    495  CE2 TYR A 222      20.925 -21.943  -3.595  1.00-0.402           C  
ANISOU  495  CE2 TYR A 222    16514  11887  11109   1841   2300   -935       C  
ATOM    496  CZ  TYR A 222      20.618 -21.806  -4.940  1.00-0.402           C  
ANISOU  496  CZ  TYR A 222    17842  13079  12183   1777   2361   -989       C  
ATOM    497  OH  TYR A 222      19.982 -22.825  -5.608  1.00-0.402           O  
ANISOU  497  OH  TYR A 222    18367  13176  12346   1798   2371  -1077       O  
ATOM    498  N   LYS A 223      25.038 -19.364  -4.817  1.00 0.635           N  
ANISOU  498  N   LYS A 223    14393  11222   9759   1965   2685   -803       N  
ATOM    499  CA  LYS A 223      25.634 -20.177  -5.878  1.00 0.635           C  
ANISOU  499  CA  LYS A 223    14368  11104   9536   2129   2846   -872       C  
ATOM    500  C   LYS A 223      27.091 -20.592  -5.601  1.00 0.635           C  
ANISOU  500  C   LYS A 223    14504  11585   9919   2347   2964   -856       C  
ATOM    501  O   LYS A 223      27.608 -21.484  -6.287  1.00 0.635           O  
ANISOU  501  O   LYS A 223    14570  11538   9822   2535   3095   -918       O  
ATOM    502  CB  LYS A 223      25.515 -19.460  -7.235  1.00 0.635           C  
ANISOU  502  CB  LYS A 223    14749  11494   9744   2008   2933   -886       C  
ATOM    503  N   LYS A 224      27.750 -19.953  -4.605  1.00 1.059           N  
ANISOU  503  N   LYS A 224    13561  11062   9361   2327   2918   -775       N  
ATOM    504  CA  LYS A 224      29.134 -20.271  -4.242  1.00 1.059           C  
ANISOU  504  CA  LYS A 224    13192  11088   9275   2525   3010   -747       C  
ATOM    505  C   LYS A 224      29.210 -21.154  -2.968  1.00 1.059           C  
ANISOU  505  C   LYS A 224    13337  11169   9526   2681   2914   -732       C  
ATOM    506  O   LYS A 224      30.204 -21.114  -2.238  1.00 1.059           O  
ANISOU  506  O   LYS A 224    13083  11314   9594   2787   2919   -678       O  
ATOM    507  CB  LYS A 224      30.021 -19.002  -4.163  1.00 1.059           C  
ANISOU  507  CB  LYS A 224    13191  11643   9628   2407   3045   -669       C  
ATOM    508  CG  LYS A 224      29.564 -17.929  -3.167  1.00 1.059           C  
ANISOU  508  CG  LYS A 224    14174  12751  10808   2186   2882   -600       C  
ATOM    509  CD  LYS A 224      30.469 -16.697  -3.162  1.00 1.059           C  
ANISOU  509  CD  LYS A 224    14681  13767  11626   2053   2925   -531       C  
ATOM    510  CE  LYS A 224      30.015 -15.616  -4.118  1.00 1.059           C  
ANISOU  510  CE  LYS A 224    15535  14553  12333   1836   2962   -523       C  
ATOM    511  NZ  LYS A 224      30.954 -14.462  -4.135  1.00 1.059           N  
ANISOU  511  NZ  LYS A 224    15699  15194  12785   1704   3017   -455       N  
ATOM    512  N   LEU A 225      28.170 -21.984  -2.742  1.00 0.126           N  
ANISOU  512  N   LEU A 225    12810  10140   8715   2698   2831   -780       N  
ATOM    513  CA  LEU A 225      28.104 -22.922  -1.619  1.00 0.126           C  
ANISOU  513  CA  LEU A 225    12705   9880   8634   2842   2745   -769       C  
ATOM    514  C   LEU A 225      27.872 -24.364  -2.093  1.00 0.126           C  
ANISOU  514  C   LEU A 225    13424  10122   9003   3033   2811   -852       C  
ATOM    515  O   LEU A 225      27.049 -24.586  -2.982  1.00 0.126           O  
ANISOU  515  O   LEU A 225    13556   9873   8799   2950   2833   -922       O  
ATOM    516  CB  LEU A 225      27.010 -22.521  -0.611  1.00 0.126           C  
ANISOU  516  CB  LEU A 225    12697   9713   8638   2655   2558   -732       C  
ATOM    517  CG  LEU A 225      27.266 -21.279   0.233  1.00 0.126           C  
ANISOU  517  CG  LEU A 225    12966  10405   9253   2500   2469   -647       C  
ATOM    518  CD1 LEU A 225      25.972 -20.592   0.576  1.00 0.126           C  
ANISOU  518  CD1 LEU A 225    13062  10289   9258   2263   2332   -635       C  
ATOM    519  CD2 LEU A 225      28.015 -21.615   1.500  1.00 0.126           C  
ANISOU  519  CD2 LEU A 225    13110  10801   9663   2640   2412   -590       C  
ATOM    520  N   TYR A 226      28.591 -25.337  -1.492  1.00 0.673           N  
ANISOU  520  N   TYR A 226    12989   9696   8633   3286   2839   -843       N  
ATOM    521  CA  TYR A 226      28.448 -26.772  -1.782  1.00 0.673           C  
ANISOU  521  CA  TYR A 226    13221   9447   8531   3490   2899   -917       C  
ATOM    522  C   TYR A 226      28.246 -27.587  -0.502  1.00 0.673           C  
ANISOU  522  C   TYR A 226    13849   9874   9168   3599   2787   -880       C  
ATOM    523  O   TYR A 226      28.685 -27.159   0.568  1.00 0.673           O  
ANISOU  523  O   TYR A 226    13600   9982   9244   3608   2705   -795       O  
ATOM    524  CB  TYR A 226      29.614 -27.329  -2.629  1.00 0.673           C  
ANISOU  524  CB  TYR A 226    13341   9703   8635   3749   3096   -956       C  
ATOM    525  CG  TYR A 226      30.994 -27.172  -2.026  1.00 0.673           C  
ANISOU  525  CG  TYR A 226    13257  10189   8965   3936   3143   -880       C  
ATOM    526  CD1 TYR A 226      31.490 -28.100  -1.114  1.00 0.673           C  
ANISOU  526  CD1 TYR A 226    13465  10366   9245   4181   3117   -848       C  
ATOM    527  CD2 TYR A 226      31.837 -26.140  -2.427  1.00 0.673           C  
ANISOU  527  CD2 TYR A 226    13116  10615   9129   3874   3220   -840       C  
ATOM    528  CE1 TYR A 226      32.766 -27.968  -0.568  1.00 0.673           C  
ANISOU  528  CE1 TYR A 226    13237  10695   9408   4358   3151   -775       C  
ATOM    529  CE2 TYR A 226      33.122 -26.009  -1.902  1.00 0.673           C  
ANISOU  529  CE2 TYR A 226    12944  11002   9351   4037   3262   -770       C  
ATOM    530  CZ  TYR A 226      33.585 -26.928  -0.976  1.00 0.673           C  
ANISOU  530  CZ  TYR A 226    13979  12028  10471   4282   3224   -738       C  
ATOM    531  OH  TYR A 226      34.852 -26.796  -0.462  1.00 0.673           O  
ANISOU  531  OH  TYR A 226    14019  12650  10910   4445   3256   -666       O  
ATOM    532  N   HIS A 227      27.582 -28.756  -0.610  1.00 2.385           N  
ANISOU  532  N   HIS A 227    13798   9241   8744   3673   2783   -944       N  
ATOM    533  CA  HIS A 227      27.326 -29.644   0.527  1.00 2.385           C  
ANISOU  533  CA  HIS A 227    13952   9120   8839   3776   2688   -913       C  
ATOM    534  C   HIS A 227      28.611 -30.315   1.005  1.00 2.385           C  
ANISOU  534  C   HIS A 227    14409   9792   9468   4101   2760   -872       C  
ATOM    535  O   HIS A 227      29.374 -30.841   0.198  1.00 2.385           O  
ANISOU  535  O   HIS A 227    14400   9781   9376   4311   2914   -920       O  
ATOM    536  CB  HIS A 227      26.255 -30.688   0.187  1.00 2.385           C  
ANISOU  536  CB  HIS A 227    14456   8926   8877   3747   2675   -995       C  
ATOM    537  N   SER A 228      28.861 -30.251   2.316  1.00-0.103           N  
ANISOU  537  N   SER A 228    13999   9593   9307   4142   2647   -781       N  
ATOM    538  CA  SER A 228      30.042 -30.810   2.971  1.00-0.103           C  
ANISOU  538  CA  SER A 228    13884   9733   9396   4441   2679   -721       C  
ATOM    539  C   SER A 228      29.641 -31.531   4.262  1.00-0.103           C  
ANISOU  539  C   SER A 228    14472  10036   9911   4501   2548   -666       C  
ATOM    540  O   SER A 228      28.675 -31.136   4.918  1.00-0.103           O  
ANISOU  540  O   SER A 228    14403   9838   9818   4270   2411   -640       O  
ATOM    541  CB  SER A 228      31.049 -29.701   3.273  1.00-0.103           C  
ANISOU  541  CB  SER A 228    14028  10625  10021   4419   2674   -645       C  
ATOM    542  OG  SER A 228      32.081 -30.120   4.153  1.00-0.103           O  
ANISOU  542  OG  SER A 228    15119  12019  11354   4676   2663   -571       O  
ATOM    543  N   ASP A 229      30.392 -32.579   4.623  1.00 0.590           N  
ANISOU  543  N   ASP A 229    14114   9582   9513   4816   2595   -643       N  
ATOM    544  CA  ASP A 229      30.141 -33.361   5.831  1.00 0.590           C  
ANISOU  544  CA  ASP A 229    14264   9445   9571   4911   2484   -582       C  
ATOM    545  C   ASP A 229      30.614 -32.631   7.087  1.00 0.590           C  
ANISOU  545  C   ASP A 229    14587  10298  10296   4886   2353   -467       C  
ATOM    546  O   ASP A 229      30.040 -32.844   8.160  1.00 0.590           O  
ANISOU  546  O   ASP A 229    14668  10179  10319   4829   2222   -413       O  
ATOM    547  CB  ASP A 229      30.818 -34.738   5.735  1.00 0.590           C  
ANISOU  547  CB  ASP A 229    14676   9539   9772   5277   2585   -596       C  
ATOM    548  N   ALA A 230      31.665 -31.781   6.963  1.00 0.385           N  
ANISOU  548  N   ALA A 230    13825  10208   9932   4921   2389   -430       N  
ATOM    549  CA  ALA A 230      32.236 -31.063   8.108  1.00 0.385           C  
ANISOU  549  CA  ALA A 230    13501  10429  10001   4897   2267   -326       C  
ATOM    550  C   ALA A 230      32.780 -29.652   7.813  1.00 0.385           C  
ANISOU  550  C   ALA A 230    13409  10991  10290   4717   2274   -311       C  
ATOM    551  O   ALA A 230      33.183 -29.355   6.685  1.00 0.385           O  
ANISOU  551  O   ALA A 230    13195  10944  10112   4718   2410   -364       O  
ATOM    552  CB  ALA A 230      33.327 -31.913   8.751  1.00 0.385           C  
ANISOU  552  CB  ALA A 230    13523  10619  10144   5254   2279   -259       C  
ATOM    553  N   CYS A 231      32.785 -28.793   8.857  1.00-0.776           N  
ANISOU  553  N   CYS A 231    12670  10601   9817   4560   2127   -236       N  
ATOM    554  CA  CYS A 231      33.339 -27.438   8.848  1.00-0.776           C  
ANISOU  554  CA  CYS A 231    12212  10767   9734   4381   2106   -206       C  
ATOM    555  C   CYS A 231      34.721 -27.560   9.501  1.00-0.776           C  
ANISOU  555  C   CYS A 231    12603  11720  10478   4608   2091   -126       C  
ATOM    556  O   CYS A 231      34.799 -27.917  10.686  1.00-0.776           O  
ANISOU  556  O   CYS A 231    12593  11709  10511   4697   1966    -57       O  
ATOM    557  CB  CYS A 231      32.456 -26.465   9.631  1.00-0.776           C  
ANISOU  557  CB  CYS A 231    12112  10653   9668   4068   1951   -181       C  
ATOM    558  SG  CYS A 231      30.795 -26.201   8.945  1.00-0.776           S  
ANISOU  558  SG  CYS A 231    12842  10795  10028   3790   1950   -263       S  
ATOM    559  N   SER A 232      35.805 -27.270   8.745  1.00 0.964           N  
ANISOU  559  N   SER A 232    11881  11490  10011   4700   2215   -129       N  
ATOM    560  CA  SER A 232      37.183 -27.323   9.260  1.00 0.964           C  
ANISOU  560  CA  SER A 232    11517  11746  10028   4909   2209    -52       C  
ATOM    561  C   SER A 232      37.425 -26.299  10.394  1.00 0.964           C  
ANISOU  561  C   SER A 232    11740  12436  10572   4712   2036     24       C  
ATOM    562  O   SER A 232      38.388 -26.444  11.150  1.00 0.964           O  
ANISOU  562  O   SER A 232    11538  12683  10652   4874   1975    100       O  
ATOM    563  CB  SER A 232      38.195 -27.118   8.137  1.00 0.964           C  
ANISOU  563  CB  SER A 232    11774  12441  10489   5008   2389    -77       C  
ATOM    564  OG  SER A 232      37.843 -27.850   6.974  1.00 0.964           O  
ANISOU  564  OG  SER A 232    13492  13704  11876   5130   2553   -164       O  
ATOM    565  N   SER A 233      36.541 -25.279  10.508  1.00-0.653           N  
ANISOU  565  N   SER A 233    11212  11793   9991   4369   1956      3       N  
ATOM    566  CA  SER A 233      36.576 -24.237  11.537  1.00-0.653           C  
ANISOU  566  CA  SER A 233    10919  11836   9930   4143   1794     59       C  
ATOM    567  C   SER A 233      35.835 -24.694  12.804  1.00-0.653           C  
ANISOU  567  C   SER A 233    11504  12060  10336   4154   1632     97       C  
ATOM    568  O   SER A 233      35.973 -24.067  13.860  1.00-0.653           O  
ANISOU  568  O   SER A 233    11325  12152  10335   4038   1485    153       O  
ATOM    569  CB  SER A 233      35.948 -22.951  11.006  1.00-0.653           C  
ANISOU  569  CB  SER A 233    11262  12162  10256   3790   1799     15       C  
ATOM    570  OG  SER A 233      34.580 -23.145  10.692  1.00-0.653           O  
ANISOU  570  OG  SER A 233    12390  12648  11005   3682   1798    -43       O  
ATOM    571  N   LYS A 234      35.039 -25.786  12.682  1.00 0.827           N  
ANISOU  571  N   LYS A 234    11226  11157   9689   4281   1661     65       N  
ATOM    572  CA  LYS A 234      34.218 -26.399  13.737  1.00 0.827           C  
ANISOU  572  CA  LYS A 234    11286  10771   9510   4302   1536     96       C  
ATOM    573  C   LYS A 234      33.208 -25.397  14.326  1.00 0.827           C  
ANISOU  573  C   LYS A 234    11449  10816   9622   3968   1414     92       C  
ATOM    574  O   LYS A 234      32.976 -25.362  15.541  1.00 0.827           O  
ANISOU  574  O   LYS A 234    11633  10963   9798   3933   1272    147       O  
ATOM    575  CB  LYS A 234      35.084 -27.091  14.820  1.00 0.827           C  
ANISOU  575  CB  LYS A 234    11505  11220   9870   4565   1451    187       C  
ATOM    576  CG  LYS A 234      36.065 -28.126  14.276  1.00 0.827           C  
ANISOU  576  CG  LYS A 234    12728  12555  11142   4925   1574    196       C  
ATOM    577  CD  LYS A 234      37.484 -27.574  14.208  1.00 0.827           C  
ANISOU  577  CD  LYS A 234    13626  14244  12496   5003   1590    242       C  
ATOM    578  N   ALA A 235      32.610 -24.574  13.443  1.00 1.610           N  
ANISOU  578  N   ALA A 235    10505   9811   8635   3730   1474     28       N  
ATOM    579  CA  ALA A 235      31.623 -23.549  13.797  1.00 1.610           C  
ANISOU  579  CA  ALA A 235    10298   9491   8376   3417   1382     16       C  
ATOM    580  C   ALA A 235      30.755 -23.184  12.593  1.00 1.610           C  
ANISOU  580  C   ALA A 235    10443   9345   8331   3249   1479    -63       C  
ATOM    581  O   ALA A 235      31.193 -23.308  11.444  1.00 1.610           O  
ANISOU  581  O   ALA A 235    10496   9475   8396   3320   1615   -105       O  
ATOM    582  CB  ALA A 235      32.320 -22.300  14.329  1.00 1.610           C  
ANISOU  582  CB  ALA A 235    10065   9827   8484   3259   1304     57       C  
ATOM    583  N   VAL A 236      29.524 -22.729  12.866  1.00-0.448           N  
ANISOU  583  N   VAL A 236     9605   8185   7317   3030   1408    -82       N  
ATOM    584  CA  VAL A 236      28.569 -22.294  11.844  1.00-0.448           C  
ANISOU  584  CA  VAL A 236     9447   7754   6977   2848   1471   -148       C  
ATOM    585  C   VAL A 236      28.351 -20.772  11.922  1.00-0.448           C  
ANISOU  585  C   VAL A 236     9380   7939   7066   2575   1420   -142       C  
ATOM    586  O   VAL A 236      28.605 -20.171  12.964  1.00-0.448           O  
ANISOU  586  O   VAL A 236     9068   7872   6924   2502   1313    -94       O  
ATOM    587  CB  VAL A 236      27.241 -23.107  11.849  1.00-0.448           C  
ANISOU  587  CB  VAL A 236    10162   7857   7332   2829   1453   -182       C  
ATOM    588  CG1 VAL A 236      27.494 -24.579  11.504  1.00-0.448           C  
ANISOU  588  CG1 VAL A 236    10224   7627   7203   3090   1532   -202       C  
ATOM    589  CG2 VAL A 236      26.477 -22.960  13.175  1.00-0.448           C  
ANISOU  589  CG2 VAL A 236    10166   7718   7290   2725   1311   -138       C  
ATOM    590  N   VAL A 237      27.899 -20.152  10.823  1.00-0.436           N  
ANISOU  590  N   VAL A 237     8739   7223   6349   2428   1496   -191       N  
ATOM    591  CA  VAL A 237      27.667 -18.707  10.782  1.00-0.436           C  
ANISOU  591  CA  VAL A 237     8443   7116   6167   2176   1460   -186       C  
ATOM    592  C   VAL A 237      26.412 -18.326  11.567  1.00-0.436           C  
ANISOU  592  C   VAL A 237     8623   7007   6206   2011   1346   -181       C  
ATOM    593  O   VAL A 237      25.369 -18.963  11.418  1.00-0.436           O  
ANISOU  593  O   VAL A 237     8702   6662   6032   2014   1343   -210       O  
ATOM    594  CB  VAL A 237      27.613 -18.169   9.316  1.00-0.436           C  
ANISOU  594  CB  VAL A 237     8872   7553   6546   2085   1582   -232       C  
ATOM    595  CG1 VAL A 237      27.244 -16.682   9.265  1.00-0.436           C  
ANISOU  595  CG1 VAL A 237     8751   7552   6497   1823   1544   -223       C  
ATOM    596  CG2 VAL A 237      28.923 -18.422   8.586  1.00-0.436           C  
ANISOU  596  CG2 VAL A 237     8619   7644   6460   2238   1705   -233       C  
ATOM    597  N   SER A 238      26.538 -17.281  12.404  1.00-0.145           N  
ANISOU  597  N   SER A 238     7870   6493   5618   1864   1255   -145       N  
ATOM    598  CA  SER A 238      25.463 -16.639  13.147  1.00-0.145           C  
ANISOU  598  CA  SER A 238     7800   6225   5452   1689   1156   -139       C  
ATOM    599  C   SER A 238      25.397 -15.249  12.511  1.00-0.145           C  
ANISOU  599  C   SER A 238     8346   6919   6072   1482   1183   -152       C  
ATOM    600  O   SER A 238      26.385 -14.495  12.536  1.00-0.145           O  
ANISOU  600  O   SER A 238     8165   7122   6114   1430   1189   -132       O  
ATOM    601  CB  SER A 238      25.792 -16.544  14.632  1.00-0.145           C  
ANISOU  601  CB  SER A 238     7893   6475   5660   1700   1034    -90       C  
ATOM    602  OG  SER A 238      24.723 -15.901  15.310  1.00-0.145           O  
ANISOU  602  OG  SER A 238     8655   7032   6312   1534    953    -89       O  
ATOM    603  N   LEU A 239      24.264 -14.933  11.881  1.00-0.545           N  
ANISOU  603  N   LEU A 239     7905   6177   5440   1367   1204   -184       N  
ATOM    604  CA  LEU A 239      24.153 -13.696  11.135  1.00-0.545           C  
ANISOU  604  CA  LEU A 239     7644   6002   5208   1191   1242   -193       C  
ATOM    605  C   LEU A 239      23.064 -12.767  11.605  1.00-0.545           C  
ANISOU  605  C   LEU A 239     8075   6252   5549   1014   1166   -189       C  
ATOM    606  O   LEU A 239      21.889 -13.128  11.623  1.00-0.545           O  
ANISOU  606  O   LEU A 239     8259   6109   5543   1003   1142   -205       O  
ATOM    607  CB  LEU A 239      23.985 -14.028   9.640  1.00-0.545           C  
ANISOU  607  CB  LEU A 239     7666   5889   5097   1225   1359   -232       C  
ATOM    608  CG  LEU A 239      23.941 -12.843   8.680  1.00-0.545           C  
ANISOU  608  CG  LEU A 239     8175   6476   5611   1063   1416   -237       C  
ATOM    609  CD1 LEU A 239      25.260 -12.113   8.633  1.00-0.545           C  
ANISOU  609  CD1 LEU A 239     7964   6694   5650   1024   1454   -209       C  
ATOM    610  CD2 LEU A 239      23.548 -13.292   7.326  1.00-0.545           C  
ANISOU  610  CD2 LEU A 239     8275   6374   5524   1100   1513   -277       C  
ATOM    611  N   ARG A 240      23.458 -11.542  11.940  1.00 1.231           N  
ANISOU  611  N   ARG A 240     7458   5852   5066    871   1135   -169       N  
ATOM    612  CA  ARG A 240      22.516 -10.520  12.364  1.00 1.231           C  
ANISOU  612  CA  ARG A 240     7511   5745   5037    707   1073   -165       C  
ATOM    613  C   ARG A 240      22.579  -9.364  11.386  1.00 1.231           C  
ANISOU  613  C   ARG A 240     8042   6334   5573    564   1134   -168       C  
ATOM    614  O   ARG A 240      23.648  -8.800  11.146  1.00 1.231           O  
ANISOU  614  O   ARG A 240     7918   6504   5611    516   1171   -155       O  
ATOM    615  CB  ARG A 240      22.762 -10.093  13.817  1.00 1.231           C  
ANISOU  615  CB  ARG A 240     7396   5751   5019    660    967   -141       C  
ATOM    616  CG  ARG A 240      22.457 -11.215  14.809  1.00 1.231           C  
ANISOU  616  CG  ARG A 240     8382   6608   5946    792    902   -132       C  
ATOM    617  CD  ARG A 240      22.219 -10.698  16.197  1.00 1.231           C  
ANISOU  617  CD  ARG A 240     8537   6764   6109    719    795   -114       C  
ATOM    618  NE  ARG A 240      21.041  -9.831  16.254  1.00 1.231           N  
ANISOU  618  NE  ARG A 240     8803   6793   6237    580    777   -126       N  
ATOM    619  CZ  ARG A 240      20.685  -9.138  17.327  1.00 1.231           C  
ANISOU  619  CZ  ARG A 240     9639   7590   7047    491    699   -119       C  
ATOM    620  NH1 ARG A 240      21.401  -9.215  18.441  1.00 1.231           N  
ANISOU  620  NH1 ARG A 240     7689   5816   5187    513    624   -101       N  
ATOM    621  NH2 ARG A 240      19.608  -8.363  17.295  1.00 1.231           N  
ANISOU  621  NH2 ARG A 240     7381   5116   4663    386    696   -131       N  
ATOM    622  N   CYS A 241      21.438  -9.055  10.780  1.00 0.177           N  
ANISOU  622  N   CYS A 241     7694   5706   5043    500   1148   -181       N  
ATOM    623  CA  CYS A 241      21.324  -8.024   9.758  1.00 0.177           C  
ANISOU  623  CA  CYS A 241     7720   5720   5023    376   1207   -179       C  
ATOM    624  C   CYS A 241      20.981  -6.643  10.303  1.00 0.177           C  
ANISOU  624  C   CYS A 241     8225   6192   5526    213   1152   -160       C  
ATOM    625  O   CYS A 241      21.107  -5.666   9.578  1.00 0.177           O  
ANISOU  625  O   CYS A 241     8375   6361   5657    102   1199   -148       O  
ATOM    626  CB  CYS A 241      20.336  -8.459   8.682  1.00 0.177           C  
ANISOU  626  CB  CYS A 241     7960   5690   5060    407   1252   -201       C  
ATOM    627  SG  CYS A 241      20.802  -9.987   7.827  1.00 0.177           S  
ANISOU  627  SG  CYS A 241     8532   6260   5590    587   1336   -234       S  
ATOM    628  N   ILE A 242      20.543  -6.554  11.551  1.00 0.537           N  
ANISOU  628  N   ILE A 242     7537   5433   4836    200   1060   -156       N  
ATOM    629  CA  ILE A 242      20.155  -5.292  12.180  1.00 0.537           C  
ANISOU  629  CA  ILE A 242     7523   5347   4791     59   1007   -145       C  
ATOM    630  C   ILE A 242      20.211  -5.432  13.707  1.00 0.537           C  
ANISOU  630  C   ILE A 242     8037   5897   5356     72    911   -144       C  
ATOM    631  O   ILE A 242      19.919  -6.502  14.244  1.00 0.537           O  
ANISOU  631  O   ILE A 242     7774   5575   5072    188    878   -148       O  
ATOM    632  CB  ILE A 242      18.760  -4.799  11.627  1.00 0.537           C  
ANISOU  632  CB  ILE A 242     8109   5627   5183     14   1015   -146       C  
ATOM    633  CG1 ILE A 242      18.394  -3.370  12.113  1.00 0.537           C  
ANISOU  633  CG1 ILE A 242     8157   5579   5181   -125    979   -133       C  
ATOM    634  CG2 ILE A 242      17.611  -5.797  11.889  1.00 0.537           C  
ANISOU  634  CG2 ILE A 242     8373   5679   5334    113    981   -159       C  
ATOM    635  CD1 ILE A 242      17.374  -2.676  11.247  1.00 0.537           C  
ANISOU  635  CD1 ILE A 242     9023   6217   5886   -172   1009   -123       C  
ATOM    636  N   ALA A 243      20.629  -4.351  14.393  1.00 1.311           N  
ANISOU  636  N   ALA A 243     7845   5792   5216    -54    868   -138       N  
ATOM    637  CA  ALA A 243      20.668  -4.245  15.846  1.00 1.311           C  
ANISOU  637  CA  ALA A 243     7826   5794   5217    -71    773   -139       C  
ATOM    638  C   ALA A 243      19.201  -4.096  16.238  1.00 1.311           C  
ANISOU  638  C   ALA A 243     8565   6207   5770    -69    745   -147       C  
ATOM    639  O   ALA A 243      18.605  -3.051  15.966  1.00 1.311           O  
ANISOU  639  O   ALA A 243     8984   6467   6091   -167    760   -148       O  
ATOM    640  CB  ALA A 243      21.447  -2.993  16.257  1.00 1.311           C  
ANISOU  640  CB  ALA A 243     7833   5946   5296   -232    745   -138       C  
ATOM    641  N   CYS A 244      18.587  -5.175  16.745  1.00-1.074           N  
ANISOU  641  N   CYS A 244     7680   5218   4833     47    717   -147       N  
ATOM    642  CA  CYS A 244      17.175  -5.170  17.132  1.00-1.074           C  
ANISOU  642  CA  CYS A 244     7612   4878   4609     56    696   -151       C  
ATOM    643  C   CYS A 244      16.933  -5.865  18.463  1.00-1.074           C  
ANISOU  643  C   CYS A 244     7715   4945   4687    120    628   -147       C  
ATOM    644  O   CYS A 244      17.805  -6.581  18.954  1.00-1.074           O  
ANISOU  644  O   CYS A 244     7517   4912   4581    187    598   -139       O  
ATOM    645  CB  CYS A 244      16.302  -5.772  16.031  1.00-1.074           C  
ANISOU  645  CB  CYS A 244     7693   4806   4606    114    752   -153       C  
ATOM    646  SG  CYS A 244      16.739  -7.472  15.573  1.00-1.074           S  
ANISOU  646  SG  CYS A 244     8210   5385   5165    263    781   -156       S  
ATOM    647  N   GLY A 245      15.708  -5.726  18.960  1.00-1.239           N  
ANISOU  647  N   GLY A 245     7232   4245   4074    112    612   -148       N  
ATOM    648  CA  GLY A 245      15.216  -6.422  20.136  1.00-1.239           C  
ANISOU  648  CA  GLY A 245     7361   4293   4142    171    562   -140       C  
ATOM    649  C   GLY A 245      15.836  -6.093  21.477  1.00-1.239           C  
ANISOU  649  C   GLY A 245     8041   5065   4840    143    491   -140       C  
ATOM    650  O   GLY A 245      15.861  -6.957  22.351  1.00-1.239           O  
ANISOU  650  O   GLY A 245     7834   4857   4612    217    449   -125       O  
ATOM    651  N   VAL A 246      16.305  -4.852  21.656  1.00 1.915           N  
ANISOU  651  N   VAL A 246     7939   5025   4756     31    474   -154       N  
ATOM    652  CA  VAL A 246      16.886  -4.349  22.915  1.00 1.915           C  
ANISOU  652  CA  VAL A 246     8099   5263   4911    -24    398   -162       C  
ATOM    653  C   VAL A 246      16.007  -3.174  23.415  1.00 1.915           C  
ANISOU  653  C   VAL A 246     8912   5864   5574   -115    396   -184       C  
ATOM    654  O   VAL A 246      15.567  -2.360  22.610  1.00 1.915           O  
ANISOU  654  O   VAL A 246     8822   5669   5448   -172    447   -192       O  
ATOM    655  CB  VAL A 246      18.391  -3.969  22.740  1.00 1.915           C  
ANISOU  655  CB  VAL A 246     8535   5985   5508    -86    374   -164       C  
ATOM    656  CG1 VAL A 246      18.930  -3.186  23.929  1.00 1.915           C  
ANISOU  656  CG1 VAL A 246     8481   5996   5429   -184    292   -181       C  
ATOM    657  CG2 VAL A 246      19.247  -5.212  22.505  1.00 1.915           C  
ANISOU  657  CG2 VAL A 246     8411   6078   5525     36    370   -140       C  
ATOM    658  N   ASN A 247      15.733  -3.120  24.738  1.00 0.220           N  
ANISOU  658  N   ASN A 247     8969   5846   5529   -115    341   -191       N  
ATOM    659  CA  ASN A 247      14.913  -2.091  25.396  1.00 0.220           C  
ANISOU  659  CA  ASN A 247     9123   5790   5521   -180    340   -216       C  
ATOM    660  C   ASN A 247      15.454  -1.786  26.819  1.00 0.220           C  
ANISOU  660  C   ASN A 247    10268   6969   6597   -228    258   -234       C  
ATOM    661  O   ASN A 247      16.451  -2.390  27.224  1.00 0.220           O  
ANISOU  661  O   ASN A 247    10037   6947   6462   -210    198   -222       O  
ATOM    662  CB  ASN A 247      13.449  -2.562  25.454  1.00 0.220           C  
ANISOU  662  CB  ASN A 247     8738   5207   5033   -100    384   -203       C  
ATOM    663  CG  ASN A 247      13.166  -3.676  26.456  1.00 0.220           C  
ANISOU  663  CG  ASN A 247    11039   7499   7289    -15    351   -183       C  
ATOM    664  OD1 ASN A 247      14.072  -4.341  26.992  1.00 0.220           O  
ANISOU  664  OD1 ASN A 247     9463   6070   5768     15    294   -170       O  
ATOM    665  ND2 ASN A 247      11.889  -3.921  26.726  1.00 0.220           N  
ANISOU  665  ND2 ASN A 247     9871   6165   6018     29    387   -174       N  
ATOM    666  N   LEU A 248      14.766  -0.887  27.581  1.00 2.310           N  
ANISOU  666  N   LEU A 248    10565   7060   6719   -280    256   -264       N  
ATOM    667  CA  LEU A 248      15.124  -0.478  28.952  1.00 2.310           C  
ANISOU  667  CA  LEU A 248    10833   7309   6871   -335    182   -291       C  
ATOM    668  C   LEU A 248      15.542  -1.667  29.826  1.00 2.310           C  
ANISOU  668  C   LEU A 248    11745   8364   7812   -254    115   -263       C  
ATOM    669  O   LEU A 248      14.754  -2.596  30.034  1.00 2.310           O  
ANISOU  669  O   LEU A 248    11800   8346   7830   -148    140   -233       O  
ATOM    670  CB  LEU A 248      13.989   0.320  29.618  1.00 2.310           C  
ANISOU  670  CB  LEU A 248    11017   7210   6838   -347    215   -320       C  
ATOM    671  N   ASN A 249      16.817  -1.631  30.295  1.00 2.728           N  
ANISOU  671  N   ASN A 249    11404   8237   7542   -311     28   -269       N  
ATOM    672  CA  ASN A 249      17.523  -2.627  31.120  1.00 2.728           C  
ANISOU  672  CA  ASN A 249    14790  11807  10971   -243    -57   -239       C  
ATOM    673  C   ASN A 249      17.899  -3.856  30.296  1.00 2.728           C  
ANISOU  673  C   ASN A 249    18512  15715  14883   -127    -38   -191       C  
ATOM    674  O   ASN A 249      18.359  -3.719  29.163  1.00 2.728           O  
ANISOU  674  O   ASN A 249    13643  10983  10174   -152     -2   -191       O  
ATOM    675  CB  ASN A 249      16.749  -3.020  32.400  1.00 2.728           C  
ANISOU  675  CB  ASN A 249    14950  11791  10930   -181    -80   -231       C  
ATOM    676  CG  ASN A 249      16.108  -1.871  33.146  1.00 2.728           C  
ANISOU  676  CG  ASN A 249    17365  13972  13124   -269    -74   -281       C  
ATOM    677  OD1 ASN A 249      16.761  -0.890  33.526  1.00 2.728           O  
ANISOU  677  OD1 ASN A 249    17010  13635  12719   -393   -125   -326       O  
ATOM    678  ND2 ASN A 249      14.806  -1.973  33.373  1.00 2.728           N  
ANISOU  678  ND2 ASN A 249    15954  12334  11572   -207     -7   -276       N  
ATOM    679  N   ILE A 256      -5.262  -0.891  25.637  1.00-1.187           N  
ANISOU  679  N   ILE A 256     7800   3785   3825    533   1036     42       N  
ATOM    680  CA  ILE A 256      -4.915  -2.020  26.490  1.00-1.187           C  
ANISOU  680  CA  ILE A 256     7705   3698   3707    470   1029     39       C  
ATOM    681  C   ILE A 256      -5.814  -1.970  27.733  1.00-1.187           C  
ANISOU  681  C   ILE A 256     8173   4198   4128    515   1103     49       C  
ATOM    682  O   ILE A 256      -5.839  -0.944  28.414  1.00-1.187           O  
ANISOU  682  O   ILE A 256     8255   4169   4097    578   1143     24       O  
ATOM    683  CB  ILE A 256      -3.401  -1.979  26.910  1.00-1.187           C  
ANISOU  683  CB  ILE A 256     8009   3845   3900    425    983     -3       C  
ATOM    684  CG1 ILE A 256      -2.424  -1.922  25.695  1.00-1.187           C  
ANISOU  684  CG1 ILE A 256     7765   3579   3701    385    923    -14       C  
ATOM    685  CG2 ILE A 256      -3.033  -3.113  27.887  1.00-1.187           C  
ANISOU  685  CG2 ILE A 256     7501   3333   3348    379    973      0       C  
ATOM    686  CD1 ILE A 256      -2.382  -3.153  24.695  1.00-1.187           C  
ANISOU  686  CD1 ILE A 256     7885   3808   3936    334    885      8       C  
ATOM    687  N   VAL A 257      -6.488  -3.085  28.064  1.00-0.981           N  
ANISOU  687  N   VAL A 257     7530   3683   3551    474   1123     82       N  
ATOM    688  CA  VAL A 257      -7.332  -3.162  29.277  1.00-0.981           C  
ANISOU  688  CA  VAL A 257     7495   3694   3471    505   1202     98       C  
ATOM    689  C   VAL A 257      -6.528  -3.898  30.348  1.00-0.981           C  
ANISOU  689  C   VAL A 257     8214   4293   4058    450   1189     86       C  
ATOM    690  O   VAL A 257      -5.938  -4.932  30.035  1.00-0.981           O  
ANISOU  690  O   VAL A 257     7957   4028   3826    377   1135     95       O  
ATOM    691  CB  VAL A 257      -8.691  -3.879  29.006  1.00-0.981           C  
ANISOU  691  CB  VAL A 257     7796   4233   3930    486   1242    151       C  
ATOM    692  CG1 VAL A 257      -9.586  -3.892  30.253  1.00-0.981           C  
ANISOU  692  CG1 VAL A 257     7669   4174   3763    521   1338    170       C  
ATOM    693  CG2 VAL A 257      -9.420  -3.251  27.811  1.00-0.981           C  
ANISOU  693  CG2 VAL A 257     7703   4284   3980    538   1233    169       C  
ATOM    694  N   GLY A 258      -6.515  -3.360  31.581  1.00-1.049           N  
ANISOU  694  N   GLY A 258     8071   4052   3764    493   1239     65       N  
ATOM    695  CA  GLY A 258      -5.857  -3.974  32.735  1.00-1.049           C  
ANISOU  695  CA  GLY A 258     8156   4027   3699    453   1229     59       C  
ATOM    696  C   GLY A 258      -4.340  -3.908  32.722  1.00-1.049           C  
ANISOU  696  C   GLY A 258     8654   4377   4108    420   1141     21       C  
ATOM    697  O   GLY A 258      -3.681  -4.705  33.399  1.00-1.049           O  
ANISOU  697  O   GLY A 258     8365   4030   3734    379   1107     28       O  
ATOM    698  N   GLY A 259      -3.794  -2.953  31.971  1.00-1.443           N  
ANISOU  698  N   GLY A 259     8288   3958   3761    438   1105    -15       N  
ATOM    699  CA  GLY A 259      -2.350  -2.753  31.860  1.00-1.443           C  
ANISOU  699  CA  GLY A 259     8439   4002   3853    400   1024    -51       C  
ATOM    700  C   GLY A 259      -1.841  -1.581  32.688  1.00-1.443           C  
ANISOU  700  C   GLY A 259     8982   4385   4219    420   1027   -104       C  
ATOM    701  O   GLY A 259      -2.523  -1.112  33.594  1.00-1.443           O  
ANISOU  701  O   GLY A 259     8831   4179   3953    467   1093   -115       O  
ATOM    702  N   GLU A 260      -0.636  -1.097  32.373  1.00 1.142           N  
ANISOU  702  N   GLU A 260     8680   4008   3889    379    958   -140       N  
ATOM    703  CA  GLU A 260       0.028   0.001  33.075  1.00 1.142           C  
ANISOU  703  CA  GLU A 260     8850   4012   3884    368    943   -197       C  
ATOM    704  C   GLU A 260       0.780   0.873  32.088  1.00 1.142           C  
ANISOU  704  C   GLU A 260     8990   4101   4064    335    902   -224       C  
ATOM    705  O   GLU A 260       1.293   0.347  31.105  1.00 1.142           O  
ANISOU  705  O   GLU A 260     8873   4088   4094    300    858   -203       O  
ATOM    706  CB  GLU A 260       1.015  -0.602  34.077  1.00 1.142           C  
ANISOU  706  CB  GLU A 260     9125   4267   4057    317    879   -209       C  
ATOM    707  CG  GLU A 260       1.465   0.355  35.156  1.00 1.142           C  
ANISOU  707  CG  GLU A 260    10456   5429   5164    302    870   -267       C  
ATOM    708  CD  GLU A 260       2.205  -0.267  36.327  1.00 1.142           C  
ANISOU  708  CD  GLU A 260    12870   7834   7452    265    811   -271       C  
ATOM    709  OE1 GLU A 260       2.526  -1.479  36.275  1.00 1.142           O  
ANISOU  709  OE1 GLU A 260    12303   7386   6977    254    770   -225       O  
ATOM    710  OE2 GLU A 260       2.460   0.470  37.306  1.00 1.142           O  
ANISOU  710  OE2 GLU A 260    10937   5759   5311    250    804   -321       O  
ATOM    711  N   SER A 261       0.896   2.185  32.381  1.00 1.059           N  
ANISOU  711  N   SER A 261     8625   3559   3551    340    919   -273       N  
ATOM    712  CA  SER A 261       1.630   3.155  31.568  1.00 1.059           C  
ANISOU  712  CA  SER A 261     8606   3448   3530    294    888   -300       C  
ATOM    713  C   SER A 261       3.016   2.637  31.240  1.00 1.059           C  
ANISOU  713  C   SER A 261     8861   3795   3865    199    798   -303       C  
ATOM    714  O   SER A 261       3.755   2.204  32.131  1.00 1.059           O  
ANISOU  714  O   SER A 261     8618   3572   3561    155    746   -320       O  
ATOM    715  CB  SER A 261       1.776   4.476  32.325  1.00 1.059           C  
ANISOU  715  CB  SER A 261     9149   3746   3842    288    907   -361       C  
ATOM    716  OG  SER A 261       0.594   5.248  32.209  1.00 1.059           O  
ANISOU  716  OG  SER A 261    10445   4937   5080    390    995   -358       O  
ATOM    717  N   ALA A 262       3.365   2.684  29.963  1.00-0.844           N  
ANISOU  717  N   ALA A 262     8441   3441   3582    174    780   -285       N  
ATOM    718  CA  ALA A 262       4.670   2.291  29.486  1.00-0.844           C  
ANISOU  718  CA  ALA A 262     8310   3415   3546     93    709   -286       C  
ATOM    719  C   ALA A 262       5.713   3.323  29.929  1.00-0.844           C  
ANISOU  719  C   ALA A 262     9042   4026   4152      3    667   -339       C  
ATOM    720  O   ALA A 262       5.437   4.538  29.977  1.00-0.844           O  
ANISOU  720  O   ALA A 262     8742   3530   3716     -3    701   -370       O  
ATOM    721  CB  ALA A 262       4.648   2.193  27.971  1.00-0.844           C  
ANISOU  721  CB  ALA A 262     8300   3488   3689     95    717   -255       C  
ATOM    722  N   LEU A 263       6.912   2.833  30.248  1.00 1.639           N  
ANISOU  722  N   LEU A 263     8980   4081   4133    -67    592   -348       N  
ATOM    723  CA  LEU A 263       8.040   3.690  30.629  1.00 1.639           C  
ANISOU  723  CA  LEU A 263     9120   4158   4184   -177    536   -396       C  
ATOM    724  C   LEU A 263       8.796   4.135  29.371  1.00 1.639           C  
ANISOU  724  C   LEU A 263     9386   4480   4568   -248    527   -390       C  
ATOM    725  O   LEU A 263       8.697   3.455  28.346  1.00 1.639           O  
ANISOU  725  O   LEU A 263     9004   4235   4351   -210    544   -348       O  
ATOM    726  CB  LEU A 263       9.002   2.912  31.559  1.00 1.639           C  
ANISOU  726  CB  LEU A 263     9147   4332   4222   -216    451   -402       C  
ATOM    727  CG  LEU A 263       8.429   2.344  32.852  1.00 1.639           C  
ANISOU  727  CG  LEU A 263     9951   5097   4901   -156    451   -401       C  
ATOM    728  CD1 LEU A 263       9.526   1.761  33.727  1.00 1.639           C  
ANISOU  728  CD1 LEU A 263    10010   5287   4952   -201    354   -405       C  
ATOM    729  CD2 LEU A 263       7.649   3.376  33.615  1.00 1.639           C  
ANISOU  729  CD2 LEU A 263    10221   5119   4940   -145    501   -446       C  
ATOM    730  N   PRO A 264       9.551   5.263  29.397  1.00 1.667           N  
ANISOU  730  N   PRO A 264     9339   4320   4428   -360    504   -431       N  
ATOM    731  CA  PRO A 264      10.310   5.643  28.189  1.00 1.667           C  
ANISOU  731  CA  PRO A 264     9143   4191   4346   -438    502   -418       C  
ATOM    732  C   PRO A 264      11.381   4.596  27.854  1.00 1.667           C  
ANISOU  732  C   PRO A 264     9252   4604   4665   -465    447   -393       C  
ATOM    733  O   PRO A 264      12.102   4.144  28.743  1.00 1.667           O  
ANISOU  733  O   PRO A 264     8952   4427   4375   -496    379   -408       O  
ATOM    734  CB  PRO A 264      10.922   7.001  28.552  1.00 1.667           C  
ANISOU  734  CB  PRO A 264     9511   4366   4546   -569    483   -471       C  
ATOM    735  CG  PRO A 264      10.854   7.100  30.021  1.00 1.667           C  
ANISOU  735  CG  PRO A 264    10090   4849   4953   -576    446   -517       C  
ATOM    736  CD  PRO A 264       9.757   6.226  30.509  1.00 1.667           C  
ANISOU  736  CD  PRO A 264     9581   4360   4443   -429    481   -492       C  
ATOM    737  N   GLY A 265      11.418   4.164  26.591  1.00-0.760           N  
ANISOU  737  N   GLY A 265     8790   4261   4361   -438    478   -353       N  
ATOM    738  CA  GLY A 265      12.384   3.185  26.115  1.00-0.760           C  
ANISOU  738  CA  GLY A 265     8508   4256   4277   -444    444   -329       C  
ATOM    739  C   GLY A 265      12.047   1.738  26.417  1.00-0.760           C  
ANISOU  739  C   GLY A 265     8887   4764   4737   -331    432   -300       C  
ATOM    740  O   GLY A 265      12.803   0.848  26.019  1.00-0.760           O  
ANISOU  740  O   GLY A 265     8866   4951   4868   -313    409   -278       O  
ATOM    741  N   ALA A 266      10.906   1.473  27.093  1.00-0.442           N  
ANISOU  741  N   ALA A 266     8184   3932   3929   -251    454   -297       N  
ATOM    742  CA  ALA A 266      10.499   0.102  27.393  1.00-0.442           C  
ANISOU  742  CA  ALA A 266     7964   3801   3765   -156    449   -265       C  
ATOM    743  C   ALA A 266      10.011  -0.613  26.113  1.00-0.442           C  
ANISOU  743  C   ALA A 266     8280   4174   4201    -96    496   -230       C  
ATOM    744  O   ALA A 266      10.336  -1.781  25.904  1.00-0.442           O  
ANISOU  744  O   ALA A 266     8046   4069   4066    -49    480   -206       O  
ATOM    745  CB  ALA A 266       9.424   0.076  28.483  1.00-0.442           C  
ANISOU  745  CB  ALA A 266     8107   3799   3759   -104    467   -270       C  
ATOM    746  N   TRP A 267       9.252   0.080  25.247  1.00-0.577           N  
ANISOU  746  N   TRP A 267     7903   3693   3804    -94    550   -226       N  
ATOM    747  CA  TRP A 267       8.761  -0.530  23.993  1.00-0.577           C  
ANISOU  747  CA  TRP A 267     7903   3743   3900    -47    588   -195       C  
ATOM    748  C   TRP A 267       9.171   0.399  22.832  1.00-0.577           C  
ANISOU  748  C   TRP A 267     8338   4160   4357   -104    611   -197       C  
ATOM    749  O   TRP A 267       8.331   1.115  22.281  1.00-0.577           O  
ANISOU  749  O   TRP A 267     8402   4103   4363    -90    651   -188       O  
ATOM    750  CB  TRP A 267       7.238  -0.786  24.102  1.00-0.577           C  
ANISOU  750  CB  TRP A 267     7832   3584   3781     24    628   -176       C  
ATOM    751  CG  TRP A 267       6.874  -1.381  25.430  1.00-0.577           C  
ANISOU  751  CG  TRP A 267     7970   3705   3856     58    613   -177       C  
ATOM    752  CD1 TRP A 267       6.337  -0.726  26.505  1.00-0.577           C  
ANISOU  752  CD1 TRP A 267     8423   4041   4181     63    624   -194       C  
ATOM    753  CD2 TRP A 267       7.226  -2.691  25.892  1.00-0.577           C  
ANISOU  753  CD2 TRP A 267     7886   3712   3816     86    582   -161       C  
ATOM    754  NE1 TRP A 267       6.259  -1.579  27.585  1.00-0.577           N  
ANISOU  754  NE1 TRP A 267     8281   3922   4000     90    605   -187       N  
ATOM    755  CE2 TRP A 267       6.794  -2.792  27.236  1.00-0.577           C  
ANISOU  755  CE2 TRP A 267     8354   4115   4175    104    577   -163       C  
ATOM    756  CE3 TRP A 267       7.821  -3.817  25.280  1.00-0.577           C  
ANISOU  756  CE3 TRP A 267     7912   3851   3946    107    565   -143       C  
ATOM    757  CZ2 TRP A 267       6.952  -3.958  27.983  1.00-0.577           C  
ANISOU  757  CZ2 TRP A 267     8223   4025   4034    136    550   -142       C  
ATOM    758  CZ3 TRP A 267       7.959  -4.981  26.022  1.00-0.577           C  
ANISOU  758  CZ3 TRP A 267     8116   4082   4140    147    539   -125       C  
ATOM    759  CH2 TRP A 267       7.558  -5.033  27.364  1.00-0.577           C  
ANISOU  759  CH2 TRP A 267     8266   4165   4180    158    529   -121       C  
ATOM    760  N   PRO A 268      10.493   0.470  22.504  1.00-1.400           N  
ANISOU  760  N   PRO A 268     7747   3693   3844   -170    588   -205       N  
ATOM    761  CA  PRO A 268      10.955   1.490  21.545  1.00-1.400           C  
ANISOU  761  CA  PRO A 268     7787   3701   3882   -245    614   -206       C  
ATOM    762  C   PRO A 268      10.581   1.273  20.065  1.00-1.400           C  
ANISOU  762  C   PRO A 268     8115   4044   4259   -213    661   -177       C  
ATOM    763  O   PRO A 268      10.754   2.187  19.262  1.00-1.400           O  
ANISOU  763  O   PRO A 268     7988   3850   4098   -268    690   -169       O  
ATOM    764  CB  PRO A 268      12.470   1.522  21.776  1.00-1.400           C  
ANISOU  764  CB  PRO A 268     7906   3988   4086   -329    574   -221       C  
ATOM    765  CG  PRO A 268      12.800   0.124  22.205  1.00-1.400           C  
ANISOU  765  CG  PRO A 268     8290   4544   4570   -256    540   -213       C  
ATOM    766  CD  PRO A 268      11.637  -0.282  23.070  1.00-1.400           C  
ANISOU  766  CD  PRO A 268     7724   3850   3909   -181    536   -212       C  
ATOM    767  N   TRP A 269      10.044   0.097  19.716  1.00-1.224           N  
ANISOU  767  N   TRP A 269     7530   3526   3733   -131    668   -160       N  
ATOM    768  CA  TRP A 269       9.570  -0.238  18.372  1.00-1.224           C  
ANISOU  768  CA  TRP A 269     7443   3446   3671    -98    704   -137       C  
ATOM    769  C   TRP A 269       8.121   0.196  18.183  1.00-1.224           C  
ANISOU  769  C   TRP A 269     7813   3673   3956    -54    724   -120       C  
ATOM    770  O   TRP A 269       7.625   0.164  17.058  1.00-1.224           O  
ANISOU  770  O   TRP A 269     7623   3472   3764    -34    748    -99       O  
ATOM    771  CB  TRP A 269       9.659  -1.753  18.154  1.00-1.224           C  
ANISOU  771  CB  TRP A 269     7241   3362   3552    -36    697   -134       C  
ATOM    772  CG  TRP A 269       9.299  -2.535  19.378  1.00-1.224           C  
ANISOU  772  CG  TRP A 269     7353   3471   3656      9    665   -138       C  
ATOM    773  CD1 TRP A 269       8.047  -2.871  19.812  1.00-1.224           C  
ANISOU  773  CD1 TRP A 269     7696   3730   3947     54    669   -128       C  
ATOM    774  CD2 TRP A 269      10.214  -3.048  20.348  1.00-1.224           C  
ANISOU  774  CD2 TRP A 269     7278   3487   3621     12    626   -149       C  
ATOM    775  NE1 TRP A 269       8.131  -3.560  20.997  1.00-1.224           N  
ANISOU  775  NE1 TRP A 269     7550   3599   3792     79    640   -131       N  
ATOM    776  CE2 TRP A 269       9.451  -3.689  21.347  1.00-1.224           C  
ANISOU  776  CE2 TRP A 269     7720   3870   4013     59    609   -143       C  
ATOM    777  CE3 TRP A 269      11.615  -3.044  20.461  1.00-1.224           C  
ANISOU  777  CE3 TRP A 269     7344   3699   3767    -20    603   -159       C  
ATOM    778  CZ2 TRP A 269      10.042  -4.371  22.409  1.00-1.224           C  
ANISOU  778  CZ2 TRP A 269     7657   3864   3958     82    568   -144       C  
ATOM    779  CZ3 TRP A 269      12.196  -3.704  21.533  1.00-1.224           C  
ANISOU  779  CZ3 TRP A 269     7469   3904   3917      8    555   -160       C  
ATOM    780  CH2 TRP A 269      11.415  -4.355  22.487  1.00-1.224           C  
ANISOU  780  CH2 TRP A 269     7612   3961   3989     61    536   -152       C  
ATOM    781  N   GLN A 270       7.424   0.553  19.284  1.00-1.046           N  
ANISOU  781  N   GLN A 270     7576   3342   3650    -32    716   -127       N  
ATOM    782  CA  GLN A 270       6.027   0.977  19.199  1.00-1.046           C  
ANISOU  782  CA  GLN A 270     7653   3314   3663     24    739   -108       C  
ATOM    783  C   GLN A 270       5.862   2.307  18.467  1.00-1.046           C  
ANISOU  783  C   GLN A 270     7927   3455   3855      7    766    -94       C  
ATOM    784  O   GLN A 270       6.547   3.287  18.787  1.00-1.046           O  
ANISOU  784  O   GLN A 270     8116   3546   3973    -54    767   -111       O  
ATOM    785  CB  GLN A 270       5.369   1.049  20.587  1.00-1.046           C  
ANISOU  785  CB  GLN A 270     7810   3408   3760     59    735   -121       C  
ATOM    786  CG  GLN A 270       3.919   1.570  20.593  1.00-1.046           C  
ANISOU  786  CG  GLN A 270     7981   3493   3875    129    768   -100       C  
ATOM    787  CD  GLN A 270       2.857   0.562  20.182  1.00-1.046           C  
ANISOU  787  CD  GLN A 270     8841   4460   4814    183    773    -72       C  
ATOM    788  OE1 GLN A 270       2.197   0.646  19.138  1.00-1.046           O  
ANISOU  788  OE1 GLN A 270     8126   3769   4125    209    782    -44       O  
ATOM    789  NE2 GLN A 270       2.640  -0.393  20.998  1.00-1.046           N  
ANISOU  789  NE2 GLN A 270     7740   3421   3742    194    764    -76       N  
ATOM    790  N   VAL A 271       4.932   2.333  17.492  1.00-0.895           N  
ANISOU  790  N   VAL A 271     7198   2717   3124     57    783    -61       N  
ATOM    791  CA  VAL A 271       4.552   3.557  16.788  1.00-0.895           C  
ANISOU  791  CA  VAL A 271     7320   2697   3152     66    807    -35       C  
ATOM    792  C   VAL A 271       3.043   3.806  16.890  1.00-0.895           C  
ANISOU  792  C   VAL A 271     7877   3209   3678    165    819     -7       C  
ATOM    793  O   VAL A 271       2.254   2.867  17.029  1.00-0.895           O  
ANISOU  793  O   VAL A 271     7642   3097   3521    211    809      0       O  
ATOM    794  CB  VAL A 271       5.055   3.696  15.316  1.00-0.895           C  
ANISOU  794  CB  VAL A 271     7794   3189   3628     29    818     -9       C  
ATOM    795  CG1 VAL A 271       6.557   3.929  15.247  1.00-0.895           C  
ANISOU  795  CG1 VAL A 271     7946   3360   3792    -73    822    -31       C  
ATOM    796  CG2 VAL A 271       4.623   2.537  14.429  1.00-0.895           C  
ANISOU  796  CG2 VAL A 271     7467   3008   3383     63    807      6       C  
ATOM    797  N   SER A 272       2.653   5.077  16.790  1.00-1.139           N  
ANISOU  797  N   SER A 272     7779   2937   3465    196    843     10       N  
ATOM    798  CA  SER A 272       1.261   5.507  16.723  1.00-1.139           C  
ANISOU  798  CA  SER A 272     7661   2780   3316    306    859     45       C  
ATOM    799  C   SER A 272       1.072   5.955  15.258  1.00-1.139           C  
ANISOU  799  C   SER A 272     8223   3312   3846    322    858     94       C  
ATOM    800  O   SER A 272       1.825   6.795  14.758  1.00-1.139           O  
ANISOU  800  O   SER A 272     8117   3060   3643    269    872    101       O  
ATOM    801  CB  SER A 272       1.016   6.681  17.662  1.00-1.139           C  
ANISOU  801  CB  SER A 272     8022   2931   3542    346    891     30       C  
ATOM    802  OG  SER A 272      -0.299   7.186  17.501  1.00-1.139           O  
ANISOU  802  OG  SER A 272     8513   3389   4005    470    913     69       O  
ATOM    803  N   LEU A 273       0.084   5.365  14.575  1.00-0.791           N  
ANISOU  803  N   LEU A 273     7867   3100   3565    384    840    130       N  
ATOM    804  CA  LEU A 273      -0.216   5.700  13.187  1.00-0.791           C  
ANISOU  804  CA  LEU A 273     7756   2981   3417    408    830    180       C  
ATOM    805  C   LEU A 273      -1.457   6.596  13.138  1.00-0.791           C  
ANISOU  805  C   LEU A 273     8440   3596   4045    533    840    228       C  
ATOM    806  O   LEU A 273      -2.541   6.201  13.590  1.00-0.791           O  
ANISOU  806  O   LEU A 273     8372   3663   4063    610    833    238       O  
ATOM    807  CB  LEU A 273      -0.367   4.438  12.337  1.00-0.791           C  
ANISOU  807  CB  LEU A 273     7638   3068   3403    382    794    185       C  
ATOM    808  CG  LEU A 273       0.839   3.459  12.355  1.00-0.791           C  
ANISOU  808  CG  LEU A 273     8112   3614   3934    282    790    138       C  
ATOM    809  CD1 LEU A 273       0.472   2.114  11.747  1.00-0.791           C  
ANISOU  809  CD1 LEU A 273     8016   3692   3925    272    759    134       C  
ATOM    810  CD2 LEU A 273       2.045   4.066  11.678  1.00-0.791           C  
ANISOU  810  CD2 LEU A 273     8376   3774   4120    211    811    138       C  
ATOM    811  N   HIS A 274      -1.272   7.818  12.611  1.00-0.256           N  
ANISOU  811  N   HIS A 274     8185   3129   3643    555    859    262       N  
ATOM    812  CA  HIS A 274      -2.301   8.830  12.516  1.00-0.256           C  
ANISOU  812  CA  HIS A 274     8301   3131   3674    687    873    312       C  
ATOM    813  C   HIS A 274      -2.916   9.015  11.142  1.00-0.256           C  
ANISOU  813  C   HIS A 274     9132   4008   4482    748    843    384       C  
ATOM    814  O   HIS A 274      -2.229   8.892  10.130  1.00-0.256           O  
ANISOU  814  O   HIS A 274     9088   3950   4397    671    829    398       O  
ATOM    815  CB  HIS A 274      -1.731  10.184  12.990  1.00-0.256           C  
ANISOU  815  CB  HIS A 274     8552   3052   3736    682    919    303       C  
ATOM    816  CG  HIS A 274      -1.529  10.297  14.478  1.00-0.256           C  
ANISOU  816  CG  HIS A 274     8980   3403   4148    670    948    240       C  
ATOM    817  ND1 HIS A 274      -1.682  11.506  15.135  1.00-0.256           N  
ANISOU  817  ND1 HIS A 274     9294   3435   4292    729    991    233       N  
ATOM    818  CD2 HIS A 274      -1.166   9.354  15.382  1.00-0.256           C  
ANISOU  818  CD2 HIS A 274     9078   3650   4357    605    939    184       C  
ATOM    819  CE1 HIS A 274      -1.417  11.257  16.409  1.00-0.256           C  
ANISOU  819  CE1 HIS A 274     9243   3383   4253    694   1005    169       C  
ATOM    820  NE2 HIS A 274      -1.120   9.969  16.604  1.00-0.256           N  
ANISOU  820  NE2 HIS A 274     9118   3520   4299    622    973    142       N  
ATOM    821  N   VAL A 275      -4.214   9.391  11.129  1.00 1.683           N  
ANISOU  821  N   VAL A 275     9017   3944   4383    895    837    433       N  
ATOM    822  CA  VAL A 275      -5.009   9.829   9.977  1.00 1.683           C  
ANISOU  822  CA  VAL A 275     9175   4127   4499    992    804    514       C  
ATOM    823  C   VAL A 275      -5.784  11.081  10.455  1.00 1.683           C  
ANISOU  823  C   VAL A 275    10231   5004   5453   1156    842    553       C  
ATOM    824  O   VAL A 275      -6.412  11.043  11.515  1.00 1.683           O  
ANISOU  824  O   VAL A 275     9992   4829   5287   1229    869    530       O  
ATOM    825  CB  VAL A 275      -5.946   8.750   9.359  1.00 1.683           C  
ANISOU  825  CB  VAL A 275     9491   4785   4985   1012    740    538       C  
ATOM    826  CG1 VAL A 275      -6.897   9.370   8.316  1.00 1.683           C  
ANISOU  826  CG1 VAL A 275     9490   4816   4933   1138    701    628       C  
ATOM    827  CG2 VAL A 275      -5.135   7.636   8.709  1.00 1.683           C  
ANISOU  827  CG2 VAL A 275     9338   4742   4878    864    709    501       C  
ATOM    828  N   GLN A 276      -5.738  12.175   9.682  1.00 1.212           N  
ANISOU  828  N   GLN A 276    10432   4968   5474   1217    848    615       N  
ATOM    829  CA  GLN A 276      -6.425  13.443  10.021  1.00 1.212           C  
ANISOU  829  CA  GLN A 276    10706   5017   5613   1387    888    658       C  
ATOM    830  C   GLN A 276      -6.111  13.896  11.455  1.00 1.212           C  
ANISOU  830  C   GLN A 276    11343   5453   6186   1384    955    589       C  
ATOM    831  O   GLN A 276      -7.018  14.251  12.225  1.00 1.212           O  
ANISOU  831  O   GLN A 276    11359   5473   6218   1532    989    592       O  
ATOM    832  CB  GLN A 276      -7.949  13.375   9.751  1.00 1.212           C  
ANISOU  832  CB  GLN A 276    10782   5343   5810   1572    854    726       C  
ATOM    833  CG  GLN A 276      -8.326  13.298   8.268  1.00 1.212           C  
ANISOU  833  CG  GLN A 276    12922   7599   7940   1604    783    809       C  
ATOM    834  CD  GLN A 276      -9.805  13.523   8.059  1.00 1.212           C  
ANISOU  834  CD  GLN A 276    15900  10777  11004   1808    752    885       C  
ATOM    835  OE1 GLN A 276     -10.346  14.610   8.329  1.00 1.212           O  
ANISOU  835  OE1 GLN A 276    15734  10418  10725   1981    791    931       O  
ATOM    836  NE2 GLN A 276     -10.494  12.500   7.573  1.00 1.212           N  
ANISOU  836  NE2 GLN A 276    14266   9537   9571   1795    680    902       N  
ATOM    837  N   ASN A 277      -4.806  13.817  11.817  1.00 2.447           N  
ANISOU  837  N   ASN A 277    10848   4808   5626   1211    974    524       N  
ATOM    838  CA  ASN A 277      -4.231  14.245  13.089  1.00 2.447           C  
ANISOU  838  CA  ASN A 277    10843   4587   5528   1162   1026    450       C  
ATOM    839  C   ASN A 277      -4.730  13.453  14.334  1.00 2.447           C  
ANISOU  839  C   ASN A 277    10854   4816   5698   1189   1037    393       C  
ATOM    840  O   ASN A 277      -4.595  13.949  15.445  1.00 2.447           O  
ANISOU  840  O   ASN A 277    10869   4646   5614   1201   1084    342       O  
ATOM    841  CB  ASN A 277      -4.432  15.780  13.270  1.00 2.447           C  
ANISOU  841  CB  ASN A 277    11877   5210   6305   1270   1079    476       C  
ATOM    842  CG  ASN A 277      -3.499  16.421  14.266  1.00 2.447           C  
ANISOU  842  CG  ASN A 277    16451   9469  10709   1166   1125    400       C  
ATOM    843  OD1 ASN A 277      -2.292  16.549  14.034  1.00 2.447           O  
ANISOU  843  OD1 ASN A 277    16555   9438  10734    992   1120    376       O  
ATOM    844  ND2 ASN A 277      -4.042  16.834  15.402  1.00 2.447           N  
ANISOU  844  ND2 ASN A 277    15336   8244   9536   1266   1170    361       N  
ATOM    845  N   VAL A 278      -5.251  12.211  14.170  1.00 1.445           N  
ANISOU  845  N   VAL A 278     9928   4264   4999   1182    996    398       N  
ATOM    846  CA  VAL A 278      -5.702  11.401  15.315  1.00 1.445           C  
ANISOU  846  CA  VAL A 278     9618   4160   4833   1192   1009    351       C  
ATOM    847  C   VAL A 278      -5.194   9.952  15.194  1.00 1.445           C  
ANISOU  847  C   VAL A 278     9504   4311   4891   1049    963    319       C  
ATOM    848  O   VAL A 278      -5.101   9.432  14.079  1.00 1.445           O  
ANISOU  848  O   VAL A 278     9268   4209   4720   1004    915    351       O  
ATOM    849  CB  VAL A 278      -7.242  11.443  15.574  1.00 1.445           C  
ANISOU  849  CB  VAL A 278    10190   4916   5505   1375   1027    395       C  
ATOM    850  CG1 VAL A 278      -7.775  12.883  15.662  1.00 1.445           C  
ANISOU  850  CG1 VAL A 278    10377   4830   5514   1545   1078    430       C  
ATOM    851  CG2 VAL A 278      -8.017  10.631  14.533  1.00 1.445           C  
ANISOU  851  CG2 VAL A 278    10022   5085   5521   1396    964    454       C  
ATOM    852  N   HIS A 279      -4.894   9.302  16.343  1.00-0.861           N  
ANISOU  852  N   HIS A 279     8565   3433   4008    987    979    258       N  
ATOM    853  CA  HIS A 279      -4.438   7.910  16.372  1.00-0.861           C  
ANISOU  853  CA  HIS A 279     8207   3297   3796    868    941    228       C  
ATOM    854  C   HIS A 279      -5.538   7.016  15.813  1.00-0.861           C  
ANISOU  854  C   HIS A 279     8726   4118   4488    915    908    270       C  
ATOM    855  O   HIS A 279      -6.704   7.118  16.236  1.00-0.861           O  
ANISOU  855  O   HIS A 279     8648   4154   4473   1026    930    295       O  
ATOM    856  CB  HIS A 279      -4.120   7.480  17.843  1.00-0.861           C  
ANISOU  856  CB  HIS A 279     7977   3063   3574    826    967    165       C  
ATOM    857  CG  HIS A 279      -3.812   6.019  17.990  1.00-0.861           C  
ANISOU  857  CG  HIS A 279     8013   3318   3754    731    933    142       C  
ATOM    858  ND1 HIS A 279      -2.527   5.532  17.828  1.00-0.861           N  
ANISOU  858  ND1 HIS A 279     8046   3326   3782    607    905    108       N  
ATOM    859  CD2 HIS A 279      -4.643   4.979  18.248  1.00-0.861           C  
ANISOU  859  CD2 HIS A 279     7935   3476   3818    747    926    153       C  
ATOM    860  CE1 HIS A 279      -2.610   4.232  18.046  1.00-0.861           C  
ANISOU  860  CE1 HIS A 279     7810   3283   3671    565    883     98       C  
ATOM    861  NE2 HIS A 279      -3.866   3.853  18.277  1.00-0.861           N  
ANISOU  861  NE2 HIS A 279     7794   3418   3739    636    894    124       N  
ATOM    862  N   VAL A 280      -5.146   6.097  14.924  1.00 0.754           N  
ANISOU  862  N   VAL A 280     8242   3769   4080    822    858    273       N  
ATOM    863  CA  VAL A 280      -6.024   5.112  14.316  1.00 0.754           C  
ANISOU  863  CA  VAL A 280     8143   3945   4131    826    815    302       C  
ATOM    864  C   VAL A 280      -5.562   3.683  14.664  1.00 0.754           C  
ANISOU  864  C   VAL A 280     8444   4376   4528    709    796    256       C  
ATOM    865  O   VAL A 280      -6.378   2.850  15.048  1.00 0.754           O  
ANISOU  865  O   VAL A 280     8083   4210   4287    711    790    260       O  
ATOM    866  CB  VAL A 280      -6.133   5.321  12.771  1.00 0.754           C  
ANISOU  866  CB  VAL A 280     8782   4606   4741    835    768    352       C  
ATOM    867  CG1 VAL A 280      -6.883   4.164  12.099  1.00 0.754           C  
ANISOU  867  CG1 VAL A 280     8621   4722   4718    802    711    369       C  
ATOM    868  CG2 VAL A 280      -6.801   6.657  12.442  1.00 0.754           C  
ANISOU  868  CG2 VAL A 280     8848   4561   4717    974    782    411       C  
ATOM    869  N   CYS A 281      -4.262   3.413  14.539  1.00-1.466           N  
ANISOU  869  N   CYS A 281     8151   3976   4181    611    791    217       N  
ATOM    870  CA  CYS A 281      -3.709   2.071  14.701  1.00-1.466           C  
ANISOU  870  CA  CYS A 281     8199   4120   4301    513    771    179       C  
ATOM    871  C   CYS A 281      -2.308   2.110  15.283  1.00-1.466           C  
ANISOU  871  C   CYS A 281     8083   3867   4124    445    787    132       C  
ATOM    872  O   CYS A 281      -1.668   3.153  15.264  1.00-1.466           O  
ANISOU  872  O   CYS A 281     7914   3533   3855    445    806    129       O  
ATOM    873  CB  CYS A 281      -3.723   1.355  13.337  1.00-1.466           C  
ANISOU  873  CB  CYS A 281     8515   4537   4647    467    725    193       C  
ATOM    874  SG  CYS A 281      -5.243   0.406  13.013  1.00-1.466           S  
ANISOU  874  SG  CYS A 281     8999   5275   5260    481    685    223       S  
ATOM    875  N   GLY A 282      -1.831   0.950  15.727  1.00-1.377           N  
ANISOU  875  N   GLY A 282     7758   3615   3858    382    776     99       N  
ATOM    876  CA  GLY A 282      -0.481   0.758  16.243  1.00-1.377           C  
ANISOU  876  CA  GLY A 282     7740   3523   3811    318    780     57       C  
ATOM    877  C   GLY A 282       0.389   0.150  15.156  1.00-1.377           C  
ANISOU  877  C   GLY A 282     7989   3806   4074    258    760     49       C  
ATOM    878  O   GLY A 282      -0.134  -0.289  14.135  1.00-1.377           O  
ANISOU  878  O   GLY A 282     7793   3682   3900    262    741     69       O  
ATOM    879  N   GLY A 283       1.701   0.120  15.384  1.00-1.056           N  
ANISOU  879  N   GLY A 283     7439   3212   3509    206    764     19       N  
ATOM    880  CA  GLY A 283       2.699  -0.446  14.481  1.00-1.056           C  
ANISOU  880  CA  GLY A 283     7208   3021   3295    157    759      6       C  
ATOM    881  C   GLY A 283       3.987  -0.792  15.202  1.00-1.056           C  
ANISOU  881  C   GLY A 283     7776   3604   3890    115    759    -28       C  
ATOM    882  O   GLY A 283       4.219  -0.320  16.328  1.00-1.056           O  
ANISOU  882  O   GLY A 283     7631   3412   3727    110    760    -42       O  
ATOM    883  N   SER A 284       4.836  -1.620  14.545  1.00-0.928           N  
ANISOU  883  N   SER A 284     7305   3203   3457     89    758    -43       N  
ATOM    884  CA  SER A 284       6.129  -2.108  15.058  1.00-0.928           C  
ANISOU  884  CA  SER A 284     7212   3168   3414     63    756    -70       C  
ATOM    885  C   SER A 284       7.274  -1.831  14.089  1.00-0.928           C  
ANISOU  885  C   SER A 284     7585   3581   3796     23    779    -74       C  
ATOM    886  O   SER A 284       7.231  -2.286  12.937  1.00-0.928           O  
ANISOU  886  O   SER A 284     7585   3606   3788     30    794    -69       O  
ATOM    887  CB  SER A 284       6.062  -3.605  15.324  1.00-0.928           C  
ANISOU  887  CB  SER A 284     7268   3282   3514     93    741    -83       C  
ATOM    888  OG  SER A 284       5.040  -3.854  16.266  1.00-0.928           O  
ANISOU  888  OG  SER A 284     8035   4020   4271    118    727    -76       O  
ATOM    889  N   ILE A 285       8.272  -1.045  14.542  1.00-0.963           N  
ANISOU  889  N   ILE A 285     7233   3236   3455    -28    784    -82       N  
ATOM    890  CA  ILE A 285       9.459  -0.673  13.739  1.00-0.963           C  
ANISOU  890  CA  ILE A 285     7097   3163   3343    -83    813    -83       C  
ATOM    891  C   ILE A 285      10.308  -1.944  13.586  1.00-0.963           C  
ANISOU  891  C   ILE A 285     7332   3548   3671    -56    816   -102       C  
ATOM    892  O   ILE A 285      10.647  -2.553  14.591  1.00-0.963           O  
ANISOU  892  O   ILE A 285     7041   3317   3436    -34    787   -117       O  
ATOM    893  CB  ILE A 285      10.293   0.457  14.440  1.00-0.963           C  
ANISOU  893  CB  ILE A 285     7377   3424   3617   -162    810    -90       C  
ATOM    894  CG1 ILE A 285       9.495   1.775  14.579  1.00-0.963           C  
ANISOU  894  CG1 ILE A 285     7450   3304   3567   -181    815    -73       C  
ATOM    895  CG2 ILE A 285      11.631   0.738  13.705  1.00-0.963           C  
ANISOU  895  CG2 ILE A 285     7203   3361   3495   -235    842    -89       C  
ATOM    896  CD1 ILE A 285      10.089   2.732  15.697  1.00-0.963           C  
ANISOU  896  CD1 ILE A 285     7486   3274   3567   -254    798    -95       C  
ATOM    897  N   ILE A 286      10.649  -2.311  12.345  1.00-0.866           N  
ANISOU  897  N   ILE A 286     7073   3336   3413    -51    853    -99       N  
ATOM    898  CA  ILE A 286      11.533  -3.441  12.025  1.00-0.866           C  
ANISOU  898  CA  ILE A 286     6983   3375   3397    -13    871   -118       C  
ATOM    899  C   ILE A 286      12.843  -2.949  11.373  1.00-0.866           C  
ANISOU  899  C   ILE A 286     7507   4026   3977    -64    918   -116       C  
ATOM    900  O   ILE A 286      13.873  -3.597  11.542  1.00-0.866           O  
ANISOU  900  O   ILE A 286     7315   3988   3884    -39    929   -130       O  
ATOM    901  CB  ILE A 286      10.854  -4.596  11.262  1.00-0.866           C  
ANISOU  901  CB  ILE A 286     7323   3667   3686     49    879   -128       C  
ATOM    902  CG1 ILE A 286      10.115  -4.088  10.012  1.00-0.866           C  
ANISOU  902  CG1 ILE A 286     7338   3595   3598     28    899   -111       C  
ATOM    903  CG2 ILE A 286       9.919  -5.392  12.239  1.00-0.866           C  
ANISOU  903  CG2 ILE A 286     7248   3524   3601     94    833   -133       C  
ATOM    904  CD1 ILE A 286       9.898  -5.146   8.928  1.00-0.866           C  
ANISOU  904  CD1 ILE A 286     7499   3738   3700     67    919   -128       C  
ATOM    905  N   THR A 287      12.836  -1.765  10.703  1.00-0.268           N  
ANISOU  905  N   THR A 287     7387   3847   3795   -137    946    -93       N  
ATOM    906  CA  THR A 287      14.042  -1.159  10.109  1.00-0.268           C  
ANISOU  906  CA  THR A 287     7263   3838   3716   -210    997    -85       C  
ATOM    907  C   THR A 287      13.889   0.355  10.246  1.00-0.268           C  
ANISOU  907  C   THR A 287     7937   4388   4314   -306    996    -60       C  
ATOM    908  O   THR A 287      12.797   0.781  10.641  1.00-0.268           O  
ANISOU  908  O   THR A 287     7875   4156   4162   -289    962    -52       O  
ATOM    909  CB  THR A 287      14.285  -1.608   8.606  1.00-0.268           C  
ANISOU  909  CB  THR A 287     7793   4407   4208   -187   1064    -80       C  
ATOM    910  OG1 THR A 287      13.467  -0.851   7.707  1.00-0.268           O  
ANISOU  910  OG1 THR A 287     7862   4313   4132   -215   1079    -51       O  
ATOM    911  CG2 THR A 287      14.138  -3.112   8.349  1.00-0.268           C  
ANISOU  911  CG2 THR A 287     7240   3892   3669    -82   1066   -108       C  
ATOM    912  N   PRO A 288      14.877   1.223   9.881  1.00 1.218           N  
ANISOU  912  N   PRO A 288     7872   4386   4268   -409   1037    -46       N  
ATOM    913  CA  PRO A 288      14.612   2.676   9.966  1.00 1.218           C  
ANISOU  913  CA  PRO A 288     8016   4346   4298   -501   1037    -22       C  
ATOM    914  C   PRO A 288      13.484   3.153   9.033  1.00 1.218           C  
ANISOU  914  C   PRO A 288     8582   4699   4697   -469   1054     13       C  
ATOM    915  O   PRO A 288      13.021   4.281   9.198  1.00 1.218           O  
ANISOU  915  O   PRO A 288     8543   4466   4544   -511   1048     35       O  
ATOM    916  CB  PRO A 288      15.957   3.333   9.577  1.00 1.218           C  
ANISOU  916  CB  PRO A 288     8191   4649   4529   -627   1088    -10       C  
ATOM    917  CG  PRO A 288      16.964   2.249   9.585  1.00 1.218           C  
ANISOU  917  CG  PRO A 288     8556   5302   5072   -592   1101    -33       C  
ATOM    918  CD  PRO A 288      16.239   0.953   9.367  1.00 1.218           C  
ANISOU  918  CD  PRO A 288     7989   4732   4503   -447   1090    -48       C  
ATOM    919  N   GLU A 289      13.052   2.331   8.050  1.00 0.335           N  
ANISOU  919  N   GLU A 289     8001   4145   4092   -395   1074     18       N  
ATOM    920  CA  GLU A 289      11.989   2.781   7.142  1.00 0.335           C  
ANISOU  920  CA  GLU A 289     8132   4098   4066   -364   1078     55       C  
ATOM    921  C   GLU A 289      10.779   1.848   7.058  1.00 0.335           C  
ANISOU  921  C   GLU A 289     8492   4434   4407   -258   1035     45       C  
ATOM    922  O   GLU A 289       9.762   2.249   6.507  1.00 0.335           O  
ANISOU  922  O   GLU A 289     8562   4374   4362   -226   1021     77       O  
ATOM    923  CB  GLU A 289      12.527   3.114   5.725  1.00 0.335           C  
ANISOU  923  CB  GLU A 289     8405   4375   4259   -412   1147     88       C  
ATOM    924  CG  GLU A 289      13.508   2.114   5.145  1.00 0.335           C  
ANISOU  924  CG  GLU A 289     9916   6096   5865   -405   1196     62       C  
ATOM    925  CD  GLU A 289      14.143   2.489   3.815  1.00 0.335           C  
ANISOU  925  CD  GLU A 289    13840  10038   9709   -460   1277     93       C  
ATOM    926  OE1 GLU A 289      14.098   3.683   3.430  1.00 0.335           O  
ANISOU  926  OE1 GLU A 289    12546   8600   8296   -534   1300    140       O  
ATOM    927  OE2 GLU A 289      14.698   1.578   3.159  1.00 0.335           O  
ANISOU  927  OE2 GLU A 289    13765  10108   9677   -424   1323     71       O  
ATOM    928  N   TRP A 290      10.847   0.652   7.654  1.00-0.970           N  
ANISOU  928  N   TRP A 290     7860   3920   3882   -206   1011      5       N  
ATOM    929  CA  TRP A 290       9.760  -0.316   7.588  1.00-0.970           C  
ANISOU  929  CA  TRP A 290     7719   3758   3723   -125    972     -7       C  
ATOM    930  C   TRP A 290       9.042  -0.535   8.914  1.00-0.970           C  
ANISOU  930  C   TRP A 290     7962   3976   4016    -89    919    -20       C  
ATOM    931  O   TRP A 290       9.682  -0.703   9.956  1.00-0.970           O  
ANISOU  931  O   TRP A 290     7442   3522   3584   -100    909    -42       O  
ATOM    932  CB  TRP A 290      10.254  -1.643   7.009  1.00-0.970           C  
ANISOU  932  CB  TRP A 290     7473   3620   3514    -89    995    -39       C  
ATOM    933  CG  TRP A 290      10.543  -1.581   5.526  1.00-0.970           C  
ANISOU  933  CG  TRP A 290     7614   3758   3562   -104   1047    -27       C  
ATOM    934  CD1 TRP A 290      11.771  -1.535   4.929  1.00-0.970           C  
ANISOU  934  CD1 TRP A 290     7992   4236   3965   -138   1114    -30       C  
ATOM    935  CD2 TRP A 290       9.579  -1.622   4.464  1.00-0.970           C  
ANISOU  935  CD2 TRP A 290     7607   3657   3419    -85   1035     -9       C  
ATOM    936  NE1 TRP A 290      11.634  -1.581   3.553  1.00-0.970           N  
ANISOU  936  NE1 TRP A 290     8050   4251   3896   -137   1152    -18       N  
ATOM    937  CE2 TRP A 290      10.297  -1.627   3.242  1.00-0.970           C  
ANISOU  937  CE2 TRP A 290     8211   4288   3950   -106   1099     -5       C  
ATOM    938  CE3 TRP A 290       8.174  -1.661   4.426  1.00-0.970           C  
ANISOU  938  CE3 TRP A 290     7745   3709   3492    -52    976      6       C  
ATOM    939  CZ2 TRP A 290       9.658  -1.674   1.997  1.00-0.970           C  
ANISOU  939  CZ2 TRP A 290     8084   4084   3668    -97   1100     11       C  
ATOM    940  CZ3 TRP A 290       7.541  -1.689   3.192  1.00-0.970           C  
ANISOU  940  CZ3 TRP A 290     7974   3884   3587    -44    969     24       C  
ATOM    941  CH2 TRP A 290       8.279  -1.720   1.995  1.00-0.970           C  
ANISOU  941  CH2 TRP A 290     8079   3998   3602    -67   1028     25       C  
ATOM    942  N   ILE A 291       7.702  -0.524   8.851  1.00-0.975           N  
ANISOU  942  N   ILE A 291     7613   3547   3609    -46    886     -3       N  
ATOM    943  CA  ILE A 291       6.781  -0.704   9.981  1.00-0.975           C  
ANISOU  943  CA  ILE A 291     7426   3336   3455     -7    844     -8       C  
ATOM    944  C   ILE A 291       5.797  -1.840   9.668  1.00-0.975           C  
ANISOU  944  C   ILE A 291     7749   3689   3780     38    815    -15       C  
ATOM    945  O   ILE A 291       5.215  -1.858   8.583  1.00-0.975           O  
ANISOU  945  O   ILE A 291     7855   3778   3819     46    810      3       O  
ATOM    946  CB  ILE A 291       6.044   0.624  10.326  1.00-0.975           C  
ANISOU  946  CB  ILE A 291     7790   3577   3753     -1    837     25       C  
ATOM    947  CG1 ILE A 291       7.034   1.676  10.914  1.00-0.975           C  
ANISOU  947  CG1 ILE A 291     7773   3501   3723    -62    859     21       C  
ATOM    948  CG2 ILE A 291       4.839   0.400  11.301  1.00-0.975           C  
ANISOU  948  CG2 ILE A 291     7672   3449   3660     56    803     25       C  
ATOM    949  CD1 ILE A 291       6.603   3.129  10.763  1.00-0.975           C  
ANISOU  949  CD1 ILE A 291     7683   3240   3517    -70    871     57       C  
ATOM    950  N   VAL A 292       5.590  -2.756  10.634  1.00-0.494           N  
ANISOU  950  N   VAL A 292     7150   3129   3246     60    793    -39       N  
ATOM    951  CA  VAL A 292       4.642  -3.862  10.513  1.00-0.494           C  
ANISOU  951  CA  VAL A 292     7129   3125   3226     84    766    -47       C  
ATOM    952  C   VAL A 292       3.348  -3.401  11.168  1.00-0.494           C  
ANISOU  952  C   VAL A 292     7546   3527   3651    105    739    -21       C  
ATOM    953  O   VAL A 292       3.400  -2.890  12.278  1.00-0.494           O  
ANISOU  953  O   VAL A 292     7662   3623   3793    114    742    -19       O  
ATOM    954  CB  VAL A 292       5.185  -5.159  11.197  1.00-0.494           C  
ANISOU  954  CB  VAL A 292     7682   3708   3829     95    764    -81       C  
ATOM    955  CG1 VAL A 292       4.148  -6.277  11.165  1.00-0.494           C  
ANISOU  955  CG1 VAL A 292     7716   3728   3848    101    737    -88       C  
ATOM    956  CG2 VAL A 292       6.469  -5.637  10.534  1.00-0.494           C  
ANISOU  956  CG2 VAL A 292     7650   3709   3798     95    797   -106       C  
ATOM    957  N   THR A 293       2.194  -3.590  10.513  1.00-1.153           N  
ANISOU  957  N   THR A 293     6850   2850   2930    115    714     -2       N  
ATOM    958  CA  THR A 293       0.879  -3.216  11.068  1.00-1.153           C  
ANISOU  958  CA  THR A 293     6676   2703   2784    145    693     27       C  
ATOM    959  C   THR A 293      -0.157  -4.239  10.610  1.00-1.153           C  
ANISOU  959  C   THR A 293     7326   3427   3450    130    657     28       C  
ATOM    960  O   THR A 293       0.237  -5.268  10.084  1.00-1.153           O  
ANISOU  960  O   THR A 293     7369   3462   3467     97    652     -3       O  
ATOM    961  CB  THR A 293       0.540  -1.708  10.768  1.00-1.153           C  
ANISOU  961  CB  THR A 293     6972   2950   3034    180    700     68       C  
ATOM    962  OG1 THR A 293      -0.569  -1.277  11.576  1.00-1.153           O  
ANISOU  962  OG1 THR A 293     7425   3430   3524    228    693     92       O  
ATOM    963  CG2 THR A 293       0.314  -1.396   9.258  1.00-1.153           C  
ANISOU  963  CG2 THR A 293     6696   2671   2684    179    685     96       C  
ATOM    964  N   ALA A 294      -1.458  -4.003  10.851  1.00-1.476           N  
ANISOU  964  N   ALA A 294     6979   3154   3144    153    635     59       N  
ATOM    965  CA  ALA A 294      -2.496  -4.949  10.435  1.00-1.476           C  
ANISOU  965  CA  ALA A 294     6881   3151   3071    120    595     61       C  
ATOM    966  C   ALA A 294      -3.109  -4.515   9.104  1.00-1.476           C  
ANISOU  966  C   ALA A 294     7465   3786   3611    126    557     90       C  
ATOM    967  O   ALA A 294      -3.273  -3.312   8.846  1.00-1.476           O  
ANISOU  967  O   ALA A 294     7356   3667   3481    181    561    129       O  
ATOM    968  CB  ALA A 294      -3.578  -5.055  11.511  1.00-1.476           C  
ANISOU  968  CB  ALA A 294     6951   3315   3233    134    594     82       C  
ATOM    969  N   ALA A 295      -3.436  -5.489   8.242  1.00-1.298           N  
ANISOU  969  N   ALA A 295     7195   3551   3305     69    519     72       N  
ATOM    970  CA  ALA A 295      -4.068  -5.204   6.964  1.00-1.298           C  
ANISOU  970  CA  ALA A 295     7192   3608   3247     66    470     98       C  
ATOM    971  C   ALA A 295      -5.437  -4.543   7.145  1.00-1.298           C  
ANISOU  971  C   ALA A 295     7816   4388   3958    111    434    154       C  
ATOM    972  O   ALA A 295      -5.832  -3.749   6.288  1.00-1.298           O  
ANISOU  972  O   ALA A 295     7746   4355   3845    153    404    196       O  
ATOM    973  CB  ALA A 295      -4.210  -6.491   6.139  1.00-1.298           C  
ANISOU  973  CB  ALA A 295     7307   3723   3296    -17    432     57       C  
ATOM    974  N   HIS A 296      -6.171  -4.867   8.242  1.00-1.474           N  
ANISOU  974  N   HIS A 296     7371   4043   3631    109    440    160       N  
ATOM    975  CA  HIS A 296      -7.485  -4.256   8.465  1.00-1.474           C  
ANISOU  975  CA  HIS A 296     7298   4151   3661    164    416    215       C  
ATOM    976  C   HIS A 296      -7.395  -2.751   8.718  1.00-1.474           C  
ANISOU  976  C   HIS A 296     7683   4482   4035    280    450    257       C  
ATOM    977  O   HIS A 296      -8.386  -2.050   8.490  1.00-1.474           O  
ANISOU  977  O   HIS A 296     7575   4503   3975    351    424    311       O  
ATOM    978  CB  HIS A 296      -8.301  -4.977   9.558  1.00-1.474           C  
ANISOU  978  CB  HIS A 296     7229   4213   3720    129    426    213       C  
ATOM    979  CG  HIS A 296      -7.985  -4.583  10.961  1.00-1.474           C  
ANISOU  979  CG  HIS A 296     7679   4598   4209    180    494    210       C  
ATOM    980  ND1 HIS A 296      -7.141  -5.342  11.751  1.00-1.474           N  
ANISOU  980  ND1 HIS A 296     7912   4704   4413    131    530    165       N  
ATOM    981  CD2 HIS A 296      -8.484  -3.573  11.707  1.00-1.474           C  
ANISOU  981  CD2 HIS A 296     7827   4795   4414    277    529    246       C  
ATOM    982  CE1 HIS A 296      -7.113  -4.738  12.918  1.00-1.474           C  
ANISOU  982  CE1 HIS A 296     7816   4586   4351    191    581    175       C  
ATOM    983  NE2 HIS A 296      -7.891  -3.660  12.929  1.00-1.474           N  
ANISOU  983  NE2 HIS A 296     7783   4645   4363    279    586    219       N  
ATOM    984  N   CYS A 297      -6.225  -2.258   9.187  1.00-1.466           N  
ANISOU  984  N   CYS A 297     7413   4024   3697    298    505    234       N  
ATOM    985  CA  CYS A 297      -5.993  -0.825   9.441  1.00-1.466           C  
ANISOU  985  CA  CYS A 297     7744   4247   3982    390    541    266       C  
ATOM    986  C   CYS A 297      -5.976  -0.009   8.145  1.00-1.466           C  
ANISOU  986  C   CYS A 297     7966   4421   4102    427    514    307       C  
ATOM    987  O   CYS A 297      -6.310   1.178   8.163  1.00-1.466           O  
ANISOU  987  O   CYS A 297     7877   4282   3980    520    526    354       O  
ATOM    988  CB  CYS A 297      -4.688  -0.616  10.197  1.00-1.466           C  
ANISOU  988  CB  CYS A 297     8169   4493   4355    371    597    225       C  
ATOM    989  SG  CYS A 297      -4.710  -1.218  11.895  1.00-1.466           S  
ANISOU  989  SG  CYS A 297     8835   5182   5108    357    634    191       S  
ATOM    990  N   VAL A 298      -5.530  -0.633   7.049  1.00-0.432           N  
ANISOU  990  N   VAL A 298     7606   4050   3672    358    483    289       N  
ATOM    991  CA  VAL A 298      -5.348   0.030   5.761  1.00-0.432           C  
ANISOU  991  CA  VAL A 298     7709   4087   3648    378    461    325       C  
ATOM    992  C   VAL A 298      -6.380  -0.383   4.721  1.00-0.432           C  
ANISOU  992  C   VAL A 298     8227   4769   4167    371    381    354       C  
ATOM    993  O   VAL A 298      -6.170  -0.154   3.541  1.00-0.432           O  
ANISOU  993  O   VAL A 298     8239   4734   4055    364    354    374       O  
ATOM    994  CB  VAL A 298      -3.898  -0.118   5.240  1.00-0.432           C  
ANISOU  994  CB  VAL A 298     8307   4525   4133    313    499    286       C  
ATOM    995  CG1 VAL A 298      -2.946   0.705   6.083  1.00-0.432           C  
ANISOU  995  CG1 VAL A 298     8321   4385   4131    330    567    278       C  
ATOM    996  CG2 VAL A 298      -3.449  -1.584   5.168  1.00-0.432           C  
ANISOU  996  CG2 VAL A 298     8229   4484   4076    223    494    221       C  
ATOM    997  N   GLU A 299      -7.526  -0.895   5.155  1.00 1.385           N  
ANISOU  997  N   GLU A 299     7981   4724   4055    373    341    363       N  
ATOM    998  CA  GLU A 299      -8.622  -1.224   4.243  1.00 1.385           C  
ANISOU  998  CA  GLU A 299     8106   5045   4201    363    254    396       C  
ATOM    999  C   GLU A 299      -9.154   0.089   3.661  1.00 1.385           C  
ANISOU  999  C   GLU A 299     8519   5473   4566    484    229    478       C  
ATOM   1000  O   GLU A 299      -8.976   1.122   4.291  1.00 1.385           O  
ANISOU 1000  O   GLU A 299     8384   5227   4426    578    284    506       O  
ATOM   1001  CB  GLU A 299      -9.755  -1.916   5.020  1.00 1.385           C  
ANISOU 1001  CB  GLU A 299     8257   5431   4534    340    229    396       C  
ATOM   1002  CG  GLU A 299      -9.955  -3.363   4.598  1.00 1.385           C  
ANISOU 1002  CG  GLU A 299     9930   7191   6213    202    177    346       C  
ATOM   1003  CD  GLU A 299     -11.054  -4.060   5.372  1.00 1.385           C  
ANISOU 1003  CD  GLU A 299    11710   9196   8169    158    159    348       C  
ATOM   1004  OE1 GLU A 299     -12.242  -3.892   5.012  1.00 1.385           O  
ANISOU 1004  OE1 GLU A 299    13753  11488  10311    181     96    399       O  
ATOM   1005  OE2 GLU A 299     -10.727  -4.775   6.343  1.00 1.385           O  
ANISOU 1005  OE2 GLU A 299     8610   6034   5110     99    209    304       O  
ATOM   1006  N   LYS A 300      -9.811   0.052   2.487  1.00 1.276           N  
ANISOU 1006  N   LYS A 300     8456   5530   4454    485    145    516       N  
ATOM   1007  CA  LYS A 300     -10.405   1.246   1.864  1.00 1.276           C  
ANISOU 1007  CA  LYS A 300     8618   5717   4562    612    109    605       C  
ATOM   1008  C   LYS A 300     -11.318   1.963   2.876  1.00 1.276           C  
ANISOU 1008  C   LYS A 300     9734   6956   5833    740    130    654       C  
ATOM   1009  O   LYS A 300     -11.969   1.280   3.676  1.00 1.276           O  
ANISOU 1009  O   LYS A 300     9864   7281   6138    710    129    631       O  
ATOM   1010  CB  LYS A 300     -11.178   0.880   0.580  1.00 1.276           C  
ANISOU 1010  CB  LYS A 300     8788   6069   4691    584     -4    637       C  
ATOM   1011  CG  LYS A 300     -10.281   0.394  -0.544  1.00 1.276           C  
ANISOU 1011  CG  LYS A 300     9946   7071   5648    485    -18    598       C  
ATOM   1012  CD  LYS A 300     -11.004   0.298  -1.880  1.00 1.276           C  
ANISOU 1012  CD  LYS A 300    10894   8158   6505    479   -131    642       C  
ATOM   1013  CE  LYS A 300     -10.529  -0.867  -2.723  1.00 1.276           C  
ANISOU 1013  CE  LYS A 300    12105   9327   7586    332   -165    570       C  
ATOM   1014  NZ  LYS A 300      -9.084  -0.781  -3.075  1.00 1.276           N  
ANISOU 1014  NZ  LYS A 300    13504  10435   8797    299    -82    531       N  
ATOM   1015  N   PRO A 301     -11.306   3.314   2.977  1.00 2.693           N  
ANISOU 1015  N   PRO A 301     9542   6624   5570    882    165    715       N  
ATOM   1016  CA  PRO A 301     -10.611   4.298   2.132  1.00 2.693           C  
ANISOU 1016  CA  PRO A 301     9601   6431   5414    928    177    756       C  
ATOM   1017  C   PRO A 301      -9.204   4.705   2.603  1.00 2.693           C  
ANISOU 1017  C   PRO A 301     9812   6323   5508    887    275    711       C  
ATOM   1018  O   PRO A 301      -8.656   5.681   2.091  1.00 2.693           O  
ANISOU 1018  O   PRO A 301    10010   6294   5534    930    301    752       O  
ATOM   1019  CB  PRO A 301     -11.595   5.468   2.141  1.00 2.693           C  
ANISOU 1019  CB  PRO A 301     9850   6733   5676   1112    158    851       C  
ATOM   1020  CG  PRO A 301     -12.140   5.453   3.558  1.00 2.693           C  
ANISOU 1020  CG  PRO A 301    10385   7381   6398   1171    209    833       C  
ATOM   1021  CD  PRO A 301     -12.170   3.992   3.970  1.00 2.693           C  
ANISOU 1021  CD  PRO A 301     9683   6865   5843   1019    197    755       C  
ATOM   1022  N   LEU A 302      -8.598   3.942   3.519  1.00 1.824           N  
ANISOU 1022  N   LEU A 302     8928   5424   4708    794    324    632       N  
ATOM   1023  CA  LEU A 302      -7.273   4.265   4.062  1.00 1.824           C  
ANISOU 1023  CA  LEU A 302     8791   5033   4490    747    409    587       C  
ATOM   1024  C   LEU A 302      -6.165   3.401   3.479  1.00 1.824           C  
ANISOU 1024  C   LEU A 302     8963   5144   4594    612    417    528       C  
ATOM   1025  O   LEU A 302      -5.131   3.192   4.113  1.00 1.824           O  
ANISOU 1025  O   LEU A 302     8733   4801   4366    548    476    473       O  
ATOM   1026  CB  LEU A 302      -7.289   4.204   5.610  1.00 1.824           C  
ANISOU 1026  CB  LEU A 302     8714   4961   4537    761    464    546       C  
ATOM   1027  CG  LEU A 302      -8.321   5.085   6.309  1.00 1.824           C  
ANISOU 1027  CG  LEU A 302     9141   5431   5023    906    477    595       C  
ATOM   1028  CD1 LEU A 302      -8.359   4.789   7.800  1.00 1.824           C  
ANISOU 1028  CD1 LEU A 302     9165   5484   5162    902    531    546       C  
ATOM   1029  CD2 LEU A 302      -8.078   6.591   6.020  1.00 1.824           C  
ANISOU 1029  CD2 LEU A 302     9088   5120   4798   1008    509    652       C  
ATOM   1030  N   ASN A 303      -6.358   2.935   2.248  1.00 1.631           N  
ANISOU 1030  N   ASN A 303     8591   4847   4151    574    357    541       N  
ATOM   1031  CA  ASN A 303      -5.360   2.110   1.579  1.00 1.631           C  
ANISOU 1031  CA  ASN A 303     8639   4835   4114    461    369    486       C  
ATOM   1032  C   ASN A 303      -4.197   2.916   1.017  1.00 1.631           C  
ANISOU 1032  C   ASN A 303     9215   5185   4522    447    429    501       C  
ATOM   1033  O   ASN A 303      -3.078   2.402   0.949  1.00 1.631           O  
ANISOU 1033  O   ASN A 303     9200   5099   4476    364    477    446       O  
ATOM   1034  CB  ASN A 303      -5.996   1.215   0.514  1.00 1.631           C  
ANISOU 1034  CB  ASN A 303     8760   5109   4205    415    286    482       C  
ATOM   1035  CG  ASN A 303      -6.833   1.945  -0.490  1.00 1.631           C  
ANISOU 1035  CG  ASN A 303    10898   7297   6252    490    217    565       C  
ATOM   1036  OD1 ASN A 303      -7.730   2.722  -0.143  1.00 1.631           O  
ANISOU 1036  OD1 ASN A 303     9737   6210   5159    598    194    628       O  
ATOM   1037  ND2 ASN A 303      -6.571   1.686  -1.764  1.00 1.631           N  
ANISOU 1037  ND2 ASN A 303    10673   7038   5864    443    184    568       N  
ATOM   1038  N   ASN A 304      -4.450   4.177   0.640  1.00 1.625           N  
ANISOU 1038  N   ASN A 304     8864   4722   4064    531    429    578       N  
ATOM   1039  CA  ASN A 304      -3.445   5.062   0.058  1.00 1.625           C  
ANISOU 1039  CA  ASN A 304     8906   4536   3929    512    486    607       C  
ATOM   1040  C   ASN A 304      -2.480   5.592   1.115  1.00 1.625           C  
ANISOU 1040  C   ASN A 304     9371   4843   4422    484    570    575       C  
ATOM   1041  O   ASN A 304      -2.932   5.940   2.197  1.00 1.625           O  
ANISOU 1041  O   ASN A 304     9325   4798   4471    542    578    573       O  
ATOM   1042  CB  ASN A 304      -4.120   6.176  -0.718  1.00 1.625           C  
ANISOU 1042  CB  ASN A 304     9222   4768   4102    612    451    706       C  
ATOM   1043  CG  ASN A 304      -4.767   5.738  -2.019  1.00 1.625           C  
ANISOU 1043  CG  ASN A 304    12193   7866   6990    617    367    741       C  
ATOM   1044  OD1 ASN A 304      -4.579   4.615  -2.522  1.00 1.625           O  
ANISOU 1044  OD1 ASN A 304    11135   6920   5940    529    343    685       O  
ATOM   1045  ND2 ASN A 304      -5.544   6.640  -2.607  1.00 1.625           N  
ANISOU 1045  ND2 ASN A 304    11718   7364   6418    726    319    834       N  
ATOM   1046  N   PRO A 305      -1.156   5.654   0.847  1.00 1.115           N  
ANISOU 1046  N   PRO A 305     9131   4481   4102    393    634    549       N  
ATOM   1047  CA  PRO A 305      -0.212   6.114   1.886  1.00 1.115           C  
ANISOU 1047  CA  PRO A 305     9120   4349   4129    350    704    515       C  
ATOM   1048  C   PRO A 305      -0.303   7.587   2.288  1.00 1.115           C  
ANISOU 1048  C   PRO A 305     9223   4230   4133    405    734    569       C  
ATOM   1049  O   PRO A 305       0.136   7.933   3.378  1.00 1.115           O  
ANISOU 1049  O   PRO A 305     8833   3760   3792    385    772    535       O  
ATOM   1050  CB  PRO A 305       1.173   5.819   1.278  1.00 1.115           C  
ANISOU 1050  CB  PRO A 305     9435   4627   4383    239    760    485       C  
ATOM   1051  CG  PRO A 305       0.925   4.973   0.083  1.00 1.115           C  
ANISOU 1051  CG  PRO A 305    10036   5338   4930    228    724    484       C  
ATOM   1052  CD  PRO A 305      -0.444   5.286  -0.393  1.00 1.115           C  
ANISOU 1052  CD  PRO A 305     9461   4796   4307    322    648    547       C  
ATOM   1053  N   TRP A 306      -0.870   8.450   1.444  1.00 0.304           N  
ANISOU 1053  N   TRP A 306     8848   3742   3606    477    714    651       N  
ATOM   1054  CA  TRP A 306      -0.926   9.897   1.774  1.00 0.304           C  
ANISOU 1054  CA  TRP A 306     9099   3729   3726    535    749    705       C  
ATOM   1055  C   TRP A 306      -1.662  10.209   3.070  1.00 0.304           C  
ANISOU 1055  C   TRP A 306     9618   4242   4344    628    745    690       C  
ATOM   1056  O   TRP A 306      -1.337  11.194   3.740  1.00 0.304           O  
ANISOU 1056  O   TRP A 306     9524   3917   4167    636    794    694       O  
ATOM   1057  CB  TRP A 306      -1.467  10.745   0.621  1.00 0.304           C  
ANISOU 1057  CB  TRP A 306     9129   3626   3561    615    725    806       C  
ATOM   1058  CG  TRP A 306      -2.894  10.509   0.225  1.00 0.304           C  
ANISOU 1058  CG  TRP A 306     9233   3904   3710    748    640    855       C  
ATOM   1059  CD1 TRP A 306      -3.332   9.730  -0.798  1.00 0.304           C  
ANISOU 1059  CD1 TRP A 306     9518   4382   3998    743    574    869       C  
ATOM   1060  CD2 TRP A 306      -4.059  11.161   0.760  1.00 0.304           C  
ANISOU 1060  CD2 TRP A 306     9249   3910   3754    906    611    903       C  
ATOM   1061  NE1 TRP A 306      -4.703   9.805  -0.897  1.00 0.304           N  
ANISOU 1061  NE1 TRP A 306     9381   4387   3913    878    498    922       N  
ATOM   1062  CE2 TRP A 306      -5.171  10.701   0.023  1.00 0.304           C  
ANISOU 1062  CE2 TRP A 306     9582   4473   4134    988    523    948       C  
ATOM   1063  CE3 TRP A 306      -4.270  12.106   1.778  1.00 0.304           C  
ANISOU 1063  CE3 TRP A 306     9617   4094   4104    991    654    911       C  
ATOM   1064  CZ2 TRP A 306      -6.472  11.154   0.265  1.00 0.304           C  
ANISOU 1064  CZ2 TRP A 306     9543   4520   4149   1157    476   1007       C  
ATOM   1065  CZ3 TRP A 306      -5.570  12.522   2.053  1.00 0.304           C  
ANISOU 1065  CZ3 TRP A 306     9808   4350   4338   1166    617    963       C  
ATOM   1066  CH2 TRP A 306      -6.650  12.071   1.281  1.00 0.304           C  
ANISOU 1066  CH2 TRP A 306     9739   4540   4336   1252    530   1015       C  
ATOM   1067  N   HIS A 307      -2.627   9.355   3.437  1.00 2.460           N  
ANISOU 1067  N   HIS A 307     9163   4037   4058    688    693    670       N  
ATOM   1068  CA  HIS A 307      -3.427   9.548   4.640  1.00 2.460           C  
ANISOU 1068  CA  HIS A 307     9066   3976   4066    783    694    657       C  
ATOM   1069  C   HIS A 307      -2.602   9.461   5.921  1.00 2.460           C  
ANISOU 1069  C   HIS A 307     9216   4054   4274    706    748    580       C  
ATOM   1070  O   HIS A 307      -2.957  10.072   6.925  1.00 2.460           O  
ANISOU 1070  O   HIS A 307     9219   3957   4275    776    775    574       O  
ATOM   1071  CB  HIS A 307      -4.470   8.423   4.722  1.00 2.460           C  
ANISOU 1071  CB  HIS A 307     8985   4217   4172    820    632    644       C  
ATOM   1072  CG  HIS A 307      -5.545   8.464   3.694  1.00 2.460           C  
ANISOU 1072  CG  HIS A 307     9388   4751   4557    911    562    717       C  
ATOM   1073  ND1 HIS A 307      -6.584   9.364   3.780  1.00 2.460           N  
ANISOU 1073  ND1 HIS A 307     9680   5019   4825   1070    547    787       N  
ATOM   1074  CD2 HIS A 307      -5.754   7.657   2.633  1.00 2.460           C  
ANISOU 1074  CD2 HIS A 307     9592   5126   4769    867    499    726       C  
ATOM   1075  CE1 HIS A 307      -7.384   9.084   2.770  1.00 2.460           C  
ANISOU 1075  CE1 HIS A 307     9515   5034   4669   1116    470    842       C  
ATOM   1076  NE2 HIS A 307      -6.922   8.073   2.047  1.00 2.460           N  
ANISOU 1076  NE2 HIS A 307     9533   5164   4696    990    437    805       N  
ATOM   1077  N   TRP A 308      -1.542   8.651   5.898  1.00 0.385           N  
ANISOU 1077  N   TRP A 308     8423   3327   3534    573    762    522       N  
ATOM   1078  CA  TRP A 308      -0.825   8.230   7.091  1.00 0.385           C  
ANISOU 1078  CA  TRP A 308     8354   3275   3559    499    793    446       C  
ATOM   1079  C   TRP A 308       0.451   8.944   7.439  1.00 0.385           C  
ANISOU 1079  C   TRP A 308     8826   3542   3938    403    846    421       C  
ATOM   1080  O   TRP A 308       1.247   9.265   6.564  1.00 0.385           O  
ANISOU 1080  O   TRP A 308     8822   3448   3835    330    868    442       O  
ATOM   1081  CB  TRP A 308      -0.513   6.727   6.978  1.00 0.385           C  
ANISOU 1081  CB  TRP A 308     8014   3172   3363    425    768    394       C  
ATOM   1082  CG  TRP A 308      -1.715   5.848   6.808  1.00 0.385           C  
ANISOU 1082  CG  TRP A 308     7942   3318   3400    486    713    403       C  
ATOM   1083  CD1 TRP A 308      -2.254   5.407   5.634  1.00 0.385           C  
ANISOU 1083  CD1 TRP A 308     8257   3745   3698    498    665    436       C  
ATOM   1084  CD2 TRP A 308      -2.494   5.263   7.857  1.00 0.385           C  
ANISOU 1084  CD2 TRP A 308     7782   3299   3380    527    699    377       C  
ATOM   1085  NE1 TRP A 308      -3.329   4.579   5.891  1.00 0.385           N  
ANISOU 1085  NE1 TRP A 308     8031   3730   3604    535    617    430       N  
ATOM   1086  CE2 TRP A 308      -3.511   4.494   7.249  1.00 0.385           C  
ANISOU 1086  CE2 TRP A 308     8207   3927   3880    555    642    397       C  
ATOM   1087  CE3 TRP A 308      -2.436   5.314   9.270  1.00 0.385           C  
ANISOU 1087  CE3 TRP A 308     7906   3397   3564    535    729    338       C  
ATOM   1088  CZ2 TRP A 308      -4.431   3.738   8.004  1.00 0.385           C  
ANISOU 1088  CZ2 TRP A 308     7914   3821   3734    579    620    381       C  
ATOM   1089  CZ3 TRP A 308      -3.342   4.570  10.006  1.00 0.385           C  
ANISOU 1089  CZ3 TRP A 308     7863   3530   3654    570    712    324       C  
ATOM   1090  CH2 TRP A 308      -4.340   3.816   9.378  1.00 0.385           C  
ANISOU 1090  CH2 TRP A 308     7809   3682   3684    591    661    348       C  
ATOM   1091  N   THR A 309       0.658   9.091   8.769  1.00 0.559           N  
ANISOU 1091  N   THR A 309     8557   3221   3709    392    867    372       N  
ATOM   1092  CA  THR A 309       1.839   9.623   9.460  1.00 0.559           C  
ANISOU 1092  CA  THR A 309     8686   3196   3783    287    906    330       C  
ATOM   1093  C   THR A 309       2.119   8.742  10.694  1.00 0.559           C  
ANISOU 1093  C   THR A 309     9106   3765   4349    252    897    259       C  
ATOM   1094  O   THR A 309       1.180   8.240  11.323  1.00 0.559           O  
ANISOU 1094  O   THR A 309     8946   3715   4274    335    878    249       O  
ATOM   1095  CB  THR A 309       1.719  11.123   9.813  1.00 0.559           C  
ANISOU 1095  CB  THR A 309     9590   3782   4502    321    940    355       C  
ATOM   1096  OG1 THR A 309       0.538  11.338  10.562  1.00 0.559           O  
ANISOU 1096  OG1 THR A 309     9649   3821   4569    459    934    360       O  
ATOM   1097  CG2 THR A 309       1.720  12.028   8.586  1.00 0.559           C  
ANISOU 1097  CG2 THR A 309     9774   3778   4513    332    955    430       C  
ATOM   1098  N   ALA A 310       3.414   8.530  11.000  1.00-0.805           N  
ANISOU 1098  N   ALA A 310     8611   3290   3884    129    910    214       N  
ATOM   1099  CA  ALA A 310       3.893   7.711  12.108  1.00-0.805           C  
ANISOU 1099  CA  ALA A 310     8320   3133   3715     87    897    152       C  
ATOM   1100  C   ALA A 310       4.613   8.521  13.181  1.00-0.805           C  
ANISOU 1100  C   ALA A 310     8931   3582   4252     18    914    113       C  
ATOM   1101  O   ALA A 310       5.423   9.404  12.857  1.00-0.805           O  
ANISOU 1101  O   ALA A 310     9051   3548   4268    -69    938    121       O  
ATOM   1102  CB  ALA A 310       4.810   6.618  11.578  1.00-0.805           C  
ANISOU 1102  CB  ALA A 310     8284   3299   3796     12    890    131       C  
ATOM   1103  N   PHE A 311       4.326   8.203  14.474  1.00 0.478           N  
ANISOU 1103  N   PHE A 311     8461   3145   3825     48    900     71       N  
ATOM   1104  CA  PHE A 311       4.967   8.841  15.637  1.00 0.478           C  
ANISOU 1104  CA  PHE A 311     8377   2922   3664    -18    906     24       C  
ATOM   1105  C   PHE A 311       5.704   7.772  16.459  1.00 0.478           C  
ANISOU 1105  C   PHE A 311     8659   3410   4082    -75    874    -25       C  
ATOM   1106  O   PHE A 311       5.101   6.789  16.926  1.00 0.478           O  
ANISOU 1106  O   PHE A 311     8356   3254   3876     -7    857    -33       O  
ATOM   1107  CB  PHE A 311       3.952   9.627  16.495  1.00 0.478           C  
ANISOU 1107  CB  PHE A 311     8618   2967   3783     79    924     19       C  
ATOM   1108  CG  PHE A 311       3.373  10.843  15.799  1.00 0.478           C  
ANISOU 1108  CG  PHE A 311     8914   3015   3916    140    956     67       C  
ATOM   1109  CD1 PHE A 311       2.236  10.737  15.004  1.00 0.478           C  
ANISOU 1109  CD1 PHE A 311     9239   3394   4266    266    958    125       C  
ATOM   1110  CD2 PHE A 311       3.960  12.100  15.950  1.00 0.478           C  
ANISOU 1110  CD2 PHE A 311     9257   3063   4070     68    981     57       C  
ATOM   1111  CE1 PHE A 311       1.706  11.868  14.355  1.00 0.478           C  
ANISOU 1111  CE1 PHE A 311     9381   3304   4249    337    983    178       C  
ATOM   1112  CE2 PHE A 311       3.403  13.237  15.338  1.00 0.478           C  
ANISOU 1112  CE2 PHE A 311     9800   3339   4438    136   1014    107       C  
ATOM   1113  CZ  PHE A 311       2.277  13.112  14.551  1.00 0.478           C  
ANISOU 1113  CZ  PHE A 311     9571   3173   4239    279   1014    170       C  
ATOM   1114  N   ALA A 312       7.022   7.969  16.605  1.00-0.099           N  
ANISOU 1114  N   ALA A 312     8236   2999   3664   -202    867    -52       N  
ATOM   1115  CA  ALA A 312       7.947   7.072  17.304  1.00-0.099           C  
ANISOU 1115  CA  ALA A 312     8001   2964   3554   -262    833    -92       C  
ATOM   1116  C   ALA A 312       8.592   7.802  18.485  1.00-0.099           C  
ANISOU 1116  C   ALA A 312     8805   3651   4269   -347    816   -139       C  
ATOM   1117  O   ALA A 312       8.844   9.003  18.400  1.00-0.099           O  
ANISOU 1117  O   ALA A 312     8824   3455   4146   -415    835   -141       O  
ATOM   1118  CB  ALA A 312       9.038   6.606  16.340  1.00-0.099           C  
ANISOU 1118  CB  ALA A 312     7888   3027   3552   -338    837    -80       C  
ATOM   1119  N   GLY A 313       8.885   7.062  19.548  1.00-1.376           N  
ANISOU 1119  N   GLY A 313     8405   3381   3937   -349    777   -174       N  
ATOM   1120  CA  GLY A 313       9.558   7.566  20.746  1.00-1.376           C  
ANISOU 1120  CA  GLY A 313     8600   3505   4054   -435    745   -223       C  
ATOM   1121  C   GLY A 313       8.827   8.583  21.596  1.00-1.376           C  
ANISOU 1121  C   GLY A 313     9191   3812   4442   -409    761   -249       C  
ATOM   1122  O   GLY A 313       9.451   9.234  22.441  1.00-1.376           O  
ANISOU 1122  O   GLY A 313     9205   3714   4348   -504    738   -294       O  
ATOM   1123  N   ILE A 314       7.508   8.726  21.384  1.00 0.182           N  
ANISOU 1123  N   ILE A 314     8802   3309   3996   -280    801   -223       N  
ATOM   1124  CA  ILE A 314       6.630   9.667  22.105  1.00 0.182           C  
ANISOU 1124  CA  ILE A 314     8799   3034   3799   -215    833   -242       C  
ATOM   1125  C   ILE A 314       5.556   8.810  22.794  1.00 0.182           C  
ANISOU 1125  C   ILE A 314     9018   3362   4074    -85    839   -239       C  
ATOM   1126  O   ILE A 314       4.862   8.051  22.112  1.00 0.182           O  
ANISOU 1126  O   ILE A 314     8647   3148   3832     -2    849   -195       O  
ATOM   1127  CB  ILE A 314       6.008  10.697  21.109  1.00 0.182           C  
ANISOU 1127  CB  ILE A 314     9239   3254   4127   -166    883   -200       C  
ATOM   1128  CG1 ILE A 314       7.102  11.527  20.387  1.00 0.182           C  
ANISOU 1128  CG1 ILE A 314     9466   3363   4288   -311    884   -196       C  
ATOM   1129  CG2 ILE A 314       5.018  11.625  21.843  1.00 0.182           C  
ANISOU 1129  CG2 ILE A 314     9245   2978   3934    -67    924   -217       C  
ATOM   1130  CD1 ILE A 314       6.630  12.279  19.003  1.00 0.182           C  
ANISOU 1130  CD1 ILE A 314     9495   3233   4242   -267    929   -131       C  
ATOM   1131  N   LEU A 315       5.455   8.883  24.143  1.00 0.373           N  
ANISOU 1131  N   LEU A 315     8539   2808   3496    -78    832   -285       N  
ATOM   1132  CA  LEU A 315       4.500   8.060  24.905  1.00 0.373           C  
ANISOU 1132  CA  LEU A 315     8437   2811   3436     30    845   -282       C  
ATOM   1133  C   LEU A 315       3.090   8.624  24.893  1.00 0.373           C  
ANISOU 1133  C   LEU A 315     9169   3409   4087    168    910   -261       C  
ATOM   1134  O   LEU A 315       2.123   7.875  25.022  1.00 0.373           O  
ANISOU 1134  O   LEU A 315     9044   3430   4055    265    930   -234       O  
ATOM   1135  CB  LEU A 315       4.961   7.911  26.379  1.00 0.373           C  
ANISOU 1135  CB  LEU A 315     8408   2756   3314    -17    814   -337       C  
ATOM   1136  CG  LEU A 315       6.348   7.256  26.603  1.00 0.373           C  
ANISOU 1136  CG  LEU A 315     8954   3476   3953   -138    740   -355       C  
ATOM   1137  CD1 LEU A 315       6.748   7.284  28.094  1.00 0.373           C  
ANISOU 1137  CD1 LEU A 315     8881   3349   3750   -181    704   -409       C  
ATOM   1138  CD2 LEU A 315       6.397   5.811  26.059  1.00 0.373           C  
ANISOU 1138  CD2 LEU A 315     8691   3501   3912   -105    719   -312       C  
ATOM   1139  N   ARG A 316       2.979   9.943  24.704  1.00 0.290           N  
ANISOU 1139  N   ARG A 316     8907   2872   3652    177    944   -270       N  
ATOM   1140  CA  ARG A 316       1.736  10.686  24.831  1.00 0.290           C  
ANISOU 1140  CA  ARG A 316     8993   2787   3623    320   1009   -257       C  
ATOM   1141  C   ARG A 316       1.199  11.267  23.536  1.00 0.290           C  
ANISOU 1141  C   ARG A 316     9496   3226   4137    390   1035   -198       C  
ATOM   1142  O   ARG A 316       1.911  11.999  22.855  1.00 0.290           O  
ANISOU 1142  O   ARG A 316     9494   3066   4055    311   1026   -193       O  
ATOM   1143  CB  ARG A 316       1.934  11.788  25.889  1.00 0.290           C  
ANISOU 1143  CB  ARG A 316     9037   2508   3404    300   1034   -322       C  
ATOM   1144  CG  ARG A 316       2.106  11.177  27.307  1.00 0.290           C  
ANISOU 1144  CG  ARG A 316     9804   3346   4140    274   1017   -375       C  
ATOM   1145  CD  ARG A 316       2.259  12.222  28.390  1.00 0.290           C  
ANISOU 1145  CD  ARG A 316    10279   3495   4331    255   1040   -446       C  
ATOM   1146  NE  ARG A 316       1.029  12.997  28.529  1.00 0.290           N  
ANISOU 1146  NE  ARG A 316    10141   3157   4059    421   1127   -439       N  
ATOM   1147  CZ  ARG A 316       0.875  14.027  29.338  1.00 0.290           C  
ANISOU 1147  CZ  ARG A 316    11091   3774   4735    450   1172   -497       C  
ATOM   1148  NH1 ARG A 316       1.886  14.444  30.091  1.00 0.290           N  
ANISOU 1148  NH1 ARG A 316     9909   2408   3371    305   1131   -570       N  
ATOM   1149  NH2 ARG A 316      -0.291  14.658  29.400  1.00 0.290           N  
ANISOU 1149  NH2 ARG A 316    10914   3444   4457    626   1259   -483       N  
ATOM   1150  N   GLN A 317      -0.100  11.038  23.268  1.00-0.232           N  
ANISOU 1150  N   GLN A 317     9009   2846   3730    542   1071   -152       N  
ATOM   1151  CA  GLN A 317      -0.805  11.587  22.101  1.00-0.232           C  
ANISOU 1151  CA  GLN A 317     9052   2845   3778    637   1092    -88       C  
ATOM   1152  C   GLN A 317      -0.790  13.125  22.038  1.00-0.232           C  
ANISOU 1152  C   GLN A 317    10042   3449   4520    673   1133    -94       C  
ATOM   1153  O   GLN A 317      -0.736  13.686  20.940  1.00-0.232           O  
ANISOU 1153  O   GLN A 317    10119   3427   4561    678   1131    -46       O  
ATOM   1154  CB  GLN A 317      -2.248  11.076  22.041  1.00-0.232           C  
ANISOU 1154  CB  GLN A 317     9127   3130   3986    795   1119    -42       C  
ATOM   1155  CG  GLN A 317      -2.352   9.563  21.759  1.00-0.232           C  
ANISOU 1155  CG  GLN A 317     9719   4082   4818    754   1076    -21       C  
ATOM   1156  CD  GLN A 317      -1.902   9.183  20.354  1.00-0.232           C  
ANISOU 1156  CD  GLN A 317     9712   4187   4914    690   1029     19       C  
ATOM   1157  OE1 GLN A 317      -2.141   9.897  19.396  1.00-0.232           O  
ANISOU 1157  OE1 GLN A 317     8513   2894   3665    737   1034     63       O  
ATOM   1158  NE2 GLN A 317      -1.245   8.042  20.196  1.00-0.232           N  
ANISOU 1158  NE2 GLN A 317     8722   3392   4056    589    985      8       N  
ATOM   1159  N   SER A 318      -0.812  13.808  23.205  1.00 0.703           N  
ANISOU 1159  N   SER A 318    10031   3197   4317    693   1171   -153       N  
ATOM   1160  CA  SER A 318      -0.794  15.278  23.256  1.00 0.703           C  
ANISOU 1160  CA  SER A 318    10228   2974   4239    725   1215   -168       C  
ATOM   1161  C   SER A 318       0.588  15.857  22.888  1.00 0.703           C  
ANISOU 1161  C   SER A 318    11095   3636   4987    533   1179   -192       C  
ATOM   1162  O   SER A 318       0.711  17.060  22.701  1.00 0.703           O  
ANISOU 1162  O   SER A 318    11416   3594   5080    533   1211   -195       O  
ATOM   1163  CB  SER A 318      -1.257  15.790  24.625  1.00 0.703           C  
ANISOU 1163  CB  SER A 318    10619   3158   4441    804   1270   -231       C  
ATOM   1164  OG  SER A 318      -0.368  15.389  25.655  1.00 0.703           O  
ANISOU 1164  OG  SER A 318    10803   3359   4589    659   1235   -305       O  
ATOM   1165  N   PHE A 319       1.621  15.009  22.831  1.00 0.896           N  
ANISOU 1165  N   PHE A 319    10666   3435   4707    371   1118   -210       N  
ATOM   1166  CA  PHE A 319       2.987  15.393  22.468  1.00 0.896           C  
ANISOU 1166  CA  PHE A 319    10596   3262   4578    175   1082   -230       C  
ATOM   1167  C   PHE A 319       3.322  14.996  21.006  1.00 0.896           C  
ANISOU 1167  C   PHE A 319    10497   3348   4642    132   1060   -161       C  
ATOM   1168  O   PHE A 319       4.481  15.097  20.588  1.00 0.896           O  
ANISOU 1168  O   PHE A 319    10328   3182   4482    -34   1033   -168       O  
ATOM   1169  CB  PHE A 319       3.999  14.830  23.498  1.00 0.896           C  
ANISOU 1169  CB  PHE A 319    10745   3530   4763     26   1031   -301       C  
ATOM   1170  CG  PHE A 319       4.057  15.655  24.772  1.00 0.896           C  
ANISOU 1170  CG  PHE A 319    11133   3611   4894      5   1049   -378       C  
ATOM   1171  CD1 PHE A 319       3.188  15.399  25.829  1.00 0.896           C  
ANISOU 1171  CD1 PHE A 319    11373   3859   5092    131   1078   -408       C  
ATOM   1172  CD2 PHE A 319       4.943  16.723  24.892  1.00 0.896           C  
ANISOU 1172  CD2 PHE A 319    11663   3828   5208   -144   1042   -421       C  
ATOM   1173  CE1 PHE A 319       3.217  16.189  26.995  1.00 0.896           C  
ANISOU 1173  CE1 PHE A 319    11689   3867   5141    118   1100   -484       C  
ATOM   1174  CE2 PHE A 319       4.966  17.520  26.059  1.00 0.896           C  
ANISOU 1174  CE2 PHE A 319    12227   4072   5502   -168   1057   -499       C  
ATOM   1175  CZ  PHE A 319       4.104  17.245  27.101  1.00 0.896           C  
ANISOU 1175  CZ  PHE A 319    11854   3705   5078    -31   1087   -532       C  
ATOM   1176  N   MET A 320       2.286  14.585  20.231  1.00 2.601           N  
ANISOU 1176  N   MET A 320     9648   2652   3912    280   1074    -95       N  
ATOM   1177  CA  MET A 320       2.378  14.195  18.811  1.00 2.601           C  
ANISOU 1177  CA  MET A 320     9396   2567   3790    267   1056    -28       C  
ATOM   1178  C   MET A 320       1.769  15.339  17.983  1.00 2.601           C  
ANISOU 1178  C   MET A 320    10922   3814   5145    363   1096     32       C  
ATOM   1179  O   MET A 320       0.562  15.367  17.708  1.00 2.601           O  
ANISOU 1179  O   MET A 320    11022   3950   5267    537   1114     79       O  
ATOM   1180  CB  MET A 320       1.661  12.862  18.544  1.00 2.601           C  
ANISOU 1180  CB  MET A 320     9281   2824   3917    353   1032      1       C  
ATOM   1181  CG  MET A 320       2.315  11.675  19.229  1.00 2.601           C  
ANISOU 1181  CG  MET A 320     9264   3064   4059    263    993    -46       C  
ATOM   1182  SD  MET A 320       1.336  10.169  19.086  1.00 2.601           S  
ANISOU 1182  SD  MET A 320     9182   3351   4216    362    974    -18       S  
ATOM   1183  CE  MET A 320       2.269   9.063  20.147  1.00 2.601           C  
ANISOU 1183  CE  MET A 320     8693   3043   3830    254    936    -79       C  
ATOM   1184  N   PHE A 321       2.617  16.309  17.639  1.00 0.026           N  
ANISOU 1184  N   PHE A 321    10923   3532   4967    246   1108     31       N  
ATOM   1185  CA  PHE A 321       2.215  17.519  16.927  1.00 0.026           C  
ANISOU 1185  CA  PHE A 321    11341   3612   5171    317   1148     87       C  
ATOM   1186  C   PHE A 321       2.128  17.338  15.432  1.00 0.026           C  
ANISOU 1186  C   PHE A 321    12105   4490   6005    334   1137    173       C  
ATOM   1187  O   PHE A 321       2.938  16.609  14.857  1.00 0.026           O  
ANISOU 1187  O   PHE A 321    11803   4420   5848    207   1108    176       O  
ATOM   1188  CB  PHE A 321       3.153  18.679  17.291  1.00 0.026           C  
ANISOU 1188  CB  PHE A 321    11805   3679   5380    169   1171     47       C  
ATOM   1189  CG  PHE A 321       3.380  18.821  18.784  1.00 0.026           C  
ANISOU 1189  CG  PHE A 321    12198   3962   5687    125   1172    -48       C  
ATOM   1190  CD1 PHE A 321       2.354  19.243  19.628  1.00 0.026           C  
ANISOU 1190  CD1 PHE A 321    12819   4405   6181    295   1211    -71       C  
ATOM   1191  CD2 PHE A 321       4.619  18.534  19.347  1.00 0.026           C  
ANISOU 1191  CD2 PHE A 321    12484   4335   6015    -82   1134   -113       C  
ATOM   1192  CE1 PHE A 321       2.573  19.405  21.007  1.00 0.026           C  
ANISOU 1192  CE1 PHE A 321    12925   4386   6174    251   1215   -162       C  
ATOM   1193  CE2 PHE A 321       4.831  18.681  20.729  1.00 0.026           C  
ANISOU 1193  CE2 PHE A 321    12871   4616   6302   -127   1126   -200       C  
ATOM   1194  CZ  PHE A 321       3.810  19.127  21.544  1.00 0.026           C  
ANISOU 1194  CZ  PHE A 321    12716   4251   5993     37   1168   -226       C  
ATOM   1195  N   TYR A 322       1.124  17.995  14.808  1.00 0.849           N  
ANISOU 1195  N   TYR A 322    12290   4515   6081    501   1161    244       N  
ATOM   1196  CA  TYR A 322       0.897  18.036  13.354  1.00 0.849           C  
ANISOU 1196  CA  TYR A 322    12519   4788   6317    541   1150    336       C  
ATOM   1197  C   TYR A 322       2.137  18.642  12.703  1.00 0.849           C  
ANISOU 1197  C   TYR A 322    13241   5303   6899    351   1165    347       C  
ATOM   1198  O   TYR A 322       2.642  19.675  13.164  1.00 0.849           O  
ANISOU 1198  O   TYR A 322    13259   4956   6696    274   1199    321       O  
ATOM   1199  CB  TYR A 322      -0.333  18.909  13.011  1.00 0.849           C  
ANISOU 1199  CB  TYR A 322    12977   5028   6624    759   1176    408       C  
ATOM   1200  CG  TYR A 322      -0.738  18.864  11.551  0.50 0.849           C  
ANISOU 1200  CG  TYR A 322    13285   5421   6946    827   1153    508       C  
ATOM   1201  CD1 TYR A 322      -1.460  17.789  11.039  0.50 0.849           C  
ANISOU 1201  CD1 TYR A 322    13359   5899   7253    908   1105    539       C  
ATOM   1202  CD2 TYR A 322      -0.436  19.915  10.691  0.50 0.849           C  
ANISOU 1202  CD2 TYR A 322    13609   5405   7031    808   1177    574       C  
ATOM   1203  CE1 TYR A 322      -1.839  17.744   9.697  0.50 0.849           C  
ANISOU 1203  CE1 TYR A 322    13453   6073   7345    965   1075    627       C  
ATOM   1204  CE2 TYR A 322      -0.815  19.885   9.349  0.50 0.849           C  
ANISOU 1204  CE2 TYR A 322    13716   5584   7130    873   1152    670       C  
ATOM   1205  CZ  TYR A 322      -1.517  18.797   8.856  0.50 0.849           C  
ANISOU 1205  CZ  TYR A 322    14354   6641   8003    953   1098    694       C  
ATOM   1206  OH  TYR A 322      -1.893  18.762   7.534  0.50 0.849           O  
ANISOU 1206  OH  TYR A 322    14381   6739   8006   1012   1066    786       O  
ATOM   1207  N   GLY A 323       2.622  17.965  11.670  1.00 0.196           N  
ANISOU 1207  N   GLY A 323    12910   5211   6696    271   1141    382       N  
ATOM   1208  CA  GLY A 323       3.813  18.354  10.925  1.00 0.196           C  
ANISOU 1208  CA  GLY A 323    12965   5154   6662     85   1160    401       C  
ATOM   1209  C   GLY A 323       5.090  17.699  11.424  1.00 0.196           C  
ANISOU 1209  C   GLY A 323    13216   5610   7060   -115   1148    327       C  
ATOM   1210  O   GLY A 323       6.102  17.736  10.714  1.00 0.196           O  
ANISOU 1210  O   GLY A 323    13336   5761   7179   -270   1162    343       O  
ATOM   1211  N   ALA A 324       5.052  17.091  12.644  1.00-0.029           N  
ANISOU 1211  N   ALA A 324    12196   4745   6167   -108   1123    249       N  
ATOM   1212  CA  ALA A 324       6.180  16.403  13.295  1.00-0.029           C  
ANISOU 1212  CA  ALA A 324    11885   4654   6007   -270   1100    178       C  
ATOM   1213  C   ALA A 324       6.209  14.866  13.107  1.00-0.029           C  
ANISOU 1213  C   ALA A 324    11797   5010   6199   -247   1062    167       C  
ATOM   1214  O   ALA A 324       7.175  14.213  13.519  1.00-0.029           O  
ANISOU 1214  O   ALA A 324    11829   5250   6369   -365   1042    119       O  
ATOM   1215  CB  ALA A 324       6.216  16.739  14.771  1.00-0.029           C  
ANISOU 1215  CB  ALA A 324    12005   4634   6055   -288   1093    101       C  
ATOM   1216  N   GLY A 325       5.177  14.302  12.492  1.00 1.133           N  
ANISOU 1216  N   GLY A 325    10685   4035   5162    -97   1050    213       N  
ATOM   1217  CA  GLY A 325       5.141  12.867  12.243  1.00 1.133           C  
ANISOU 1217  CA  GLY A 325    10230   3954   4939    -77   1017    203       C  
ATOM   1218  C   GLY A 325       5.931  12.485  11.005  1.00 1.133           C  
ANISOU 1218  C   GLY A 325    10440   4300   5202   -167   1025    235       C  
ATOM   1219  O   GLY A 325       6.333  13.359  10.231  1.00 1.133           O  
ANISOU 1219  O   GLY A 325    10804   4472   5419   -230   1058    278       O  
ATOM   1220  N   TYR A 326       6.162  11.187  10.812  1.00 0.806           N  
ANISOU 1220  N   TYR A 326     9483   3654   4437   -173   1001    214       N  
ATOM   1221  CA  TYR A 326       6.869  10.670   9.643  1.00 0.806           C  
ANISOU 1221  CA  TYR A 326     9251   3575   4261   -240   1015    237       C  
ATOM   1222  C   TYR A 326       5.843  10.282   8.609  1.00 0.806           C  
ANISOU 1222  C   TYR A 326     9428   3808   4426   -125   1000    289       C  
ATOM   1223  O   TYR A 326       5.022   9.381   8.850  1.00 0.806           O  
ANISOU 1223  O   TYR A 326     9168   3712   4277    -32    963    275       O  
ATOM   1224  CB  TYR A 326       7.770   9.471  10.011  1.00 0.806           C  
ANISOU 1224  CB  TYR A 326     9165   3776   4371   -306   1001    181       C  
ATOM   1225  CG  TYR A 326       9.057   9.890  10.683  1.00 0.806           C  
ANISOU 1225  CG  TYR A 326     9584   4183   4805   -451   1014    143       C  
ATOM   1226  CD1 TYR A 326       9.088  10.210  12.043  1.00 0.806           C  
ANISOU 1226  CD1 TYR A 326     9945   4467   5155   -468    991     96       C  
ATOM   1227  CD2 TYR A 326      10.240  10.000   9.958  1.00 0.806           C  
ANISOU 1227  CD2 TYR A 326     9666   4339   4907   -575   1051    154       C  
ATOM   1228  CE1 TYR A 326      10.268  10.618  12.662  1.00 0.806           C  
ANISOU 1228  CE1 TYR A 326    10112   4634   5331   -613    992     59       C  
ATOM   1229  CE2 TYR A 326      11.423  10.424  10.564  1.00 0.806           C  
ANISOU 1229  CE2 TYR A 326     9829   4522   5098   -721   1058    121       C  
ATOM   1230  CZ  TYR A 326      11.432  10.731  11.918  1.00 0.806           C  
ANISOU 1230  CZ  TYR A 326    10946   5563   6203   -743   1023     73       C  
ATOM   1231  OH  TYR A 326      12.597  11.128  12.525  1.00 0.806           O  
ANISOU 1231  OH  TYR A 326    10840   5494   6125   -897   1019     39       O  
ATOM   1232  N   GLN A 327       5.869  10.972   7.459  1.00 1.976           N  
ANISOU 1232  N   GLN A 327     9077   3318   3932   -137   1026    351       N  
ATOM   1233  CA  GLN A 327       4.950  10.655   6.372  1.00 1.976           C  
ANISOU 1233  CA  GLN A 327     8967   3265   3792    -36   1004    405       C  
ATOM   1234  C   GLN A 327       5.215   9.222   5.900  1.00 1.976           C  
ANISOU 1234  C   GLN A 327     8992   3582   3972    -54    986    373       C  
ATOM   1235  O   GLN A 327       6.371   8.849   5.668  1.00 1.976           O  
ANISOU 1235  O   GLN A 327     8899   3585   3931   -159   1018    347       O  
ATOM   1236  CB  GLN A 327       5.117  11.637   5.181  1.00 1.976           C  
ANISOU 1236  CB  GLN A 327     9364   3455   3986    -62   1038    481       C  
ATOM   1237  CG  GLN A 327       4.179  11.363   3.988  1.00 1.976           C  
ANISOU 1237  CG  GLN A 327     8665   2810   3232     41   1006    543       C  
ATOM   1238  CD  GLN A 327       2.720  11.558   4.333  1.00 1.976           C  
ANISOU 1238  CD  GLN A 327     9935   4053   4498    203    957    571       C  
ATOM   1239  OE1 GLN A 327       2.324  12.590   4.862  1.00 1.976           O  
ANISOU 1239  OE1 GLN A 327     9889   3778   4344    260    969    595       O  
ATOM   1240  NE2 GLN A 327       1.894  10.566   4.041  1.00 1.976           N  
ANISOU 1240  NE2 GLN A 327     8925   3276   3603    278    904    567       N  
ATOM   1241  N   VAL A 328       4.131   8.458   5.701  1.00-0.769           N  
ANISOU 1241  N   VAL A 328     8204   2930   3249     50    938    379       N  
ATOM   1242  CA  VAL A 328       4.175   7.124   5.100  1.00-0.769           C  
ANISOU 1242  CA  VAL A 328     7966   2920   3113     44    917    354       C  
ATOM   1243  C   VAL A 328       4.211   7.292   3.542  1.00-0.769           C  
ANISOU 1243  C   VAL A 328     9123   4042   4134     36    928    408       C  
ATOM   1244  O   VAL A 328       3.445   8.081   2.977  1.00-0.769           O  
ANISOU 1244  O   VAL A 328     9145   3931   4023    100    912    473       O  
ATOM   1245  CB  VAL A 328       2.994   6.246   5.605  1.00-0.769           C  
ANISOU 1245  CB  VAL A 328     8098   3200   3360    136    860    335       C  
ATOM   1246  CG1 VAL A 328       2.905   4.889   4.844  1.00-0.769           C  
ANISOU 1246  CG1 VAL A 328     7747   3041   3074    127    834    311       C  
ATOM   1247  CG2 VAL A 328       3.116   6.016   7.114  1.00-0.769           C  
ANISOU 1247  CG2 VAL A 328     7981   3116   3359    131    860    281       C  
ATOM   1248  N   GLU A 329       5.133   6.580   2.866  1.00 0.025           N  
ANISOU 1248  N   GLU A 329     8797   3827   3831    -38    959    382       N  
ATOM   1249  CA  GLU A 329       5.239   6.625   1.415  1.00 0.025           C  
ANISOU 1249  CA  GLU A 329     9014   4022   3911    -52    976    425       C  
ATOM   1250  C   GLU A 329       4.654   5.401   0.725  1.00 0.025           C  
ANISOU 1250  C   GLU A 329     9330   4500   4255     -9    931    403       C  
ATOM   1251  O   GLU A 329       4.222   5.531  -0.420  1.00 0.025           O  
ANISOU 1251  O   GLU A 329     9302   4435   4088     15    916    449       O  
ATOM   1252  CB  GLU A 329       6.667   6.912   0.927  1.00 0.025           C  
ANISOU 1252  CB  GLU A 329     9321   4307   4174   -166   1056    424       C  
ATOM   1253  CG  GLU A 329       7.708   5.827   1.147  1.00 0.025           C  
ANISOU 1253  CG  GLU A 329    11252   6440   6257   -222   1090    353       C  
ATOM   1254  CD  GLU A 329       9.033   6.135   0.469  1.00 0.025           C  
ANISOU 1254  CD  GLU A 329    15009  10209   9968   -326   1175    363       C  
ATOM   1255  OE1 GLU A 329       9.023   6.823  -0.576  1.00 0.025           O  
ANISOU 1255  OE1 GLU A 329    13143   8225   7926   -345   1206    423       O  
ATOM   1256  OE2 GLU A 329      10.085   5.694   0.985  1.00 0.025           O  
ANISOU 1256  OE2 GLU A 329    15361  10700  10461   -386   1212    317       O  
ATOM   1257  N   LYS A 330       4.645   4.215   1.394  1.00 0.268           N  
ANISOU 1257  N   LYS A 330     8696   4027   3780     -4    910    335       N  
ATOM   1258  CA  LYS A 330       4.112   2.990   0.787  1.00 0.268           C  
ANISOU 1258  CA  LYS A 330     8592   4049   3689     22    868    306       C  
ATOM   1259  C   LYS A 330       3.290   2.166   1.751  1.00 0.268           C  
ANISOU 1259  C   LYS A 330     8623   4185   3863     64    812    267       C  
ATOM   1260  O   LYS A 330       3.607   2.111   2.943  1.00 0.268           O  
ANISOU 1260  O   LYS A 330     8228   3810   3588     57    825    236       O  
ATOM   1261  CB  LYS A 330       5.221   2.122   0.154  1.00 0.268           C  
ANISOU 1261  CB  LYS A 330     8820   4349   3909    -35    922    259       C  
ATOM   1262  CG  LYS A 330       5.731   2.670  -1.165  1.00 0.268           C  
ANISOU 1262  CG  LYS A 330    10883   6335   5796    -70    971    302       C  
ATOM   1263  CD  LYS A 330       6.762   1.772  -1.806  1.00 0.268           C  
ANISOU 1263  CD  LYS A 330    11970   7505   6873   -112   1034    254       C  
ATOM   1264  CE  LYS A 330       7.422   2.466  -2.978  1.00 0.268           C  
ANISOU 1264  CE  LYS A 330    12760   8217   7494   -158   1101    302       C  
ATOM   1265  NZ  LYS A 330       8.521   3.365  -2.538  1.00 0.268           N  
ANISOU 1265  NZ  LYS A 330    12982   8414   7767   -229   1176    320       N  
ATOM   1266  N   VAL A 331       2.219   1.530   1.236  1.00-0.571           N  
ANISOU 1266  N   VAL A 331     7958   3592   3179    100    749    271       N  
ATOM   1267  CA  VAL A 331       1.325   0.668   2.048  1.00-0.571           C  
ANISOU 1267  CA  VAL A 331     7786   3533   3137    127    695    239       C  
ATOM   1268  C   VAL A 331       1.180  -0.638   1.268  1.00-0.571           C  
ANISOU 1268  C   VAL A 331     8130   3954   3449     97    667    196       C  
ATOM   1269  O   VAL A 331       0.951  -0.573   0.061  1.00-0.571           O  
ANISOU 1269  O   VAL A 331     7797   3604   2981     93    647    219       O  
ATOM   1270  CB  VAL A 331      -0.058   1.368   2.284  1.00-0.571           C  
ANISOU 1270  CB  VAL A 331     8397   4162   3763    201    637    296       C  
ATOM   1271  CG1 VAL A 331      -1.092   0.380   2.840  1.00-0.571           C  
ANISOU 1271  CG1 VAL A 331     8343   4258   3832    214    581    270       C  
ATOM   1272  CG2 VAL A 331       0.076   2.573   3.222  1.00-0.571           C  
ANISOU 1272  CG2 VAL A 331     8285   3941   3670    238    672    326       C  
ATOM   1273  N   ILE A 332       1.426  -1.816   1.909  1.00-0.508           N  
ANISOU 1273  N   ILE A 332     7925   3807   3339     73    671    132       N  
ATOM   1274  CA  ILE A 332       1.344  -3.117   1.207  1.00-0.508           C  
ANISOU 1274  CA  ILE A 332     8006   3917   3365     40    650     82       C  
ATOM   1275  C   ILE A 332       0.571  -4.095   2.106  1.00-0.508           C  
ANISOU 1275  C   ILE A 332     8318   4300   3791     34    606     50       C  
ATOM   1276  O   ILE A 332       1.034  -4.390   3.209  1.00-0.508           O  
ANISOU 1276  O   ILE A 332     8111   4094   3690     38    635     25       O  
ATOM   1277  CB  ILE A 332       2.761  -3.682   0.845  1.00-0.508           C  
ANISOU 1277  CB  ILE A 332     8610   4477   3925     14    725     33       C  
ATOM   1278  CG1 ILE A 332       3.661  -2.627   0.134  1.00-0.508           C  
ANISOU 1278  CG1 ILE A 332     8922   4733   4147      7    786     69       C  
ATOM   1279  CG2 ILE A 332       2.656  -4.969  -0.018  1.00-0.508           C  
ANISOU 1279  CG2 ILE A 332     8833   4687   4045    -11    710    -22       C  
ATOM   1280  CD1 ILE A 332       5.200  -2.912   0.236  1.00-0.508           C  
ANISOU 1280  CD1 ILE A 332    10457   6275   5717    -12    874     30       C  
ATOM   1281  N   SER A 333      -0.602  -4.577   1.650  1.00 1.118           N  
ANISOU 1281  N   SER A 333     7735   3780   3182     18    535     55       N  
ATOM   1282  CA  SER A 333      -1.415  -5.520   2.418  1.00 1.118           C  
ANISOU 1282  CA  SER A 333     7691   3807   3237     -7    494     30       C  
ATOM   1283  C   SER A 333      -1.049  -6.934   1.948  1.00 1.118           C  
ANISOU 1283  C   SER A 333     8152   4205   3614    -63    497    -40       C  
ATOM   1284  O   SER A 333      -0.733  -7.112   0.769  1.00 1.118           O  
ANISOU 1284  O   SER A 333     7934   3932   3249    -82    498    -58       O  
ATOM   1285  CB  SER A 333      -2.897  -5.280   2.155  1.00 1.118           C  
ANISOU 1285  CB  SER A 333     8065   4307   3639     -6    413     74       C  
ATOM   1286  OG  SER A 333      -3.389  -4.252   2.988  1.00 1.118           O  
ANISOU 1286  OG  SER A 333     9833   6134   5515     59    416    129       O  
ATOM   1287  N   HIS A 334      -1.141  -7.940   2.842  1.00-1.137           N  
ANISOU 1287  N   HIS A 334     7751   3795   3286    -89    498    -78       N  
ATOM   1288  CA  HIS A 334      -0.845  -9.326   2.468  1.00-1.137           C  
ANISOU 1288  CA  HIS A 334     7770   3716   3208   -136    503   -145       C  
ATOM   1289  C   HIS A 334      -1.769  -9.742   1.307  1.00-1.137           C  
ANISOU 1289  C   HIS A 334     8254   4216   3568   -199    432   -156       C  
ATOM   1290  O   HIS A 334      -2.950  -9.402   1.378  1.00-1.137           O  
ANISOU 1290  O   HIS A 334     7917   4009   3296   -220    365   -116       O  
ATOM   1291  CB  HIS A 334      -1.039 -10.265   3.662  1.00-1.137           C  
ANISOU 1291  CB  HIS A 334     7821   3748   3348   -157    504   -168       C  
ATOM   1292  CG  HIS A 334      -0.406 -11.606   3.449  1.00-1.137           C  
ANISOU 1292  CG  HIS A 334     8425   4199   3843   -180    532   -236       C  
ATOM   1293  ND1 HIS A 334      -1.043 -12.603   2.713  1.00-1.137           N  
ANISOU 1293  ND1 HIS A 334     8755   4457   4044   -256    487   -278       N  
ATOM   1294  CD2 HIS A 334       0.818 -12.049   3.818  1.00-1.137           C  
ANISOU 1294  CD2 HIS A 334     8749   4426   4158   -131    598   -268       C  
ATOM   1295  CE1 HIS A 334      -0.202 -13.622   2.698  1.00-1.137           C  
ANISOU 1295  CE1 HIS A 334     8846   4381   4040   -244    535   -335       C  
ATOM   1296  NE2 HIS A 334       0.932 -13.337   3.349  1.00-1.137           N  
ANISOU 1296  NE2 HIS A 334     8871   4398   4141   -161    602   -328       N  
ATOM   1297  N   PRO A 335      -1.274 -10.451   0.250  1.00-0.022           N  
ANISOU 1297  N   PRO A 335     8345   4186   3478   -227    444   -211       N  
ATOM   1298  CA  PRO A 335      -2.166 -10.830  -0.883  1.00-0.022           C  
ANISOU 1298  CA  PRO A 335     8362   4213   3354   -298    367   -226       C  
ATOM   1299  C   PRO A 335      -3.327 -11.744  -0.498  1.00-0.022           C  
ANISOU 1299  C   PRO A 335     8843   4739   3874   -388    294   -243       C  
ATOM   1300  O   PRO A 335      -4.337 -11.780  -1.216  1.00-0.022           O  
ANISOU 1300  O   PRO A 335     8814   4798   3793   -451    208   -233       O  
ATOM   1301  CB  PRO A 335      -1.238 -11.560  -1.851  1.00-0.022           C  
ANISOU 1301  CB  PRO A 335     8695   4370   3478   -305    415   -295       C  
ATOM   1302  CG  PRO A 335       0.127 -11.196  -1.456  1.00-0.022           C  
ANISOU 1302  CG  PRO A 335     9317   4944   4148   -223    517   -295       C  
ATOM   1303  CD  PRO A 335       0.108 -10.922   0.013  1.00-0.022           C  
ANISOU 1303  CD  PRO A 335     8624   4326   3669   -192    529   -262       C  
ATOM   1304  N   ASN A 336      -3.170 -12.506   0.616  1.00 0.896           N  
ANISOU 1304  N   ASN A 336     8185   4023   3303   -399    326   -268       N  
ATOM   1305  CA  ASN A 336      -4.195 -13.429   1.105  1.00 0.896           C  
ANISOU 1305  CA  ASN A 336     8086   3948   3242   -496    271   -282       C  
ATOM   1306  C   ASN A 336      -5.026 -12.849   2.247  1.00 0.896           C  
ANISOU 1306  C   ASN A 336     8419   4475   3798   -484    252   -217       C  
ATOM   1307  O   ASN A 336      -5.745 -13.601   2.915  1.00 0.896           O  
ANISOU 1307  O   ASN A 336     8369   4450   3808   -560    229   -223       O  
ATOM   1308  CB  ASN A 336      -3.599 -14.803   1.476  1.00 0.896           C  
ANISOU 1308  CB  ASN A 336     8245   3881   3303   -528    315   -352       C  
ATOM   1309  CG  ASN A 336      -2.913 -15.509   0.333  1.00 0.896           C  
ANISOU 1309  CG  ASN A 336     9710   5142   4529   -540    336   -425       C  
ATOM   1310  OD1 ASN A 336      -1.724 -15.829   0.409  1.00 0.896           O  
ANISOU 1310  OD1 ASN A 336     9444   4723   4201   -466    416   -460       O  
ATOM   1311  ND2 ASN A 336      -3.635 -15.760  -0.747  1.00 0.896           N  
ANISOU 1311  ND2 ASN A 336     8512   3944   3189   -627    265   -450       N  
ATOM   1312  N   TYR A 337      -4.966 -11.507   2.473  1.00-0.714           N  
ANISOU 1312  N   TYR A 337     7774   3959   3265   -394    266   -154       N  
ATOM   1313  CA  TYR A 337      -5.809 -10.919   3.521  1.00-0.714           C  
ANISOU 1313  CA  TYR A 337     7528   3892   3215   -371    254    -95       C  
ATOM   1314  C   TYR A 337      -7.279 -11.101   3.124  1.00-0.714           C  
ANISOU 1314  C   TYR A 337     8351   4906   4084   -451    163    -71       C  
ATOM   1315  O   TYR A 337      -7.645 -10.897   1.964  1.00-0.714           O  
ANISOU 1315  O   TYR A 337     8312   4919   3955   -472    102    -66       O  
ATOM   1316  CB  TYR A 337      -5.479  -9.445   3.794  1.00-0.714           C  
ANISOU 1316  CB  TYR A 337     7613   4040   3379   -257    288    -38       C  
ATOM   1317  CG  TYR A 337      -6.468  -8.758   4.721  1.00-0.714           C  
ANISOU 1317  CG  TYR A 337     7707   4319   3650   -221    275     22       C  
ATOM   1318  CD1 TYR A 337      -6.653  -9.201   6.028  1.00-0.714           C  
ANISOU 1318  CD1 TYR A 337     7893   4523   3948   -234    306     19       C  
ATOM   1319  CD2 TYR A 337      -7.246  -7.689   4.278  1.00-0.714           C  
ANISOU 1319  CD2 TYR A 337     7732   4498   3721   -166    232     84       C  
ATOM   1320  CE1 TYR A 337      -7.559  -8.572   6.889  1.00-0.714           C  
ANISOU 1320  CE1 TYR A 337     7792   4593   4000   -194    306     72       C  
ATOM   1321  CE2 TYR A 337      -8.168  -7.064   5.126  1.00-0.714           C  
ANISOU 1321  CE2 TYR A 337     7703   4642   3853   -115    229    138       C  
ATOM   1322  CZ  TYR A 337      -8.328  -7.518   6.427  1.00-0.714           C  
ANISOU 1322  CZ  TYR A 337     8483   5444   4744   -132    269    129       C  
ATOM   1323  OH  TYR A 337      -9.243  -6.933   7.269  1.00-0.714           O  
ANISOU 1323  OH  TYR A 337     8167   5302   4580    -79    276    179       O  
ATOM   1324  N   ASP A 338      -8.078 -11.588   4.063  1.00-0.117           N  
ANISOU 1324  N   ASP A 338     8324   4981   4185   -504    154    -59       N  
ATOM   1325  CA  ASP A 338      -9.505 -11.842   3.908  1.00-0.117           C  
ANISOU 1325  CA  ASP A 338     8419   5300   4367   -593     73    -33       C  
ATOM   1326  C   ASP A 338     -10.186 -10.977   4.957  1.00-0.117           C  
ANISOU 1326  C   ASP A 338     8808   5902   4969   -518     94     36       C  
ATOM   1327  O   ASP A 338     -10.066 -11.255   6.150  1.00-0.117           O  
ANISOU 1327  O   ASP A 338     8653   5712   4894   -515    152     36       O  
ATOM   1328  CB  ASP A 338      -9.809 -13.333   4.163  1.00-0.117           C  
ANISOU 1328  CB  ASP A 338     8755   5548   4652   -741     59    -85       C  
ATOM   1329  CG  ASP A 338     -11.228 -13.779   3.853  1.00-0.117           C  
ANISOU 1329  CG  ASP A 338    10563   7582   6529   -872    -31    -70       C  
ATOM   1330  OD1 ASP A 338     -12.066 -12.915   3.497  1.00-0.117           O  
ANISOU 1330  OD1 ASP A 338    10445   7730   6524   -834    -88    -12       O  
ATOM   1331  OD2 ASP A 338     -11.503 -14.997   3.957  1.00-0.117           O  
ANISOU 1331  OD2 ASP A 338    11899   8827   7802  -1014    -47   -114       O  
ATOM   1332  N   SER A 339     -10.894  -9.934   4.512  1.00 1.088           N  
ANISOU 1332  N   SER A 339     8369   5673   4610   -452     48     96       N  
ATOM   1333  CA  SER A 339     -11.552  -8.956   5.383  1.00 1.088           C  
ANISOU 1333  CA  SER A 339     8390   5893   4818   -352     72    165       C  
ATOM   1334  C   SER A 339     -12.742  -9.509   6.170  1.00 1.088           C  
ANISOU 1334  C   SER A 339     9013   6746   5613   -428     57    186       C  
ATOM   1335  O   SER A 339     -13.062  -8.952   7.212  1.00 1.088           O  
ANISOU 1335  O   SER A 339     8835   6670   5574   -352    111    225       O  
ATOM   1336  CB  SER A 339     -11.947  -7.708   4.595  1.00 1.088           C  
ANISOU 1336  CB  SER A 339     8777   6415   5217   -245     27    226       C  
ATOM   1337  OG  SER A 339     -12.801  -8.043   3.516  1.00 1.088           O  
ANISOU 1337  OG  SER A 339    10077   7883   6497   -321    -77    235       O  
ATOM   1338  N   LYS A 340     -13.378 -10.603   5.703  1.00 2.458           N  
ANISOU 1338  N   LYS A 340     8829   6635   5412   -584     -8    159       N  
ATOM   1339  CA  LYS A 340     -14.522 -11.198   6.414  1.00 2.458           C  
ANISOU 1339  CA  LYS A 340     8735   6773   5483   -683    -20    180       C  
ATOM   1340  C   LYS A 340     -14.060 -11.957   7.657  1.00 2.458           C  
ANISOU 1340  C   LYS A 340     9369   7233   6114   -727     67    152       C  
ATOM   1341  O   LYS A 340     -14.611 -11.755   8.742  1.00 2.458           O  
ANISOU 1341  O   LYS A 340     9390   7404   6291   -701    116    192       O  
ATOM   1342  CB  LYS A 340     -15.338 -12.135   5.493  1.00 2.458           C  
ANISOU 1342  CB  LYS A 340     9101   7261   5817   -860   -124    158       C  
ATOM   1343  CG  LYS A 340     -16.037 -11.433   4.328  1.00 2.458           C  
ANISOU 1343  CG  LYS A 340    11069   9463   7807   -827   -227    197       C  
ATOM   1344  N   THR A 341     -13.048 -12.829   7.494  1.00 0.164           N  
ANISOU 1344  N   THR A 341     8925   6471   5484   -785     88     85       N  
ATOM   1345  CA  THR A 341     -12.511 -13.684   8.558  1.00 0.164           C  
ANISOU 1345  CA  THR A 341     8857   6196   5373   -827    160     57       C  
ATOM   1346  C   THR A 341     -11.309 -13.082   9.306  1.00 0.164           C  
ANISOU 1346  C   THR A 341     9160   6311   5642   -684    244     54       C  
ATOM   1347  O   THR A 341     -10.928 -13.597  10.358  1.00 0.164           O  
ANISOU 1347  O   THR A 341     9240   6261   5712   -692    304     46       O  
ATOM   1348  CB  THR A 341     -12.090 -15.029   7.959  1.00 0.164           C  
ANISOU 1348  CB  THR A 341     9761   6845   6081   -961    135    -14       C  
ATOM   1349  OG1 THR A 341     -11.040 -14.800   7.017  1.00 0.164           O  
ANISOU 1349  OG1 THR A 341     9156   6045   5314   -891    130    -55       O  
ATOM   1350  CG2 THR A 341     -13.245 -15.778   7.305  1.00 0.164           C  
ANISOU 1350  CG2 THR A 341     9728   6962   6055  -1137     49    -22       C  
ATOM   1351  N   LYS A 342     -10.688 -12.038   8.739  1.00 1.336           N  
ANISOU 1351  N   LYS A 342     8453   5579   4904   -563    244     60       N  
ATOM   1352  CA  LYS A 342      -9.462 -11.394   9.227  1.00 1.336           C  
ANISOU 1352  CA  LYS A 342     8430   5383   4836   -442    311     53       C  
ATOM   1353  C   LYS A 342      -8.240 -12.337   9.097  1.00 1.336           C  
ANISOU 1353  C   LYS A 342     8652   5317   4894   -472    338    -10       C  
ATOM   1354  O   LYS A 342      -7.230 -12.137   9.764  1.00 1.336           O  
ANISOU 1354  O   LYS A 342     8668   5198   4888   -399    395    -20       O  
ATOM   1355  CB  LYS A 342      -9.598 -10.789  10.644  1.00 1.336           C  
ANISOU 1355  CB  LYS A 342     8691   5712   5220   -366    374     91       C  
ATOM   1356  CG  LYS A 342     -10.726  -9.790  10.791  1.00 1.336           C  
ANISOU 1356  CG  LYS A 342    10170   7459   6850   -304    362    152       C  
ATOM   1357  CD  LYS A 342     -10.277  -8.348  10.639  1.00 1.336           C  
ANISOU 1357  CD  LYS A 342    11055   8315   7732   -157    388    176       C  
ATOM   1358  CE  LYS A 342     -11.435  -7.401  10.868  1.00 1.336           C  
ANISOU 1358  CE  LYS A 342    12050   9555   8870    -76    386    238       C  
ATOM   1359  NZ  LYS A 342     -12.493  -7.537   9.821  1.00 1.336           N  
ANISOU 1359  NZ  LYS A 342    12554  10283   9430   -113    304    267       N  
ATOM   1360  N   ASN A 343      -8.313 -13.340   8.214  1.00 0.042           N  
ANISOU 1360  N   ASN A 343     8067   4640   4189   -575    295    -54       N  
ATOM   1361  CA  ASN A 343      -7.173 -14.231   7.992  1.00 0.042           C  
ANISOU 1361  CA  ASN A 343     7991   4286   3946   -585    325   -115       C  
ATOM   1362  C   ASN A 343      -6.051 -13.454   7.284  1.00 0.042           C  
ANISOU 1362  C   ASN A 343     8154   4370   4038   -481    348   -129       C  
ATOM   1363  O   ASN A 343      -6.358 -12.563   6.483  1.00 0.042           O  
ANISOU 1363  O   ASN A 343     7831   4171   3730   -452    313   -105       O  
ATOM   1364  CB  ASN A 343      -7.580 -15.469   7.192  1.00 0.042           C  
ANISOU 1364  CB  ASN A 343     8330   4520   4148   -721    277   -164       C  
ATOM   1365  CG  ASN A 343      -6.649 -16.641   7.399  1.00 0.042           C  
ANISOU 1365  CG  ASN A 343    10410   6298   6070   -737    321   -220       C  
ATOM   1366  OD1 ASN A 343      -6.622 -17.598   6.616  1.00 0.042           O  
ANISOU 1366  OD1 ASN A 343     9911   5632   5405   -819    297   -275       O  
ATOM   1367  ND2 ASN A 343      -5.851 -16.580   8.452  1.00 0.042           N  
ANISOU 1367  ND2 ASN A 343     9054   4858   4753   -652    385   -208       N  
ATOM   1368  N   ASN A 344      -4.765 -13.715   7.653  1.00-0.633           N  
ANISOU 1368  N   ASN A 344     7583   3614   3403   -419    408   -159       N  
ATOM   1369  CA  ASN A 344      -3.581 -13.049   7.056  1.00-0.633           C  
ANISOU 1369  CA  ASN A 344     7399   3365   3162   -331    441   -172       C  
ATOM   1370  C   ASN A 344      -3.649 -11.536   7.241  1.00-0.633           C  
ANISOU 1370  C   ASN A 344     7788   3904   3662   -254    447   -119       C  
ATOM   1371  O   ASN A 344      -3.351 -10.759   6.323  1.00-0.633           O  
ANISOU 1371  O   ASN A 344     7335   3470   3162   -219    442   -111       O  
ATOM   1372  CB  ASN A 344      -3.383 -13.480   5.572  1.00-0.633           C  
ANISOU 1372  CB  ASN A 344     7449   3324   3045   -369    417   -218       C  
ATOM   1373  CG  ASN A 344      -3.251 -14.985   5.446  1.00-0.633           C  
ANISOU 1373  CG  ASN A 344     8755   4433   4214   -438    419   -278       C  
ATOM   1374  OD1 ASN A 344      -2.307 -15.580   5.961  1.00-0.633           O  
ANISOU 1374  OD1 ASN A 344     8573   4095   3992   -392    473   -305       O  
ATOM   1375  ND2 ASN A 344      -4.209 -15.642   4.802  1.00-0.633           N  
ANISOU 1375  ND2 ASN A 344     7674   3349   3055   -550    358   -300       N  
ATOM   1376  N   ASP A 345      -4.031 -11.119   8.471  1.00-1.479           N  
ANISOU 1376  N   ASP A 345     7365   3566   3367   -226    464    -81       N  
ATOM   1377  CA  ASP A 345      -4.196  -9.701   8.805  1.00-1.479           C  
ANISOU 1377  CA  ASP A 345     7235   3549   3330   -151    474    -33       C  
ATOM   1378  C   ASP A 345      -2.853  -9.016   9.094  1.00-1.479           C  
ANISOU 1378  C   ASP A 345     7814   4033   3890    -78    527    -40       C  
ATOM   1379  O   ASP A 345      -2.540  -8.728  10.254  1.00-1.479           O  
ANISOU 1379  O   ASP A 345     7818   4028   3957    -41    560    -30       O  
ATOM   1380  CB  ASP A 345      -5.174  -9.541   9.995  1.00-1.479           C  
ANISOU 1380  CB  ASP A 345     7140   3579   3363   -149    478      5       C  
ATOM   1381  CG  ASP A 345      -5.614  -8.110  10.257  1.00-1.479           C  
ANISOU 1381  CG  ASP A 345     7428   3983   3733    -67    485     55       C  
ATOM   1382  OD1 ASP A 345      -5.371  -7.250   9.394  1.00-1.479           O  
ANISOU 1382  OD1 ASP A 345     7407   3957   3668    -24    474     69       O  
ATOM   1383  OD2 ASP A 345      -6.217  -7.861  11.318  1.00-1.479           O  
ANISOU 1383  OD2 ASP A 345     7362   3999   3760    -44    507     81       O  
ATOM   1384  N   ILE A 346      -2.078  -8.740   8.036  1.00-0.975           N  
ANISOU 1384  N   ILE A 346     7392   3551   3380    -64    533    -56       N  
ATOM   1385  CA  ILE A 346      -0.769  -8.094   8.129  1.00-0.975           C  
ANISOU 1385  CA  ILE A 346     7396   3488   3370    -13    583    -62       C  
ATOM   1386  C   ILE A 346      -0.530  -7.160   6.938  1.00-0.975           C  
ANISOU 1386  C   ILE A 346     7977   4071   3881      4    582    -44       C  
ATOM   1387  O   ILE A 346      -0.928  -7.459   5.815  1.00-0.975           O  
ANISOU 1387  O   ILE A 346     7934   4032   3755    -26    551    -50       O  
ATOM   1388  CB  ILE A 346       0.394  -9.128   8.350  1.00-0.975           C  
ANISOU 1388  CB  ILE A 346     7920   3906   3855    -14    618   -111       C  
ATOM   1389  CG1 ILE A 346       1.724  -8.383   8.722  1.00-0.975           C  
ANISOU 1389  CG1 ILE A 346     8159   4131   4125     35    666   -110       C  
ATOM   1390  CG2 ILE A 346       0.556 -10.080   7.103  1.00-0.975           C  
ANISOU 1390  CG2 ILE A 346     7974   3883   3783    -48    611   -153       C  
ATOM   1391  CD1 ILE A 346       2.958  -9.213   9.061  1.00-0.975           C  
ANISOU 1391  CD1 ILE A 346     9518   5432   5479     57    702   -147       C  
ATOM   1392  N   ALA A 347       0.067  -5.989   7.209  1.00-1.313           N  
ANISOU 1392  N   ALA A 347     7674   3757   3601     46    615    -18       N  
ATOM   1393  CA  ALA A 347       0.432  -5.015   6.202  1.00-1.313           C  
ANISOU 1393  CA  ALA A 347     7545   3602   3395     59    627      6       C  
ATOM   1394  C   ALA A 347       1.737  -4.359   6.583  1.00-1.313           C  
ANISOU 1394  C   ALA A 347     8163   4167   4024     72    683      2       C  
ATOM   1395  O   ALA A 347       2.108  -4.348   7.758  1.00-1.313           O  
ANISOU 1395  O   ALA A 347     8253   4258   4193     81    699     -8       O  
ATOM   1396  CB  ALA A 347      -0.654  -3.965   6.037  1.00-1.313           C  
ANISOU 1396  CB  ALA A 347     7591   3697   3447     92    592     64       C  
ATOM   1397  N   LEU A 348       2.441  -3.817   5.587  1.00-1.164           N  
ANISOU 1397  N   LEU A 348     7699   3665   3477     64    712     11       N  
ATOM   1398  CA  LEU A 348       3.698  -3.111   5.816  1.00-1.164           C  
ANISOU 1398  CA  LEU A 348     7512   3446   3302     56    767     11       C  
ATOM   1399  C   LEU A 348       3.534  -1.654   5.459  1.00-1.164           C  
ANISOU 1399  C   LEU A 348     8068   3945   3798     62    774     65       C  
ATOM   1400  O   LEU A 348       2.795  -1.327   4.531  1.00-1.164           O  
ANISOU 1400  O   LEU A 348     8207   4067   3850     74    748     99       O  
ATOM   1401  CB  LEU A 348       4.822  -3.722   4.947  1.00-1.164           C  
ANISOU 1401  CB  LEU A 348     7469   3407   3209     36    812    -22       C  
ATOM   1402  CG  LEU A 348       5.385  -5.077   5.345  1.00-1.164           C  
ANISOU 1402  CG  LEU A 348     7847   3811   3634     46    825    -76       C  
ATOM   1403  CD1 LEU A 348       6.363  -5.569   4.287  1.00-1.164           C  
ANISOU 1403  CD1 LEU A 348     7693   3656   3409     43    878   -104       C  
ATOM   1404  CD2 LEU A 348       6.095  -5.019   6.722  1.00-1.164           C  
ANISOU 1404  CD2 LEU A 348     8143   4145   4054     56    838    -85       C  
ATOM   1405  N   MET A 349       4.223  -0.768   6.176  1.00-0.323           N  
ANISOU 1405  N   MET A 349     7704   3541   3466     50    805     74       N  
ATOM   1406  CA  MET A 349       4.240   0.642   5.786  1.00-0.323           C  
ANISOU 1406  CA  MET A 349     7725   3461   3400     46    823    123       C  
ATOM   1407  C   MET A 349       5.709   1.075   5.641  1.00-0.323           C  
ANISOU 1407  C   MET A 349     8190   3907   3855    -16    882    114       C  
ATOM   1408  O   MET A 349       6.552   0.735   6.477  1.00-0.323           O  
ANISOU 1408  O   MET A 349     8075   3850   3836    -41    899     78       O  
ATOM   1409  CB  MET A 349       3.498   1.545   6.798  1.00-0.323           C  
ANISOU 1409  CB  MET A 349     7969   3639   3663     85    804    148       C  
ATOM   1410  CG  MET A 349       1.979   1.458   6.729  1.00-0.323           C  
ANISOU 1410  CG  MET A 349     8277   3981   3972    152    754    177       C  
ATOM   1411  SD  MET A 349       1.300   2.550   8.009  1.00-0.323           S  
ANISOU 1411  SD  MET A 349     8788   4409   4502    212    755    200       S  
ATOM   1412  CE  MET A 349      -0.422   2.416   7.690  1.00-0.323           C  
ANISOU 1412  CE  MET A 349     8268   3984   4003    296    702    242       C  
ATOM   1413  N   LYS A 350       6.028   1.776   4.560  1.00-0.535           N  
ANISOU 1413  N   LYS A 350     7809   3459   3360    -43    914    151       N  
ATOM   1414  CA  LYS A 350       7.375   2.287   4.388  1.00-0.535           C  
ANISOU 1414  CA  LYS A 350     7744   3388   3289   -116    977    150       C  
ATOM   1415  C   LYS A 350       7.315   3.811   4.583  1.00-0.535           C  
ANISOU 1415  C   LYS A 350     8522   4002   3979   -144    989    198       C  
ATOM   1416  O   LYS A 350       6.440   4.470   4.014  1.00-0.535           O  
ANISOU 1416  O   LYS A 350     8571   3933   3909   -104    971    249       O  
ATOM   1417  CB  LYS A 350       7.932   1.940   2.996  1.00-0.535           C  
ANISOU 1417  CB  LYS A 350     8002   3682   3465   -141   1021    155       C  
ATOM   1418  CG  LYS A 350       9.435   2.150   2.914  1.00-0.535           C  
ANISOU 1418  CG  LYS A 350     8558   4302   4064   -217   1094    145       C  
ATOM   1419  CD  LYS A 350       9.898   2.381   1.493  1.00-0.535           C  
ANISOU 1419  CD  LYS A 350     9646   5369   5022   -252   1154    175       C  
ATOM   1420  CE  LYS A 350      11.354   2.754   1.471  1.00-0.535           C  
ANISOU 1420  CE  LYS A 350    10664   6470   6096   -338   1232    173       C  
ATOM   1421  NZ  LYS A 350      11.788   3.161   0.111  1.00-0.535           N  
ANISOU 1421  NZ  LYS A 350    11841   7612   7131   -382   1302    212       N  
ATOM   1422  N   LEU A 351       8.250   4.362   5.368  1.00-1.328           N  
ANISOU 1422  N   LEU A 351     7956   3422   3464   -212   1018    183       N  
ATOM   1423  CA  LEU A 351       8.321   5.793   5.602  1.00-1.328           C  
ANISOU 1423  CA  LEU A 351     8083   3360   3489   -256   1035    220       C  
ATOM   1424  C   LEU A 351       9.086   6.488   4.510  1.00-1.328           C  
ANISOU 1424  C   LEU A 351     8954   4163   4247   -336   1094    261       C  
ATOM   1425  O   LEU A 351      10.031   5.927   3.969  1.00-1.328           O  
ANISOU 1425  O   LEU A 351     8824   4178   4172   -387   1137    244       O  
ATOM   1426  CB  LEU A 351       8.972   6.085   6.969  1.00-1.328           C  
ANISOU 1426  CB  LEU A 351     8035   3318   3527   -312   1031    181       C  
ATOM   1427  CG  LEU A 351       8.280   5.488   8.192  1.00-1.328           C  
ANISOU 1427  CG  LEU A 351     8377   3708   3962   -241    979    142       C  
ATOM   1428  CD1 LEU A 351       9.097   5.766   9.428  1.00-1.328           C  
ANISOU 1428  CD1 LEU A 351     8396   3740   4045   -309    976    103       C  
ATOM   1429  CD2 LEU A 351       6.856   6.024   8.341  1.00-1.328           C  
ANISOU 1429  CD2 LEU A 351     8143   3326   3639   -149    950    174       C  
ATOM   1430  N   GLN A 352       8.705   7.746   4.227  1.00 0.173           N  
ANISOU 1430  N   GLN A 352     9095   4074   4224   -344   1105    318       N  
ATOM   1431  CA  GLN A 352       9.337   8.607   3.240  1.00 0.173           C  
ANISOU 1431  CA  GLN A 352     9169   4027   4153   -427   1165    370       C  
ATOM   1432  C   GLN A 352      10.777   8.946   3.670  1.00 0.173           C  
ANISOU 1432  C   GLN A 352     9969   4881   5022   -572   1217    345       C  
ATOM   1433  O   GLN A 352      11.664   9.000   2.826  1.00 0.173           O  
ANISOU 1433  O   GLN A 352    10089   5061   5118   -656   1279    365       O  
ATOM   1434  CB  GLN A 352       8.501   9.891   3.108  1.00 0.173           C  
ANISOU 1434  CB  GLN A 352     9475   4038   4262   -388   1155    435       C  
ATOM   1435  CG  GLN A 352       8.599  10.591   1.785  1.00 0.173           C  
ANISOU 1435  CG  GLN A 352    11084   5501   5675   -415   1197    511       C  
ATOM   1436  CD  GLN A 352       7.262  11.196   1.447  1.00 0.173           C  
ANISOU 1436  CD  GLN A 352    13099   7325   7535   -289   1153    574       C  
ATOM   1437  OE1 GLN A 352       6.380  10.537   0.859  1.00 0.173           O  
ANISOU 1437  OE1 GLN A 352    12020   6351   6461   -189   1106    588       O  
ATOM   1438  NE2 GLN A 352       7.086  12.465   1.815  1.00 0.173           N  
ANISOU 1438  NE2 GLN A 352    10872   4816   5165   -291   1164    613       N  
ATOM   1439  N   LYS A 353      10.996   9.187   4.977  1.00 0.533           N  
ANISOU 1439  N   LYS A 353     9635   4532   4769   -605   1192    304       N  
ATOM   1440  CA  LYS A 353      12.296   9.560   5.560  1.00 0.533           C  
ANISOU 1440  CA  LYS A 353     9604   4561   4811   -750   1223    277       C  
ATOM   1441  C   LYS A 353      12.655   8.551   6.656  1.00 0.533           C  
ANISOU 1441  C   LYS A 353     9738   4935   5158   -731   1182    207       C  
ATOM   1442  O   LYS A 353      11.773   8.219   7.450  1.00 0.533           O  
ANISOU 1442  O   LYS A 353     9766   4931   5209   -635   1126    183       O  
ATOM   1443  CB  LYS A 353      12.243  10.991   6.153  1.00 0.533           C  
ANISOU 1443  CB  LYS A 353    10003   4664   5058   -823   1224    295       C  
ATOM   1444  N   PRO A 354      13.911   8.039   6.724  1.00-0.715           N  
ANISOU 1444  N   PRO A 354     9081   4525   4656   -812   1208    178       N  
ATOM   1445  CA  PRO A 354      14.222   7.031   7.758  1.00-0.715           C  
ANISOU 1445  CA  PRO A 354     8877   4543   4643   -775   1163    120       C  
ATOM   1446  C   PRO A 354      14.268   7.629   9.158  1.00-0.715           C  
ANISOU 1446  C   PRO A 354     9177   4755   4946   -824   1114     89       C  
ATOM   1447  O   PRO A 354      14.576   8.812   9.346  1.00-0.715           O  
ANISOU 1447  O   PRO A 354     8950   4356   4614   -936   1128    101       O  
ATOM   1448  CB  PRO A 354      15.579   6.455   7.331  1.00-0.715           C  
ANISOU 1448  CB  PRO A 354     8952   4904   4871   -839   1211    108       C  
ATOM   1449  CG  PRO A 354      15.847   7.011   5.946  1.00-0.715           C  
ANISOU 1449  CG  PRO A 354     9739   5627   5544   -900   1288    160       C  
ATOM   1450  CD  PRO A 354      15.080   8.295   5.851  1.00-0.715           C  
ANISOU 1450  CD  PRO A 354     9338   4891   4928   -931   1283    202       C  
ATOM   1451  N   LEU A 355      13.909   6.804  10.132  1.00-0.797           N  
ANISOU 1451  N   LEU A 355     8686   4357   4553   -741   1058     48       N  
ATOM   1452  CA  LEU A 355      13.921   7.142  11.543  1.00-0.797           C  
ANISOU 1452  CA  LEU A 355     8664   4280   4537   -770   1007     11       C  
ATOM   1453  C   LEU A 355      15.348   7.202  12.059  1.00-0.797           C  
ANISOU 1453  C   LEU A 355     9401   5213   5398   -899   1001    -16       C  
ATOM   1454  O   LEU A 355      16.233   6.513  11.556  1.00-0.797           O  
ANISOU 1454  O   LEU A 355     9224   5294   5367   -915   1027    -15       O  
ATOM   1455  CB  LEU A 355      13.162   6.078  12.343  1.00-0.797           C  
ANISOU 1455  CB  LEU A 355     8557   4245   4502   -640    955    -19       C  
ATOM   1456  CG  LEU A 355      11.689   5.896  12.056  1.00-0.797           C  
ANISOU 1456  CG  LEU A 355     9136   4682   4993   -514    948      2       C  
ATOM   1457  CD1 LEU A 355      11.233   4.524  12.532  1.00-0.797           C  
ANISOU 1457  CD1 LEU A 355     9075   4771   5043   -410    912    -23       C  
ATOM   1458  CD2 LEU A 355      10.858   6.991  12.710  1.00-0.797           C  
ANISOU 1458  CD2 LEU A 355     9230   4509   4934   -503    936      6       C  
ATOM   1459  N   THR A 356      15.546   7.994  13.102  1.00 0.777           N  
ANISOU 1459  N   THR A 356     9518   5215   5457   -984    966    -42       N  
ATOM   1460  CA  THR A 356      16.815   8.138  13.804  1.00 0.777           C  
ANISOU 1460  CA  THR A 356     9492   5370   5539  -1117    940    -71       C  
ATOM   1461  C   THR A 356      16.675   7.264  15.038  1.00 0.777           C  
ANISOU 1461  C   THR A 356     9617   5621   5758  -1035    868   -113       C  
ATOM   1462  O   THR A 356      15.803   7.530  15.867  1.00 0.777           O  
ANISOU 1462  O   THR A 356     9844   5645   5867   -984    834   -133       O  
ATOM   1463  CB  THR A 356      17.051   9.618  14.162  1.00 0.777           C  
ANISOU 1463  CB  THR A 356    10948   6572   6829  -1274    941    -77       C  
ATOM   1464  OG1 THR A 356      17.033  10.388  12.962  1.00 0.777           O  
ANISOU 1464  OG1 THR A 356    11386   6859   7156  -1334   1012    -27       O  
ATOM   1465  CG2 THR A 356      18.361   9.847  14.905  1.00 0.777           C  
ANISOU 1465  CG2 THR A 356    10774   6587   6759  -1438    903   -110       C  
ATOM   1466  N   PHE A 357      17.468   6.186  15.121  1.00-0.006           N  
ANISOU 1466  N   PHE A 357     8848   5178   5190  -1005    852   -122       N  
ATOM   1467  CA  PHE A 357      17.447   5.301  16.278  1.00-0.006           C  
ANISOU 1467  CA  PHE A 357     8661   5118   5088   -927    782   -154       C  
ATOM   1468  C   PHE A 357      18.265   5.897  17.436  1.00-0.006           C  
ANISOU 1468  C   PHE A 357     9428   5938   5865  -1056    720   -187       C  
ATOM   1469  O   PHE A 357      19.307   6.531  17.216  1.00-0.006           O  
ANISOU 1469  O   PHE A 357     9459   6080   5948  -1206    730   -185       O  
ATOM   1470  CB  PHE A 357      17.895   3.872  15.932  1.00-0.006           C  
ANISOU 1470  CB  PHE A 357     8531   5278   5144   -821    788   -147       C  
ATOM   1471  CG  PHE A 357      17.017   3.082  14.981  1.00-0.006           C  
ANISOU 1471  CG  PHE A 357     8442   5128   5029   -687    832   -126       C  
ATOM   1472  CD1 PHE A 357      15.658   3.366  14.856  1.00-0.006           C  
ANISOU 1472  CD1 PHE A 357     8724   5143   5156   -628    838   -118       C  
ATOM   1473  CD2 PHE A 357      17.542   2.041  14.233  1.00-0.006           C  
ANISOU 1473  CD2 PHE A 357     8350   5252   5067   -618    866   -118       C  
ATOM   1474  CE1 PHE A 357      14.847   2.629  13.992  1.00-0.006           C  
ANISOU 1474  CE1 PHE A 357     8696   5079   5107   -519    868   -100       C  
ATOM   1475  CE2 PHE A 357      16.733   1.311  13.359  1.00-0.006           C  
ANISOU 1475  CE2 PHE A 357     8663   5490   5333   -509    902   -106       C  
ATOM   1476  CZ  PHE A 357      15.382   1.581  13.282  1.00-0.006           C  
ANISOU 1476  CZ  PHE A 357     8535   5111   5057   -465    896    -98       C  
ATOM   1477  N   ASN A 358      17.745   5.740  18.660  1.00-0.634           N  
ANISOU 1477  N   ASN A 358     9089   5507   5459  -1007    658   -217       N  
ATOM   1478  CA  ASN A 358      18.311   6.244  19.921  1.00-0.634           C  
ANISOU 1478  CA  ASN A 358     8998   5425   5334  -1112    585   -257       C  
ATOM   1479  C   ASN A 358      17.775   5.371  21.071  1.00-0.634           C  
ANISOU 1479  C   ASN A 358     9418   5859   5746   -990    524   -276       C  
ATOM   1480  O   ASN A 358      17.210   4.319  20.788  1.00-0.634           O  
ANISOU 1480  O   ASN A 358     9416   5914   5805   -844    541   -256       O  
ATOM   1481  CB  ASN A 358      17.966   7.743  20.102  1.00-0.634           C  
ANISOU 1481  CB  ASN A 358     9336   5421   5446  -1233    598   -276       C  
ATOM   1482  CG  ASN A 358      16.497   8.105  19.974  1.00-0.634           C  
ANISOU 1482  CG  ASN A 358    11834   7577   7752  -1125    637   -268       C  
ATOM   1483  OD1 ASN A 358      15.600   7.426  20.472  1.00-0.634           O  
ANISOU 1483  OD1 ASN A 358    10241   5949   6143   -984    623   -272       O  
ATOM   1484  ND2 ASN A 358      16.216   9.203  19.308  1.00-0.634           N  
ANISOU 1484  ND2 ASN A 358    11741   7225   7508  -1189    689   -254       N  
ATOM   1485  N   ASP A 359      17.894   5.789  22.346  1.00 0.972           N  
ANISOU 1485  N   ASP A 359     9050   5418   5281  -1051    457   -315       N  
ATOM   1486  CA  ASP A 359      17.394   4.957  23.444  1.00 0.972           C  
ANISOU 1486  CA  ASP A 359     9060   5438   5267   -937    404   -328       C  
ATOM   1487  C   ASP A 359      15.857   4.868  23.505  1.00 0.972           C  
ANISOU 1487  C   ASP A 359     9149   5258   5211   -810    447   -323       C  
ATOM   1488  O   ASP A 359      15.344   3.971  24.165  1.00 0.972           O  
ANISOU 1488  O   ASP A 359     9055   5194   5121   -698    424   -320       O  
ATOM   1489  CB  ASP A 359      17.997   5.378  24.794  1.00 0.972           C  
ANISOU 1489  CB  ASP A 359     9478   5870   5613  -1038    317   -372       C  
ATOM   1490  CG  ASP A 359      19.453   4.964  24.961  1.00 0.972           C  
ANISOU 1490  CG  ASP A 359    11788   8550   8121  -1113    251   -368       C  
ATOM   1491  OD1 ASP A 359      19.822   3.860  24.477  1.00 0.972           O  
ANISOU 1491  OD1 ASP A 359    11952   8978   8479  -1012    257   -333       O  
ATOM   1492  OD2 ASP A 359      20.223   5.736  25.579  1.00 0.972           O  
ANISOU 1492  OD2 ASP A 359    12715   9508   9009  -1271    193   -402       O  
ATOM   1493  N   LEU A 360      15.138   5.720  22.748  1.00 0.758           N  
ANISOU 1493  N   LEU A 360     8530   4402   4477   -820    512   -314       N  
ATOM   1494  CA  LEU A 360      13.669   5.751  22.711  1.00 0.758           C  
ANISOU 1494  CA  LEU A 360     8460   4103   4285   -700    555   -304       C  
ATOM   1495  C   LEU A 360      13.042   5.138  21.453  1.00 0.758           C  
ANISOU 1495  C   LEU A 360     8399   4086   4308   -602    611   -259       C  
ATOM   1496  O   LEU A 360      11.838   4.869  21.427  1.00 0.758           O  
ANISOU 1496  O   LEU A 360     8161   3738   4016   -492    636   -245       O  
ATOM   1497  CB  LEU A 360      13.195   7.219  22.858  1.00 0.758           C  
ANISOU 1497  CB  LEU A 360     8648   3963   4256   -763    583   -325       C  
ATOM   1498  CG  LEU A 360      13.573   7.947  24.167  1.00 0.758           C  
ANISOU 1498  CG  LEU A 360     9263   4452   4723   -858    532   -381       C  
ATOM   1499  CD1 LEU A 360      13.215   9.433  24.087  1.00 0.758           C  
ANISOU 1499  CD1 LEU A 360     9525   4361   4759   -928    570   -401       C  
ATOM   1500  CD2 LEU A 360      12.920   7.299  25.374  1.00 0.758           C  
ANISOU 1500  CD2 LEU A 360     9364   4542   4770   -758    502   -401       C  
ATOM   1501  N   VAL A 361      13.830   5.008  20.380  1.00-0.763           N  
ANISOU 1501  N   VAL A 361     7965   3806   3993   -649    633   -236       N  
ATOM   1502  CA  VAL A 361      13.370   4.545  19.058  1.00-0.763           C  
ANISOU 1502  CA  VAL A 361     7778   3649   3860   -577    687   -198       C  
ATOM   1503  C   VAL A 361      14.358   3.493  18.588  1.00-0.763           C  
ANISOU 1503  C   VAL A 361     8202   4367   4472   -568    682   -189       C  
ATOM   1504  O   VAL A 361      15.526   3.803  18.363  1.00-0.763           O  
ANISOU 1504  O   VAL A 361     8137   4447   4487   -669    681   -191       O  
ATOM   1505  CB  VAL A 361      13.251   5.702  18.022  1.00-0.763           C  
ANISOU 1505  CB  VAL A 361     8339   4037   4321   -642    740   -175       C  
ATOM   1506  CG1 VAL A 361      12.627   5.214  16.715  1.00-0.763           C  
ANISOU 1506  CG1 VAL A 361     8246   3959   4255   -558    787   -135       C  
ATOM   1507  CG2 VAL A 361      12.475   6.890  18.573  1.00-0.763           C  
ANISOU 1507  CG2 VAL A 361     8505   3894   4286   -656    746   -187       C  
ATOM   1508  N   LYS A 362      13.897   2.253  18.466  1.00-0.100           N  
ANISOU 1508  N   LYS A 362     7775   4027   4114   -449    681   -179       N  
ATOM   1509  CA  LYS A 362      14.720   1.097  18.077  1.00-0.100           C  
ANISOU 1509  CA  LYS A 362     7670   4170   4168   -406    681   -172       C  
ATOM   1510  C   LYS A 362      13.815   0.021  17.460  1.00-0.100           C  
ANISOU 1510  C   LYS A 362     7881   4352   4380   -285    705   -157       C  
ATOM   1511  O   LYS A 362      12.655  -0.110  17.868  1.00-0.100           O  
ANISOU 1511  O   LYS A 362     7650   3974   4064   -229    696   -155       O  
ATOM   1512  CB  LYS A 362      15.353   0.470  19.344  1.00-0.100           C  
ANISOU 1512  CB  LYS A 362     8141   4788   4710   -391    614   -189       C  
ATOM   1513  CG  LYS A 362      16.516   1.233  19.971  1.00-0.100           C  
ANISOU 1513  CG  LYS A 362     8997   5763   5609   -515    573   -207       C  
ATOM   1514  CD  LYS A 362      16.816   0.701  21.353  1.00-0.100           C  
ANISOU 1514  CD  LYS A 362     9381   6236   6012   -488    495   -222       C  
ATOM   1515  CE  LYS A 362      18.098   1.267  21.899  1.00-0.100           C  
ANISOU 1515  CE  LYS A 362     9941   6979   6645   -609    442   -238       C  
ATOM   1516  NZ  LYS A 362      18.355   0.772  23.266  1.00-0.100           N  
ANISOU 1516  NZ  LYS A 362    10695   7809   7394   -581    357   -251       N  
ATOM   1517  N   PRO A 363      14.332  -0.862  16.590  1.00-0.672           N  
ANISOU 1517  N   PRO A 363     7450   4069   4045   -241    734   -149       N  
ATOM   1518  CA  PRO A 363      13.454  -1.917  16.068  1.00-0.672           C  
ANISOU 1518  CA  PRO A 363     7385   3948   3957   -139    751   -142       C  
ATOM   1519  C   PRO A 363      13.362  -3.152  16.966  1.00-0.672           C  
ANISOU 1519  C   PRO A 363     7632   4240   4240    -53    712   -148       C  
ATOM   1520  O   PRO A 363      14.230  -3.391  17.819  1.00-0.672           O  
ANISOU 1520  O   PRO A 363     7269   4004   3947    -53    674   -155       O  
ATOM   1521  CB  PRO A 363      14.077  -2.258  14.717  1.00-0.672           C  
ANISOU 1521  CB  PRO A 363     7560   4229   4186   -132    805   -135       C  
ATOM   1522  CG  PRO A 363      15.519  -1.863  14.832  1.00-0.672           C  
ANISOU 1522  CG  PRO A 363     7988   4855   4727   -199    809   -139       C  
ATOM   1523  CD  PRO A 363      15.682  -0.910  15.970  1.00-0.672           C  
ANISOU 1523  CD  PRO A 363     7421   4254   4139   -283    761   -146       C  
ATOM   1524  N   VAL A 364      12.283  -3.935  16.761  1.00-0.613           N  
ANISOU 1524  N   VAL A 364     7030   3529   3580     15    718   -144       N  
ATOM   1525  CA  VAL A 364      12.041  -5.237  17.379  1.00-0.613           C  
ANISOU 1525  CA  VAL A 364     6938   3433   3493     95    694   -144       C  
ATOM   1526  C   VAL A 364      12.541  -6.273  16.337  1.00-0.613           C  
ANISOU 1526  C   VAL A 364     7647   4210   4245    153    729   -148       C  
ATOM   1527  O   VAL A 364      12.538  -5.956  15.148  1.00-0.613           O  
ANISOU 1527  O   VAL A 364     7615   4176   4202    130    772   -150       O  
ATOM   1528  CB  VAL A 364      10.539  -5.423  17.759  1.00-0.613           C  
ANISOU 1528  CB  VAL A 364     7320   3654   3781    115    686   -136       C  
ATOM   1529  CG1 VAL A 364       9.611  -5.433  16.538  1.00-0.613           C  
ANISOU 1529  CG1 VAL A 364     7374   3631   3788    116    720   -130       C  
ATOM   1530  CG2 VAL A 364      10.332  -6.650  18.615  1.00-0.613           C  
ANISOU 1530  CG2 VAL A 364     7260   3573   3710    178    660   -132       C  
ATOM   1531  N   CYS A 365      12.999  -7.478  16.761  1.00-1.136           N  
ANISOU 1531  N   CYS A 365     7496   4104   4127    232    715   -149       N  
ATOM   1532  CA  CYS A 365      13.492  -8.466  15.799  1.00-1.136           C  
ANISOU 1532  CA  CYS A 365     7568   4214   4220    300    755   -159       C  
ATOM   1533  C   CYS A 365      12.351  -9.237  15.175  1.00-1.136           C  
ANISOU 1533  C   CYS A 365     7934   4403   4477    325    773   -165       C  
ATOM   1534  O   CYS A 365      11.427  -9.666  15.877  1.00-1.136           O  
ANISOU 1534  O   CYS A 365     7783   4132   4263    332    743   -158       O  
ATOM   1535  CB  CYS A 365      14.506  -9.429  16.422  1.00-1.136           C  
ANISOU 1535  CB  CYS A 365     7795   4551   4518    390    737   -155       C  
ATOM   1536  SG  CYS A 365      16.009  -8.651  17.074  1.00-1.136           S  
ANISOU 1536  SG  CYS A 365     8285   5314   5165    358    708   -147       S  
ATOM   1537  N   LEU A 366      12.464  -9.509  13.861  1.00-1.070           N  
ANISOU 1537  N   LEU A 366     7450   3909   3966    338    821   -181       N  
ATOM   1538  CA  LEU A 366      11.494 -10.357  13.184  1.00-1.070           C  
ANISOU 1538  CA  LEU A 366     7525   3822   3928    355    833   -194       C  
ATOM   1539  C   LEU A 366      11.730 -11.798  13.690  1.00-1.070           C  
ANISOU 1539  C   LEU A 366     7946   4175   4322    444    826   -201       C  
ATOM   1540  O   LEU A 366      12.883 -12.169  13.952  1.00-1.070           O  
ANISOU 1540  O   LEU A 366     7633   3970   4081    514    836   -201       O  
ATOM   1541  CB  LEU A 366      11.662 -10.306  11.655  1.00-1.070           C  
ANISOU 1541  CB  LEU A 366     7550   3847   3908    348    886   -213       C  
ATOM   1542  CG  LEU A 366      11.087  -9.085  10.929  1.00-1.070           C  
ANISOU 1542  CG  LEU A 366     8051   4342   4377    266    892   -200       C  
ATOM   1543  CD1 LEU A 366      11.472  -9.139   9.442  1.00-1.070           C  
ANISOU 1543  CD1 LEU A 366     7765   4067   4036    268    950   -217       C  
ATOM   1544  CD2 LEU A 366       9.533  -9.012  11.089  1.00-1.070           C  
ANISOU 1544  CD2 LEU A 366     8346   4507   4595    229    852   -190       C  
ATOM   1545  N   PRO A 367      10.655 -12.585  13.905  1.00-0.970           N  
ANISOU 1545  N   PRO A 367     7635   3691   3911    441    807   -202       N  
ATOM   1546  CA  PRO A 367      10.842 -13.957  14.402  1.00-0.970           C  
ANISOU 1546  CA  PRO A 367     7858   3805   4080    521    803   -204       C  
ATOM   1547  C   PRO A 367      11.414 -14.898  13.344  1.00-0.970           C  
ANISOU 1547  C   PRO A 367     8747   4629   4906    592    852   -237       C  
ATOM   1548  O   PRO A 367      11.002 -14.843  12.187  1.00-0.970           O  
ANISOU 1548  O   PRO A 367     8811   4638   4901    554    880   -263       O  
ATOM   1549  CB  PRO A 367       9.431 -14.362  14.839  1.00-0.970           C  
ANISOU 1549  CB  PRO A 367     8098   3880   4225    466    774   -194       C  
ATOM   1550  CG  PRO A 367       8.538 -13.613  13.894  1.00-0.970           C  
ANISOU 1550  CG  PRO A 367     8452   4238   4558    382    780   -204       C  
ATOM   1551  CD  PRO A 367       9.230 -12.287  13.660  1.00-0.970           C  
ANISOU 1551  CD  PRO A 367     7782   3739   3988    364    790   -199       C  
ATOM   1552  N   ASN A 368      12.369 -15.751  13.746  1.00 0.494           N  
ANISOU 1552  N   ASN A 368     8496   4383   4669    702    862   -235       N  
ATOM   1553  CA  ASN A 368      13.007 -16.716  12.855  1.00 0.494           C  
ANISOU 1553  CA  ASN A 368     8650   4463   4756    797    918   -267       C  
ATOM   1554  C   ASN A 368      12.275 -18.046  12.933  1.00 0.494           C  
ANISOU 1554  C   ASN A 368     9176   4699   5105    821    914   -280       C  
ATOM   1555  O   ASN A 368      11.752 -18.363  14.003  1.00 0.494           O  
ANISOU 1555  O   ASN A 368     9063   4497   4966    806    869   -250       O  
ATOM   1556  CB  ASN A 368      14.462 -16.963  13.297  1.00 0.494           C  
ANISOU 1556  CB  ASN A 368     8850   4833   5072    924    932   -252       C  
ATOM   1557  CG  ASN A 368      15.391 -15.791  13.132  1.00 0.494           C  
ANISOU 1557  CG  ASN A 368     9070   5354   5470    899    944   -243       C  
ATOM   1558  OD1 ASN A 368      15.264 -14.998  12.200  1.00 0.494           O  
ANISOU 1558  OD1 ASN A 368     8609   4952   5018    823    977   -259       O  
ATOM   1559  ND2 ASN A 368      16.354 -15.665  14.035  1.00 0.494           N  
ANISOU 1559  ND2 ASN A 368     7322   3800   3858    957    916   -213       N  
ATOM   1560  N   PRO A 369      12.257 -18.884  11.861  1.00 0.663           N  
ANISOU 1560  N   PRO A 369     9013   4365   4802    857    962   -325       N  
ATOM   1561  CA  PRO A 369      11.679 -20.225  12.016  1.00 0.663           C  
ANISOU 1561  CA  PRO A 369     9195   4241   4799    880    959   -338       C  
ATOM   1562  C   PRO A 369      12.478 -20.947  13.108  1.00 0.663           C  
ANISOU 1562  C   PRO A 369     9942   4964   5569   1011    950   -303       C  
ATOM   1563  O   PRO A 369      13.681 -20.685  13.268  1.00 0.663           O  
ANISOU 1563  O   PRO A 369     9878   5107   5638   1116    966   -289       O  
ATOM   1564  CB  PRO A 369      11.911 -20.868  10.646  1.00 0.663           C  
ANISOU 1564  CB  PRO A 369     9502   4406   4963    921   1022   -398       C  
ATOM   1565  CG  PRO A 369      12.999 -20.096  10.023  1.00 0.663           C  
ANISOU 1565  CG  PRO A 369     9851   5013   5448    978   1070   -405       C  
ATOM   1566  CD  PRO A 369      12.821 -18.704  10.504  1.00 0.663           C  
ANISOU 1566  CD  PRO A 369     9172   4584   4945    883   1027   -366       C  
ATOM   1567  N   GLY A 370      11.794 -21.784  13.886  1.00 0.886           N  
ANISOU 1567  N   GLY A 370     9507   4297   5012    996    919   -282       N  
ATOM   1568  CA  GLY A 370      12.409 -22.545  14.955  1.00 0.886           C  
ANISOU 1568  CA  GLY A 370     9391   4112   4879   1119    904   -241       C  
ATOM   1569  C   GLY A 370      12.623 -21.777  16.238  1.00 0.886           C  
ANISOU 1569  C   GLY A 370     9736   4676   5379   1110    847   -183       C  
ATOM   1570  O   GLY A 370      13.572 -22.082  16.964  1.00 0.886           O  
ANISOU 1570  O   GLY A 370     9653   4665   5346   1237    834   -149       O  
ATOM   1571  N   MET A 371      11.738 -20.790  16.554  1.00 0.205           N  
ANISOU 1571  N   MET A 371     9147   4188   4854    966    812   -172       N  
ATOM   1572  CA  MET A 371      11.815 -20.047  17.836  1.00 0.205           C  
ANISOU 1572  CA  MET A 371     9022   4232   4840    945    758   -124       C  
ATOM   1573  C   MET A 371      11.604 -21.001  19.028  1.00 0.205           C  
ANISOU 1573  C   MET A 371    10002   5022   5704    991    729    -77       C  
ATOM   1574  O   MET A 371      12.167 -20.775  20.100  1.00 0.205           O  
ANISOU 1574  O   MET A 371     9885   5025   5651   1042    688    -35       O  
ATOM   1575  CB  MET A 371      10.761 -18.930  17.919  1.00 0.205           C  
ANISOU 1575  CB  MET A 371     9168   4461   5035    793    738   -124       C  
ATOM   1576  CG  MET A 371      11.080 -17.690  17.076  1.00 0.205           C  
ANISOU 1576  CG  MET A 371     9472   4988   5471    747    753   -151       C  
ATOM   1577  SD  MET A 371      12.798 -17.129  17.148  1.00 0.205           S  
ANISOU 1577  SD  MET A 371     9634   5433   5803    842    755   -146       S  
ATOM   1578  CE  MET A 371      12.885 -16.614  18.811  1.00 0.205           C  
ANISOU 1578  CE  MET A 371     9087   4987   5316    828    687    -99       C  
ATOM   1579  N   MET A 372      10.787 -22.064  18.826  1.00 1.007           N  
ANISOU 1579  N   MET A 372     9947   4662   5465    964    749    -84       N  
ATOM   1580  CA  MET A 372      10.436 -23.084  19.835  1.00 1.007           C  
ANISOU 1580  CA  MET A 372    10158   4629   5523    989    733    -38       C  
ATOM   1581  C   MET A 372       9.840 -22.446  21.090  1.00 1.007           C  
ANISOU 1581  C   MET A 372    10125   4687   5531    908    689     10       C  
ATOM   1582  O   MET A 372      10.307 -22.674  22.214  1.00 1.007           O  
ANISOU 1582  O   MET A 372     9950   4510   5336    981    657     61       O  
ATOM   1583  CB  MET A 372      11.616 -24.015  20.161  1.00 1.007           C  
ANISOU 1583  CB  MET A 372    10697   5087   6011   1176    736    -13       C  
ATOM   1584  CG  MET A 372      12.167 -24.738  18.947  1.00 1.007           C  
ANISOU 1584  CG  MET A 372    11579   5846   6824   1271    791    -62       C  
ATOM   1585  SD  MET A 372      12.743 -26.391  19.370  1.00 1.007           S  
ANISOU 1585  SD  MET A 372    12787   6705   7819   1448    808    -29       S  
ATOM   1586  CE  MET A 372      14.068 -25.996  20.591  1.00 1.007           C  
ANISOU 1586  CE  MET A 372    12243   6461   7444   1610    751     42       C  
ATOM   1587  N   LEU A 373       8.822 -21.597  20.883  1.00 0.061           N  
ANISOU 1587  N   LEU A 373     9183   3834   4645    765    689     -6       N  
ATOM   1588  CA  LEU A 373       8.171 -20.946  22.011  1.00 0.061           C  
ANISOU 1588  CA  LEU A 373     8944   3676   4436    690    660     32       C  
ATOM   1589  C   LEU A 373       7.399 -21.954  22.868  1.00 0.061           C  
ANISOU 1589  C   LEU A 373     9572   4055   4896    657    663     77       C  
ATOM   1590  O   LEU A 373       6.969 -22.995  22.361  1.00 0.061           O  
ANISOU 1590  O   LEU A 373     9385   3625   4573    635    689     67       O  
ATOM   1591  CB  LEU A 373       7.227 -19.835  21.513  1.00 0.061           C  
ANISOU 1591  CB  LEU A 373     8736   3612   4323    563    667      5       C  
ATOM   1592  CG  LEU A 373       7.847 -18.683  20.718  1.00 0.061           C  
ANISOU 1592  CG  LEU A 373     8929   4038   4667    571    667    -31       C  
ATOM   1593  CD1 LEU A 373       6.810 -17.612  20.462  1.00 0.061           C  
ANISOU 1593  CD1 LEU A 373     8661   3876   4464    457    670    -43       C  
ATOM   1594  CD2 LEU A 373       9.084 -18.106  21.419  1.00 0.061           C  
ANISOU 1594  CD2 LEU A 373     8979   4269   4816    654    637    -15       C  
ATOM   1595  N   GLN A 374       7.232 -21.641  24.181  1.00 1.383           N  
ANISOU 1595  N   GLN A 374     9302   3833   4618    647    638    126       N  
ATOM   1596  CA  GLN A 374       6.467 -22.484  25.101  1.00 1.383           C  
ANISOU 1596  CA  GLN A 374     9358   3670   4513    605    646    177       C  
ATOM   1597  C   GLN A 374       4.983 -22.421  24.668  1.00 1.383           C  
ANISOU 1597  C   GLN A 374     9578   3846   4719    444    679    161       C  
ATOM   1598  O   GLN A 374       4.564 -21.377  24.151  1.00 1.383           O  
ANISOU 1598  O   GLN A 374     9297   3767   4574    381    681    128       O  
ATOM   1599  CB  GLN A 374       6.615 -21.972  26.568  1.00 1.383           C  
ANISOU 1599  CB  GLN A 374     9532   3941   4686    624    614    228       C  
ATOM   1600  CG  GLN A 374       8.059 -21.858  27.104  1.00 1.383           C  
ANISOU 1600  CG  GLN A 374    11870   6385   7060    770    565    247       C  
ATOM   1601  CD  GLN A 374       8.893 -23.116  26.940  1.00 1.383           C  
ANISOU 1601  CD  GLN A 374    15835  10157  10918    902    562    269       C  
ATOM   1602  OE1 GLN A 374       9.895 -23.128  26.216  1.00 1.383           O  
ANISOU 1602  OE1 GLN A 374    15381   9797  10551   1003    556    240       O  
ATOM   1603  NE2 GLN A 374       8.505 -24.204  27.610  1.00 1.383           N  
ANISOU 1603  NE2 GLN A 374    15386   9430  10272    911    572    322       N  
ATOM   1604  N   PRO A 375       4.170 -23.480  24.895  1.00 1.122           N  
ANISOU 1604  N   PRO A 375     9497   3516   4479    373    704    189       N  
ATOM   1605  CA  PRO A 375       2.740 -23.426  24.502  1.00 1.122           C  
ANISOU 1605  CA  PRO A 375     9501   3522   4493    209    731    178       C  
ATOM   1606  C   PRO A 375       2.009 -22.200  25.047  1.00 1.122           C  
ANISOU 1606  C   PRO A 375     9637   3915   4764    143    733    189       C  
ATOM   1607  O   PRO A 375       1.117 -21.660  24.387  1.00 1.122           O  
ANISOU 1607  O   PRO A 375     9233   3640   4454     48    744    162       O  
ATOM   1608  CB  PRO A 375       2.152 -24.698  25.114  1.00 1.122           C  
ANISOU 1608  CB  PRO A 375    10018   3745   4811    150    754    226       C  
ATOM   1609  CG  PRO A 375       3.306 -25.622  25.273  1.00 1.122           C  
ANISOU 1609  CG  PRO A 375    10743   4244   5398    293    743    242       C  
ATOM   1610  CD  PRO A 375       4.512 -24.776  25.524  1.00 1.122           C  
ANISOU 1610  CD  PRO A 375     9967   3692   4752    436    707    237       C  
ATOM   1611  N   GLU A 376       2.391 -21.771  26.261  1.00 0.522           N  
ANISOU 1611  N   GLU A 376     9204   3550   4328    201    721    228       N  
ATOM   1612  CA  GLU A 376       1.833 -20.594  26.930  1.00 0.522           C  
ANISOU 1612  CA  GLU A 376     9055   3614   4276    161    727    237       C  
ATOM   1613  C   GLU A 376       2.931 -19.558  27.204  1.00 0.522           C  
ANISOU 1613  C   GLU A 376     9241   3973   4553    261    689    219       C  
ATOM   1614  O   GLU A 376       3.008 -18.998  28.291  1.00 0.522           O  
ANISOU 1614  O   GLU A 376     9094   3895   4392    278    681    243       O  
ATOM   1615  CB  GLU A 376       1.068 -21.004  28.202  1.00 0.522           C  
ANISOU 1615  CB  GLU A 376     9326   3796   4432    107    757    298       C  
ATOM   1616  CG  GLU A 376      -0.096 -21.935  27.882  1.00 0.522           C  
ANISOU 1616  CG  GLU A 376    10715   5045   5750    -21    797    315       C  
ATOM   1617  CD  GLU A 376      -0.970 -22.281  29.067  1.00 0.522           C  
ANISOU 1617  CD  GLU A 376    12336   6604   7271    -95    839    378       C  
ATOM   1618  OE1 GLU A 376      -0.447 -22.907  30.012  1.00 0.522           O  
ANISOU 1618  OE1 GLU A 376    10963   5058   5743    -40    835    427       O  
ATOM   1619  OE2 GLU A 376      -2.173 -21.937  29.050  1.00 0.522           O  
ANISOU 1619  OE2 GLU A 376    10526   4926   5536   -205    879    383       O  
ATOM   1620  N   GLN A 377       3.760 -19.272  26.177  1.00 0.230           N  
ANISOU 1620  N   GLN A 377     8575   3380   3978    315    668    173       N  
ATOM   1621  CA  GLN A 377       4.875 -18.330  26.259  1.00 0.230           C  
ANISOU 1621  CA  GLN A 377     8339   3317   3840    392    633    152       C  
ATOM   1622  C   GLN A 377       4.419 -16.992  26.829  1.00 0.230           C  
ANISOU 1622  C   GLN A 377     8564   3708   4135    348    634    147       C  
ATOM   1623  O   GLN A 377       3.347 -16.523  26.452  1.00 0.230           O  
ANISOU 1623  O   GLN A 377     8334   3527   3951    270    665    135       O  
ATOM   1624  CB  GLN A 377       5.496 -18.142  24.862  1.00 0.230           C  
ANISOU 1624  CB  GLN A 377     8369   3416   3967    420    631    103       C  
ATOM   1625  CG  GLN A 377       6.674 -17.163  24.825  1.00 0.230           C  
ANISOU 1625  CG  GLN A 377     8408   3649   4121    482    599     81       C  
ATOM   1626  CD  GLN A 377       8.017 -17.750  25.209  1.00 0.230           C  
ANISOU 1626  CD  GLN A 377     9601   4839   5298    598    566     98       C  
ATOM   1627  OE1 GLN A 377       8.220 -18.955  25.223  1.00 0.230           O  
ANISOU 1627  OE1 GLN A 377     9149   4220   4749    658    571    119       O  
ATOM   1628  NE2 GLN A 377       8.982 -16.901  25.511  1.00 0.230           N  
ANISOU 1628  NE2 GLN A 377     8670   4097   4463    634    530     90       N  
ATOM   1629  N   LEU A 378       5.214 -16.408  27.765  1.00 1.528           N  
ANISOU 1629  N   LEU A 378     8341   3564   3910    399    598    155       N  
ATOM   1630  CA  LEU A 378       4.981 -15.101  28.392  1.00 1.528           C  
ANISOU 1630  CA  LEU A 378     8320   3669   3925    369    596    142       C  
ATOM   1631  C   LEU A 378       5.327 -14.016  27.387  1.00 1.528           C  
ANISOU 1631  C   LEU A 378     8671   4164   4411    357    591     93       C  
ATOM   1632  O   LEU A 378       6.470 -13.950  26.923  1.00 1.528           O  
ANISOU 1632  O   LEU A 378     8485   4046   4287    404    559     75       O  
ATOM   1633  CB  LEU A 378       5.856 -14.941  29.653  1.00 1.528           C  
ANISOU 1633  CB  LEU A 378     8469   3835   4003    422    548    163       C  
ATOM   1634  CG  LEU A 378       5.496 -13.791  30.605  1.00 1.528           C  
ANISOU 1634  CG  LEU A 378     9196   4625   4696    387    550    153       C  
ATOM   1635  CD1 LEU A 378       5.639 -14.245  32.071  1.00 1.528           C  
ANISOU 1635  CD1 LEU A 378     9450   4797   4793    415    527    197       C  
ATOM   1636  CD2 LEU A 378       6.380 -12.594  30.378  1.00 1.528           C  
ANISOU 1636  CD2 LEU A 378     9619   5192   5209    391    511    108       C  
ATOM   1637  N   CYS A 379       4.337 -13.167  27.057  1.00-0.829           N  
ANISOU 1637  N   CYS A 379     8008   3552   3793    299    625     77       N  
ATOM   1638  CA  CYS A 379       4.459 -12.096  26.059  1.00-0.829           C  
ANISOU 1638  CA  CYS A 379     7726   3377   3617    281    628     38       C  
ATOM   1639  C   CYS A 379       3.963 -10.772  26.644  1.00-0.829           C  
ANISOU 1639  C   CYS A 379     7715   3418   3603    257    642     27       C  
ATOM   1640  O   CYS A 379       3.366 -10.756  27.720  1.00-0.829           O  
ANISOU 1640  O   CYS A 379     7379   3043   3189    251    658     46       O  
ATOM   1641  CB  CYS A 379       3.698 -12.442  24.770  1.00-0.829           C  
ANISOU 1641  CB  CYS A 379     7729   3370   3668    246    656     29       C  
ATOM   1642  SG  CYS A 379       4.135 -14.038  24.025  1.00-0.829           S  
ANISOU 1642  SG  CYS A 379     8285   3811   4187    270    651     33       S  
ATOM   1643  N   TRP A 380       4.220  -9.675  25.924  1.00 0.420           N  
ANISOU 1643  N   TRP A 380     7399   3173   3357    246    640     -4       N  
ATOM   1644  CA  TRP A 380       3.754  -8.340  26.256  1.00 0.420           C  
ANISOU 1644  CA  TRP A 380     7488   3281   3434    230    658    -20       C  
ATOM   1645  C   TRP A 380       3.039  -7.719  25.064  1.00 0.420           C  
ANISOU 1645  C   TRP A 380     7984   3813   4001    213    687    -28       C  
ATOM   1646  O   TRP A 380       3.409  -7.959  23.900  1.00 0.420           O  
ANISOU 1646  O   TRP A 380     7943   3801   4022    208    678    -36       O  
ATOM   1647  CB  TRP A 380       4.922  -7.437  26.696  1.00 0.420           C  
ANISOU 1647  CB  TRP A 380     7429   3247   3361    229    621    -47       C  
ATOM   1648  CG  TRP A 380       5.418  -7.734  28.086  1.00 0.420           C  
ANISOU 1648  CG  TRP A 380     7748   3537   3586    243    588    -39       C  
ATOM   1649  CD1 TRP A 380       6.272  -8.732  28.456  1.00 0.420           C  
ANISOU 1649  CD1 TRP A 380     8134   3936   3962    274    546    -20       C  
ATOM   1650  CD2 TRP A 380       5.123  -6.989  29.282  1.00 0.420           C  
ANISOU 1650  CD2 TRP A 380     7919   3657   3646    235    593    -48       C  
ATOM   1651  NE1 TRP A 380       6.498  -8.680  29.823  1.00 0.420           N  
ANISOU 1651  NE1 TRP A 380     8236   4006   3953    282    518    -12       N  
ATOM   1652  CE2 TRP A 380       5.800  -7.623  30.351  1.00 0.420           C  
ANISOU 1652  CE2 TRP A 380     8494   4220   4142    253    548    -33       C  
ATOM   1653  CE3 TRP A 380       4.354  -5.843  29.554  1.00 0.420           C  
ANISOU 1653  CE3 TRP A 380     8205   3894   3877    223    633    -69       C  
ATOM   1654  CZ2 TRP A 380       5.724  -7.155  31.668  1.00 0.420           C  
ANISOU 1654  CZ2 TRP A 380     8559   4228   4067    248    539    -40       C  
ATOM   1655  CZ3 TRP A 380       4.291  -5.371  30.858  1.00 0.420           C  
ANISOU 1655  CZ3 TRP A 380     8615   4237   4148    223    632    -81       C  
ATOM   1656  CH2 TRP A 380       4.943  -6.045  31.904  1.00 0.420           C  
ANISOU 1656  CH2 TRP A 380     8751   4364   4200    230    586    -67       C  
ATOM   1657  N   ILE A 381       2.020  -6.911  25.357  1.00-0.844           N  
ANISOU 1657  N   ILE A 381     7429   3255   3427    213    722    -25       N  
ATOM   1658  CA  ILE A 381       1.301  -6.123  24.343  1.00-0.844           C  
ANISOU 1658  CA  ILE A 381     7299   3162   3353    213    745    -26       C  
ATOM   1659  C   ILE A 381       1.387  -4.674  24.787  1.00-0.844           C  
ANISOU 1659  C   ILE A 381     7606   3425   3608    228    757    -46       C  
ATOM   1660  O   ILE A 381       1.464  -4.403  25.989  1.00-0.844           O  
ANISOU 1660  O   ILE A 381     7555   3323   3473    237    763    -55       O  
ATOM   1661  CB  ILE A 381      -0.172  -6.570  24.127  1.00-0.844           C  
ANISOU 1661  CB  ILE A 381     7531   3445   3623    209    778      3       C  
ATOM   1662  CG1 ILE A 381      -0.948  -6.692  25.493  1.00-0.844           C  
ANISOU 1662  CG1 ILE A 381     7386   3290   3420    220    815     21       C  
ATOM   1663  CG2 ILE A 381      -0.207  -7.882  23.305  1.00-0.844           C  
ANISOU 1663  CG2 ILE A 381     7423   3355   3557    175    760     13       C  
ATOM   1664  CD1 ILE A 381      -2.459  -6.766  25.412  1.00-0.844           C  
ANISOU 1664  CD1 ILE A 381     7280   3274   3367    219    859     51       C  
ATOM   1665  N   SER A 382       1.411  -3.756  23.833  1.00-0.936           N  
ANISOU 1665  N   SER A 382     7205   3022   3234    229    761    -54       N  
ATOM   1666  CA  SER A 382       1.432  -2.325  24.131  1.00-0.936           C  
ANISOU 1666  CA  SER A 382     7161   2897   3121    243    778    -72       C  
ATOM   1667  C   SER A 382       0.592  -1.576  23.095  1.00-0.936           C  
ANISOU 1667  C   SER A 382     7524   3266   3516    273    803    -55       C  
ATOM   1668  O   SER A 382       0.426  -2.058  21.976  1.00-0.936           O  
ANISOU 1668  O   SER A 382     7463   3276   3531    264    791    -38       O  
ATOM   1669  CB  SER A 382       2.865  -1.793  24.197  1.00-0.936           C  
ANISOU 1669  CB  SER A 382     7516   3204   3441    200    743   -103       C  
ATOM   1670  OG  SER A 382       3.552  -1.971  22.966  1.00-0.936           O  
ANISOU 1670  OG  SER A 382     7806   3548   3807    173    724   -101       O  
ATOM   1671  N   GLY A 383       0.063  -0.414  23.472  1.00-1.443           N  
ANISOU 1671  N   GLY A 383     7378   3035   3298    314    836    -59       N  
ATOM   1672  CA  GLY A 383      -0.745   0.390  22.567  1.00-1.443           C  
ANISOU 1672  CA  GLY A 383     7436   3089   3373    362    858    -36       C  
ATOM   1673  C   GLY A 383      -1.491   1.530  23.240  1.00-1.443           C  
ANISOU 1673  C   GLY A 383     7861   3412   3707    434    906    -38       C  
ATOM   1674  O   GLY A 383      -1.531   1.633  24.475  1.00-1.443           O  
ANISOU 1674  O   GLY A 383     7835   3326   3600    446    929    -61       O  
ATOM   1675  N   TRP A 384      -2.133   2.342  22.411  1.00-1.266           N  
ANISOU 1675  N   TRP A 384     7212   2742   3061    491    923    -13       N  
ATOM   1676  CA  TRP A 384      -2.942   3.502  22.790  1.00-1.266           C  
ANISOU 1676  CA  TRP A 384     7469   2894   3233    587    974     -7       C  
ATOM   1677  C   TRP A 384      -4.454   3.175  22.654  1.00-1.266           C  
ANISOU 1677  C   TRP A 384     8028   3633   3901    672   1004     38       C  
ATOM   1678  O   TRP A 384      -5.285   4.094  22.617  1.00-1.266           O  
ANISOU 1678  O   TRP A 384     8100   3667   3939    776   1045     58       O  
ATOM   1679  CB  TRP A 384      -2.560   4.751  21.940  1.00-1.266           C  
ANISOU 1679  CB  TRP A 384     7548   2800   3221    602    972     -2       C  
ATOM   1680  CG  TRP A 384      -1.229   5.367  22.275  1.00-1.266           C  
ANISOU 1680  CG  TRP A 384     7765   2823   3311    519    957    -48       C  
ATOM   1681  CD1 TRP A 384      -0.978   6.348  23.197  1.00-1.266           C  
ANISOU 1681  CD1 TRP A 384     8287   3128   3665    528    985    -87       C  
ATOM   1682  CD2 TRP A 384       0.020   5.099  21.618  1.00-1.266           C  
ANISOU 1682  CD2 TRP A 384     7663   2730   3235    412    912    -59       C  
ATOM   1683  NE1 TRP A 384       0.361   6.687  23.176  1.00-1.266           N  
ANISOU 1683  NE1 TRP A 384     8290   3016   3596    417    952   -122       N  
ATOM   1684  CE2 TRP A 384       0.997   5.932  22.215  1.00-1.266           C  
ANISOU 1684  CE2 TRP A 384     8279   3157   3715    349    910   -103       C  
ATOM   1685  CE3 TRP A 384       0.408   4.234  20.575  1.00-1.266           C  
ANISOU 1685  CE3 TRP A 384     7600   2820   3295    364    877    -39       C  
ATOM   1686  CZ2 TRP A 384       2.356   5.875  21.844  1.00-1.266           C  
ANISOU 1686  CZ2 TRP A 384     8040   2919   3488    234    872   -121       C  
ATOM   1687  CZ3 TRP A 384       1.740   4.212  20.179  1.00-1.266           C  
ANISOU 1687  CZ3 TRP A 384     7680   2881   3372    267    849    -58       C  
ATOM   1688  CH2 TRP A 384       2.698   5.024  20.801  1.00-1.266           C  
ANISOU 1688  CH2 TRP A 384     7839   2889   3423    202    847    -96       C  
ATOM   1689  N   GLY A 385      -4.793   1.878  22.619  1.00-1.443           N  
ANISOU 1689  N   GLY A 385     7471   3271   3470    628    986     55       N  
ATOM   1690  CA  GLY A 385      -6.183   1.439  22.558  1.00-1.443           C  
ANISOU 1690  CA  GLY A 385     7342   3347   3461    680   1010     97       C  
ATOM   1691  C   GLY A 385      -6.970   1.785  23.821  1.00-1.443           C  
ANISOU 1691  C   GLY A 385     7942   3952   4021    757   1083     94       C  
ATOM   1692  O   GLY A 385      -6.393   2.069  24.880  1.00-1.443           O  
ANISOU 1692  O   GLY A 385     7667   3521   3616    750   1108     54       O  
ATOM   1693  N   ALA A 386      -8.301   1.731  23.725  1.00 1.028           N  
ANISOU 1693  N   ALA A 386     7672   3877   3863    828   1117    137       N  
ATOM   1694  CA  ALA A 386      -9.195   1.953  24.855  1.00 1.028           C  
ANISOU 1694  CA  ALA A 386     7859   4118   4038    907   1198    142       C  
ATOM   1695  C   ALA A 386      -8.812   1.061  26.076  1.00 1.028           C  
ANISOU 1695  C   ALA A 386     8613   4850   4739    829   1218    115       C  
ATOM   1696  O   ALA A 386      -8.318  -0.065  25.891  1.00 1.028           O  
ANISOU 1696  O   ALA A 386     8334   4619   4508    719   1169    115       O  
ATOM   1697  CB  ALA A 386     -10.621   1.667  24.421  1.00 1.028           C  
ANISOU 1697  CB  ALA A 386     7872   4426   4234    961   1218    200       C  
ATOM   1698  N   THR A 387      -8.976   1.597  27.309  1.00-0.377           N  
ANISOU 1698  N   THR A 387     8480   4614   4481    890   1289     91       N  
ATOM   1699  CA  THR A 387      -8.660   0.907  28.582  1.00-0.377           C  
ANISOU 1699  CA  THR A 387     8580   4670   4493    833   1314     69       C  
ATOM   1700  C   THR A 387      -9.888   0.157  29.159  1.00-0.377           C  
ANISOU 1700  C   THR A 387     8997   5321   5018    844   1382    111       C  
ATOM   1701  O   THR A 387      -9.832  -0.393  30.254  1.00-0.377           O  
ANISOU 1701  O   THR A 387     8876   5176   4817    808   1418    104       O  
ATOM   1702  CB  THR A 387      -8.019   1.903  29.599  1.00-0.377           C  
ANISOU 1702  CB  THR A 387     9468   5291   5152    875   1346     12       C  
ATOM   1703  OG1 THR A 387      -8.932   2.971  29.840  1.00-0.377           O  
ANISOU 1703  OG1 THR A 387     9288   5089   4929   1013   1428     14       O  
ATOM   1704  CG2 THR A 387      -6.681   2.492  29.100  1.00-0.377           C  
ANISOU 1704  CG2 THR A 387     9411   5018   4995    826   1274    -29       C  
ATOM   1705  N   GLU A 388     -10.996   0.162  28.411  1.00 1.123           N  
ANISOU 1705  N   GLU A 388     8565   5122   4762    891   1398    159       N  
ATOM   1706  CA  GLU A 388     -12.268  -0.491  28.716  1.00 1.123           C  
ANISOU 1706  CA  GLU A 388     8477   5314   4822    893   1458    207       C  
ATOM   1707  C   GLU A 388     -13.027  -0.613  27.403  1.00 1.123           C  
ANISOU 1707  C   GLU A 388     9013   6091   5566    898   1414    254       C  
ATOM   1708  O   GLU A 388     -12.810   0.195  26.498  1.00 1.123           O  
ANISOU 1708  O   GLU A 388     8628   5640   5179    959   1372    251       O  
ATOM   1709  CB  GLU A 388     -13.094   0.297  29.763  1.00 1.123           C  
ANISOU 1709  CB  GLU A 388     8744   5605   5030   1024   1575    207       C  
ATOM   1710  CG  GLU A 388     -13.378   1.763  29.435  1.00 1.123           C  
ANISOU 1710  CG  GLU A 388    10706   7486   6949   1188   1606    198       C  
ATOM   1711  CD  GLU A 388     -14.431   2.469  30.276  1.00 1.123           C  
ANISOU 1711  CD  GLU A 388    13502  10364   9728   1339   1730    207       C  
ATOM   1712  OE1 GLU A 388     -15.280   1.780  30.887  1.00 1.123           O  
ANISOU 1712  OE1 GLU A 388    12485   9582   8811   1322   1798    240       O  
ATOM   1713  OE2 GLU A 388     -14.420   3.721  30.302  1.00 1.123           O  
ANISOU 1713  OE2 GLU A 388    13316  10000   9422   1478   1765    183       O  
ATOM   1714  N   GLU A 389     -13.905  -1.621  27.290  1.00-0.186           N  
ANISOU 1714  N   GLU A 389     8894   6245   5615    824   1421    299       N  
ATOM   1715  CA  GLU A 389     -14.702  -1.836  26.084  1.00-0.186           C  
ANISOU 1715  CA  GLU A 389     8917   6529   5839    811   1371    343       C  
ATOM   1716  C   GLU A 389     -15.558  -0.597  25.806  1.00-0.186           C  
ANISOU 1716  C   GLU A 389     9666   7402   6657    985   1411    370       C  
ATOM   1717  O   GLU A 389     -16.066   0.015  26.747  1.00-0.186           O  
ANISOU 1717  O   GLU A 389     9609   7361   6564   1096   1509    371       O  
ATOM   1718  CB  GLU A 389     -15.588  -3.079  26.245  1.00-0.186           C  
ANISOU 1718  CB  GLU A 389     8977   6864   6054    693   1386    385       C  
ATOM   1719  CG  GLU A 389     -16.066  -3.641  24.915  1.00-0.186           C  
ANISOU 1719  CG  GLU A 389     9919   8017   7165    612   1299    415       C  
ATOM   1720  CD  GLU A 389     -16.941  -4.870  25.037  1.00-0.186           C  
ANISOU 1720  CD  GLU A 389    11569   9930   8962    474   1310    454       C  
ATOM   1721  OE1 GLU A 389     -18.105  -4.817  24.582  1.00-0.186           O  
ANISOU 1721  OE1 GLU A 389    11372  10068   8962    491   1313    501       O  
ATOM   1722  OE2 GLU A 389     -16.465  -5.886  25.591  1.00-0.186           O  
ANISOU 1722  OE2 GLU A 389     9686   7919   6993    348   1315    440       O  
ATOM   1723  N   LYS A 390     -15.660  -0.198  24.523  1.00 1.111           N  
ANISOU 1723  N   LYS A 390     9458   7254   6525   1018   1337    390       N  
ATOM   1724  CA  LYS A 390     -16.415   0.982  24.067  1.00 1.111           C  
ANISOU 1724  CA  LYS A 390     9512   7408   6637   1194   1357    424       C  
ATOM   1725  C   LYS A 390     -15.815   2.335  24.569  1.00 1.111           C  
ANISOU 1725  C   LYS A 390    10192   7759   7105   1337   1409    386       C  
ATOM   1726  O   LYS A 390     -16.462   3.379  24.441  1.00 1.111           O  
ANISOU 1726  O   LYS A 390    10349   7953   7273   1508   1450    412       O  
ATOM   1727  CB  LYS A 390     -17.924   0.864  24.406  1.00 1.111           C  
ANISOU 1727  CB  LYS A 390     9706   7997   7040   1261   1424    481       C  
ATOM   1728  CG  LYS A 390     -18.687  -0.137  23.549  1.00 1.111           C  
ANISOU 1728  CG  LYS A 390    11617  10263   9180   1148   1352    530       C  
ATOM   1729  CD  LYS A 390     -20.088  -0.384  24.103  1.00 1.111           C  
ANISOU 1729  CD  LYS A 390    12500  11554  10276   1184   1428    583       C  
ATOM   1730  N   GLY A 391     -14.590   2.299  25.098  1.00 0.109           N  
ANISOU 1730  N   GLY A 391     9514   6763   6231   1266   1403    326       N  
ATOM   1731  CA  GLY A 391     -13.891   3.481  25.598  1.00 0.109           C  
ANISOU 1731  CA  GLY A 391     9506   6416   6000   1360   1441    280       C  
ATOM   1732  C   GLY A 391     -13.157   4.226  24.498  1.00 0.109           C  
ANISOU 1732  C   GLY A 391     9819   6527   6232   1376   1369    275       C  
ATOM   1733  O   GLY A 391     -13.066   3.743  23.367  1.00 0.109           O  
ANISOU 1733  O   GLY A 391     9818   6640   6337   1306   1287    302       O  
ATOM   1734  N   LYS A 392     -12.640   5.419  24.819  1.00 2.265           N  
ANISOU 1734  N   LYS A 392     9236   5633   5447   1462   1403    239       N  
ATOM   1735  CA  LYS A 392     -11.903   6.261  23.877  1.00 2.265           C  
ANISOU 1735  CA  LYS A 392     9124   5286   5224   1475   1349    235       C  
ATOM   1736  C   LYS A 392     -10.409   5.898  23.881  1.00 2.265           C  
ANISOU 1736  C   LYS A 392     9172   5119   5158   1314   1291    182       C  
ATOM   1737  O   LYS A 392      -9.926   5.308  24.835  1.00 2.265           O  
ANISOU 1737  O   LYS A 392     8966   4873   4902   1231   1304    140       O  
ATOM   1738  CB  LYS A 392     -12.087   7.752  24.261  1.00 2.265           C  
ANISOU 1738  CB  LYS A 392     9553   5454   5470   1641   1420    222       C  
ATOM   1739  N   THR A 393      -9.677   6.296  22.825  1.00 1.358           N  
ANISOU 1739  N   THR A 393     8851   4664   4789   1276   1229    186       N  
ATOM   1740  CA  THR A 393      -8.220   6.156  22.661  1.00 1.358           C  
ANISOU 1740  CA  THR A 393     8763   4378   4597   1139   1177    141       C  
ATOM   1741  C   THR A 393      -7.519   6.641  23.964  1.00 1.358           C  
ANISOU 1741  C   THR A 393     8836   4200   4480   1122   1220     76       C  
ATOM   1742  O   THR A 393      -7.879   7.668  24.543  1.00 1.358           O  
ANISOU 1742  O   THR A 393     8686   3878   4194   1231   1282     62       O  
ATOM   1743  CB  THR A 393      -7.790   7.033  21.452  1.00 1.358           C  
ANISOU 1743  CB  THR A 393     9837   5293   5599   1157   1140    163       C  
ATOM   1744  OG1 THR A 393      -8.558   6.643  20.326  1.00 1.358           O  
ANISOU 1744  OG1 THR A 393    10063   5755   5982   1188   1101    224       O  
ATOM   1745  CG2 THR A 393      -6.288   6.967  21.127  1.00 1.358           C  
ANISOU 1745  CG2 THR A 393     9066   4349   4740   1015   1091    124       C  
ATOM   1746  N   SER A 394      -6.549   5.874  24.420  1.00-0.452           N  
ANISOU 1746  N   SER A 394     8169   3516   3798    991   1184     37       N  
ATOM   1747  CA  SER A 394      -5.776   6.242  25.582  1.00-0.452           C  
ANISOU 1747  CA  SER A 394     8363   3494   3814    952   1204    -25       C  
ATOM   1748  C   SER A 394      -4.798   7.350  25.176  1.00-0.452           C  
ANISOU 1748  C   SER A 394     8956   3804   4246    919   1182    -54       C  
ATOM   1749  O   SER A 394      -4.133   7.259  24.145  1.00-0.452           O  
ANISOU 1749  O   SER A 394     8639   3495   3978    848   1127    -39       O  
ATOM   1750  CB  SER A 394      -5.018   5.031  26.127  1.00-0.452           C  
ANISOU 1750  CB  SER A 394     8618   3842   4113    828   1162    -48       C  
ATOM   1751  OG  SER A 394      -4.168   5.452  27.180  1.00-0.452           O  
ANISOU 1751  OG  SER A 394     8595   3612   3909    783   1165   -107       O  
ATOM   1752  N   GLU A 395      -4.705   8.384  26.009  1.00 0.810           N  
ANISOU 1752  N   GLU A 395     8993   3581   4077    964   1229    -97       N  
ATOM   1753  CA  GLU A 395      -3.783   9.496  25.788  1.00 0.810           C  
ANISOU 1753  CA  GLU A 395     9116   3398   4015    917   1214   -131       C  
ATOM   1754  C   GLU A 395      -2.327   8.992  25.995  1.00 0.810           C  
ANISOU 1754  C   GLU A 395     9657   3925   4544    741   1145   -174       C  
ATOM   1755  O   GLU A 395      -1.411   9.463  25.330  1.00 0.810           O  
ANISOU 1755  O   GLU A 395     9795   3944   4636    656   1107   -180       O  
ATOM   1756  CB  GLU A 395      -4.119  10.633  26.760  1.00 0.810           C  
ANISOU 1756  CB  GLU A 395     9443   3438   4105   1007   1286   -175       C  
ATOM   1757  CG  GLU A 395      -3.574  11.980  26.316  1.00 0.810           C  
ANISOU 1757  CG  GLU A 395    11194   4841   5653    997   1289   -193       C  
ATOM   1758  CD  GLU A 395      -2.165  12.294  26.778  1.00 0.810           C  
ANISOU 1758  CD  GLU A 395    12189   5625   6490    829   1244   -260       C  
ATOM   1759  OE1 GLU A 395      -1.806  11.933  27.921  1.00 0.810           O  
ANISOU 1759  OE1 GLU A 395    12564   6000   6801    772   1237   -314       O  
ATOM   1760  OE2 GLU A 395      -1.419  12.913  25.993  1.00 0.810           O  
ANISOU 1760  OE2 GLU A 395    10400   3680   4641    750   1213   -256       O  
ATOM   1761  N   VAL A 396      -2.141   7.998  26.879  1.00 0.760           N  
ANISOU 1761  N   VAL A 396     8873   3286   3812    692   1129   -195       N  
ATOM   1762  CA  VAL A 396      -0.821   7.456  27.216  1.00 0.760           C  
ANISOU 1762  CA  VAL A 396     8604   3034   3539    549   1062   -231       C  
ATOM   1763  C   VAL A 396      -0.609   6.063  26.650  1.00 0.760           C  
ANISOU 1763  C   VAL A 396     8593   3300   3742    498   1014   -194       C  
ATOM   1764  O   VAL A 396      -1.561   5.272  26.561  1.00 0.760           O  
ANISOU 1764  O   VAL A 396     8437   3328   3711    559   1036   -156       O  
ATOM   1765  CB  VAL A 396      -0.549   7.471  28.765  1.00 0.760           C  
ANISOU 1765  CB  VAL A 396     8959   3287   3735    525   1071   -288       C  
ATOM   1766  CG1 VAL A 396      -0.638   8.869  29.350  1.00 0.760           C  
ANISOU 1766  CG1 VAL A 396     9122   3131   3647    561   1117   -337       C  
ATOM   1767  CG2 VAL A 396      -1.459   6.501  29.519  1.00 0.760           C  
ANISOU 1767  CG2 VAL A 396     8838   3346   3685    591   1108   -267       C  
ATOM   1768  N   LEU A 397       0.654   5.718  26.360  1.00-1.373           N  
ANISOU 1768  N   LEU A 397     7876   2614   3062    383    951   -210       N  
ATOM   1769  CA  LEU A 397       0.949   4.366  25.913  1.00-1.373           C  
ANISOU 1769  CA  LEU A 397     7665   2634   3027    342    908   -183       C  
ATOM   1770  C   LEU A 397       0.890   3.415  27.117  1.00-1.373           C  
ANISOU 1770  C   LEU A 397     8484   3536   3842    339    902   -193       C  
ATOM   1771  O   LEU A 397       1.532   3.678  28.135  1.00-1.373           O  
ANISOU 1771  O   LEU A 397     8619   3572   3852    298    885   -235       O  
ATOM   1772  CB  LEU A 397       2.325   4.293  25.218  1.00-1.373           C  
ANISOU 1772  CB  LEU A 397     7672   2665   3079    237    852   -193       C  
ATOM   1773  CG  LEU A 397       2.769   2.924  24.693  1.00-1.373           C  
ANISOU 1773  CG  LEU A 397     8069   3274   3641    204    812   -170       C  
ATOM   1774  CD1 LEU A 397       1.944   2.488  23.500  1.00-1.373           C  
ANISOU 1774  CD1 LEU A 397     7913   3224   3601    252    828   -125       C  
ATOM   1775  CD2 LEU A 397       4.243   2.923  24.369  1.00-1.373           C  
ANISOU 1775  CD2 LEU A 397     8396   3629   3995    108    764   -190       C  
ATOM   1776  N   ASN A 398       0.154   2.285  26.972  1.00-0.693           N  
ANISOU 1776  N   ASN A 398     8012   3239   3497    372    912   -154       N  
ATOM   1777  CA  ASN A 398       0.006   1.279  28.018  1.00-0.693           C  
ANISOU 1777  CA  ASN A 398     7978   3279   3458    369    912   -151       C  
ATOM   1778  C   ASN A 398       0.602  -0.028  27.574  1.00-0.693           C  
ANISOU 1778  C   ASN A 398     8180   3620   3782    317    861   -130       C  
ATOM   1779  O   ASN A 398       0.727  -0.285  26.377  1.00-0.693           O  
ANISOU 1779  O   ASN A 398     7861   3375   3574    303    843   -112       O  
ATOM   1780  CB  ASN A 398      -1.468   1.082  28.362  1.00-0.693           C  
ANISOU 1780  CB  ASN A 398     7987   3354   3489    448    979   -122       C  
ATOM   1781  CG  ASN A 398      -2.040   2.262  29.105  1.00-0.693           C  
ANISOU 1781  CG  ASN A 398     8916   4136   4271    518   1041   -147       C  
ATOM   1782  OD1 ASN A 398      -1.463   2.750  30.072  1.00-0.693           O  
ANISOU 1782  OD1 ASN A 398     8068   3139   3261    498   1037   -192       O  
ATOM   1783  ND2 ASN A 398      -3.192   2.741  28.675  1.00-0.693           N  
ANISOU 1783  ND2 ASN A 398     8744   4001   4145    607   1097   -120       N  
ATOM   1784  N   ALA A 399       0.993  -0.847  28.528  1.00-0.611           N  
ANISOU 1784  N   ALA A 399     7849   3310   3414    295    839   -133       N  
ATOM   1785  CA  ALA A 399       1.568  -2.146  28.201  1.00-0.611           C  
ANISOU 1785  CA  ALA A 399     7711   3276   3370    262    794   -112       C  
ATOM   1786  C   ALA A 399       1.092  -3.198  29.199  1.00-0.611           C  
ANISOU 1786  C   ALA A 399     8108   3699   3731    274    808    -87       C  
ATOM   1787  O   ALA A 399       0.813  -2.866  30.354  1.00-0.611           O  
ANISOU 1787  O   ALA A 399     8026   3549   3525    291    833    -98       O  
ATOM   1788  CB  ALA A 399       3.090  -2.059  28.195  1.00-0.611           C  
ANISOU 1788  CB  ALA A 399     7801   3358   3451    211    730   -138       C  
ATOM   1789  N   ALA A 400       0.972  -4.468  28.750  1.00-0.950           N  
ANISOU 1789  N   ALA A 400     7880   3550   3590    263    797    -54       N  
ATOM   1790  CA  ALA A 400       0.524  -5.528  29.650  1.00-0.950           C  
ANISOU 1790  CA  ALA A 400     7783   3456   3447    264    813    -23       C  
ATOM   1791  C   ALA A 400       1.122  -6.877  29.321  1.00-0.950           C  
ANISOU 1791  C   ALA A 400     7988   3682   3696    244    772      0       C  
ATOM   1792  O   ALA A 400       1.326  -7.223  28.156  1.00-0.950           O  
ANISOU 1792  O   ALA A 400     7728   3466   3536    232    755      1       O  
ATOM   1793  CB  ALA A 400      -0.997  -5.631  29.640  1.00-0.950           C  
ANISOU 1793  CB  ALA A 400     7814   3542   3513    280    883      6       C  
ATOM   1794  N   LYS A 401       1.321  -7.691  30.371  1.00 0.532           N  
ANISOU 1794  N   LYS A 401     7576   3224   3192    245    762     22       N  
ATOM   1795  CA  LYS A 401       1.795  -9.060  30.171  1.00 0.532           C  
ANISOU 1795  CA  LYS A 401     7343   2976   2974    241    730     50       C  
ATOM   1796  C   LYS A 401       0.579  -9.913  29.776  1.00 0.532           C  
ANISOU 1796  C   LYS A 401     8100   3743   3771    213    779     85       C  
ATOM   1797  O   LYS A 401      -0.505  -9.786  30.355  1.00 0.532           O  
ANISOU 1797  O   LYS A 401     7875   3531   3515    203    834    104       O  
ATOM   1798  CB  LYS A 401       2.425  -9.564  31.483  1.00 0.532           C  
ANISOU 1798  CB  LYS A 401     7718   3284   3215    258    700     69       C  
ATOM   1799  CG  LYS A 401       2.995 -10.979  31.411  1.00 0.532           C  
ANISOU 1799  CG  LYS A 401     9812   5332   5296    273    665    104       C  
ATOM   1800  CD  LYS A 401       3.209 -11.572  32.815  1.00 0.532           C  
ANISOU 1800  CD  LYS A 401    10802   6240   6128    293    648    139       C  
ATOM   1801  CE  LYS A 401       1.956 -12.130  33.448  1.00 0.532           C  
ANISOU 1801  CE  LYS A 401    12322   7688   7561    266    715    183       C  
ATOM   1802  NZ  LYS A 401       2.270 -13.189  34.448  1.00 0.532           N  
ANISOU 1802  NZ  LYS A 401    14109   9362   9198    288    693    234       N  
ATOM   1803  N   VAL A 402       0.768 -10.792  28.786  1.00-0.993           N  
ANISOU 1803  N   VAL A 402     8030   3670   3766    198    760     92       N  
ATOM   1804  CA  VAL A 402      -0.240 -11.742  28.293  1.00-0.993           C  
ANISOU 1804  CA  VAL A 402     7865   3499   3631    153    791    120       C  
ATOM   1805  C   VAL A 402       0.461 -13.088  28.041  1.00-0.993           C  
ANISOU 1805  C   VAL A 402     8443   3970   4166    153    759    134       C  
ATOM   1806  O   VAL A 402       1.653 -13.112  27.718  1.00-0.993           O  
ANISOU 1806  O   VAL A 402     8436   3949   4169    197    715    114       O  
ATOM   1807  CB  VAL A 402      -0.999 -11.232  27.015  1.00-0.993           C  
ANISOU 1807  CB  VAL A 402     8101   3839   3992    127    806    104       C  
ATOM   1808  CG1 VAL A 402      -1.981 -10.093  27.326  1.00-0.993           C  
ANISOU 1808  CG1 VAL A 402     7945   3779   3870    137    851    104       C  
ATOM   1809  CG2 VAL A 402      -0.036 -10.821  25.905  1.00-0.993           C  
ANISOU 1809  CG2 VAL A 402     7955   3710   3906    149    765     68       C  
ATOM   1810  N   LEU A 403      -0.274 -14.193  28.139  1.00-0.104           N  
ANISOU 1810  N   LEU A 403     7854   3306   3530    106    785    169       N  
ATOM   1811  CA  LEU A 403       0.315 -15.492  27.832  1.00-0.104           C  
ANISOU 1811  CA  LEU A 403     7986   3295   3598    111    761    181       C  
ATOM   1812  C   LEU A 403      -0.287 -15.985  26.533  1.00-0.104           C  
ANISOU 1812  C   LEU A 403     8207   3514   3880     52    769    165       C  
ATOM   1813  O   LEU A 403      -1.470 -15.731  26.278  1.00-0.104           O  
ANISOU 1813  O   LEU A 403     7967   3365   3701    -16    799    171       O  
ATOM   1814  CB  LEU A 403      -0.019 -16.507  28.948  1.00-0.104           C  
ANISOU 1814  CB  LEU A 403     8158   3326   3629     90    783    234       C  
ATOM   1815  CG  LEU A 403       0.987 -16.682  30.094  1.00-0.104           C  
ANISOU 1815  CG  LEU A 403     8958   4045   4312    164    752    258       C  
ATOM   1816  CD1 LEU A 403       1.314 -15.396  30.770  1.00-0.104           C  
ANISOU 1816  CD1 LEU A 403     8900   4108   4275    200    739    238       C  
ATOM   1817  CD2 LEU A 403       0.468 -17.680  31.119  1.00-0.104           C  
ANISOU 1817  CD2 LEU A 403     9721   4655   4919    132    783    320       C  
ATOM   1818  N   LEU A 404       0.480 -16.745  25.741  1.00-0.598           N  
ANISOU 1818  N   LEU A 404     7890   3095   3538     76    742    147       N  
ATOM   1819  CA  LEU A 404      -0.081 -17.353  24.534  1.00-0.598           C  
ANISOU 1819  CA  LEU A 404     8038   3204   3703     12    747    128       C  
ATOM   1820  C   LEU A 404      -1.159 -18.356  24.974  1.00-0.598           C  
ANISOU 1820  C   LEU A 404     8655   3712   4237    -82    777    167       C  
ATOM   1821  O   LEU A 404      -1.015 -18.972  26.026  1.00-0.598           O  
ANISOU 1821  O   LEU A 404     8593   3527   4065    -70    789    206       O  
ATOM   1822  CB  LEU A 404       1.009 -18.110  23.726  1.00-0.598           C  
ANISOU 1822  CB  LEU A 404     8160   3196   3776     69    722    101       C  
ATOM   1823  CG  LEU A 404       2.088 -17.244  23.009  1.00-0.598           C  
ANISOU 1823  CG  LEU A 404     8760   3916   4469    144    699     61       C  
ATOM   1824  CD1 LEU A 404       2.831 -18.064  21.947  1.00-0.598           C  
ANISOU 1824  CD1 LEU A 404     9019   4061   4685    182    693     29       C  
ATOM   1825  CD2 LEU A 404       1.481 -16.059  22.331  1.00-0.598           C  
ANISOU 1825  CD2 LEU A 404     8735   4064   4559    103    703     39       C  
ATOM   1826  N   ILE A 405      -2.231 -18.506  24.198  1.00-0.599           N  
ANISOU 1826  N   ILE A 405     8245   3357   3877   -181    788    158       N  
ATOM   1827  CA  ILE A 405      -3.271 -19.491  24.503  1.00-0.599           C  
ANISOU 1827  CA  ILE A 405     8389   3413   3952   -296    816    193       C  
ATOM   1828  C   ILE A 405      -3.167 -20.543  23.398  1.00-0.599           C  
ANISOU 1828  C   ILE A 405     9131   3981   4617   -348    796    162       C  
ATOM   1829  O   ILE A 405      -3.143 -20.151  22.231  1.00-0.599           O  
ANISOU 1829  O   ILE A 405     8742   3676   4299   -351    771    118       O  
ATOM   1830  CB  ILE A 405      -4.670 -18.805  24.617  1.00-0.599           C  
ANISOU 1830  CB  ILE A 405     8729   3987   4420   -378    845    211       C  
ATOM   1831  CG1 ILE A 405      -4.709 -17.915  25.890  1.00-0.599           C  
ANISOU 1831  CG1 ILE A 405     8808   4175   4523   -316    878    241       C  
ATOM   1832  CG2 ILE A 405      -5.804 -19.859  24.684  1.00-0.599           C  
ANISOU 1832  CG2 ILE A 405     8792   3995   4437   -526    871    242       C  
ATOM   1833  CD1 ILE A 405      -5.720 -16.759  25.897  1.00-0.599           C  
ANISOU 1833  CD1 ILE A 405     8977   4608   4842   -325    906    245       C  
ATOM   1834  N   GLU A 406      -3.020 -21.872  23.751  1.00-0.325           N  
ANISOU 1834  N   GLU A 406     9014   3592   4328   -380    806    184       N  
ATOM   1835  CA  GLU A 406      -2.882 -22.917  22.719  1.00-0.325           C  
ANISOU 1835  CA  GLU A 406     9205   3567   4408   -425    791    148       C  
ATOM   1836  C   GLU A 406      -4.047 -22.848  21.734  1.00-0.325           C  
ANISOU 1836  C   GLU A 406     9644   4128   4921   -567    781    122       C  
ATOM   1837  O   GLU A 406      -5.188 -22.681  22.170  1.00-0.325           O  
ANISOU 1837  O   GLU A 406     9405   4035   4754   -672    801    156       O  
ATOM   1838  CB  GLU A 406      -2.771 -24.317  23.356  1.00-0.325           C  
ANISOU 1838  CB  GLU A 406     9624   3656   4614   -452    812    184       C  
ATOM   1839  CG  GLU A 406      -1.563 -24.503  24.268  1.00-0.325           C  
ANISOU 1839  CG  GLU A 406    11090   4993   5992   -299    810    214       C  
ATOM   1840  CD  GLU A 406      -1.614 -25.698  25.207  1.00-0.325           C  
ANISOU 1840  CD  GLU A 406    14596   8205   9292   -320    835    273       C  
ATOM   1841  OE1 GLU A 406      -2.060 -26.788  24.776  1.00-0.325           O  
ANISOU 1841  OE1 GLU A 406    13630   6988   8181   -418    848    270       O  
ATOM   1842  OE2 GLU A 406      -1.202 -25.544  26.381  1.00-0.325           O  
ANISOU 1842  OE2 GLU A 406    14471   8085   9133   -242    840    324       O  
ATOM   1843  N   THR A 407      -3.762 -22.962  20.399  1.00 0.135           N  
ANISOU 1843  N   THR A 407     9460   3903   4723   -567    751     63       N  
ATOM   1844  CA  THR A 407      -4.761 -22.855  19.343  1.00 0.135           C  
ANISOU 1844  CA  THR A 407     9380   3949   4706   -693    726     33       C  
ATOM   1845  C   THR A 407      -5.896 -23.864  19.523  1.00 0.135           C  
ANISOU 1845  C   THR A 407     9995   4463   5242   -874    735     55       C  
ATOM   1846  O   THR A 407      -7.047 -23.458  19.361  1.00 0.135           O  
ANISOU 1846  O   THR A 407     9795   4503   5172   -984    727     69       O  
ATOM   1847  CB  THR A 407      -4.100 -22.888  17.943  1.00 0.135           C  
ANISOU 1847  CB  THR A 407    10619   5116   5897   -651    695    -35       C  
ATOM   1848  OG1 THR A 407      -3.312 -21.696  17.799  1.00 0.135           O  
ANISOU 1848  OG1 THR A 407    10098   4776   5498   -515    690    -44       O  
ATOM   1849  CG2 THR A 407      -5.120 -22.967  16.801  1.00 0.135           C  
ANISOU 1849  CG2 THR A 407    10092   4678   5391   -793    658    -68       C  
ATOM   1850  N   GLN A 408      -5.596 -25.139  19.907  1.00 0.732           N  
ANISOU 1850  N   GLN A 408     9907   4031   4946   -904    755     64       N  
ATOM   1851  CA  GLN A 408      -6.616 -26.159  20.164  1.00 0.732           C  
ANISOU 1851  CA  GLN A 408    10026   4013   4965  -1091    770     90       C  
ATOM   1852  C   GLN A 408      -7.604 -25.654  21.247  1.00 0.732           C  
ANISOU 1852  C   GLN A 408    10231   4475   5313  -1159    805    159       C  
ATOM   1853  O   GLN A 408      -8.817 -25.799  21.094  1.00 0.732           O  
ANISOU 1853  O   GLN A 408    10080   4469   5232  -1328    804    173       O  
ATOM   1854  CB  GLN A 408      -5.955 -27.480  20.608  1.00 0.732           C  
ANISOU 1854  CB  GLN A 408    10566   4112   5242  -1073    795    100       C  
ATOM   1855  CG  GLN A 408      -6.927 -28.654  20.750  1.00 0.732           C  
ANISOU 1855  CG  GLN A 408    13611   6942   8137  -1283    811    120       C  
ATOM   1856  CD  GLN A 408      -6.343 -29.783  21.560  1.00 0.732           C  
ANISOU 1856  CD  GLN A 408    16620   9528  10891  -1249    847    157       C  
ATOM   1857  OE1 GLN A 408      -6.077 -29.648  22.762  1.00 0.732           O  
ANISOU 1857  OE1 GLN A 408    16298   9202  10562  -1174    881    224       O  
ATOM   1858  NE2 GLN A 408      -6.146 -30.930  20.924  1.00 0.732           N  
ANISOU 1858  NE2 GLN A 408    15532   8057   9569  -1300    841    115       N  
ATOM   1859  N   ARG A 409      -7.083 -25.029  22.312  1.00 1.429           N  
ANISOU 1859  N   ARG A 409     9805   4123   4935  -1027    834    200       N  
ATOM   1860  CA  ARG A 409      -7.916 -24.446  23.363  1.00 1.429           C  
ANISOU 1860  CA  ARG A 409     9654   4213   4907  -1063    877    260       C  
ATOM   1861  C   ARG A 409      -8.682 -23.227  22.815  1.00 1.429           C  
ANISOU 1861  C   ARG A 409     9598   4557   5095  -1072    860    245       C  
ATOM   1862  O   ARG A 409      -9.885 -23.112  23.047  1.00 1.429           O  
ANISOU 1862  O   ARG A 409     9358   4531   4965  -1190    883    279       O  
ATOM   1863  CB  ARG A 409      -7.068 -24.051  24.583  1.00 1.429           C  
ANISOU 1863  CB  ARG A 409     9567   4082   4781   -910    905    297       C  
ATOM   1864  CG  ARG A 409      -7.874 -23.476  25.723  1.00 1.429           C  
ANISOU 1864  CG  ARG A 409    10234   4965   5540   -937    958    355       C  
ATOM   1865  CD  ARG A 409      -6.995 -23.196  26.922  1.00 1.429           C  
ANISOU 1865  CD  ARG A 409    11186   5833   6410   -798    978    387       C  
ATOM   1866  NE  ARG A 409      -7.087 -24.264  27.921  1.00 1.429           N  
ANISOU 1866  NE  ARG A 409    10342   4740   5373   -855   1019    448       N  
ATOM   1867  CZ  ARG A 409      -6.604 -24.170  29.157  1.00 1.429           C  
ANISOU 1867  CZ  ARG A 409    11243   5570   6178   -768   1044    494       C  
ATOM   1868  NH1 ARG A 409      -5.977 -23.072  29.549  1.00 1.429           N  
ANISOU 1868  NH1 ARG A 409     9242   3725   4255   -630   1030    479       N  
ATOM   1869  NH2 ARG A 409      -6.713 -25.189  29.997  1.00 1.429           N  
ANISOU 1869  NH2 ARG A 409    10457   4537   5198   -824   1080    555       N  
ATOM   1870  N   CYS A 410      -8.006 -22.340  22.087  1.00-1.409           N  
ANISOU 1870  N   CYS A 410     9122   4182   4699   -950    822    201       N  
ATOM   1871  CA  CYS A 410      -8.658 -21.159  21.516  1.00-1.409           C  
ANISOU 1871  CA  CYS A 410     9093   4496   4877   -940    803    190       C  
ATOM   1872  C   CYS A 410      -9.778 -21.491  20.518  1.00-1.409           C  
ANISOU 1872  C   CYS A 410     9188   4722   5036  -1099    768    176       C  
ATOM   1873  O   CYS A 410     -10.709 -20.693  20.364  1.00-1.409           O  
ANISOU 1873  O   CYS A 410     8784   4639   4815  -1122    764    194       O  
ATOM   1874  CB  CYS A 410      -7.636 -20.206  20.899  1.00-1.409           C  
ANISOU 1874  CB  CYS A 410     9258   4699   5084   -786    772    148       C  
ATOM   1875  SG  CYS A 410      -8.209 -18.494  20.807  1.00-1.409           S  
ANISOU 1875  SG  CYS A 410     9682   5500   5733   -713    772    159       S  
ATOM   1876  N   ASN A 411      -9.665 -22.651  19.837  1.00-0.173           N  
ANISOU 1876  N   ASN A 411     8811   4092   4501  -1202    741    143       N  
ATOM   1877  CA  ASN A 411     -10.617 -23.127  18.836  1.00-0.173           C  
ANISOU 1877  CA  ASN A 411     8875   4226   4582  -1372    696    119       C  
ATOM   1878  C   ASN A 411     -11.786 -23.921  19.414  1.00-0.173           C  
ANISOU 1878  C   ASN A 411     9764   5152   5474  -1567    723    165       C  
ATOM   1879  O   ASN A 411     -12.690 -24.281  18.653  1.00-0.173           O  
ANISOU 1879  O   ASN A 411     9687   5181   5433  -1731    681    149       O  
ATOM   1880  CB  ASN A 411      -9.909 -23.945  17.736  1.00-0.173           C  
ANISOU 1880  CB  ASN A 411     9174   4218   4686  -1391    652     50       C  
ATOM   1881  CG  ASN A 411      -9.515 -23.123  16.534  1.00-0.173           C  
ANISOU 1881  CG  ASN A 411    10565   5733   6139  -1304    601      0       C  
ATOM   1882  OD1 ASN A 411     -10.175 -22.144  16.169  1.00-0.173           O  
ANISOU 1882  OD1 ASN A 411     9710   5210   5469  -1299    574     12       O  
ATOM   1883  ND2 ASN A 411      -8.427 -23.491  15.892  1.00-0.173           N  
ANISOU 1883  ND2 ASN A 411     9169   4075   4585  -1225    590    -54       N  
ATOM   1884  N   SER A 412     -11.776 -24.204  20.748  1.00 0.590           N  
ANISOU 1884  N   SER A 412     9428   4735   5095  -1560    792    221       N  
ATOM   1885  CA  SER A 412     -12.851 -24.931  21.419  1.00 0.590           C  
ANISOU 1885  CA  SER A 412     9377   4720   5044  -1746    833    274       C  
ATOM   1886  C   SER A 412     -14.204 -24.215  21.319  1.00 0.590           C  
ANISOU 1886  C   SER A 412     9749   5563   5679  -1831    833    305       C  
ATOM   1887  O   SER A 412     -14.249 -22.995  21.144  1.00 0.590           O  
ANISOU 1887  O   SER A 412     9613   5716   5724  -1702    822    303       O  
ATOM   1888  CB  SER A 412     -12.487 -25.246  22.866  1.00 0.590           C  
ANISOU 1888  CB  SER A 412    10065   5232   5622  -1696    910    333       C  
ATOM   1889  OG  SER A 412     -12.370 -24.082  23.659  1.00 0.590           O  
ANISOU 1889  OG  SER A 412    11035   6442   6733  -1545    948    363       O  
ATOM   1890  N   ARG A 413     -15.300 -24.991  21.391  1.00 1.048           N  
ANISOU 1890  N   ARG A 413     9551   5437   5499  -2052    844    334       N  
ATOM   1891  CA  ARG A 413     -16.686 -24.534  21.247  1.00 1.048           C  
ANISOU 1891  CA  ARG A 413     9441   5790   5644  -2166    840    367       C  
ATOM   1892  C   ARG A 413     -17.035 -23.328  22.116  1.00 1.048           C  
ANISOU 1892  C   ARG A 413     9957   6658   6372  -2023    904    419       C  
ATOM   1893  O   ARG A 413     -17.747 -22.439  21.647  1.00 1.048           O  
ANISOU 1893  O   ARG A 413     9935   7031   6580  -1993    878    424       O  
ATOM   1894  CB  ARG A 413     -17.675 -25.695  21.489  1.00 1.048           C  
ANISOU 1894  CB  ARG A 413     9709   6033   5870  -2436    862    401       C  
ATOM   1895  N   TYR A 414     -16.493 -23.273  23.350  1.00 1.489           N  
ANISOU 1895  N   TYR A 414     9391   5933   5712  -1922    984    454       N  
ATOM   1896  CA  TYR A 414     -16.747 -22.196  24.310  1.00 1.489           C  
ANISOU 1896  CA  TYR A 414     9198   6006   5665  -1784   1056    498       C  
ATOM   1897  C   TYR A 414     -15.844 -20.958  24.107  1.00 1.489           C  
ANISOU 1897  C   TYR A 414     9309   6138   5813  -1544   1030    461       C  
ATOM   1898  O   TYR A 414     -16.106 -19.921  24.718  1.00 1.489           O  
ANISOU 1898  O   TYR A 414     9274   6336   5906  -1423   1080    486       O  
ATOM   1899  CB  TYR A 414     -16.689 -22.728  25.774  1.00 1.489           C  
ANISOU 1899  CB  TYR A 414     9580   6217   5913  -1808   1154    556       C  
ATOM   1900  CG  TYR A 414     -15.430 -23.498  26.125  0.50 1.489           C  
ANISOU 1900  CG  TYR A 414    10209   6358   6256  -1759   1148    541       C  
ATOM   1901  CD1 TYR A 414     -15.352 -24.875  25.932  0.50 1.489           C  
ANISOU 1901  CD1 TYR A 414    10670   6490   6520  -1920   1134    541       C  
ATOM   1902  CD2 TYR A 414     -14.334 -22.857  26.694  0.50 1.489           C  
ANISOU 1902  CD2 TYR A 414    10398   6412   6366  -1553   1157    530       C  
ATOM   1903  CE1 TYR A 414     -14.193 -25.586  26.248  0.50 1.489           C  
ANISOU 1903  CE1 TYR A 414    11102   6474   6689  -1853   1129    532       C  
ATOM   1904  CE2 TYR A 414     -13.172 -23.556  27.017  0.50 1.489           C  
ANISOU 1904  CE2 TYR A 414    10727   6330   6451  -1495   1145    522       C  
ATOM   1905  CZ  TYR A 414     -13.106 -24.921  26.794  0.50 1.489           C  
ANISOU 1905  CZ  TYR A 414    12097   7381   7633  -1635   1133    525       C  
ATOM   1906  OH  TYR A 414     -11.960 -25.610  27.118  0.50 1.489           O  
ANISOU 1906  OH  TYR A 414    12620   7499   7915  -1558   1123    523       O  
ATOM   1907  N   VAL A 415     -14.813 -21.045  23.238  1.00 1.235           N  
ANISOU 1907  N   VAL A 415     8445   5032   4833  -1479    958    401       N  
ATOM   1908  CA  VAL A 415     -13.938 -19.900  22.993  1.00 1.235           C  
ANISOU 1908  CA  VAL A 415     8185   4787   4604  -1274    934    367       C  
ATOM   1909  C   VAL A 415     -14.247 -19.315  21.584  1.00 1.235           C  
ANISOU 1909  C   VAL A 415     8833   5640   5383  -1269    856    330       C  
ATOM   1910  O   VAL A 415     -15.255 -18.614  21.449  1.00 1.235           O  
ANISOU 1910  O   VAL A 415     8658   5821   5409  -1272    860    357       O  
ATOM   1911  CB  VAL A 415     -12.421 -20.177  23.268  1.00 1.235           C  
ANISOU 1911  CB  VAL A 415     8653   4876   4862  -1163    927    337       C  
ATOM   1912  CG1 VAL A 415     -11.590 -18.896  23.165  1.00 1.235           C  
ANISOU 1912  CG1 VAL A 415     8492   4771   4752   -968    913    310       C  
ATOM   1913  CG2 VAL A 415     -12.202 -20.842  24.627  1.00 1.235           C  
ANISOU 1913  CG2 VAL A 415     8721   4743   4785  -1179    995    382       C  
ATOM   1914  N   TYR A 416     -13.426 -19.605  20.541  1.00-0.858           N  
ANISOU 1914  N   TYR A 416     8505   5102   4943  -1256    787    273       N  
ATOM   1915  CA  TYR A 416     -13.714 -19.030  19.221  1.00-0.858           C  
ANISOU 1915  CA  TYR A 416     8281   5064   4821  -1249    714    243       C  
ATOM   1916  C   TYR A 416     -14.201 -20.069  18.206  1.00-0.858           C  
ANISOU 1916  C   TYR A 416     9254   5981   5733  -1435    650    213       C  
ATOM   1917  O   TYR A 416     -14.280 -19.746  17.028  1.00-0.858           O  
ANISOU 1917  O   TYR A 416     9340   6160   5852  -1435    579    181       O  
ATOM   1918  CB  TYR A 416     -12.551 -18.165  18.669  1.00-0.858           C  
ANISOU 1918  CB  TYR A 416     8174   4855   4671  -1073    686    202       C  
ATOM   1919  CG  TYR A 416     -12.442 -16.799  19.326  1.00-0.858           C  
ANISOU 1919  CG  TYR A 416     7877   4726   4489   -909    727    228       C  
ATOM   1920  CD1 TYR A 416     -13.534 -15.934  19.371  1.00-0.858           C  
ANISOU 1920  CD1 TYR A 416     7730   4926   4535   -887    738    266       C  
ATOM   1921  CD2 TYR A 416     -11.241 -16.361  19.876  1.00-0.858           C  
ANISOU 1921  CD2 TYR A 416     7994   4653   4514   -772    754    213       C  
ATOM   1922  CE1 TYR A 416     -13.445 -14.689  19.992  1.00-0.858           C  
ANISOU 1922  CE1 TYR A 416     7771   5081   4654   -731    782    286       C  
ATOM   1923  CE2 TYR A 416     -11.133 -15.104  20.474  1.00-0.858           C  
ANISOU 1923  CE2 TYR A 416     7851   4632   4450   -634    790    229       C  
ATOM   1924  CZ  TYR A 416     -12.239 -14.273  20.534  1.00-0.858           C  
ANISOU 1924  CZ  TYR A 416     8333   5419   5101   -611    807    264       C  
ATOM   1925  OH  TYR A 416     -12.130 -13.015  21.081  1.00-0.858           O  
ANISOU 1925  OH  TYR A 416     7972   5141   4791   -468    845    275       O  
ATOM   1926  N   ASP A 417     -14.617 -21.271  18.672  1.00 1.793           N  
ANISOU 1926  N   ASP A 417     9192   5778   5578  -1603    674    229       N  
ATOM   1927  CA  ASP A 417     -15.188 -22.353  17.857  1.00 1.793           C  
ANISOU 1927  CA  ASP A 417     9263   5772   5571  -1813    620    202       C  
ATOM   1928  C   ASP A 417     -14.654 -22.442  16.402  1.00 1.793           C  
ANISOU 1928  C   ASP A 417     9752   6128   5956  -1806    533    129       C  
ATOM   1929  O   ASP A 417     -15.313 -21.979  15.462  1.00 1.793           O  
ANISOU 1929  O   ASP A 417     9651   6293   5975  -1847    466    118       O  
ATOM   1930  CB  ASP A 417     -16.727 -22.241  17.862  1.00 1.793           C  
ANISOU 1930  CB  ASP A 417     9352   6276   5878  -1964    611    248       C  
ATOM   1931  CG  ASP A 417     -17.500 -23.476  17.431  1.00 1.793           C  
ANISOU 1931  CG  ASP A 417    11105   7969   7559  -2228    572    236       C  
ATOM   1932  OD1 ASP A 417     -16.884 -24.567  17.335  1.00 1.793           O  
ANISOU 1932  OD1 ASP A 417    11463   7901   7664  -2305    571    198       O  
ATOM   1933  OD2 ASP A 417     -18.726 -23.362  17.225  1.00 1.793           O  
ANISOU 1933  OD2 ASP A 417    11996   9236   8644  -2359    546    267       O  
ATOM   1934  N   ASN A 418     -13.441 -22.996  16.245  1.00 2.332           N  
ANISOU 1934  N   ASN A 418     9449   5422   5427  -1740    539     81       N  
ATOM   1935  CA  ASN A 418     -12.747 -23.273  14.978  1.00 2.332           C  
ANISOU 1935  CA  ASN A 418     9555   5318   5378  -1726    479      7       C  
ATOM   1936  C   ASN A 418     -12.468 -22.055  14.049  1.00 2.332           C  
ANISOU 1936  C   ASN A 418     9777   5754   5708  -1589    432    -14       C  
ATOM   1937  O   ASN A 418     -12.183 -22.269  12.867  1.00 2.332           O  
ANISOU 1937  O   ASN A 418     9670   5538   5489  -1612    376    -72       O  
ATOM   1938  CB  ASN A 418     -13.468 -24.388  14.191  1.00 2.332           C  
ANISOU 1938  CB  ASN A 418     9719   5375   5422  -1956    424    -30       C  
ATOM   1939  CG  ASN A 418     -13.339 -25.739  14.842  1.00 2.332           C  
ANISOU 1939  CG  ASN A 418    12249   7532   7744  -2072    468    -30       C  
ATOM   1940  OD1 ASN A 418     -14.333 -26.401  15.135  1.00 2.332           O  
ANISOU 1940  OD1 ASN A 418    12239   7572   7747  -2272    469     -4       O  
ATOM   1941  ND2 ASN A 418     -12.111 -26.192  15.079  1.00 2.332           N  
ANISOU 1941  ND2 ASN A 418    11142   6043   6438  -1949    506    -56       N  
ATOM   1942  N   LEU A 419     -12.456 -20.812  14.580  1.00 2.196           N  
ANISOU 1942  N   LEU A 419     9107   5337   5221  -1443    461     30       N  
ATOM   1943  CA  LEU A 419     -12.159 -19.619  13.763  1.00 2.196           C  
ANISOU 1943  CA  LEU A 419     8975   5372   5172  -1310    424     18       C  
ATOM   1944  C   LEU A 419     -10.654 -19.259  13.708  1.00 2.196           C  
ANISOU 1944  C   LEU A 419     9314   5478   5401  -1139    451    -15       C  
ATOM   1945  O   LEU A 419     -10.277 -18.304  13.012  1.00 2.196           O  
ANISOU 1945  O   LEU A 419     9297   5554   5425  -1034    428    -26       O  
ATOM   1946  CB  LEU A 419     -12.932 -18.376  14.266  1.00 2.196           C  
ANISOU 1946  CB  LEU A 419     8817   5593   5255  -1232    440     80       C  
ATOM   1947  CG  LEU A 419     -14.445 -18.310  14.087  1.00 2.196           C  
ANISOU 1947  CG  LEU A 419     9276   6410   5892  -1354    404    119       C  
ATOM   1948  CD1 LEU A 419     -15.006 -17.147  14.886  1.00 2.196           C  
ANISOU 1948  CD1 LEU A 419     9120   6565   5948  -1237    450    182       C  
ATOM   1949  CD2 LEU A 419     -14.838 -18.160  12.614  1.00 2.196           C  
ANISOU 1949  CD2 LEU A 419     9399   6661   6020  -1408    305     91       C  
ATOM   1950  N   ILE A 420      -9.814 -19.968  14.479  1.00-0.587           N  
ANISOU 1950  N   ILE A 420     8526   4406   4482  -1109    502    -23       N  
ATOM   1951  CA  ILE A 420      -8.376 -19.689  14.574  1.00-0.587           C  
ANISOU 1951  CA  ILE A 420     8359   4050   4232   -951    530    -47       C  
ATOM   1952  C   ILE A 420      -7.590 -20.506  13.578  1.00-0.587           C  
ANISOU 1952  C   ILE A 420     8917   4332   4596   -962    509   -112       C  
ATOM   1953  O   ILE A 420      -7.456 -21.723  13.734  1.00-0.587           O  
ANISOU 1953  O   ILE A 420     9375   4525   4894  -1034    521   -132       O  
ATOM   1954  CB  ILE A 420      -7.836 -19.828  16.022  1.00-0.587           C  
ANISOU 1954  CB  ILE A 420     8544   4126   4401   -881    593    -11       C  
ATOM   1955  CG1 ILE A 420      -8.763 -19.118  17.051  1.00-0.587           C  
ANISOU 1955  CG1 ILE A 420     8244   4089   4272   -886    623     51       C  
ATOM   1956  CG2 ILE A 420      -6.364 -19.380  16.117  1.00-0.587           C  
ANISOU 1956  CG2 ILE A 420     8517   3974   4326   -716    612    -32       C  
ATOM   1957  CD1 ILE A 420      -9.043 -17.491  16.843  1.00-0.587           C  
ANISOU 1957  CD1 ILE A 420     7890   4045   4103   -781    615     69       C  
ATOM   1958  N   THR A 421      -7.060 -19.839  12.565  1.00-0.516           N  
ANISOU 1958  N   THR A 421     8271   3732   3948   -886    484   -144       N  
ATOM   1959  CA  THR A 421      -6.315 -20.501  11.499  1.00-0.516           C  
ANISOU 1959  CA  THR A 421     8559   3782   4051   -884    470   -211       C  
ATOM   1960  C   THR A 421      -4.804 -20.568  11.858  1.00-0.516           C  
ANISOU 1960  C   THR A 421     9386   4413   4802   -731    522   -227       C  
ATOM   1961  O   THR A 421      -4.423 -19.911  12.835  1.00-0.516           O  
ANISOU 1961  O   THR A 421     9098   4219   4625   -638    554   -186       O  
ATOM   1962  CB  THR A 421      -6.497 -19.700  10.199  1.00-0.516           C  
ANISOU 1962  CB  THR A 421     8916   4304   4439   -876    421   -232       C  
ATOM   1963  OG1 THR A 421      -5.723 -18.512  10.319  1.00-0.516           O  
ANISOU 1963  OG1 THR A 421     8204   3705   3824   -726    447   -212       O  
ATOM   1964  CG2 THR A 421      -7.965 -19.384   9.878  1.00-0.516           C  
ANISOU 1964  CG2 THR A 421     8494   4152   4135   -997    361   -203       C  
ATOM   1965  N   PRO A 422      -3.928 -21.263  11.050  1.00 0.965           N  
ANISOU 1965  N   PRO A 422     9159   3942   4397   -697    531   -287       N  
ATOM   1966  CA  PRO A 422      -2.472 -21.260  11.328  1.00 0.965           C  
ANISOU 1966  CA  PRO A 422     9143   3797   4340   -541    580   -298       C  
ATOM   1967  C   PRO A 422      -1.817 -19.884  11.129  1.00 0.965           C  
ANISOU 1967  C   PRO A 422     9238   4110   4575   -426    588   -284       C  
ATOM   1968  O   PRO A 422      -0.665 -19.686  11.535  1.00 0.965           O  
ANISOU 1968  O   PRO A 422     9191   4031   4546   -303    626   -281       O  
ATOM   1969  CB  PRO A 422      -1.931 -22.271  10.294  1.00 0.965           C  
ANISOU 1969  CB  PRO A 422     9620   3996   4596   -544    587   -369       C  
ATOM   1970  CG  PRO A 422      -3.129 -23.177  10.017  1.00 0.965           C  
ANISOU 1970  CG  PRO A 422    10328   4592   5195   -725    548   -387       C  
ATOM   1971  CD  PRO A 422      -4.203 -22.127   9.883  1.00 0.965           C  
ANISOU 1971  CD  PRO A 422     9592   4200   4648   -798    500   -349       C  
ATOM   1972  N   ALA A 423      -2.544 -18.932  10.507  1.00-0.512           N  
ANISOU 1972  N   ALA A 423     8361   3456   3796   -467    552   -272       N  
ATOM   1973  CA  ALA A 423      -2.030 -17.577  10.325  1.00-0.512           C  
ANISOU 1973  CA  ALA A 423     8120   3400   3673   -372    560   -253       C  
ATOM   1974  C   ALA A 423      -2.393 -16.652  11.526  1.00-0.512           C  
ANISOU 1974  C   ALA A 423     8432   3894   4154   -341    568   -193       C  
ATOM   1975  O   ALA A 423      -2.119 -15.445  11.495  1.00-0.512           O  
ANISOU 1975  O   ALA A 423     8059   3666   3877   -275    573   -173       O  
ATOM   1976  CB  ALA A 423      -2.539 -16.998   9.012  1.00-0.512           C  
ANISOU 1976  CB  ALA A 423     8094   3486   3634   -413    520   -267       C  
ATOM   1977  N   MET A 424      -2.985 -17.233  12.589  1.00-1.337           N  
ANISOU 1977  N   MET A 424     7914   3348   3654   -391    574   -166       N  
ATOM   1978  CA  MET A 424      -3.438 -16.521  13.796  1.00-1.337           C  
ANISOU 1978  CA  MET A 424     7617   3203   3491   -370    589   -113       C  
ATOM   1979  C   MET A 424      -2.884 -17.187  15.067  1.00-1.337           C  
ANISOU 1979  C   MET A 424     8251   3693   4081   -336    624    -98       C  
ATOM   1980  O   MET A 424      -2.668 -18.399  15.081  1.00-1.337           O  
ANISOU 1980  O   MET A 424     8176   3410   3879   -369    630   -117       O  
ATOM   1981  CB  MET A 424      -4.976 -16.566  13.902  1.00-1.337           C  
ANISOU 1981  CB  MET A 424     7667   3404   3614   -479    565    -83       C  
ATOM   1982  CG  MET A 424      -5.719 -15.817  12.808  1.00-1.337           C  
ANISOU 1982  CG  MET A 424     7714   3640   3727   -507    520    -82       C  
ATOM   1983  SD  MET A 424      -7.486 -16.223  12.994  1.00-1.337           S  
ANISOU 1983  SD  MET A 424     7888   4000   3989   -650    489    -48       S  
ATOM   1984  CE  MET A 424      -8.132 -15.744  11.314  1.00-1.337           C  
ANISOU 1984  CE  MET A 424     7258   3531   3372   -692    413    -63       C  
ATOM   1985  N   ILE A 425      -2.675 -16.390  16.121  1.00 0.098           N  
ANISOU 1985  N   ILE A 425     8040   3578   3957   -271    645    -64       N  
ATOM   1986  CA  ILE A 425      -2.209 -16.805  17.456  1.00 0.098           C  
ANISOU 1986  CA  ILE A 425     8341   3781   4223   -232    672    -40       C  
ATOM   1987  C   ILE A 425      -3.157 -16.134  18.453  1.00 0.098           C  
ANISOU 1987  C   ILE A 425     8505   4104   4484   -253    688      5       C  
ATOM   1988  O   ILE A 425      -3.414 -14.936  18.311  1.00 0.098           O  
ANISOU 1988  O   ILE A 425     7987   3757   4067   -220    686     12       O  
ATOM   1989  CB  ILE A 425      -0.754 -16.277  17.769  1.00 0.098           C  
ANISOU 1989  CB  ILE A 425     9124   4543   5012   -111    682    -50       C  
ATOM   1990  CG1 ILE A 425       0.317 -16.824  16.820  1.00 0.098           C  
ANISOU 1990  CG1 ILE A 425     9491   4789   5304    -64    679    -92       C  
ATOM   1991  CG2 ILE A 425      -0.353 -16.596  19.232  1.00 0.098           C  
ANISOU 1991  CG2 ILE A 425     9734   5079   5587    -69    698    -18       C  
ATOM   1992  CD1 ILE A 425       1.733 -16.184  17.087  1.00 0.098           C  
ANISOU 1992  CD1 ILE A 425    10532   5876   6388     46    687    -98       C  
ATOM   1993  N   CYS A 426      -3.572 -16.856  19.514  1.00-1.442           N  
ANISOU 1993  N   CYS A 426     8436   3964   4370   -294    711     37       N  
ATOM   1994  CA  CYS A 426      -4.370 -16.283  20.594  1.00-1.442           C  
ANISOU 1994  CA  CYS A 426     8634   4299   4640   -303    740     80       C  
ATOM   1995  C   CYS A 426      -3.442 -15.968  21.764  1.00-1.442           C  
ANISOU 1995  C   CYS A 426     8648   4249   4614   -210    759     93       C  
ATOM   1996  O   CYS A 426      -2.482 -16.700  22.015  1.00-1.442           O  
ANISOU 1996  O   CYS A 426     8446   3873   4311   -172    752     86       O  
ATOM   1997  CB  CYS A 426      -5.480 -17.242  21.021  1.00-1.442           C  
ANISOU 1997  CB  CYS A 426     9018   4662   4997   -421    759    112       C  
ATOM   1998  SG  CYS A 426      -6.759 -17.513  19.763  1.00-1.442           S  
ANISOU 1998  SG  CYS A 426     9592   5372   5641   -554    728    101       S  
ATOM   1999  N   ALA A 427      -3.718 -14.871  22.476  1.00-1.388           N  
ANISOU 1999  N   ALA A 427     7960   3701   3997   -167    779    110       N  
ATOM   2000  CA  ALA A 427      -2.973 -14.473  23.670  1.00-1.388           C  
ANISOU 2000  CA  ALA A 427     7831   3527   3820    -93    793    120       C  
ATOM   2001  C   ALA A 427      -3.882 -13.689  24.577  1.00-1.388           C  
ANISOU 2001  C   ALA A 427     7986   3810   4019    -92    834    147       C  
ATOM   2002  O   ALA A 427      -4.801 -13.014  24.101  1.00-1.388           O  
ANISOU 2002  O   ALA A 427     8001   3984   4136   -107    845    149       O  
ATOM   2003  CB  ALA A 427      -1.727 -13.667  23.323  1.00-1.388           C  
ANISOU 2003  CB  ALA A 427     7818   3516   3822    -10    764     86       C  
ATOM   2004  N   GLY A 428      -3.640 -13.808  25.869  1.00-1.336           N  
ANISOU 2004  N   GLY A 428     7341   3098   3291    -67    857    169       N  
ATOM   2005  CA  GLY A 428      -4.428 -13.122  26.887  1.00-1.336           C  
ANISOU 2005  CA  GLY A 428     7298   3150   3257    -57    907    192       C  
ATOM   2006  C   GLY A 428      -4.716 -14.050  28.041  1.00-1.336           C  
ANISOU 2006  C   GLY A 428     8017   3777   3868    -96    942    235       C  
ATOM   2007  O   GLY A 428      -3.835 -14.823  28.436  1.00-1.336           O  
ANISOU 2007  O   GLY A 428     8057   3650   3794    -82    917    242       O  
ATOM   2008  N   PHE A 429      -5.958 -13.980  28.599  1.00 0.517           N  
ANISOU 2008  N   PHE A 429     7499   3373   3383   -141   1004    269       N  
ATOM   2009  CA  PHE A 429      -6.395 -14.817  29.737  1.00 0.517           C  
ANISOU 2009  CA  PHE A 429     7570   3369   3347   -192   1053    318       C  
ATOM   2010  C   PHE A 429      -7.843 -15.211  29.509  1.00 0.517           C  
ANISOU 2010  C   PHE A 429     8546   4495   4419   -294   1102    351       C  
ATOM   2011  O   PHE A 429      -8.663 -14.348  29.190  1.00 0.517           O  
ANISOU 2011  O   PHE A 429     8485   4650   4497   -280   1128    346       O  
ATOM   2012  CB  PHE A 429      -6.250 -14.058  31.108  1.00 0.517           C  
ANISOU 2012  CB  PHE A 429     7528   3323   3214   -121   1094    326       C  
ATOM   2013  CG  PHE A 429      -4.843 -13.569  31.366  1.00 0.517           C  
ANISOU 2013  CG  PHE A 429     7683   3364   3285    -32   1037    291       C  
ATOM   2014  CD1 PHE A 429      -3.914 -14.386  32.007  1.00 0.517           C  
ANISOU 2014  CD1 PHE A 429     8123   3625   3578    -19   1004    309       C  
ATOM   2015  CD2 PHE A 429      -4.412 -12.328  30.873  1.00 0.517           C  
ANISOU 2015  CD2 PHE A 429     7767   3522   3442     34   1011    242       C  
ATOM   2016  CE1 PHE A 429      -2.583 -13.974  32.158  1.00 0.517           C  
ANISOU 2016  CE1 PHE A 429     8287   3724   3692     57    942    278       C  
ATOM   2017  CE2 PHE A 429      -3.081 -11.922  31.011  1.00 0.517           C  
ANISOU 2017  CE2 PHE A 429     8048   3717   3662     93    954    210       C  
ATOM   2018  CZ  PHE A 429      -2.174 -12.745  31.663  1.00 0.517           C  
ANISOU 2018  CZ  PHE A 429     7917   3447   3407    104    918    227       C  
ATOM   2019  N   LEU A 430      -8.173 -16.501  29.688  1.00 1.222           N  
ANISOU 2019  N   LEU A 430     8458   4299   4256   -398   1117    388       N  
ATOM   2020  CA  LEU A 430      -9.548 -16.956  29.467  1.00 1.222           C  
ANISOU 2020  CA  LEU A 430     8284   4281   4179   -522   1161    422       C  
ATOM   2021  C   LEU A 430     -10.552 -16.397  30.493  1.00 1.222           C  
ANISOU 2021  C   LEU A 430     8746   4934   4688   -519   1251    460       C  
ATOM   2022  O   LEU A 430     -11.731 -16.295  30.176  1.00 1.222           O  
ANISOU 2022  O   LEU A 430     8580   5006   4674   -587   1287    480       O  
ATOM   2023  CB  LEU A 430      -9.617 -18.472  29.335  1.00 1.222           C  
ANISOU 2023  CB  LEU A 430     8324   4128   4112   -650   1153    448       C  
ATOM   2024  CG  LEU A 430      -9.040 -19.017  28.000  1.00 1.222           C  
ANISOU 2024  CG  LEU A 430     8675   4353   4458   -674   1074    404       C  
ATOM   2025  CD1 LEU A 430      -9.367 -20.484  27.837  1.00 1.222           C  
ANISOU 2025  CD1 LEU A 430     8816   4305   4489   -819   1076    428       C  
ATOM   2026  CD2 LEU A 430      -9.601 -18.295  26.806  1.00 1.222           C  
ANISOU 2026  CD2 LEU A 430     8021   3936   3990   -684   1042    369       C  
ATOM   2027  N   GLN A 431     -10.073 -15.925  31.661  1.00 0.504           N  
ANISOU 2027  N   GLN A 431     8457   4567   4281   -431   1286    467       N  
ATOM   2028  CA  GLN A 431     -10.911 -15.257  32.671  1.00 0.504           C  
ANISOU 2028  CA  GLN A 431     8325   4599   4169   -402   1380    494       C  
ATOM   2029  C   GLN A 431     -11.144 -13.770  32.263  1.00 0.504           C  
ANISOU 2029  C   GLN A 431     8976   5449   4961   -290   1383    453       C  
ATOM   2030  O   GLN A 431     -11.934 -13.084  32.908  1.00 0.504           O  
ANISOU 2030  O   GLN A 431     9055   5692   5084   -248   1464    468       O  
ATOM   2031  CB  GLN A 431     -10.275 -15.342  34.074  1.00 0.504           C  
ANISOU 2031  CB  GLN A 431     8490   4575   4116   -352   1411    512       C  
ATOM   2032  CG  GLN A 431      -8.935 -14.597  34.233  1.00 0.504           C  
ANISOU 2032  CG  GLN A 431     8451   4392   3980   -228   1346    462       C  
ATOM   2033  CD  GLN A 431      -7.736 -15.512  34.123  1.00 0.504           C  
ANISOU 2033  CD  GLN A 431     9345   5039   4744   -234   1268    462       C  
ATOM   2034  OE1 GLN A 431      -7.680 -16.404  33.287  1.00 0.504           O  
ANISOU 2034  OE1 GLN A 431     8261   3891   3694   -302   1230    467       O  
ATOM   2035  NE2 GLN A 431      -6.734 -15.300  34.954  1.00 0.504           N  
ANISOU 2035  NE2 GLN A 431     8701   4251   3945   -157   1239    453       N  
ATOM   2036  N   GLY A 432     -10.430 -13.297  31.229  1.00-0.639           N  
ANISOU 2036  N   GLY A 432     8365   4805   4404   -239   1302    405       N  
ATOM   2037  CA  GLY A 432     -10.506 -11.918  30.768  1.00-0.639           C  
ANISOU 2037  CA  GLY A 432     8178   4749   4320   -133   1296    369       C  
ATOM   2038  C   GLY A 432      -9.693 -10.990  31.642  1.00-0.639           C  
ANISOU 2038  C   GLY A 432     8564   5007   4571    -21   1307    338       C  
ATOM   2039  O   GLY A 432      -8.674 -11.406  32.206  1.00-0.639           O  
ANISOU 2039  O   GLY A 432     8474   4713   4326    -19   1274    330       O  
ATOM   2040  N   ASN A 433     -10.163  -9.713  31.769  1.00 0.322           N  
ANISOU 2040  N   ASN A 433     8204   4765   4264     74   1351    320       N  
ATOM   2041  CA  ASN A 433      -9.616  -8.609  32.582  1.00 0.322           C  
ANISOU 2041  CA  ASN A 433     8256   4709   4187    181   1373    284       C  
ATOM   2042  C   ASN A 433      -8.373  -7.905  32.002  1.00 0.322           C  
ANISOU 2042  C   ASN A 433     8657   4964   4544    231   1290    229       C  
ATOM   2043  O   ASN A 433      -8.201  -6.718  32.264  1.00 0.322           O  
ANISOU 2043  O   ASN A 433     8733   5000   4569    317   1307    195       O  
ATOM   2044  CB  ASN A 433      -9.346  -9.026  34.047  1.00 0.322           C  
ANISOU 2044  CB  ASN A 433     8578   4898   4315    171   1417    298       C  
ATOM   2045  CG  ASN A 433     -10.532  -9.640  34.742  1.00 0.322           C  
ANISOU 2045  CG  ASN A 433    10990   7444   6748    120   1514    354       C  
ATOM   2046  OD1 ASN A 433     -11.663  -9.148  34.645  1.00 0.322           O  
ANISOU 2046  OD1 ASN A 433     9942   6608   5828    149   1587    369       O  
ATOM   2047  ND2 ASN A 433     -10.291 -10.737  35.460  1.00 0.322           N  
ANISOU 2047  ND2 ASN A 433    10058   6394   5689     43   1520    390       N  
ATOM   2048  N   VAL A 434      -7.490  -8.625  31.296  1.00-0.201           N  
ANISOU 2048  N   VAL A 434     8111   4330   4005    178   1207    222       N  
ATOM   2049  CA  VAL A 434      -6.273  -8.076  30.668  1.00-0.201           C  
ANISOU 2049  CA  VAL A 434     7988   4099   3860    211   1131    176       C  
ATOM   2050  C   VAL A 434      -6.356  -8.460  29.196  1.00-0.201           C  
ANISOU 2050  C   VAL A 434     8121   4308   4134    171   1083    178       C  
ATOM   2051  O   VAL A 434      -6.520  -9.643  28.898  1.00-0.201           O  
ANISOU 2051  O   VAL A 434     8020   4211   4058     96   1068    203       O  
ATOM   2052  CB  VAL A 434      -4.945  -8.561  31.322  1.00-0.201           C  
ANISOU 2052  CB  VAL A 434     8505   4439   4232    201   1080    162       C  
ATOM   2053  CG1 VAL A 434      -3.738  -7.919  30.632  1.00-0.201           C  
ANISOU 2053  CG1 VAL A 434     8436   4305   4170    228   1008    117       C  
ATOM   2054  CG2 VAL A 434      -4.921  -8.244  32.814  1.00-0.201           C  
ANISOU 2054  CG2 VAL A 434     8577   4435   4142    233   1123    162       C  
ATOM   2055  N   ASP A 435      -6.296  -7.463  28.279  1.00-1.225           N  
ANISOU 2055  N   ASP A 435     7618   3850   3704    218   1062    153       N  
ATOM   2056  CA  ASP A 435      -6.447  -7.711  26.830  1.00-1.225           C  
ANISOU 2056  CA  ASP A 435     7574   3885   3779    184   1017    155       C  
ATOM   2057  C   ASP A 435      -6.105  -6.468  26.007  1.00-1.225           C  
ANISOU 2057  C   ASP A 435     7838   4143   4071    247    993    129       C  
ATOM   2058  O   ASP A 435      -5.937  -5.355  26.549  1.00-1.225           O  
ANISOU 2058  O   ASP A 435     7745   3992   3914    316   1019    110       O  
ATOM   2059  CB  ASP A 435      -7.933  -8.114  26.548  1.00-1.225           C  
ANISOU 2059  CB  ASP A 435     7691   4202   4022    146   1053    196       C  
ATOM   2060  CG  ASP A 435      -8.284  -8.972  25.327  1.00-1.225           C  
ANISOU 2060  CG  ASP A 435     8462   5054   4888     64   1007    208       C  
ATOM   2061  OD1 ASP A 435      -7.361  -9.328  24.547  1.00-1.225           O  
ANISOU 2061  OD1 ASP A 435     8083   4563   4476     42    948    182       O  
ATOM   2062  OD2 ASP A 435      -9.485  -9.295  25.156  1.00-1.225           O  
ANISOU 2062  OD2 ASP A 435     9066   5839   5598     18   1030    241       O  
ATOM   2063  N   SER A 436      -6.053  -6.654  24.684  1.00-0.895           N  
ANISOU 2063  N   SER A 436     7238   3591   3549    220    947    127       N  
ATOM   2064  CA  SER A 436      -5.893  -5.573  23.731  1.00-0.895           C  
ANISOU 2064  CA  SER A 436     7373   3732   3714    271    926    115       C  
ATOM   2065  C   SER A 436      -7.321  -5.030  23.491  1.00-0.895           C  
ANISOU 2065  C   SER A 436     8241   4777   4682    316    960    148       C  
ATOM   2066  O   SER A 436      -8.297  -5.687  23.856  1.00-0.895           O  
ANISOU 2066  O   SER A 436     8247   4918   4755    283    989    178       O  
ATOM   2067  CB  SER A 436      -5.268  -6.081  22.431  1.00-0.895           C  
ANISOU 2067  CB  SER A 436     7546   3885   3913    223    867    103       C  
ATOM   2068  OG  SER A 436      -6.004  -7.175  21.910  1.00-0.895           O  
ANISOU 2068  OG  SER A 436     8034   4473   4468    155    852    123       O  
ATOM   2069  N   CYS A 437      -7.452  -3.836  22.930  1.00-1.442           N  
ANISOU 2069  N   CYS A 437     8068   4606   4518    392    961    148       N  
ATOM   2070  CA  CYS A 437      -8.772  -3.253  22.672  1.00-1.442           C  
ANISOU 2070  CA  CYS A 437     8146   4861   4695    459    990    186       C  
ATOM   2071  C   CYS A 437      -8.723  -2.339  21.431  1.00-1.442           C  
ANISOU 2071  C   CYS A 437     8189   4898   4753    513    952    193       C  
ATOM   2072  O   CYS A 437      -7.654  -2.212  20.842  1.00-1.442           O  
ANISOU 2072  O   CYS A 437     8100   4664   4594    484    912    167       O  
ATOM   2073  CB  CYS A 437      -9.301  -2.521  23.909  1.00-1.442           C  
ANISOU 2073  CB  CYS A 437     8393   5103   4900    546   1069    189       C  
ATOM   2074  SG  CYS A 437     -11.101  -2.299  23.919  1.00-1.442           S  
ANISOU 2074  SG  CYS A 437     8932   5939   5600    617   1123    244       S  
ATOM   2075  N   GLN A 438      -9.869  -1.749  21.014  1.00-1.071           N  
ANISOU 2075  N   GLN A 438     7645   4520   4301    590    966    233       N  
ATOM   2076  CA  GLN A 438      -9.984  -0.843  19.839  1.00-1.071           C  
ANISOU 2076  CA  GLN A 438     7718   4595   4380    657    930    254       C  
ATOM   2077  C   GLN A 438      -8.891   0.258  19.901  1.00-1.071           C  
ANISOU 2077  C   GLN A 438     8218   4820   4722    705    940    223       C  
ATOM   2078  O   GLN A 438      -8.809   0.962  20.916  1.00-1.071           O  
ANISOU 2078  O   GLN A 438     8565   5049   4985    768    996    205       O  
ATOM   2079  CB  GLN A 438     -11.386  -0.183  19.833  1.00-1.071           C  
ANISOU 2079  CB  GLN A 438     7809   4890   4576    773    963    304       C  
ATOM   2080  N   GLY A 439      -8.060   0.359  18.854  1.00-1.409           N  
ANISOU 2080  N   GLY A 439     7367   3870   3823    663    888    214       N  
ATOM   2081  CA  GLY A 439      -6.942   1.293  18.800  1.00-1.409           C  
ANISOU 2081  CA  GLY A 439     7135   3393   3450    675    892    186       C  
ATOM   2082  C   GLY A 439      -5.594   0.632  19.055  1.00-1.409           C  
ANISOU 2082  C   GLY A 439     7510   3656   3772    571    872    139       C  
ATOM   2083  O   GLY A 439      -4.555   1.227  18.761  1.00-1.409           O  
ANISOU 2083  O   GLY A 439     7332   3316   3502    550    863    119       O  
ATOM   2084  N   ASP A 440      -5.575  -0.602  19.632  1.00-1.473           N  
ANISOU 2084  N   ASP A 440     7226   3456   3541    505    868    126       N  
ATOM   2085  CA  ASP A 440      -4.308  -1.347  19.808  1.00-1.473           C  
ANISOU 2085  CA  ASP A 440     7287   3431   3561    421    844     88       C  
ATOM   2086  C   ASP A 440      -3.899  -2.098  18.540  1.00-1.473           C  
ANISOU 2086  C   ASP A 440     7719   3906   4032    360    796     89       C  
ATOM   2087  O   ASP A 440      -2.722  -2.459  18.372  1.00-1.473           O  
ANISOU 2087  O   ASP A 440     7678   3787   3953    311    778     60       O  
ATOM   2088  CB  ASP A 440      -4.384  -2.342  20.965  1.00-1.473           C  
ANISOU 2088  CB  ASP A 440     7301   3477   3586    386    860     78       C  
ATOM   2089  CG  ASP A 440      -4.451  -1.651  22.297  1.00-1.473           C  
ANISOU 2089  CG  ASP A 440     8095   4191   4304    434    907     66       C  
ATOM   2090  OD1 ASP A 440      -3.705  -0.644  22.488  1.00-1.473           O  
ANISOU 2090  OD1 ASP A 440     7783   3729   3895    456    911     40       O  
ATOM   2091  OD2 ASP A 440      -5.254  -2.094  23.152  1.00-1.473           O  
ANISOU 2091  OD2 ASP A 440     8028   4202   4260    446    942     80       O  
ATOM   2092  N   SER A 441      -4.885  -2.335  17.661  1.00-1.479           N  
ANISOU 2092  N   SER A 441     7100   3421   3483    365    776    120       N  
ATOM   2093  CA  SER A 441      -4.730  -3.100  16.425  1.00-1.479           C  
ANISOU 2093  CA  SER A 441     7274   3643   3678    307    730    119       C  
ATOM   2094  C   SER A 441      -3.586  -2.615  15.561  1.00-1.479           C  
ANISOU 2094  C   SER A 441     7802   4052   4132    297    717    103       C  
ATOM   2095  O   SER A 441      -3.351  -1.406  15.469  1.00-1.479           O  
ANISOU 2095  O   SER A 441     7772   3938   4049    345    733    112       O  
ATOM   2096  CB  SER A 441      -6.042  -3.150  15.655  1.00-1.479           C  
ANISOU 2096  CB  SER A 441     7930   4469   4411    320    705    158       C  
ATOM   2097  OG  SER A 441      -6.938  -4.038  16.322  1.00-1.479           O  
ANISOU 2097  OG  SER A 441     9108   5780   5671    285    712    167       O  
ATOM   2098  N   GLY A 442      -2.852  -3.578  15.007  1.00-1.466           N  
ANISOU 2098  N   GLY A 442     7294   3526   3612    234    695     77       N  
ATOM   2099  CA  GLY A 442      -1.655  -3.355  14.214  1.00-1.466           C  
ANISOU 2099  CA  GLY A 442     7152   3297   3410    214    692     58       C  
ATOM   2100  C   GLY A 442      -0.392  -3.352  15.062  1.00-1.466           C  
ANISOU 2100  C   GLY A 442     7448   3506   3683    201    712     26       C  
ATOM   2101  O   GLY A 442       0.714  -3.528  14.544  1.00-1.466           O  
ANISOU 2101  O   GLY A 442     7242   3264   3453    173    712      5       O  
ATOM   2102  N   GLY A 443      -0.560  -3.172  16.369  1.00-1.443           N  
ANISOU 2102  N   GLY A 443     6935   2976   3176    220    729     23       N  
ATOM   2103  CA  GLY A 443       0.535  -3.091  17.331  1.00-1.443           C  
ANISOU 2103  CA  GLY A 443     6979   2953   3193    208    738     -4       C  
ATOM   2104  C   GLY A 443       1.255  -4.387  17.659  1.00-1.443           C  
ANISOU 2104  C   GLY A 443     7588   3576   3820    179    725    -25       C  
ATOM   2105  O   GLY A 443       0.834  -5.459  17.241  1.00-1.443           O  
ANISOU 2105  O   GLY A 443     7436   3461   3690    163    714    -22       O  
ATOM   2106  N   PRO A 444       2.303  -4.305  18.505  1.00-1.455           N  
ANISOU 2106  N   PRO A 444     7152   3104   3367    173    724    -45       N  
ATOM   2107  CA  PRO A 444       3.095  -5.501  18.818  1.00-1.455           C  
ANISOU 2107  CA  PRO A 444     7007   2972   3236    164    709    -59       C  
ATOM   2108  C   PRO A 444       2.582  -6.457  19.896  1.00-1.455           C  
ANISOU 2108  C   PRO A 444     7496   3449   3712    172    706    -50       C  
ATOM   2109  O   PRO A 444       1.978  -6.049  20.896  1.00-1.455           O  
ANISOU 2109  O   PRO A 444     7323   3262   3513    183    718    -41       O  
ATOM   2110  CB  PRO A 444       4.433  -4.910  19.291  1.00-1.455           C  
ANISOU 2110  CB  PRO A 444     7203   3162   3426    155    700    -79       C  
ATOM   2111  CG  PRO A 444       4.059  -3.577  19.919  1.00-1.455           C  
ANISOU 2111  CG  PRO A 444     7642   3545   3817    154    711    -78       C  
ATOM   2112  CD  PRO A 444       2.904  -3.076  19.090  1.00-1.455           C  
ANISOU 2112  CD  PRO A 444     7224   3118   3397    171    730    -56       C  
ATOM   2113  N   LEU A 445       2.928  -7.740  19.708  1.00-1.185           N  
ANISOU 2113  N   LEU A 445     7260   3204   3478    169    695    -54       N  
ATOM   2114  CA  LEU A 445       2.809  -8.841  20.656  1.00-1.185           C  
ANISOU 2114  CA  LEU A 445     7166   3068   3351    175    691    -44       C  
ATOM   2115  C   LEU A 445       4.249  -9.372  20.637  1.00-1.185           C  
ANISOU 2115  C   LEU A 445     7588   3482   3774    202    672    -59       C  
ATOM   2116  O   LEU A 445       4.712  -9.893  19.619  1.00-1.185           O  
ANISOU 2116  O   LEU A 445     7460   3355   3661    208    674    -73       O  
ATOM   2117  CB  LEU A 445       1.802  -9.932  20.226  1.00-1.185           C  
ANISOU 2117  CB  LEU A 445     7207   3084   3382    146    697    -31       C  
ATOM   2118  CG  LEU A 445       1.786 -11.210  21.128  1.00-1.185           C  
ANISOU 2118  CG  LEU A 445     7733   3527   3850    145    696    -16       C  
ATOM   2119  CD1 LEU A 445       1.016 -10.990  22.401  1.00-1.185           C  
ANISOU 2119  CD1 LEU A 445     7888   3688   3981    138    713     10       C  
ATOM   2120  CD2 LEU A 445       1.191 -12.396  20.407  1.00-1.185           C  
ANISOU 2120  CD2 LEU A 445     7845   3578   3934    104    697    -15       C  
ATOM   2121  N   VAL A 446       4.993  -9.131  21.709  1.00-0.674           N  
ANISOU 2121  N   VAL A 446     7339   3242   3511    221    655    -59       N  
ATOM   2122  CA  VAL A 446       6.423  -9.459  21.750  1.00-0.674           C  
ANISOU 2122  CA  VAL A 446     7315   3259   3513    253    632    -69       C  
ATOM   2123  C   VAL A 446       6.775 -10.459  22.858  1.00-0.674           C  
ANISOU 2123  C   VAL A 446     8043   3943   4191    293    608    -50       C  
ATOM   2124  O   VAL A 446       6.046 -10.540  23.830  1.00-0.674           O  
ANISOU 2124  O   VAL A 446     8103   3948   4189    284    610    -31       O  
ATOM   2125  CB  VAL A 446       7.296  -8.160  21.838  1.00-0.674           C  
ANISOU 2125  CB  VAL A 446     7605   3631   3844    232    619    -86       C  
ATOM   2126  CG1 VAL A 446       7.098  -7.267  20.606  1.00-0.674           C  
ANISOU 2126  CG1 VAL A 446     7485   3532   3757    199    644    -98       C  
ATOM   2127  CG2 VAL A 446       7.010  -7.368  23.132  1.00-0.674           C  
ANISOU 2127  CG2 VAL A 446     7614   3612   3796    215    605    -85       C  
ATOM   2128  N   THR A 447       7.900 -11.183  22.725  1.00-0.305           N  
ANISOU 2128  N   THR A 447     7514   3444   3686    345    590    -51       N  
ATOM   2129  CA  THR A 447       8.409 -12.075  23.780  1.00-0.305           C  
ANISOU 2129  CA  THR A 447     7548   3442   3669    400    560    -26       C  
ATOM   2130  C   THR A 447       9.925 -11.917  23.872  1.00-0.305           C  
ANISOU 2130  C   THR A 447     7972   4004   4168    446    525    -32       C  
ATOM   2131  O   THR A 447      10.588 -11.570  22.882  1.00-0.305           O  
ANISOU 2131  O   THR A 447     7631   3763   3916    446    538    -55       O  
ATOM   2132  CB  THR A 447       7.999 -13.559  23.558  1.00-0.305           C  
ANISOU 2132  CB  THR A 447     7989   3737   4036    435    577     -8       C  
ATOM   2133  OG1 THR A 447       8.074 -14.230  24.819  1.00-0.305           O  
ANISOU 2133  OG1 THR A 447     8120   3792   4080    472    553     28       O  
ATOM   2134  CG2 THR A 447       8.899 -14.294  22.572  1.00-0.305           C  
ANISOU 2134  CG2 THR A 447     7838   3592   3919    498    586    -23       C  
ATOM   2135  N   SER A 448      10.468 -12.237  25.038  1.00 0.193           N  
ANISOU 2135  N   SER A 448     7539   3587   3699    488    480     -9       N  
ATOM   2136  CA  SER A 448      11.898 -12.186  25.275  1.00 0.193           C  
ANISOU 2136  CA  SER A 448     7502   3712   3741    537    435     -7       C  
ATOM   2137  C   SER A 448      12.435 -13.600  25.310  1.00 0.193           C  
ANISOU 2137  C   SER A 448     8258   4422   4473    648    427     22       C  
ATOM   2138  O   SER A 448      11.951 -14.423  26.100  1.00 0.193           O  
ANISOU 2138  O   SER A 448     8558   4574   4655    681    417     55       O  
ATOM   2139  CB  SER A 448      12.200 -11.498  26.608  1.00 0.193           C  
ANISOU 2139  CB  SER A 448     7860   4131   4064    508    377      0       C  
ATOM   2140  OG  SER A 448      13.584 -11.658  26.874  1.00 0.193           O  
ANISOU 2140  OG  SER A 448     8208   4654   4493    562    323      9       O  
ATOM   2141  N   LYS A 449      13.451 -13.883  24.478  1.00 0.764           N  
ANISOU 2141  N   LYS A 449     7654   3939   3973    710    435     11       N  
ATOM   2142  CA  LYS A 449      14.112 -15.191  24.440  1.00 0.764           C  
ANISOU 2142  CA  LYS A 449     7787   4037   4089    839    432     37       C  
ATOM   2143  C   LYS A 449      15.542 -14.992  23.987  1.00 0.764           C  
ANISOU 2143  C   LYS A 449     8524   5027   4986    900    421     29       C  
ATOM   2144  O   LYS A 449      15.766 -14.237  23.026  1.00 0.764           O  
ANISOU 2144  O   LYS A 449     8496   5119   5059    844    456     -6       O  
ATOM   2145  CB  LYS A 449      13.383 -16.177  23.517  1.00 0.764           C  
ANISOU 2145  CB  LYS A 449     8011   4042   4224    863    494     27       C  
ATOM   2146  CG  LYS A 449      13.829 -17.605  23.753  1.00 0.764           C  
ANISOU 2146  CG  LYS A 449     8593   4493   4723    997    491     59       C  
ATOM   2147  CD  LYS A 449      13.111 -18.604  22.881  1.00 0.764           C  
ANISOU 2147  CD  LYS A 449     7883   3532   3896   1007    549     44       C  
ATOM   2148  CE  LYS A 449      13.589 -20.005  23.244  1.00 0.764           C  
ANISOU 2148  CE  LYS A 449     9384   4865   5287   1148    546     79       C  
ATOM   2149  NZ  LYS A 449      12.606 -21.030  22.826  1.00 0.764           N  
ANISOU 2149  NZ  LYS A 449     9844   5001   5569   1122    588     74       N  
ATOM   2150  N   ASN A 450      16.510 -15.676  24.666  1.00 0.391           N  
ANISOU 2150  N   ASN A 450     7938   4533   4424   1018    373     65       N  
ATOM   2151  CA  ASN A 450      17.951 -15.548  24.389  1.00 0.391           C  
ANISOU 2151  CA  ASN A 450     7813   4702   4475   1088    356     66       C  
ATOM   2152  C   ASN A 450      18.388 -14.051  24.501  1.00 0.391           C  
ANISOU 2152  C   ASN A 450     8297   5434   5090    958    323     42       C  
ATOM   2153  O   ASN A 450      19.254 -13.600  23.751  1.00 0.391           O  
ANISOU 2153  O   ASN A 450     8206   5573   5157    949    345     24       O  
ATOM   2154  CB  ASN A 450      18.294 -16.145  22.999  1.00 0.391           C  
ANISOU 2154  CB  ASN A 450     7950   4839   4665   1165    436     43       C  
ATOM   2155  CG  ASN A 450      19.766 -16.350  22.731  1.00 0.391           C  
ANISOU 2155  CG  ASN A 450    10618   7797   7504   1280    432     54       C  
ATOM   2156  OD1 ASN A 450      20.548 -16.719  23.619  1.00 0.391           O  
ANISOU 2156  OD1 ASN A 450    10118   7436   7051   1373    366     95       O  
ATOM   2157  ND2 ASN A 450      20.173 -16.115  21.489  1.00 0.391           N  
ANISOU 2157  ND2 ASN A 450     9282   6574   6268   1278    503     21       N  
ATOM   2158  N   ASN A 451      17.754 -13.294  25.431  1.00 0.698           N  
ANISOU 2158  N   ASN A 451     7891   4960   4602    853    279     40       N  
ATOM   2159  CA  ASN A 451      17.970 -11.855  25.718  1.00 0.698           C  
ANISOU 2159  CA  ASN A 451     7831   5050   4605    716    245     14       C  
ATOM   2160  C   ASN A 451      17.683 -10.930  24.515  1.00 0.698           C  
ANISOU 2160  C   ASN A 451     8103   5329   4934    613    314    -28       C  
ATOM   2161  O   ASN A 451      18.352  -9.900  24.321  1.00 0.698           O  
ANISOU 2161  O   ASN A 451     7980   5391   4917    525    302    -47       O  
ATOM   2162  CB  ASN A 451      19.360 -11.592  26.304  1.00 0.698           C  
ANISOU 2162  CB  ASN A 451     8558   6085   5468    731    168     28       C  
ATOM   2163  CG  ASN A 451      19.613 -12.324  27.589  1.00 0.698           C  
ANISOU 2163  CG  ASN A 451    12628  10153   9464    822     86     72       C  
ATOM   2164  OD1 ASN A 451      18.936 -12.112  28.606  1.00 0.698           O  
ANISOU 2164  OD1 ASN A 451    12486   9861   9171    775     46     78       O  
ATOM   2165  ND2 ASN A 451      20.597 -13.210  27.561  1.00 0.698           N  
ANISOU 2165  ND2 ASN A 451    11756   9444   8688    963     63    108       N  
ATOM   2166  N   ILE A 452      16.684 -11.309  23.701  1.00 0.443           N  
ANISOU 2166  N   ILE A 452     7532   4551   4284    621    382    -38       N  
ATOM   2167  CA  ILE A 452      16.261 -10.537  22.536  1.00 0.443           C  
ANISOU 2167  CA  ILE A 452     7398   4390   4173    537    445    -69       C  
ATOM   2168  C   ILE A 452      14.733 -10.433  22.580  1.00 0.443           C  
ANISOU 2168  C   ILE A 452     7622   4363   4255    489    470    -75       C  
ATOM   2169  O   ILE A 452      14.083 -11.433  22.895  1.00 0.443           O  
ANISOU 2169  O   ILE A 452     7352   3934   3889    549    473    -57       O  
ATOM   2170  CB  ILE A 452      16.713 -11.248  21.210  1.00 0.443           C  
ANISOU 2170  CB  ILE A 452     7736   4772   4577    612    510    -77       C  
ATOM   2171  CG1 ILE A 452      18.259 -11.431  21.101  1.00 0.443           C  
ANISOU 2171  CG1 ILE A 452     7738   5061   4744    679    499    -68       C  
ATOM   2172  CG2 ILE A 452      16.141 -10.572  19.966  1.00 0.443           C  
ANISOU 2172  CG2 ILE A 452     7624   4599   4454    531    575   -104       C  
ATOM   2173  CD1 ILE A 452      19.101 -10.210  20.748  1.00 0.443           C  
ANISOU 2173  CD1 ILE A 452     8406   5974   5554    575    501    -82       C  
ATOM   2174  N   TRP A 453      14.164  -9.245  22.227  1.00-0.468           N  
ANISOU 2174  N   TRP A 453     7018   3724   3637    385    491    -96       N  
ATOM   2175  CA  TRP A 453      12.715  -9.085  22.078  1.00-0.468           C  
ANISOU 2175  CA  TRP A 453     7140   3650   3652    349    521    -99       C  
ATOM   2176  C   TRP A 453      12.342  -9.391  20.606  1.00-0.468           C  
ANISOU 2176  C   TRP A 453     7495   3958   4017    357    580   -110       C  
ATOM   2177  O   TRP A 453      12.897  -8.783  19.685  1.00-0.468           O  
ANISOU 2177  O   TRP A 453     7175   3734   3766    325    607   -124       O  
ATOM   2178  CB  TRP A 453      12.256  -7.685  22.483  1.00-0.468           C  
ANISOU 2178  CB  TRP A 453     7134   3613   3609    255    513   -113       C  
ATOM   2179  CG  TRP A 453      12.319  -7.461  23.962  1.00-0.468           C  
ANISOU 2179  CG  TRP A 453     7389   3858   3804    245    460   -108       C  
ATOM   2180  CD1 TRP A 453      13.329  -6.866  24.659  1.00-0.468           C  
ANISOU 2180  CD1 TRP A 453     7765   4360   4215    208    408   -117       C  
ATOM   2181  CD2 TRP A 453      11.376  -7.928  24.935  1.00-0.468           C  
ANISOU 2181  CD2 TRP A 453     7445   3775   3745    270    452    -91       C  
ATOM   2182  NE1 TRP A 453      13.043  -6.879  26.010  1.00-0.468           N  
ANISOU 2182  NE1 TRP A 453     7870   4398   4216    210    365   -110       N  
ATOM   2183  CE2 TRP A 453      11.845  -7.518  26.206  1.00-0.468           C  
ANISOU 2183  CE2 TRP A 453     8089   4453   4342    251    397    -93       C  
ATOM   2184  CE3 TRP A 453      10.135  -8.584  24.853  1.00-0.468           C  
ANISOU 2184  CE3 TRP A 453     7607   3794   3836    294    489    -76       C  
ATOM   2185  CZ2 TRP A 453      11.120  -7.750  27.382  1.00-0.468           C  
ANISOU 2185  CZ2 TRP A 453     8029   4278   4154    264    384    -79       C  
ATOM   2186  CZ3 TRP A 453       9.417  -8.806  26.016  1.00-0.468           C  
ANISOU 2186  CZ3 TRP A 453     7866   3956   3989    300    480    -59       C  
ATOM   2187  CH2 TRP A 453       9.925  -8.423  27.267  1.00-0.468           C  
ANISOU 2187  CH2 TRP A 453     7970   4086   4036    292    431    -59       C  
ATOM   2188  N   TRP A 454      11.413 -10.343  20.404  1.00 0.573           N  
ANISOU 2188  N   TRP A 454     7253   3564   3695    391    599   -103       N  
ATOM   2189  CA  TRP A 454      10.953 -10.820  19.090  1.00 0.573           C  
ANISOU 2189  CA  TRP A 454     7384   3625   3804    397    645   -117       C  
ATOM   2190  C   TRP A 454       9.498 -10.441  18.843  1.00 0.573           C  
ANISOU 2190  C   TRP A 454     7628   3754   3980    337    658   -116       C  
ATOM   2191  O   TRP A 454       8.678 -10.537  19.762  1.00 0.573           O  
ANISOU 2191  O   TRP A 454     7147   3197   3446    324    641   -100       O  
ATOM   2192  CB  TRP A 454      11.054 -12.356  19.044  1.00 0.573           C  
ANISOU 2192  CB  TRP A 454     7329   3474   3697    481    652   -112       C  
ATOM   2193  CG  TRP A 454      12.398 -12.891  19.426  1.00 0.573           C  
ANISOU 2193  CG  TRP A 454     7352   3606   3781    570    636   -103       C  
ATOM   2194  CD1 TRP A 454      12.825 -13.226  20.674  1.00 0.573           C  
ANISOU 2194  CD1 TRP A 454     7689   3968   4115    616    589    -77       C  
ATOM   2195  CD2 TRP A 454      13.493 -13.163  18.536  1.00 0.573           C  
ANISOU 2195  CD2 TRP A 454     7252   3623   3756    631    668   -118       C  
ATOM   2196  NE1 TRP A 454      14.118 -13.702  20.624  1.00 0.573           N  
ANISOU 2196  NE1 TRP A 454     7590   4004   4095    709    582    -71       N  
ATOM   2197  CE2 TRP A 454      14.550 -13.683  19.321  1.00 0.573           C  
ANISOU 2197  CE2 TRP A 454     7745   4223   4306    722    636    -97       C  
ATOM   2198  CE3 TRP A 454      13.651 -13.100  17.144  1.00 0.573           C  
ANISOU 2198  CE3 TRP A 454     7359   3749   3877    627    724   -145       C  
ATOM   2199  CZ2 TRP A 454      15.770 -14.093  18.761  1.00 0.573           C  
ANISOU 2199  CZ2 TRP A 454     7570   4199   4223    814    661   -102       C  
ATOM   2200  CZ3 TRP A 454      14.859 -13.502  16.584  1.00 0.573           C  
ANISOU 2200  CZ3 TRP A 454     7569   4091   4163    711    756   -154       C  
ATOM   2201  CH2 TRP A 454      15.891 -14.020  17.385  1.00 0.573           C  
ANISOU 2201  CH2 TRP A 454     7594   4239   4262    808    727   -132       C  
ATOM   2202  N   LEU A 455       9.168 -10.059  17.598  1.00-0.911           N  
ANISOU 2202  N   LEU A 455     7189   3311   3541    304    689   -130       N  
ATOM   2203  CA  LEU A 455       7.792  -9.696  17.224  1.00-0.911           C  
ANISOU 2203  CA  LEU A 455     7148   3193   3451    256    696   -125       C  
ATOM   2204  C   LEU A 455       7.033 -10.977  16.907  1.00-0.911           C  
ANISOU 2204  C   LEU A 455     7972   3905   4207    268    701   -127       C  
ATOM   2205  O   LEU A 455       7.175 -11.515  15.823  1.00-0.911           O  
ANISOU 2205  O   LEU A 455     8014   3916   4221    277    720   -146       O  
ATOM   2206  CB  LEU A 455       7.767  -8.729  16.018  1.00-0.911           C  
ANISOU 2206  CB  LEU A 455     6983   3067   3298    218    719   -132       C  
ATOM   2207  CG  LEU A 455       6.390  -8.159  15.624  1.00-0.911           C  
ANISOU 2207  CG  LEU A 455     7318   3353   3595    180    718   -120       C  
ATOM   2208  CD1 LEU A 455       5.737  -7.340  16.794  1.00-0.911           C  
ANISOU 2208  CD1 LEU A 455     7211   3236   3489    166    704   -102       C  
ATOM   2209  CD2 LEU A 455       6.482  -7.342  14.320  1.00-0.911           C  
ANISOU 2209  CD2 LEU A 455     7253   3311   3521    155    739   -121       C  
ATOM   2210  N   ILE A 456       6.247 -11.470  17.856  1.00-0.185           N  
ANISOU 2210  N   ILE A 456     7651   3514   3847    261    686   -109       N  
ATOM   2211  CA  ILE A 456       5.506 -12.727  17.692  1.00-0.185           C  
ANISOU 2211  CA  ILE A 456     7727   3466   3847    253    689   -108       C  
ATOM   2212  C   ILE A 456       4.191 -12.514  16.972  1.00-0.185           C  
ANISOU 2212  C   ILE A 456     7806   3537   3911    187    692   -107       C  
ATOM   2213  O   ILE A 456       3.790 -13.354  16.170  1.00-0.185           O  
ANISOU 2213  O   ILE A 456     7583   3235   3629    164    695   -123       O  
ATOM   2214  CB  ILE A 456       5.354 -13.429  19.091  1.00-0.185           C  
ANISOU 2214  CB  ILE A 456     8092   3759   4169    271    676    -81       C  
ATOM   2215  CG1 ILE A 456       6.739 -13.638  19.737  1.00-0.185           C  
ANISOU 2215  CG1 ILE A 456     8074   3773   4169    347    661    -77       C  
ATOM   2216  CG2 ILE A 456       4.583 -14.771  19.022  1.00-0.185           C  
ANISOU 2216  CG2 ILE A 456     8221   3730   4202    247    682    -75       C  
ATOM   2217  CD1 ILE A 456       7.793 -14.469  18.825  1.00-0.185           C  
ANISOU 2217  CD1 ILE A 456     7687   3361   3776    415    677   -100       C  
ATOM   2218  N   GLY A 457       3.529 -11.409  17.272  1.00-1.443           N  
ANISOU 2218  N   GLY A 457     7358   3168   3509    161    688    -91       N  
ATOM   2219  CA  GLY A 457       2.248 -11.117  16.662  1.00-1.443           C  
ANISOU 2219  CA  GLY A 457     7406   3245   3561    111    685    -82       C  
ATOM   2220  C   GLY A 457       1.947  -9.659  16.408  1.00-1.443           C  
ANISOU 2220  C   GLY A 457     7640   3567   3842    112    688    -71       C  
ATOM   2221  O   GLY A 457       2.630  -8.770  16.926  1.00-1.443           O  
ANISOU 2221  O   GLY A 457     7516   3467   3741    137    693    -70       O  
ATOM   2222  N   ASP A 458       0.914  -9.424  15.580  1.00-0.516           N  
ANISOU 2222  N   ASP A 458     7095   3065   3304     82    679    -61       N  
ATOM   2223  CA  ASP A 458       0.368  -8.091  15.340  1.00-0.516           C  
ANISOU 2223  CA  ASP A 458     7186   3225   3427     94    680    -41       C  
ATOM   2224  C   ASP A 458      -1.110  -8.136  15.779  1.00-0.516           C  
ANISOU 2224  C   ASP A 458     7421   3530   3700     77    676    -12       C  
ATOM   2225  O   ASP A 458      -1.847  -9.028  15.339  1.00-0.516           O  
ANISOU 2225  O   ASP A 458     6991   3122   3268     31    658    -11       O  
ATOM   2226  CB  ASP A 458       0.572  -7.604  13.880  1.00-0.516           C  
ANISOU 2226  CB  ASP A 458     7467   3519   3684     90    673    -46       C  
ATOM   2227  CG  ASP A 458      -0.300  -8.268  12.829  1.00-0.516           C  
ANISOU 2227  CG  ASP A 458     8236   4312   4429     50    648    -47       C  
ATOM   2228  OD1 ASP A 458      -0.150  -9.493  12.618  1.00-0.516           O  
ANISOU 2228  OD1 ASP A 458     8214   4232   4365     20    642    -72       O  
ATOM   2229  OD2 ASP A 458      -1.143  -7.572  12.242  1.00-0.516           O  
ANISOU 2229  OD2 ASP A 458     7680   3826   3885     51    630    -22       O  
ATOM   2230  N   THR A 459      -1.523  -7.206  16.654  1.00-1.032           N  
ANISOU 2230  N   THR A 459     6982   3126   3290    112    693      8       N  
ATOM   2231  CA  THR A 459      -2.892  -7.132  17.195  1.00-1.032           C  
ANISOU 2231  CA  THR A 459     6960   3197   3318    112    703     38       C  
ATOM   2232  C   THR A 459      -3.911  -7.110  16.035  1.00-1.032           C  
ANISOU 2232  C   THR A 459     7448   3793   3846     92    675     57       C  
ATOM   2233  O   THR A 459      -3.886  -6.220  15.200  1.00-1.032           O  
ANISOU 2233  O   THR A 459     7021   3383   3414    125    664     66       O  
ATOM   2234  CB  THR A 459      -3.025  -6.005  18.213  1.00-1.032           C  
ANISOU 2234  CB  THR A 459     7602   3837   3961    170    735     50       C  
ATOM   2235  OG1 THR A 459      -1.952  -6.095  19.157  1.00-1.032           O  
ANISOU 2235  OG1 THR A 459     7584   3719   3891    176    745     28       O  
ATOM   2236  CG2 THR A 459      -4.356  -6.047  18.962  1.00-1.032           C  
ANISOU 2236  CG2 THR A 459     6882   3221   3293    180    760     80       C  
ATOM   2237  N   SER A 460      -4.753  -8.147  15.962  1.00-1.474           N  
ANISOU 2237  N   SER A 460     7170   3582   3598     30    660     64       N  
ATOM   2238  CA  SER A 460      -5.674  -8.310  14.852  1.00-1.474           C  
ANISOU 2238  CA  SER A 460     7049   3576   3512    -10    621     77       C  
ATOM   2239  C   SER A 460      -7.161  -8.140  15.219  1.00-1.474           C  
ANISOU 2239  C   SER A 460     7637   4359   4207    -15    622    119       C  
ATOM   2240  O   SER A 460      -7.802  -7.238  14.674  1.00-1.474           O  
ANISOU 2240  O   SER A 460     7362   4205   3983     35    607    148       O  
ATOM   2241  CB  SER A 460      -5.419  -9.652  14.174  1.00-1.474           C  
ANISOU 2241  CB  SER A 460     7142   3591   3541    -95    592     46       C  
ATOM   2242  OG  SER A 460      -6.354  -9.899  13.137  1.00-1.474           O  
ANISOU 2242  OG  SER A 460     7845   4406   4264   -151    545     54       O  
ATOM   2243  N   TRP A 461      -7.724  -9.038  16.066  1.00-0.956           N  
ANISOU 2243  N   TRP A 461     7450   4210   4053    -76    641    126       N  
ATOM   2244  CA  TRP A 461      -9.159  -9.015  16.418  1.00-0.956           C  
ANISOU 2244  CA  TRP A 461     7367   4347   4089    -96    649    168       C  
ATOM   2245  C   TRP A 461      -9.515  -9.735  17.731  1.00-0.956           C  
ANISOU 2245  C   TRP A 461     7773   4757   4511   -141    698    180       C  
ATOM   2246  O   TRP A 461      -8.647 -10.328  18.381  1.00-0.956           O  
ANISOU 2246  O   TRP A 461     7701   4500   4345   -157    719    158       O  
ATOM   2247  CB  TRP A 461     -10.017  -9.577  15.252  1.00-0.956           C  
ANISOU 2247  CB  TRP A 461     7121   4244   3890   -183    586    175       C  
ATOM   2248  CG  TRP A 461      -9.791 -11.035  14.965  1.00-0.956           C  
ANISOU 2248  CG  TRP A 461     7345   4350   4035   -311    561    142       C  
ATOM   2249  CD1 TRP A 461      -8.807 -11.573  14.192  1.00-0.956           C  
ANISOU 2249  CD1 TRP A 461     7822   4629   4384   -336    535     96       C  
ATOM   2250  CD2 TRP A 461     -10.604 -12.132  15.399  1.00-0.956           C  
ANISOU 2250  CD2 TRP A 461     7443   4507   4164   -432    565    152       C  
ATOM   2251  NE1 TRP A 461      -8.957 -12.936  14.109  1.00-0.956           N  
ANISOU 2251  NE1 TRP A 461     7791   4509   4289   -456    520     74       N  
ATOM   2252  CE2 TRP A 461     -10.036 -13.311  14.863  1.00-0.956           C  
ANISOU 2252  CE2 TRP A 461     7965   4826   4554   -525    537    109       C  
ATOM   2253  CE3 TRP A 461     -11.720 -12.247  16.251  1.00-0.956           C  
ANISOU 2253  CE3 TRP A 461     7564   4822   4404   -471    597    195       C  
ATOM   2254  CZ2 TRP A 461     -10.565 -14.578  15.118  1.00-0.956           C  
ANISOU 2254  CZ2 TRP A 461     7911   4733   4470   -663    535    106       C  
ATOM   2255  CZ3 TRP A 461     -12.236 -13.506  16.508  1.00-0.956           C  
ANISOU 2255  CZ3 TRP A 461     7763   5009   4588   -617    597    196       C  
ATOM   2256  CH2 TRP A 461     -11.688 -14.648  15.911  1.00-0.956           C  
ANISOU 2256  CH2 TRP A 461     7985   5006   4666   -717    562    152       C  
ATOM   2257  N   GLY A 462     -10.811  -9.685  18.063  1.00-1.344           N  
ANISOU 2257  N   GLY A 462     7422   4632   4281   -160    716    220       N  
ATOM   2258  CA  GLY A 462     -11.444 -10.305  19.223  1.00-1.344           C  
ANISOU 2258  CA  GLY A 462     7453   4724   4347   -213    770    244       C  
ATOM   2259  C   GLY A 462     -12.876  -9.824  19.402  1.00-1.344           C  
ANISOU 2259  C   GLY A 462     8349   5930   5410   -196    794    293       C  
ATOM   2260  O   GLY A 462     -13.223  -8.753  18.887  1.00-1.344           O  
ANISOU 2260  O   GLY A 462     8510   6223   5643    -98    780    309       O  
ATOM   2261  N   SER A 463     -13.733 -10.610  20.125  1.00 1.696           N  
ANISOU 2261  N   SER A 463     7948   5654   5071   -289    833    322       N  
ATOM   2262  CA  SER A 463     -15.122 -10.213  20.431  1.00 1.696           C  
ANISOU 2262  CA  SER A 463     7697   5738   5000   -274    870    373       C  
ATOM   2263  C   SER A 463     -15.045  -9.390  21.705  1.00 1.696           C  
ANISOU 2263  C   SER A 463     8060   6073   5341   -147    963    384       C  
ATOM   2264  O   SER A 463     -14.604  -9.905  22.741  1.00 1.696           O  
ANISOU 2264  O   SER A 463     7912   5762   5089   -179   1014    377       O  
ATOM   2265  CB  SER A 463     -16.028 -11.417  20.671  1.00 1.696           C  
ANISOU 2265  CB  SER A 463     8196   6381   5569   -444    880    399       C  
ATOM   2266  OG  SER A 463     -15.934 -12.425  19.679  1.00 1.696           O  
ANISOU 2266  OG  SER A 463     9919   8055   7259   -587    798    377       O  
ATOM   2267  N   GLY A 464     -15.411  -8.110  21.603  1.00-0.578           N  
ANISOU 2267  N   GLY A 464     7590   5732   4944      0    981    400       N  
ATOM   2268  CA  GLY A 464     -15.333  -7.163  22.709  1.00-0.578           C  
ANISOU 2268  CA  GLY A 464     7755   5846   5065    136   1067    402       C  
ATOM   2269  C   GLY A 464     -13.900  -7.010  23.174  1.00-0.578           C  
ANISOU 2269  C   GLY A 464     8561   6302   5672    166   1069    354       C  
ATOM   2270  O   GLY A 464     -12.970  -7.312  22.416  1.00-0.578           O  
ANISOU 2270  O   GLY A 464     8619   6186   5651    124   1000    322       O  
ATOM   2271  N   CYS A 465     -13.712  -6.596  24.432  1.00-1.441           N  
ANISOU 2271  N   CYS A 465     8132   5777   5157    233   1146    348       N  
ATOM   2272  CA  CYS A 465     -12.392  -6.380  25.035  1.00-1.441           C  
ANISOU 2272  CA  CYS A 465     8273   5613   5112    263   1147    304       C  
ATOM   2273  C   CYS A 465     -12.400  -6.939  26.454  1.00-1.441           C  
ANISOU 2273  C   CYS A 465     8694   5972   5447    230   1217    310       C  
ATOM   2274  O   CYS A 465     -13.336  -6.640  27.202  1.00-1.441           O  
ANISOU 2274  O   CYS A 465     8509   5941   5313    274   1297    338       O  
ATOM   2275  CB  CYS A 465     -12.056  -4.888  25.055  1.00-1.441           C  
ANISOU 2275  CB  CYS A 465     8382   5631   5163    408   1163    283       C  
ATOM   2276  SG  CYS A 465     -11.878  -4.127  23.421  1.00-1.441           S  
ANISOU 2276  SG  CYS A 465     8899   6162   5734    455   1084    280       S  
ATOM   2277  N   ALA A 466     -11.348  -7.709  26.839  1.00-0.742           N  
ANISOU 2277  N   ALA A 466     8266   5321   4882    164   1189    287       N  
ATOM   2278  CA  ALA A 466     -11.129  -8.270  28.202  1.00-0.742           C  
ANISOU 2278  CA  ALA A 466     8278   5222   4769    135   1242    294       C  
ATOM   2279  C   ALA A 466     -12.295  -9.104  28.788  1.00-0.742           C  
ANISOU 2279  C   ALA A 466     8392   5508   4951     54   1308    345       C  
ATOM   2280  O   ALA A 466     -12.389  -9.253  30.014  1.00-0.742           O  
ANISOU 2280  O   ALA A 466     8396   5463   4856     59   1376    359       O  
ATOM   2281  CB  ALA A 466     -10.742  -7.155  29.166  1.00-0.742           C  
ANISOU 2281  CB  ALA A 466     8418   5251   4789    250   1289    268       C  
ATOM   2282  N   LYS A 467     -13.166  -9.646  27.912  1.00 0.384           N  
ANISOU 2282  N   LYS A 467     7820   5140   4538    -28   1286    373       N  
ATOM   2283  CA  LYS A 467     -14.311 -10.481  28.282  1.00 0.384           C  
ANISOU 2283  CA  LYS A 467     7730   5244   4537   -133   1341    423       C  
ATOM   2284  C   LYS A 467     -13.835 -11.901  28.469  1.00 0.384           C  
ANISOU 2284  C   LYS A 467     8375   5702   5069   -272   1316    431       C  
ATOM   2285  O   LYS A 467     -12.921 -12.331  27.761  1.00 0.384           O  
ANISOU 2285  O   LYS A 467     8468   5606   5092   -301   1237    400       O  
ATOM   2286  CB  LYS A 467     -15.370 -10.477  27.170  1.00 0.384           C  
ANISOU 2286  CB  LYS A 467     7888   5704   4913   -176   1310    447       C  
ATOM   2287  CG  LYS A 467     -16.721  -9.948  27.607  1.00 0.384           C  
ANISOU 2287  CG  LYS A 467    10162   8309   7349   -127   1397    491       C  
ATOM   2288  CD  LYS A 467     -16.817  -8.454  27.403  1.00 0.384           C  
ANISOU 2288  CD  LYS A 467    11193   9413   8428     58   1409    477       C  
ATOM   2289  CE  LYS A 467     -17.821  -7.801  28.320  1.00 0.384           C  
ANISOU 2289  CE  LYS A 467    12671  11122   9991    156   1524    510       C  
ATOM   2290  NZ  LYS A 467     -17.775  -6.315  28.214  1.00 0.384           N  
ANISOU 2290  NZ  LYS A 467    13068  11504  10380    354   1542    490       N  
ATOM   2291  N   ALA A 468     -14.455 -12.629  29.417  1.00 0.528           N  
ANISOU 2291  N   ALA A 468     7859   5228   4526   -355   1390    475       N  
ATOM   2292  CA  ALA A 468     -14.157 -14.034  29.701  1.00 0.528           C  
ANISOU 2292  CA  ALA A 468     7854   5032   4397   -493   1380    495       C  
ATOM   2293  C   ALA A 468     -14.422 -14.884  28.442  1.00 0.528           C  
ANISOU 2293  C   ALA A 468     8370   5584   4997   -625   1306    491       C  
ATOM   2294  O   ALA A 468     -15.404 -14.637  27.723  1.00 0.528           O  
ANISOU 2294  O   ALA A 468     8072   5569   4888   -661   1297    503       O  
ATOM   2295  CB  ALA A 468     -15.011 -14.520  30.872  1.00 0.528           C  
ANISOU 2295  CB  ALA A 468     7840   5106   4362   -564   1486    552       C  
ATOM   2296  N   TYR A 469     -13.497 -15.822  28.133  1.00-0.088           N  
ANISOU 2296  N   TYR A 469     8086   5010   4564   -684   1246    471       N  
ATOM   2297  CA  TYR A 469     -13.569 -16.751  26.990  1.00-0.088           C  
ANISOU 2297  CA  TYR A 469     8059   4931   4552   -811   1176    456       C  
ATOM   2298  C   TYR A 469     -13.543 -16.045  25.600  1.00-0.088           C  
ANISOU 2298  C   TYR A 469     8291   5296   4911   -764   1099    414       C  
ATOM   2299  O   TYR A 469     -13.802 -16.680  24.581  1.00-0.088           O  
ANISOU 2299  O   TYR A 469     8081   5098   4731   -871   1041    401       O  
ATOM   2300  CB  TYR A 469     -14.786 -17.700  27.141  1.00-0.088           C  
ANISOU 2300  CB  TYR A 469     8171   5178   4723   -996   1215    505       C  
ATOM   2301  CG  TYR A 469     -14.663 -18.611  28.340  1.00-0.088           C  
ANISOU 2301  CG  TYR A 469     8649   5447   5028  -1064   1281    547       C  
ATOM   2302  CD1 TYR A 469     -13.928 -19.789  28.270  1.00-0.088           C  
ANISOU 2302  CD1 TYR A 469     9148   5596   5329  -1137   1246    541       C  
ATOM   2303  CD2 TYR A 469     -15.230 -18.267  29.564  1.00-0.088           C  
ANISOU 2303  CD2 TYR A 469     8736   5664   5129  -1039   1380    594       C  
ATOM   2304  CE1 TYR A 469     -13.786 -20.620  29.381  1.00-0.088           C  
ANISOU 2304  CE1 TYR A 469     9451   5683   5451  -1190   1304    588       C  
ATOM   2305  CE2 TYR A 469     -15.088 -19.086  30.682  1.00-0.088           C  
ANISOU 2305  CE2 TYR A 469     9083   5804   5293  -1098   1441    639       C  
ATOM   2306  CZ  TYR A 469     -14.373 -20.268  30.582  1.00-0.088           C  
ANISOU 2306  CZ  TYR A 469    10345   6715   6358  -1175   1400    638       C  
ATOM   2307  OH  TYR A 469     -14.226 -21.090  31.672  1.00-0.088           O  
ANISOU 2307  OH  TYR A 469    11081   7227   6897  -1228   1456    690       O  
ATOM   2308  N   ARG A 470     -13.211 -14.735  25.569  1.00 0.048           N  
ANISOU 2308  N   ARG A 470     7777   4859   4449   -606   1098    394       N  
ATOM   2309  CA  ARG A 470     -13.077 -13.954  24.328  1.00 0.048           C  
ANISOU 2309  CA  ARG A 470     7587   4763   4351   -543   1031    361       C  
ATOM   2310  C   ARG A 470     -11.676 -13.272  24.337  1.00 0.048           C  
ANISOU 2310  C   ARG A 470     7878   4834   4526   -411   1006    318       C  
ATOM   2311  O   ARG A 470     -11.582 -12.056  24.521  1.00 0.048           O  
ANISOU 2311  O   ARG A 470     7765   4792   4451   -288   1025    312       O  
ATOM   2312  CB  ARG A 470     -14.232 -12.924  24.186  1.00 0.048           C  
ANISOU 2312  CB  ARG A 470     7392   4916   4352   -484   1058    389       C  
ATOM   2313  CG  ARG A 470     -15.652 -13.510  24.168  1.00 0.048           C  
ANISOU 2313  CG  ARG A 470     8408   6216   5519   -614   1082    435       C  
ATOM   2314  CD  ARG A 470     -15.923 -14.372  22.953  1.00 0.048           C  
ANISOU 2314  CD  ARG A 470    10285   8122   7429   -761    998    423       C  
ATOM   2315  NE  ARG A 470     -17.241 -15.010  23.006  1.00 0.048           N  
ANISOU 2315  NE  ARG A 470    11197   9304   8480   -912   1018    467       N  
ATOM   2316  CZ  ARG A 470     -17.456 -16.269  23.376  1.00 0.048           C  
ANISOU 2316  CZ  ARG A 470    11984   9987   9192  -1084   1037    482       C  
ATOM   2317  NH1 ARG A 470     -16.444 -17.042  23.747  1.00 0.048           N  
ANISOU 2317  NH1 ARG A 470     9438   7062   6428  -1109   1039    460       N  
ATOM   2318  NH2 ARG A 470     -18.687 -16.760  23.390  1.00 0.048           N  
ANISOU 2318  NH2 ARG A 470    10527   8808   7879  -1231   1055    524       N  
ATOM   2319  N   PRO A 471     -10.564 -14.032  24.207  1.00-1.259           N  
ANISOU 2319  N   PRO A 471     7553   4240   4056   -432    969    290       N  
ATOM   2320  CA  PRO A 471      -9.243 -13.382  24.227  1.00-1.259           C  
ANISOU 2320  CA  PRO A 471     7637   4162   4056   -316    946    253       C  
ATOM   2321  C   PRO A 471      -8.844 -12.665  22.924  1.00-1.259           C  
ANISOU 2321  C   PRO A 471     7942   4502   4414   -267    888    218       C  
ATOM   2322  O   PRO A 471      -9.601 -12.599  21.936  1.00-1.259           O  
ANISOU 2322  O   PRO A 471     7693   4408   4265   -309    859    221       O  
ATOM   2323  CB  PRO A 471      -8.293 -14.537  24.535  1.00-1.259           C  
ANISOU 2323  CB  PRO A 471     8030   4291   4292   -353    931    245       C  
ATOM   2324  CG  PRO A 471      -8.952 -15.742  23.949  1.00-1.259           C  
ANISOU 2324  CG  PRO A 471     8558   4800   4817   -491    915    255       C  
ATOM   2325  CD  PRO A 471     -10.442 -15.492  23.979  1.00-1.259           C  
ANISOU 2325  CD  PRO A 471     7871   4388   4278   -558    947    290       C  
ATOM   2326  N   GLY A 472      -7.621 -12.150  22.934  1.00-1.267           N  
ANISOU 2326  N   GLY A 472     7394   3813   3793   -183    870    186       N  
ATOM   2327  CA  GLY A 472      -7.063 -11.449  21.786  1.00-1.267           C  
ANISOU 2327  CA  GLY A 472     7180   3602   3604   -135    825    155       C  
ATOM   2328  C   GLY A 472      -6.549 -12.409  20.740  1.00-1.267           C  
ANISOU 2328  C   GLY A 472     7630   3941   4004   -195    777    128       C  
ATOM   2329  O   GLY A 472      -6.005 -13.455  21.083  1.00-1.267           O  
ANISOU 2329  O   GLY A 472     7544   3692   3823   -231    776    122       O  
ATOM   2330  N   VAL A 473      -6.730 -12.054  19.456  1.00-1.221           N  
ANISOU 2330  N   VAL A 473     7043   3432   3467   -201    737    114       N  
ATOM   2331  CA  VAL A 473      -6.266 -12.828  18.298  1.00-1.221           C  
ANISOU 2331  CA  VAL A 473     7102   3389   3464   -251    693     81       C  
ATOM   2332  C   VAL A 473      -5.252 -11.934  17.546  1.00-1.221           C  
ANISOU 2332  C   VAL A 473     7307   3556   3653   -169    676     54       C  
ATOM   2333  O   VAL A 473      -5.503 -10.737  17.322  1.00-1.221           O  
ANISOU 2333  O   VAL A 473     7037   3400   3446   -112    676     66       O  
ATOM   2334  CB  VAL A 473      -7.419 -13.312  17.383  1.00-1.221           C  
ANISOU 2334  CB  VAL A 473     7377   3787   3788   -351    659     88       C  
ATOM   2335  CG1 VAL A 473      -6.899 -14.294  16.334  1.00-1.221           C  
ANISOU 2335  CG1 VAL A 473     7374   3625   3677   -412    620     45       C  
ATOM   2336  CG2 VAL A 473      -8.540 -13.950  18.200  1.00-1.221           C  
ANISOU 2336  CG2 VAL A 473     7170   3672   3630   -439    685    124       C  
ATOM   2337  N   TYR A 474      -4.083 -12.501  17.245  1.00-1.323           N  
ANISOU 2337  N   TYR A 474     7009   3093   3264   -157    667     20       N  
ATOM   2338  CA  TYR A 474      -2.971 -11.762  16.623  1.00-1.323           C  
ANISOU 2338  CA  TYR A 474     7082   3131   3320    -89    661     -4       C  
ATOM   2339  C   TYR A 474      -2.517 -12.451  15.359  1.00-1.323           C  
ANISOU 2339  C   TYR A 474     7659   3626   3828   -117    637    -39       C  
ATOM   2340  O   TYR A 474      -2.551 -13.679  15.309  1.00-1.323           O  
ANISOU 2340  O   TYR A 474     7602   3457   3700   -168    633    -54       O  
ATOM   2341  CB  TYR A 474      -1.781 -11.700  17.611  1.00-1.323           C  
ANISOU 2341  CB  TYR A 474     7157   3112   3361    -28    682    -11       C  
ATOM   2342  CG  TYR A 474      -2.168 -11.054  18.926  1.00-1.323           C  
ANISOU 2342  CG  TYR A 474     7192   3201   3430     -1    707     17       C  
ATOM   2343  CD1 TYR A 474      -2.797 -11.791  19.934  1.00-1.323           C  
ANISOU 2343  CD1 TYR A 474     7364   3354   3584    -36    726     41       C  
ATOM   2344  CD2 TYR A 474      -1.913  -9.706  19.162  1.00-1.323           C  
ANISOU 2344  CD2 TYR A 474     7070   3129   3339     55    717     18       C  
ATOM   2345  CE1 TYR A 474      -3.224 -11.177  21.119  1.00-1.323           C  
ANISOU 2345  CE1 TYR A 474     7579   3622   3817     -9    757     65       C  
ATOM   2346  CE2 TYR A 474      -2.366  -9.077  20.317  1.00-1.323           C  
ANISOU 2346  CE2 TYR A 474     7089   3182   3368     82    744     38       C  
ATOM   2347  CZ  TYR A 474      -2.996  -9.821  21.304  1.00-1.323           C  
ANISOU 2347  CZ  TYR A 474     7994   4085   4258     54    766     60       C  
ATOM   2348  OH  TYR A 474      -3.423  -9.184  22.430  1.00-1.323           O  
ANISOU 2348  OH  TYR A 474     7626   3749   3885     86    801     76       O  
ATOM   2349  N   GLY A 475      -2.022 -11.683  14.376  1.00-0.813           N  
ANISOU 2349  N   GLY A 475     7422   3416   3590    -82    628    -53       N  
ATOM   2350  CA  GLY A 475      -1.447 -12.296  13.176  1.00-0.813           C  
ANISOU 2350  CA  GLY A 475     7482   3387   3565    -98    616    -91       C  
ATOM   2351  C   GLY A 475      -0.186 -13.049  13.574  1.00-0.813           C  
ANISOU 2351  C   GLY A 475     7885   3650   3909    -57    641   -117       C  
ATOM   2352  O   GLY A 475       0.603 -12.545  14.389  1.00-0.813           O  
ANISOU 2352  O   GLY A 475     7685   3463   3748      1    660   -107       O  
ATOM   2353  N   ASN A 476      -0.016 -14.277  13.070  1.00-0.622           N  
ANISOU 2353  N   ASN A 476     7610   3238   3533    -86    639   -148       N  
ATOM   2354  CA  ASN A 476       1.154 -15.116  13.379  1.00-0.622           C  
ANISOU 2354  CA  ASN A 476     7715   3198   3571    -30    664   -171       C  
ATOM   2355  C   ASN A 476       2.295 -14.619  12.500  1.00-0.622           C  
ANISOU 2355  C   ASN A 476     8027   3535   3880     33    683   -196       C  
ATOM   2356  O   ASN A 476       2.400 -15.028  11.348  1.00-0.622           O  
ANISOU 2356  O   ASN A 476     7898   3342   3666     19    686   -231       O  
ATOM   2357  CB  ASN A 476       0.844 -16.618  13.120  1.00-0.622           C  
ANISOU 2357  CB  ASN A 476     7956   3248   3680    -80    661   -196       C  
ATOM   2358  CG  ASN A 476       1.882 -17.575  13.665  1.00-0.622           C  
ANISOU 2358  CG  ASN A 476     9809   4932   5457     -8    687   -207       C  
ATOM   2359  OD1 ASN A 476       3.009 -17.211  14.029  1.00-0.622           O  
ANISOU 2359  OD1 ASN A 476     9402   4568   5098     86    705   -203       O  
ATOM   2360  ND2 ASN A 476       1.521 -18.833  13.725  1.00-0.622           N  
ANISOU 2360  ND2 ASN A 476     8802   3728   4325    -52    687   -220       N  
ATOM   2361  N   VAL A 477       3.097 -13.665  13.019  1.00-0.981           N  
ANISOU 2361  N   VAL A 477     7662   3271   3603     90    697   -180       N  
ATOM   2362  CA  VAL A 477       4.166 -12.968  12.276  1.00-0.981           C  
ANISOU 2362  CA  VAL A 477     7617   3288   3580    134    720   -194       C  
ATOM   2363  C   VAL A 477       5.211 -13.959  11.681  1.00-0.981           C  
ANISOU 2363  C   VAL A 477     8287   3864   4177    187    751   -232       C  
ATOM   2364  O   VAL A 477       5.691 -13.750  10.552  1.00-0.981           O  
ANISOU 2364  O   VAL A 477     8033   3627   3889    198    775   -256       O  
ATOM   2365  CB  VAL A 477       4.790 -11.823  13.136  1.00-0.981           C  
ANISOU 2365  CB  VAL A 477     7996   3782   4063    165    725   -169       C  
ATOM   2366  CG1 VAL A 477       6.025 -11.222  12.464  1.00-0.981           C  
ANISOU 2366  CG1 VAL A 477     7974   3830   4070    198    754   -182       C  
ATOM   2367  CG2 VAL A 477       3.761 -10.716  13.368  1.00-0.981           C  
ANISOU 2367  CG2 VAL A 477     7874   3732   3985    125    706   -139       C  
ATOM   2368  N   MET A 478       5.479 -15.059  12.386  1.00-0.560           N  
ANISOU 2368  N   MET A 478     8329   3793   4177    224    754   -237       N  
ATOM   2369  CA  MET A 478       6.412 -16.090  11.928  1.00-0.560           C  
ANISOU 2369  CA  MET A 478     8745   4097   4513    295    787   -271       C  
ATOM   2370  C   MET A 478       6.027 -16.654  10.560  1.00-0.560           C  
ANISOU 2370  C   MET A 478     8854   4088   4487    260    800   -315       C  
ATOM   2371  O   MET A 478       6.909 -16.972   9.767  1.00-0.560           O  
ANISOU 2371  O   MET A 478     8774   3974   4354    321    841   -349       O  
ATOM   2372  CB  MET A 478       6.519 -17.232  12.934  1.00-0.560           C  
ANISOU 2372  CB  MET A 478     9336   4542   5049    337    783   -261       C  
ATOM   2373  CG  MET A 478       7.906 -17.772  13.025  1.00-0.560           C  
ANISOU 2373  CG  MET A 478    10352   5545   6068    459    815   -271       C  
ATOM   2374  SD  MET A 478       7.919 -19.510  13.511  1.00-0.560           S  
ANISOU 2374  SD  MET A 478    11739   6648   7294    517    822   -275       S  
ATOM   2375  CE  MET A 478       8.606 -19.372  15.073  1.00-0.560           C  
ANISOU 2375  CE  MET A 478    11244   6248   6899    593    798   -222       C  
ATOM   2376  N   VAL A 479       4.714 -16.763  10.298  1.00 0.574           N  
ANISOU 2376  N   VAL A 479     8368   3552   3946    160    764   -315       N  
ATOM   2377  CA  VAL A 479       4.144 -17.277   9.049  1.00 0.574           C  
ANISOU 2377  CA  VAL A 479     8554   3629   3992    101    757   -357       C  
ATOM   2378  C   VAL A 479       4.367 -16.279   7.889  1.00 0.574           C  
ANISOU 2378  C   VAL A 479     8740   3939   4190     98    768   -365       C  
ATOM   2379  O   VAL A 479       4.525 -16.698   6.746  1.00 0.574           O  
ANISOU 2379  O   VAL A 479     8966   4074   4285     95    785   -409       O  
ATOM   2380  CB  VAL A 479       2.638 -17.644   9.255  1.00 0.574           C  
ANISOU 2380  CB  VAL A 479     9313   4344   4718    -17    706   -346       C  
ATOM   2381  CG1 VAL A 479       1.966 -18.075   7.949  1.00 0.574           C  
ANISOU 2381  CG1 VAL A 479     9477   4423   4740    -99    683   -389       C  
ATOM   2382  CG2 VAL A 479       2.478 -18.748  10.307  1.00 0.574           C  
ANISOU 2382  CG2 VAL A 479     9403   4272   4760    -23    707   -337       C  
ATOM   2383  N   PHE A 480       4.452 -14.983   8.208  1.00-0.027           N  
ANISOU 2383  N   PHE A 480     8151   3535   3740    105    762   -324       N  
ATOM   2384  CA  PHE A 480       4.581 -13.868   7.283  1.00-0.027           C  
ANISOU 2384  CA  PHE A 480     8170   3668   3775     96    770   -315       C  
ATOM   2385  C   PHE A 480       6.010 -13.325   7.022  1.00-0.027           C  
ANISOU 2385  C   PHE A 480     8490   4066   4142    167    828   -318       C  
ATOM   2386  O   PHE A 480       6.158 -12.502   6.127  1.00-0.027           O  
ANISOU 2386  O   PHE A 480     8221   3861   3855    153    843   -312       O  
ATOM   2387  CB  PHE A 480       3.688 -12.713   7.768  1.00-0.027           C  
ANISOU 2387  CB  PHE A 480     8375   4004   4086     55    729   -264       C  
ATOM   2388  CG  PHE A 480       2.274 -13.052   8.196  1.00-0.027           C  
ANISOU 2388  CG  PHE A 480     8671   4293   4386    -13    677   -249       C  
ATOM   2389  CD1 PHE A 480       1.441 -13.806   7.375  1.00-0.027           C  
ANISOU 2389  CD1 PHE A 480     9171   4720   4776    -80    645   -275       C  
ATOM   2390  CD2 PHE A 480       1.729 -12.491   9.347  1.00-0.027           C  
ANISOU 2390  CD2 PHE A 480     9031   4739   4861    -16    661   -207       C  
ATOM   2391  CE1 PHE A 480       0.119 -14.067   7.746  1.00-0.027           C  
ANISOU 2391  CE1 PHE A 480     9264   4846   4894   -155    596   -256       C  
ATOM   2392  CE2 PHE A 480       0.402 -12.742   9.708  1.00-0.027           C  
ANISOU 2392  CE2 PHE A 480     9349   5086   5199    -78    621   -188       C  
ATOM   2393  CZ  PHE A 480      -0.386 -13.542   8.912  1.00-0.027           C  
ANISOU 2393  CZ  PHE A 480     9092   4779   4853   -151    589   -210       C  
ATOM   2394  N   THR A 481       7.036 -13.778   7.775  1.00 0.424           N  
ANISOU 2394  N   THR A 481     8097   3676   3807    240    859   -323       N  
ATOM   2395  CA  THR A 481       8.422 -13.293   7.710  1.00 0.424           C  
ANISOU 2395  CA  THR A 481     8074   3773   3865    302    910   -321       C  
ATOM   2396  C   THR A 481       9.035 -13.372   6.289  1.00 0.424           C  
ANISOU 2396  C   THR A 481     9156   4846   4854    323    968   -354       C  
ATOM   2397  O   THR A 481       9.748 -12.452   5.892  1.00 0.424           O  
ANISOU 2397  O   THR A 481     9245   5067   5005    324   1004   -338       O  
ATOM   2398  CB  THR A 481       9.290 -13.989   8.794  1.00 0.424           C  
ANISOU 2398  CB  THR A 481     9344   5051   5207    384    920   -319       C  
ATOM   2399  OG1 THR A 481       8.782 -13.671  10.105  1.00 0.424           O  
ANISOU 2399  OG1 THR A 481     8688   4424   4631    358    871   -283       O  
ATOM   2400  CG2 THR A 481      10.731 -13.543   8.776  1.00 0.424           C  
ANISOU 2400  CG2 THR A 481     9288   5160   5258    445    967   -315       C  
ATOM   2401  N   ASP A 482       8.771 -14.437   5.525  1.00 0.187           N  
ANISOU 2401  N   ASP A 482     9211   4737   4750    332    980   -400       N  
ATOM   2402  CA  ASP A 482       9.388 -14.534   4.211  1.00 0.187           C  
ANISOU 2402  CA  ASP A 482     9173   4682   4605    359   1042   -435       C  
ATOM   2403  C   ASP A 482       8.663 -13.638   3.203  1.00 0.187           C  
ANISOU 2403  C   ASP A 482     9144   4679   4505    276   1022   -422       C  
ATOM   2404  O   ASP A 482       9.341 -13.002   2.394  1.00 0.187           O  
ANISOU 2404  O   ASP A 482     8926   4543   4274    285   1075   -418       O  
ATOM   2405  CB  ASP A 482       9.583 -15.969   3.757  1.00 0.187           C  
ANISOU 2405  CB  ASP A 482     9751   5061   5020    417   1075   -495       C  
ATOM   2406  CG  ASP A 482      11.020 -16.157   3.297  1.00 0.187           C  
ANISOU 2406  CG  ASP A 482    11992   7369   7276    525   1169   -518       C  
ATOM   2407  OD1 ASP A 482      11.327 -15.794   2.128  1.00 0.187           O  
ANISOU 2407  OD1 ASP A 482    11784   7189   6985    519   1221   -536       O  
ATOM   2408  OD2 ASP A 482      11.856 -16.596   4.124  1.00 0.187           O  
ANISOU 2408  OD2 ASP A 482    13066   8493   8454    618   1191   -510       O  
ATOM   2409  N   TRP A 483       7.323 -13.447   3.363  1.00-1.368           N  
ANISOU 2409  N   TRP A 483     8467   3964   3805    196    945   -403       N  
ATOM   2410  CA  TRP A 483       6.581 -12.469   2.574  1.00-1.368           C  
ANISOU 2410  CA  TRP A 483     8419   3967   3715    130    913   -375       C  
ATOM   2411  C   TRP A 483       7.148 -11.051   2.887  1.00-1.368           C  
ANISOU 2411  C   TRP A 483     8496   4204   3930    136    935   -321       C  
ATOM   2412  O   TRP A 483       7.400 -10.293   1.964  1.00-1.368           O  
ANISOU 2412  O   TRP A 483     8548   4293   3927    121    963   -306       O  
ATOM   2413  CB  TRP A 483       5.067 -12.519   2.868  1.00-1.368           C  
ANISOU 2413  CB  TRP A 483     8349   3874   3639     58    826   -358       C  
ATOM   2414  CG  TRP A 483       4.317 -11.379   2.225  1.00-1.368           C  
ANISOU 2414  CG  TRP A 483     8438   4046   3715     12    787   -314       C  
ATOM   2415  CD1 TRP A 483       3.978 -11.268   0.906  1.00-1.368           C  
ANISOU 2415  CD1 TRP A 483     8848   4423   3971    -20    774   -324       C  
ATOM   2416  CD2 TRP A 483       3.875 -10.170   2.856  1.00-1.368           C  
ANISOU 2416  CD2 TRP A 483     8398   4120   3802      5    758   -252       C  
ATOM   2417  NE1 TRP A 483       3.350 -10.068   0.677  1.00-1.368           N  
ANISOU 2417  NE1 TRP A 483     8783   4452   3938    -41    736   -265       N  
ATOM   2418  CE2 TRP A 483       3.261  -9.377   1.859  1.00-1.368           C  
ANISOU 2418  CE2 TRP A 483     8906   4658   4232    -23    728   -222       C  
ATOM   2419  CE3 TRP A 483       3.913  -9.684   4.176  1.00-1.368           C  
ANISOU 2419  CE3 TRP A 483     8531   4321   4093     24    754   -220       C  
ATOM   2420  CZ2 TRP A 483       2.689  -8.129   2.138  1.00-1.368           C  
ANISOU 2420  CZ2 TRP A 483     8824   4660   4225    -23    699   -158       C  
ATOM   2421  CZ3 TRP A 483       3.347  -8.448   4.449  1.00-1.368           C  
ANISOU 2421  CZ3 TRP A 483     8681   4548   4310     17    728   -165       C  
ATOM   2422  CH2 TRP A 483       2.748  -7.683   3.437  1.00-1.368           C  
ANISOU 2422  CH2 TRP A 483     8805   4690   4356     -1    703   -134       C  
ATOM   2423  N   ILE A 484       7.402 -10.727   4.176  1.00-1.354           N  
ANISOU 2423  N   ILE A 484     7776   3559   3368    154    925   -294       N  
ATOM   2424  CA  ILE A 484       7.992  -9.429   4.580  1.00-1.354           C  
ANISOU 2424  CA  ILE A 484     7582   3491   3292    148    944   -251       C  
ATOM   2425  C   ILE A 484       9.354  -9.216   3.883  1.00-1.354           C  
ANISOU 2425  C   ILE A 484     8132   4113   3843    174   1025   -261       C  
ATOM   2426  O   ILE A 484       9.581  -8.149   3.300  1.00-1.354           O  
ANISOU 2426  O   ILE A 484     8041   4072   3740    138   1049   -230       O  
ATOM   2427  CB  ILE A 484       8.113  -9.317   6.135  1.00-1.354           C  
ANISOU 2427  CB  ILE A 484     7759   3721   3616    163    918   -233       C  
ATOM   2428  CG1 ILE A 484       6.714  -9.245   6.800  1.00-1.354           C  
ANISOU 2428  CG1 ILE A 484     7718   3636   3581    130    851   -212       C  
ATOM   2429  CG2 ILE A 484       8.990  -8.108   6.554  1.00-1.354           C  
ANISOU 2429  CG2 ILE A 484     7561   3639   3525    151    943   -202       C  
ATOM   2430  CD1 ILE A 484       6.717  -9.477   8.400  1.00-1.354           C  
ANISOU 2430  CD1 ILE A 484     7564   3500   3534    150    827   -203       C  
ATOM   2431  N   TYR A 485      10.257 -10.214   3.967  1.00 0.727           N  
ANISOU 2431  N   TYR A 485     7846   3833   3572    239   1070   -299       N  
ATOM   2432  CA  TYR A 485      11.590 -10.145   3.335  1.00 0.727           C  
ANISOU 2432  CA  TYR A 485     8113   4201   3859    277   1157   -310       C  
ATOM   2433  C   TYR A 485      11.511  -9.800   1.866  1.00 0.727           C  
ANISOU 2433  C   TYR A 485     8643   4693   4239    246   1199   -315       C  
ATOM   2434  O   TYR A 485      12.294  -8.982   1.399  1.00 0.727           O  
ANISOU 2434  O   TYR A 485     8520   4680   4149    226   1257   -291       O  
ATOM   2435  CB  TYR A 485      12.341 -11.484   3.476  1.00 0.727           C  
ANISOU 2435  CB  TYR A 485     8445   4510   4190    376   1198   -356       C  
ATOM   2436  CG  TYR A 485      12.788 -11.818   4.884  1.00 0.727           C  
ANISOU 2436  CG  TYR A 485     8828   4964   4727    425   1171   -346       C  
ATOM   2437  CD1 TYR A 485      13.190 -10.818   5.770  1.00 0.727           C  
ANISOU 2437  CD1 TYR A 485     8939   5234   5001    389   1149   -304       C  
ATOM   2438  CD2 TYR A 485      12.899 -13.140   5.302  1.00 0.727           C  
ANISOU 2438  CD2 TYR A 485     9176   5211   5040    510   1170   -377       C  
ATOM   2439  CE1 TYR A 485      13.652 -11.126   7.049  1.00 0.727           C  
ANISOU 2439  CE1 TYR A 485     8950   5318   5139    435   1120   -294       C  
ATOM   2440  CE2 TYR A 485      13.344 -13.458   6.584  1.00 0.727           C  
ANISOU 2440  CE2 TYR A 485     9343   5441   5334    564   1143   -360       C  
ATOM   2441  CZ  TYR A 485      13.735 -12.450   7.448  1.00 0.727           C  
ANISOU 2441  CZ  TYR A 485    10102   6379   6258    527   1116   -319       C  
ATOM   2442  OH  TYR A 485      14.158 -12.781   8.712  1.00 0.727           O  
ANISOU 2442  OH  TYR A 485    10630   6969   6894    578   1081   -303       O  
ATOM   2443  N   ARG A 486      10.576 -10.431   1.137  1.00 0.452           N  
ANISOU 2443  N   ARG A 486     8659   4554   4083    234   1169   -344       N  
ATOM   2444  CA  ARG A 486      10.384 -10.236  -0.311  1.00 0.452           C  
ANISOU 2444  CA  ARG A 486     8749   4585   3991    206   1198   -352       C  
ATOM   2445  C   ARG A 486       9.887  -8.818  -0.652  1.00 0.452           C  
ANISOU 2445  C   ARG A 486     9252   5129   4485    134   1170   -290       C  
ATOM   2446  O   ARG A 486      10.323  -8.232  -1.653  1.00 0.452           O  
ANISOU 2446  O   ARG A 486     9166   5063   4309    116   1225   -274       O  
ATOM   2447  CB  ARG A 486       9.434 -11.309  -0.866  1.00 0.452           C  
ANISOU 2447  CB  ARG A 486     9092   4748   4149    199   1154   -402       C  
ATOM   2448  N   GLN A 487       8.998  -8.252   0.190  1.00 0.115           N  
ANISOU 2448  N   GLN A 487     8792   4674   4108    101   1092   -251       N  
ATOM   2449  CA  GLN A 487       8.497  -6.886  -0.037  1.00 0.115           C  
ANISOU 2449  CA  GLN A 487     8760   4658   4063     51   1065   -188       C  
ATOM   2450  C   GLN A 487       9.609  -5.872   0.191  1.00 0.115           C  
ANISOU 2450  C   GLN A 487     9164   5160   4565     35   1129   -154       C  
ATOM   2451  O   GLN A 487       9.717  -4.896  -0.560  1.00 0.115           O  
ANISOU 2451  O   GLN A 487     9207   5192   4528     -3   1156   -112       O  
ATOM   2452  CB  GLN A 487       7.296  -6.558   0.879  1.00 0.115           C  
ANISOU 2452  CB  GLN A 487     8813   4699   4189     36    975   -159       C  
ATOM   2453  CG  GLN A 487       6.119  -7.536   0.798  1.00 0.115           C  
ANISOU 2453  CG  GLN A 487     9386   5204   4696     32    906   -188       C  
ATOM   2454  CD  GLN A 487       5.700  -7.917  -0.605  1.00 0.115           C  
ANISOU 2454  CD  GLN A 487    11900   7646   7014     12    896   -208       C  
ATOM   2455  OE1 GLN A 487       5.126  -7.119  -1.356  1.00 0.115           O  
ANISOU 2455  OE1 GLN A 487    10366   6111   5392    -12    867   -167       O  
ATOM   2456  NE2 GLN A 487       5.980  -9.157  -0.981  1.00 0.115           N  
ANISOU 2456  NE2 GLN A 487    11375   7047   6401     25    919   -273       N  
ATOM   2457  N   MET A 488      10.455  -6.120   1.208  1.00-0.567           N  
ANISOU 2457  N   MET A 488     8409   4499   3972     59   1152   -169       N  
ATOM   2458  CA  MET A 488      11.576  -5.234   1.522  1.00-0.567           C  
ANISOU 2458  CA  MET A 488     8316   4525   3992     29   1206   -141       C  
ATOM   2459  C   MET A 488      12.625  -5.303   0.420  1.00-0.567           C  
ANISOU 2459  C   MET A 488     9016   5290   4635     30   1304   -151       C  
ATOM   2460  O   MET A 488      13.182  -4.276   0.024  1.00-0.567           O  
ANISOU 2460  O   MET A 488     9020   5344   4637    -29   1352   -111       O  
ATOM   2461  CB  MET A 488      12.186  -5.589   2.879  1.00-0.567           C  
ANISOU 2461  CB  MET A 488     8411   4722   4269     57   1193   -158       C  
ATOM   2462  CG  MET A 488      11.264  -5.315   4.060  1.00-0.567           C  
ANISOU 2462  CG  MET A 488     8759   5016   4674     47   1110   -142       C  
ATOM   2463  SD  MET A 488      12.205  -5.206   5.612  1.00-0.567           S  
ANISOU 2463  SD  MET A 488     9029   5421   5141     51   1100   -145       S  
ATOM   2464  CE  MET A 488      12.792  -6.879   5.756  1.00-0.567           C  
ANISOU 2464  CE  MET A 488     8436   4875   4587    149   1119   -194       C  
ATOM   2465  N   ARG A 489      12.852  -6.506  -0.114  1.00-0.087           N  
ANISOU 2465  N   ARG A 489     8845   5104   4400     94   1338   -203       N  
ATOM   2466  CA  ARG A 489      13.792  -6.717  -1.227  1.00-0.087           C  
ANISOU 2466  CA  ARG A 489     8869   5184   4348    112   1443   -220       C  
ATOM   2467  C   ARG A 489      13.265  -6.061  -2.516  1.00-0.087           C  
ANISOU 2467  C   ARG A 489     9610   5822   4884     59   1456   -191       C  
ATOM   2468  O   ARG A 489      14.034  -5.397  -3.211  1.00-0.087           O  
ANISOU 2468  O   ARG A 489     9663   5945   4909     22   1538   -163       O  
ATOM   2469  CB  ARG A 489      14.036  -8.220  -1.432  1.00-0.087           C  
ANISOU 2469  CB  ARG A 489     8767   5044   4198    208   1473   -289       C  
ATOM   2470  N   ALA A 490      11.948  -6.211  -2.807  1.00 0.581           N  
ANISOU 2470  N   ALA A 490     9411   5469   4545     50   1373   -192       N  
ATOM   2471  CA  ALA A 490      11.287  -5.676  -4.008  1.00 0.581           C  
ANISOU 2471  CA  ALA A 490     9680   5634   4603     10   1363   -163       C  
ATOM   2472  C   ALA A 490      11.326  -4.168  -4.083  1.00 0.581           C  
ANISOU 2472  C   ALA A 490    10366   6332   5295    -55   1368    -84       C  
ATOM   2473  O   ALA A 490      11.306  -3.611  -5.170  1.00 0.581           O  
ANISOU 2473  O   ALA A 490    10396   6306   5156    -86   1401    -50       O  
ATOM   2474  CB  ALA A 490       9.849  -6.160  -4.090  1.00 0.581           C  
ANISOU 2474  CB  ALA A 490     9878   5708   4696     13   1256   -178       C  
ATOM   2475  N   ASP A 491      11.387  -3.502  -2.930  1.00 0.152           N  
ANISOU 2475  N   ASP A 491     9980   5996   5080    -76   1337    -54       N  
ATOM   2476  CA  ASP A 491      11.444  -2.050  -2.871  1.00 0.152           C  
ANISOU 2476  CA  ASP A 491    10940   6930   6036   -140   1342     18       C  
ATOM   2477  C   ASP A 491      12.841  -1.525  -3.233  1.00 0.152           C  
ANISOU 2477  C   ASP A 491    13968  10061   9099   -192   1454     36       C  
ATOM   2478  O   ASP A 491      13.843  -1.971  -2.671  1.00 0.152           O  
ANISOU 2478  O   ASP A 491    10413   6659   5707   -182   1502      3       O  
ATOM   2479  CB  ASP A 491      11.009  -1.577  -1.485  1.00 0.152           C  
ANISOU 2479  CB  ASP A 491    11038   7026   6284   -146   1272     33       C  
ATOM   2480  CG  ASP A 491      10.852  -0.084  -1.423  1.00 0.152           C  
ANISOU 2480  CG  ASP A 491    11808   7711   7011   -203   1267    104       C  
ATOM   2481  OD1 ASP A 491       9.787   0.412  -1.837  1.00 0.152           O  
ANISOU 2481  OD1 ASP A 491    11921   7700   6994   -190   1214    144       O  
ATOM   2482  OD2 ASP A 491      11.811   0.593  -0.993  1.00 0.152           O  
ANISOU 2482  OD2 ASP A 491    12267   8224   7557   -262   1317    119       O  
TER    2483      ASP A 491                                                      
HETATM 2484  C1  NAG B   1      33.805 -24.572  -7.213  1.00 90.52           C  
ANISOU 2484  C1  NAG B   1    13437  11655   9300   3836   3881   -962       C  
HETATM 2485  C2  NAG B   1      33.287 -26.000  -7.412  1.00 89.81           C  
ANISOU 2485  C2  NAG B   1    13693  11292   9140   4032   3900  -1058       C  
HETATM 2486  C3  NAG B   1      33.712 -26.597  -8.756  1.00 91.46           C  
ANISOU 2486  C3  NAG B   1    14052  11494   9206   4200   4118  -1149       C  
HETATM 2487  C4  NAG B   1      33.463 -25.621  -9.903  1.00 94.05           C  
ANISOU 2487  C4  NAG B   1    14394  11912   9431   3973   4189  -1164       C  
HETATM 2488  C5  NAG B   1      34.162 -24.296  -9.593  1.00 92.96           C  
ANISOU 2488  C5  NAG B   1    13876  12065   9380   3822   4184  -1055       C  
HETATM 2489  C6  NAG B   1      34.030 -23.236 -10.675  1.00 90.53           C  
ANISOU 2489  C6  NAG B   1    13557  11864   8976   3597   4261  -1051       C  
HETATM 2490  C7  NAG B   1      33.006 -27.687  -5.623  1.00 87.04           C  
ANISOU 2490  C7  NAG B   1    13499  10663   8910   4315   3730  -1048       C  
HETATM 2491  C8  NAG B   1      33.720 -28.513  -4.594  1.00 85.75           C  
ANISOU 2491  C8  NAG B   1    13236  10510   8836   4591   3709  -1003       C  
HETATM 2492  N2  NAG B   1      33.771 -26.831  -6.320  1.00 87.49           N  
ANISOU 2492  N2  NAG B   1    13326  10973   8944   4267   3852  -1025       N  
HETATM 2493  O3  NAG B   1      32.993 -27.801  -8.983  1.00 91.72           O  
ANISOU 2493  O3  NAG B   1    14458  11233   9160   4311   4110  -1247       O  
HETATM 2494  O4  NAG B   1      33.939 -26.201 -11.117  1.00 97.76           O  
ANISOU 2494  O4  NAG B   1    14993  12389   9760   4145   4402  -1247       O  
HETATM 2495  O5  NAG B   1      33.623 -23.743  -8.373  1.00 92.10           O  
ANISOU 2495  O5  NAG B   1    13669  11925   9398   3649   3969   -982       O  
HETATM 2496  O6  NAG B   1      32.689 -22.790 -10.858  1.00 90.13           O  
ANISOU 2496  O6  NAG B   1    13733  11634   8879   3342   4120  -1070       O  
HETATM 2497  O7  NAG B   1      31.797 -27.786  -5.809  1.00 87.69           O  
ANISOU 2497  O7  NAG B   1    13853  10526   8940   4143   3639  -1098       O  
HETATM 2498  C1  NAG B   2      33.045 -26.337 -12.228  1.00101.90           C  
ANISOU 2498  C1  NAG B   2    15849  12743  10126   4030   4430  -1342       C  
HETATM 2499  C2  NAG B   2      33.897 -26.357 -13.497  1.00103.85           C  
ANISOU 2499  C2  NAG B   2    16080  13136  10240   4154   4677  -1387       C  
HETATM 2500  C3  NAG B   2      33.041 -26.594 -14.743  1.00105.31           C  
ANISOU 2500  C3  NAG B   2    16632  13146  10235   4058   4719  -1496       C  
HETATM 2501  C4  NAG B   2      32.164 -27.830 -14.569  1.00105.87           C  
ANISOU 2501  C4  NAG B   2    17063  12894  10266   4145   4632  -1594       C  
HETATM 2502  C5  NAG B   2      31.367 -27.730 -13.269  1.00104.23           C  
ANISOU 2502  C5  NAG B   2    16828  12569  10207   4011   4389  -1534       C  
HETATM 2503  C6  NAG B   2      30.548 -28.966 -12.968  1.00104.25           C  
ANISOU 2503  C6  NAG B   2    17164  12259  10185   4090   4302  -1617       C  
HETATM 2504  C7  NAG B   2      35.965 -25.015 -13.606  1.00105.39           C  
ANISOU 2504  C7  NAG B   2    15639  13884  10519   4197   4897  -1246       C  
HETATM 2505  C8  NAG B   2      36.531 -23.626 -13.658  1.00104.92           C  
ANISOU 2505  C8  NAG B   2    15255  14106  10504   3992   4928  -1144       C  
HETATM 2506  N2  NAG B   2      34.623 -25.101 -13.602  1.00104.65           N  
ANISOU 2506  N2  NAG B   2    15844  13534  10383   4021   4737  -1292       N  
HETATM 2507  O3  NAG B   2      33.892 -26.768 -15.872  1.00105.10           O  
ANISOU 2507  O3  NAG B   2    16612  13245  10078   4212   4964  -1546       O  
HETATM 2508  O4  NAG B   2      31.292 -27.970 -15.688  1.00107.29           O  
ANISOU 2508  O4  NAG B   2    17577  12921  10270   4017   4644  -1692       O  
HETATM 2509  O5  NAG B   2      32.268 -27.540 -12.160  1.00103.63           O  
ANISOU 2509  O5  NAG B   2    16414  12663  10297   4129   4372  -1433       O  
HETATM 2510  O6  NAG B   2      29.692 -28.774 -11.850  1.00104.56           O  
ANISOU 2510  O6  NAG B   2    17192  12192  10343   3921   4077  -1561       O  
HETATM 2511  O7  NAG B   2      36.686 -26.011 -13.569  1.00105.41           O  
ANISOU 2511  O7  NAG B   2    15635  13892  10524   4506   5013  -1282       O  
HETATM 2512  C2  GBS A 601      -9.771  -6.594  20.191  1.00 48.57           C  
ANISOU 2512  C2  GBS A 601     8213   5252   4988    164    848    221       C  
HETATM 2513  C3  GBS A 601     -10.383  -5.387  19.865  1.00 49.90           C  
ANISOU 2513  C3  GBS A 601     8326   5475   5159    266    857    244       C  
HETATM 2514  C4  GBS A 601      -9.821  -4.550  18.918  1.00 51.90           C  
ANISOU 2514  C4  GBS A 601     8623   5686   5410    320    820    235       C  
HETATM 2515  C6  GBS A 601      -7.987  -3.930  17.343  1.00 55.22           C  
ANISOU 2515  C6  GBS A 601     9183   5978   5821    322    753    193       C  
HETATM 2516  C1  GBS A 601      -8.586  -6.949  19.545  1.00 50.17           C  
ANISOU 2516  C1  GBS A 601     8505   5368   5191    127    803    184       C  
HETATM 2517  N4  GBS A 601      -8.498  -8.407  22.128  1.00 44.27           N  
ANISOU 2517  N4  GBS A 601     7823   4574   4422     55    889    190       N  
HETATM 2518  C5  GBS A 601      -8.628  -4.893  18.279  1.00 53.03           C  
ANISOU 2518  C5  GBS A 601     8853   5745   5550    269    779    199       C  
HETATM 2519  C18 GBS A 601      -9.817  -8.294  21.949  1.00 44.54           C  
ANISOU 2519  C18 GBS A 601     7745   4715   4464     46    906    225       C  
HETATM 2520  O   GBS A 601      -7.986  -2.731  17.507  1.00 56.58           O  
ANISOU 2520  O   GBS A 601     9382   6127   5989    414    778    204       O  
HETATM 2521  N2  GBS A 601     -10.432  -7.436  21.122  1.00 46.68           N  
ANISOU 2521  N2  GBS A 601     7935   5054   4745    103    888    240       N  
HETATM 2522  N3  GBS A 601     -10.614  -9.109  22.642  1.00 42.03           N  
ANISOU 2522  N3  GBS A 601     7382   4446   4140    -24    943    253       N  
HETATM 2523  C   GBS A 601      -8.026  -6.110  18.596  1.00 50.85           C  
ANISOU 2523  C   GBS A 601     8621   5426   5275    178    771    173       C  
HETATM 2524  UNK UNX A 602       5.891  11.895  25.882  1.00 31.13           X  
ANISOU 2524  UNK UNX A 602     7982   1494   2353   -194    867   -409       X  
HETATM 2525  UNK UNX A 603       9.778  14.407  10.424  1.00 56.67           X  
HETATM 2526  UNK UNX A 604      13.872 -23.793  -7.304  1.00 56.38           X  
HETATM 2527  O   HOH A 701      -4.660  -7.671   0.360  1.00 48.51           O  
HETATM 2528  O   HOH A 702      -6.057 -12.479  12.102  1.00 35.07           O  
HETATM 2529  O   HOH A 703      -4.836 -10.111  24.459  1.00 32.18           O  
HETATM 2530  O   HOH A 704      15.059  -9.511  26.410  1.00 51.62           O  
HETATM 2531  O   HOH A 705       3.070  -4.758  14.725  1.00 28.76           O  
HETATM 2532  O   HOH A 706      -5.973  -4.204   3.631  1.00 34.97           O  
HETATM 2533  O   HOH A 707      15.170   1.369  24.895  1.00 46.15           O  
HETATM 2534  O   HOH A 708       7.039  15.423  21.288  1.00 53.61           O  
HETATM 2535  O   HOH A 709       4.845 -19.129   5.676  1.00 50.86           O  
HETATM 2536  O   HOH A 710      14.098  -5.883  12.918  1.00 38.74           O  
HETATM 2537  O   HOH A 711      14.918  10.690  11.262  1.00 53.33           O  
HETATM 2538  O   HOH A 712      -2.396 -19.613  19.708  1.00 33.95           O  
HETATM 2539  O   HOH A 713      -3.747 -13.541  10.525  1.00 31.96           O  
HETATM 2540  O   HOH A 714      -4.634  12.170   6.804  1.00 43.40           O  
HETATM 2541  O   HOH A 715      -8.077  -1.044  32.192  1.00 42.23           O  
HETATM 2542  O   HOH A 716      11.027  10.559  18.701  1.00 50.92           O  
HETATM 2543  O   HOH A 717      -2.663 -19.379  28.344  1.00 36.63           O  
HETATM 2544  O   HOH A 718       1.017 -21.785  21.693  1.00 39.69           O  
HETATM 2545  O   HOH A 719      -2.184 -21.058  15.085  1.00 54.07           O  
HETATM 2546  O   HOH A 720      -3.974  -0.476  30.317  1.00 34.30           O  
HETATM 2547  O   HOH A 721       5.645   7.081  19.709  1.00 31.12           O  
HETATM 2548  O   HOH A 722     -17.970 -13.772  27.817  1.00 55.09           O  
HETATM 2549  O   HOH A 723      15.378 -12.349  12.758  1.00 39.13           O  
HETATM 2550  O   HOH A 724     -15.151  -6.074  29.137  1.00 51.41           O  
HETATM 2551  O   HOH A 725      -7.331 -19.025  32.680  1.00 43.71           O  
HETATM 2552  O   HOH A 726      -1.166  14.086  14.205  1.00 53.69           O  
HETATM 2553  O   HOH A 727       0.073 -17.414   1.686  1.00 41.20           O  
HETATM 2554  O   HOH A 728     -10.295  -6.182  14.459  1.00 51.67           O  
HETATM 2555  O   HOH A 729      15.726 -23.349  18.030  1.00 45.98           O  
HETATM 2556  O   HOH A 730      -1.437  -9.256  32.853  1.00 38.40           O  
HETATM 2557  O   HOH A 731       1.645   3.028  37.736  1.00 42.33           O  
HETATM 2558  O   HOH A 732       8.749   9.693   6.686  1.00 48.20           O  
HETATM 2559  O   HOH A 733       3.725 -21.541  21.563  1.00 41.88           O  
HETATM 2560  O   HOH A 734      -1.553  11.654   8.838  1.00 41.80           O  
HETATM 2561  O   HOH A 735     -13.008  -9.769  24.960  1.00 37.39           O  
HETATM 2562  O   HOH A 736       4.959 -15.702  15.409  1.00 33.03           O  
HETATM 2563  O   HOH A 737      13.480  -1.975   1.465  1.00 52.86           O  
HETATM 2564  O   HOH A 738      -4.773 -27.078  24.643  1.00 69.84           O  
HETATM 2565  O   HOH A 739      15.330  -0.630   5.718  1.00 50.80           O  
HETATM 2566  O   HOH A 740       9.067   4.334  19.038  1.00 38.47           O  
HETATM 2567  O   HOH A 741      -3.849   1.610  25.938  1.00 28.76           O  
HETATM 2568  O   HOH A 742       9.965 -16.794  10.560  1.00 63.22           O  
HETATM 2569  O   HOH A 743      -3.693 -17.258  29.707  1.00 31.93           O  
HETATM 2570  O   HOH A 744      -0.344  -4.461  20.679  1.00 32.12           O  
HETATM 2571  O   HOH A 745      19.295 -20.552  16.637  1.00 43.67           O  
HETATM 2572  O   HOH A 746       3.189   5.816  28.725  1.00 29.38           O  
HETATM 2573  O   HOH A 747      -1.719  -6.653  33.570  1.00 47.39           O  
HETATM 2574  O   HOH A 748      20.607  -7.263  20.250  1.00 58.48           O  
HETATM 2575  O   HOH A 749      17.590   0.667  25.936  1.00 78.17           O  
HETATM 2576  O   HOH A 750      -1.878   1.468  19.495  1.00 25.29           O  
HETATM 2577  O   HOH A 751      11.676 -17.187  26.333  1.00 46.06           O  
HETATM 2578  O   HOH A 752      15.398 -13.744  27.247  1.00 46.09           O  
HETATM 2579  O   HOH A 753      30.617  -9.289  12.785  1.00 65.63           O  
HETATM 2580  O   HOH A 754       4.629  14.042  30.416  1.00 36.17           O  
HETATM 2581  O   HOH A 755      -7.263   8.710  -1.850  1.00 66.24           O  
HETATM 2582  O   HOH A 756      -0.344  13.145   5.499  1.00 50.23           O  
HETATM 2583  O   HOH A 757      18.952 -10.309  11.079  1.00 51.45           O  
HETATM 2584  O   HOH A 758      -0.537  -1.034  19.545  1.00 31.93           O  
HETATM 2585  O   HOH A 759      13.602  10.225  19.485  1.00 75.77           O  
HETATM 2586  O   HOH A 760     -10.479   3.974  27.311  1.00 37.16           O  
HETATM 2587  O   HOH A 761       8.617 -12.194  27.398  1.00 43.32           O  
HETATM 2588  O   HOH A 762      -2.591   4.199  32.208  1.00 40.73           O  
HETATM 2589  O   HOH A 763      -7.467 -11.849  27.423  1.00 29.97           O  
HETATM 2590  O   HOH A 764       7.843   3.703  23.288  1.00 33.72           O  
HETATM 2591  O   HOH A 765       7.870   2.546  25.798  1.00 33.05           O  
HETATM 2592  O   HOH A 766      14.722  -8.413  12.332  1.00 35.83           O  
HETATM 2593  O   HOH A 767      -5.236 -20.570  28.445  1.00 41.10           O  
HETATM 2594  O   HOH A 768       5.615 -15.503   4.310  1.00 30.40           O  
HETATM 2595  O   HOH A 769      16.105  -2.643  19.839  1.00 43.08           O  
HETATM 2596  O   HOH A 770      12.639   6.091   2.854  1.00 61.85           O  
HETATM 2597  O   HOH A 771      10.717 -20.328  25.068  1.00 45.43           O  
HETATM 2598  O   HOH A 772      -6.108 -18.374  30.339  1.00 39.06           O  
HETATM 2599  O   HOH A 773       1.890   7.800  32.060  1.00 37.93           O  
HETATM 2600  O   HOH A 774      19.262  -9.294  14.025  1.00 41.20           O  
HETATM 2601  O   HOH A 775      10.198   4.802  23.790  1.00 39.28           O  
HETATM 2602  O   HOH A 776     -13.949  -3.684  29.295  1.00 51.79           O  
HETATM 2603  O   HOH A 777      -4.544 -17.204  34.825  1.00 34.68           O  
HETATM 2604  O   HOH A 778      -6.961  11.654   5.552  1.00 46.12           O  
HETATM 2605  O   HOH A 779       2.374  15.098  11.162  1.00 51.15           O  
HETATM 2606  O   HOH A 780       5.594  -4.069  22.750  1.00 37.12           O  
HETATM 2607  O   HOH A 781       9.548   7.448  24.769  1.00 40.98           O  
HETATM 2608  O   HOH A 782       3.035 -15.291   4.014  1.00 36.27           O  
HETATM 2609  O   HOH A 783      -4.822  11.076  18.698  1.00 42.81           O  
HETATM 2610  O   HOH A 784      11.854   8.930  -0.120  1.00 69.64           O  
HETATM 2611  O   HOH A 785       7.366 -21.582  18.314  1.00 43.67           O  
HETATM 2612  O   HOH A 786     -14.497  -1.468  22.120  1.00 58.55           O  
HETATM 2613  O   HOH A 787       0.892  -6.719  33.135  1.00 30.59           O  
HETATM 2614  O   HOH A 788     -16.391 -11.335  31.253  1.00 49.53           O  
HETATM 2615  O   HOH A 789       7.451 -17.183   6.753  1.00 38.95           O  
HETATM 2616  O   HOH A 790       6.193   4.725  21.372  1.00 38.16           O  
HETATM 2617  O   HOH A 791       4.053 -23.028  28.431  1.00 50.66           O  
HETATM 2618  O   HOH A 792     -10.081 -11.429  27.196  1.00 37.32           O  
HETATM 2619  O   HOH A 793       5.529  15.509  17.762  1.00 51.87           O  
HETATM 2620  O   HOH A 794       4.092  -0.780  31.620  1.00 42.48           O  
HETATM 2621  O   HOH A 795       7.990  10.684  15.548  1.00 38.96           O  
HETATM 2622  O   HOH A 796      14.551 -16.369   8.413  1.00 50.37           O  
HETATM 2623  O   HOH A 797      16.906  -5.439  26.486  1.00 52.83           O  
HETATM 2624  O   HOH A 798      -2.838 -26.440  20.373  1.00 58.45           O  
HETATM 2625  O   HOH A 799      -0.675 -23.517  20.152  1.00 51.21           O  
HETATM 2626  O   HOH A 800      -9.710  -2.795   1.101  1.00 51.52           O  
HETATM 2627  O   HOH A 801       7.753 -17.943  28.878  1.00 52.76           O  
HETATM 2628  O   HOH A 802      17.242 -26.958  11.444  1.00 57.30           O  
HETATM 2629  O   HOH A 803       0.782  -4.105  36.929  1.00 74.39           O  
HETATM 2630  O   HOH A 804       6.703  -0.360  30.660  1.00 40.71           O  
HETATM 2631  O   HOH A 805      13.040   9.150  15.037  1.00 61.66           O  
HETATM 2632  O   HOH A 806     -12.245  -6.935  16.400  1.00 52.56           O  
HETATM 2633  O   HOH A 807       8.410  12.916   6.729  1.00 44.94           O  
HETATM 2634  O   HOH A 808      -4.160 -19.799   7.037  1.00 41.46           O  
HETATM 2635  O   HOH A 809      -3.185  15.900  28.181  1.00 62.95           O  
HETATM 2636  O   HOH A 810      11.812 -20.547   5.966  1.00 66.38           O  
HETATM 2637  O   HOH A 811      18.725  -2.245  19.354  1.00 58.04           O  
HETATM 2638  O   HOH A 812      16.827  -9.867  13.062  1.00 36.55           O  
HETATM 2639  O   HOH A 813       1.304 -17.296   4.099  1.00 57.80           O  
HETATM 2640  O   HOH A 814       0.274 -19.910  19.908  1.00 49.69           O  
HETATM 2641  O   HOH A 815      23.058 -13.860  19.000  1.00 64.48           O  
HETATM 2642  O   HOH A 816      18.414 -23.046  17.499  1.00 54.90           O  
HETATM 2643  O   HOH A 817       7.006 -17.110  16.675  1.00 49.24           O  
HETATM 2644  O   HOH A 818      -8.091  -4.773   2.069  1.00 50.84           O  
CONECT  177  558                                                                
CONECT  281  627                                                                
CONECT  462 2484                                                                
CONECT  558  177                                                                
CONECT  627  281                                                                
CONECT  646 1536                                                                
CONECT  874  989                                                                
CONECT  989  874                                                                
CONECT 1536  646                                                                
CONECT 1875 1998                                                                
CONECT 1998 1875                                                                
CONECT 2074 2276                                                                
CONECT 2097 2515                                                                
CONECT 2276 2074                                                                
CONECT 2484  462 2485 2495                                                      
CONECT 2485 2484 2486 2492                                                      
CONECT 2486 2485 2487 2493                                                      
CONECT 2487 2486 2488 2494                                                      
CONECT 2488 2487 2489 2495                                                      
CONECT 2489 2488 2496                                                           
CONECT 2490 2491 2492 2497                                                      
CONECT 2491 2490                                                                
CONECT 2492 2485 2490                                                           
CONECT 2493 2486                                                                
CONECT 2494 2487 2498                                                           
CONECT 2495 2484 2488                                                           
CONECT 2496 2489                                                                
CONECT 2497 2490                                                                
CONECT 2498 2494 2499 2509                                                      
CONECT 2499 2498 2500 2506                                                      
CONECT 2500 2499 2501 2507                                                      
CONECT 2501 2500 2502 2508                                                      
CONECT 2502 2501 2503 2509                                                      
CONECT 2503 2502 2510                                                           
CONECT 2504 2505 2506 2511                                                      
CONECT 2505 2504                                                                
CONECT 2506 2499 2504                                                           
CONECT 2507 2500                                                                
CONECT 2508 2501                                                                
CONECT 2509 2498 2502                                                           
CONECT 2510 2503                                                                
CONECT 2511 2504                                                                
CONECT 2512 2513 2516 2521                                                      
CONECT 2513 2512 2514                                                           
CONECT 2514 2513 2518                                                           
CONECT 2515 2097 2518 2520                                                      
CONECT 2516 2512 2523                                                           
CONECT 2517 2519                                                                
CONECT 2518 2514 2515 2523                                                      
CONECT 2519 2517 2521 2522                                                      
CONECT 2520 2515                                                                
CONECT 2521 2512 2519                                                           
CONECT 2522 2519                                                                
CONECT 2523 2516 2518                                                           
MASTER      366    0    6    6   22    0    0    6 2643    1   54   31          
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.