CNRS Nantes University UFIP UFIP
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***  PROTEIN BINDING 10-JUN-10 3NFK  ***

elNémo ID: 23011717495482996

Job options:

ID        	=	 23011717495482996
JOBID     	=	 PROTEIN BINDING 10-JUN-10 3NFK
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PROTEIN BINDING                         10-JUN-10   3NFK              
TITLE     CRYSTAL STRUCTURE OF THE PTPN4 PDZ DOMAIN COMPLEXED WITH THE C-       
TITLE    2 TERMINUS OF A RABIES VIRUS G PROTEIN                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 4;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PDZ DOMAIN (UNP RESIDUES 499-604);                         
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE MEG1, PTPASE-MEG1, MEG;        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLYCOPROTEIN G;                                            
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 512-524;                                      
COMPND  11 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: PTPN4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) STAR;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST15;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: RABIES VIRUS;                                   
SOURCE  14 ORGANISM_TAXID: 11292;                                               
SOURCE  15 OTHER_DETAILS: CYTO13-ATT PEPTIDE HAS BEEN CHEMICALLY SYNTHETIZED.   
SOURCE  16 THE SEQUENCE OCCURS NATURALLY IN RABIES VIRUS G PROTEIN              
KEYWDS    PDZ-PDZ-BINDING SITE COMPLEX, PROTEIN BINDING                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABAULT,F.CORDIER,M.LAFAGE,J.COCKBURN,A.HAOUZ,F.A.REY,M.DELEPIERRE, 
AUTHOR   2 H.BUC,M.LAFON,N.WOLFF                                                
REVDAT   2   30-NOV-11 3NFK    1       JRNL                                     
REVDAT   1   24-AUG-11 3NFK    0                                                
JRNL        AUTH   N.BABAULT,F.CORDIER,M.LAFAGE,J.COCKBURN,A.HAOUZ,C.PREHAUD,   
JRNL        AUTH 2 F.A.REY,M.DELEPIERRE,H.BUC,M.LAFON,N.WOLFF                   
JRNL        TITL   PEPTIDES TARGETING THE PDZ DOMAIN OF PTPN4 ARE EFFICIENT     
JRNL        TITL 2 INDUCERS OF GLIOBLASTOMA CELL DEATH.                         
JRNL        REF    STRUCTURE                     V.  19  1518 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22000519                                                     
JRNL        DOI    10.1016/J.STR.2011.07.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.3                                         
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) : 1.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42710                          
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                      : 0.204                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2155                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.43                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.47                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.70                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3160                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1876                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3001                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1853                   
REMARK   3   BIN FREE R VALUE                        : 0.2333                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.03                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 159                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1548                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.22030                                             
REMARK   3    B22 (A**2) : 0.75720                                              
REMARK   3    B33 (A**2) : 0.46310                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.17                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.06                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1600   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 2160   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 579    ; 2.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 47     ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 232    ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 1600   ; 20.000 ; NULL                
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   : 201    ; 5.000  ; NULL                
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   : 1976   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.10                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 13.85                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A  513    A  604                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   33.1435  -18.5056   15.3124           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0748 T22:   -0.0464                                    
REMARK   3     T33:   -0.0379 T12:    0.0017                                    
REMARK   3     T13:   -0.0011 T23:    0.0080                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0555 L22:    1.2897                                    
REMARK   3     L33:    0.6118 L12:    0.0333                                    
REMARK   3     L13:   -0.0672 L23:   -0.0627                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0058 S12:    0.0209 S13:    0.0121                     
REMARK   3     S21:   -0.0172 S22:    0.0061 S23:   -0.1331                     
REMARK   3     S31:    0.0005 S32:    0.0419 S33:   -0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   C    1    C   13                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   24.4260   -9.4236   18.0277           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0200 T22:   -0.0039                                    
REMARK   3     T33:    0.0056 T12:   -0.0048                                    
REMARK   3     T13:   -0.0143 T23:   -0.0058                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1534 L22:    3.4346                                    
REMARK   3     L33:    1.7466 L12:   -0.8889                                    
REMARK   3     L13:   -1.1209 L23:   -0.2264                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0393 S12:    0.1537 S13:    0.0018                     
REMARK   3     S21:   -0.1086 S22:   -0.0241 S23:    0.2286                     
REMARK   3     S31:    0.0717 S32:   -0.1022 S33:   -0.0152                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   B  594    B  604                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   27.3935   -1.7889   -5.2299           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0365 T22:    0.0188                                    
REMARK   3     T33:   -0.0154 T12:   -0.0055                                    
REMARK   3     T13:   -0.0006 T23:    0.0221                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4659 L22:    3.2971                                    
REMARK   3     L33:    1.8874 L12:   -1.3715                                    
REMARK   3     L13:    0.2031 L23:   -1.0075                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0566 S12:   -0.0667 S13:    0.0731                     
REMARK   3     S21:    0.0211 S22:    0.1581 S23:    0.0588                     
REMARK   3     S31:   -0.1304 S32:   -0.1310 S33:   -0.1014                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   D    9    D   13                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   34.6610    1.0037    2.3660           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0233 T22:    0.0082                                    
REMARK   3     T33:   -0.0320 T12:    0.0300                                    
REMARK   3     T13:   -0.0207 T23:   -0.0216                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0207 L22:    0.0000                                    
REMARK   3     L33:    0.3054 L12:    0.3334                                    
REMARK   3     L13:   -0.8913 L23:   -0.1162                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0160 S12:   -0.0145 S13:    0.0308                     
REMARK   3     S21:    0.0268 S22:   -0.0158 S23:   -0.0154                     
REMARK   3     S31:   -0.0331 S32:    0.0132 S33:    0.0318                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059766.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY COOLED               
REMARK 200                                   MONOCHROMATOR CRYSTAL              
REMARK 200  OPTICS                         : BI-MORPH MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.300                              
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: PDB ENTRY 2VPH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 1500, 20% GLYCEROL, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.71500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.71500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6040 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 870 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5880 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       53.43000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000      -26.85000            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000       40.90000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D                               
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     SER A   500                                                      
REMARK 465     PRO A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     LYS A   503                                                      
REMARK 465     PRO A   504                                                      
REMARK 465     THR A   505                                                      
REMARK 465     PRO A   506                                                      
REMARK 465     ASN A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     GLY A   509                                                      
REMARK 465     ILE A   510                                                      
REMARK 465     PRO A   511                                                      
REMARK 465     HIS A   512                                                      
REMARK 465     GLY B   498                                                      
REMARK 465     SER B   499                                                      
REMARK 465     SER B   500                                                      
REMARK 465     PRO B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     LYS B   503                                                      
REMARK 465     PRO B   504                                                      
REMARK 465     THR B   505                                                      
REMARK 465     PRO B   506                                                      
REMARK 465     ASN B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     GLY B   509                                                      
REMARK 465     ILE B   510                                                      
REMARK 465     PRO B   511                                                      
REMARK 465     ARG B   592                                                      
REMARK 465     HIS B   593                                                      
REMARK 465     SER D     1                                                      
REMARK 465     TRP D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     SER D     7                                                      
REMARK 465     GLY D     8                                                      
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     HIS A 593    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR B 536    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET B 598    CG   SD   CE                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VPH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PTPN4-PDZ                                       
REMARK 900 RELATED ID: 2CS5   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF PTPN4-PDZ                                      
REMARK 900 RELATED ID: 3NFL   RELATED DB: PDB                                   
DBREF  3NFK A  499   604  UNP    P29074   PTN4_HUMAN     499    604             
DBREF  3NFK B  499   604  UNP    P29074   PTN4_HUMAN     499    604             
DBREF  3NFK C    1    13  UNP    P03524   VGLG_RABVE     512    524             
DBREF  3NFK D    1    13  UNP    P03524   VGLG_RABVE     512    524             
SEQADV 3NFK GLY A  498  UNP  P29074              EXPRESSION TAG                 
SEQADV 3NFK GLY B  498  UNP  P29074              EXPRESSION TAG                 
SEQRES   1 A  107  GLY SER SER PRO GLU LYS PRO THR PRO ASN GLY GLY ILE          
SEQRES   2 A  107  PRO HIS ASP ASN LEU VAL LEU ILE ARG MET LYS PRO ASP          
SEQRES   3 A  107  GLU ASN GLY ARG PHE GLY PHE ASN VAL LYS GLY GLY TYR          
SEQRES   4 A  107  ASP GLN LYS MET PRO VAL ILE VAL SER ARG VAL ALA PRO          
SEQRES   5 A  107  GLY THR PRO ALA ASP LEU CYS VAL PRO ARG LEU ASN GLU          
SEQRES   6 A  107  GLY ASP GLN VAL VAL LEU ILE ASN GLY ARG ASP ILE ALA          
SEQRES   7 A  107  GLU HIS THR HIS ASP GLN VAL VAL LEU PHE ILE LYS ALA          
SEQRES   8 A  107  SER CYS GLU ARG HIS SER GLY GLU LEU MET LEU LEU VAL          
SEQRES   9 A  107  ARG PRO ASN                                                  
SEQRES   1 B  107  GLY SER SER PRO GLU LYS PRO THR PRO ASN GLY GLY ILE          
SEQRES   2 B  107  PRO HIS ASP ASN LEU VAL LEU ILE ARG MET LYS PRO ASP          
SEQRES   3 B  107  GLU ASN GLY ARG PHE GLY PHE ASN VAL LYS GLY GLY TYR          
SEQRES   4 B  107  ASP GLN LYS MET PRO VAL ILE VAL SER ARG VAL ALA PRO          
SEQRES   5 B  107  GLY THR PRO ALA ASP LEU CYS VAL PRO ARG LEU ASN GLU          
SEQRES   6 B  107  GLY ASP GLN VAL VAL LEU ILE ASN GLY ARG ASP ILE ALA          
SEQRES   7 B  107  GLU HIS THR HIS ASP GLN VAL VAL LEU PHE ILE LYS ALA          
SEQRES   8 B  107  SER CYS GLU ARG HIS SER GLY GLU LEU MET LEU LEU VAL          
SEQRES   9 B  107  ARG PRO ASN                                                  
SEQRES   1 C   13  SER TRP GLU SER HIS LYS SER GLY GLY GLU THR ARG LEU          
SEQRES   1 D   13  SER TRP GLU SER HIS LYS SER GLY GLY GLU THR ARG LEU          
HET    GOL  A   1       6                                                       
HET    GOL  A 605       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   7  HOH   *181(H2 O)                                                    
HELIX    1   1 TYR A  536  LYS A  539  5                                   4    
HELIX    2   2 THR A  551  CYS A  556  1                                   6    
HELIX    3   3 THR A  578  ALA A  588  1                                  11    
HELIX    4   4 SER A  589  ARG A  592  5                                   4    
HELIX    5   5 TYR B  536  LYS B  539  5                                   4    
HELIX    6   6 THR B  551  CYS B  556  1                                   6    
HELIX    7   7 THR B  578  ALA B  588  1                                  11    
SHEET    1   A 4 VAL A 516  MET A 520  0                                        
SHEET    2   A 4 LEU A 597  ARG A 602 -1  O  LEU A 599   N  ILE A 518           
SHEET    3   A 4 GLN A 565  ILE A 569 -1  N  VAL A 567   O  LEU A 600           
SHEET    4   A 4 ARG A 572  ASP A 573 -1  O  ARG A 572   N  ILE A 569           
SHEET    1   B 4 MET A 540  VAL A 547  0                                        
SHEET    2   B 4 PHE A 530  GLY A 535 -1  N  GLY A 535   O  MET A 540           
SHEET    3   B 4 GLU C  10  ARG C  12 -1  O  THR C  11   N  VAL A 532           
SHEET    4   B 4 LYS C   6  SER C   7 -1  N  SER C   7   O  GLU C  10           
SHEET    1   C 4 VAL B 516  MET B 520  0                                        
SHEET    2   C 4 LEU B 597  ARG B 602 -1  O  LEU B 599   N  ILE B 518           
SHEET    3   C 4 GLN B 565  ILE B 569 -1  N  VAL B 567   O  LEU B 600           
SHEET    4   C 4 ARG B 572  ASP B 573 -1  O  ARG B 572   N  ILE B 569           
SHEET    1   D 3 MET B 540  VAL B 547  0                                        
SHEET    2   D 3 PHE B 530  GLY B 535 -1  N  GLY B 535   O  MET B 540           
SHEET    3   D 3 GLU D  10  ARG D  12 -1  O  THR D  11   N  VAL B 532           
SSBOND   1 CYS A  590    CYS B  590                          1555   1555  2.08  
CISPEP   1 VAL A  557    PRO A  558          0       -11.94                     
CISPEP   2 VAL B  557    PRO B  558          0         1.24                     
SITE     1 AC1  6 HOH A  61  HOH A 315  ASP A 537  PRO A 549                    
SITE     2 AC1  6 GLY A 550  ASP B 554                                          
SITE     1 AC2  9 HOH A  23  HOH A  28  VAL A 547  ARG A 559                    
SITE     2 AC2  9 GLU A 562  ASP A 580  ASP B 580  TRP C   2                    
SITE     3 AC2  9 HOH C  53                                                     
CRYST1   53.430   53.700   81.800  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018716  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012225        0.00000                         
ATOM      1  N   ASP A 513      48.264 -24.342  19.914  1.00 23.96           N  
ANISOU    1  N   ASP A 513     2085   2970   4049    226   -319    188       N  
ATOM      2  CA  ASP A 513      48.245 -25.792  19.826  1.00 22.81           C  
ANISOU    2  CA  ASP A 513     1943   2793   3932    278   -303    206       C  
ATOM      3  C   ASP A 513      46.897 -26.289  20.311  1.00 25.07           C  
ANISOU    3  C   ASP A 513     2338   3081   4107    278   -320    216       C  
ATOM      4  O   ASP A 513      46.123 -25.481  20.816  1.00 22.27           O  
ANISOU    4  O   ASP A 513     2044   2756   3661    241   -351    210       O  
ATOM      5  CB  ASP A 513      49.418 -26.416  20.629  1.00 26.45           C  
ANISOU    5  CB  ASP A 513     2315   3238   4495    317   -385    243       C  
ATOM      6  CG  ASP A 513      49.324 -26.279  22.144  1.00 39.91           C  
ANISOU    6  CG  ASP A 513     4048   4967   6150    310   -517    277       C  
ATOM      7  OD1 ASP A 513      48.640 -25.349  22.618  1.00 39.57           O  
ANISOU    7  OD1 ASP A 513     4069   4957   6010    265   -548    262       O  
ATOM      8  OD2 ASP A 513      49.942 -27.103  22.854  1.00 46.71           O  
ANISOU    8  OD2 ASP A 513     4868   5812   7066    350   -589    319       O  
ATOM      9  N   ASN A 514      46.611 -27.595  20.121  1.00 22.55           N  
ANISOU    9  N   ASN A 514     2041   2725   3800    318   -292    229       N  
ATOM     10  CA  ASN A 514      45.363 -28.292  20.470  1.00 20.93           C  
ANISOU   10  CA  ASN A 514     1930   2511   3510    320   -295    242       C  
ATOM     11  C   ASN A 514      44.167 -27.708  19.738  1.00 21.34           C  
ANISOU   11  C   ASN A 514     2054   2583   3473    281   -231    205       C  
ATOM     12  O   ASN A 514      43.030 -27.795  20.188  1.00 23.82           O  
ANISOU   12  O   ASN A 514     2442   2905   3703    265   -245    213       O  
ATOM     13  CB  ASN A 514      45.126 -28.337  22.004  1.00 29.15           C  
ANISOU   13  CB  ASN A 514     3008   3571   4499    318   -400    288       C  
ATOM     14  CG  ASN A 514      43.997 -29.271  22.400  1.00 53.59           C  
ANISOU   14  CG  ASN A 514     6186   6646   7530    326   -397    314       C  
ATOM     15  OD1 ASN A 514      43.821 -30.360  21.833  1.00 56.28           O  
ANISOU   15  OD1 ASN A 514     6532   6941   7911    353   -347    315       O  
ATOM     16  ND2 ASN A 514      43.149 -28.829  23.314  1.00 39.57           N  
ANISOU   16  ND2 ASN A 514     4478   4904   5654    298   -438    329       N  
ATOM     17  N   LEU A 515      44.422 -27.172  18.576  1.00 15.29           N  
ANISOU   17  N   LEU A 515     1261   1820   2727    269   -158    168       N  
ATOM     18  CA  LEU A 515      43.379 -26.493  17.833  1.00 12.33           C  
ANISOU   18  CA  LEU A 515      948   1468   2271    233   -106    139       C  
ATOM     19  C   LEU A 515      42.508 -27.425  17.031  1.00 13.14           C  
ANISOU   19  C   LEU A 515     1103   1546   2343    243    -47    118       C  
ATOM     20  O   LEU A 515      42.953 -28.496  16.612  1.00 13.87           O  
ANISOU   20  O   LEU A 515     1175   1602   2495    277    -14    112       O  
ATOM     21  CB  LEU A 515      44.027 -25.440  16.936  1.00 12.13           C  
ANISOU   21  CB  LEU A 515      878   1459   2273    212    -56    116       C  
ATOM     22  CG  LEU A 515      44.932 -24.435  17.664  1.00 15.03           C  
ANISOU   22  CG  LEU A 515     1185   1844   2682    194   -114    129       C  
ATOM     23  CD1 LEU A 515      45.595 -23.485  16.650  1.00 17.90           C  
ANISOU   23  CD1 LEU A 515     1501   2216   3086    171    -49    111       C  
ATOM     24  CD2 LEU A 515      44.160 -23.621  18.671  1.00 14.40           C  
ANISOU   24  CD2 LEU A 515     1158   1790   2523    163   -182    136       C  
ATOM     25  N   VAL A 516      41.260 -27.020  16.840  1.00 11.18           N  
ANISOU   25  N   VAL A 516      923   1319   2008    213    -36    107       N  
ATOM     26  CA  VAL A 516      40.251 -27.798  16.148  1.00 10.91           C  
ANISOU   26  CA  VAL A 516      942   1266   1935    211      6     85       C  
ATOM     27  C   VAL A 516      39.722 -26.922  15.008  1.00 12.26           C  
ANISOU   27  C   VAL A 516     1140   1466   2052    182     57     54       C  
ATOM     28  O   VAL A 516      39.327 -25.762  15.232  1.00 11.18           O  
ANISOU   28  O   VAL A 516     1016   1362   1871    155     38     62       O  
ATOM     29  CB  VAL A 516      39.117 -28.178  17.148  1.00 14.78           C  
ANISOU   29  CB  VAL A 516     1487   1756   2375    202    -41    111       C  
ATOM     30  CG1 VAL A 516      37.974 -28.919  16.450  1.00 15.91           C  
ANISOU   30  CG1 VAL A 516     1680   1879   2484    192     -4     88       C  
ATOM     31  CG2 VAL A 516      39.652 -29.007  18.306  1.00 15.96           C  
ANISOU   31  CG2 VAL A 516     1617   1878   2567    230    -95    154       C  
ATOM     32  N   LEU A 517      39.683 -27.488  13.795  1.00 11.31           N  
ANISOU   32  N   LEU A 517     1033   1331   1933    189    121     19       N  
ATOM     33  CA  LEU A 517      39.178 -26.782  12.626  1.00 11.71           C  
ANISOU   33  CA  LEU A 517     1116   1410   1922    164    167     -7       C  
ATOM     34  C   LEU A 517      37.784 -27.249  12.317  1.00 15.39           C  
ANISOU   34  C   LEU A 517     1646   1876   2326    148    162    -24       C  
ATOM     35  O   LEU A 517      37.574 -28.435  12.024  1.00 17.22           O  
ANISOU   35  O   LEU A 517     1896   2074   2572    161    177    -48       O  
ATOM     36  CB  LEU A 517      40.089 -27.069  11.424  1.00 13.63           C  
ANISOU   36  CB  LEU A 517     1336   1644   2196    180    244    -39       C  
ATOM     37  CG  LEU A 517      39.808 -26.266  10.127  1.00 16.58           C  
ANISOU   37  CG  LEU A 517     1743   2052   2503    156    299    -58       C  
ATOM     38  CD1 LEU A 517      40.085 -24.809  10.323  1.00 18.92           C  
ANISOU   38  CD1 LEU A 517     2016   2379   2793    133    288    -26       C  
ATOM     39  CD2 LEU A 517      40.730 -26.733   8.985  1.00 20.66           C  
ANISOU   39  CD2 LEU A 517     2244   2559   3046    176    386    -93       C  
ATOM     40  N   ILE A 518      36.841 -26.321  12.378  1.00 12.93           N  
ANISOU   40  N   ILE A 518     1364   1597   1953    119    139    -12       N  
ATOM     41  CA  ILE A 518      35.445 -26.648  12.122  1.00 14.64           C  
ANISOU   41  CA  ILE A 518     1630   1816   2116    101    127    -25       C  
ATOM     42  C   ILE A 518      34.931 -25.910  10.913  1.00 15.08           C  
ANISOU   42  C   ILE A 518     1716   1905   2111     80    152    -42       C  
ATOM     43  O   ILE A 518      35.265 -24.747  10.715  1.00 13.88           O  
ANISOU   43  O   ILE A 518     1552   1778   1945     72    160    -25       O  
ATOM     44  CB  ILE A 518      34.629 -26.265  13.357  1.00 18.27           C  
ANISOU   44  CB  ILE A 518     2096   2286   2561     89     74      8       C  
ATOM     45  CG1 ILE A 518      35.063 -27.127  14.578  1.00 21.07           C  
ANISOU   45  CG1 ILE A 518     2433   2610   2963    109     45     32       C  
ATOM     46  CG2 ILE A 518      33.085 -26.429  13.079  1.00 21.73           C  
ANISOU   46  CG2 ILE A 518     2574   2732   2951     66     62     -1       C  
ATOM     47  CD1 ILE A 518      34.514 -26.688  15.910  1.00 22.78           C  
ANISOU   47  CD1 ILE A 518     2657   2840   3159    100     -1     66       C  
ATOM     48  N   ARG A 519      34.131 -26.595  10.103  1.00 15.67           N  
ANISOU   48  N   ARG A 519     1829   1975   2149     70    160    -73       N  
ATOM     49  CA  ARG A 519      33.458 -26.000   8.974  1.00 15.92           C  
ANISOU   49  CA  ARG A 519     1896   2040   2111     50    169    -86       C  
ATOM     50  C   ARG A 519      31.968 -26.209   9.202  1.00 17.94           C  
ANISOU   50  C   ARG A 519     2176   2299   2339     29    122    -86       C  
ATOM     51  O   ARG A 519      31.532 -27.237   9.735  1.00 17.79           O  
ANISOU   51  O   ARG A 519     2159   2251   2351     29    105    -96       O  
ATOM     52  CB  ARG A 519      33.894 -26.640   7.665  1.00 19.70           C  
ANISOU   52  CB  ARG A 519     2403   2516   2565     55    220   -133       C  
ATOM     53  CG  ARG A 519      35.333 -26.329   7.312  1.00 28.35           C  
ANISOU   53  CG  ARG A 519     3470   3613   3689     74    280   -132       C  
ATOM     54  CD  ARG A 519      35.762 -27.066   6.062  1.00 48.48           C  
ANISOU   54  CD  ARG A 519     6050   6158   6213     83    342   -185       C  
ATOM     55  NE  ARG A 519      37.206 -26.955   5.852  1.00 60.62           N  
ANISOU   55  NE  ARG A 519     7547   7689   7798    106    409   -186       N  
ATOM     56  CZ  ARG A 519      38.093 -27.834   6.303  1.00 77.61           C  
ANISOU   56  CZ  ARG A 519     9656   9798  10033    136    433   -201       C  
ATOM     57  NH1 ARG A 519      37.695 -28.900   6.985  1.00 62.28           N  
ANISOU   57  NH1 ARG A 519     7716   7815   8133    147    395   -214       N  
ATOM     58  NH2 ARG A 519      39.385 -27.656   6.073  1.00 72.80           N  
ANISOU   58  NH2 ARG A 519     9000   9185   9474    157    494   -199       N  
ATOM     59  N   MET A 520      31.177 -25.205   8.864  1.00 13.33           N  
ANISOU   59  N   MET A 520     1606   1751   1709     13    101    -68       N  
ATOM     60  CA  MET A 520      29.722 -25.312   8.997  1.00 11.83           C  
ANISOU   60  CA  MET A 520     1426   1567   1500     -7     56    -66       C  
ATOM     61  C   MET A 520      29.034 -24.399   8.018  1.00 12.06           C  
ANISOU   61  C   MET A 520     1477   1634   1469    -20     41    -58       C  
ATOM     62  O   MET A 520      29.479 -23.274   7.778  1.00 11.37           O  
ANISOU   62  O   MET A 520     1388   1567   1364    -15     54    -31       O  
ATOM     63  CB  MET A 520      29.228 -24.979  10.416  1.00 12.39           C  
ANISOU   63  CB  MET A 520     1470   1631   1605     -6     29    -31       C  
ATOM     64  CG  MET A 520      29.516 -23.575  10.878  1.00 13.09           C  
ANISOU   64  CG  MET A 520     1542   1739   1691      1     27      3       C  
ATOM     65  SD  MET A 520      28.933 -23.202  12.587  1.00 17.09           S  
ANISOU   65  SD  MET A 520     2028   2239   2226      3      1     33       S  
ATOM     66  CE  MET A 520      30.260 -23.840  13.506  1.00 15.32           C  
ANISOU   66  CE  MET A 520     1788   1990   2041     21     11     36       C  
ATOM     67  N   LYS A 521      27.986 -24.897   7.426  1.00 12.62           N  
ANISOU   67  N   LYS A 521     1569   1713   1513    -39     10    -80       N  
ATOM     68  CA  LYS A 521      27.149 -24.065   6.566  1.00 12.26           C  
ANISOU   68  CA  LYS A 521     1541   1706   1412    -51    -22    -66       C  
ATOM     69  C   LYS A 521      26.056 -23.456   7.452  1.00 12.86           C  
ANISOU   69  C   LYS A 521     1583   1784   1520    -54    -62    -30       C  
ATOM     70  O   LYS A 521      25.580 -24.104   8.382  1.00 11.60           O  
ANISOU   70  O   LYS A 521     1400   1602   1407    -58    -71    -34       O  
ATOM     71  CB  LYS A 521      26.514 -24.904   5.458  1.00 15.53           C  
ANISOU   71  CB  LYS A 521     1992   2130   1780    -71    -46   -111       C  
ATOM     72  CG  LYS A 521      27.555 -25.389   4.467  1.00 18.79           C  
ANISOU   72  CG  LYS A 521     2446   2544   2149    -66      3   -151       C  
ATOM     73  CD  LYS A 521      26.899 -25.956   3.225  1.00 24.84           C  
ANISOU   73  CD  LYS A 521     3261   3330   2846    -88    -27   -198       C  
ATOM     74  CE  LYS A 521      27.939 -26.230   2.163  1.00 34.10           C  
ANISOU   74  CE  LYS A 521     4484   4513   3960    -80     32   -237       C  
ATOM     75  NZ  LYS A 521      27.834 -27.621   1.657  1.00 38.19           N  
ANISOU   75  NZ  LYS A 521     5036   5005   4470    -93     35   -316       N  
ATOM     76  N   PRO A 522      25.573 -22.252   7.144  1.00 10.02           N  
ANISOU   76  N   PRO A 522     1220   1450   1137    -51    -83      5       N  
ATOM     77  CA  PRO A 522      24.458 -21.688   7.915  1.00  9.71           C  
ANISOU   77  CA  PRO A 522     1145   1411   1134    -50   -115     34       C  
ATOM     78  C   PRO A 522      23.148 -22.397   7.562  1.00 12.34           C  
ANISOU   78  C   PRO A 522     1469   1752   1469    -71   -163     16       C  
ATOM     79  O   PRO A 522      23.088 -23.152   6.559  1.00 12.55           O  
ANISOU   79  O   PRO A 522     1525   1787   1455    -88   -180    -19       O  
ATOM     80  CB  PRO A 522      24.396 -20.237   7.425  1.00 11.63           C  
ANISOU   80  CB  PRO A 522     1392   1673   1352    -38   -124     75       C  
ATOM     81  CG  PRO A 522      24.904 -20.307   5.991  1.00 14.26           C  
ANISOU   81  CG  PRO A 522     1772   2031   1615    -44   -120     66       C  
ATOM     82  CD  PRO A 522      25.997 -21.359   6.043  1.00 11.73           C  
ANISOU   82  CD  PRO A 522     1467   1694   1297    -46    -74     25       C  
ATOM     83  N   ASP A 523      22.102 -22.130   8.381  1.00 10.77           N  
ANISOU   83  N   ASP A 523     1228   1549   1317    -71   -183     36       N  
ATOM     84  CA  ASP A 523      20.791 -22.611   8.043  1.00 10.63           C  
ANISOU   84  CA  ASP A 523     1187   1540   1314    -92   -231     26       C  
ATOM     85  C   ASP A 523      20.269 -21.797   6.849  1.00 16.06           C  
ANISOU   85  C   ASP A 523     1885   2262   1956    -90   -281     45       C  
ATOM     86  O   ASP A 523      20.958 -20.897   6.352  1.00 15.17           O  
ANISOU   86  O   ASP A 523     1800   2162   1801    -73   -268     69       O  
ATOM     87  CB  ASP A 523      19.868 -22.599   9.272  1.00 12.06           C  
ANISOU   87  CB  ASP A 523     1314   1705   1564    -92   -226     44       C  
ATOM     88  CG  ASP A 523      19.498 -21.245   9.824  1.00 12.65           C  
ANISOU   88  CG  ASP A 523     1359   1787   1660    -65   -220     84       C  
ATOM     89  OD1 ASP A 523      19.695 -20.247   9.122  1.00 13.05           O  
ANISOU   89  OD1 ASP A 523     1424   1853   1679    -50   -236    106       O  
ATOM     90  OD2 ASP A 523      18.979 -21.197  10.954  1.00 15.47           O  
ANISOU   90  OD2 ASP A 523     1681   2131   2066    -60   -197     95       O  
ATOM     91  N   GLU A 524      19.064 -22.126   6.374  1.00 15.71           N  
ANISOU   91  N   GLU A 524     1815   2231   1921   -110   -340     38       N  
ATOM     92  CA  GLU A 524      18.481 -21.458   5.211  1.00 16.97           C  
ANISOU   92  CA  GLU A 524     1985   2428   2035   -109   -403     59       C  
ATOM     93  C   GLU A 524      18.291 -19.971   5.396  1.00 21.92           C  
ANISOU   93  C   GLU A 524     2590   3061   2677    -76   -405    119       C  
ATOM     94  O   GLU A 524      18.268 -19.222   4.401  1.00 23.33           O  
ANISOU   94  O   GLU A 524     2796   3266   2803    -66   -440    149       O  
ATOM     95  CB  GLU A 524      17.188 -22.157   4.819  1.00 18.63           C  
ANISOU   95  CB  GLU A 524     2161   2649   2269   -139   -474     38       C  
ATOM     96  CG  GLU A 524      17.430 -23.546   4.240  1.00 22.01           C  
ANISOU   96  CG  GLU A 524     2627   3070   2664   -175   -484    -28       C  
ATOM     97  CD  GLU A 524      16.182 -24.304   3.812  1.00 30.00           C  
ANISOU   97  CD  GLU A 524     3606   4090   3704   -213   -561    -57       C  
ATOM     98  OE1 GLU A 524      15.079 -23.718   3.862  1.00 27.47           O  
ANISOU   98  OE1 GLU A 524     3226   3785   3426   -211   -613    -22       O  
ATOM     99  OE2 GLU A 524      16.298 -25.515   3.526  1.00 33.79           O  
ANISOU   99  OE2 GLU A 524     4111   4550   4176   -246   -565   -117       O  
ATOM    100  N   ASN A 525      18.250 -19.520   6.656  1.00 15.92           N  
ANISOU  100  N   ASN A 525     1791   2275   1984    -57   -362    136       N  
ATOM    101  CA  ASN A 525      18.149 -18.119   7.004  1.00 15.67           C  
ANISOU  101  CA  ASN A 525     1739   2236   1978    -23   -352    183       C  
ATOM    102  C   ASN A 525      19.440 -17.435   7.432  1.00 16.78           C  
ANISOU  102  C   ASN A 525     1913   2358   2105     -6   -292    193       C  
ATOM    103  O   ASN A 525      19.401 -16.346   8.003  1.00 17.49           O  
ANISOU  103  O   ASN A 525     1985   2430   2232     19   -274    222       O  
ATOM    104  CB  ASN A 525      16.989 -17.844   7.932  1.00 16.65           C  
ANISOU  104  CB  ASN A 525     1792   2347   2186    -12   -356    196       C  
ATOM    105  CG  ASN A 525      15.683 -17.969   7.186  1.00 25.18           C  
ANISOU  105  CG  ASN A 525     2832   3451   3286    -21   -431    208       C  
ATOM    106  OD1 ASN A 525      15.242 -17.040   6.491  1.00 23.32           O  
ANISOU  106  OD1 ASN A 525     2587   3228   3045      0   -478    249       O  
ATOM    107  ND2 ASN A 525      15.136 -19.168   7.160  1.00 16.16           N  
ANISOU  107  ND2 ASN A 525     1668   2313   2158    -55   -453    172       N  
ATOM    108  N   GLY A 526      20.584 -18.079   7.162  1.00 13.18           N  
ANISOU  108  N   GLY A 526     1503   1903   1603    -19   -261    166       N  
ATOM    109  CA  GLY A 526      21.895 -17.473   7.343  1.00 12.98           C  
ANISOU  109  CA  GLY A 526     1505   1863   1563     -8   -211    176       C  
ATOM    110  C   GLY A 526      22.465 -17.531   8.749  1.00 13.62           C  
ANISOU  110  C   GLY A 526     1568   1915   1691     -1   -165    161       C  
ATOM    111  O   GLY A 526      23.474 -16.874   9.046  1.00 15.53           O  
ANISOU  111  O   GLY A 526     1822   2143   1936      7   -132    170       O  
ATOM    112  N   ARG A 527      21.817 -18.287   9.638  1.00 11.67           N  
ANISOU  112  N   ARG A 527     1293   1661   1481     -8   -166    141       N  
ATOM    113  CA  ARG A 527      22.214 -18.348  11.043  1.00 10.88           C  
ANISOU  113  CA  ARG A 527     1180   1538   1415     -1   -128    132       C  
ATOM    114  C   ARG A 527      22.953 -19.624  11.377  1.00 10.60           C  
ANISOU  114  C   ARG A 527     1159   1494   1372    -15   -108    103       C  
ATOM    115  O   ARG A 527      22.660 -20.696  10.828  1.00 10.51           O  
ANISOU  115  O   ARG A 527     1154   1488   1351    -33   -123     83       O  
ATOM    116  CB  ARG A 527      21.016 -18.197  11.956  1.00 13.01           C  
ANISOU  116  CB  ARG A 527     1409   1803   1731      5   -129    138       C  
ATOM    117  CG  ARG A 527      20.313 -16.852  11.684  1.00 15.73           C  
ANISOU  117  CG  ARG A 527     1732   2147   2097     27   -146    168       C  
ATOM    118  CD  ARG A 527      19.251 -16.528  12.727  1.00 25.28           C  
ANISOU  118  CD  ARG A 527     2898   3347   3360     41   -130    171       C  
ATOM    119  NE  ARG A 527      18.508 -15.311  12.381  1.00 34.04           N  
ANISOU  119  NE  ARG A 527     3981   4451   4502     67   -148    200       N  
ATOM    120  CZ  ARG A 527      17.343 -15.290  11.734  1.00 47.67           C  
ANISOU  120  CZ  ARG A 527     5668   6190   6255     70   -190    218       C  
ATOM    121  NH1 ARG A 527      16.752 -16.425  11.373  1.00 26.81           N  
ANISOU  121  NH1 ARG A 527     3007   3568   3611     44   -218    206       N  
ATOM    122  NH2 ARG A 527      16.750 -14.135  11.462  1.00 41.28           N  
ANISOU  122  NH2 ARG A 527     4834   5371   5482     99   -207    249       N  
ATOM    123  N   PHE A 528      23.904 -19.503  12.281  1.00  8.72           N  
ANISOU  123  N   PHE A 528      929   1242   1144     -6    -79    101       N  
ATOM    124  CA  PHE A 528      24.753 -20.634  12.676  1.00  8.16           C  
ANISOU  124  CA  PHE A 528      869   1158   1073    -13    -62     82       C  
ATOM    125  C   PHE A 528      24.363 -21.220  14.031  1.00  8.88           C  
ANISOU  125  C   PHE A 528      948   1237   1190    -14    -52     83       C  
ATOM    126  O   PHE A 528      24.656 -22.395  14.247  1.00  9.87           O  
ANISOU  126  O   PHE A 528     1080   1348   1323    -21    -46     73       O  
ATOM    127  CB  PHE A 528      26.200 -20.189  12.727  1.00  8.83           C  
ANISOU  127  CB  PHE A 528      965   1236   1152     -3    -42     82       C  
ATOM    128  CG  PHE A 528      26.744 -19.815  11.375  1.00  8.31           C  
ANISOU  128  CG  PHE A 528      917   1183   1058     -5    -37     83       C  
ATOM    129  CD1 PHE A 528      27.113 -20.796  10.455  1.00  9.52           C  
ANISOU  129  CD1 PHE A 528     1089   1340   1190    -12    -30     60       C  
ATOM    130  CD2 PHE A 528      26.878 -18.487  11.015  1.00  9.42           C  
ANISOU  130  CD2 PHE A 528     1058   1327   1193      1    -36    107       C  
ATOM    131  CE1 PHE A 528      27.642 -20.455   9.217  1.00 11.27           C  
ANISOU  131  CE1 PHE A 528     1333   1576   1373    -14    -16     61       C  
ATOM    132  CE2 PHE A 528      27.373 -18.138   9.752  1.00 10.39           C  
ANISOU  132  CE2 PHE A 528     1202   1463   1283     -2    -25    116       C  
ATOM    133  CZ  PHE A 528      27.749 -19.123   8.859  1.00 10.12           C  
ANISOU  133  CZ  PHE A 528     1189   1439   1216    -10    -14     93       C  
ATOM    134  N   GLY A 529      23.777 -20.435  14.933  1.00  7.35           N  
ANISOU  134  N   GLY A 529      739   1044   1008     -5    -45     96       N  
ATOM    135  CA  GLY A 529      23.320 -20.988  16.206  1.00  8.47           C  
ANISOU  135  CA  GLY A 529      876   1180   1164     -7    -28    100       C  
ATOM    136  C   GLY A 529      24.267 -20.849  17.366  1.00 10.52           C  
ANISOU  136  C   GLY A 529     1153   1432   1410      3    -15    102       C  
ATOM    137  O   GLY A 529      24.019 -21.453  18.410  1.00 11.88           O  
ANISOU  137  O   GLY A 529     1330   1601   1581      1     -1    110       O  
ATOM    138  N   PHE A 530      25.345 -20.082  17.223  1.00  7.72           N  
ANISOU  138  N   PHE A 530      808   1077   1047     12    -21     97       N  
ATOM    139  CA  PHE A 530      26.260 -19.845  18.314  1.00  7.61           C  
ANISOU  139  CA  PHE A 530      809   1060   1024     20    -21     95       C  
ATOM    140  C   PHE A 530      26.316 -18.374  18.627  1.00  9.47           C  
ANISOU  140  C   PHE A 530     1045   1295   1258     28    -20     87       C  
ATOM    141  O   PHE A 530      26.033 -17.519  17.778  1.00  9.03           O  
ANISOU  141  O   PHE A 530      979   1236   1214     30    -20     88       O  
ATOM    142  CB  PHE A 530      27.647 -20.444  18.053  1.00  8.58           C  
ANISOU  142  CB  PHE A 530      935   1174   1151     20    -32     93       C  
ATOM    143  CG  PHE A 530      28.458 -19.756  16.986  1.00  7.63           C  
ANISOU  143  CG  PHE A 530      806   1053   1040     20    -33     86       C  
ATOM    144  CD1 PHE A 530      29.424 -18.808  17.326  1.00  9.83           C  
ANISOU  144  CD1 PHE A 530     1081   1328   1327     23    -40     83       C  
ATOM    145  CD2 PHE A 530      28.276 -20.071  15.642  1.00  9.11           C  
ANISOU  145  CD2 PHE A 530      992   1243   1225     15    -27     84       C  
ATOM    146  CE1 PHE A 530      30.181 -18.183  16.343  1.00 10.84           C  
ANISOU  146  CE1 PHE A 530     1198   1452   1468     19    -32     83       C  
ATOM    147  CE2 PHE A 530      29.050 -19.455  14.658  1.00  9.42           C  
ANISOU  147  CE2 PHE A 530     1029   1285   1265     15    -18     84       C  
ATOM    148  CZ  PHE A 530      29.988 -18.497  15.015  1.00 10.18           C  
ANISOU  148  CZ  PHE A 530     1117   1374   1377     16    -17     87       C  
ATOM    149  N   ASN A 531      26.674 -18.108  19.885  1.00  8.65           N  
ANISOU  149  N   ASN A 531      957   1191   1138     31    -20     79       N  
ATOM    150  CA  ASN A 531      26.886 -16.730  20.323  1.00  8.62           C  
ANISOU  150  CA  ASN A 531      960   1179   1135     37    -21     61       C  
ATOM    151  C   ASN A 531      28.337 -16.580  20.663  1.00  9.33           C  
ANISOU  151  C   ASN A 531     1056   1265   1225     31    -47     52       C  
ATOM    152  O   ASN A 531      29.015 -17.537  21.022  1.00  9.67           O  
ANISOU  152  O   ASN A 531     1102   1314   1258     29    -63     60       O  
ATOM    153  CB  ASN A 531      26.102 -16.440  21.619  1.00  9.80           C  
ANISOU  153  CB  ASN A 531     1129   1335   1261     44     -1     49       C  
ATOM    154  CG  ASN A 531      24.624 -16.522  21.504  1.00 10.53           C  
ANISOU  154  CG  ASN A 531     1206   1432   1364     50     30     57       C  
ATOM    155  OD1 ASN A 531      24.058 -16.913  20.491  1.00 10.98           O  
ANISOU  155  OD1 ASN A 531     1237   1490   1445     47     29     73       O  
ATOM    156  ND2 ASN A 531      23.949 -16.264  22.620  1.00 14.23           N  
ANISOU  156  ND2 ASN A 531     1689   1906   1812     58     60     44       N  
ATOM    157  N   VAL A 532      28.822 -15.331  20.572  1.00  9.18           N  
ANISOU  157  N   VAL A 532     1034   1230   1223     29    -54     36       N  
ATOM    158  CA  VAL A 532      30.190 -15.037  20.996  1.00  9.64           C  
ANISOU  158  CA  VAL A 532     1091   1281   1291     19    -83     23       C  
ATOM    159  C   VAL A 532      30.219 -13.855  21.962  1.00 10.12           C  
ANISOU  159  C   VAL A 532     1171   1330   1346     15    -92    -10       C  
ATOM    160  O   VAL A 532      29.350 -12.983  21.894  1.00  9.25           O  
ANISOU  160  O   VAL A 532     1068   1204   1243     22    -69    -22       O  
ATOM    161  CB  VAL A 532      31.145 -14.716  19.822  1.00 12.93           C  
ANISOU  161  CB  VAL A 532     1478   1684   1749      9    -84     33       C  
ATOM    162  CG1 VAL A 532      31.375 -15.949  18.941  1.00 13.58           C  
ANISOU  162  CG1 VAL A 532     1547   1779   1834     13    -75     55       C  
ATOM    163  CG2 VAL A 532      30.661 -13.521  18.985  1.00 14.07           C  
ANISOU  163  CG2 VAL A 532     1619   1808   1918      8    -64     37       C  
ATOM    164  N   LYS A 533      31.215 -13.855  22.865  1.00  9.68           N  
ANISOU  164  N   LYS A 533     1124   1278   1278      6   -130    -28       N  
ATOM    165  CA  LYS A 533      31.566 -12.727  23.719  1.00 10.03           C  
ANISOU  165  CA  LYS A 533     1186   1305   1319     -5   -151    -70       C  
ATOM    166  C   LYS A 533      33.040 -12.429  23.409  1.00 11.09           C  
ANISOU  166  C   LYS A 533     1287   1426   1501    -25   -189    -73       C  
ATOM    167  O   LYS A 533      33.724 -13.262  22.775  1.00 10.57           O  
ANISOU  167  O   LYS A 533     1189   1370   1458    -25   -196    -43       O  
ATOM    168  CB  LYS A 533      31.433 -13.055  25.225  1.00 12.09           C  
ANISOU  168  CB  LYS A 533     1491   1591   1511     -2   -172    -92       C  
ATOM    169  CG  LYS A 533      29.992 -13.208  25.701  1.00 15.65           C  
ANISOU  169  CG  LYS A 533     1974   2055   1918     15   -124    -94       C  
ATOM    170  CD  LYS A 533      29.907 -13.623  27.149  1.00 17.24           C  
ANISOU  170  CD  LYS A 533     2225   2285   2041     17   -136   -108       C  
ATOM    171  CE  LYS A 533      28.485 -13.814  27.592  1.00 20.69           C  
ANISOU  171  CE  LYS A 533     2687   2735   2440     33    -76   -106       C  
ATOM    172  NZ  LYS A 533      28.428 -14.060  29.078  1.00 26.22           N  
ANISOU  172  NZ  LYS A 533     3447   3465   3051     33    -80   -122       N  
ATOM    173  N   GLY A 534      33.529 -11.276  23.861  1.00  9.59           N  
ANISOU  173  N   GLY A 534     1102   1211   1333    -43   -212   -111       N  
ATOM    174  CA  GLY A 534      34.942 -10.966  23.689  1.00 10.22           C  
ANISOU  174  CA  GLY A 534     1142   1275   1466    -68   -251   -116       C  
ATOM    175  C   GLY A 534      35.289 -10.148  22.456  1.00 12.26           C  
ANISOU  175  C   GLY A 534     1363   1497   1798    -82   -222   -100       C  
ATOM    176  O   GLY A 534      34.419  -9.726  21.689  1.00 10.37           O  
ANISOU  176  O   GLY A 534     1133   1242   1567    -71   -177    -84       O  
ATOM    177  N   GLY A 535      36.578  -9.941  22.271  1.00 11.19           N  
ANISOU  177  N   GLY A 535     1184   1349   1719   -107   -249   -100       N  
ATOM    178  CA  GLY A 535      37.094  -9.099  21.203  1.00 11.25           C  
ANISOU  178  CA  GLY A 535     1155   1319   1801   -127   -220    -83       C  
ATOM    179  C   GLY A 535      38.021  -8.055  21.803  1.00 11.10           C  
ANISOU  179  C   GLY A 535     1116   1263   1837   -164   -262   -122       C  
ATOM    180  O   GLY A 535      38.057  -7.826  23.022  1.00 11.72           O  
ANISOU  180  O   GLY A 535     1222   1344   1886   -172   -313   -170       O  
ATOM    181  N   TYR A 536      38.793  -7.409  20.950  1.00 10.66           N  
ANISOU  181  N   TYR A 536     1016   1174   1861   -190   -241   -102       N  
ATOM    182  CA  TYR A 536      39.812  -6.460  21.394  1.00 10.53           C  
ANISOU  182  CA  TYR A 536      966   1117   1916   -234   -282   -136       C  
ATOM    183  C   TYR A 536      39.233  -5.346  22.261  1.00 12.79           C  
ANISOU  183  C   TYR A 536     1302   1364   2194   -245   -304   -192       C  
ATOM    184  O   TYR A 536      39.847  -4.932  23.237  1.00 14.22           O  
ANISOU  184  O   TYR A 536     1481   1533   2390   -273   -366   -245       O  
ATOM    185  CB  TYR A 536      40.515  -5.862  20.181  1.00 13.69           C  
ANISOU  185  CB  TYR A 536     1315   1481   2406   -260   -234    -95       C  
ATOM    186  CG  TYR A 536      41.569  -4.851  20.536  1.00 17.24           C  
ANISOU  186  CG  TYR A 536     1722   1882   2948   -311   -270   -125       C  
ATOM    187  CD1 TYR A 536      42.850  -5.251  20.903  1.00 19.19           C  
ANISOU  187  CD1 TYR A 536     1902   2143   3245   -335   -319   -135       C  
ATOM    188  CD2 TYR A 536      41.298  -3.485  20.488  1.00 19.41           C  
ANISOU  188  CD2 TYR A 536     2017   2089   3270   -336   -256   -143       C  
ATOM    189  CE1 TYR A 536      43.826  -4.316  21.236  1.00 20.52           C  
ANISOU  189  CE1 TYR A 536     2023   2265   3508   -388   -358   -166       C  
ATOM    190  CE2 TYR A 536      42.248  -2.548  20.866  1.00 22.15           C  
ANISOU  190  CE2 TYR A 536     2326   2384   3708   -389   -293   -177       C  
ATOM    191  CZ  TYR A 536      43.514  -2.966  21.214  1.00 23.49           C  
ANISOU  191  CZ  TYR A 536     2427   2574   3927   -417   -345   -188       C  
ATOM    192  OH  TYR A 536      44.442  -2.006  21.511  1.00 24.55           O  
ANISOU  192  OH  TYR A 536     2515   2652   4161   -475   -382   -221       O  
ATOM    193  N   ASP A 537      38.036  -4.854  21.891  1.00 12.05           N  
ANISOU  193  N   ASP A 537     1252   1248   2077   -222   -254   -184       N  
ATOM    194  CA  ASP A 537      37.372  -3.792  22.648  1.00 11.15           C  
ANISOU  194  CA  ASP A 537     1188   1090   1960   -224   -262   -240       C  
ATOM    195  C   ASP A 537      36.865  -4.255  24.006  1.00 13.62           C  
ANISOU  195  C   ASP A 537     1551   1441   2182   -206   -299   -294       C  
ATOM    196  O   ASP A 537      36.618  -3.407  24.872  1.00 13.94           O  
ANISOU  196  O   ASP A 537     1632   1448   2217   -216   -317   -358       O  
ATOM    197  CB  ASP A 537      36.209  -3.260  21.818  1.00 10.82           C  
ANISOU  197  CB  ASP A 537     1170   1018   1925   -196   -197   -206       C  
ATOM    198  CG  ASP A 537      35.219  -4.293  21.353  1.00 10.31           C  
ANISOU  198  CG  ASP A 537     1119   1007   1792   -152   -164   -163       C  
ATOM    199  OD1 ASP A 537      35.641  -5.429  21.030  1.00 10.25           O  
ANISOU  199  OD1 ASP A 537     1088   1050   1757   -148   -169   -131       O  
ATOM    200  OD2 ASP A 537      34.017  -3.952  21.236  1.00 11.35           O  
ANISOU  200  OD2 ASP A 537     1281   1124   1907   -122   -131   -159       O  
ATOM    201  N   GLN A 538      36.718  -5.556  24.207  1.00 12.36           N  
ANISOU  201  N   GLN A 538     1395   1347   1954   -182   -307   -270       N  
ATOM    202  CA  GLN A 538      36.286  -6.123  25.479  1.00 12.35           C  
ANISOU  202  CA  GLN A 538     1444   1388   1860   -167   -339   -307       C  
ATOM    203  C   GLN A 538      37.501  -6.588  26.307  1.00 16.63           C  
ANISOU  203  C   GLN A 538     1969   1960   2391   -191   -421   -328       C  
ATOM    204  O   GLN A 538      37.314  -7.059  27.428  1.00 18.67           O  
ANISOU  204  O   GLN A 538     2272   2256   2565   -183   -458   -356       O  
ATOM    205  CB  GLN A 538      35.304  -7.265  25.264  1.00 11.20           C  
ANISOU  205  CB  GLN A 538     1316   1290   1648   -126   -299   -264       C  
ATOM    206  CG  GLN A 538      33.992  -6.768  24.645  1.00 11.32           C  
ANISOU  206  CG  GLN A 538     1351   1281   1671   -100   -230   -251       C  
ATOM    207  CD  GLN A 538      32.953  -7.853  24.611  1.00 11.22           C  
ANISOU  207  CD  GLN A 538     1354   1314   1594    -66   -197   -219       C  
ATOM    208  OE1 GLN A 538      33.069  -8.905  25.285  1.00 12.51           O  
ANISOU  208  OE1 GLN A 538     1531   1524   1697    -60   -221   -214       O  
ATOM    209  NE2 GLN A 538      31.937  -7.637  23.806  1.00 10.79           N  
ANISOU  209  NE2 GLN A 538     1297   1246   1558    -44   -146   -192       N  
ATOM    210  N   LYS A 539      38.717  -6.503  25.728  1.00 14.79           N  
ANISOU  210  N   LYS A 539     1668   1710   2241   -220   -447   -308       N  
ATOM    211  CA  LYS A 539      39.969  -6.899  26.396  1.00 15.08           C  
ANISOU  211  CA  LYS A 539     1669   1771   2291   -245   -531   -322       C  
ATOM    212  C   LYS A 539      39.939  -8.347  26.807  1.00 19.18           C  
ANISOU  212  C   LYS A 539     2196   2353   2738   -213   -555   -287       C  
ATOM    213  O   LYS A 539      40.492  -8.741  27.845  1.00 19.51           O  
ANISOU  213  O   LYS A 539     2247   2427   2740   -219   -633   -307       O  
ATOM    214  CB  LYS A 539      40.301  -6.001  27.612  1.00 18.14           C  
ANISOU  214  CB  LYS A 539     2091   2140   2664   -278   -603   -402       C  
ATOM    215  CG  LYS A 539      40.329  -4.517  27.322  1.00 23.58           C  
ANISOU  215  CG  LYS A 539     2776   2752   3429   -312   -583   -444       C  
ATOM    216  CD  LYS A 539      40.585  -3.776  28.637  1.00 35.83           C  
ANISOU  216  CD  LYS A 539     4374   4290   4950   -343   -659   -535       C  
ATOM    217  CE  LYS A 539      39.664  -2.603  28.878  1.00 46.60           C  
ANISOU  217  CE  LYS A 539     5801   5597   6307   -343   -616   -596       C  
ATOM    218  NZ  LYS A 539      39.858  -1.528  27.868  1.00 45.37           N  
ANISOU  218  NZ  LYS A 539     5602   5359   6276   -368   -571   -584       N  
ATOM    219  N   MET A 540      39.247  -9.157  25.995  1.00 16.74           N  
ANISOU  219  N   MET A 540     1887   2062   2412   -179   -489   -234       N  
ATOM    220  CA AMET A 540      39.241 -10.578  26.254  0.50 17.09           C  
ANISOU  220  CA AMET A 540     1933   2155   2404   -150   -504   -196       C  
ATOM    221  CA BMET A 540      39.046 -10.579  26.253  0.50 16.03           C  
ANISOU  221  CA BMET A 540     1808   2022   2261   -147   -496   -196       C  
ATOM    222  C   MET A 540      39.165 -11.350  24.965  1.00 17.92           C  
ANISOU  222  C   MET A 540     1998   2262   2547   -129   -443   -139       C  
ATOM    223  O   MET A 540      38.767 -10.804  23.923  1.00 15.46           O  
ANISOU  223  O   MET A 540     1677   1924   2273   -131   -381   -127       O  
ATOM    224  CB AMET A 540      38.204 -10.996  27.303  0.50 20.22           C  
ANISOU  224  CB AMET A 540     2409   2584   2689   -127   -507   -210       C  
ATOM    225  CB BMET A 540      37.617 -10.803  26.806  0.50 18.00           C  
ANISOU  225  CB BMET A 540     2135   2291   2415   -120   -460   -204       C  
ATOM    226  CG AMET A 540      36.804 -10.729  26.908  0.50 24.00           C  
ANISOU  226  CG AMET A 540     2929   3052   3138   -108   -428   -209       C  
ATOM    227  CG BMET A 540      37.418 -10.331  28.252  0.50 22.77           C  
ANISOU  227  CG BMET A 540     2802   2907   2941   -129   -506   -260       C  
ATOM    228  SD AMET A 540      35.733 -11.350  28.207  0.50 29.80           S  
ANISOU  228  SD AMET A 540     3746   3830   3748    -84   -425   -220       S  
ATOM    229  SD BMET A 540      38.580 -11.021  29.467  0.50 29.11           S  
ANISOU  229  SD BMET A 540     3606   3753   3703   -140   -619   -264       S  
ATOM    230  CE AMET A 540      34.171 -10.875  27.534  0.50 24.78           C  
ANISOU  230  CE AMET A 540     3130   3172   3114    -64   -329   -219       C  
ATOM    231  CE BMET A 540      38.097 -12.739  29.476  0.50 25.43           C  
ANISOU  231  CE BMET A 540     3153   3331   3179    -98   -597   -191       C  
ATOM    232  N   PRO A 541      39.603 -12.629  24.967  1.00 16.60           N  
ANISOU  232  N   PRO A 541     1807   2125   2376   -108   -461   -102       N  
ATOM    233  CA  PRO A 541      39.577 -13.369  23.705  1.00 14.45           C  
ANISOU  233  CA  PRO A 541     1499   1852   2140    -90   -400    -58       C  
ATOM    234  C   PRO A 541      38.122 -13.608  23.254  1.00 14.26           C  
ANISOU  234  C   PRO A 541     1527   1833   2060    -69   -337    -46       C  
ATOM    235  O   PRO A 541      37.166 -13.543  24.067  1.00 13.48           O  
ANISOU  235  O   PRO A 541     1484   1745   1891    -61   -340    -62       O  
ATOM    236  CB  PRO A 541      40.227 -14.712  24.055  1.00 17.90           C  
ANISOU  236  CB  PRO A 541     1911   2314   2578    -68   -439    -29       C  
ATOM    237  CG  PRO A 541      40.040 -14.849  25.540  1.00 24.64           C  
ANISOU  237  CG  PRO A 541     2814   3191   3356    -66   -507    -45       C  
ATOM    238  CD  PRO A 541      40.148 -13.462  26.073  1.00 19.04           C  
ANISOU  238  CD  PRO A 541     2120   2466   2647    -99   -537    -97       C  
ATOM    239  N   VAL A 542      37.949 -13.834  21.944  1.00 11.88           N  
ANISOU  239  N   VAL A 542     1203   1522   1788    -61   -277    -19       N  
ATOM    240  CA  VAL A 542      36.635 -14.170  21.410  1.00 11.44           C  
ANISOU  240  CA  VAL A 542     1185   1473   1687    -43   -226     -4       C  
ATOM    241  C   VAL A 542      36.307 -15.595  21.841  1.00 12.52           C  
ANISOU  241  C   VAL A 542     1339   1635   1782    -19   -235     15       C  
ATOM    242  O   VAL A 542      37.087 -16.514  21.577  1.00 12.08           O  
ANISOU  242  O   VAL A 542     1250   1584   1756    -10   -243     34       O  
ATOM    243  CB  VAL A 542      36.559 -13.993  19.885  1.00 13.91           C  
ANISOU  243  CB  VAL A 542     1478   1775   2034    -44   -169     18       C  
ATOM    244  CG1 VAL A 542      35.222 -14.479  19.357  1.00 12.81           C  
ANISOU  244  CG1 VAL A 542     1372   1646   1848    -26   -132     32       C  
ATOM    245  CG2 VAL A 542      36.765 -12.524  19.521  1.00 15.09           C  
ANISOU  245  CG2 VAL A 542     1618   1893   2224    -67   -158      8       C  
ATOM    246  N   ILE A 543      35.234 -15.768  22.588  1.00 11.78           N  
ANISOU  246  N   ILE A 543     1294   1555   1628    -10   -234     10       N  
ATOM    247  CA  ILE A 543      34.833 -17.081  23.152  1.00 10.92           C  
ANISOU  247  CA  ILE A 543     1207   1466   1477      8   -240     33       C  
ATOM    248  C   ILE A 543      33.403 -17.378  22.731  1.00 12.74           C  
ANISOU  248  C   ILE A 543     1464   1699   1678     17   -190     42       C  
ATOM    249  O   ILE A 543      32.535 -16.481  22.745  1.00 13.31           O  
ANISOU  249  O   ILE A 543     1555   1768   1735     13   -167     24       O  
ATOM    250  CB  ILE A 543      34.933 -17.071  24.722  1.00 16.14           C  
ANISOU  250  CB  ILE A 543     1905   2145   2083      7   -291     22       C  
ATOM    251  CG1 ILE A 543      36.326 -16.620  25.234  1.00 18.89           C  
ANISOU  251  CG1 ILE A 543     2225   2491   2460     -6   -356      6       C  
ATOM    252  CG2 ILE A 543      34.524 -18.427  25.385  1.00 20.22           C  
ANISOU  252  CG2 ILE A 543     2450   2678   2553     25   -296     57       C  
ATOM    253  CD1 ILE A 543      37.442 -17.621  25.120  1.00 28.20           C  
ANISOU  253  CD1 ILE A 543     3359   3672   3683      5   -392     37       C  
ATOM    254  N   VAL A 544      33.136 -18.663  22.438  1.00 10.46           N  
ANISOU  254  N   VAL A 544     1174   1413   1387     29   -176     68       N  
ATOM    255  CA  VAL A 544      31.772 -19.105  22.151  1.00 10.13           C  
ANISOU  255  CA  VAL A 544     1152   1375   1322     32   -137     78       C  
ATOM    256  C   VAL A 544      31.061 -19.153  23.485  1.00 12.45           C  
ANISOU  256  C   VAL A 544     1485   1683   1562     34   -140     79       C  
ATOM    257  O   VAL A 544      31.490 -19.862  24.414  1.00 12.11           O  
ANISOU  257  O   VAL A 544     1459   1649   1493     39   -168     96       O  
ATOM    258  CB  VAL A 544      31.793 -20.487  21.481  1.00 11.57           C  
ANISOU  258  CB  VAL A 544     1323   1549   1525     40   -125    100       C  
ATOM    259  CG1 VAL A 544      30.364 -20.991  21.259  1.00 11.18           C  
ANISOU  259  CG1 VAL A 544     1289   1501   1458     38    -92    108       C  
ATOM    260  CG2 VAL A 544      32.539 -20.393  20.153  1.00 11.73           C  
ANISOU  260  CG2 VAL A 544     1310   1558   1590     39   -112     93       C  
ATOM    261  N   SER A 545      29.965 -18.398  23.612  1.00 10.11           N  
ANISOU  261  N   SER A 545     1205   1391   1247     32   -110     63       N  
ATOM    262  CA  SER A 545      29.248 -18.311  24.864  1.00  9.54           C  
ANISOU  262  CA  SER A 545     1172   1334   1120     35    -98     59       C  
ATOM    263  C   SER A 545      27.966 -19.130  24.925  1.00 12.03           C  
ANISOU  263  C   SER A 545     1494   1655   1423     37    -55     82       C  
ATOM    264  O   SER A 545      27.409 -19.327  26.017  1.00 13.28           O  
ANISOU  264  O   SER A 545     1686   1829   1532     39    -37     89       O  
ATOM    265  CB  SER A 545      28.959 -16.846  25.166  1.00 11.99           C  
ANISOU  265  CB  SER A 545     1494   1640   1422     33    -89     18       C  
ATOM    266  OG  SER A 545      28.298 -16.254  24.057  1.00 11.80           O  
ANISOU  266  OG  SER A 545     1442   1599   1442     35    -59     15       O  
ATOM    267  N   ARG A 546      27.452 -19.581  23.762  1.00  8.37           N  
ANISOU  267  N   ARG A 546      999   1180   1001     35    -36     94       N  
ATOM    268  CA  ARG A 546      26.242 -20.386  23.716  1.00  8.80           C  
ANISOU  268  CA  ARG A 546     1050   1236   1059     31     -1    115       C  
ATOM    269  C   ARG A 546      26.237 -21.112  22.388  1.00  9.81           C  
ANISOU  269  C   ARG A 546     1148   1349   1231     25     -6    123       C  
ATOM    270  O   ARG A 546      26.712 -20.577  21.370  1.00  9.44           O  
ANISOU  270  O   ARG A 546     1083   1297   1208     26    -19    109       O  
ATOM    271  CB  ARG A 546      24.979 -19.487  23.785  1.00 11.29           C  
ANISOU  271  CB  ARG A 546     1357   1557   1377     34     38     99       C  
ATOM    272  CG  ARG A 546      23.713 -20.313  24.012  1.00 18.08           C  
ANISOU  272  CG  ARG A 546     2208   2421   2243     28     78    122       C  
ATOM    273  CD  ARG A 546      22.458 -19.497  24.259  1.00 30.78           C  
ANISOU  273  CD  ARG A 546     3800   4035   3860     35    123    108       C  
ATOM    274  NE  ARG A 546      21.305 -20.401  24.271  1.00 43.48           N  
ANISOU  274  NE  ARG A 546     5384   5643   5491     23    158    134       N  
ATOM    275  CZ  ARG A 546      20.528 -20.641  23.219  1.00 57.42           C  
ANISOU  275  CZ  ARG A 546     7103   7401   7312     14    155    139       C  
ATOM    276  NH1 ARG A 546      20.717 -19.983  22.080  1.00 34.55           N  
ANISOU  276  NH1 ARG A 546     4186   4500   4442     21    122    124       N  
ATOM    277  NH2 ARG A 546      19.532 -21.514  23.309  1.00 46.25           N  
ANISOU  277  NH2 ARG A 546     5663   5984   5924     -2    184    161       N  
ATOM    278  N   VAL A 547      25.707 -22.334  22.391  1.00  9.25           N  
ANISOU  278  N   VAL A 547     1075   1270   1170     17      7    146       N  
ATOM    279  CA  VAL A 547      25.478 -23.114  21.185  1.00  9.01           C  
ANISOU  279  CA  VAL A 547     1023   1224   1178      8      6    146       C  
ATOM    280  C   VAL A 547      24.053 -23.628  21.328  1.00 11.60           C  
ANISOU  280  C   VAL A 547     1338   1549   1519     -7     35    159       C  
ATOM    281  O   VAL A 547      23.748 -24.339  22.307  1.00 12.19           O  
ANISOU  281  O   VAL A 547     1428   1620   1583    -12     54    185       O  
ATOM    282  CB  VAL A 547      26.474 -24.254  21.009  1.00 10.80           C  
ANISOU  282  CB  VAL A 547     1255   1429   1421     10    -13    157       C  
ATOM    283  CG1 VAL A 547      26.087 -25.117  19.798  1.00 12.28           C  
ANISOU  283  CG1 VAL A 547     1427   1596   1644     -2     -9    147       C  
ATOM    284  CG2 VAL A 547      27.908 -23.712  20.867  1.00 10.78           C  
ANISOU  284  CG2 VAL A 547     1251   1428   1416     24    -39    145       C  
ATOM    285  N   ALA A 548      23.180 -23.273  20.380  1.00  9.53           N  
ANISOU  285  N   ALA A 548     1047   1291   1283    -14     37    145       N  
ATOM    286  CA  ALA A 548      21.772 -23.639  20.449  1.00 10.08           C  
ANISOU  286  CA  ALA A 548     1091   1361   1379    -30     61    155       C  
ATOM    287  C   ALA A 548      21.487 -25.049  19.883  1.00 10.15           C  
ANISOU  287  C   ALA A 548     1090   1345   1423    -54     55    161       C  
ATOM    288  O   ALA A 548      22.062 -25.456  18.861  1.00 10.00           O  
ANISOU  288  O   ALA A 548     1074   1314   1412    -57     27    143       O  
ATOM    289  CB  ALA A 548      20.929 -22.607  19.724  1.00 11.43           C  
ANISOU  289  CB  ALA A 548     1229   1546   1569    -26     57    141       C  
ATOM    290  N   PRO A 549      20.572 -25.783  20.512  1.00  9.56           N  
ANISOU  290  N   PRO A 549     1003   1260   1370    -73     84    184       N  
ATOM    291  CA  PRO A 549      20.291 -27.144  20.040  1.00  9.27           C  
ANISOU  291  CA  PRO A 549      958   1190   1376   -100     77    187       C  
ATOM    292  C   PRO A 549      19.773 -27.213  18.601  1.00  9.85           C  
ANISOU  292  C   PRO A 549     1001   1260   1480   -117     44    155       C  
ATOM    293  O   PRO A 549      18.931 -26.413  18.217  1.00 10.63           O  
ANISOU  293  O   PRO A 549     1066   1383   1589   -118     38    147       O  
ATOM    294  CB  PRO A 549      19.182 -27.642  20.992  1.00 11.87           C  
ANISOU  294  CB  PRO A 549     1269   1512   1730   -120    123    221       C  
ATOM    295  CG  PRO A 549      19.321 -26.791  22.243  1.00 15.73           C  
ANISOU  295  CG  PRO A 549     1780   2029   2167    -97    157    239       C  
ATOM    296  CD  PRO A 549      19.795 -25.441  21.725  1.00 10.33           C  
ANISOU  296  CD  PRO A 549     1097   1371   1456    -71    130    206       C  
ATOM    297  N   GLY A 550      20.328 -28.138  17.815  1.00  9.60           N  
ANISOU  297  N   GLY A 550      985   1201   1462   -128     21    135       N  
ATOM    298  CA  GLY A 550      19.834 -28.422  16.469  1.00  9.98           C  
ANISOU  298  CA  GLY A 550     1016   1246   1532   -150    -14     99       C  
ATOM    299  C   GLY A 550      20.229 -27.424  15.416  1.00 11.17           C  
ANISOU  299  C   GLY A 550     1172   1428   1643   -132    -44     73       C  
ATOM    300  O   GLY A 550      19.704 -27.485  14.301  1.00 12.22           O  
ANISOU  300  O   GLY A 550     1294   1568   1780   -150    -78     47       O  
ATOM    301  N   THR A 551      21.132 -26.529  15.741  1.00  8.90           N  
ANISOU  301  N   THR A 551      904   1158   1318   -102    -35     82       N  
ATOM    302  CA  THR A 551      21.626 -25.541  14.809  1.00  9.16           C  
ANISOU  302  CA  THR A 551      946   1217   1316    -86    -55     67       C  
ATOM    303  C   THR A 551      22.926 -26.015  14.180  1.00  8.33           C  
ANISOU  303  C   THR A 551      874   1099   1192    -78    -56     45       C  
ATOM    304  O   THR A 551      23.522 -27.003  14.644  1.00  9.58           O  
ANISOU  304  O   THR A 551     1045   1226   1367    -77    -42     45       O  
ATOM    305  CB  THR A 551      21.859 -24.226  15.526  1.00  8.42           C  
ANISOU  305  CB  THR A 551      851   1145   1205    -61    -41     87       C  
ATOM    306  OG1 THR A 551      22.892 -24.371  16.506  1.00  8.05           O  
ANISOU  306  OG1 THR A 551      827   1087   1146    -46    -21     97       O  
ATOM    307  CG2 THR A 551      20.551 -23.656  16.124  1.00 10.23           C  
ANISOU  307  CG2 THR A 551     1045   1386   1456    -62    -30    103       C  
ATOM    308  N   PRO A 552      23.433 -25.362  13.125  1.00  8.43           N  
ANISOU  308  N   PRO A 552      900   1131   1171    -69    -68     29       N  
ATOM    309  CA  PRO A 552      24.678 -25.835  12.502  1.00  9.11           C  
ANISOU  309  CA  PRO A 552     1013   1205   1243    -61    -56      6       C  
ATOM    310  C   PRO A 552      25.833 -25.976  13.484  1.00  9.03           C  
ANISOU  310  C   PRO A 552     1005   1177   1248    -40    -33     22       C  
ATOM    311  O   PRO A 552      26.625 -26.936  13.388  1.00  9.57           O  
ANISOU  311  O   PRO A 552     1084   1217   1333    -34    -21      7       O  
ATOM    312  CB  PRO A 552      24.964 -24.771  11.425  1.00  9.92           C  
ANISOU  312  CB  PRO A 552     1128   1340   1303    -54    -63      2       C  
ATOM    313  CG  PRO A 552      23.542 -24.360  11.012  1.00 10.78           C  
ANISOU  313  CG  PRO A 552     1220   1470   1407    -69    -98      8       C  
ATOM    314  CD  PRO A 552      22.796 -24.288  12.324  1.00  9.51           C  
ANISOU  314  CD  PRO A 552     1028   1300   1285    -69    -91     33       C  
ATOM    315  N   ALA A 553      25.932 -25.049  14.440  1.00  7.79           N  
ANISOU  315  N   ALA A 553      838   1034   1087    -27    -30     49       N  
ATOM    316  CA  ALA A 553      27.017 -25.090  15.416  1.00  7.40           C  
ANISOU  316  CA  ALA A 553      791    974   1046    -10    -22     64       C  
ATOM    317  C   ALA A 553      26.913 -26.300  16.357  1.00  8.50           C  
ANISOU  317  C   ALA A 553      934   1084   1210    -12    -19     80       C  
ATOM    318  O   ALA A 553      27.915 -26.729  16.947  1.00  8.14           O  
ANISOU  318  O   ALA A 553      894   1022   1179      5    -19     92       O  
ATOM    319  CB  ALA A 553      27.069 -23.786  16.206  1.00  8.76           C  
ANISOU  319  CB  ALA A 553      959   1168   1203      0    -25     81       C  
ATOM    320  N   ASP A 554      25.670 -26.795  16.553  1.00  7.97           N  
ANISOU  320  N   ASP A 554      863   1010   1154    -32    -17     86       N  
ATOM    321  CA  ASP A 554      25.456 -27.954  17.404  1.00  7.52           C  
ANISOU  321  CA  ASP A 554      812    921   1124    -38     -8    108       C  
ATOM    322  C   ASP A 554      25.674 -29.251  16.630  1.00  8.86           C  
ANISOU  322  C   ASP A 554      989   1049   1330    -47     -8     86       C  
ATOM    323  O   ASP A 554      25.886 -30.290  17.245  1.00  8.88           O  
ANISOU  323  O   ASP A 554      999   1012   1363    -45     -1    106       O  
ATOM    324  CB  ASP A 554      24.009 -27.903  17.907  1.00  7.51           C  
ANISOU  324  CB  ASP A 554      797    929   1129    -60      3    125       C  
ATOM    325  CG  ASP A 554      23.619 -29.033  18.804  1.00  9.10           C  
ANISOU  325  CG  ASP A 554     1003   1096   1357    -73     20    157       C  
ATOM    326  OD1 ASP A 554      24.342 -29.278  19.806  1.00  9.63           O  
ANISOU  326  OD1 ASP A 554     1091   1155   1412    -56     25    189       O  
ATOM    327  OD2 ASP A 554      22.614 -29.702  18.504  1.00 10.29           O  
ANISOU  327  OD2 ASP A 554     1138   1227   1543   -102     26    153       O  
ATOM    328  N   LEU A 555      25.501 -29.198  15.290  1.00  8.28           N  
ANISOU  328  N   LEU A 555      915    982   1250    -57    -16     44       N  
ATOM    329  CA  LEU A 555      25.509 -30.427  14.472  1.00  9.16           C  
ANISOU  329  CA  LEU A 555     1038   1051   1391    -71    -15      8       C  
ATOM    330  C   LEU A 555      26.750 -30.625  13.632  1.00 10.34           C  
ANISOU  330  C   LEU A 555     1202   1190   1536    -49     -4    -26       C  
ATOM    331  O   LEU A 555      26.846 -31.622  12.910  1.00 10.41           O  
ANISOU  331  O   LEU A 555     1225   1162   1567    -56      2    -64       O  
ATOM    332  CB  LEU A 555      24.267 -30.421  13.554  1.00  9.14           C  
ANISOU  332  CB  LEU A 555     1029   1062   1383   -104    -36    -22       C  
ATOM    333  CG  LEU A 555      22.926 -30.280  14.247  1.00  9.94           C  
ANISOU  333  CG  LEU A 555     1102   1171   1503   -128    -42      7       C  
ATOM    334  CD1 LEU A 555      21.815 -30.202  13.220  1.00 10.40           C  
ANISOU  334  CD1 LEU A 555     1146   1246   1561   -159    -73    -24       C  
ATOM    335  CD2 LEU A 555      22.681 -31.488  15.169  1.00 11.73           C  
ANISOU  335  CD2 LEU A 555     1328   1347   1783   -143    -24     32       C  
ATOM    336  N   CYS A 556      27.725 -29.723  13.777  1.00  9.26           N  
ANISOU  336  N   CYS A 556     1060   1080   1377    -23      2    -13       N  
ATOM    337  CA  CYS A 556      28.920 -29.789  12.967  1.00  8.71           C  
ANISOU  337  CA  CYS A 556      997   1006   1307     -2     22    -41       C  
ATOM    338  C   CYS A 556      29.900 -30.843  13.417  1.00 10.74           C  
ANISOU  338  C   CYS A 556     1250   1214   1619     23     37    -38       C  
ATOM    339  O   CYS A 556      29.700 -31.496  14.450  1.00  9.99           O  
ANISOU  339  O   CYS A 556     1151   1087   1556     24     27     -4       O  
ATOM    340  CB  CYS A 556      29.543 -28.406  12.828  1.00  9.43           C  
ANISOU  340  CB  CYS A 556     1078   1142   1364     11     26    -29       C  
ATOM    341  SG  CYS A 556      29.826 -27.559  14.380  1.00 10.71           S  
ANISOU  341  SG  CYS A 556     1219   1320   1531     23      9     22       S  
ATOM    342  N   VAL A 557      30.972 -31.016  12.631  1.00 11.46           N  
ANISOU  342  N   VAL A 557     1340   1295   1721     44     64    -69       N  
ATOM    343  CA  VAL A 557      31.971 -32.057  12.850  1.00 13.26           C  
ANISOU  343  CA  VAL A 557     1557   1469   2012     74     82    -73       C  
ATOM    344  C   VAL A 557      33.318 -31.461  13.251  1.00 15.42           C  
ANISOU  344  C   VAL A 557     1796   1757   2305    106     89    -48       C  
ATOM    345  O   VAL A 557      34.032 -30.983  12.349  1.00 17.68           O  
ANISOU  345  O   VAL A 557     2074   2063   2580    115    121    -77       O  
ATOM    346  CB  VAL A 557      32.120 -32.930  11.583  1.00 17.10           C  
ANISOU  346  CB  VAL A 557     2065   1922   2509     75    117   -139       C  
ATOM    347  CG1 VAL A 557      33.241 -33.967  11.754  1.00 17.95           C  
ANISOU  347  CG1 VAL A 557     2157   1969   2695    114    143   -145       C  
ATOM    348  CG2 VAL A 557      30.796 -33.573  11.189  1.00 16.64           C  
ANISOU  348  CG2 VAL A 557     2039   1846   2439     37    100   -168       C  
ATOM    349  N   PRO A 558      33.744 -31.530  14.531  1.00 12.45           N  
ANISOU  349  N   PRO A 558     1400   1371   1961    124     61      3       N  
ATOM    350  CA  PRO A 558      32.955 -31.917  15.708  1.00 11.67           C  
ANISOU  350  CA  PRO A 558     1314   1259   1863    113     28     47       C  
ATOM    351  C   PRO A 558      32.106 -30.717  16.121  1.00 11.51           C  
ANISOU  351  C   PRO A 558     1301   1294   1778     87      9     65       C  
ATOM    352  O   PRO A 558      32.172 -29.659  15.472  1.00 11.61           O  
ANISOU  352  O   PRO A 558     1309   1347   1755     80     17     44       O  
ATOM    353  CB  PRO A 558      34.039 -32.267  16.730  1.00 12.83           C  
ANISOU  353  CB  PRO A 558     1436   1384   2056    148      6     92       C  
ATOM    354  CG  PRO A 558      35.091 -31.196  16.446  1.00 16.38           C  
ANISOU  354  CG  PRO A 558     1851   1872   2500    161      8     82       C  
ATOM    355  CD  PRO A 558      35.075 -31.025  14.947  1.00 14.28           C  
ANISOU  355  CD  PRO A 558     1591   1614   2222    153     55     24       C  
ATOM    356  N   ARG A 559      31.359 -30.859  17.197  1.00 10.43           N  
ANISOU  356  N   ARG A 559     1177   1157   1630     76    -10    104       N  
ATOM    357  CA  ARG A 559      30.495 -29.784  17.665  1.00  8.26           C  
ANISOU  357  CA  ARG A 559      909    929   1302     55    -21    117       C  
ATOM    358  C   ARG A 559      31.305 -28.569  18.073  1.00  8.68           C  
ANISOU  358  C   ARG A 559      947   1020   1331     68    -37    126       C  
ATOM    359  O   ARG A 559      32.385 -28.729  18.626  1.00 10.77           O  
ANISOU  359  O   ARG A 559     1197   1275   1619     91    -54    144       O  
ATOM    360  CB  ARG A 559      29.719 -30.290  18.884  1.00  9.26           C  
ANISOU  360  CB  ARG A 559     1052   1044   1423     45    -28    162       C  
ATOM    361  CG  ARG A 559      28.550 -29.372  19.185  1.00 11.18           C  
ANISOU  361  CG  ARG A 559     1300   1328   1622     22    -24    165       C  
ATOM    362  CD  ARG A 559      28.183 -29.507  20.631  1.00 14.23           C  
ANISOU  362  CD  ARG A 559     1703   1718   1986     21    -27    214       C  
ATOM    363  NE  ARG A 559      26.902 -28.881  20.942  1.00  9.81           N  
ANISOU  363  NE  ARG A 559     1145   1186   1396     -1     -9    216       N  
ATOM    364  CZ  ARG A 559      26.742 -28.046  21.948  1.00 10.48           C  
ANISOU  364  CZ  ARG A 559     1242   1305   1435      3     -8    233       C  
ATOM    365  NH1 ARG A 559      27.796 -27.663  22.688  1.00 12.30           N  
ANISOU  365  NH1 ARG A 559     1486   1549   1639     24    -34    246       N  
ATOM    366  NH2 ARG A 559      25.539 -27.574  22.232  1.00 12.19           N  
ANISOU  366  NH2 ARG A 559     1456   1541   1634    -13     18    235       N  
ATOM    367  N   LEU A 560      30.748 -27.369  17.858  1.00  9.03           N  
ANISOU  367  N   LEU A 560      993   1103   1335     53    -35    114       N  
ATOM    368  CA  LEU A 560      31.339 -26.155  18.420  1.00  8.49           C  
ANISOU  368  CA  LEU A 560      915   1065   1246     59    -52    122       C  
ATOM    369  C   LEU A 560      30.850 -26.133  19.874  1.00 12.37           C  
ANISOU  369  C   LEU A 560     1426   1565   1710     57    -70    154       C  
ATOM    370  O   LEU A 560      29.684 -26.464  20.144  1.00 14.91           O  
ANISOU  370  O   LEU A 560     1764   1886   2017     43    -57    164       O  
ATOM    371  CB  LEU A 560      30.834 -24.928  17.661  1.00  9.02           C  
ANISOU  371  CB  LEU A 560      980   1160   1287     45    -41    101       C  
ATOM    372  CG  LEU A 560      31.487 -23.618  18.062  1.00 10.22           C  
ANISOU  372  CG  LEU A 560     1122   1332   1429     48    -55    101       C  
ATOM    373  CD1 LEU A 560      32.969 -23.582  17.694  1.00 11.75           C  
ANISOU  373  CD1 LEU A 560     1287   1518   1658     60    -57     96       C  
ATOM    374  CD2 LEU A 560      30.752 -22.472  17.391  1.00 11.49           C  
ANISOU  374  CD2 LEU A 560     1286   1511   1568     35    -43     89       C  
ATOM    375  N   ASN A 561      31.720 -25.804  20.821  1.00 10.20           N  
ANISOU  375  N   ASN A 561     1149   1299   1428     70   -101    170       N  
ATOM    376  CA  ASN A 561      31.330 -25.847  22.228  1.00  9.80           C  
ANISOU  376  CA  ASN A 561     1127   1260   1336     69   -117    201       C  
ATOM    377  C   ASN A 561      31.477 -24.526  22.934  1.00 10.40           C  
ANISOU  377  C   ASN A 561     1212   1369   1370     65   -137    189       C  
ATOM    378  O   ASN A 561      32.393 -23.742  22.658  1.00 10.33           O  
ANISOU  378  O   ASN A 561     1180   1367   1377     67   -156    169       O  
ATOM    379  CB  ASN A 561      32.146 -26.909  22.982  1.00 10.07           C  
ANISOU  379  CB  ASN A 561     1165   1273   1389     88   -148    240       C  
ATOM    380  CG  ASN A 561      31.820 -28.293  22.570  1.00 12.82           C  
ANISOU  380  CG  ASN A 561     1514   1578   1777     91   -127    256       C  
ATOM    381  OD1 ASN A 561      30.660 -28.707  22.697  1.00 15.38           O  
ANISOU  381  OD1 ASN A 561     1859   1896   2088     74    -99    267       O  
ATOM    382  ND2 ASN A 561      32.814 -29.016  22.073  1.00 13.13           N  
ANISOU  382  ND2 ASN A 561     1529   1585   1874    112   -135    256       N  
ATOM    383  N   GLU A 562      30.630 -24.319  23.922  1.00  9.69           N  
ANISOU  383  N   GLU A 562     1155   1297   1230     57   -129    201       N  
ATOM    384  CA  GLU A 562      30.791 -23.171  24.812  1.00  9.42           C  
ANISOU  384  CA  GLU A 562     1140   1290   1148     55   -149    185       C  
ATOM    385  C   GLU A 562      32.166 -23.214  25.447  1.00 12.74           C  
ANISOU  385  C   GLU A 562     1557   1714   1569     66   -207    195       C  
ATOM    386  O   GLU A 562      32.654 -24.305  25.810  1.00 13.03           O  
ANISOU  386  O   GLU A 562     1595   1738   1616     79   -231    232       O  
ATOM    387  CB  GLU A 562      29.716 -23.201  25.902  1.00 10.83           C  
ANISOU  387  CB  GLU A 562     1361   1486   1266     49   -124    200       C  
ATOM    388  CG  GLU A 562      28.350 -22.970  25.340  1.00 13.15           C  
ANISOU  388  CG  GLU A 562     1648   1780   1570     39    -70    187       C  
ATOM    389  CD  GLU A 562      27.574 -24.207  24.951  1.00 25.28           C  
ANISOU  389  CD  GLU A 562     3176   3295   3135     32    -40    216       C  
ATOM    390  OE1 GLU A 562      28.179 -25.298  24.756  1.00 19.52           O  
ANISOU  390  OE1 GLU A 562     2441   2541   2433     37    -58    241       O  
ATOM    391  OE2 GLU A 562      26.329 -24.066  24.861  1.00 24.90           O  
ANISOU  391  OE2 GLU A 562     3123   3252   3088     21      1    213       O  
ATOM    392  N   GLY A 563      32.818 -22.062  25.479  1.00 10.84           N  
ANISOU  392  N   GLY A 563     1304   1485   1329     60   -233    162       N  
ATOM    393  CA  GLY A 563      34.160 -21.971  26.039  1.00 11.14           C  
ANISOU  393  CA  GLY A 563     1328   1529   1377     66   -297    165       C  
ATOM    394  C   GLY A 563      35.256 -22.083  24.999  1.00 11.83           C  
ANISOU  394  C   GLY A 563     1354   1595   1545     72   -306    160       C  
ATOM    395  O   GLY A 563      36.416 -21.731  25.281  1.00 13.63           O  
ANISOU  395  O   GLY A 563     1552   1826   1800     72   -357    155       O  
ATOM    396  N   ASP A 564      34.888 -22.498  23.761  1.00  9.69           N  
ANISOU  396  N   ASP A 564     1062   1304   1314     74   -255    158       N  
ATOM    397  CA  ASP A 564      35.895 -22.573  22.721  1.00  9.25           C  
ANISOU  397  CA  ASP A 564      954   1233   1329     81   -249    149       C  
ATOM    398  C   ASP A 564      36.351 -21.170  22.383  1.00 10.69           C  
ANISOU  398  C   ASP A 564     1114   1423   1526     62   -251    119       C  
ATOM    399  O   ASP A 564      35.521 -20.260  22.236  1.00 10.66           O  
ANISOU  399  O   ASP A 564     1133   1425   1491     47   -228     99       O  
ATOM    400  CB  ASP A 564      35.318 -23.202  21.454  1.00 10.11           C  
ANISOU  400  CB  ASP A 564     1059   1324   1459     83   -192    145       C  
ATOM    401  CG  ASP A 564      35.141 -24.724  21.454  1.00 13.08           C  
ANISOU  401  CG  ASP A 564     1442   1675   1851    101   -184    170       C  
ATOM    402  OD1 ASP A 564      35.553 -25.377  22.442  1.00 12.21           O  
ANISOU  402  OD1 ASP A 564     1338   1560   1742    115   -222    201       O  
ATOM    403  OD2 ASP A 564      34.556 -25.236  20.470  1.00 12.25           O  
ANISOU  403  OD2 ASP A 564     1341   1555   1757     98   -141    158       O  
ATOM    404  N   GLN A 565      37.671 -20.971  22.262  1.00 10.10           N  
ANISOU  404  N   GLN A 565      988   1341   1507     64   -279    116       N  
ATOM    405  CA  GLN A 565      38.221 -19.659  21.936  1.00 10.98           C  
ANISOU  405  CA  GLN A 565     1072   1453   1647     42   -280     91       C  
ATOM    406  C   GLN A 565      38.441 -19.601  20.430  1.00 12.04           C  
ANISOU  406  C   GLN A 565     1174   1574   1828     41   -219     87       C  
ATOM    407  O   GLN A 565      39.087 -20.503  19.869  1.00 12.71           O  
ANISOU  407  O   GLN A 565     1224   1648   1957     59   -201     98       O  
ATOM    408  CB  GLN A 565      39.560 -19.457  22.653  1.00 12.32           C  
ANISOU  408  CB  GLN A 565     1197   1624   1860     39   -346     90       C  
ATOM    409  CG  GLN A 565      40.182 -18.111  22.299  1.00 21.20           C  
ANISOU  409  CG  GLN A 565     2286   2741   3028     10   -346     64       C  
ATOM    410  CD  GLN A 565      41.544 -17.877  22.912  1.00 41.34           C  
ANISOU  410  CD  GLN A 565     4779   5291   5636      1   -414     61       C  
ATOM    411  OE1 GLN A 565      41.890 -18.432  23.962  1.00 40.28           O  
ANISOU  411  OE1 GLN A 565     4650   5171   5485     12   -483     73       O  
ATOM    412  NE2 GLN A 565      42.328 -16.996  22.293  1.00 25.13           N  
ANISOU  412  NE2 GLN A 565     2672   3223   3654    -23   -400     47       N  
ATOM    413  N   VAL A 566      37.906 -18.557  19.773  1.00 10.52           N  
ANISOU  413  N   VAL A 566      994   1380   1623     22   -184     73       N  
ATOM    414  CA  VAL A 566      38.039 -18.459  18.317  1.00 10.38           C  
ANISOU  414  CA  VAL A 566      957   1354   1631     20   -124     74       C  
ATOM    415  C   VAL A 566      39.392 -17.856  17.958  1.00 12.17           C  
ANISOU  415  C   VAL A 566     1125   1571   1929      7   -120     73       C  
ATOM    416  O   VAL A 566      39.698 -16.741  18.386  1.00 14.16           O  
ANISOU  416  O   VAL A 566     1366   1817   2198    -16   -145     63       O  
ATOM    417  CB  VAL A 566      36.862 -17.667  17.719  1.00 13.34           C  
ANISOU  417  CB  VAL A 566     1372   1731   1964      8    -92     71       C  
ATOM    418  CG1 VAL A 566      36.953 -17.614  16.191  1.00 13.09           C  
ANISOU  418  CG1 VAL A 566     1332   1697   1942      6    -34     77       C  
ATOM    419  CG2 VAL A 566      35.534 -18.317  18.125  1.00 13.08           C  
ANISOU  419  CG2 VAL A 566     1385   1709   1875     19    -96     72       C  
ATOM    420  N   VAL A 567      40.217 -18.591  17.195  1.00 10.70           N  
ANISOU  420  N   VAL A 567      897   1378   1789     21    -86     80       N  
ATOM    421  CA  VAL A 567      41.555 -18.142  16.791  1.00 11.41           C  
ANISOU  421  CA  VAL A 567      918   1459   1958     10    -70     81       C  
ATOM    422  C   VAL A 567      41.511 -17.569  15.378  1.00 13.88           C  
ANISOU  422  C   VAL A 567     1233   1769   2271     -3      8     86       C  
ATOM    423  O   VAL A 567      42.017 -16.467  15.153  1.00 13.86           O  
ANISOU  423  O   VAL A 567     1204   1758   2306    -30     20     90       O  
ATOM    424  CB  VAL A 567      42.565 -19.327  16.883  1.00 15.75           C  
ANISOU  424  CB  VAL A 567     1413   2002   2569     39    -75     88       C  
ATOM    425  CG1 VAL A 567      43.955 -18.919  16.370  1.00 18.11           C  
ANISOU  425  CG1 VAL A 567     1628   2291   2961     30    -47     90       C  
ATOM    426  CG2 VAL A 567      42.642 -19.844  18.324  1.00 15.48           C  
ANISOU  426  CG2 VAL A 567     1380   1971   2529     53   -161     94       C  
ATOM    427  N   LEU A 568      40.886 -18.308  14.435  1.00 11.05           N  
ANISOU  427  N   LEU A 568      911   1418   1868     13     59     85       N  
ATOM    428  CA  LEU A 568      40.759 -17.852  13.037  1.00 11.50           C  
ANISOU  428  CA  LEU A 568      984   1480   1904      2    131     92       C  
ATOM    429  C   LEU A 568      39.331 -17.951  12.596  1.00 11.43           C  
ANISOU  429  C   LEU A 568     1047   1484   1812      5    135     91       C  
ATOM    430  O   LEU A 568      38.597 -18.847  13.023  1.00 10.71           O  
ANISOU  430  O   LEU A 568      983   1396   1688     21    108     80       O  
ATOM    431  CB  LEU A 568      41.530 -18.734  12.063  1.00 12.84           C  
ANISOU  431  CB  LEU A 568     1127   1650   2101     21    197     86       C  
ATOM    432  CG  LEU A 568      43.038 -18.952  12.246  1.00 16.98           C  
ANISOU  432  CG  LEU A 568     1567   2162   2724     28    211     86       C  
ATOM    433  CD1 LEU A 568      43.592 -19.832  11.104  1.00 16.63           C  
ANISOU  433  CD1 LEU A 568     1508   2118   2695     51    296     74       C  
ATOM    434  CD2 LEU A 568      43.813 -17.634  12.274  1.00 15.17           C  
ANISOU  434  CD2 LEU A 568     1288   1925   2551     -6    216    103       C  
ATOM    435  N   ILE A 569      38.924 -17.008  11.713  1.00 10.23           N  
ANISOU  435  N   ILE A 569      921   1337   1628    -13    169    107       N  
ATOM    436  CA  ILE A 569      37.632 -17.033  11.074  1.00  9.02           C  
ANISOU  436  CA  ILE A 569      828   1199   1400    -11    173    110       C  
ATOM    437  C   ILE A 569      37.913 -16.979   9.595  1.00 11.76           C  
ANISOU  437  C   ILE A 569     1190   1559   1720    -15    240    121       C  
ATOM    438  O   ILE A 569      38.464 -15.974   9.120  1.00 12.40           O  
ANISOU  438  O   ILE A 569     1257   1634   1821    -33    273    146       O  
ATOM    439  CB  ILE A 569      36.714 -15.875  11.509  1.00 10.47           C  
ANISOU  439  CB  ILE A 569     1036   1377   1565    -24    137    125       C  
ATOM    440  CG1 ILE A 569      36.476 -15.976  13.022  1.00 12.10           C  
ANISOU  440  CG1 ILE A 569     1235   1575   1789    -19     79    109       C  
ATOM    441  CG2 ILE A 569      35.385 -15.904  10.697  1.00 11.21           C  
ANISOU  441  CG2 ILE A 569     1182   1488   1588    -20    140    134       C  
ATOM    442  CD1 ILE A 569      35.697 -14.851  13.611  1.00 15.69           C  
ANISOU  442  CD1 ILE A 569     1708   2018   2235    -28     50    113       C  
ATOM    443  N   ASN A 570      37.523 -18.020   8.856  1.00 11.01           N  
ANISOU  443  N   ASN A 570     1127   1479   1576     -1    262    101       N  
ATOM    444  CA  ASN A 570      37.829 -18.088   7.422  1.00 11.42           C  
ANISOU  444  CA  ASN A 570     1203   1549   1588     -4    331    104       C  
ATOM    445  C   ASN A 570      39.304 -17.765   7.161  1.00 14.84           C  
ANISOU  445  C   ASN A 570     1583   1973   2084     -9    392    114       C  
ATOM    446  O   ASN A 570      39.636 -17.018   6.239  1.00 16.10           O  
ANISOU  446  O   ASN A 570     1753   2141   2225    -24    446    141       O  
ATOM    447  CB  ASN A 570      36.904 -17.183   6.616  1.00 12.46           C  
ANISOU  447  CB  ASN A 570     1386   1697   1649    -18    328    135       C  
ATOM    448  CG  ASN A 570      35.480 -17.645   6.725  1.00 12.74           C  
ANISOU  448  CG  ASN A 570     1464   1745   1630    -12    273    121       C  
ATOM    449  OD1 ASN A 570      35.201 -18.854   6.707  1.00 13.87           O  
ANISOU  449  OD1 ASN A 570     1620   1892   1758     -1    265     84       O  
ATOM    450  ND2 ASN A 570      34.574 -16.696   6.788  1.00 11.82           N  
ANISOU  450  ND2 ASN A 570     1368   1631   1493    -20    236    151       N  
ATOM    451  N   GLY A 571      40.163 -18.320   8.002  1.00 13.92           N  
ANISOU  451  N   GLY A 571     1407   1837   2044      4    381     97       N  
ATOM    452  CA  GLY A 571      41.617 -18.165   7.856  1.00 15.02           C  
ANISOU  452  CA  GLY A 571     1478   1965   2263      2    435    103       C  
ATOM    453  C   GLY A 571      42.251 -16.907   8.396  1.00 19.08           C  
ANISOU  453  C   GLY A 571     1943   2464   2844    -26    420    133       C  
ATOM    454  O   GLY A 571      43.491 -16.795   8.422  1.00 22.03           O  
ANISOU  454  O   GLY A 571     2244   2825   3300    -30    455    137       O  
ATOM    455  N   ARG A 572      41.417 -15.959   8.849  1.00 15.19           N  
ANISOU  455  N   ARG A 572     1482   1966   2324    -44    367    150       N  
ATOM    456  CA  ARG A 572      41.880 -14.665   9.315  1.00 15.56           C  
ANISOU  456  CA  ARG A 572     1493   1990   2430    -74    351    174       C  
ATOM    457  C   ARG A 572      42.108 -14.644  10.792  1.00 16.13           C  
ANISOU  457  C   ARG A 572     1525   2045   2557    -75    271    154       C  
ATOM    458  O   ARG A 572      41.236 -15.057  11.545  1.00 13.72           O  
ANISOU  458  O   ARG A 572     1256   1747   2212    -60    213    137       O  
ATOM    459  CB  ARG A 572      40.844 -13.626   8.954  1.00 16.61           C  
ANISOU  459  CB  ARG A 572     1685   2120   2507    -89    342    201       C  
ATOM    460  CG  ARG A 572      41.272 -12.200   9.236  1.00 21.71           C  
ANISOU  460  CG  ARG A 572     2302   2732   3214   -123    337    227       C  
ATOM    461  CD  ARG A 572      40.077 -11.289   9.287  1.00 20.67           C  
ANISOU  461  CD  ARG A 572     2228   2589   3038   -127    304    246       C  
ATOM    462  NE  ARG A 572      39.256 -11.369   8.077  1.00 25.01           N  
ANISOU  462  NE  ARG A 572     2839   3162   3502   -117    339    274       N  
ATOM    463  CZ  ARG A 572      39.364 -10.557   7.031  1.00 40.51           C  
ANISOU  463  CZ  ARG A 572     4823   5119   5450   -133    392    323       C  
ATOM    464  NH1 ARG A 572      40.262  -9.576   7.030  1.00 30.90           N  
ANISOU  464  NH1 ARG A 572     3566   3868   4309   -164    422    351       N  
ATOM    465  NH2 ARG A 572      38.549 -10.691   5.997  1.00 28.17           N  
ANISOU  465  NH2 ARG A 572     3322   3585   3797   -122    409    348       N  
ATOM    466  N   ASP A 573      43.276 -14.147  11.215  1.00 16.65           N  
ANISOU  466  N   ASP A 573     1520   2092   2716    -95    267    157       N  
ATOM    467  CA  ASP A 573      43.627 -13.973  12.601  1.00 15.93           C  
ANISOU  467  CA  ASP A 573     1389   1986   2676   -102    185    139       C  
ATOM    468  C   ASP A 573      42.825 -12.781  13.130  1.00 18.63           C  
ANISOU  468  C   ASP A 573     1774   2310   2993   -125    141    139       C  
ATOM    469  O   ASP A 573      42.991 -11.650  12.653  1.00 20.86           O  
ANISOU  469  O   ASP A 573     2052   2569   3304   -155    171    160       O  
ATOM    470  CB  ASP A 573      45.147 -13.701  12.680  1.00 18.31           C  
ANISOU  470  CB  ASP A 573     1595   2271   3091   -122    198    143       C  
ATOM    471  CG  ASP A 573      45.695 -13.441  14.060  1.00 25.64           C  
ANISOU  471  CG  ASP A 573     2475   3187   4080   -135    105    123       C  
ATOM    472  OD1 ASP A 573      44.899 -13.402  15.022  1.00 22.14           O  
ANISOU  472  OD1 ASP A 573     2082   2747   3585   -130     33    105       O  
ATOM    473  OD2 ASP A 573      46.917 -13.214  14.174  1.00 33.63           O  
ANISOU  473  OD2 ASP A 573     3400   4185   5192   -154    104    126       O  
ATOM    474  N   ILE A 574      41.992 -13.018  14.128  1.00 14.44           N  
ANISOU  474  N   ILE A 574     1283   1786   2416   -112     75    118       N  
ATOM    475  CA  ILE A 574      41.126 -11.958  14.668  1.00 14.49           C  
ANISOU  475  CA  ILE A 574     1334   1775   2397   -127     40    111       C  
ATOM    476  C   ILE A 574      41.587 -11.303  15.973  1.00 18.07           C  
ANISOU  476  C   ILE A 574     1763   2208   2896   -149    -30     82       C  
ATOM    477  O   ILE A 574      40.819 -10.560  16.581  1.00 17.45           O  
ANISOU  477  O   ILE A 574     1726   2114   2789   -155    -61     65       O  
ATOM    478  CB  ILE A 574      39.675 -12.497  14.786  1.00 16.17           C  
ANISOU  478  CB  ILE A 574     1615   2008   2520    -99     28    106       C  
ATOM    479  CG1 ILE A 574      39.618 -13.739  15.727  1.00 17.06           C  
ANISOU  479  CG1 ILE A 574     1728   2143   2610    -74    -17     85       C  
ATOM    480  CG2 ILE A 574      39.093 -12.768  13.389  1.00 19.78           C  
ANISOU  480  CG2 ILE A 574     2105   2481   2931    -88     90    133       C  
ATOM    481  CD1 ILE A 574      38.226 -14.068  16.244  1.00 20.69           C  
ANISOU  481  CD1 ILE A 574     2247   2616   2997    -56    -40     76       C  
ATOM    482  N   ALA A 575      42.821 -11.567  16.419  1.00 17.99           N  
ANISOU  482  N   ALA A 575     1685   2196   2953   -159    -59     73       N  
ATOM    483  CA  ALA A 575      43.298 -11.049  17.711  1.00 19.03           C  
ANISOU  483  CA  ALA A 575     1795   2314   3120   -181   -140     40       C  
ATOM    484  C   ALA A 575      43.153  -9.561  17.970  1.00 23.11           C  
ANISOU  484  C   ALA A 575     2327   2791   3664   -219   -154     23       C  
ATOM    485  O   ALA A 575      42.893  -9.161  19.105  1.00 26.10           O  
ANISOU  485  O   ALA A 575     2732   3162   4022   -228   -220    -15       O  
ATOM    486  CB  ALA A 575      44.744 -11.485  17.942  1.00 20.98           C  
ANISOU  486  CB  ALA A 575     1954   2565   3454   -189   -167     40       C  
ATOM    487  N   GLU A 576      43.355  -8.739  16.962  1.00 18.70           N  
ANISOU  487  N   GLU A 576     1753   2202   3152   -242    -92     50       N  
ATOM    488  CA  GLU A 576      43.323  -7.294  17.219  1.00 18.74           C  
ANISOU  488  CA  GLU A 576     1766   2155   3201   -281   -106     35       C  
ATOM    489  C   GLU A 576      42.003  -6.654  16.828  1.00 16.75           C  
ANISOU  489  C   GLU A 576     1588   1884   2892   -267    -73     47       C  
ATOM    490  O   GLU A 576      41.875  -5.430  16.878  1.00 18.33           O  
ANISOU  490  O   GLU A 576     1800   2032   3132   -294    -72     42       O  
ATOM    491  CB  GLU A 576      44.491  -6.599  16.492  1.00 22.32           C  
ANISOU  491  CB  GLU A 576     2147   2573   3763   -324    -64     62       C  
ATOM    492  CG  GLU A 576      45.876  -7.189  16.771  1.00 36.39           C  
ANISOU  492  CG  GLU A 576     3835   4369   5622   -337    -90     54       C  
ATOM    493  CD  GLU A 576      46.355  -7.260  18.213  1.00 69.33           C  
ANISOU  493  CD  GLU A 576     7982   8545   9814   -349   -199      2       C  
ATOM    494  OE1 GLU A 576      46.005  -6.363  19.015  1.00 68.29           O  
ANISOU  494  OE1 GLU A 576     7887   8383   9676   -373   -252    -38       O  
ATOM    495  OE2 GLU A 576      47.123  -8.198  18.529  1.00 70.46           O  
ANISOU  495  OE2 GLU A 576     8070   8721   9983   -335   -233      1       O  
ATOM    496  N   HIS A 577      41.007  -7.495  16.476  1.00 13.65           N  
ANISOU  496  N   HIS A 577     1243   1531   2413   -226    -51     63       N  
ATOM    497  CA  HIS A 577      39.733  -7.025  15.992  1.00 12.91           C  
ANISOU  497  CA  HIS A 577     1210   1426   2269   -208    -22     81       C  
ATOM    498  C   HIS A 577      38.696  -6.880  17.078  1.00 13.23           C  
ANISOU  498  C   HIS A 577     1301   1466   2261   -190    -68     40       C  
ATOM    499  O   HIS A 577      38.682  -7.635  18.057  1.00 13.34           O  
ANISOU  499  O   HIS A 577     1321   1511   2239   -178   -113      7       O  
ATOM    500  CB  HIS A 577      39.204  -7.953  14.878  1.00 13.20           C  
ANISOU  500  CB  HIS A 577     1266   1503   2245   -178     28    121       C  
ATOM    501  CG  HIS A 577      39.982  -7.854  13.602  1.00 16.41           C  
ANISOU  501  CG  HIS A 577     1643   1908   2685   -194     92    166       C  
ATOM    502  ND1 HIS A 577      40.869  -8.847  13.219  1.00 20.54           N  
ANISOU  502  ND1 HIS A 577     2124   2461   3219   -189    118    171       N  
ATOM    503  CD2 HIS A 577      39.949  -6.901  12.645  1.00 19.13           C  
ANISOU  503  CD2 HIS A 577     1997   2221   3050   -211    141    211       C  
ATOM    504  CE1 HIS A 577      41.396  -8.434  12.071  1.00 20.30           C  
ANISOU  504  CE1 HIS A 577     2077   2420   3214   -206    186    213       C  
ATOM    505  NE2 HIS A 577      40.850  -7.294  11.667  1.00 20.23           N  
ANISOU  505  NE2 HIS A 577     2102   2377   3207   -220    201    242       N  
ATOM    506  N   THR A 578      37.833  -5.874  16.902  1.00 11.17           N  
ANISOU  506  N   THR A 578     1075   1166   2001   -187    -52     46       N  
ATOM    507  CA  THR A 578      36.792  -5.683  17.893  1.00 10.94           C  
ANISOU  507  CA  THR A 578     1093   1134   1930   -167    -81      5       C  
ATOM    508  C   THR A 578      35.752  -6.791  17.748  1.00 11.55           C  
ANISOU  508  C   THR A 578     1198   1264   1927   -128    -71     19       C  
ATOM    509  O   THR A 578      35.656  -7.484  16.715  1.00 10.99           O  
ANISOU  509  O   THR A 578     1120   1221   1834   -116    -39     61       O  
ATOM    510  CB  THR A 578      36.081  -4.349  17.678  1.00 11.54           C  
ANISOU  510  CB  THR A 578     1195   1150   2039   -167    -62     10       C  
ATOM    511  OG1 THR A 578      35.315  -4.402  16.462  1.00 12.62           O  
ANISOU  511  OG1 THR A 578     1346   1295   2155   -144    -18     70       O  
ATOM    512  CG2 THR A 578      37.011  -3.155  17.723  1.00 11.62           C  
ANISOU  512  CG2 THR A 578     1181   1096   2141   -210    -66     -1       C  
ATOM    513  N   HIS A 579      34.879  -6.877  18.760  1.00  9.91           N  
ANISOU  513  N   HIS A 579     1025   1065   1676   -108    -93    -18       N  
ATOM    514  CA  HIS A 579      33.764  -7.798  18.734  1.00  9.13           C  
ANISOU  514  CA  HIS A 579      950   1007   1512    -75    -81     -8       C  
ATOM    515  C   HIS A 579      32.940  -7.633  17.451  1.00 10.33           C  
ANISOU  515  C   HIS A 579     1108   1156   1662    -59    -43     41       C  
ATOM    516  O   HIS A 579      32.620  -8.638  16.803  1.00  9.53           O  
ANISOU  516  O   HIS A 579     1005   1093   1523    -45    -31     67       O  
ATOM    517  CB  HIS A 579      32.856  -7.502  19.951  1.00  9.33           C  
ANISOU  517  CB  HIS A 579     1012   1028   1506    -60    -95    -53       C  
ATOM    518  CG  HIS A 579      31.687  -8.424  20.119  1.00  9.54           C  
ANISOU  518  CG  HIS A 579     1058   1093   1473    -30    -81    -45       C  
ATOM    519  ND1 HIS A 579      31.751  -9.541  20.934  1.00  9.89           N  
ANISOU  519  ND1 HIS A 579     1113   1180   1466    -25   -100    -57       N  
ATOM    520  CD2 HIS A 579      30.452  -8.364  19.566  1.00 10.44           C  
ANISOU  520  CD2 HIS A 579     1179   1208   1580     -6    -52    -22       C  
ATOM    521  CE1 HIS A 579      30.547 -10.114  20.865  1.00  8.86           C  
ANISOU  521  CE1 HIS A 579      995   1071   1302     -2    -76    -43       C  
ATOM    522  NE2 HIS A 579      29.730  -9.432  20.069  1.00  9.08           N  
ANISOU  522  NE2 HIS A 579     1018   1076   1355     10    -50    -25       N  
ATOM    523  N   ASP A 580      32.498  -6.397  17.140  1.00 10.04           N  
ANISOU  523  N   ASP A 580     1080   1071   1664    -58    -29     52       N  
ATOM    524  CA  ASP A 580      31.639  -6.218  15.976  1.00  8.97           C  
ANISOU  524  CA  ASP A 580      952    935   1522    -38     -4    103       C  
ATOM    525  C   ASP A 580      32.392  -6.467  14.668  1.00 11.39           C  
ANISOU  525  C   ASP A 580     1245   1255   1830    -54     19    153       C  
ATOM    526  O   ASP A 580      31.754  -6.886  13.693  1.00 10.25           O  
ANISOU  526  O   ASP A 580     1111   1137   1648    -38     31    192       O  
ATOM    527  CB  ASP A 580      30.960  -4.859  16.015  1.00 10.04           C  
ANISOU  527  CB  ASP A 580     1100   1011   1704    -27      4    107       C  
ATOM    528  CG  ASP A 580      29.845  -4.731  17.049  1.00  9.76           C  
ANISOU  528  CG  ASP A 580     1081    971   1656      1     -2     64       C  
ATOM    529  OD1 ASP A 580      29.471  -5.771  17.684  1.00  9.56           O  
ANISOU  529  OD1 ASP A 580     1060    994   1578     11    -10     40       O  
ATOM    530  OD2 ASP A 580      29.344  -3.601  17.227  1.00 12.52           O  
ANISOU  530  OD2 ASP A 580     1440   1265   2053     13      6     57       O  
ATOM    531  N   GLN A 581      33.705  -6.248  14.634  1.00 10.25           N  
ANISOU  531  N   GLN A 581     1076   1094   1726    -85     25    151       N  
ATOM    532  CA  GLN A 581      34.468  -6.595  13.429  1.00 10.53           C  
ANISOU  532  CA  GLN A 581     1096   1148   1758    -98     59    195       C  
ATOM    533  C   GLN A 581      34.443  -8.099  13.220  1.00 12.97           C  
ANISOU  533  C   GLN A 581     1403   1516   2008    -84     59    188       C  
ATOM    534  O   GLN A 581      34.241  -8.562  12.081  1.00 12.63           O  
ANISOU  534  O   GLN A 581     1373   1501   1926    -76     87    223       O  
ATOM    535  CB  GLN A 581      35.891  -6.100  13.545  1.00 12.17           C  
ANISOU  535  CB  GLN A 581     1266   1326   2034   -135     68    191       C  
ATOM    536  CG  GLN A 581      35.994  -4.611  13.224  1.00 12.27           C  
ANISOU  536  CG  GLN A 581     1281   1273   2110   -155     85    218       C  
ATOM    537  CD  GLN A 581      37.303  -4.003  13.636  1.00 16.95           C  
ANISOU  537  CD  GLN A 581     1830   1825   2785   -198     83    200       C  
ATOM    538  OE1 GLN A 581      38.142  -4.607  14.290  1.00 14.66           O  
ANISOU  538  OE1 GLN A 581     1505   1555   2509   -212     59    163       O  
ATOM    539  NE2 GLN A 581      37.426  -2.701  13.406  1.00 24.40           N  
ANISOU  539  NE2 GLN A 581     2774   2701   3795   -221     98    223       N  
ATOM    540  N   VAL A 582      34.533  -8.861  14.328  1.00  9.71           N  
ANISOU  540  N   VAL A 582      983   1123   1584    -78     28    144       N  
ATOM    541  CA  VAL A 582      34.458 -10.334  14.303  1.00  9.93           C  
ANISOU  541  CA  VAL A 582     1010   1197   1565    -63     24    135       C  
ATOM    542  C   VAL A 582      33.082 -10.774  13.852  1.00 10.72           C  
ANISOU  542  C   VAL A 582     1143   1321   1612    -39     26    148       C  
ATOM    543  O   VAL A 582      32.963 -11.725  13.057  1.00 10.82           O  
ANISOU  543  O   VAL A 582     1160   1363   1586    -32     41    159       O  
ATOM    544  CB  VAL A 582      34.846 -10.879  15.701  1.00 11.44           C  
ANISOU  544  CB  VAL A 582     1190   1397   1761    -62    -15     94       C  
ATOM    545  CG1 VAL A 582      34.421 -12.340  15.884  1.00 12.12           C  
ANISOU  545  CG1 VAL A 582     1286   1520   1799    -42    -23     88       C  
ATOM    546  CG2 VAL A 582      36.354 -10.739  15.912  1.00 12.60           C  
ANISOU  546  CG2 VAL A 582     1293   1530   1963    -86    -22     86       C  
ATOM    547  N   VAL A 583      31.999 -10.130  14.337  1.00  9.08           N  
ANISOU  547  N   VAL A 583      952   1097   1401    -27     11    143       N  
ATOM    548  CA  VAL A 583      30.662 -10.460  13.889  1.00  8.48           C  
ANISOU  548  CA  VAL A 583      894   1040   1287     -6      9    158       C  
ATOM    549  C   VAL A 583      30.542 -10.271  12.369  1.00 11.30           C  
ANISOU  549  C   VAL A 583     1261   1405   1627     -7     27    204       C  
ATOM    550  O   VAL A 583      30.017 -11.186  11.693  1.00 10.05           O  
ANISOU  550  O   VAL A 583     1114   1282   1423      1     25    211       O  
ATOM    551  CB  VAL A 583      29.608  -9.631  14.669  1.00  9.89           C  
ANISOU  551  CB  VAL A 583     1080   1194   1483     10     -3    145       C  
ATOM    552  CG1 VAL A 583      28.208  -9.718  14.046  1.00 10.25           C  
ANISOU  552  CG1 VAL A 583     1132   1254   1510     32     -7    170       C  
ATOM    553  CG2 VAL A 583      29.589 -10.052  16.123  1.00  9.80           C  
ANISOU  553  CG2 VAL A 583     1071   1189   1464     12    -16    100       C  
ATOM    554  N   LEU A 584      31.063  -9.154  11.834  1.00 10.75           N  
ANISOU  554  N   LEU A 584     1192   1304   1589    -18     44    234       N  
ATOM    555  CA  LEU A 584      30.946  -8.980  10.379  1.00 10.39           C  
ANISOU  555  CA  LEU A 584     1165   1270   1514    -19     63    285       C  
ATOM    556  C   LEU A 584      31.757 -10.059   9.649  1.00 12.32           C  
ANISOU  556  C   LEU A 584     1411   1553   1718    -29     89    282       C  
ATOM    557  O   LEU A 584      31.275 -10.575   8.631  1.00 12.28           O  
ANISOU  557  O   LEU A 584     1431   1581   1655    -23     92    301       O  
ATOM    558  CB  LEU A 584      31.406  -7.581   9.964  1.00 11.32           C  
ANISOU  558  CB  LEU A 584     1284   1341   1676    -31     83    327       C  
ATOM    559  CG  LEU A 584      31.162  -7.242   8.450  1.00 14.96           C  
ANISOU  559  CG  LEU A 584     1775   1814   2097    -29    101    393       C  
ATOM    560  CD1 LEU A 584      29.714  -7.476   8.057  1.00 16.09           C  
ANISOU  560  CD1 LEU A 584     1938   1982   2195     -2     63    409       C  
ATOM    561  CD2 LEU A 584      31.579  -5.823   8.140  1.00 17.78           C  
ANISOU  561  CD2 LEU A 584     2134   2114   2508    -42    122    441       C  
ATOM    562  N   PHE A 585      32.958 -10.431  10.143  1.00 10.28           N  
ANISOU  562  N   PHE A 585     1125   1291   1490    -44    106    255       N  
ATOM    563  CA  PHE A 585      33.700 -11.504   9.460  1.00 10.04           C  
ANISOU  563  CA  PHE A 585     1092   1292   1431    -48    138    248       C  
ATOM    564  C   PHE A 585      32.866 -12.793   9.444  1.00 11.16           C  
ANISOU  564  C   PHE A 585     1252   1469   1521    -31    116    222       C  
ATOM    565  O   PHE A 585      32.843 -13.504   8.419  1.00 10.97           O  
ANISOU  565  O   PHE A 585     1249   1472   1446    -29    137    225       O  
ATOM    566  CB  PHE A 585      35.000 -11.812  10.189  1.00 11.22           C  
ANISOU  566  CB  PHE A 585     1198   1430   1634    -59    148    221       C  
ATOM    567  CG  PHE A 585      36.010 -10.702  10.089  1.00 12.78           C  
ANISOU  567  CG  PHE A 585     1368   1595   1893    -84    174    243       C  
ATOM    568  CD1 PHE A 585      36.102  -9.916   8.935  1.00 16.72           C  
ANISOU  568  CD1 PHE A 585     1885   2085   2382    -95    217    292       C  
ATOM    569  CD2 PHE A 585      36.867 -10.433  11.141  1.00 16.38           C  
ANISOU  569  CD2 PHE A 585     1781   2025   2415    -98    154    217       C  
ATOM    570  CE1 PHE A 585      37.053  -8.889   8.834  1.00 19.79           C  
ANISOU  570  CE1 PHE A 585     2245   2437   2837   -123    247    318       C  
ATOM    571  CE2 PHE A 585      37.797  -9.395  11.050  1.00 19.54           C  
ANISOU  571  CE2 PHE A 585     2151   2390   2884   -127    176    236       C  
ATOM    572  CZ  PHE A 585      37.870  -8.622   9.902  1.00 18.30           C  
ANISOU  572  CZ  PHE A 585     2009   2220   2725   -140    225    286       C  
ATOM    573  N   ILE A 586      32.152 -13.098  10.536  1.00  9.75           N  
ANISOU  573  N   ILE A 586     1067   1287   1351    -20     78    196       N  
ATOM    574  CA  ILE A 586      31.315 -14.299  10.503  1.00  8.98           C  
ANISOU  574  CA  ILE A 586      984   1216   1214     -9     60    176       C  
ATOM    575  C   ILE A 586      30.207 -14.184   9.457  1.00 11.02           C  
ANISOU  575  C   ILE A 586     1270   1493   1424     -5     48    199       C  
ATOM    576  O   ILE A 586      29.849 -15.179   8.831  1.00 12.39           O  
ANISOU  576  O   ILE A 586     1460   1692   1555     -4     45    186       O  
ATOM    577  CB  ILE A 586      30.749 -14.559  11.927  1.00 10.26           C  
ANISOU  577  CB  ILE A 586     1134   1370   1395     -1     28    151       C  
ATOM    578  CG1 ILE A 586      31.929 -14.983  12.866  1.00 10.96           C  
ANISOU  578  CG1 ILE A 586     1199   1449   1517     -5     30    129       C  
ATOM    579  CG2 ILE A 586      29.659 -15.675  11.927  1.00 11.73           C  
ANISOU  579  CG2 ILE A 586     1331   1577   1550      6     11    138       C  
ATOM    580  CD1 ILE A 586      31.630 -14.901  14.382  1.00 10.35           C  
ANISOU  580  CD1 ILE A 586     1117   1362   1452      0      0    110       C  
ATOM    581  N   LYS A 587      29.655 -12.990   9.303  1.00  9.45           N  
ANISOU  581  N   LYS A 587     1076   1280   1236     -1     37    232       N  
ATOM    582  CA  LYS A 587      28.556 -12.760   8.357  1.00 10.76           C  
ANISOU  582  CA  LYS A 587     1263   1462   1362      7     14    262       C  
ATOM    583  C   LYS A 587      29.060 -12.501   6.938  1.00 13.70           C  
ANISOU  583  C   LYS A 587     1668   1851   1687     -2     38    298       C  
ATOM    584  O   LYS A 587      28.231 -12.358   6.023  1.00 14.15           O  
ANISOU  584  O   LYS A 587     1749   1928   1697      3     13    327       O  
ATOM    585  CB  LYS A 587      27.669 -11.621   8.880  1.00 13.99           C  
ANISOU  585  CB  LYS A 587     1661   1844   1812     22    -11    284       C  
ATOM    586  CG  LYS A 587      27.058 -12.015  10.225  1.00 15.81           C  
ANISOU  586  CG  LYS A 587     1867   2067   2073     31    -26    246       C  
ATOM    587  CD  LYS A 587      25.979 -11.056  10.725  1.00 20.59           C  
ANISOU  587  CD  LYS A 587     2458   2648   2718     51    -44    259       C  
ATOM    588  CE  LYS A 587      24.658 -11.241   9.993  1.00 20.24           C  
ANISOU  588  CE  LYS A 587     2409   2626   2654     64    -79    283       C  
ATOM    589  NZ  LYS A 587      23.549 -10.566  10.742  1.00 25.16           N  
ANISOU  589  NZ  LYS A 587     3004   3227   3330     88    -90    284       N  
ATOM    590  N   ALA A 588      30.385 -12.442   6.720  1.00 12.54           N  
ANISOU  590  N   ALA A 588     1519   1698   1549    -15     87    298       N  
ATOM    591  CA  ALA A 588      30.931 -12.159   5.378  1.00 12.81           C  
ANISOU  591  CA  ALA A 588     1585   1748   1534    -25    125    336       C  
ATOM    592  C   ALA A 588      30.868 -13.441   4.550  1.00 12.90           C  
ANISOU  592  C   ALA A 588     1626   1802   1471    -26    133    305       C  
ATOM    593  O   ALA A 588      31.809 -14.229   4.494  1.00 13.85           O  
ANISOU  593  O   ALA A 588     1740   1929   1593    -31    176    272       O  
ATOM    594  CB  ALA A 588      32.368 -11.660   5.491  1.00 14.38           C  
ANISOU  594  CB  ALA A 588     1761   1922   1780    -41    182    345       C  
ATOM    595  N   SER A 589      29.702 -13.663   3.932  1.00 12.10           N  
ANISOU  595  N   SER A 589     1556   1729   1313    -20     87    313       N  
ATOM    596  CA  SER A 589      29.457 -14.897   3.188  1.00 10.34           C  
ANISOU  596  CA  SER A 589     1366   1543   1020    -24     81    274       C  
ATOM    597  C   SER A 589      30.433 -15.215   2.050  1.00 14.76           C  
ANISOU  597  C   SER A 589     1966   2128   1516    -34    144    271       C  
ATOM    598  O   SER A 589      30.655 -16.383   1.736  1.00 14.66           O  
ANISOU  598  O   SER A 589     1969   2131   1469    -36    161    218       O  
ATOM    599  CB  SER A 589      28.022 -14.930   2.662  1.00 11.97           C  
ANISOU  599  CB  SER A 589     1595   1775   1179    -21     11    287       C  
ATOM    600  OG  SER A 589      27.885 -13.959   1.631  1.00 15.04           O  
ANISOU  600  OG  SER A 589     2021   2179   1514    -20      7    349       O  
ATOM    601  N   CYS A 590      31.007 -14.189   1.415  1.00 13.51           N  
ANISOU  601  N   CYS A 590     1825   1968   1340    -39    184    326       N  
ATOM    602  CA  CYS A 590      31.928 -14.436   0.306  1.00 14.19           C  
ANISOU  602  CA  CYS A 590     1951   2080   1360    -48    257    328       C  
ATOM    603  C   CYS A 590      33.328 -14.855   0.710  1.00 17.31           C  
ANISOU  603  C   CYS A 590     2307   2456   1815    -51    333    295       C  
ATOM    604  O   CYS A 590      34.141 -15.203  -0.142  1.00 18.04           O  
ANISOU  604  O   CYS A 590     2424   2568   1862    -56    405    286       O  
ATOM    605  CB  CYS A 590      31.937 -13.272  -0.675  1.00 15.31           C  
ANISOU  605  CB  CYS A 590     2136   2234   1449    -55    274    407       C  
ATOM    606  SG  CYS A 590      30.323 -13.005  -1.460  1.00 19.36           S  
ANISOU  606  SG  CYS A 590     2704   2782   1871    -48    179    445       S  
ATOM    607  N   GLU A 591      33.628 -14.804   2.026  1.00 14.12           N  
ANISOU  607  N   GLU A 591     1839   2013   1513    -47    318    278       N  
ATOM    608  CA  GLU A 591      34.919 -15.232   2.569  1.00 13.81           C  
ANISOU  608  CA  GLU A 591     1750   1954   1544    -47    373    248       C  
ATOM    609  C   GLU A 591      34.868 -16.683   2.987  1.00 15.21           C  
ANISOU  609  C   GLU A 591     1917   2133   1728    -34    360    181       C  
ATOM    610  O   GLU A 591      35.865 -17.233   3.441  1.00 15.01           O  
ANISOU  610  O   GLU A 591     1849   2092   1762    -28    397    153       O  
ATOM    611  CB  GLU A 591      35.321 -14.339   3.734  1.00 15.28           C  
ANISOU  611  CB  GLU A 591     1878   2099   1830    -53    357    269       C  
ATOM    612  CG  GLU A 591      35.489 -12.909   3.276  1.00 17.17           C  
ANISOU  612  CG  GLU A 591     2125   2323   2074    -68    378    336       C  
ATOM    613  CD  GLU A 591      35.823 -11.878   4.334  1.00 21.32           C  
ANISOU  613  CD  GLU A 591     2602   2802   2698    -79    359    353       C  
ATOM    614  OE1 GLU A 591      36.252 -12.266   5.447  1.00 21.61           O  
ANISOU  614  OE1 GLU A 591     2589   2820   2800    -76    340    313       O  
ATOM    615  OE2 GLU A 591      35.676 -10.676   4.030  1.00 19.93           O  
ANISOU  615  OE2 GLU A 591     2438   2604   2530    -89    363    408       O  
ATOM    616  N   ARG A 592      33.703 -17.334   2.789  1.00 14.93           N  
ANISOU  616  N   ARG A 592     1919   2117   1637    -30    307    157       N  
ATOM    617  CA  ARG A 592      33.543 -18.734   3.094  1.00 14.99           C  
ANISOU  617  CA  ARG A 592     1924   2120   1651    -21    294     95       C  
ATOM    618  C   ARG A 592      34.063 -19.533   1.920  1.00 25.06           C  
ANISOU  618  C   ARG A 592     3241   3417   2863    -20    354     59       C  
ATOM    619  O   ARG A 592      34.051 -19.051   0.791  1.00 29.19           O  
ANISOU  619  O   ARG A 592     3813   3971   3307    -28    382     81       O  
ATOM    620  CB  ARG A 592      32.054 -19.036   3.333  1.00 13.06           C  
ANISOU  620  CB  ARG A 592     1698   1884   1381    -23    214     86       C  
ATOM    621  CG  ARG A 592      31.527 -18.293   4.554  1.00 13.20           C  
ANISOU  621  CG  ARG A 592     1674   1879   1462    -21    165    115       C  
ATOM    622  CD  ARG A 592      30.051 -18.492   4.792  1.00 12.87           C  
ANISOU  622  CD  ARG A 592     1640   1844   1405    -22     96    112       C  
ATOM    623  NE  ARG A 592      29.580 -17.549   5.801  1.00 11.22           N  
ANISOU  623  NE  ARG A 592     1397   1616   1248    -17     65    144       N  
ATOM    624  CZ  ARG A 592      28.311 -17.156   5.947  1.00 11.58           C  
ANISOU  624  CZ  ARG A 592     1441   1668   1292    -15     13    161       C  
ATOM    625  NH1 ARG A 592      27.351 -17.654   5.157  1.00 11.91           N  
ANISOU  625  NH1 ARG A 592     1507   1735   1283    -21    -24    153       N  
ATOM    626  NH2 ARG A 592      28.003 -16.206   6.820  1.00 10.70           N  
ANISOU  626  NH2 ARG A 592     1301   1534   1228     -7     -2    187       N  
ATOM    627  N   HIS A 593      34.538 -20.726   2.179  1.00 22.60           N  
ANISOU  627  N   HIS A 593     2914   3087   2586     -8    377      4       N  
ATOM    628  CA  HIS A 593      34.988 -21.595   1.100  1.00 23.03           C  
ANISOU  628  CA  HIS A 593     3010   3156   2584     -3    438    -45       C  
ATOM    629  C   HIS A 593      33.923 -22.658   0.913  1.00 25.40           C  
ANISOU  629  C   HIS A 593     3351   3458   2841     -7    384    -98       C  
ATOM    630  O   HIS A 593      33.550 -23.369   1.852  1.00 23.04           O  
ANISOU  630  O   HIS A 593     3022   3128   2605     -2    341   -120       O  
ATOM    631  CB  HIS A 593      36.374 -22.182   1.376  1.00 24.56           C  
ANISOU  631  CB  HIS A 593     3156   3322   2855     16    513    -72       C  
ATOM    632  N   SER A 594      33.378 -22.727  -0.310  1.00 24.19           N  
ANISOU  632  N   SER A 594     3270   3343   2579    -20    382   -114       N  
ATOM    633  CA  SER A 594      32.309 -23.665  -0.673  1.00 24.13           C  
ANISOU  633  CA  SER A 594     3307   3341   2521    -32    323   -168       C  
ATOM    634  C   SER A 594      31.074 -23.499   0.240  1.00 24.15           C  
ANISOU  634  C   SER A 594     3278   3334   2566    -41    226   -144       C  
ATOM    635  O   SER A 594      30.391 -24.476   0.553  1.00 23.45           O  
ANISOU  635  O   SER A 594     3187   3224   2499    -48    183   -188       O  
ATOM    636  CB  SER A 594      32.825 -25.103  -0.692  1.00 30.35           C  
ANISOU  636  CB  SER A 594     4098   4095   3340    -20    365   -249       C  
ATOM    637  OG  SER A 594      34.010 -25.174  -1.468  1.00 42.72           O  
ANISOU  637  OG  SER A 594     5683   5669   4878     -7    467   -270       O  
ATOM    638  N   GLY A 595      30.832 -22.253   0.673  1.00 19.57           N  
ANISOU  638  N   GLY A 595     2670   2762   2004    -41    200    -74       N  
ATOM    639  CA  GLY A 595      29.688 -21.881   1.500  1.00 18.46           C  
ANISOU  639  CA  GLY A 595     2498   2615   1902    -47    120    -44       C  
ATOM    640  C   GLY A 595      29.865 -22.185   2.978  1.00 18.94           C  
ANISOU  640  C   GLY A 595     2496   2633   2066    -37    115    -46       C  
ATOM    641  O   GLY A 595      28.949 -21.933   3.755  1.00 17.18           O  
ANISOU  641  O   GLY A 595     2246   2403   1879    -40     61    -25       O  
ATOM    642  N   GLU A 596      31.026 -22.711   3.378  1.00 16.28           N  
ANISOU  642  N   GLU A 596     2137   2270   1780    -23    172    -67       N  
ATOM    643  CA  GLU A 596      31.238 -23.078   4.776  1.00 14.64           C  
ANISOU  643  CA  GLU A 596     1877   2024   1661    -12    161    -66       C  
ATOM    644  C   GLU A 596      32.015 -22.028   5.524  1.00 14.32           C  
ANISOU  644  C   GLU A 596     1795   1977   1669     -4    178    -21       C  
ATOM    645  O   GLU A 596      33.083 -21.563   5.065  1.00 14.77           O  
ANISOU  645  O   GLU A 596     1846   2038   1727      1    232    -10       O  
ATOM    646  CB  GLU A 596      32.042 -24.383   4.880  1.00 16.09           C  
ANISOU  646  CB  GLU A 596     2054   2176   1884      1    201   -115       C  
ATOM    647  CG  GLU A 596      31.267 -25.608   4.444  1.00 22.47           C  
ANISOU  647  CG  GLU A 596     2896   2972   2668    -10    178   -169       C  
ATOM    648  CD  GLU A 596      32.114 -26.850   4.291  1.00 32.90           C  
ANISOU  648  CD  GLU A 596     4220   4257   4023      6    227   -222       C  
ATOM    649  OE1 GLU A 596      33.279 -26.729   3.850  1.00 31.21           O  
ANISOU  649  OE1 GLU A 596     4002   4045   3813     23    293   -229       O  
ATOM    650  OE2 GLU A 596      31.610 -27.945   4.622  1.00 40.64           O  
ANISOU  650  OE2 GLU A 596     5204   5203   5036      2    203   -255       O  
ATOM    651  N   LEU A 597      31.455 -21.613   6.652  1.00 10.01           N  
ANISOU  651  N   LEU A 597     1221   1420   1164     -4    134      4       N  
ATOM    652  CA  LEU A 597      32.188 -20.811   7.607  1.00  9.67           C  
ANISOU  652  CA  LEU A 597     1136   1362   1175      3    141     33       C  
ATOM    653  C   LEU A 597      33.258 -21.738   8.237  1.00 11.76           C  
ANISOU  653  C   LEU A 597     1370   1600   1497     17    165     10       C  
ATOM    654  O   LEU A 597      32.940 -22.851   8.665  1.00 12.01           O  
ANISOU  654  O   LEU A 597     1402   1614   1545     23    148    -14       O  
ATOM    655  CB  LEU A 597      31.242 -20.341   8.716  1.00  9.45           C  
ANISOU  655  CB  LEU A 597     1093   1328   1170      1     90     52       C  
ATOM    656  CG  LEU A 597      31.895 -19.665   9.944  1.00 11.17           C  
ANISOU  656  CG  LEU A 597     1274   1527   1441      6     85     69       C  
ATOM    657  CD1 LEU A 597      32.424 -18.288   9.575  1.00 11.13           C  
ANISOU  657  CD1 LEU A 597     1264   1525   1440      0    104     99       C  
ATOM    658  CD2 LEU A 597      30.905 -19.556  11.065  1.00 10.65           C  
ANISOU  658  CD2 LEU A 597     1203   1457   1387      7     45     75       C  
ATOM    659  N   MET A 598      34.510 -21.287   8.245  1.00 11.12           N  
ANISOU  659  N   MET A 598     1259   1513   1452     23    202     21       N  
ATOM    660  CA  MET A 598      35.601 -22.035   8.848  1.00 11.88           C  
ANISOU  660  CA  MET A 598     1314   1585   1613     40    219      6       C  
ATOM    661  C   MET A 598      36.000 -21.335  10.145  1.00 14.51           C  
ANISOU  661  C   MET A 598     1606   1908   1999     40    183     32       C  
ATOM    662  O   MET A 598      36.263 -20.115  10.153  1.00 16.02           O  
ANISOU  662  O   MET A 598     1784   2105   2196     27    185     56       O  
ATOM    663  CB  MET A 598      36.809 -22.022   7.873  1.00 16.17           C  
ANISOU  663  CB  MET A 598     1844   2132   2168     46    291     -3       C  
ATOM    664  CG  MET A 598      38.033 -22.747   8.391  1.00 23.82           C  
ANISOU  664  CG  MET A 598     2759   3075   3218     69    312    -15       C  
ATOM    665  SD  MET A 598      39.633 -21.870   8.146  1.00 34.28           S  
ANISOU  665  SD  MET A 598     4019   4399   4606     67    370      6       S  
ATOM    666  CE  MET A 598      39.550 -20.786   9.669  1.00 28.10           C  
ANISOU  666  CE  MET A 598     3201   3610   3865     51    288     42       C  
ATOM    667  N   LEU A 599      35.993 -22.074  11.252  1.00 11.24           N  
ANISOU  667  N   LEU A 599     1176   1476   1619     52    147     29       N  
ATOM    668  CA  LEU A 599      36.487 -21.543  12.516  1.00 10.35           C  
ANISOU  668  CA  LEU A 599     1028   1356   1548     52    108     47       C  
ATOM    669  C   LEU A 599      37.627 -22.410  12.961  1.00 11.40           C  
ANISOU  669  C   LEU A 599     1119   1469   1744     74    110     43       C  
ATOM    670  O   LEU A 599      37.523 -23.656  12.927  1.00 13.66           O  
ANISOU  670  O   LEU A 599     1414   1738   2039     92    114     29       O  
ATOM    671  CB  LEU A 599      35.433 -21.584  13.642  1.00 10.55           C  
ANISOU  671  CB  LEU A 599     1076   1382   1551     49     56     56       C  
ATOM    672  CG  LEU A 599      34.139 -20.832  13.321  1.00 11.70           C  
ANISOU  672  CG  LEU A 599     1256   1544   1644     34     50     60       C  
ATOM    673  CD1 LEU A 599      33.141 -20.971  14.481  1.00 12.81           C  
ANISOU  673  CD1 LEU A 599     1411   1684   1770     33     12     66       C  
ATOM    674  CD2 LEU A 599      34.417 -19.330  13.110  1.00 13.61           C  
ANISOU  674  CD2 LEU A 599     1490   1792   1890     21     56     75       C  
ATOM    675  N   LEU A 600      38.727 -21.784  13.405  1.00  9.43           N  
ANISOU  675  N   LEU A 600      820   1216   1547     73    101     55       N  
ATOM    676  CA  LEU A 600      39.821 -22.525  14.039  1.00  9.72           C  
ANISOU  676  CA  LEU A 600      805   1234   1654     95     85     58       C  
ATOM    677  C   LEU A 600      39.680 -22.150  15.506  1.00 11.37           C  
ANISOU  677  C   LEU A 600     1011   1446   1861     89     10     75       C  
ATOM    678  O   LEU A 600      39.726 -20.962  15.811  1.00 10.61           O  
ANISOU  678  O   LEU A 600      911   1362   1760     67     -9     79       O  
ATOM    679  CB  LEU A 600      41.199 -22.149  13.472  1.00 10.77           C  
ANISOU  679  CB  LEU A 600      874   1364   1855     97    127     57       C  
ATOM    680  CG  LEU A 600      42.323 -22.945  14.109  1.00 12.18           C  
ANISOU  680  CG  LEU A 600      989   1522   2117    125    104     63       C  
ATOM    681  CD1 LEU A 600      42.214 -24.429  13.795  1.00 12.42           C  
ANISOU  681  CD1 LEU A 600     1033   1528   2158    159    130     48       C  
ATOM    682  CD2 LEU A 600      43.665 -22.423  13.659  1.00 13.55           C  
ANISOU  682  CD2 LEU A 600     1087   1693   2369    122    143     65       C  
ATOM    683  N   VAL A 601      39.410 -23.144  16.381  1.00  9.99           N  
ANISOU  683  N   VAL A 601      850   1261   1684    108    -29     84       N  
ATOM    684  CA  VAL A 601      39.162 -22.839  17.792  1.00  9.76           C  
ANISOU  684  CA  VAL A 601      834   1241   1632    102    -97    101       C  
ATOM    685  C   VAL A 601      40.062 -23.619  18.721  1.00 11.40           C  
ANISOU  685  C   VAL A 601     1007   1436   1888    127   -147    122       C  
ATOM    686  O   VAL A 601      40.628 -24.661  18.353  1.00 11.40           O  
ANISOU  686  O   VAL A 601      979   1412   1940    154   -128    126       O  
ATOM    687  CB  VAL A 601      37.665 -23.123  18.153  1.00 11.20           C  
ANISOU  687  CB  VAL A 601     1081   1430   1744     96   -102    104       C  
ATOM    688  CG1 VAL A 601      36.713 -22.374  17.227  1.00 11.00           C  
ANISOU  688  CG1 VAL A 601     1085   1417   1677     76    -63     88       C  
ATOM    689  CG2 VAL A 601      37.356 -24.623  18.129  1.00 10.98           C  
ANISOU  689  CG2 VAL A 601     1069   1379   1725    117    -94    113       C  
ATOM    690  N   ARG A 602      40.217 -23.095  19.959  1.00 10.84           N  
ANISOU  690  N   ARG A 602      938   1380   1800    118   -214    134       N  
ATOM    691  CA  ARG A 602      40.937 -23.789  21.000  1.00 11.15           C  
ANISOU  691  CA  ARG A 602      955   1413   1867    140   -278    161       C  
ATOM    692  C   ARG A 602      39.906 -24.210  22.049  1.00 14.34           C  
ANISOU  692  C   ARG A 602     1427   1826   2194    140   -311    183       C  
ATOM    693  O   ARG A 602      39.321 -23.333  22.728  1.00 13.35           O  
ANISOU  693  O   ARG A 602     1341   1726   2006    117   -333    173       O  
ATOM    694  CB  ARG A 602      42.008 -22.872  21.602  1.00 13.46           C  
ANISOU  694  CB  ARG A 602     1199   1720   2197    127   -337    158       C  
ATOM    695  CG  ARG A 602      42.900 -23.611  22.602  1.00 22.78           C  
ANISOU  695  CG  ARG A 602     2344   2896   3414    152   -415    191       C  
ATOM    696  CD  ARG A 602      43.952 -22.680  23.178  1.00 32.84           C  
ANISOU  696  CD  ARG A 602     3565   4186   4728    134   -482    182       C  
ATOM    697  NE  ARG A 602      45.042 -22.450  22.229  1.00 42.06           N  
ANISOU  697  NE  ARG A 602     4643   5337   5999    134   -446    171       N  
ATOM    698  CZ  ARG A 602      45.233 -21.326  21.545  1.00 49.96           C  
ANISOU  698  CZ  ARG A 602     5620   6340   7023    101   -407    142       C  
ATOM    699  NH1 ARG A 602      44.410 -20.294  21.703  1.00 42.02           N  
ANISOU  699  NH1 ARG A 602     4671   5348   5946     67   -404    120       N  
ATOM    700  NH2 ARG A 602      46.249 -21.224  20.698  1.00 27.36           N  
ANISOU  700  NH2 ARG A 602     2675   3464   4258    103   -365    139       N  
ATOM    701  N   PRO A 603      39.674 -25.522  22.230  1.00 13.78           N  
ANISOU  701  N   PRO A 603     1373   1733   2131    166   -309    211       N  
ATOM    702  CA  PRO A 603      38.748 -25.953  23.306  1.00 14.78           C  
ANISOU  702  CA  PRO A 603     1563   1868   2187    164   -335    241       C  
ATOM    703  C   PRO A 603      39.234 -25.464  24.687  1.00 18.70           C  
ANISOU  703  C   PRO A 603     2068   2392   2645    161   -417    260       C  
ATOM    704  O   PRO A 603      40.436 -25.290  24.894  1.00 19.79           O  
ANISOU  704  O   PRO A 603     2153   2532   2835    171   -467    264       O  
ATOM    705  CB  PRO A 603      38.839 -27.485  23.241  1.00 17.96           C  
ANISOU  705  CB  PRO A 603     1963   2230   2633    195   -328    275       C  
ATOM    706  CG  PRO A 603      39.217 -27.777  21.815  1.00 21.38           C  
ANISOU  706  CG  PRO A 603     2355   2636   3134    205   -268    242       C  
ATOM    707  CD  PRO A 603      40.228 -26.681  21.504  1.00 15.93           C  
ANISOU  707  CD  PRO A 603     1609   1967   2478    197   -278    218       C  
ATOM    708  N   ASN A 604      38.285 -25.228  25.634  1.00 20.16           N  
ANISOU  708  N   ASN A 604     2319   2601   2740    146   -429    269       N  
ATOM    709  CA  ASN A 604      38.602 -24.751  26.993  1.00 34.42           C  
ANISOU  709  CA  ASN A 604     4152   4440   4487    141   -503    280       C  
ATOM    710  C   ASN A 604      39.311 -25.807  27.824  1.00 58.61           C  
ANISOU  710  C   ASN A 604     7212   7495   7562    170   -569    338       C  
ATOM    711  O   ASN A 604      39.149 -26.989  27.546  1.00 37.43           O  
ANISOU  711  O   ASN A 604     4528   4779   4914    193   -544    375       O  
ATOM    712  CB  ASN A 604      37.347 -24.226  27.722  1.00 35.76           C  
ANISOU  712  CB  ASN A 604     4397   4637   4553    119   -482    270       C  
ATOM    713  CG  ASN A 604      36.227 -25.216  27.992  1.00 57.59           C  
ANISOU  713  CG  ASN A 604     7213   7392   7276    126   -439    309       C  
ATOM    714  OD1 ASN A 604      36.245 -26.381  27.573  1.00 57.34           O  
ANISOU  714  OD1 ASN A 604     7167   7327   7293    144   -421    343       O  
ATOM    715  ND2 ASN A 604      35.181 -24.742  28.657  1.00 43.75           N  
ANISOU  715  ND2 ASN A 604     5519   5666   5440    109   -414    301       N  
TER     716      ASN A 604                                                      
ATOM    717  N   HIS B 512      14.759   6.234 -11.681  1.00 32.35           N  
ANISOU  717  N   HIS B 512     3390   4584   4320    648   -294   1100       N  
ATOM    718  CA  HIS B 512      14.574   4.793 -11.858  1.00 31.28           C  
ANISOU  718  CA  HIS B 512     3143   4491   4251    519   -414   1102       C  
ATOM    719  C   HIS B 512      14.513   4.372 -13.347  1.00 31.55           C  
ANISOU  719  C   HIS B 512     3233   4511   4245    454   -615   1083       C  
ATOM    720  O   HIS B 512      13.931   3.349 -13.705  1.00 28.40           O  
ANISOU  720  O   HIS B 512     2724   4140   3926    372   -771   1111       O  
ATOM    721  CB  HIS B 512      13.385   4.271 -11.025  1.00 32.92           C  
ANISOU  721  CB  HIS B 512     3109   4779   4621    543   -397   1226       C  
ATOM    722  CG  HIS B 512      13.629   4.278  -9.545  1.00 35.98           C  
ANISOU  722  CG  HIS B 512     3479   5177   5014    595   -206   1227       C  
ATOM    723  ND1 HIS B 512      12.585   4.439  -8.644  1.00 39.38           N  
ANISOU  723  ND1 HIS B 512     3740   5672   5550    707    -97   1362       N  
ATOM    724  CD2 HIS B 512      14.786   4.143  -8.852  1.00 36.16           C  
ANISOU  724  CD2 HIS B 512     3640   5155   4944    563   -111   1116       C  
ATOM    725  CE1 HIS B 512      13.138   4.392  -7.441  1.00 37.98           C  
ANISOU  725  CE1 HIS B 512     3630   5485   5317    750     60   1321       C  
ATOM    726  NE2 HIS B 512      14.457   4.211  -7.513  1.00 36.60           N  
ANISOU  726  NE2 HIS B 512     3636   5244   5027    660     42   1170       N  
ATOM    727  N   ASP B 513      15.147   5.167 -14.210  1.00 27.71           N  
ANISOU  727  N   ASP B 513     2933   3968   3628    496   -611   1036       N  
ATOM    728  CA  ASP B 513      15.305   4.849 -15.634  1.00 27.43           C  
ANISOU  728  CA  ASP B 513     3018   3907   3498    467   -772   1006       C  
ATOM    729  C   ASP B 513      16.800   4.986 -15.970  1.00 27.52           C  
ANISOU  729  C   ASP B 513     3243   3844   3371    439   -671    909       C  
ATOM    730  O   ASP B 513      17.573   5.427 -15.108  1.00 25.53           O  
ANISOU  730  O   ASP B 513     3016   3561   3124    436   -506    873       O  
ATOM    731  CB  ASP B 513      14.407   5.696 -16.550  1.00 31.01           C  
ANISOU  731  CB  ASP B 513     3477   4373   3931    578   -875   1088       C  
ATOM    732  CG  ASP B 513      14.569   7.202 -16.453  1.00 37.79           C  
ANISOU  732  CG  ASP B 513     4424   5195   4740    707   -724   1123       C  
ATOM    733  OD1 ASP B 513      13.810   7.918 -17.130  1.00 39.65           O  
ANISOU  733  OD1 ASP B 513     4662   5442   4962    812   -797   1200       O  
ATOM    734  OD2 ASP B 513      15.458   7.664 -15.692  1.00 36.78           O  
ANISOU  734  OD2 ASP B 513     4368   5016   4592    702   -545   1072       O  
ATOM    735  N   ASN B 514      17.219   4.543 -17.180  1.00 23.56           N  
ANISOU  735  N   ASN B 514     2889   3311   2750    420   -774    868       N  
ATOM    736  CA  ASN B 514      18.622   4.559 -17.627  1.00 22.50           C  
ANISOU  736  CA  ASN B 514     2943   3112   2493    405   -669    801       C  
ATOM    737  C   ASN B 514      19.517   3.758 -16.665  1.00 23.09           C  
ANISOU  737  C   ASN B 514     2976   3182   2616    304   -575    730       C  
ATOM    738  O   ASN B 514      20.689   4.048 -16.484  1.00 22.49           O  
ANISOU  738  O   ASN B 514     2979   3060   2506    291   -435    692       O  
ATOM    739  CB  ASN B 514      19.121   5.997 -17.848  1.00 29.02           C  
ANISOU  739  CB  ASN B 514     3875   3881   3268    492   -522    839       C  
ATOM    740  CG  ASN B 514      20.391   6.096 -18.654  1.00 62.98           C  
ANISOU  740  CG  ASN B 514     8363   8116   7450    497   -427    814       C  
ATOM    741  OD1 ASN B 514      20.400   5.912 -19.878  1.00 61.68           O  
ANISOU  741  OD1 ASN B 514     8342   7939   7153    553   -499    828       O  
ATOM    742  ND2 ASN B 514      21.495   6.393 -17.977  1.00 54.69           N  
ANISOU  742  ND2 ASN B 514     7315   7019   6446    449   -264    784       N  
ATOM    743  N   LEU B 515      18.952   2.737 -16.046  1.00 16.73           N  
ANISOU  743  N   LEU B 515     2033   2420   1902    233   -658    721       N  
ATOM    744  CA  LEU B 515      19.711   1.978 -15.087  1.00 14.87           C  
ANISOU  744  CA  LEU B 515     1758   2184   1709    153   -575    664       C  
ATOM    745  C   LEU B 515      20.549   0.889 -15.748  1.00 16.84           C  
ANISOU  745  C   LEU B 515     2127   2398   1872     97   -621    592       C  
ATOM    746  O   LEU B 515      20.237   0.478 -16.866  1.00 16.45           O  
ANISOU  746  O   LEU B 515     2173   2333   1745    110   -761    584       O  
ATOM    747  CB  LEU B 515      18.738   1.393 -14.064  1.00 15.31           C  
ANISOU  747  CB  LEU B 515     1617   2296   1905    116   -612    708       C  
ATOM    748  CG  LEU B 515      17.828   2.404 -13.392  1.00 19.47           C  
ANISOU  748  CG  LEU B 515     2025   2861   2510    201   -550    792       C  
ATOM    749  CD1 LEU B 515      16.841   1.696 -12.475  1.00 22.63           C  
ANISOU  749  CD1 LEU B 515     2222   3321   3056    174   -571    863       C  
ATOM    750  CD2 LEU B 515      18.645   3.416 -12.548  1.00 20.83           C  
ANISOU  750  CD2 LEU B 515     2262   3002   2652    254   -369    759       C  
ATOM    751  N   VAL B 516      21.620   0.449 -15.062  1.00 14.58           N  
ANISOU  751  N   VAL B 516     1851   2098   1592     49   -509    537       N  
ATOM    752  CA  VAL B 516      22.544  -0.560 -15.554  1.00 15.55           C  
ANISOU  752  CA  VAL B 516     2084   2186   1638     14   -517    474       C  
ATOM    753  C   VAL B 516      22.686  -1.649 -14.511  1.00 17.34           C  
ANISOU  753  C   VAL B 516     2214   2428   1947    -64   -514    442       C  
ATOM    754  O   VAL B 516      22.863  -1.364 -13.314  1.00 14.50           O  
ANISOU  754  O   VAL B 516     1753   2093   1663    -76   -416    449       O  
ATOM    755  CB  VAL B 516      23.915   0.087 -15.893  1.00 19.14           C  
ANISOU  755  CB  VAL B 516     2653   2601   2019     53   -359    460       C  
ATOM    756  CG1 VAL B 516      24.912  -0.954 -16.394  1.00 19.80           C  
ANISOU  756  CG1 VAL B 516     2846   2656   2023     44   -338    410       C  
ATOM    757  CG2 VAL B 516      23.757   1.201 -16.937  1.00 19.85           C  
ANISOU  757  CG2 VAL B 516     2847   2666   2028    140   -343    513       C  
ATOM    758  N   LEU B 517      22.575  -2.903 -14.969  1.00 16.47           N  
ANISOU  758  N   LEU B 517     2152   2294   1813   -108   -631    407       N  
ATOM    759  CA  LEU B 517      22.684  -4.084 -14.133  1.00 16.83           C  
ANISOU  759  CA  LEU B 517     2127   2336   1931   -181   -641    383       C  
ATOM    760  C   LEU B 517      24.113  -4.599 -14.198  1.00 18.03           C  
ANISOU  760  C   LEU B 517     2391   2456   2004   -173   -542    320       C  
ATOM    761  O   LEU B 517      24.633  -4.894 -15.282  1.00 18.32           O  
ANISOU  761  O   LEU B 517     2590   2449   1923   -133   -564    284       O  
ATOM    762  CB  LEU B 517      21.641  -5.132 -14.584  1.00 18.53           C  
ANISOU  762  CB  LEU B 517     2323   2522   2196   -242   -844    389       C  
ATOM    763  CG  LEU B 517      21.353  -6.261 -13.629  1.00 23.25           C  
ANISOU  763  CG  LEU B 517     2804   3111   2918   -328   -866    403       C  
ATOM    764  CD1 LEU B 517      20.923  -5.759 -12.255  1.00 23.83           C  
ANISOU  764  CD1 LEU B 517     2689   3254   3112   -326   -747    480       C  
ATOM    765  CD2 LEU B 517      20.279  -7.165 -14.209  1.00 26.95           C  
ANISOU  765  CD2 LEU B 517     3248   3528   3463   -402  -1092    417       C  
ATOM    766  N   ILE B 518      24.781  -4.595 -13.044  1.00 16.10           N  
ANISOU  766  N   ILE B 518     2066   2235   1816   -189   -422    314       N  
ATOM    767  CA  ILE B 518      26.177  -5.015 -12.920  1.00 16.00           C  
ANISOU  767  CA  ILE B 518     2115   2203   1760   -178   -321    269       C  
ATOM    768  C   ILE B 518      26.223  -6.332 -12.145  1.00 17.64           C  
ANISOU  768  C   ILE B 518     2282   2405   2017   -228   -350    249       C  
ATOM    769  O   ILE B 518      25.511  -6.505 -11.144  1.00 18.15           O  
ANISOU  769  O   ILE B 518     2226   2498   2172   -264   -366    282       O  
ATOM    770  CB  ILE B 518      26.974  -3.894 -12.212  1.00 20.00           C  
ANISOU  770  CB  ILE B 518     2565   2732   2302   -157   -189    277       C  
ATOM    771  CG1 ILE B 518      26.940  -2.602 -13.055  1.00 22.67           C  
ANISOU  771  CG1 ILE B 518     2957   3055   2601   -110   -154    309       C  
ATOM    772  CG2 ILE B 518      28.441  -4.308 -11.921  1.00 22.16           C  
ANISOU  772  CG2 ILE B 518     2855   2993   2572   -153    -94    244       C  
ATOM    773  CD1 ILE B 518      27.235  -1.489 -12.376  1.00 32.08           C  
ANISOU  773  CD1 ILE B 518     4089   4248   3850   -104    -78    321       C  
ATOM    774  N   ARG B 519      27.037  -7.264 -12.624  1.00 16.18           N  
ANISOU  774  N   ARG B 519     2204   2176   1767   -215   -343    205       N  
ATOM    775  CA  ARG B 519      27.204  -8.558 -11.978  1.00 16.88           C  
ANISOU  775  CA  ARG B 519     2278   2242   1893   -251   -363    186       C  
ATOM    776  C   ARG B 519      28.678  -8.836 -11.824  1.00 17.17           C  
ANISOU  776  C   ARG B 519     2360   2276   1889   -204   -245    157       C  
ATOM    777  O   ARG B 519      29.449  -8.646 -12.768  1.00 17.30           O  
ANISOU  777  O   ARG B 519     2482   2272   1819   -143   -190    142       O  
ATOM    778  CB  ARG B 519      26.548  -9.666 -12.815  1.00 21.72           C  
ANISOU  778  CB  ARG B 519     2996   2778   2477   -281   -515    161       C  
ATOM    779  CG  ARG B 519      25.068  -9.850 -12.479  1.00 38.95           C  
ANISOU  779  CG  ARG B 519     5063   4959   4778   -362   -646    210       C  
ATOM    780  CD  ARG B 519      24.366 -10.812 -13.420  1.00 54.48           C  
ANISOU  780  CD  ARG B 519     7133   6832   6736   -407   -841    179       C  
ATOM    781  NE  ARG B 519      24.037 -10.185 -14.701  1.00 66.20           N  
ANISOU  781  NE  ARG B 519     8732   8302   8119   -362   -938    156       N  
ATOM    782  CZ  ARG B 519      22.800  -9.984 -15.151  1.00 80.75           C  
ANISOU  782  CZ  ARG B 519    10526  10135  10021   -405  -1109    186       C  
ATOM    783  NH1 ARG B 519      21.752 -10.367 -14.430  1.00 64.74           N  
ANISOU  783  NH1 ARG B 519     8314   8108   8176   -503  -1192    252       N  
ATOM    784  NH2 ARG B 519      22.602  -9.408 -16.329  1.00 68.63           N  
ANISOU  784  NH2 ARG B 519     9120   8588   8368   -343  -1197    162       N  
ATOM    785  N   MET B 520      29.086  -9.259 -10.635  1.00 14.12           N  
ANISOU  785  N   MET B 520     1888   1914   1564   -219   -198    159       N  
ATOM    786  CA  MET B 520      30.491  -9.566 -10.387  1.00 13.54           C  
ANISOU  786  CA  MET B 520     1827   1843   1473   -174   -101    139       C  
ATOM    787  C   MET B 520      30.646 -10.661  -9.377  1.00 16.05           C  
ANISOU  787  C   MET B 520     2112   2157   1830   -186   -108    137       C  
ATOM    788  O   MET B 520      29.852 -10.788  -8.438  1.00 15.82           O  
ANISOU  788  O   MET B 520     2004   2148   1860   -225   -142    164       O  
ATOM    789  CB  MET B 520      31.280  -8.327  -9.956  1.00 13.78           C  
ANISOU  789  CB  MET B 520     1774   1921   1541   -156    -13    151       C  
ATOM    790  CG  MET B 520      30.829  -7.759  -8.621  1.00 13.49           C  
ANISOU  790  CG  MET B 520     1625   1928   1571   -183    -26    160       C  
ATOM    791  SD  MET B 520      31.711  -6.253  -8.208  1.00 13.85           S  
ANISOU  791  SD  MET B 520     1603   1992   1666   -172     33    155       S  
ATOM    792  CE  MET B 520      30.834  -5.088  -9.115  1.00 12.48           C  
ANISOU  792  CE  MET B 520     1461   1805   1476   -177     25    181       C  
ATOM    793  N   LYS B 521      31.708 -11.438  -9.554  1.00 14.52           N  
ANISOU  793  N   LYS B 521     1978   1939   1601   -136    -58    116       N  
ATOM    794  CA  LYS B 521      32.024 -12.492  -8.606  1.00 14.00           C  
ANISOU  794  CA  LYS B 521     1890   1864   1563   -129    -54    118       C  
ATOM    795  C   LYS B 521      33.131 -11.977  -7.671  1.00 14.37           C  
ANISOU  795  C   LYS B 521     1836   1976   1648    -91     20    123       C  
ATOM    796  O   LYS B 521      34.018 -11.243  -8.147  1.00 14.33           O  
ANISOU  796  O   LYS B 521     1811   1991   1644    -60     82    122       O  
ATOM    797  CB  LYS B 521      32.531 -13.737  -9.371  1.00 18.57           C  
ANISOU  797  CB  LYS B 521     2611   2365   2079    -80    -54     91       C  
ATOM    798  CG  LYS B 521      31.401 -14.462 -10.095  1.00 26.95           C  
ANISOU  798  CG  LYS B 521     3785   3337   3117   -130   -175     73       C  
ATOM    799  CD  LYS B 521      31.785 -15.877 -10.480  1.00 41.35           C  
ANISOU  799  CD  LYS B 521     5759   5060   4892    -87   -196     40       C  
ATOM    800  CE  LYS B 521      30.558 -16.677 -10.851  1.00 57.43           C  
ANISOU  800  CE  LYS B 521     7877   6989   6954   -169   -355     25       C  
ATOM    801  NZ  LYS B 521      30.680 -18.106 -10.447  1.00 68.03           N  
ANISOU  801  NZ  LYS B 521     9293   8233   8324   -171   -383     20       N  
ATOM    802  N   PRO B 522      33.111 -12.321  -6.374  1.00 12.77           N  
ANISOU  802  N   PRO B 522     1571   1801   1480    -90     11    136       N  
ATOM    803  CA  PRO B 522      34.180 -11.881  -5.478  1.00 12.72           C  
ANISOU  803  CA  PRO B 522     1483   1847   1502    -49     41    129       C  
ATOM    804  C   PRO B 522      35.496 -12.568  -5.836  1.00 14.09           C  
ANISOU  804  C   PRO B 522     1672   2009   1674     14     92    126       C  
ATOM    805  O   PRO B 522      35.505 -13.638  -6.467  1.00 16.62           O  
ANISOU  805  O   PRO B 522     2088   2275   1951     41    107    126       O  
ATOM    806  CB  PRO B 522      33.679 -12.345  -4.105  1.00 14.65           C  
ANISOU  806  CB  PRO B 522     1705   2113   1750    -40     13    149       C  
ATOM    807  CG  PRO B 522      32.862 -13.560  -4.408  1.00 19.18           C  
ANISOU  807  CG  PRO B 522     2348   2625   2314    -65     -2    176       C  
ATOM    808  CD  PRO B 522      32.124 -13.160  -5.657  1.00 15.42           C  
ANISOU  808  CD  PRO B 522     1911   2115   1833   -120    -31    167       C  
ATOM    809  N   ASP B 523      36.618 -11.966  -5.402  1.00 11.92           N  
ANISOU  809  N   ASP B 523     1300   1777   1453     41    112    126       N  
ATOM    810  CA  ASP B 523      37.896 -12.580  -5.640  1.00 12.35           C  
ANISOU  810  CA  ASP B 523     1332   1831   1529    112    168    143       C  
ATOM    811  C   ASP B 523      38.121 -13.713  -4.613  1.00 16.29           C  
ANISOU  811  C   ASP B 523     1842   2336   2013    163    137    146       C  
ATOM    812  O   ASP B 523      37.224 -13.977  -3.805  1.00 16.67           O  
ANISOU  812  O   ASP B 523     1922   2383   2030    139     85    141       O  
ATOM    813  CB  ASP B 523      39.011 -11.530  -5.663  1.00 13.43           C  
ANISOU  813  CB  ASP B 523     1335   2003   1766    111    192    160       C  
ATOM    814  CG  ASP B 523      39.286 -10.827  -4.352  1.00 15.21           C  
ANISOU  814  CG  ASP B 523     1456   2266   2056     84     96    136       C  
ATOM    815  OD1 ASP B 523      38.880 -11.361  -3.278  1.00 12.95           O  
ANISOU  815  OD1 ASP B 523     1204   1996   1721    105     31    114       O  
ATOM    816  OD2 ASP B 523      39.996  -9.798  -4.368  1.00 17.36           O  
ANISOU  816  OD2 ASP B 523     1620   2544   2431     53     84    143       O  
ATOM    817  N   GLU B 524      39.315 -14.338  -4.608  1.00 16.49           N  
ANISOU  817  N   GLU B 524     1832   2369   2064    244    179    167       N  
ATOM    818  CA  GLU B 524      39.598 -15.469  -3.713  1.00 18.10           C  
ANISOU  818  CA  GLU B 524     2058   2572   2246    311    155    177       C  
ATOM    819  C   GLU B 524      39.633 -15.076  -2.229  1.00 23.21           C  
ANISOU  819  C   GLU B 524     2634   3275   2911    310     64    167       C  
ATOM    820  O   GLU B 524      39.697 -15.963  -1.384  1.00 26.22           O  
ANISOU  820  O   GLU B 524     3051   3657   3256    370     41    182       O  
ATOM    821  CB  GLU B 524      40.890 -16.197  -4.135  1.00 20.67           C  
ANISOU  821  CB  GLU B 524     2361   2896   2598    417    229    211       C  
ATOM    822  CG  GLU B 524      42.155 -15.358  -4.046  1.00 29.15           C  
ANISOU  822  CG  GLU B 524     3255   4033   3789    437    238    239       C  
ATOM    823  CD  GLU B 524      43.459 -16.118  -4.234  1.00 51.53           C  
ANISOU  823  CD  GLU B 524     6027   6880   6671    558    312    294       C  
ATOM    824  OE1 GLU B 524      43.423 -17.293  -4.667  1.00 47.32           O  
ANISOU  824  OE1 GLU B 524     5625   6296   6059    643    380    305       O  
ATOM    825  OE2 GLU B 524      44.525 -15.527  -3.950  1.00 47.13           O  
ANISOU  825  OE2 GLU B 524     5287   6377   6242    570    296    331       O  
ATOM    826  N   ASN B 525      39.563 -13.772  -1.917  1.00 17.52           N  
ANISOU  826  N   ASN B 525     1836   2590   2231    254      9    140       N  
ATOM    827  CA  ASN B 525      39.550 -13.246  -0.543  1.00 17.64           C  
ANISOU  827  CA  ASN B 525     1820   2645   2238    266    -94    113       C  
ATOM    828  C   ASN B 525      38.156 -12.672  -0.195  1.00 19.19           C  
ANISOU  828  C   ASN B 525     2086   2835   2371    219   -108     97       C  
ATOM    829  O   ASN B 525      38.010 -11.977   0.820  1.00 20.20           O  
ANISOU  829  O   ASN B 525     2214   2988   2473    236   -182     68       O  
ATOM    830  CB  ASN B 525      40.643 -12.194  -0.355  1.00 19.61           C  
ANISOU  830  CB  ASN B 525     1936   2920   2593    250   -166     90       C  
ATOM    831  CG  ASN B 525      42.036 -12.736  -0.623  1.00 31.50           C  
ANISOU  831  CG  ASN B 525     3337   4444   4189    306   -147    129       C  
ATOM    832  OD1 ASN B 525      42.452 -13.764  -0.081  1.00 29.75           O  
ANISOU  832  OD1 ASN B 525     3132   4237   3934    392   -158    149       O  
ATOM    833  ND2 ASN B 525      42.775 -12.059  -1.473  1.00 28.91           N  
ANISOU  833  ND2 ASN B 525     2893   4111   3982    267   -104    155       N  
ATOM    834  N   GLY B 526      37.172 -12.907  -1.077  1.00 15.40           N  
ANISOU  834  N   GLY B 526     1664   2318   1869    167    -44    117       N  
ATOM    835  CA  GLY B 526      35.809 -12.418  -0.868  1.00 15.32           C  
ANISOU  835  CA  GLY B 526     1693   2305   1824    126    -45    124       C  
ATOM    836  C   GLY B 526      35.635 -10.916  -1.035  1.00 18.90           C  
ANISOU  836  C   GLY B 526     2106   2770   2304     82    -72     89       C  
ATOM    837  O   GLY B 526      34.679 -10.318  -0.525  1.00 18.71           O  
ANISOU  837  O   GLY B 526     2105   2755   2247     80    -82     91       O  
ATOM    838  N   ARG B 527      36.552 -10.284  -1.789  1.00 15.53           N  
ANISOU  838  N   ARG B 527     1619   2336   1947     53    -71     69       N  
ATOM    839  CA  ARG B 527      36.520  -8.836  -2.010  1.00 15.11           C  
ANISOU  839  CA  ARG B 527     1528   2274   1939      5    -95     43       C  
ATOM    840  C   ARG B 527      36.019  -8.529  -3.408  1.00 13.66           C  
ANISOU  840  C   ARG B 527     1363   2062   1764    -45    -28     67       C  
ATOM    841  O   ARG B 527      36.241  -9.300  -4.343  1.00 13.03           O  
ANISOU  841  O   ARG B 527     1310   1967   1675    -38     30     93       O  
ATOM    842  CB  ARG B 527      37.929  -8.246  -1.888  1.00 18.04           C  
ANISOU  842  CB  ARG B 527     1799   2643   2412     -1   -141     24       C  
ATOM    843  CG  ARG B 527      38.583  -8.423  -0.519  1.00 28.48           C  
ANISOU  843  CG  ARG B 527     3101   3989   3730     53   -249    -11       C  
ATOM    844  CD  ARG B 527      40.091  -8.237  -0.571  1.00 46.27           C  
ANISOU  844  CD  ARG B 527     5223   6241   6117     44   -298     -7       C  
ATOM    845  NE  ARG B 527      40.499  -6.834  -0.694  1.00 61.94           N  
ANISOU  845  NE  ARG B 527     7134   8183   8218    -30   -361    -31       N  
ATOM    846  CZ  ARG B 527      41.707  -6.432  -1.083  1.00 76.69           C  
ANISOU  846  CZ  ARG B 527     8853  10032  10253    -72   -377      0       C  
ATOM    847  NH1 ARG B 527      42.629  -7.320  -1.436  1.00 61.62           N  
ANISOU  847  NH1 ARG B 527     6852   8156   8405    -32   -319     60       N  
ATOM    848  NH2 ARG B 527      41.987  -5.138  -1.164  1.00 66.43           N  
ANISOU  848  NH2 ARG B 527     7492   8673   9075   -152   -440    -16       N  
ATOM    849  N   PHE B 528      35.404  -7.354  -3.550  1.00 11.50           N  
ANISOU  849  N   PHE B 528     1093   1776   1500    -81    -40     57       N  
ATOM    850  CA  PHE B 528      34.900  -6.897  -4.840  1.00 10.61           C  
ANISOU  850  CA  PHE B 528     1007   1637   1386   -118     11     82       C  
ATOM    851  C   PHE B 528      35.726  -5.762  -5.440  1.00 13.26           C  
ANISOU  851  C   PHE B 528     1289   1943   1805   -147     36     89       C  
ATOM    852  O   PHE B 528      35.747  -5.637  -6.664  1.00 13.78           O  
ANISOU  852  O   PHE B 528     1380   1989   1866   -154    105    126       O  
ATOM    853  CB  PHE B 528      33.454  -6.462  -4.688  1.00 11.34           C  
ANISOU  853  CB  PHE B 528     1140   1733   1433   -127     -8     87       C  
ATOM    854  CG  PHE B 528      32.521  -7.590  -4.388  1.00 11.58           C  
ANISOU  854  CG  PHE B 528     1204   1779   1415   -116    -14    112       C  
ATOM    855  CD1 PHE B 528      32.215  -8.537  -5.362  1.00 12.97           C  
ANISOU  855  CD1 PHE B 528     1426   1931   1571   -135     -3    133       C  
ATOM    856  CD2 PHE B 528      31.985  -7.750  -3.110  1.00 11.59           C  
ANISOU  856  CD2 PHE B 528     1202   1808   1392    -78    -30    119       C  
ATOM    857  CE1 PHE B 528      31.338  -9.597  -5.073  1.00 12.96           C  
ANISOU  857  CE1 PHE B 528     1445   1921   1558   -143    -24    163       C  
ATOM    858  CE2 PHE B 528      31.126  -8.814  -2.819  1.00 12.75           C  
ANISOU  858  CE2 PHE B 528     1362   1959   1522    -74    -19    168       C  
ATOM    859  CZ  PHE B 528      30.808  -9.727  -3.796  1.00 12.28           C  
ANISOU  859  CZ  PHE B 528     1326   1865   1475   -118    -23    190       C  
ATOM    860  N   GLY B 529      36.385  -4.962  -4.608  1.00 12.17           N  
ANISOU  860  N   GLY B 529     1088   1794   1742   -162    -24     59       N  
ATOM    861  CA  GLY B 529      37.251  -3.905  -5.093  1.00 14.20           C  
ANISOU  861  CA  GLY B 529     1272   2005   2119   -207     -8     79       C  
ATOM    862  C   GLY B 529      36.667  -2.523  -5.224  1.00 15.79           C  
ANISOU  862  C   GLY B 529     1501   2155   2343   -244    -26     69       C  
ATOM    863  O   GLY B 529      37.268  -1.682  -5.882  1.00 18.17           O  
ANISOU  863  O   GLY B 529     1751   2404   2747   -287     14    108       O  
ATOM    864  N   PHE B 530      35.532  -2.241  -4.588  1.00 13.11           N  
ANISOU  864  N   PHE B 530     1239   1823   1919   -220    -73     30       N  
ATOM    865  CA  PHE B 530      34.998  -0.898  -4.674  1.00 12.54           C  
ANISOU  865  CA  PHE B 530     1203   1695   1866   -238    -87     21       C  
ATOM    866  C   PHE B 530      34.653  -0.420  -3.291  1.00 15.94           C  
ANISOU  866  C   PHE B 530     1684   2111   2260   -200   -186    -51       C  
ATOM    867  O   PHE B 530      34.519  -1.224  -2.367  1.00 16.04           O  
ANISOU  867  O   PHE B 530     1718   2174   2201   -148   -222    -79       O  
ATOM    868  CB  PHE B 530      33.737  -0.846  -5.560  1.00 12.26           C  
ANISOU  868  CB  PHE B 530     1232   1677   1750   -218    -22     64       C  
ATOM    869  CG  PHE B 530      32.533  -1.617  -5.042  1.00 11.12           C  
ANISOU  869  CG  PHE B 530     1130   1593   1503   -169    -34     61       C  
ATOM    870  CD1 PHE B 530      31.496  -0.961  -4.370  1.00 11.74           C  
ANISOU  870  CD1 PHE B 530     1250   1672   1539   -124    -55     51       C  
ATOM    871  CD2 PHE B 530      32.392  -2.977  -5.305  1.00 11.37           C  
ANISOU  871  CD2 PHE B 530     1158   1671   1490   -164    -13     84       C  
ATOM    872  CE1 PHE B 530      30.360  -1.659  -3.956  1.00 11.66           C  
ANISOU  872  CE1 PHE B 530     1250   1718   1463    -79    -42     80       C  
ATOM    873  CE2 PHE B 530      31.243  -3.663  -4.909  1.00 12.03           C  
ANISOU  873  CE2 PHE B 530     1261   1795   1515   -136    -21    103       C  
ATOM    874  CZ  PHE B 530      30.242  -3.009  -4.222  1.00 12.00           C  
ANISOU  874  CZ  PHE B 530     1270   1801   1488    -96    -29    110       C  
ATOM    875  N   ASN B 531      34.490   0.887  -3.159  1.00 13.96           N  
ANISOU  875  N   ASN B 531     1473   1785   2048   -211   -223    -78       N  
ATOM    876  CA  ASN B 531      34.087   1.508  -1.904  1.00 13.86           C  
ANISOU  876  CA  ASN B 531     1551   1740   1977   -150   -314   -154       C  
ATOM    877  C   ASN B 531      32.727   2.157  -2.091  1.00 14.93           C  
ANISOU  877  C   ASN B 531     1769   1871   2035    -93   -256   -131       C  
ATOM    878  O   ASN B 531      32.389   2.611  -3.203  1.00 14.79           O  
ANISOU  878  O   ASN B 531     1734   1832   2053   -127   -187    -74       O  
ATOM    879  CB  ASN B 531      35.063   2.612  -1.460  1.00 15.29           C  
ANISOU  879  CB  ASN B 531     1732   1804   2274   -201   -436   -219       C  
ATOM    880  CG  ASN B 531      36.507   2.215  -1.290  1.00 22.88           C  
ANISOU  880  CG  ASN B 531     2579   2754   3360   -269   -516   -231       C  
ATOM    881  OD1 ASN B 531      36.902   1.068  -1.494  1.00 21.92           O  
ANISOU  881  OD1 ASN B 531     2382   2715   3232   -267   -470   -192       O  
ATOM    882  ND2 ASN B 531      37.310   3.175  -0.853  1.00 25.28           N  
ANISOU  882  ND2 ASN B 531     2871   2944   3789   -326   -652   -288       N  
ATOM    883  N   VAL B 532      31.947   2.230  -1.003  1.00 14.12           N  
ANISOU  883  N   VAL B 532     1758   1785   1820     12   -278   -167       N  
ATOM    884  CA  VAL B 532      30.683   2.961  -1.034  1.00 14.38           C  
ANISOU  884  CA  VAL B 532     1862   1810   1790     89   -222   -141       C  
ATOM    885  C   VAL B 532      30.644   4.005   0.041  1.00 18.51           C  
ANISOU  885  C   VAL B 532     2520   2249   2264    175   -297   -225       C  
ATOM    886  O   VAL B 532      31.200   3.806   1.129  1.00 17.34           O  
ANISOU  886  O   VAL B 532     2434   2089   2067    218   -387   -300       O  
ATOM    887  CB  VAL B 532      29.410   2.102  -0.956  1.00 18.42           C  
ANISOU  887  CB  VAL B 532     2355   2428   2217    163   -128    -63       C  
ATOM    888  CG1 VAL B 532      29.210   1.286  -2.224  1.00 19.19           C  
ANISOU  888  CG1 VAL B 532     2350   2579   2361     81    -74     14       C  
ATOM    889  CG2 VAL B 532      29.375   1.235   0.295  1.00 17.98           C  
ANISOU  889  CG2 VAL B 532     2332   2428   2070    246   -137    -79       C  
ATOM    890  N   LYS B 533      29.950   5.111  -0.247  1.00 16.46           N  
ANISOU  890  N   LYS B 533     2327   1927   2002    216   -265   -214       N  
ATOM    891  CA  LYS B 533      29.637   6.160   0.714  1.00 16.40           C  
ANISOU  891  CA  LYS B 533     2484   1829   1919    331   -316   -289       C  
ATOM    892  C   LYS B 533      28.104   6.312   0.686  1.00 17.96           C  
ANISOU  892  C   LYS B 533     2712   2088   2026    465   -185   -207       C  
ATOM    893  O   LYS B 533      27.438   5.917  -0.286  1.00 16.39           O  
ANISOU  893  O   LYS B 533     2398   1965   1865    428    -94   -105       O  
ATOM    894  CB  LYS B 533      30.281   7.501   0.338  1.00 19.24           C  
ANISOU  894  CB  LYS B 533     2897   2025   2390    258   -400   -345       C  
ATOM    895  CG  LYS B 533      31.740   7.618   0.714  1.00 32.62           C  
ANISOU  895  CG  LYS B 533     4579   3627   4188    152   -561   -436       C  
ATOM    896  CD  LYS B 533      32.299   8.991   0.353  1.00 40.77           C  
ANISOU  896  CD  LYS B 533     5656   4475   5360     68   -643   -475       C  
ATOM    897  CE  LYS B 533      33.781   9.062   0.640  1.00 48.88           C  
ANISOU  897  CE  LYS B 533     6621   5409   6541    -63   -813   -543       C  
ATOM    898  NZ  LYS B 533      34.457  10.109  -0.172  1.00 57.37           N  
ANISOU  898  NZ  LYS B 533     7643   6328   7829   -203   -843   -515       N  
ATOM    899  N   GLY B 534      27.549   6.858   1.753  1.00 17.26           N  
ANISOU  899  N   GLY B 534     2776   1966   1815    630   -181   -249       N  
ATOM    900  CA  GLY B 534      26.118   7.161   1.784  1.00 17.51           C  
ANISOU  900  CA  GLY B 534     2830   2046   1775    779    -46   -160       C  
ATOM    901  C   GLY B 534      25.241   6.148   2.483  1.00 19.88           C  
ANISOU  901  C   GLY B 534     3092   2482   1981    900     68    -73       C  
ATOM    902  O   GLY B 534      25.715   5.135   3.009  1.00 19.32           O  
ANISOU  902  O   GLY B 534     2994   2469   1878    878     46    -84       O  
ATOM    903  N   GLY B 535      23.953   6.444   2.496  1.00 18.55           N  
ANISOU  903  N   GLY B 535     2913   2359   1778   1034    197     28       N  
ATOM    904  CA  GLY B 535      22.972   5.602   3.163  1.00 19.35           C  
ANISOU  904  CA  GLY B 535     2957   2580   1814   1163    334    146       C  
ATOM    905  C   GLY B 535      21.983   6.467   3.902  1.00 25.39           C  
ANISOU  905  C   GLY B 535     3849   3328   2471   1402    449    185       C  
ATOM    906  O   GLY B 535      22.251   7.652   4.126  1.00 26.43           O  
ANISOU  906  O   GLY B 535     4161   3337   2544   1475    391     82       O  
ATOM    907  N   TYR B 536      20.831   5.885   4.250  1.00 24.54           N  
ANISOU  907  N   TYR B 536     3640   3333   2350   1525    615    344       N  
ATOM    908  CA  TYR B 536      19.731   6.600   4.907  1.00 28.28           C  
ANISOU  908  CA  TYR B 536     4199   3815   2732   1781    771    426       C  
ATOM    909  C   TYR B 536      20.165   7.404   6.150  1.00 33.37           C  
ANISOU  909  C   TYR B 536     5157   4355   3167   1986    750    292       C  
ATOM    910  O   TYR B 536      19.754   8.552   6.304  1.00 34.42           O  
ANISOU  910  O   TYR B 536     5437   4408   3234   2141    784    265       O  
ATOM    911  CB  TYR B 536      18.582   5.641   5.223  1.00 31.97           C  
ANISOU  911  CB  TYR B 536     4484   4425   3238   1871    959    636       C  
ATOM    912  N   ASP B 537      21.035   6.825   6.991  1.00 30.24           N  
ANISOU  912  N   ASP B 537     4878   3947   2664   1987    673    198       N  
ATOM    913  CA  ASP B 537      21.601   7.450   8.187  1.00 30.91           C  
ANISOU  913  CA  ASP B 537     5281   3925   2538   2166    600     46       C  
ATOM    914  C   ASP B 537      22.494   8.680   7.910  1.00 36.88           C  
ANISOU  914  C   ASP B 537     6209   4498   3307   2087    390   -150       C  
ATOM    915  O   ASP B 537      22.567   9.581   8.752  1.00 38.71           O  
ANISOU  915  O   ASP B 537     6724   4610   3373   2276    346   -262       O  
ATOM    916  CB  ASP B 537      22.360   6.404   9.020  1.00 30.81           C  
ANISOU  916  CB  ASP B 537     5319   3955   2432   2159    541      2       C  
ATOM    917  CG  ASP B 537      23.566   5.774   8.333  1.00 26.34           C  
ANISOU  917  CG  ASP B 537     4618   3381   2010   1871    353    -81       C  
ATOM    918  OD1 ASP B 537      23.471   5.471   7.114  1.00 26.82           O  
ANISOU  918  OD1 ASP B 537     4441   3484   2265   1667    359    -12       O  
ATOM    919  OD2 ASP B 537      24.558   5.481   9.036  1.00 33.93           O  
ANISOU  919  OD2 ASP B 537     5704   4304   2883   1867    211   -199       O  
ATOM    920  N   GLN B 538      23.156   8.717   6.733  1.00 31.57           N  
ANISOU  920  N   GLN B 538     5373   3793   2830   1817    267   -184       N  
ATOM    921  CA  GLN B 538      24.037   9.802   6.286  1.00 30.56           C  
ANISOU  921  CA  GLN B 538     5347   3490   2775   1697     82   -333       C  
ATOM    922  C   GLN B 538      23.248  10.854   5.494  1.00 34.33           C  
ANISOU  922  C   GLN B 538     5812   3911   3319   1732    160   -275       C  
ATOM    923  O   GLN B 538      23.844  11.845   5.062  1.00 33.79           O  
ANISOU  923  O   GLN B 538     5829   3685   3323   1642     33   -374       O  
ATOM    924  CB  GLN B 538      25.175   9.253   5.390  1.00 29.93           C  
ANISOU  924  CB  GLN B 538     5083   3412   2877   1402    -56   -368       C  
ATOM    925  CG  GLN B 538      26.161   8.307   6.095  1.00 27.71           C  
ANISOU  925  CG  GLN B 538     4811   3164   2553   1349   -168   -440       C  
ATOM    926  CD  GLN B 538      27.367   7.915   5.275  1.00 34.97           C  
ANISOU  926  CD  GLN B 538     5569   4067   3653   1087   -303   -479       C  
ATOM    927  OE1 GLN B 538      27.729   8.534   4.256  1.00 29.40           O  
ANISOU  927  OE1 GLN B 538     4785   3285   3101    935   -347   -483       O  
ATOM    928  NE2 GLN B 538      28.051   6.882   5.729  1.00 31.99           N  
ANISOU  928  NE2 GLN B 538     5145   3756   3255   1044   -361   -499       N  
ATOM    929  N   LYS B 539      21.925  10.614   5.265  1.00 30.07           N  
ANISOU  929  N   LYS B 539     5149   3499   2777   1853    364   -101       N  
ATOM    930  CA  LYS B 539      21.004  11.448   4.473  1.00 30.14           C  
ANISOU  930  CA  LYS B 539     5105   3493   2855   1906    458     -9       C  
ATOM    931  C   LYS B 539      21.580  11.755   3.072  1.00 31.74           C  
ANISOU  931  C   LYS B 539     5179   3638   3241   1656    350    -25       C  
ATOM    932  O   LYS B 539      21.448  12.864   2.540  1.00 31.21           O  
ANISOU  932  O   LYS B 539     5186   3458   3215   1671    333    -40       O  
ATOM    933  CB  LYS B 539      20.556  12.707   5.240  1.00 35.56           C  
ANISOU  933  CB  LYS B 539     6070   4049   3394   2165    499    -68       C  
ATOM    934  CG  LYS B 539      19.585  12.434   6.393  1.00 51.25           C  
ANISOU  934  CG  LYS B 539     8146   6125   5200   2467    690     20       C  
ATOM    935  CD  LYS B 539      18.217  11.913   5.916  1.00 62.24           C  
ANISOU  935  CD  LYS B 539     9269   7697   6681   2535    909    261       C  
ATOM    936  CE  LYS B 539      17.052  12.691   6.483  1.00 75.91           C  
ANISOU  936  CE  LYS B 539    11117   9424   8300   2860   1103    356       C  
ATOM    937  NZ  LYS B 539      16.813  12.378   7.917  1.00 87.36           N  
ANISOU  937  NZ  LYS B 539    12751  10906   9534   3128   1234    368       N  
ATOM    938  N   MET B 540      22.266  10.755   2.501  1.00 26.52           N  
ANISOU  938  N   MET B 540     4344   3051   2682   1439    283    -18       N  
ATOM    939  CA  MET B 540      22.927  10.889   1.213  1.00 26.78           C  
ANISOU  939  CA  MET B 540     4264   3041   2869   1215    198    -25       C  
ATOM    940  C   MET B 540      22.688   9.613   0.408  1.00 24.39           C  
ANISOU  940  C   MET B 540     3718   2898   2650   1086    241     88       C  
ATOM    941  O   MET B 540      22.618   8.531   1.000  1.00 21.05           O  
ANISOU  941  O   MET B 540     3233   2578   2186   1099    272    114       O  
ATOM    942  CB  MET B 540      24.453  11.079   1.415  1.00 30.83           C  
ANISOU  942  CB  MET B 540     4867   3426   3423   1070     26   -177       C  
ATOM    943  CG  MET B 540      24.861  12.445   1.991  1.00 38.63           C  
ANISOU  943  CG  MET B 540     6099   4208   4372   1143    -72   -307       C  
ATOM    944  SD  MET B 540      24.798  13.813   0.799  1.00 46.13           S  
ANISOU  944  SD  MET B 540     7070   5005   5452   1077    -75   -279       S  
ATOM    945  CE  MET B 540      26.317  13.517  -0.112  1.00 42.34           C  
ANISOU  945  CE  MET B 540     6448   4474   5166    780   -196   -307       C  
ATOM    946  N   PRO B 541      22.615   9.681  -0.940  1.00 19.97           N  
ANISOU  946  N   PRO B 541     3037   2350   2200    962    233    151       N  
ATOM    947  CA  PRO B 541      22.450   8.439  -1.704  1.00 17.62           C  
ANISOU  947  CA  PRO B 541     2544   2183   1968    842    243    236       C  
ATOM    948  C   PRO B 541      23.673   7.548  -1.560  1.00 18.52           C  
ANISOU  948  C   PRO B 541     2635   2302   2100    699    165    159       C  
ATOM    949  O   PRO B 541      24.773   8.035  -1.258  1.00 18.81           O  
ANISOU  949  O   PRO B 541     2772   2231   2143    648     82     49       O  
ATOM    950  CB  PRO B 541      22.320   8.923  -3.155  1.00 21.00           C  
ANISOU  950  CB  PRO B 541     2916   2587   2479    759    227    290       C  
ATOM    951  CG  PRO B 541      22.906  10.272  -3.182  1.00 27.04           C  
ANISOU  951  CG  PRO B 541     3834   3191   3250    771    191    214       C  
ATOM    952  CD  PRO B 541      22.689  10.866  -1.821  1.00 23.56           C  
ANISOU  952  CD  PRO B 541     3547   2690   2714    936    210    149       C  
ATOM    953  N   VAL B 542      23.480   6.252  -1.801  1.00 15.77           N  
ANISOU  953  N   VAL B 542     2149   2067   1775    634    183    221       N  
ATOM    954  CA  VAL B 542      24.577   5.275  -1.807  1.00 13.85           C  
ANISOU  954  CA  VAL B 542     1869   1840   1554    506    121    167       C  
ATOM    955  C   VAL B 542      25.326   5.423  -3.144  1.00 17.47           C  
ANISOU  955  C   VAL B 542     2287   2254   2097    361     74    159       C  
ATOM    956  O   VAL B 542      24.720   5.273  -4.213  1.00 16.08           O  
ANISOU  956  O   VAL B 542     2040   2118   1953    331     94    237       O  
ATOM    957  CB  VAL B 542      24.023   3.850  -1.627  1.00 17.89           C  
ANISOU  957  CB  VAL B 542     2263   2471   2063    499    163    245       C  
ATOM    958  CG1 VAL B 542      25.148   2.831  -1.679  1.00 16.60           C  
ANISOU  958  CG1 VAL B 542     2071   2318   1919    381    105    193       C  
ATOM    959  CG2 VAL B 542      23.254   3.738  -0.307  1.00 19.34           C  
ANISOU  959  CG2 VAL B 542     2484   2699   2165    662    245    283       C  
ATOM    960  N   ILE B 543      26.584   5.866  -3.066  1.00 14.40           N  
ANISOU  960  N   ILE B 543     1955   1772   1744    290     10     73       N  
ATOM    961  CA  ILE B 543      27.422   6.153  -4.234  1.00 14.77           C  
ANISOU  961  CA  ILE B 543     1972   1761   1879    171     -7     79       C  
ATOM    962  C   ILE B 543      28.693   5.349  -4.170  1.00 17.41           C  
ANISOU  962  C   ILE B 543     2253   2101   2259     70    -49     37       C  
ATOM    963  O   ILE B 543      29.325   5.262  -3.112  1.00 18.20           O  
ANISOU  963  O   ILE B 543     2386   2177   2351     78   -112    -39       O  
ATOM    964  CB  ILE B 543      27.719   7.697  -4.302  1.00 19.02           C  
ANISOU  964  CB  ILE B 543     2608   2153   2465    179    -28     46       C  
ATOM    965  CG1 ILE B 543      26.430   8.557  -4.323  1.00 20.09           C  
ANISOU  965  CG1 ILE B 543     2808   2277   2548    306     22     91       C  
ATOM    966  CG2 ILE B 543      28.718   8.107  -5.417  1.00 20.64           C  
ANISOU  966  CG2 ILE B 543     2781   2279   2781     58    -26     71       C  
ATOM    967  CD1 ILE B 543      25.545   8.485  -5.553  1.00 28.61           C  
ANISOU  967  CD1 ILE B 543     3822   3419   3628    315     79    200       C  
ATOM    968  N   VAL B 544      29.111   4.831  -5.325  1.00 15.42           N  
ANISOU  968  N   VAL B 544     1934   1875   2050    -12    -19     87       N  
ATOM    969  CA  VAL B 544      30.385   4.129  -5.433  1.00 14.55           C  
ANISOU  969  CA  VAL B 544     1764   1766   1997    -96    -37     66       C  
ATOM    970  C   VAL B 544      31.459   5.240  -5.382  1.00 17.67           C  
ANISOU  970  C   VAL B 544     2172   2035   2508   -156    -75     33       C  
ATOM    971  O   VAL B 544      31.486   6.115  -6.256  1.00 18.28           O  
ANISOU  971  O   VAL B 544     2265   2041   2639   -180    -31     82       O  
ATOM    972  CB  VAL B 544      30.431   3.322  -6.743  1.00 15.36           C  
ANISOU  972  CB  VAL B 544     1822   1922   2093   -135     22    135       C  
ATOM    973  CG1 VAL B 544      31.827   2.754  -6.975  1.00 14.98           C  
ANISOU  973  CG1 VAL B 544     1714   1865   2113   -202     32    130       C  
ATOM    974  CG2 VAL B 544      29.391   2.231  -6.757  1.00 14.89           C  
ANISOU  974  CG2 VAL B 544     1747   1960   1949    -97     24    161       C  
ATOM    975  N   SER B 545      32.271   5.256  -4.312  1.00 15.54           N  
ANISOU  975  N   SER B 545     1900   1725   2278   -175   -167    -47       N  
ATOM    976  CA  SER B 545      33.266   6.312  -4.102  1.00 17.43           C  
ANISOU  976  CA  SER B 545     2143   1826   2654   -245   -244    -87       C  
ATOM    977  C   SER B 545      34.658   5.960  -4.643  1.00 22.20           C  
ANISOU  977  C   SER B 545     2613   2413   3407   -354   -238    -47       C  
ATOM    978  O   SER B 545      35.536   6.838  -4.690  1.00 22.81           O  
ANISOU  978  O   SER B 545     2653   2368   3647   -437   -288    -47       O  
ATOM    979  CB  SER B 545      33.354   6.648  -2.621  1.00 19.30           C  
ANISOU  979  CB  SER B 545     2469   2010   2852   -195   -382   -203       C  
ATOM    980  OG  SER B 545      33.616   5.464  -1.878  1.00 21.46           O  
ANISOU  980  OG  SER B 545     2710   2384   3060   -167   -420   -237       O  
ATOM    981  N   ARG B 546      34.869   4.692  -5.047  1.00 17.71           N  
ANISOU  981  N   ARG B 546     1969   1959   2800   -352   -174     -5       N  
ATOM    982  CA  ARG B 546      36.158   4.251  -5.572  1.00 17.51           C  
ANISOU  982  CA  ARG B 546     1814   1933   2905   -426   -141     48       C  
ATOM    983  C   ARG B 546      35.992   2.884  -6.183  1.00 18.52           C  
ANISOU  983  C   ARG B 546     1919   2183   2936   -385    -47     95       C  
ATOM    984  O   ARG B 546      35.224   2.062  -5.668  1.00 15.68           O  
ANISOU  984  O   ARG B 546     1611   1904   2444   -325    -69     56       O  
ATOM    985  CB  ARG B 546      37.201   4.125  -4.433  1.00 22.33           C  
ANISOU  985  CB  ARG B 546     2357   2515   3613   -465   -285    -25       C  
ATOM    986  CG  ARG B 546      38.650   4.081  -4.939  1.00 32.57           C  
ANISOU  986  CG  ARG B 546     3485   3776   5114   -555   -262     48       C  
ATOM    987  CD  ARG B 546      39.648   3.827  -3.834  1.00 40.97           C  
ANISOU  987  CD  ARG B 546     4465   4826   6277   -589   -428    -20       C  
ATOM    988  NE  ARG B 546      40.977   3.520  -4.370  1.00 52.79           N  
ANISOU  988  NE  ARG B 546     5766   6322   7970   -656   -381     75       N  
ATOM    989  CZ  ARG B 546      41.590   2.347  -4.244  1.00 66.29           C  
ANISOU  989  CZ  ARG B 546     7385   8129   9672   -621   -364     96       C  
ATOM    990  NH1 ARG B 546      41.008   1.352  -3.584  1.00 49.82           N  
ANISOU  990  NH1 ARG B 546     5392   6140   7396   -532   -398     26       N  
ATOM    991  NH2 ARG B 546      42.793   2.161  -4.770  1.00 55.21           N  
ANISOU  991  NH2 ARG B 546     5793   6722   8463   -668   -302    199       N  
ATOM    992  N   VAL B 547      36.705   2.647  -7.291  1.00 16.68           N  
ANISOU  992  N   VAL B 547     1618   1952   2769   -410     66    187       N  
ATOM    993  CA  VAL B 547      36.791   1.335  -7.943  1.00 14.86           C  
ANISOU  993  CA  VAL B 547     1380   1812   2454   -365    152    227       C  
ATOM    994  C   VAL B 547      38.303   1.094  -8.121  1.00 17.29           C  
ANISOU  994  C   VAL B 547     1550   2107   2915   -400    197    284       C  
ATOM    995  O   VAL B 547      38.985   1.862  -8.810  1.00 18.11           O  
ANISOU  995  O   VAL B 547     1587   2143   3151   -440    277    370       O  
ATOM    996  CB  VAL B 547      36.007   1.202  -9.268  1.00 18.45           C  
ANISOU  996  CB  VAL B 547     1929   2289   2792   -315    260    291       C  
ATOM    997  CG1 VAL B 547      36.143  -0.223  -9.822  1.00 18.44           C  
ANISOU  997  CG1 VAL B 547     1950   2361   2696   -263    317    309       C  
ATOM    998  CG2 VAL B 547      34.527   1.528  -9.061  1.00 18.04           C  
ANISOU  998  CG2 VAL B 547     1976   2250   2628   -284    203    250       C  
ATOM    999  N   ALA B 548      38.832   0.077  -7.441  1.00 16.09           N  
ANISOU  999  N   ALA B 548     1341   2012   2760   -383    148    248       N  
ATOM   1000  CA  ALA B 548      40.274  -0.177  -7.514  1.00 18.07           C  
ANISOU 1000  CA  ALA B 548     1435   2258   3173   -407    182    310       C  
ATOM   1001  C   ALA B 548      40.633  -0.906  -8.811  1.00 17.24           C  
ANISOU 1001  C   ALA B 548     1332   2192   3028   -341    369    414       C  
ATOM   1002  O   ALA B 548      39.891  -1.797  -9.224  1.00 16.12           O  
ANISOU 1002  O   ALA B 548     1316   2104   2707   -269    409    394       O  
ATOM   1003  CB  ALA B 548      40.746  -0.955  -6.296  1.00 19.62           C  
ANISOU 1003  CB  ALA B 548     1574   2500   3379   -396     53    238       C  
ATOM   1004  N   PRO B 549      41.727  -0.547  -9.488  1.00 16.47           N  
ANISOU 1004  N   PRO B 549     1107   2059   3091   -355    487    532       N  
ATOM   1005  CA  PRO B 549      42.024  -1.207 -10.758  1.00 16.88           C  
ANISOU 1005  CA  PRO B 549     1197   2145   3071   -257    688    637       C  
ATOM   1006  C   PRO B 549      42.338  -2.691 -10.574  1.00 18.26           C  
ANISOU 1006  C   PRO B 549     1382   2397   3157   -172    700    612       C  
ATOM   1007  O   PRO B 549      42.966  -3.089  -9.588  1.00 18.04           O  
ANISOU 1007  O   PRO B 549     1236   2394   3224   -195    601    577       O  
ATOM   1008  CB  PRO B 549      43.244  -0.456 -11.281  1.00 20.16           C  
ANISOU 1008  CB  PRO B 549     1436   2505   3719   -292    815    786       C  
ATOM   1009  CG  PRO B 549      43.821   0.260 -10.109  1.00 23.39           C  
ANISOU 1009  CG  PRO B 549     1674   2860   4351   -420    641    744       C  
ATOM   1010  CD  PRO B 549      42.703   0.505  -9.149  1.00 17.00           C  
ANISOU 1010  CD  PRO B 549      996   2043   3418   -457    445    583       C  
ATOM   1011  N   GLY B 550      41.882  -3.484 -11.537  1.00 15.58           N  
ANISOU 1011  N   GLY B 550     1203   2086   2632    -66    810    628       N  
ATOM   1012  CA  GLY B 550      42.184  -4.904 -11.636  1.00 15.51           C  
ANISOU 1012  CA  GLY B 550     1243   2127   2524     36    854    619       C  
ATOM   1013  C   GLY B 550      41.332  -5.792 -10.761  1.00 16.25           C  
ANISOU 1013  C   GLY B 550     1428   2251   2495     27    698    492       C  
ATOM   1014  O   GLY B 550      41.562  -7.004 -10.698  1.00 17.10           O  
ANISOU 1014  O   GLY B 550     1579   2386   2532    103    714    477       O  
ATOM   1015  N   THR B 551      40.396  -5.194 -10.010  1.00 14.35           N  
ANISOU 1015  N   THR B 551     1210   2002   2241    -58    556    411       N  
ATOM   1016  CA  THR B 551      39.530  -5.930  -9.100  1.00 13.44           C  
ANISOU 1016  CA  THR B 551     1165   1915   2027    -66    426    315       C  
ATOM   1017  C   THR B 551      38.294  -6.404  -9.829  1.00 13.90           C  
ANISOU 1017  C   THR B 551     1400   1966   1916    -37    427    288       C  
ATOM   1018  O   THR B 551      38.010  -5.942 -10.932  1.00 14.12           O  
ANISOU 1018  O   THR B 551     1505   1968   1893    -16    498    327       O  
ATOM   1019  CB  THR B 551      39.141  -5.021  -7.929  1.00 13.62           C  
ANISOU 1019  CB  THR B 551     1131   1930   2114   -146    290    255       C  
ATOM   1020  OG1 THR B 551      38.359  -3.934  -8.422  1.00 14.50           O  
ANISOU 1020  OG1 THR B 551     1296   2003   2209   -184    297    260       O  
ATOM   1021  CG2 THR B 551      40.361  -4.517  -7.130  1.00 16.74           C  
ANISOU 1021  CG2 THR B 551     1359   2315   2688   -187    236    264       C  
ATOM   1022  N   PRO B 552      37.463  -7.252  -9.185  1.00 12.56           N  
ANISOU 1022  N   PRO B 552     1294   1813   1667    -41    334    226       N  
ATOM   1023  CA  PRO B 552      36.234  -7.689  -9.853  1.00 11.50           C  
ANISOU 1023  CA  PRO B 552     1303   1659   1407    -33    303    205       C  
ATOM   1024  C   PRO B 552      35.369  -6.529 -10.326  1.00 12.19           C  
ANISOU 1024  C   PRO B 552     1417   1733   1481    -71    285    214       C  
ATOM   1025  O   PRO B 552      34.807  -6.587 -11.410  1.00 12.79           O  
ANISOU 1025  O   PRO B 552     1607   1786   1467    -42    297    226       O  
ATOM   1026  CB  PRO B 552      35.545  -8.518  -8.769  1.00 12.54           C  
ANISOU 1026  CB  PRO B 552     1437   1808   1520    -56    206    160       C  
ATOM   1027  CG  PRO B 552      36.711  -9.157  -8.049  1.00 15.50           C  
ANISOU 1027  CG  PRO B 552     1738   2203   1947    -20    228    162       C  
ATOM   1028  CD  PRO B 552      37.705  -8.012  -7.944  1.00 13.28           C  
ANISOU 1028  CD  PRO B 552     1332   1932   1781    -38    263    189       C  
ATOM   1029  N   ALA B 553      35.250  -5.458  -9.529  1.00 11.65           N  
ANISOU 1029  N   ALA B 553     1260   1672   1494   -123    246    205       N  
ATOM   1030  CA  ALA B 553      34.399  -4.309  -9.887  1.00 12.44           C  
ANISOU 1030  CA  ALA B 553     1387   1753   1586   -148    230    216       C  
ATOM   1031  C   ALA B 553      34.951  -3.517 -11.069  1.00 14.91           C  
ANISOU 1031  C   ALA B 553     1723   2029   1912   -127    332    280       C  
ATOM   1032  O   ALA B 553      34.186  -2.875 -11.792  1.00 14.44           O  
ANISOU 1032  O   ALA B 553     1735   1952   1801   -117    333    301       O  
ATOM   1033  CB  ALA B 553      34.228  -3.391  -8.689  1.00 13.70           C  
ANISOU 1033  CB  ALA B 553     1473   1913   1821   -188    167    185       C  
ATOM   1034  N   ASP B 554      36.264  -3.599 -11.316  1.00 13.28           N  
ANISOU 1034  N   ASP B 554     1454   1813   1777   -107    428    326       N  
ATOM   1035  CA  ASP B 554      36.891  -2.906 -12.406  1.00 14.34           C  
ANISOU 1035  CA  ASP B 554     1598   1913   1939    -76    560    415       C  
ATOM   1036  C   ASP B 554      36.831  -3.748 -13.672  1.00 17.03           C  
ANISOU 1036  C   ASP B 554     2089   2255   2126     27    643    445       C  
ATOM   1037  O   ASP B 554      36.826  -3.184 -14.774  1.00 18.15           O  
ANISOU 1037  O   ASP B 554     2313   2368   2213     81    738    513       O  
ATOM   1038  CB  ASP B 554      38.352  -2.653 -12.036  1.00 14.92           C  
ANISOU 1038  CB  ASP B 554     1508   1975   2186    -99    630    470       C  
ATOM   1039  CG  ASP B 554      39.119  -1.847 -13.051  1.00 19.57           C  
ANISOU 1039  CG  ASP B 554     2065   2519   2852    -76    792    593       C  
ATOM   1040  OD1 ASP B 554      38.609  -0.794 -13.465  1.00 20.97           O  
ANISOU 1040  OD1 ASP B 554     2285   2652   3031    -99    803    622       O  
ATOM   1041  OD2 ASP B 554      40.214  -2.280 -13.440  1.00 21.11           O  
ANISOU 1041  OD2 ASP B 554     2192   2723   3106    -23    919    673       O  
ATOM   1042  N   LEU B 555      36.839  -5.082 -13.518  1.00 14.96           N  
ANISOU 1042  N   LEU B 555     1880   2016   1789     67    610    397       N  
ATOM   1043  CA  LEU B 555      36.907  -5.974 -14.664  1.00 16.12           C  
ANISOU 1043  CA  LEU B 555     2196   2146   1783    179    678    411       C  
ATOM   1044  C   LEU B 555      35.591  -6.546 -15.145  1.00 19.56           C  
ANISOU 1044  C   LEU B 555     2807   2563   2061    191    550    343       C  
ATOM   1045  O   LEU B 555      35.577  -7.188 -16.197  1.00 22.30           O  
ANISOU 1045  O   LEU B 555     3335   2879   2261    292    581    342       O  
ATOM   1046  CB  LEU B 555      37.940  -7.084 -14.404  1.00 17.45           C  
ANISOU 1046  CB  LEU B 555     2331   2327   1970    239    743    416       C  
ATOM   1047  CG  LEU B 555      39.367  -6.611 -14.030  1.00 22.75           C  
ANISOU 1047  CG  LEU B 555     2804   3018   2820    237    866    502       C  
ATOM   1048  CD1 LEU B 555      40.285  -7.796 -13.794  1.00 24.03           C  
ANISOU 1048  CD1 LEU B 555     2939   3199   2992    315    921    510       C  
ATOM   1049  CD2 LEU B 555      39.969  -5.670 -15.112  1.00 26.17           C  
ANISOU 1049  CD2 LEU B 555     3234   3428   3283    293   1045    626       C  
ATOM   1050  N   CYS B 556      34.479  -6.316 -14.420  1.00 16.96           N  
ANISOU 1050  N   CYS B 556     2433   2247   1763     98    404    291       N  
ATOM   1051  CA  CYS B 556      33.203  -6.850 -14.894  1.00 17.20           C  
ANISOU 1051  CA  CYS B 556     2596   2255   1683     96    268    242       C  
ATOM   1052  C   CYS B 556      32.691  -6.027 -16.050  1.00 20.97           C  
ANISOU 1052  C   CYS B 556     3187   2712   2067    144    273    276       C  
ATOM   1053  O   CYS B 556      33.154  -4.896 -16.269  1.00 18.46           O  
ANISOU 1053  O   CYS B 556     2821   2400   1794    157    380    341       O  
ATOM   1054  CB  CYS B 556      32.185  -6.946 -13.757  1.00 16.95           C  
ANISOU 1054  CB  CYS B 556     2461   2248   1730     -4    135    202       C  
ATOM   1055  SG  CYS B 556      31.929  -5.399 -12.863  1.00 18.34           S  
ANISOU 1055  SG  CYS B 556     2481   2461   2026    -66    146    230       S  
ATOM   1056  N   VAL B 557      31.791  -6.615 -16.854  1.00 20.73           N  
ANISOU 1056  N   VAL B 557     3319   2648   1908    177    151    236       N  
ATOM   1057  CA  VAL B 557      31.231  -5.938 -18.023  1.00 21.18           C  
ANISOU 1057  CA  VAL B 557     3514   2685   1847    242    126    262       C  
ATOM   1058  C   VAL B 557      29.688  -6.072 -18.001  1.00 25.63           C  
ANISOU 1058  C   VAL B 557     4089   3244   2406    178    -94    218       C  
ATOM   1059  O   VAL B 557      29.185  -7.192 -18.118  1.00 27.53           O  
ANISOU 1059  O   VAL B 557     4410   3447   2605    161   -234    157       O  
ATOM   1060  CB  VAL B 557      31.847  -6.430 -19.364  1.00 26.07           C  
ANISOU 1060  CB  VAL B 557     4371   3257   2277    395    205    272       C  
ATOM   1061  CG1 VAL B 557      31.281  -5.634 -20.544  1.00 27.14           C  
ANISOU 1061  CG1 VAL B 557     4662   3375   2274    479    181    308       C  
ATOM   1062  CG2 VAL B 557      33.371  -6.362 -19.351  1.00 25.55           C  
ANISOU 1062  CG2 VAL B 557     4258   3202   2246    464    441    341       C  
ATOM   1063  N   PRO B 558      28.918  -4.986 -17.806  1.00 22.21           N  
ANISOU 1063  N   PRO B 558     3563   2841   2034    138   -132    254       N  
ATOM   1064  CA  PRO B 558      29.353  -3.591 -17.621  1.00 21.57           C  
ANISOU 1064  CA  PRO B 558     3394   2782   2018    144      5    323       C  
ATOM   1065  C   PRO B 558      30.137  -3.404 -16.330  1.00 23.91           C  
ANISOU 1065  C   PRO B 558     3512   3105   2469     74    101    325       C  
ATOM   1066  O   PRO B 558      29.901  -4.103 -15.345  1.00 20.79           O  
ANISOU 1066  O   PRO B 558     3026   2731   2143      9     35    281       O  
ATOM   1067  CB  PRO B 558      28.034  -2.789 -17.582  1.00 23.53           C  
ANISOU 1067  CB  PRO B 558     3597   3049   2295    117   -113    340       C  
ATOM   1068  CG  PRO B 558      26.971  -3.718 -18.132  1.00 29.66           C  
ANISOU 1068  CG  PRO B 558     4464   3810   2996    116   -315    295       C  
ATOM   1069  CD  PRO B 558      27.444  -5.105 -17.781  1.00 24.43           C  
ANISOU 1069  CD  PRO B 558     3821   3126   2336     84   -334    234       C  
ATOM   1070  N   ARG B 559      31.079  -2.459 -16.384  1.00 19.77           N  
ANISOU 1070  N   ARG B 559     2946   2570   1997     92    250    383       N  
ATOM   1071  CA AARG B 559      31.971  -2.068 -15.302  0.50 19.64           C  
ANISOU 1071  CA AARG B 559     2771   2560   2131     31    327    389       C  
ATOM   1072  CA BARG B 559      31.941  -2.122 -15.277  0.50 19.81           C  
ANISOU 1072  CA BARG B 559     2793   2584   2152     30    321    386       C  
ATOM   1073  C   ARG B 559      31.219  -1.266 -14.248  1.00 20.43           C  
ANISOU 1073  C   ARG B 559     2763   2674   2327    -37    252    368       C  
ATOM   1074  O   ARG B 559      30.313  -0.516 -14.587  1.00 19.19           O  
ANISOU 1074  O   ARG B 559     2639   2510   2142    -23    209    389       O  
ATOM   1075  CB AARG B 559      33.108  -1.186 -15.879  0.50 21.01           C  
ANISOU 1075  CB AARG B 559     2935   2697   2351     66    496    477       C  
ATOM   1076  CB BARG B 559      33.137  -1.359 -15.836  0.50 22.16           C  
ANISOU 1076  CB BARG B 559     3081   2847   2493     66    491    469       C  
ATOM   1077  CG AARG B 559      34.254  -0.897 -14.910  0.50 24.99           C  
ANISOU 1077  CG AARG B 559     3271   3194   3029      1    560    488       C  
ATOM   1078  CG BARG B 559      34.256  -1.124 -14.856  0.50 29.13           C  
ANISOU 1078  CG BARG B 559     3798   3726   3545      3    551    477       C  
ATOM   1079  CD AARG B 559      35.248   0.145 -15.401  0.50 18.21           C  
ANISOU 1079  CD AARG B 559     2364   2283   2273      7    712    593       C  
ATOM   1080  CD BARG B 559      35.379  -0.414 -15.551  0.50 26.06           C  
ANISOU 1080  CD BARG B 559     3383   3294   3225     34    722    585       C  
ATOM   1081  NE AARG B 559      36.295   0.346 -14.393  0.50 22.16           N  
ANISOU 1081  NE AARG B 559     2686   2771   2965    -73    724    593       N  
ATOM   1082  NE BARG B 559      35.122   1.010 -15.732  0.50 17.72           N  
ANISOU 1082  NE BARG B 559     2316   2185   2233      6    747    640       N  
ATOM   1083  CZ AARG B 559      36.335   1.360 -13.529  0.50 34.74           C  
ANISOU 1083  CZ AARG B 559     4180   4319   4700   -161    663    575       C  
ATOM   1084  CZ BARG B 559      36.063   1.866 -16.120  0.50 28.95           C  
ANISOU 1084  CZ BARG B 559     3678   3549   3773      1    888    747       C  
ATOM   1085  NH1AARG B 559      35.428   2.324 -13.583  0.50 20.95           N  
ANISOU 1085  NH1AARG B 559     2492   2536   2931   -171    617    568       N  
ATOM   1086  NH1BARG B 559      37.296   1.441 -16.361  0.50 24.37           N  
ANISOU 1086  NH1BARG B 559     3025   2970   3264     26   1022    819       N  
ATOM   1087  NH2AARG B 559      37.318   1.447 -12.645  0.50 22.68           N  
ANISOU 1087  NH2AARG B 559     2503   2775   3340   -229    641    565       N  
ATOM   1088  NH2BARG B 559      35.778   3.152 -16.269  0.50 24.12           N  
ANISOU 1088  NH2BARG B 559     3070   2872   3223    -26    904    796       N  
ATOM   1089  N   LEU B 560      31.650  -1.354 -12.972  1.00 16.22           N  
ANISOU 1089  N   LEU B 560     2109   2155   1897    -94    242    332       N  
ATOM   1090  CA  LEU B 560      31.108  -0.494 -11.954  1.00 15.08           C  
ANISOU 1090  CA  LEU B 560     1892   2011   1826   -130    193    312       C  
ATOM   1091  C   LEU B 560      31.977   0.766 -12.007  1.00 18.95           C  
ANISOU 1091  C   LEU B 560     2349   2440   2410   -146    272    349       C  
ATOM   1092  O   LEU B 560      33.200   0.669 -12.085  1.00 19.91           O  
ANISOU 1092  O   LEU B 560     2425   2541   2600   -162    344    371       O  
ATOM   1093  CB  LEU B 560      31.242  -1.140 -10.568  1.00 13.78           C  
ANISOU 1093  CB  LEU B 560     1646   1879   1709   -163    143    256       C  
ATOM   1094  CG  LEU B 560      30.586  -0.363  -9.427  1.00 15.03           C  
ANISOU 1094  CG  LEU B 560     1763   2040   1909   -168     95    230       C  
ATOM   1095  CD1 LEU B 560      29.057  -0.269  -9.602  1.00 16.54           C  
ANISOU 1095  CD1 LEU B 560     1976   2260   2050   -139     47    254       C  
ATOM   1096  CD2 LEU B 560      30.895  -1.040  -8.127  1.00 13.79           C  
ANISOU 1096  CD2 LEU B 560     1554   1913   1773   -177     60    182       C  
ATOM   1097  N   ASN B 561      31.356   1.946 -12.008  1.00 16.11           N  
ANISOU 1097  N   ASN B 561     2007   2043   2069   -141    261    367       N  
ATOM   1098  CA  ASN B 561      32.106   3.196 -12.090  1.00 16.63           C  
ANISOU 1098  CA  ASN B 561     2051   2025   2241   -166    326    408       C  
ATOM   1099  C   ASN B 561      31.981   4.096 -10.878  1.00 19.73           C  
ANISOU 1099  C   ASN B 561     2405   2370   2722   -200    260    355       C  
ATOM   1100  O   ASN B 561      30.908   4.173 -10.277  1.00 16.70           O  
ANISOU 1100  O   ASN B 561     2045   2017   2284   -166    194    316       O  
ATOM   1101  CB  ASN B 561      31.656   4.000 -13.330  1.00 18.53           C  
ANISOU 1101  CB  ASN B 561     2386   2228   2428   -114    387    489       C  
ATOM   1102  CG  ASN B 561      31.977   3.305 -14.631  1.00 31.01           C  
ANISOU 1102  CG  ASN B 561     4044   3831   3907    -58    466    547       C  
ATOM   1103  OD1 ASN B 561      33.123   2.955 -14.897  1.00 29.53           O  
ANISOU 1103  OD1 ASN B 561     3824   3633   3764    -64    562    584       O  
ATOM   1104  ND2 ASN B 561      30.970   3.042 -15.447  1.00 27.31           N  
ANISOU 1104  ND2 ASN B 561     3683   3395   3297      9    420    556       N  
ATOM   1105  N   GLU B 562      33.051   4.855 -10.573  1.00 19.31           N  
ANISOU 1105  N   GLU B 562     2298   2231   2810   -259    280    362       N  
ATOM   1106  CA  GLU B 562      33.020   5.837  -9.499  1.00 20.03           C  
ANISOU 1106  CA  GLU B 562     2387   2243   2980   -286    199    301       C  
ATOM   1107  C   GLU B 562      31.900   6.837  -9.835  1.00 21.23           C  
ANISOU 1107  C   GLU B 562     2634   2355   3077   -229    207    326       C  
ATOM   1108  O   GLU B 562      31.773   7.298 -10.991  1.00 21.34           O  
ANISOU 1108  O   GLU B 562     2690   2340   3078   -208    289    413       O  
ATOM   1109  CB  GLU B 562      34.363   6.592  -9.387  1.00 22.56           C  
ANISOU 1109  CB  GLU B 562     2634   2449   3491   -374    205    323       C  
ATOM   1110  CG  GLU B 562      34.482   7.444  -8.126  1.00 33.13           C  
ANISOU 1110  CG  GLU B 562     3987   3691   4911   -409     75    229       C  
ATOM   1111  CD  GLU B 562      35.700   8.344  -8.021  1.00 63.05           C  
ANISOU 1111  CD  GLU B 562     7702   7334   8920   -515     43    250       C  
ATOM   1112  OE1 GLU B 562      36.461   8.453  -9.010  1.00 66.28           O  
ANISOU 1112  OE1 GLU B 562     8032   7712   9440   -562    158    365       O  
ATOM   1113  OE2 GLU B 562      35.874   8.971  -6.952  1.00 57.84           O  
ANISOU 1113  OE2 GLU B 562     7070   6581   8324   -546    -98    155       O  
ATOM   1114  N   GLY B 563      31.106   7.159  -8.824  1.00 17.97           N  
ANISOU 1114  N   GLY B 563     2262   1941   2625   -186    131    257       N  
ATOM   1115  CA  GLY B 563      29.985   8.067  -9.007  1.00 17.78           C  
ANISOU 1115  CA  GLY B 563     2320   1887   2550   -111    138    281       C  
ATOM   1116  C   GLY B 563      28.667   7.363  -9.271  1.00 18.77           C  
ANISOU 1116  C   GLY B 563     2449   2132   2549    -32    138    307       C  
ATOM   1117  O   GLY B 563      27.610   7.996  -9.224  1.00 18.80           O  
ANISOU 1117  O   GLY B 563     2498   2133   2513     47    135    328       O  
ATOM   1118  N   ASP B 564      28.696   6.055  -9.599  1.00 14.60           N  
ANISOU 1118  N   ASP B 564     1870   1704   1972    -52    137    315       N  
ATOM   1119  CA  ASP B 564      27.451   5.328  -9.835  1.00 14.21           C  
ANISOU 1119  CA  ASP B 564     1809   1753   1836      0    109    342       C  
ATOM   1120  C   ASP B 564      26.615   5.334  -8.569  1.00 15.53           C  
ANISOU 1120  C   ASP B 564     1954   1957   1991     56     77    310       C  
ATOM   1121  O   ASP B 564      27.166   5.175  -7.481  1.00 15.08           O  
ANISOU 1121  O   ASP B 564     1889   1888   1952     44     62    246       O  
ATOM   1122  CB  ASP B 564      27.715   3.866 -10.233  1.00 14.43           C  
ANISOU 1122  CB  ASP B 564     1801   1855   1826    -39     95    339       C  
ATOM   1123  CG  ASP B 564      28.222   3.635 -11.641  1.00 18.73           C  
ANISOU 1123  CG  ASP B 564     2394   2386   2335    -50    134    385       C  
ATOM   1124  OD1 ASP B 564      28.270   4.616 -12.434  1.00 20.86           O  
ANISOU 1124  OD1 ASP B 564     2722   2599   2604    -24    181    437       O  
ATOM   1125  OD2 ASP B 564      28.642   2.499 -11.927  1.00 18.94           O  
ANISOU 1125  OD2 ASP B 564     2417   2450   2328    -72    131    371       O  
ATOM   1126  N   GLN B 565      25.306   5.540  -8.706  1.00 14.24           N  
ANISOU 1126  N   GLN B 565     1780   1835   1794    130     71    362       N  
ATOM   1127  CA  GLN B 565      24.420   5.527  -7.563  1.00 14.09           C  
ANISOU 1127  CA  GLN B 565     1731   1859   1763    208     74    361       C  
ATOM   1128  C   GLN B 565      23.779   4.174  -7.482  1.00 17.04           C  
ANISOU 1128  C   GLN B 565     2009   2335   2129    191     50    397       C  
ATOM   1129  O   GLN B 565      23.198   3.725  -8.464  1.00 16.78           O  
ANISOU 1129  O   GLN B 565     1938   2341   2097    169     10    451       O  
ATOM   1130  CB  GLN B 565      23.353   6.606  -7.715  1.00 16.04           C  
ANISOU 1130  CB  GLN B 565     2003   2089   2003    313     96    418       C  
ATOM   1131  CG  GLN B 565      22.390   6.575  -6.546  1.00 25.07           C  
ANISOU 1131  CG  GLN B 565     3112   3283   3130    421    130    440       C  
ATOM   1132  CD  GLN B 565      21.366   7.650  -6.597  1.00 29.81           C  
ANISOU 1132  CD  GLN B 565     3734   3867   3726    548    167    501       C  
ATOM   1133  OE1 GLN B 565      21.441   8.584  -7.410  1.00 32.23           O  
ANISOU 1133  OE1 GLN B 565     4103   4103   4038    557    162    515       O  
ATOM   1134  NE2 GLN B 565      20.398   7.536  -5.700  1.00 24.85           N  
ANISOU 1134  NE2 GLN B 565     3055   3299   3086    663    220    551       N  
ATOM   1135  N   VAL B 566      23.892   3.521  -6.322  1.00 14.13           N  
ANISOU 1135  N   VAL B 566     1615   2001   1755    201     63    368       N  
ATOM   1136  CA  VAL B 566      23.320   2.189  -6.127  1.00 13.07           C  
ANISOU 1136  CA  VAL B 566     1387   1948   1633    178     49    412       C  
ATOM   1137  C   VAL B 566      21.826   2.244  -5.848  1.00 16.88           C  
ANISOU 1137  C   VAL B 566     1781   2488   2144    259     75    512       C  
ATOM   1138  O   VAL B 566      21.420   2.896  -4.898  1.00 19.01           O  
ANISOU 1138  O   VAL B 566     2070   2759   2393    369    142    526       O  
ATOM   1139  CB  VAL B 566      24.070   1.470  -5.004  1.00 14.76           C  
ANISOU 1139  CB  VAL B 566     1612   2171   1826    169     65    358       C  
ATOM   1140  CG1 VAL B 566      23.464   0.083  -4.739  1.00 14.70           C  
ANISOU 1140  CG1 VAL B 566     1511   2230   1843    145     64    418       C  
ATOM   1141  CG2 VAL B 566      25.586   1.392  -5.311  1.00 13.49           C  
ANISOU 1141  CG2 VAL B 566     1505   1957   1663     88     36    274       C  
ATOM   1142  N   VAL B 567      21.002   1.530  -6.662  1.00 14.75           N  
ANISOU 1142  N   VAL B 567     1414   2263   1927    212     15    585       N  
ATOM   1143  CA  VAL B 567      19.550   1.465  -6.522  1.00 15.37           C  
ANISOU 1143  CA  VAL B 567     1361   2401   2078    269     23    704       C  
ATOM   1144  C   VAL B 567      19.149   0.142  -5.877  1.00 16.28           C  
ANISOU 1144  C   VAL B 567     1364   2564   2259    228     31    762       C  
ATOM   1145  O   VAL B 567      18.359   0.142  -4.928  1.00 17.89           O  
ANISOU 1145  O   VAL B 567     1482   2812   2503    315    122    852       O  
ATOM   1146  CB  VAL B 567      18.875   1.680  -7.907  1.00 19.31           C  
ANISOU 1146  CB  VAL B 567     1824   2903   2612    242    -82    751       C  
ATOM   1147  CG1 VAL B 567      17.356   1.532  -7.823  1.00 21.02           C  
ANISOU 1147  CG1 VAL B 567     1865   3183   2939    286    -99    888       C  
ATOM   1148  CG2 VAL B 567      19.252   3.052  -8.468  1.00 19.13           C  
ANISOU 1148  CG2 VAL B 567     1920   2825   2523    299    -64    714       C  
ATOM   1149  N   LEU B 568      19.653  -0.979  -6.415  1.00 14.51           N  
ANISOU 1149  N   LEU B 568     1144   2323   2047    108    -52    723       N  
ATOM   1150  CA  LEU B 568      19.370  -2.325  -5.881  1.00 14.60           C  
ANISOU 1150  CA  LEU B 568     1063   2355   2130     52    -54    776       C  
ATOM   1151  C   LEU B 568      20.660  -3.041  -5.562  1.00 14.91           C  
ANISOU 1151  C   LEU B 568     1204   2362   2101      2    -45    678       C  
ATOM   1152  O   LEU B 568      21.637  -2.894  -6.291  1.00 13.79           O  
ANISOU 1152  O   LEU B 568     1167   2179   1892    -39    -91    583       O  
ATOM   1153  CB  LEU B 568      18.629  -3.261  -6.840  1.00 15.96           C  
ANISOU 1153  CB  LEU B 568     1139   2517   2407    -55   -194    830       C  
ATOM   1154  CG  LEU B 568      17.332  -2.822  -7.498  1.00 20.27           C  
ANISOU 1154  CG  LEU B 568     1561   3089   3051    -42   -272    929       C  
ATOM   1155  CD1 LEU B 568      16.797  -3.935  -8.387  1.00 21.14           C  
ANISOU 1155  CD1 LEU B 568     1601   3167   3266   -169   -453    955       C  
ATOM   1156  CD2 LEU B 568      16.279  -2.415  -6.491  1.00 23.75           C  
ANISOU 1156  CD2 LEU B 568     1846   3592   3584     60   -148   1069       C  
ATOM   1157  N   ILE B 569      20.631  -3.890  -4.522  1.00 13.85           N  
ANISOU 1157  N   ILE B 569     1027   2246   1990     11     18    719       N  
ATOM   1158  CA  ILE B 569      21.739  -4.782  -4.182  1.00 13.05           C  
ANISOU 1158  CA  ILE B 569     1001   2119   1840    -32     18    646       C  
ATOM   1159  C   ILE B 569      21.122  -6.161  -4.131  1.00 16.05           C  
ANISOU 1159  C   ILE B 569     1286   2490   2322   -106    -12    730       C  
ATOM   1160  O   ILE B 569      20.245  -6.410  -3.285  1.00 16.60           O  
ANISOU 1160  O   ILE B 569     1250   2593   2465    -62     67    849       O  
ATOM   1161  CB  ILE B 569      22.409  -4.416  -2.845  1.00 14.39           C  
ANISOU 1161  CB  ILE B 569     1241   2305   1921     68    118    609       C  
ATOM   1162  CG1 ILE B 569      23.006  -3.009  -2.947  1.00 15.00           C  
ANISOU 1162  CG1 ILE B 569     1414   2362   1923    122    119    522       C  
ATOM   1163  CG2 ILE B 569      23.505  -5.458  -2.514  1.00 14.62           C  
ANISOU 1163  CG2 ILE B 569     1328   2312   1913     26    103    549       C  
ATOM   1164  CD1 ILE B 569      23.657  -2.460  -1.666  1.00 17.57           C  
ANISOU 1164  CD1 ILE B 569     1834   2683   2157    226    175    463       C  
ATOM   1165  N   ASN B 570      21.591  -7.066  -5.030  1.00 15.89           N  
ANISOU 1165  N   ASN B 570     1312   2415   2310   -209   -119    675       N  
ATOM   1166  CA  ASN B 570      21.048  -8.433  -5.094  1.00 16.08           C  
ANISOU 1166  CA  ASN B 570     1266   2398   2444   -298   -177    741       C  
ATOM   1167  C   ASN B 570      19.521  -8.435  -5.157  1.00 21.14           C  
ANISOU 1167  C   ASN B 570     1733   3056   3244   -325   -208    881       C  
ATOM   1168  O   ASN B 570      18.871  -9.205  -4.449  1.00 22.08           O  
ANISOU 1168  O   ASN B 570     1737   3172   3482   -346   -161    999       O  
ATOM   1169  CB  ASN B 570      21.588  -9.271  -3.934  1.00 16.03           C  
ANISOU 1169  CB  ASN B 570     1278   2390   2421   -271    -81    760       C  
ATOM   1170  CG  ASN B 570      23.083  -9.392  -4.028  1.00 20.22           C  
ANISOU 1170  CG  ASN B 570     1956   2900   2827   -258    -83    629       C  
ATOM   1171  OD1 ASN B 570      23.636  -9.514  -5.127  1.00 18.32           O  
ANISOU 1171  OD1 ASN B 570     1796   2617   2550   -309   -170    546       O  
ATOM   1172  ND2 ASN B 570      23.786  -9.244  -2.913  1.00 17.06           N  
ANISOU 1172  ND2 ASN B 570     1598   2534   2351   -174     12    611       N  
ATOM   1173  N   GLY B 571      18.987  -7.522  -5.968  1.00 20.41           N  
ANISOU 1173  N   GLY B 571     1615   2982   3157   -314   -275    880       N  
ATOM   1174  CA  GLY B 571      17.554  -7.367  -6.219  1.00 22.00           C  
ANISOU 1174  CA  GLY B 571     1637   3205   3517   -334   -332   1010       C  
ATOM   1175  C   GLY B 571      16.784  -6.603  -5.165  1.00 25.48           C  
ANISOU 1175  C   GLY B 571     1951   3726   4005   -213   -167   1138       C  
ATOM   1176  O   GLY B 571      15.575  -6.411  -5.309  1.00 27.74           O  
ANISOU 1176  O   GLY B 571     2062   4041   4438   -212   -191   1268       O  
ATOM   1177  N   ARG B 572      17.474  -6.125  -4.112  1.00 21.91           N  
ANISOU 1177  N   ARG B 572     1592   3308   3426    -98     -4   1103       N  
ATOM   1178  CA  ARG B 572      16.819  -5.440  -3.005  1.00 21.91           C  
ANISOU 1178  CA  ARG B 572     1518   3374   3431     51    171   1216       C  
ATOM   1179  C   ARG B 572      16.873  -3.932  -3.116  1.00 23.62           C  
ANISOU 1179  C   ARG B 572     1813   3619   3544    169    208   1162       C  
ATOM   1180  O   ARG B 572      17.950  -3.370  -3.310  1.00 19.75           O  
ANISOU 1180  O   ARG B 572     1493   3099   2914    179    184   1015       O  
ATOM   1181  CB  ARG B 572      17.472  -5.872  -1.696  1.00 23.09           C  
ANISOU 1181  CB  ARG B 572     1750   3532   3490    128    313   1211       C  
ATOM   1182  CG  ARG B 572      16.596  -5.662  -0.484  1.00 33.63           C  
ANISOU 1182  CG  ARG B 572     2994   4927   4857    279    506   1374       C  
ATOM   1183  CD  ARG B 572      17.085  -6.468   0.704  1.00 46.39           C  
ANISOU 1183  CD  ARG B 572     4676   6542   6407    335    625   1402       C  
ATOM   1184  NE  ARG B 572      17.350  -7.879   0.394  1.00 48.07           N  
ANISOU 1184  NE  ARG B 572     4850   6699   6717    177    541   1411       N  
ATOM   1185  CZ  ARG B 572      16.467  -8.863   0.545  1.00 60.86           C  
ANISOU 1185  CZ  ARG B 572     6296   8304   8526    111    575   1585       C  
ATOM   1186  NH1 ARG B 572      16.802 -10.113   0.253  1.00 41.82           N  
ANISOU 1186  NH1 ARG B 572     3883   5817   6190    -31    485   1573       N  
ATOM   1187  NH2 ARG B 572      15.244  -8.605   0.998  1.00 49.06           N  
ANISOU 1187  NH2 ARG B 572     4622   6860   7159    191    704   1781       N  
ATOM   1188  N   ASP B 573      15.730  -3.263  -2.913  1.00 23.36           N  
ANISOU 1188  N   ASP B 573     1651   3636   3588    268    281   1293       N  
ATOM   1189  CA  ASP B 573      15.707  -1.807  -2.929  1.00 22.71           C  
ANISOU 1189  CA  ASP B 573     1653   3567   3408    400    330   1253       C  
ATOM   1190  C   ASP B 573      16.279  -1.312  -1.612  1.00 26.17           C  
ANISOU 1190  C   ASP B 573     2238   4010   3695    554    489   1209       C  
ATOM   1191  O   ASP B 573      15.731  -1.598  -0.547  1.00 28.42           O  
ANISOU 1191  O   ASP B 573     2463   4337   3997    663    638   1328       O  
ATOM   1192  CB  ASP B 573      14.272  -1.300  -3.193  1.00 25.07           C  
ANISOU 1192  CB  ASP B 573     1762   3918   3845    468    351   1415       C  
ATOM   1193  CG  ASP B 573      14.067   0.201  -3.249  1.00 31.56           C  
ANISOU 1193  CG  ASP B 573     2660   4748   4584    620    407   1398       C  
ATOM   1194  OD1 ASP B 573      14.998   0.937  -2.935  1.00 28.25           O  
ANISOU 1194  OD1 ASP B 573     2447   4287   4001    683    443   1263       O  
ATOM   1195  OD2 ASP B 573      12.922   0.634  -3.499  1.00 42.36           O  
ANISOU 1195  OD2 ASP B 573     3870   6161   6064    688    423   1533       O  
ATOM   1196  N   ILE B 574      17.410  -0.592  -1.692  1.00 22.01           N  
ANISOU 1196  N   ILE B 574     1908   3432   3021    564    450   1041       N  
ATOM   1197  CA  ILE B 574      18.118  -0.106  -0.509  1.00 21.24           C  
ANISOU 1197  CA  ILE B 574     1982   3317   2772    693    543    963       C  
ATOM   1198  C   ILE B 574      17.866   1.349  -0.124  1.00 25.12           C  
ANISOU 1198  C   ILE B 574     2580   3789   3175    865    614    943       C  
ATOM   1199  O   ILE B 574      18.534   1.852   0.782  1.00 23.31           O  
ANISOU 1199  O   ILE B 574     2528   3521   2808    968    651    849       O  
ATOM   1200  CB  ILE B 574      19.644  -0.415  -0.625  1.00 22.00           C  
ANISOU 1200  CB  ILE B 574     2217   3356   2785    588    444    796       C  
ATOM   1201  CG1 ILE B 574      20.261   0.100  -1.954  1.00 22.09           C  
ANISOU 1201  CG1 ILE B 574     2267   3316   2811    471    317    698       C  
ATOM   1202  CG2 ILE B 574      19.895  -1.907  -0.450  1.00 22.00           C  
ANISOU 1202  CG2 ILE B 574     2154   3374   2832    492    430    826       C  
ATOM   1203  CD1 ILE B 574      20.671   1.514  -1.959  1.00 32.70           C  
ANISOU 1203  CD1 ILE B 574     3742   4602   4081    542    315    614       C  
ATOM   1204  N   ALA B 575      16.907   2.026  -0.781  1.00 24.66           N  
ANISOU 1204  N   ALA B 575     2428   3749   3193    904    620   1027       N  
ATOM   1205  CA  ALA B 575      16.650   3.450  -0.536  1.00 26.21           C  
ANISOU 1205  CA  ALA B 575     2737   3912   3311   1071    682   1007       C  
ATOM   1206  C   ALA B 575      16.522   3.852   0.939  1.00 29.87           C  
ANISOU 1206  C   ALA B 575     3330   4375   3644   1291    838   1019       C  
ATOM   1207  O   ALA B 575      17.016   4.911   1.322  1.00 30.40           O  
ANISOU 1207  O   ALA B 575     3601   4365   3586   1394    837    905       O  
ATOM   1208  CB  ALA B 575      15.436   3.920  -1.325  1.00 28.36           C  
ANISOU 1208  CB  ALA B 575     2852   4224   3699   1107    688   1138       C  
ATOM   1209  N   GLU B 576      15.875   3.022   1.756  1.00 26.50           N  
ANISOU 1209  N   GLU B 576     2801   4024   3244   1369    969   1157       N  
ATOM   1210  CA  GLU B 576      15.687   3.334   3.174  1.00 27.76           C  
ANISOU 1210  CA  GLU B 576     3101   4190   3256   1611   1140   1187       C  
ATOM   1211  C   GLU B 576      16.682   2.664   4.138  1.00 29.57           C  
ANISOU 1211  C   GLU B 576     3486   4400   3350   1616   1132   1091       C  
ATOM   1212  O   GLU B 576      16.557   2.817   5.355  1.00 30.63           O  
ANISOU 1212  O   GLU B 576     3761   4540   3336   1830   1267   1114       O  
ATOM   1213  CB  GLU B 576      14.238   3.030   3.592  1.00 31.75           C  
ANISOU 1213  CB  GLU B 576     3406   4793   3863   1757   1339   1435       C  
ATOM   1214  CG  GLU B 576      13.228   4.004   3.007  1.00 45.21           C  
ANISOU 1214  CG  GLU B 576     5012   6515   5651   1851   1380   1530       C  
ATOM   1215  CD  GLU B 576      11.762   3.727   3.288  1.00 71.87           C  
ANISOU 1215  CD  GLU B 576     8138   9993   9175   1982   1569   1799       C  
ATOM   1216  OE1 GLU B 576      11.454   2.965   4.234  1.00 73.04           O  
ANISOU 1216  OE1 GLU B 576     8235  10193   9323   2072   1733   1929       O  
ATOM   1217  OE2 GLU B 576      10.914   4.297   2.564  1.00 68.64           O  
ANISOU 1217  OE2 GLU B 576     7580   9611   8891   2005   1559   1893       O  
ATOM   1218  N   HIS B 577      17.659   1.922   3.612  1.00 24.63           N  
ANISOU 1218  N   HIS B 577     2845   3750   2762   1401    979    987       N  
ATOM   1219  CA  HIS B 577      18.645   1.237   4.439  1.00 23.69           C  
ANISOU 1219  CA  HIS B 577     2855   3616   2531   1396    952    900       C  
ATOM   1220  C   HIS B 577      19.824   2.112   4.828  1.00 24.04           C  
ANISOU 1220  C   HIS B 577     3152   3565   2418   1433    838    691       C  
ATOM   1221  O   HIS B 577      20.224   3.004   4.079  1.00 22.64           O  
ANISOU 1221  O   HIS B 577     3017   3317   2266   1358    729    587       O  
ATOM   1222  CB  HIS B 577      19.106  -0.057   3.768  1.00 24.33           C  
ANISOU 1222  CB  HIS B 577     2795   3714   2733   1169    857    905       C  
ATOM   1223  CG  HIS B 577      18.014  -1.074   3.652  1.00 28.26           C  
ANISOU 1223  CG  HIS B 577     3067   4285   3387   1135    956   1110       C  
ATOM   1224  ND1 HIS B 577      17.315  -1.241   2.478  1.00 30.65           N  
ANISOU 1224  ND1 HIS B 577     3170   4603   3871    996    894   1187       N  
ATOM   1225  CD2 HIS B 577      17.545  -1.953   4.563  1.00 31.86           C  
ANISOU 1225  CD2 HIS B 577     3470   4788   3848   1218   1100   1253       C  
ATOM   1226  CE1 HIS B 577      16.442  -2.205   2.709  1.00 31.30           C  
ANISOU 1226  CE1 HIS B 577     3071   4735   4086    984    985   1369       C  
ATOM   1227  NE2 HIS B 577      16.542  -2.663   3.949  1.00 32.32           N  
ANISOU 1227  NE2 HIS B 577     3274   4885   4122   1114   1126   1425       N  
ATOM   1228  N   THR B 578      20.400   1.842   6.007  1.00 21.47           N  
ANISOU 1228  N   THR B 578     2993   3228   1936   1548    852    633       N  
ATOM   1229  CA  THR B 578      21.552   2.600   6.494  1.00 21.02           C  
ANISOU 1229  CA  THR B 578     3176   3071   1740   1581    710    430       C  
ATOM   1230  C   THR B 578      22.820   2.158   5.740  1.00 20.64           C  
ANISOU 1230  C   THR B 578     3073   2986   1783   1337    523    312       C  
ATOM   1231  O   THR B 578      22.834   1.116   5.046  1.00 18.79           O  
ANISOU 1231  O   THR B 578     2659   2808   1673   1179    520    381       O  
ATOM   1232  CB  THR B 578      21.806   2.307   7.973  1.00 24.43           C  
ANISOU 1232  CB  THR B 578     3805   3508   1970   1780    757    406       C  
ATOM   1233  OG1 THR B 578      22.177   0.926   8.089  1.00 23.50           O  
ANISOU 1233  OG1 THR B 578     3585   3454   1892   1683    757    459       O  
ATOM   1234  CG2 THR B 578      20.618   2.647   8.873  1.00 21.88           C  
ANISOU 1234  CG2 THR B 578     3564   3225   1524   2065    977    538       C  
ATOM   1235  N   HIS B 579      23.897   2.929   5.908  1.00 18.72           N  
ANISOU 1235  N   HIS B 579     2990   2641   1483   1315    367    138       N  
ATOM   1236  CA  HIS B 579      25.203   2.608   5.322  1.00 16.74           C  
ANISOU 1236  CA  HIS B 579     2690   2350   1321   1110    201     33       C  
ATOM   1237  C   HIS B 579      25.633   1.197   5.726  1.00 17.34           C  
ANISOU 1237  C   HIS B 579     2707   2499   1383   1075    204     67       C  
ATOM   1238  O   HIS B 579      26.024   0.397   4.865  1.00 15.92           O  
ANISOU 1238  O   HIS B 579     2376   2349   1325    903    173     92       O  
ATOM   1239  CB  HIS B 579      26.269   3.620   5.774  1.00 17.59           C  
ANISOU 1239  CB  HIS B 579     2983   2330   1371   1122     30   -145       C  
ATOM   1240  CG  HIS B 579      27.627   3.340   5.207  1.00 18.45           C  
ANISOU 1240  CG  HIS B 579     3015   2400   1596    922   -128   -231       C  
ATOM   1241  ND1 HIS B 579      28.013   3.843   3.974  1.00 18.36           N  
ANISOU 1241  ND1 HIS B 579     2900   2336   1741    753   -174   -242       N  
ATOM   1242  CD2 HIS B 579      28.648   2.612   5.720  1.00 20.07           C  
ANISOU 1242  CD2 HIS B 579     3228   2614   1782    884   -232   -291       C  
ATOM   1243  CE1 HIS B 579      29.241   3.382   3.760  1.00 17.64           C  
ANISOU 1243  CE1 HIS B 579     2744   2229   1730    618   -287   -298       C  
ATOM   1244  NE2 HIS B 579      29.663   2.635   4.783  1.00 18.34           N  
ANISOU 1244  NE2 HIS B 579     2890   2355   1724    688   -333   -332       N  
ATOM   1245  N   ASP B 580      25.569   0.884   7.040  1.00 17.95           N  
ANISOU 1245  N   ASP B 580     2923   2598   1298   1253    246     70       N  
ATOM   1246  CA  ASP B 580      26.008  -0.440   7.473  1.00 17.03           C  
ANISOU 1246  CA  ASP B 580     2767   2542   1162   1233    250    108       C  
ATOM   1247  C   ASP B 580      25.088  -1.572   7.007  1.00 19.57           C  
ANISOU 1247  C   ASP B 580     2895   2952   1588   1177    404    289       C  
ATOM   1248  O   ASP B 580      25.587  -2.673   6.766  1.00 17.37           O  
ANISOU 1248  O   ASP B 580     2529   2699   1371   1067    374    309       O  
ATOM   1249  CB  ASP B 580      26.233  -0.447   8.994  1.00 19.97           C  
ANISOU 1249  CB  ASP B 580     3364   2907   1316   1451    245     64       C  
ATOM   1250  CG  ASP B 580      27.465   0.321   9.463  1.00 25.47           C  
ANISOU 1250  CG  ASP B 580     4238   3504   1934   1459     18   -137       C  
ATOM   1251  OD1 ASP B 580      28.268   0.759   8.602  1.00 25.58           O  
ANISOU 1251  OD1 ASP B 580     4170   3456   2091   1272   -127   -229       O  
ATOM   1252  OD2 ASP B 580      27.677   0.411  10.697  1.00 29.12           O  
ANISOU 1252  OD2 ASP B 580     4918   3948   2199   1649    -23   -195       O  
ATOM   1253  N   GLN B 581      23.769  -1.308   6.816  1.00 19.70           N  
ANISOU 1253  N   GLN B 581     2835   3006   1646   1243    554    422       N  
ATOM   1254  CA  GLN B 581      22.892  -2.357   6.257  1.00 18.61           C  
ANISOU 1254  CA  GLN B 581     2484   2935   1654   1156    663    594       C  
ATOM   1255  C   GLN B 581      23.303  -2.608   4.808  1.00 19.92           C  
ANISOU 1255  C   GLN B 581     2510   3079   1981    918    542    549       C  
ATOM   1256  O   GLN B 581      23.331  -3.753   4.372  1.00 19.24           O  
ANISOU 1256  O   GLN B 581     2308   3012   1989    799    536    608       O  
ATOM   1257  CB  GLN B 581      21.418  -1.951   6.316  1.00 21.32           C  
ANISOU 1257  CB  GLN B 581     2745   3321   2036   1272    831    753       C  
ATOM   1258  CG  GLN B 581      20.892  -2.008   7.744  1.00 20.76           C  
ANISOU 1258  CG  GLN B 581     2793   3285   1809   1526   1004    848       C  
ATOM   1259  CD  GLN B 581      19.478  -1.501   7.840  1.00 30.43           C  
ANISOU 1259  CD  GLN B 581     3933   4555   3076   1668   1190   1016       C  
ATOM   1260  OE1 GLN B 581      19.092  -0.510   7.212  1.00 25.12           O  
ANISOU 1260  OE1 GLN B 581     3234   3861   2448   1664   1165    989       O  
ATOM   1261  NE2 GLN B 581      18.673  -2.171   8.644  1.00 34.67           N  
ANISOU 1261  NE2 GLN B 581     4417   5152   3603   1807   1393   1208       N  
ATOM   1262  N   VAL B 582      23.602  -1.530   4.052  1.00 16.25           N  
ANISOU 1262  N   VAL B 582     2070   2562   1541    860    452    451       N  
ATOM   1263  CA  VAL B 582      24.074  -1.661   2.670  1.00 14.62           C  
ANISOU 1263  CA  VAL B 582     1766   2332   1458    663    349    408       C  
ATOM   1264  C   VAL B 582      25.358  -2.506   2.616  1.00 14.70           C  
ANISOU 1264  C   VAL B 582     1790   2326   1469    563    256    327       C  
ATOM   1265  O   VAL B 582      25.495  -3.390   1.768  1.00 14.58           O  
ANISOU 1265  O   VAL B 582     1677   2320   1543    434    230    355       O  
ATOM   1266  CB  VAL B 582      24.278  -0.255   2.059  1.00 17.75           C  
ANISOU 1266  CB  VAL B 582     2218   2665   1861    650    287    323       C  
ATOM   1267  CG1 VAL B 582      25.182  -0.274   0.812  1.00 17.31           C  
ANISOU 1267  CG1 VAL B 582     2115   2568   1892    474    181    254       C  
ATOM   1268  CG2 VAL B 582      22.915   0.415   1.759  1.00 18.73           C  
ANISOU 1268  CG2 VAL B 582     2284   2812   2019    725    377    427       C  
ATOM   1269  N   VAL B 583      26.312  -2.213   3.504  1.00 13.61           N  
ANISOU 1269  N   VAL B 583     1782   2158   1232    630    193    223       N  
ATOM   1270  CA  VAL B 583      27.577  -2.959   3.557  1.00 12.61           C  
ANISOU 1270  CA  VAL B 583     1660   2020   1110    555    101    153       C  
ATOM   1271  C   VAL B 583      27.264  -4.440   3.814  1.00 15.15           C  
ANISOU 1271  C   VAL B 583     1920   2396   1440    554    173    255       C  
ATOM   1272  O   VAL B 583      27.786  -5.303   3.097  1.00 14.10           O  
ANISOU 1272  O   VAL B 583     1714   2260   1383    437    137    255       O  
ATOM   1273  CB  VAL B 583      28.512  -2.379   4.638  1.00 15.29           C  
ANISOU 1273  CB  VAL B 583     2149   2319   1341    649      2     35       C  
ATOM   1274  CG1 VAL B 583      29.640  -3.347   5.001  1.00 15.08           C  
ANISOU 1274  CG1 VAL B 583     2119   2304   1305    618    -76     -5       C  
ATOM   1275  CG2 VAL B 583      29.068  -1.039   4.186  1.00 15.01           C  
ANISOU 1275  CG2 VAL B 583     2153   2200   1349    596   -101    -72       C  
ATOM   1276  N   LEU B 584      26.371  -4.722   4.781  1.00 14.66           N  
ANISOU 1276  N   LEU B 584     1891   2374   1306    691    289    353       N  
ATOM   1277  CA  LEU B 584      25.997  -6.114   5.061  1.00 15.08           C  
ANISOU 1277  CA  LEU B 584     1881   2462   1387    687    371    472       C  
ATOM   1278  C   LEU B 584      25.313  -6.805   3.845  1.00 18.03           C  
ANISOU 1278  C   LEU B 584     2090   2834   1928    531    388    560       C  
ATOM   1279  O   LEU B 584      25.672  -7.939   3.525  1.00 16.79           O  
ANISOU 1279  O   LEU B 584     1891   2663   1826    443    363    578       O  
ATOM   1280  CB  LEU B 584      25.196  -6.273   6.361  1.00 17.35           C  
ANISOU 1280  CB  LEU B 584     2234   2789   1569    877    516    584       C  
ATOM   1281  CG  LEU B 584      24.860  -7.714   6.715  1.00 20.70           C  
ANISOU 1281  CG  LEU B 584     2596   3235   2035    873    612    724       C  
ATOM   1282  CD1 LEU B 584      26.145  -8.567   6.951  1.00 20.47           C  
ANISOU 1282  CD1 LEU B 584     2632   3188   1959    841    514    643       C  
ATOM   1283  CD2 LEU B 584      23.905  -7.771   7.851  1.00 25.19           C  
ANISOU 1283  CD2 LEU B 584     3205   3845   2523   1064    793    872       C  
ATOM   1284  N   PHE B 585      24.415  -6.117   3.135  1.00 16.61           N  
ANISOU 1284  N   PHE B 585     1832   2658   1822    499    408    601       N  
ATOM   1285  CA  PHE B 585      23.795  -6.712   1.943  1.00 16.62           C  
ANISOU 1285  CA  PHE B 585     1694   2647   1972    353    380    666       C  
ATOM   1286  C   PHE B 585      24.867  -7.086   0.927  1.00 15.75           C  
ANISOU 1286  C   PHE B 585     1603   2494   1886    221    259    557       C  
ATOM   1287  O   PHE B 585      24.778  -8.154   0.338  1.00 15.36           O  
ANISOU 1287  O   PHE B 585     1501   2421   1914    124    229    593       O  
ATOM   1288  CB  PHE B 585      22.807  -5.745   1.296  1.00 18.35           C  
ANISOU 1288  CB  PHE B 585     1842   2878   2252    353    390    708       C  
ATOM   1289  CG  PHE B 585      21.507  -5.550   2.037  1.00 22.79           C  
ANISOU 1289  CG  PHE B 585     2334   3487   2839    473    528    860       C  
ATOM   1290  CD1 PHE B 585      20.790  -6.642   2.517  1.00 28.76           C  
ANISOU 1290  CD1 PHE B 585     2988   4262   3678    475    618   1013       C  
ATOM   1291  CD2 PHE B 585      20.956  -4.282   2.177  1.00 26.30           C  
ANISOU 1291  CD2 PHE B 585     2801   3949   3244    584    577    866       C  
ATOM   1292  CE1 PHE B 585      19.587  -6.459   3.204  1.00 32.52           C  
ANISOU 1292  CE1 PHE B 585     3377   4785   4196    597    773   1182       C  
ATOM   1293  CE2 PHE B 585      19.745  -4.100   2.850  1.00 32.76           C  
ANISOU 1293  CE2 PHE B 585     3546   4815   4088    718    728   1023       C  
ATOM   1294  CZ  PHE B 585      19.074  -5.187   3.363  1.00 32.59           C  
ANISOU 1294  CZ  PHE B 585     3410   4822   4150    726    833   1187       C  
ATOM   1295  N   ILE B 586      25.916  -6.259   0.762  1.00 12.11           N  
ANISOU 1295  N   ILE B 586     1222   2014   1364    223    194    431       N  
ATOM   1296  CA  ILE B 586      26.989  -6.612  -0.150  1.00 10.71           C  
ANISOU 1296  CA  ILE B 586     1054   1802   1212    122    113    350       C  
ATOM   1297  C   ILE B 586      27.740  -7.836   0.353  1.00 15.38           C  
ANISOU 1297  C   ILE B 586     1669   2391   1783    123    108    346       C  
ATOM   1298  O   ILE B 586      28.008  -8.766  -0.427  1.00 14.26           O  
ANISOU 1298  O   ILE B 586     1507   2221   1689     42     80    349       O  
ATOM   1299  CB  ILE B 586      27.891  -5.406  -0.460  1.00 12.32           C  
ANISOU 1299  CB  ILE B 586     1308   1981   1394    117     59    247       C  
ATOM   1300  CG1 ILE B 586      27.068  -4.321  -1.217  1.00 12.85           C  
ANISOU 1300  CG1 ILE B 586     1353   2038   1492    105     66    266       C  
ATOM   1301  CG2 ILE B 586      29.114  -5.830  -1.307  1.00 12.26           C  
ANISOU 1301  CG2 ILE B 586     1297   1944   1418     34      6    188       C  
ATOM   1302  CD1 ILE B 586      27.688  -2.944  -1.142  1.00 13.10           C  
ANISOU 1302  CD1 ILE B 586     1446   2030   1501    130     34    185       C  
ATOM   1303  N   LYS B 587      28.052  -7.859   1.661  1.00 14.57           N  
ANISOU 1303  N   LYS B 587     1627   2313   1598    231    134    341       N  
ATOM   1304  CA  LYS B 587      28.772  -9.007   2.245  1.00 15.09           C  
ANISOU 1304  CA  LYS B 587     1722   2378   1633    254    130    345       C  
ATOM   1305  C   LYS B 587      27.967 -10.315   2.261  1.00 16.39           C  
ANISOU 1305  C   LYS B 587     1841   2533   1853    227    196    464       C  
ATOM   1306  O   LYS B 587      28.579 -11.405   2.314  1.00 17.38           O  
ANISOU 1306  O   LYS B 587     1985   2635   1983    211    183    467       O  
ATOM   1307  CB  LYS B 587      29.352  -8.626   3.638  1.00 19.73           C  
ANISOU 1307  CB  LYS B 587     2408   2989   2099    391    116    301       C  
ATOM   1308  CG  LYS B 587      30.677  -7.905   3.391  1.00 27.50           C  
ANISOU 1308  CG  LYS B 587     3412   3951   3084    360     -3    171       C  
ATOM   1309  CD  LYS B 587      31.304  -7.186   4.551  1.00 37.63           C  
ANISOU 1309  CD  LYS B 587     4796   5235   4266    470    -79     92       C  
ATOM   1310  CE  LYS B 587      32.415  -6.284   4.057  1.00 28.15           C  
ANISOU 1310  CE  LYS B 587     3571   3993   3129    397   -201    -17       C  
ATOM   1311  NZ  LYS B 587      33.549  -7.025   3.420  1.00 26.86           N  
ANISOU 1311  NZ  LYS B 587     3325   3828   3054    315   -244    -31       N  
ATOM   1312  N   ALA B 588      26.626 -10.233   2.166  1.00 16.20           N  
ANISOU 1312  N   ALA B 588     1748   2517   1892    216    261    568       N  
ATOM   1313  CA  ALA B 588      25.729 -11.387   2.110  1.00 15.87           C  
ANISOU 1313  CA  ALA B 588     1633   2449   1950    165    312    699       C  
ATOM   1314  C   ALA B 588      25.530 -11.927   0.703  1.00 19.02           C  
ANISOU 1314  C   ALA B 588     1977   2787   2462     13    224    685       C  
ATOM   1315  O   ALA B 588      24.734 -12.851   0.502  1.00 20.21           O  
ANISOU 1315  O   ALA B 588     2062   2893   2726    -57    228    784       O  
ATOM   1316  CB  ALA B 588      24.369 -11.006   2.695  1.00 17.95           C  
ANISOU 1316  CB  ALA B 588     1820   2749   2253    230    423    836       C  
ATOM   1317  N   SER B 589      26.259 -11.381  -0.283  1.00 15.95           N  
ANISOU 1317  N   SER B 589     1626   2386   2047    -36    139    567       N  
ATOM   1318  CA  SER B 589      26.056 -11.787  -1.691  1.00 15.09           C  
ANISOU 1318  CA  SER B 589     1504   2219   2010   -153     50    545       C  
ATOM   1319  C   SER B 589      26.204 -13.255  -1.994  1.00 19.73           C  
ANISOU 1319  C   SER B 589     2121   2729   2644   -215     13    562       C  
ATOM   1320  O   SER B 589      25.572 -13.734  -2.935  1.00 19.86           O  
ANISOU 1320  O   SER B 589     2123   2682   2741   -308    -67    577       O  
ATOM   1321  CB  SER B 589      27.005 -11.030  -2.612  1.00 15.94           C  
ANISOU 1321  CB  SER B 589     1672   2327   2058   -164     -2    428       C  
ATOM   1322  OG  SER B 589      26.709  -9.650  -2.551  1.00 15.68           O  
ANISOU 1322  OG  SER B 589     1614   2338   2004   -127     14    416       O  
ATOM   1323  N   CYS B 590      27.075 -13.960  -1.282  1.00 15.86           N  
ANISOU 1323  N   CYS B 590     1690   2233   2104   -162     51    549       N  
ATOM   1324  CA  CYS B 590      27.326 -15.373  -1.514  1.00 17.26           C  
ANISOU 1324  CA  CYS B 590     1918   2324   2317   -203     23    562       C  
ATOM   1325  C   CYS B 590      26.450 -16.315  -0.702  1.00 22.90           C  
ANISOU 1325  C   CYS B 590     2583   2999   3121   -217     76    698       C  
ATOM   1326  O   CYS B 590      26.670 -17.526  -0.750  1.00 25.94           O  
ANISOU 1326  O   CYS B 590     3019   3297   3540   -246     59    717       O  
ATOM   1327  CB  CYS B 590      28.802 -15.677  -1.331  1.00 16.10           C  
ANISOU 1327  CB  CYS B 590     1857   2183   2077   -133     32    482       C  
ATOM   1328  SG  CYS B 590      29.863 -14.758  -2.472  1.00 18.35           S  
ANISOU 1328  SG  CYS B 590     2180   2491   2301   -132    -13    355       S  
ATOM   1329  N   GLU B 591      25.430 -15.785  -0.002  1.00 18.97           N  
ANISOU 1329  N   GLU B 591     1985   2553   2669   -192    149    805       N  
ATOM   1330  CA  GLU B 591      24.481 -16.639   0.737  1.00 21.53           C  
ANISOU 1330  CA  GLU B 591     2234   2839   3108   -206    226    971       C  
ATOM   1331  C   GLU B 591      23.617 -17.416  -0.256  1.00 52.76           C  
ANISOU 1331  C   GLU B 591     6125   6681   7241   -367    118   1017       C  
ATOM   1332  O   GLU B 591      23.384 -16.921  -1.356  1.00 27.72           O  
ANISOU 1332  O   GLU B 591     2942   3499   4092   -440      3    943       O  
ATOM   1333  CB  GLU B 591      23.561 -15.786   1.623  1.00 22.99           C  
ANISOU 1333  CB  GLU B 591     2321   3113   3302   -122    348   1087       C  
ATOM   1334  CG  GLU B 591      24.213 -15.080   2.802  1.00 25.15           C  
ANISOU 1334  CG  GLU B 591     2678   3479   3397     53    448   1058       C  
ATOM   1335  CD  GLU B 591      24.689 -15.883   4.000  1.00 41.23           C  
ANISOU 1335  CD  GLU B 591     4795   5515   5356    163    543   1121       C  
ATOM   1336  OE1 GLU B 591      25.330 -15.269   4.879  1.00 32.14           O  
ANISOU 1336  OE1 GLU B 591     3738   4433   4039    309    582   1069       O  
ATOM   1337  OE2 GLU B 591      24.474 -17.114   4.051  1.00 31.20           O  
ANISOU 1337  OE2 GLU B 591     3508   4165   4183    106    564   1215       O  
ATOM   1338  N   SER B 594      24.265 -18.256  -3.943  1.00 27.66           N  
ANISOU 1338  N   SER B 594     3177   3266   4066   -603   -307    712       N  
ATOM   1339  CA  SER B 594      24.708 -17.325  -4.966  1.00 26.42           C  
ANISOU 1339  CA  SER B 594     3087   3154   3798   -579   -368    590       C  
ATOM   1340  C   SER B 594      26.222 -17.166  -4.923  1.00 29.37           C  
ANISOU 1340  C   SER B 594     3581   3570   4010   -474   -297    487       C  
ATOM   1341  O   SER B 594      26.827 -17.266  -3.864  1.00 28.84           O  
ANISOU 1341  O   SER B 594     3502   3552   3904   -398   -190    514       O  
ATOM   1342  CB  SER B 594      24.037 -15.970  -4.755  1.00 28.22           C  
ANISOU 1342  CB  SER B 594     3187   3497   4038   -557   -326    633       C  
ATOM   1343  OG  SER B 594      24.734 -14.920  -5.412  1.00 31.53           O  
ANISOU 1343  OG  SER B 594     3673   3976   4329   -503   -329    527       O  
ATOM   1344  N   GLY B 595      26.826 -16.959  -6.079  1.00 24.90           N  
ANISOU 1344  N   GLY B 595     3128   2979   3354   -461   -358    381       N  
ATOM   1345  CA  GLY B 595      28.268 -16.763  -6.140  1.00 23.54           C  
ANISOU 1345  CA  GLY B 595     3040   2848   3058   -362   -283    304       C  
ATOM   1346  C   GLY B 595      28.595 -15.391  -6.670  1.00 23.89           C  
ANISOU 1346  C   GLY B 595     3066   2975   3034   -328   -260    258       C  
ATOM   1347  O   GLY B 595      29.719 -15.151  -7.110  1.00 23.19           O  
ANISOU 1347  O   GLY B 595     3043   2904   2863   -262   -214    199       O  
ATOM   1348  N   GLU B 596      27.590 -14.518  -6.734  1.00 19.38           N  
ANISOU 1348  N   GLU B 596     2407   2445   2511   -371   -291    294       N  
ATOM   1349  CA  GLU B 596      27.801 -13.198  -7.304  1.00 18.95           C  
ANISOU 1349  CA  GLU B 596     2347   2452   2401   -341   -274    257       C  
ATOM   1350  C   GLU B 596      27.032 -12.101  -6.636  1.00 20.47           C  
ANISOU 1350  C   GLU B 596     2416   2722   2639   -341   -242    311       C  
ATOM   1351  O   GLU B 596      25.994 -12.313  -5.996  1.00 21.63           O  
ANISOU 1351  O   GLU B 596     2472   2876   2873   -373   -249    392       O  
ATOM   1352  CB  GLU B 596      27.595 -13.182  -8.844  1.00 22.62           C  
ANISOU 1352  CB  GLU B 596     2923   2857   2815   -360   -371    209       C  
ATOM   1353  CG  GLU B 596      26.163 -13.169  -9.328  1.00 33.26           C  
ANISOU 1353  CG  GLU B 596     4230   4170   4235   -438   -501    246       C  
ATOM   1354  CD  GLU B 596      25.991 -13.498 -10.804  1.00 52.35           C  
ANISOU 1354  CD  GLU B 596     6803   6503   6586   -448   -636    184       C  
ATOM   1355  OE1 GLU B 596      24.981 -14.154 -11.142  1.00 53.81           O  
ANISOU 1355  OE1 GLU B 596     6986   6610   6848   -529   -789    200       O  
ATOM   1356  OE2 GLU B 596      26.874 -13.134 -11.617  1.00 38.49           O  
ANISOU 1356  OE2 GLU B 596     5173   4750   4701   -371   -592    125       O  
ATOM   1357  N   LEU B 597      27.565 -10.907  -6.804  1.00 16.01           N  
ANISOU 1357  N   LEU B 597     1853   2209   2022   -298   -198    276       N  
ATOM   1358  CA  LEU B 597      26.936  -9.669  -6.392  1.00 13.85           C  
ANISOU 1358  CA  LEU B 597     1499   1993   1768   -280   -171    308       C  
ATOM   1359  C   LEU B 597      26.279  -9.074  -7.612  1.00 15.34           C  
ANISOU 1359  C   LEU B 597     1708   2166   1954   -306   -240    307       C  
ATOM   1360  O   LEU B 597      26.909  -8.978  -8.673  1.00 14.50           O  
ANISOU 1360  O   LEU B 597     1697   2029   1782   -298   -258    256       O  
ATOM   1361  CB  LEU B 597      27.981  -8.695  -5.836  1.00 12.16           C  
ANISOU 1361  CB  LEU B 597     1289   1820   1510   -221    -99    264       C  
ATOM   1362  CG  LEU B 597      27.532  -7.218  -5.663  1.00 13.08           C  
ANISOU 1362  CG  LEU B 597     1369   1972   1629   -192    -78    273       C  
ATOM   1363  CD1 LEU B 597      26.470  -7.057  -4.558  1.00 13.85           C  
ANISOU 1363  CD1 LEU B 597     1397   2108   1758   -156    -48    340       C  
ATOM   1364  CD2 LEU B 597      28.730  -6.336  -5.390  1.00 12.74           C  
ANISOU 1364  CD2 LEU B 597     1349   1932   1561   -160    -43    215       C  
ATOM   1365  N   MET B 598      25.016  -8.667  -7.462  1.00 13.41           N  
ANISOU 1365  N   MET B 598     1374   1946   1777   -322   -271    374       N  
ATOM   1366  CA  MET B 598      24.300  -7.980  -8.522  1.00 14.68           C  
ANISOU 1366  CA  MET B 598     1541   2101   1937   -333   -346    383       C  
ATOM   1367  C   MET B 598      23.992  -6.564  -8.011  1.00 17.47           C  
ANISOU 1367  C   MET B 598     1832   2513   2293   -273   -274    413       C  
ATOM   1368  O   MET B 598      23.513  -6.398  -6.889  1.00 20.90           O  
ANISOU 1368  O   MET B 598     2179   2987   2773   -241   -209    468       O  
ATOM   1369  CB  MET B 598      23.005  -8.732  -8.910  1.00 18.63           C  
ANISOU 1369  CB  MET B 598     1975   2567   2535   -404   -474    444       C  
ATOM   1370  N   LEU B 599      24.385  -5.543  -8.763  1.00 13.45           N  
ANISOU 1370  N   LEU B 599     1388   2000   1722   -242   -266    377       N  
ATOM   1371  CA  LEU B 599      24.037  -4.181  -8.403  1.00 13.01           C  
ANISOU 1371  CA  LEU B 599     1296   1976   1672   -185   -211    403       C  
ATOM   1372  C   LEU B 599      23.249  -3.592  -9.530  1.00 16.12           C  
ANISOU 1372  C   LEU B 599     1700   2363   2061   -179   -285    433       C  
ATOM   1373  O   LEU B 599      23.595  -3.802 -10.700  1.00 17.94           O  
ANISOU 1373  O   LEU B 599     2027   2558   2232   -196   -344    399       O  
ATOM   1374  CB  LEU B 599      25.295  -3.282  -8.241  1.00 12.11           C  
ANISOU 1374  CB  LEU B 599     1250   1846   1506   -151   -134    341       C  
ATOM   1375  CG  LEU B 599      26.240  -3.662  -7.123  1.00 13.90           C  
ANISOU 1375  CG  LEU B 599     1474   2078   1729   -145    -81    300       C  
ATOM   1376  CD1 LEU B 599      27.538  -2.860  -7.252  1.00 14.27           C  
ANISOU 1376  CD1 LEU B 599     1571   2092   1758   -139    -42    244       C  
ATOM   1377  CD2 LEU B 599      25.611  -3.388  -5.766  1.00 15.81           C  
ANISOU 1377  CD2 LEU B 599     1661   2355   1989    -89    -41    331       C  
ATOM   1378  N   LEU B 600      22.195  -2.844  -9.197  1.00 13.16           N  
ANISOU 1378  N   LEU B 600     1238   2023   1738   -136   -278    501       N  
ATOM   1379  CA  LEU B 600      21.495  -2.063 -10.219  1.00 13.45           C  
ANISOU 1379  CA  LEU B 600     1287   2058   1765   -109   -344    534       C  
ATOM   1380  C   LEU B 600      21.889  -0.613  -9.913  1.00 15.66           C  
ANISOU 1380  C   LEU B 600     1611   2333   2008    -32   -241    522       C  
ATOM   1381  O   LEU B 600      21.678  -0.156  -8.788  1.00 14.75           O  
ANISOU 1381  O   LEU B 600     1444   2239   1921     19   -161    542       O  
ATOM   1382  CB  LEU B 600      19.982  -2.250 -10.158  1.00 15.07           C  
ANISOU 1382  CB  LEU B 600     1347   2301   2078   -111   -420    633       C  
ATOM   1383  CG  LEU B 600      19.188  -1.490 -11.234  1.00 17.68           C  
ANISOU 1383  CG  LEU B 600     1680   2634   2402    -74   -515    673       C  
ATOM   1384  CD1 LEU B 600      19.479  -2.047 -12.649  1.00 16.56           C  
ANISOU 1384  CD1 LEU B 600     1667   2443   2181   -120   -659    617       C  
ATOM   1385  CD2 LEU B 600      17.703  -1.526 -10.935  1.00 19.48           C  
ANISOU 1385  CD2 LEU B 600     1720   2912   2771    -62   -568    792       C  
ATOM   1386  N   VAL B 601      22.478   0.068 -10.891  1.00 13.90           N  
ANISOU 1386  N   VAL B 601     1496   2069   1716    -19   -241    494       N  
ATOM   1387  CA  VAL B 601      22.972   1.424 -10.661  1.00 13.75           C  
ANISOU 1387  CA  VAL B 601     1528   2017   1681     36   -151    482       C  
ATOM   1388  C   VAL B 601      22.462   2.416 -11.645  1.00 17.10           C  
ANISOU 1388  C   VAL B 601     2000   2420   2076     90   -173    528       C  
ATOM   1389  O   VAL B 601      22.097   2.072 -12.782  1.00 16.89           O  
ANISOU 1389  O   VAL B 601     2012   2398   2008     86   -260    549       O  
ATOM   1390  CB  VAL B 601      24.529   1.462 -10.635  1.00 15.91           C  
ANISOU 1390  CB  VAL B 601     1878   2240   1928     -1    -85    415       C  
ATOM   1391  CG1 VAL B 601      25.098   0.471  -9.613  1.00 14.68           C  
ANISOU 1391  CG1 VAL B 601     1679   2106   1795    -43    -72    370       C  
ATOM   1392  CG2 VAL B 601      25.125   1.224 -12.021  1.00 16.27           C  
ANISOU 1392  CG2 VAL B 601     2017   2255   1909    -17    -97    414       C  
ATOM   1393  N   ARG B 602      22.520   3.687 -11.224  1.00 16.82           N  
ANISOU 1393  N   ARG B 602     1989   2349   2052    150    -99    535       N  
ATOM   1394  CA  ARG B 602      22.252   4.848 -12.053  1.00 17.19           C  
ANISOU 1394  CA  ARG B 602     2104   2355   2072    213    -91    579       C  
ATOM   1395  C   ARG B 602      23.630   5.415 -12.373  1.00 19.63           C  
ANISOU 1395  C   ARG B 602     2515   2579   2364    182    -13    543       C  
ATOM   1396  O   ARG B 602      24.317   5.872 -11.458  1.00 18.11           O  
ANISOU 1396  O   ARG B 602     2324   2340   2217    166     44    498       O  
ATOM   1397  CB  ARG B 602      21.389   5.864 -11.300  1.00 17.82           C  
ANISOU 1397  CB  ARG B 602     2147   2434   2191    306    -53    619       C  
ATOM   1398  CG  ARG B 602      21.232   7.216 -12.006  1.00 33.13           C  
ANISOU 1398  CG  ARG B 602     4173   4309   4107    382    -27    662       C  
ATOM   1399  CD  ARG B 602      20.030   7.293 -12.922  1.00 47.04           C  
ANISOU 1399  CD  ARG B 602     5901   6121   5852    446   -109    747       C  
ATOM   1400  NE  ARG B 602      19.913   8.629 -13.514  1.00 61.06           N  
ANISOU 1400  NE  ARG B 602     7771   7828   7601    534    -72    794       N  
ATOM   1401  CZ  ARG B 602      18.933   9.012 -14.324  1.00 79.08           C  
ANISOU 1401  CZ  ARG B 602    10048  10138   9861    617   -138    875       C  
ATOM   1402  NH1 ARG B 602      17.963   8.166 -14.651  1.00 64.22           N  
ANISOU 1402  NH1 ARG B 602     8056   8349   7996    614   -264    915       N  
ATOM   1403  NH2 ARG B 602      18.912  10.245 -14.810  1.00 72.80           N  
ANISOU 1403  NH2 ARG B 602     9354   9270   9038    703    -90    920       N  
ATOM   1404  N   PRO B 603      24.107   5.345 -13.635  1.00 22.02           N  
ANISOU 1404  N   PRO B 603     2904   2857   2607    176    -11    565       N  
ATOM   1405  CA  PRO B 603      25.452   5.884 -13.939  1.00 24.64           C  
ANISOU 1405  CA  PRO B 603     3304   3107   2951    147     91    561       C  
ATOM   1406  C   PRO B 603      25.547   7.386 -13.682  1.00 33.14           C  
ANISOU 1406  C   PRO B 603     4415   4093   4085    180    153    587       C  
ATOM   1407  O   PRO B 603      24.544   8.084 -13.795  1.00 33.22           O  
ANISOU 1407  O   PRO B 603     4440   4103   4078    255    128    628       O  
ATOM   1408  CB  PRO B 603      25.640   5.572 -15.432  1.00 27.44           C  
ANISOU 1408  CB  PRO B 603     3761   3461   3205    178     94    607       C  
ATOM   1409  CG  PRO B 603      24.615   4.560 -15.758  1.00 31.81           C  
ANISOU 1409  CG  PRO B 603     4300   4091   3694    192    -39    597       C  
ATOM   1410  CD  PRO B 603      23.451   4.830 -14.850  1.00 25.82           C  
ANISOU 1410  CD  PRO B 603     3431   3375   3004    206   -100    603       C  
ATOM   1411  N   ASN B 604      26.742   7.881 -13.293  1.00 34.22           N  
ANISOU 1411  N   ASN B 604     4555   4144   4303    122    224    565       N  
ATOM   1412  CA  ASN B 604      26.953   9.305 -13.000  1.00 65.02           C  
ANISOU 1412  CA  ASN B 604     8499   7925   8280    134    267    579       C  
ATOM   1413  C   ASN B 604      26.979  10.178 -14.245  1.00 92.63           C  
ANISOU 1413  C   ASN B 604    12087  11352  11756    180    337    679       C  
ATOM   1414  O   ASN B 604      26.535  11.322 -14.187  1.00 58.08           O  
ANISOU 1414  O   ASN B 604     7765   6897   7405    232    350    709       O  
ATOM   1415  CB  ASN B 604      28.207   9.528 -12.146  1.00 65.26           C  
ANISOU 1415  CB  ASN B 604     8493   7871   8431     41    285    522       C  
ATOM   1416  CG  ASN B 604      29.442   8.808 -12.631  1.00 78.97           C  
ANISOU 1416  CG  ASN B 604    10184   9616  10206    -35    337    539       C  
ATOM   1417  OD1 ASN B 604      29.458   7.578 -12.791  1.00 68.46           O  
ANISOU 1417  OD1 ASN B 604     8818   8385   8807    -40    321    522       O  
ATOM   1418  ND2 ASN B 604      30.521   9.555 -12.819  1.00 68.61           N  
ANISOU 1418  ND2 ASN B 604     8863   8189   9018    -95    403    580       N  
TER    1419      ASN B 604                                                      
ATOM   1420  N   SER C   1      24.947  -6.077  16.597  1.00 11.11           N  
ANISOU 1420  N   SER C   1     1260   1445   1518     47   -101     61       N  
ATOM   1421  CA  SER C   1      25.278  -5.205  15.460  1.00 10.97           C  
ANISOU 1421  CA  SER C   1     1271   1431   1464    103    -79    123       C  
ATOM   1422  C   SER C   1      25.254  -6.046  14.207  1.00 12.11           C  
ANISOU 1422  C   SER C   1     1469   1629   1503    136   -143    119       C  
ATOM   1423  O   SER C   1      25.083  -7.273  14.299  1.00 12.43           O  
ANISOU 1423  O   SER C   1     1518   1686   1519     99   -197     57       O  
ATOM   1424  CB  SER C   1      26.643  -4.546  15.647  1.00 12.76           C  
ANISOU 1424  CB  SER C   1     1513   1613   1723     94     11    134       C  
ATOM   1425  OG  SER C   1      26.659  -3.914  16.921  1.00 13.43           O  
ANISOU 1425  OG  SER C   1     1561   1651   1891     51     45    102       O  
ATOM   1426  N   TRP C   2      25.340  -5.376  13.025  1.00 12.70           N  
ANISOU 1426  N   TRP C   2     1596   1722   1509    211   -131    187       N  
ATOM   1427  CA  TRP C   2      25.342  -6.098  11.757  1.00 13.61           C  
ANISOU 1427  CA  TRP C   2     1797   1890   1484    257   -192    177       C  
ATOM   1428  C   TRP C   2      24.118  -7.007  11.639  1.00 15.31           C  
ANISOU 1428  C   TRP C   2     1980   2159   1679    228   -339    107       C  
ATOM   1429  O   TRP C   2      24.220  -8.139  11.184  1.00 16.59           O  
ANISOU 1429  O   TRP C   2     2199   2338   1768    205   -393     33       O  
ATOM   1430  CB  TRP C   2      26.671  -6.884  11.580  1.00 13.31           C  
ANISOU 1430  CB  TRP C   2     1827   1827   1404    245   -120    147       C  
ATOM   1431  CG  TRP C   2      27.889  -5.997  11.582  1.00 12.07           C  
ANISOU 1431  CG  TRP C   2     1674   1616   1297    268     23    215       C  
ATOM   1432  CD1 TRP C   2      28.900  -5.986  12.500  1.00 12.56           C  
ANISOU 1432  CD1 TRP C   2     1675   1632   1466    213     94    196       C  
ATOM   1433  CD2 TRP C   2      28.185  -4.958  10.642  1.00 12.59           C  
ANISOU 1433  CD2 TRP C   2     1796   1664   1325    350    112    314       C  
ATOM   1434  NE1 TRP C   2      29.805  -4.996  12.192  1.00 13.76           N  
ANISOU 1434  NE1 TRP C   2     1821   1732   1676    238    217    264       N  
ATOM   1435  CE2 TRP C   2      29.409  -4.370  11.032  1.00 15.01           C  
ANISOU 1435  CE2 TRP C   2     2059   1896   1747    325    250    345       C  
ATOM   1436  CE3 TRP C   2      27.569  -4.511   9.466  1.00 14.44           C  
ANISOU 1436  CE3 TRP C   2     2118   1938   1432    452     89    384       C  
ATOM   1437  CZ2 TRP C   2      29.989  -3.310  10.333  1.00 15.92           C  
ANISOU 1437  CZ2 TRP C   2     2209   1954   1886    385    393    447       C  
ATOM   1438  CZ3 TRP C   2      28.162  -3.487   8.745  1.00 17.20           C  
ANISOU 1438  CZ3 TRP C   2     2527   2240   1769    535    231    500       C  
ATOM   1439  CH2 TRP C   2      29.360  -2.893   9.177  1.00 17.37           C  
ANISOU 1439  CH2 TRP C   2     2499   2166   1935    496    396    532       C  
ATOM   1440  N   GLU C   3      22.950  -6.500  12.058  1.00 15.36           N  
ANISOU 1440  N   GLU C   3     1887   2180   1771    225   -394    127       N  
ATOM   1441  CA  GLU C   3      21.674  -7.226  11.990  1.00 17.28           C  
ANISOU 1441  CA  GLU C   3     2053   2467   2046    188   -532     67       C  
ATOM   1442  C   GLU C   3      21.601  -8.485  12.844  1.00 18.76           C  
ANISOU 1442  C   GLU C   3     2206   2613   2310     84   -530    -28       C  
ATOM   1443  O   GLU C   3      20.785  -9.369  12.600  1.00 21.97           O  
ANISOU 1443  O   GLU C   3     2569   3039   2741     36   -634   -102       O  
ATOM   1444  CB  GLU C   3      21.181  -7.456  10.545  1.00 20.61           C  
ANISOU 1444  CB  GLU C   3     2529   2977   2326    248   -681     52       C  
ATOM   1445  CG  GLU C   3      21.028  -6.171   9.738  1.00 25.89           C  
ANISOU 1445  CG  GLU C   3     3229   3690   2917    377   -685    173       C  
ATOM   1446  CD  GLU C   3      19.791  -5.344  10.019  1.00 53.14           C  
ANISOU 1446  CD  GLU C   3     6539   7169   6483    415   -742    240       C  
ATOM   1447  OE1 GLU C   3      18.832  -5.435   9.219  1.00 54.44           O  
ANISOU 1447  OE1 GLU C   3     6663   7427   6597    465   -913    238       O  
ATOM   1448  OE2 GLU C   3      19.800  -4.561  10.996  1.00 47.22           O  
ANISOU 1448  OE2 GLU C   3     5724   6348   5868    406   -616    296       O  
ATOM   1449  N   SER C   4      22.446  -8.543  13.877  1.00 14.03           N  
ANISOU 1449  N   SER C   4     1622   1952   1758     51   -410    -26       N  
ATOM   1450  CA ASER C   4      22.433  -9.631  14.843  0.50 13.27           C  
ANISOU 1450  CA ASER C   4     1505   1807   1731    -23   -378    -86       C  
ATOM   1451  CA BSER C   4      22.497  -9.631  14.846  0.50 13.14           C  
ANISOU 1451  CA BSER C   4     1492   1789   1711    -22   -375    -85       C  
ATOM   1452  C   SER C   4      22.243  -9.005  16.220  1.00 13.94           C  
ANISOU 1452  C   SER C   4     1531   1849   1916    -34   -291    -49       C  
ATOM   1453  O   SER C   4      22.721  -7.891  16.488  1.00 14.66           O  
ANISOU 1453  O   SER C   4     1633   1933   2004      1   -234      1       O  
ATOM   1454  CB ASER C   4      23.699 -10.473  14.762  0.50 14.97           C  
ANISOU 1454  CB ASER C   4     1816   1996   1874    -28   -328   -117       C  
ATOM   1455  CB BSER C   4      23.859 -10.309  14.806  0.50 15.02           C  
ANISOU 1455  CB BSER C   4     1826   2002   1877    -21   -315   -107       C  
ATOM   1456  OG ASER C   4      23.547 -11.520  13.808  0.50 14.46           O  
ANISOU 1456  OG ASER C   4     1809   1940   1746    -44   -397   -188       O  
ATOM   1457  OG BSER C   4      24.191 -10.701  13.480  0.50 19.20           O  
ANISOU 1457  OG BSER C   4     2442   2562   2291     10   -363   -133       O  
ATOM   1458  N   HIS C   5      21.507  -9.684  17.083  1.00 12.07           N  
ANISOU 1458  N   HIS C   5     1240   1574   1770    -83   -268    -75       N  
ATOM   1459  CA  HIS C   5      21.204  -9.194  18.421  1.00 11.39           C  
ANISOU 1459  CA  HIS C   5     1123   1445   1760    -84   -173    -44       C  
ATOM   1460  C   HIS C   5      22.427  -9.209  19.294  1.00 11.53           C  
ANISOU 1460  C   HIS C   5     1225   1441   1717    -76   -102    -46       C  
ATOM   1461  O   HIS C   5      23.092 -10.246  19.411  1.00 10.52           O  
ANISOU 1461  O   HIS C   5     1147   1301   1548    -90    -97    -72       O  
ATOM   1462  CB  HIS C   5      20.108 -10.060  19.072  1.00 13.18           C  
ANISOU 1462  CB  HIS C   5     1279   1625   2102   -131   -141    -62       C  
ATOM   1463  CG  HIS C   5      19.512  -9.421  20.287  1.00 17.73           C  
ANISOU 1463  CG  HIS C   5     1823   2157   2756   -113    -30    -19       C  
ATOM   1464  ND1 HIS C   5      19.868  -9.822  21.563  1.00 20.36           N  
ANISOU 1464  ND1 HIS C   5     2227   2439   3069   -111     79    -16       N  
ATOM   1465  CD2 HIS C   5      18.633  -8.391  20.378  1.00 21.36           C  
ANISOU 1465  CD2 HIS C   5     2204   2616   3297    -80     -6     25       C  
ATOM   1466  CE1 HIS C   5      19.135  -9.078  22.388  1.00 20.78           C  
ANISOU 1466  CE1 HIS C   5     2252   2457   3186    -85    173     20       C  
ATOM   1467  NE2 HIS C   5      18.406  -8.179  21.724  1.00 22.29           N  
ANISOU 1467  NE2 HIS C   5     2349   2672   3449    -66    133     46       N  
ATOM   1468  N   LYS C   6      22.717  -8.076  19.931  1.00  9.03           N  
ANISOU 1468  N   LYS C   6      920   1112   1398    -51    -52    -23       N  
ATOM   1469  CA  LYS C   6      23.840  -7.924  20.843  1.00  8.88           C  
ANISOU 1469  CA  LYS C   6      965   1082   1325    -47    -14    -39       C  
ATOM   1470  C   LYS C   6      23.286  -7.452  22.188  1.00 10.34           C  
ANISOU 1470  C   LYS C   6     1166   1227   1535    -39     62    -40       C  
ATOM   1471  O   LYS C   6      22.502  -6.488  22.244  1.00  9.79           O  
ANISOU 1471  O   LYS C   6     1063   1132   1523    -25    101    -21       O  
ATOM   1472  CB  LYS C   6      24.869  -6.945  20.285  1.00  9.72           C  
ANISOU 1472  CB  LYS C   6     1083   1203   1407    -35    -27    -34       C  
ATOM   1473  CG  LYS C   6      26.126  -6.828  21.146  1.00  8.79           C  
ANISOU 1473  CG  LYS C   6     1000   1084   1255    -44    -19    -67       C  
ATOM   1474  CD  LYS C   6      27.225  -6.002  20.454  1.00  8.75           C  
ANISOU 1474  CD  LYS C   6      979   1079   1266    -47    -21    -62       C  
ATOM   1475  CE  LYS C   6      28.489  -5.901  21.257  1.00 10.17           C  
ANISOU 1475  CE  LYS C   6     1156   1265   1442    -66    -39   -106       C  
ATOM   1476  NZ  LYS C   6      29.505  -5.105  20.464  1.00  9.48           N  
ANISOU 1476  NZ  LYS C   6     1027   1162   1416    -80    -18    -94       N  
ATOM   1477  N   SER C   7      23.699  -8.123  23.263  1.00 10.36           N  
ANISOU 1477  N   SER C   7     1232   1221   1483    -33     92    -56       N  
ATOM   1478  CA  SER C   7      23.213  -7.780  24.590  1.00  8.73           C  
ANISOU 1478  CA  SER C   7     1077    976   1263    -11    176    -59       C  
ATOM   1479  C   SER C   7      24.296  -8.242  25.574  1.00  9.98           C  
ANISOU 1479  C   SER C   7     1329   1158   1305     13    158    -84       C  
ATOM   1480  O   SER C   7      24.798  -9.381  25.423  1.00  9.76           O  
ANISOU 1480  O   SER C   7     1312   1150   1248     20    130    -68       O  
ATOM   1481  CB  SER C   7      21.900  -8.501  24.853  1.00 10.87           C  
ANISOU 1481  CB  SER C   7     1314   1202   1613    -10    258    -21       C  
ATOM   1482  OG  SER C   7      21.400  -8.185  26.144  1.00 11.94           O  
ANISOU 1482  OG  SER C   7     1518   1292   1728     27    373    -12       O  
ATOM   1483  N   GLY C   8      24.675  -7.399  26.533  1.00  8.82           N  
ANISOU 1483  N   GLY C   8     1253   1009   1091     30    165   -126       N  
ATOM   1484  CA  GLY C   8      25.714  -7.783  27.486  1.00  8.83           C  
ANISOU 1484  CA  GLY C   8     1337   1052    965     62    113   -155       C  
ATOM   1485  C   GLY C   8      27.041  -8.085  26.807  1.00 11.93           C  
ANISOU 1485  C   GLY C   8     1673   1504   1358     45      1   -167       C  
ATOM   1486  O   GLY C   8      27.843  -8.862  27.331  1.00 13.03           O  
ANISOU 1486  O   GLY C   8     1847   1686   1417     86    -49   -159       O  
ATOM   1487  N   GLY C   9      27.280  -7.479  25.645  1.00  9.32           N  
ANISOU 1487  N   GLY C   9     1256   1169   1115      0    -25   -173       N  
ATOM   1488  CA  GLY C   9      28.520  -7.707  24.911  1.00  9.68           C  
ANISOU 1488  CA  GLY C   9     1241   1256   1180    -11    -96   -174       C  
ATOM   1489  C   GLY C   9      28.580  -9.057  24.229  1.00 10.62           C  
ANISOU 1489  C   GLY C   9     1348   1387   1300     12    -90   -121       C  
ATOM   1490  O   GLY C   9      29.650  -9.500  23.826  1.00 11.39           O  
ANISOU 1490  O   GLY C   9     1412   1515   1401     26   -129   -112       O  
ATOM   1491  N   GLU C  10      27.421  -9.720  24.068  1.00  9.83           N  
ANISOU 1491  N   GLU C  10     1268   1251   1216     14    -32    -91       N  
ATOM   1492  CA  GLU C  10      27.325 -11.049  23.445  1.00  9.28           C  
ANISOU 1492  CA  GLU C  10     1200   1168   1159     23    -16    -61       C  
ATOM   1493  C   GLU C  10      26.442 -10.938  22.215  1.00 10.38           C  
ANISOU 1493  C   GLU C  10     1294   1288   1363    -17    -13    -65       C  
ATOM   1494  O   GLU C  10      25.350 -10.355  22.324  1.00  9.57           O  
ANISOU 1494  O   GLU C  10     1166   1164   1305    -35     10    -64       O  
ATOM   1495  CB  GLU C  10      26.637 -11.976  24.482  1.00 10.72           C  
ANISOU 1495  CB  GLU C  10     1444   1310   1318     52     53    -33       C  
ATOM   1496  CG  GLU C  10      26.346 -13.377  23.969  1.00 11.95           C  
ANISOU 1496  CG  GLU C  10     1608   1417   1514     48     96    -11       C  
ATOM   1497  CD  GLU C  10      25.654 -14.286  24.971  1.00 15.70           C  
ANISOU 1497  CD  GLU C  10     2143   1829   1994     75    198     31       C  
ATOM   1498  OE1 GLU C  10      24.901 -13.783  25.838  1.00 22.50           O  
ANISOU 1498  OE1 GLU C  10     3026   2672   2851     84    256     44       O  
ATOM   1499  OE2 GLU C  10      25.849 -15.513  24.884  1.00 12.51           O  
ANISOU 1499  OE2 GLU C  10     1772   1377   1604     94    243     57       O  
ATOM   1500  N   THR C  11      26.869 -11.509  21.084  1.00  7.61           N  
ANISOU 1500  N   THR C  11      937    943   1012    -20    -37    -68       N  
ATOM   1501  CA  THR C  11      26.091 -11.446  19.858  1.00  7.45           C  
ANISOU 1501  CA  THR C  11      892    920   1018    -46    -63    -81       C  
ATOM   1502  C   THR C  11      25.655 -12.831  19.473  1.00 10.11           C  
ANISOU 1502  C   THR C  11     1252   1219   1370    -66    -57   -105       C  
ATOM   1503  O   THR C  11      26.442 -13.770  19.601  1.00  9.25           O  
ANISOU 1503  O   THR C  11     1191   1089   1236    -43    -28   -103       O  
ATOM   1504  CB  THR C  11      26.910 -10.800  18.733  1.00  9.90           C  
ANISOU 1504  CB  THR C  11     1202   1263   1295    -28    -88    -73       C  
ATOM   1505  OG1 THR C  11      27.257  -9.469  19.154  1.00  9.19           O  
ANISOU 1505  OG1 THR C  11     1083   1185   1225    -24    -78    -57       O  
ATOM   1506  CG2 THR C  11      26.119 -10.683  17.430  1.00  9.63           C  
ANISOU 1506  CG2 THR C  11     1167   1244   1248    -32   -131    -82       C  
ATOM   1507  N   ARG C  12      24.404 -12.965  18.985  1.00 10.51           N  
ANISOU 1507  N   ARG C  12     1262   1255   1476   -109    -87   -131       N  
ATOM   1508  CA  ARG C  12      23.850 -14.204  18.479  1.00 10.55           C  
ANISOU 1508  CA  ARG C  12     1277   1213   1521   -152    -97   -181       C  
ATOM   1509  C   ARG C  12      24.091 -14.285  16.976  1.00 13.06           C  
ANISOU 1509  C   ARG C  12     1630   1564   1769   -151   -176   -228       C  
ATOM   1510  O   ARG C  12      23.651 -13.394  16.231  1.00 13.74           O  
ANISOU 1510  O   ARG C  12     1683   1708   1830   -142   -249   -226       O  
ATOM   1511  CB  ARG C  12      22.337 -14.246  18.727  1.00 14.60           C  
ANISOU 1511  CB  ARG C  12     1699   1696   2153   -208   -104   -196       C  
ATOM   1512  CG  ARG C  12      21.896 -14.219  20.159  1.00 20.29           C  
ANISOU 1512  CG  ARG C  12     2399   2369   2943   -203      3   -146       C  
ATOM   1513  CD  ARG C  12      20.382 -14.340  20.172  1.00 35.90           C  
ANISOU 1513  CD  ARG C  12     4262   4307   5071   -262      7   -161       C  
ATOM   1514  NE  ARG C  12      19.790 -13.907  21.435  1.00 44.98           N  
ANISOU 1514  NE  ARG C  12     5384   5420   6286   -240    123    -99       N  
ATOM   1515  CZ  ARG C  12      18.654 -13.221  21.526  1.00 56.04           C  
ANISOU 1515  CZ  ARG C  12     6672   6822   7799   -251    132    -80       C  
ATOM   1516  NH1 ARG C  12      18.002 -12.852  20.429  1.00 32.27           N  
ANISOU 1516  NH1 ARG C  12     3555   3863   4843   -279      7   -111       N  
ATOM   1517  NH2 ARG C  12      18.174 -12.878  22.713  1.00 47.00           N  
ANISOU 1517  NH2 ARG C  12     5525   5631   6702   -220    269    -23       N  
ATOM   1518  N   LEU C  13      24.722 -15.366  16.526  1.00 10.82           N  
ANISOU 1518  N   LEU C  13     1425   1240   1447   -149   -152   -268       N  
ATOM   1519  CA  LEU C  13      25.082 -15.606  15.115  1.00 11.91           C  
ANISOU 1519  CA  LEU C  13     1639   1397   1490   -134   -201   -320       C  
ATOM   1520  C   LEU C  13      24.369 -16.785  14.532  1.00 11.92           C  
ANISOU 1520  C   LEU C  13     1673   1337   1518   -199   -241   -425       C  
ATOM   1521  O   LEU C  13      23.742 -17.577  15.294  1.00 12.41           O  
ANISOU 1521  O   LEU C  13     1694   1320   1700   -259   -199   -447       O  
ATOM   1522  CB  LEU C  13      26.619 -15.883  14.943  1.00 12.75           C  
ANISOU 1522  CB  LEU C  13     1829   1492   1525    -64   -117   -287       C  
ATOM   1523  CG  LEU C  13      27.592 -14.714  15.072  1.00 18.89           C  
ANISOU 1523  CG  LEU C  13     2579   2327   2270     -4    -89   -207       C  
ATOM   1524  CD1 LEU C  13      27.246 -13.548  14.138  1.00 19.86           C  
ANISOU 1524  CD1 LEU C  13     2697   2512   2336     12   -147   -193       C  
ATOM   1525  CD2 LEU C  13      27.933 -14.398  16.511  1.00 23.18           C  
ANISOU 1525  CD2 LEU C  13     3058   2872   2879      1    -53   -152       C  
ATOM   1526  OXT LEU C  13      24.497 -16.988  13.313  1.00 12.66           O  
ANISOU 1526  OXT LEU C  13     1848   1450   1512   -189   -299   -490       O  
TER    1527      LEU C  13                                                      
ATOM   1528  N   GLY D   9      32.660   7.702   6.780  1.00 29.20           N  
ANISOU 1528  N   GLY D   9     4033   3670   3390    212   -108   -246       N  
ATOM   1529  CA  GLY D   9      31.411   7.410   6.080  1.00 28.17           C  
ANISOU 1529  CA  GLY D   9     3897   3531   3276    250   -112   -232       C  
ATOM   1530  C   GLY D   9      31.575   6.519   4.863  1.00 30.50           C  
ANISOU 1530  C   GLY D   9     4166   3855   3567    280   -142   -228       C  
ATOM   1531  O   GLY D   9      30.602   6.255   4.147  1.00 29.84           O  
ANISOU 1531  O   GLY D   9     4072   3778   3489    306   -144   -216       O  
ATOM   1532  N   GLU D  10      32.798   6.039   4.643  1.00 26.35           N  
ANISOU 1532  N   GLU D  10     3630   3351   3031    273   -162   -234       N  
ATOM   1533  CA  GLU D  10      33.176   5.199   3.510  1.00 24.68           C  
ANISOU 1533  CA  GLU D  10     3399   3161   2819    291   -183   -229       C  
ATOM   1534  C   GLU D  10      33.597   3.794   3.946  1.00 24.62           C  
ANISOU 1534  C   GLU D  10     3383   3170   2803    289   -203   -233       C  
ATOM   1535  O   GLU D  10      34.334   3.647   4.920  1.00 23.89           O  
ANISOU 1535  O   GLU D  10     3292   3083   2703    272   -208   -238       O  
ATOM   1536  CB  GLU D  10      34.336   5.884   2.769  1.00 26.38           C  
ANISOU 1536  CB  GLU D  10     3613   3378   3032    287   -180   -229       C  
ATOM   1537  CG  GLU D  10      34.678   5.273   1.424  1.00 32.13           C  
ANISOU 1537  CG  GLU D  10     4326   4116   3766    300   -194   -221       C  
ATOM   1538  CD  GLU D  10      35.880   5.864   0.714  1.00 44.28           C  
ANISOU 1538  CD  GLU D  10     5868   5648   5307    296   -195   -226       C  
ATOM   1539  OE1 GLU D  10      36.763   6.456   1.378  1.00 43.79           O  
ANISOU 1539  OE1 GLU D  10     5817   5586   5235    279   -188   -238       O  
ATOM   1540  OE2 GLU D  10      35.946   5.708  -0.523  1.00 30.19           O  
ANISOU 1540  OE2 GLU D  10     4077   3861   3532    306   -200   -220       O  
ATOM   1541  N   THR D  11      33.194   2.770   3.172  1.00 19.39           N  
ANISOU 1541  N   THR D  11     2708   2518   2140    303   -206   -230       N  
ATOM   1542  CA  THR D  11      33.588   1.384   3.443  1.00 18.14           C  
ANISOU 1542  CA  THR D  11     2544   2373   1975    304   -207   -231       C  
ATOM   1543  C   THR D  11      34.129   0.754   2.160  1.00 18.55           C  
ANISOU 1543  C   THR D  11     2583   2434   2029    304   -201   -218       C  
ATOM   1544  O   THR D  11      33.533   0.911   1.090  1.00 18.02           O  
ANISOU 1544  O   THR D  11     2512   2371   1964    305   -197   -216       O  
ATOM   1545  CB  THR D  11      32.411   0.545   4.009  1.00 19.92           C  
ANISOU 1545  CB  THR D  11     2776   2598   2194    314   -197   -247       C  
ATOM   1546  OG1 THR D  11      31.900   1.157   5.194  1.00 18.56           O  
ANISOU 1546  OG1 THR D  11     2620   2407   2026    310   -202   -258       O  
ATOM   1547  CG2 THR D  11      32.809  -0.914   4.333  1.00 18.13           C  
ANISOU 1547  CG2 THR D  11     2546   2383   1958    320   -182   -249       C  
ATOM   1548  N   ARG D  12      35.244   0.018   2.284  1.00 18.77           N  
ANISOU 1548  N   ARG D  12     2606   2468   2058    300   -198   -206       N  
ATOM   1549  CA  ARG D  12      35.869  -0.730   1.202  1.00 18.70           C  
ANISOU 1549  CA  ARG D  12     2590   2459   2056    293   -184   -190       C  
ATOM   1550  C   ARG D  12      35.222  -2.128   1.186  1.00 21.86           C  
ANISOU 1550  C   ARG D  12     2991   2869   2447    295   -149   -193       C  
ATOM   1551  O   ARG D  12      35.095  -2.766   2.244  1.00 22.92           O  
ANISOU 1551  O   ARG D  12     3128   3010   2573    307   -137   -197       O  
ATOM   1552  CB  ARG D  12      37.381  -0.861   1.479  1.00 21.73           C  
ANISOU 1552  CB  ARG D  12     2968   2844   2446    289   -189   -170       C  
ATOM   1553  CG  ARG D  12      38.119   0.486   1.573  1.00 32.78           C  
ANISOU 1553  CG  ARG D  12     4370   4240   3846    283   -215   -175       C  
ATOM   1554  CD  ARG D  12      39.359   0.421   2.454  1.00 50.92           C  
ANISOU 1554  CD  ARG D  12     6657   6556   6134    277   -222   -160       C  
ATOM   1555  NE  ARG D  12      39.143  -0.411   3.643  1.00 62.40           N  
ANISOU 1555  NE  ARG D  12     8103   8032   7576    285   -213   -151       N  
ATOM   1556  CZ  ARG D  12      40.028  -0.585   4.617  1.00 78.74           C  
ANISOU 1556  CZ  ARG D  12    10156  10131   9630    281   -218   -133       C  
ATOM   1557  NH1 ARG D  12      41.199   0.039   4.581  1.00 69.89           N  
ANISOU 1557  NH1 ARG D  12     9027   9027   8502    267   -233   -124       N  
ATOM   1558  NH2 ARG D  12      39.742  -1.372   5.646  1.00 63.99           N  
ANISOU 1558  NH2 ARG D  12     8281   8282   7752    292   -208   -126       N  
ATOM   1559  N   LEU D  13      34.801  -2.590   0.006  1.00 17.74           N  
ANISOU 1559  N   LEU D  13     2468   2349   1924    280   -127   -192       N  
ATOM   1560  CA  LEU D  13      34.167  -3.902  -0.218  1.00 16.59           C  
ANISOU 1560  CA  LEU D  13     2325   2216   1763    271    -79   -199       C  
ATOM   1561  C   LEU D  13      34.990  -4.780  -1.123  1.00 15.64           C  
ANISOU 1561  C   LEU D  13     2204   2086   1651    247    -39   -177       C  
ATOM   1562  O   LEU D  13      34.691  -5.988  -1.182  1.00 16.70           O  
ANISOU 1562  O   LEU D  13     2345   2228   1772    236     19   -180       O  
ATOM   1563  CB  LEU D  13      32.764  -3.757  -0.891  1.00 17.18           C  
ANISOU 1563  CB  LEU D  13     2397   2312   1819    259    -75   -220       C  
ATOM   1564  CG  LEU D  13      31.541  -3.249  -0.078  1.00 22.98           C  
ANISOU 1564  CG  LEU D  13     3134   3055   2541    279    -95   -243       C  
ATOM   1565  CD1 LEU D  13      31.359  -3.960   1.235  1.00 23.63           C  
ANISOU 1565  CD1 LEU D  13     3231   3130   2616    298    -80   -262       C  
ATOM   1566  CD2 LEU D  13      31.518  -1.751   0.055  1.00 23.47           C  
ANISOU 1566  CD2 LEU D  13     3193   3107   2619    292   -139   -235       C  
ATOM   1567  OXT LEU D  13      35.855  -4.243  -1.848  1.00 16.77           O  
ANISOU 1567  OXT LEU D  13     2345   2212   1815    235    -58   -159       O  
TER    1568      LEU D  13                                                      
HETATM 1569  C1  GOL A   1      15.466 -25.894  15.333  1.00 37.25           C  
HETATM 1570  O1  GOL A   1      16.758 -25.259  15.128  1.00 38.59           O  
HETATM 1571  C2  GOL A   1      15.509 -26.958  16.437  1.00 36.37           C  
HETATM 1572  O2  GOL A   1      16.653 -26.735  17.210  1.00 37.74           O  
HETATM 1573  C3  GOL A   1      14.443 -26.614  17.426  1.00 35.33           C  
HETATM 1574  O3  GOL A   1      14.293 -27.667  18.332  1.00 30.41           O  
HETATM 1575  C1  GOL A 605      25.638 -26.999  25.963  1.00 27.91           C  
HETATM 1576  O1  GOL A 605      25.279 -26.222  24.826  1.00 22.00           O  
HETATM 1577  C2  GOL A 605      24.487 -27.773  26.552  1.00 28.81           C  
HETATM 1578  O2  GOL A 605      23.815 -28.524  25.560  1.00 29.42           O  
HETATM 1579  C3  GOL A 605      24.941 -28.817  27.551  1.00 28.51           C  
HETATM 1580  O3  GOL A 605      25.982 -28.304  28.344  1.00 28.03           O  
HETATM 1581  O   HOH A   2      27.754 -32.187  16.461  1.00  9.19           O  
HETATM 1582  O   HOH A   4      33.522 -30.971  19.805  1.00 13.87           O  
HETATM 1583  O   HOH A   5      21.583 -32.125  18.753  1.00 10.50           O  
HETATM 1584  O   HOH A   6      31.777 -15.886   6.769  1.00 12.59           O  
HETATM 1585  O   HOH A   8      32.481  -4.111  18.995  1.00 12.47           O  
HETATM 1586  O   HOH A   9      34.919 -27.633  19.247  1.00 14.84           O  
HETATM 1587  O   HOH A  10      30.178 -31.356  22.719  1.00 12.10           O  
HETATM 1588  O   HOH A  11      17.362 -19.150  11.479  1.00 15.96           O  
HETATM 1589  O   HOH A  13      27.318 -19.696   3.228  1.00 16.34           O  
HETATM 1590  O   HOH A  14      26.477 -28.419  11.034  1.00 15.21           O  
HETATM 1591  O   HOH A  15      31.372 -11.566   2.136  1.00 17.06           O  
HETATM 1592  O   HOH A  17      21.042 -21.617  13.315  1.00 14.57           O  
HETATM 1593  O   HOH A  18      33.654  -2.307  15.798  1.00 16.27           O  
HETATM 1594  O   HOH A  19      35.240 -13.940   7.181  1.00 12.57           O  
HETATM 1595  O   HOH A  20      30.925 -29.827  10.021  1.00 15.47           O  
HETATM 1596  O   HOH A  22      35.499 -28.064  22.621  1.00 16.56           O  
HETATM 1597  O   HOH A  23      22.591 -26.102  23.824  1.00 17.81           O  
HETATM 1598  O   HOH A  24      17.642 -24.174  19.186  1.00 17.39           O  
HETATM 1599  O   HOH A  25      23.110 -19.608  20.657  1.00 19.20           O  
HETATM 1600  O   HOH A  26      33.745 -10.099   2.100  1.00 21.88           O  
HETATM 1601  O   HOH A  27      18.979 -23.454  12.522  1.00 18.27           O  
HETATM 1602  O  AHOH A  28      31.351  -1.893  17.589  0.50  9.96           O  
HETATM 1603  O  BHOH A  28      30.807  -1.778  18.659  0.50 13.37           O  
HETATM 1604  O   HOH A  29      34.985  -6.602  10.042  1.00 17.15           O  
HETATM 1605  O   HOH A  31      19.788 -26.075  11.964  1.00 16.61           O  
HETATM 1606  O   HOH A  32      36.119 -29.766  20.172  1.00 16.89           O  
HETATM 1607  O   HOH A  34      35.703  -2.508  27.267  1.00 19.84           O  
HETATM 1608  O   HOH A  36      19.941 -19.793  15.079  1.00 17.40           O  
HETATM 1609  O   HOH A  37      34.447  -8.765   5.419  1.00 25.48           O  
HETATM 1610  O   HOH A  40      13.464 -21.494   3.424  1.00 22.90           O  
HETATM 1611  O   HOH A  42      37.523 -13.521   8.480  1.00 20.75           O  
HETATM 1612  O   HOH A  49      42.640 -26.706  24.888  1.00 36.68           O  
HETATM 1613  O   HOH A  50      34.051 -29.536  10.224  1.00 19.99           O  
HETATM 1614  O   HOH A  55      37.561  -4.681  30.747  1.00 36.07           O  
HETATM 1615  O   HOH A  59      23.731 -28.294  10.111  1.00 18.71           O  
HETATM 1616  O   HOH A  61      38.305  -0.803  20.087  1.00 24.99           O  
HETATM 1617  O   HOH A  66      33.616  -3.040  31.018  1.00 25.56           O  
HETATM 1618  O   HOH A  72      23.990 -26.508   8.077  1.00 22.62           O  
HETATM 1619  O  AHOH A  73      35.345 -28.260  25.335  0.50 21.58           O  
HETATM 1620  O  BHOH A  73      33.428 -28.898  25.399  0.50 23.70           O  
HETATM 1621  O   HOH A  74      34.994  -6.846   7.223  1.00 25.94           O  
HETATM 1622  O   HOH A  75      17.418 -19.470  14.174  1.00 21.40           O  
HETATM 1623  O   HOH A  79      36.815 -31.044  12.268  1.00 24.50           O  
HETATM 1624  O   HOH A  88      23.613 -23.184   3.807  1.00 33.79           O  
HETATM 1625  O   HOH A  91      21.040 -16.014  23.295  1.00 27.56           O  
HETATM 1626  O   HOH A  94      42.575  -8.918   8.828  1.00 32.65           O  
HETATM 1627  O   HOH A  96      19.933 -26.203   7.612  1.00 28.79           O  
HETATM 1628  O   HOH A  98      43.619 -15.043  16.776  1.00 21.87           O  
HETATM 1629  O   HOH A  99      35.321  -3.996  29.338  1.00 26.73           O  
HETATM 1630  O   HOH A 101      28.294 -29.572   9.329  1.00 25.43           O  
HETATM 1631  O   HOH A 103      31.873 -26.781  26.607  1.00 21.85           O  
HETATM 1632  O   HOH A 104      20.970 -27.604  10.015  1.00 27.47           O  
HETATM 1633  O   HOH A 105      37.568   1.808  19.738  1.00 27.63           O  
HETATM 1634  O   HOH A 106      34.245  -4.320   6.228  1.00 33.43           O  
HETATM 1635  O   HOH A 108      32.828 -31.052   8.088  1.00 34.58           O  
HETATM 1636  O   HOH A 109      44.136  -9.402  14.345  1.00 37.27           O  
HETATM 1637  O   HOH A 111      33.706  -4.086  10.496  1.00 25.51           O  
HETATM 1638  O   HOH A 113      45.165 -13.275   9.213  1.00 25.43           O  
HETATM 1639  O   HOH A 117      23.929 -30.862   9.309  1.00 28.90           O  
HETATM 1640  O   HOH A 125      38.838 -14.549   5.093  1.00 28.56           O  
HETATM 1641  O   HOH A 127      40.441  -3.135  16.155  1.00 35.21           O  
HETATM 1642  O   HOH A 130      37.368  -5.175  10.058  1.00 34.69           O  
HETATM 1643  O   HOH A 131      37.022 -20.792  27.827  1.00 29.49           O  
HETATM 1644  O   HOH A 133      36.689 -32.588  10.115  1.00 41.68           O  
HETATM 1645  O   HOH A 134      25.937 -32.901  10.831  1.00 30.85           O  
HETATM 1646  O   HOH A 137      23.277 -33.067  10.546  1.00 39.65           O  
HETATM 1647  O   HOH A 138      22.066  -9.064   4.991  1.00 33.46           O  
HETATM 1648  O   HOH A 139      16.791 -21.936  14.890  1.00 34.47           O  
HETATM 1649  O   HOH A 142      17.340 -21.953  17.697  1.00 36.30           O  
HETATM 1650  O   HOH A 150      40.168  -1.105  18.091  1.00 30.61           O  
HETATM 1651  O   HOH A 151      20.488 -25.196  25.462  1.00 34.18           O  
HETATM 1652  O   HOH A 161      40.017   2.835  20.035  1.00 40.04           O  
HETATM 1653  O   HOH A 163      34.961 -22.139  29.625  1.00 34.80           O  
HETATM 1654  O   HOH A 164      44.150 -10.299  10.456  1.00 35.87           O  
HETATM 1655  O   HOH A 170      16.838 -21.223   8.256  1.00 20.47           O  
HETATM 1656  O   HOH A 173      41.377 -20.807  25.089  1.00 39.67           O  
HETATM 1657  O   HOH A 179      42.436 -30.505  19.489  1.00 26.69           O  
HETATM 1658  O   HOH A 180      22.285 -25.708   6.337  1.00 42.53           O  
HETATM 1659  O   HOH A 182      35.346 -25.402  25.063  1.00 17.46           O  
HETATM 1660  O   HOH A 187      37.736 -28.982  26.516  1.00 37.41           O  
HETATM 1661  O   HOH A 188      25.158 -20.681   2.161  1.00 34.91           O  
HETATM 1662  O   HOH A 196      44.875  -7.541  12.452  1.00 50.84           O  
HETATM 1663  O   HOH A 199      23.238 -11.366   6.310  1.00 30.49           O  
HETATM 1664  O   HOH A 203      36.267 -17.264  -0.287  1.00 34.29           O  
HETATM 1665  O   HOH A 205      21.675 -10.480   8.562  1.00 38.23           O  
HETATM 1666  O   HOH A 212      33.223 -26.568  28.883  1.00 33.01           O  
HETATM 1667  O   HOH A 216      36.632 -20.179   4.573  1.00 30.57           O  
HETATM 1668  O   HOH A 221      40.627 -12.894  20.512  1.00 37.28           O  
HETATM 1669  O   HOH A 249      34.632  -6.429  28.536  1.00 32.19           O  
HETATM 1670  O   HOH A 250      29.576 -16.690  29.221  1.00 31.51           O  
HETATM 1671  O   HOH A 256      39.558 -10.427  19.123  1.00 32.56           O  
HETATM 1672  O   HOH A 258      27.598 -32.073   8.517  1.00 45.94           O  
HETATM 1673  O   HOH A 262      40.669 -10.020  21.586  1.00 36.75           O  
HETATM 1674  O   HOH A 266      13.162 -25.012   2.745  1.00 40.35           O  
HETATM 1675  O   HOH A 280      24.937 -22.858  27.009  1.00 32.53           O  
HETATM 1676  O   HOH A 303      19.458 -20.242  17.569  1.00 28.97           O  
HETATM 1677  O   HOH A 307      46.843 -18.475  21.441  1.00 30.45           O  
HETATM 1678  O  AHOH A 311      27.686 -27.881   7.190  0.50 16.91           O  
HETATM 1679  O  BHOH A 311      27.184 -27.477   8.534  0.50 15.08           O  
HETATM 1680  O   HOH A 315      40.543  -2.556  24.285  1.00 28.66           O  
HETATM 1681  O   HOH A 318      35.309 -13.710  26.381  1.00 31.86           O  
HETATM 1682  O   HOH A 323      28.824 -19.102  28.420  1.00 38.54           O  
HETATM 1683  O   HOH B  12      44.294  -2.370  -7.414  1.00 19.11           O  
HETATM 1684  O   HOH B  16      39.747  -7.204  -5.211  1.00 19.04           O  
HETATM 1685  O   HOH B  30      35.477  -3.858 -17.225  1.00 21.98           O  
HETATM 1686  O   HOH B  33      34.788  -9.104 -12.603  1.00 20.90           O  
HETATM 1687  O   HOH B  35      33.251 -11.129 -11.904  1.00 23.56           O  
HETATM 1688  O   HOH B  38      28.725 -18.491   1.034  1.00 22.37           O  
HETATM 1689  O   HOH B  39      22.371  -9.188  -0.303  1.00 18.33           O  
HETATM 1690  O   HOH B  43      28.359   1.296 -14.313  1.00 24.81           O  
HETATM 1691  O   HOH B  44      16.900   2.260  -4.242  1.00 26.43           O  
HETATM 1692  O   HOH B  47      24.123  -4.181   8.942  1.00 22.01           O  
HETATM 1693  O   HOH B  48      28.594  -6.495 -14.997  1.00 23.35           O  
HETATM 1694  O   HOH B  52      25.370 -15.505   7.551  1.00 24.73           O  
HETATM 1695  O   HOH B  57      31.655 -16.962  -6.706  1.00 26.32           O  
HETATM 1696  O   HOH B  60      25.269   1.632  12.064  1.00 30.36           O  
HETATM 1697  O   HOH B  63      26.656  10.133  -1.152  1.00 33.41           O  
HETATM 1698  O   HOH B  64      38.363  -1.489 -16.591  1.00 28.01           O  
HETATM 1699  O   HOH B  71      30.114   0.764 -17.231  1.00 32.51           O  
HETATM 1700  O   HOH B  77      25.324   2.858   9.140  1.00 23.17           O  
HETATM 1701  O   HOH B  78      34.636  -2.256 -19.316  1.00 26.75           O  
HETATM 1702  O   HOH B  80      20.289  -7.458  -0.691  1.00 29.89           O  
HETATM 1703  O   HOH B  82      36.106 -12.123  -9.912  1.00 30.72           O  
HETATM 1704  O   HOH B  83      23.361  -2.469  10.857  1.00 24.24           O  
HETATM 1705  O   HOH B  84      38.324   0.523  -3.820  1.00 29.10           O  
HETATM 1706  O   HOH B  85      34.293 -16.085  -7.041  1.00 32.92           O  
HETATM 1707  O   HOH B  89      39.962  -9.271 -10.200  1.00 28.63           O  
HETATM 1708  O   HOH B  90      43.104  -9.446 -15.610  1.00 29.50           O  
HETATM 1709  O   HOH B  93      24.948  -7.615 -15.876  1.00 29.57           O  
HETATM 1710  O   HOH B  95      31.601  -9.565 -16.468  1.00 27.91           O  
HETATM 1711  O   HOH B 110      28.395   3.747   9.328  1.00 35.35           O  
HETATM 1712  O   HOH B 112      37.551 -10.396 -11.651  1.00 29.75           O  
HETATM 1713  O   HOH B 115      13.159  -4.640  -2.906  1.00 28.18           O  
HETATM 1714  O   HOH B 116      41.595  -8.585 -17.724  1.00 31.57           O  
HETATM 1715  O   HOH B 122      39.087  -4.015 -18.379  1.00 39.29           O  
HETATM 1716  O   HOH B 123      27.234  10.584  -8.427  1.00 29.77           O  
HETATM 1717  O   HOH B 129      32.055  -1.555 -19.111  1.00 28.87           O  
HETATM 1718  O   HOH B 136      25.061   8.393 -10.430  1.00 33.83           O  
HETATM 1719  O   HOH B 147      41.658  -5.960 -18.111  1.00 34.27           O  
HETATM 1720  O   HOH B 149      25.689 -12.699   5.330  1.00 26.99           O  
HETATM 1721  O   HOH B 152      20.331   5.555  -1.834  1.00 44.00           O  
HETATM 1722  O   HOH B 158      29.539  11.406  -7.205  1.00 41.96           O  
HETATM 1723  O   HOH B 159      24.133   5.279  11.749  1.00 40.38           O  
HETATM 1724  O   HOH B 167      22.750   9.440  -9.544  1.00 41.16           O  
HETATM 1725  O   HOH B 178      22.318   0.021  10.458  1.00 27.45           O  
HETATM 1726  O   HOH B 181      37.558  -7.754 -18.161  1.00 36.40           O  
HETATM 1727  O   HOH B 185      41.522 -11.090 -14.114  1.00 46.79           O  
HETATM 1728  O   HOH B 192      35.631   4.656 -11.746  1.00 29.71           O  
HETATM 1729  O   HOH B 198      35.964   6.850 -13.170  1.00 35.65           O  
HETATM 1730  O   HOH B 217      20.323   3.867   1.275  1.00 40.76           O  
HETATM 1731  O   HOH B 224      41.177 -13.962  -6.808  1.00 31.03           O  
HETATM 1732  O   HOH B 226      27.862   2.050 -16.891  1.00 35.52           O  
HETATM 1733  O   HOH B 298      36.814  -0.585 -19.588  1.00 36.35           O  
HETATM 1734  O   HOH B 302      21.436  -5.836   5.625  1.00 32.20           O  
HETATM 1735  O   HOH B 310      30.346   1.240  11.401  1.00 34.01           O  
HETATM 1736  O   HOH B 312      21.622   2.946 -19.028  1.00 31.56           O  
HETATM 1737  O   HOH B 313      42.039  -9.692  -2.678  1.00 41.43           O  
HETATM 1738  O   HOH B 314      37.769   5.588 -16.633  1.00 28.63           O  
HETATM 1739  O   HOH B 316      19.915   5.066  -4.534  1.00 45.74           O  
HETATM 1740  O   HOH B 317      37.677   5.236  -8.462  1.00 26.70           O  
HETATM 1741  O   HOH B 322      11.592   5.879 -13.954  1.00 35.93           O  
HETATM 1742  O   HOH C  14      27.274  -7.476  17.257  1.00 10.63           O  
HETATM 1743  O   HOH C  15      21.027  -5.739  19.246  1.00 12.24           O  
HETATM 1744  O   HOH C  21      32.386  -3.132  13.105  1.00 15.66           O  
HETATM 1745  O   HOH C  41      20.318 -12.156  16.189  1.00 27.71           O  
HETATM 1746  O   HOH C  45      24.627 -15.236  11.303  1.00 19.39           O  
HETATM 1747  O   HOH C  53      25.247  -2.510  12.864  1.00 22.90           O  
HETATM 1748  O   HOH C  54      22.950 -17.811  18.014  1.00 19.70           O  
HETATM 1749  O   HOH C  58      22.303 -10.183  27.899  1.00 21.55           O  
HETATM 1750  O   HOH C  65      24.778 -11.742  27.589  1.00 27.27           O  
HETATM 1751  O   HOH C  67      18.982  -5.964  17.500  1.00 26.27           O  
HETATM 1752  O   HOH C  69      18.636  -8.829  25.800  1.00 28.24           O  
HETATM 1753  O   HOH C  81      27.176 -10.720  29.165  1.00 34.30           O  
HETATM 1754  O   HOH C  87      30.792  -9.767  27.289  1.00 29.34           O  
HETATM 1755  O   HOH C  92      25.341 -16.952  27.141  1.00 32.47           O  
HETATM 1756  O   HOH C 107      22.051  -5.497  14.871  1.00 29.75           O  
HETATM 1757  O   HOH C 118      24.258  -0.278  14.362  1.00 25.49           O  
HETATM 1758  O  AHOH C 191      23.045 -11.839  24.357  0.50 19.63           O  
HETATM 1759  O  BHOH C 191      22.568 -11.529  22.170  0.50 13.86           O  
HETATM 1760  O   HOH D  51      32.901  -2.642   7.833  1.00 26.82           O  
HETATM 1761  O   HOH D  56      33.278  -7.539   0.542  1.00 24.13           O  
HETATM 1762  O   HOH D  68      31.005  -0.209   7.379  1.00 25.28           O  
HETATM 1763  O   HOH D  76      38.615  -4.325  -1.482  1.00 31.54           O  
HETATM 1764  O   HOH D 296      36.582   0.038   4.975  1.00 25.13           O  
HETATM 1765  O   HOH D 309      32.249   0.364   9.650  1.00 33.81           O  
CONECT  606 1328                                                                
CONECT 1328  606                                                                
CONECT 1569 1570 1571                                                           
CONECT 1570 1569                                                                
CONECT 1571 1569 1572 1573                                                      
CONECT 1572 1571                                                                
CONECT 1573 1571 1574                                                           
CONECT 1574 1573                                                                
CONECT 1575 1576 1577                                                           
CONECT 1576 1575                                                                
CONECT 1577 1575 1578 1579                                                      
CONECT 1578 1577                                                                
CONECT 1579 1577 1580                                                           
CONECT 1580 1579                                                                
MASTER      379    0    2    7   15    0    5    6 1741    4   14   20          
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.