path: root/Docking/Target/6y84.pdb

HEADER    VIRAL PROTEIN                           03-MAR-20   6Y84              
TITLE     COVID-19 MAIN PROTEASE WITH UNLIGANDED ACTIVE SITE (2019-NCOV,        
TITLE    2 CORONAVIRUS DISEASE 2019, SARS-COV-2)                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL POLYPROTEIN 1AB;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_TAXID: 2697049;                                             
SOURCE   5 STRAIN: COVID-19;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEASE, CYSTEINE PROTEASE, VIRAL PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.OWEN,P.LUKACIK,C.M.STRAIN-DAMERELL,A.DOUANGAMATH,A.J.POWELL,      
AUTHOR   2 D.FEARON,J.BRANDAO-NETO,A.D.CRAWSHAW,D.ARAGAO,M.WILLIAMS,R.FLAIG,    
AUTHOR   3 D.HALL,K.MCAAULEY,D.I.STUART,F.VON DELFT,M.A.WALSH                   
REVDAT   1   11-MAR-20 6Y84    0                                                
JRNL        AUTH   C.D.OWEN,P.LUKACIK,C.M.STRAIN-DAMERELL,A.DOUANGAMATH,        
JRNL        AUTH 2 A.J.POWELL,D.FEARON,J.BRANDAO-NETO,A.D.CRAWSHAW,D.ARAGAO,    
JRNL        AUTH 3 M.WILLIAMS,R.FLAIG,D.HALL,K.MCAAULEY,D.I.STUART,F.VON DELFT, 
JRNL        AUTH 4 M.A.WALSH                                                    
JRNL        TITL   COVID-19 MAIN PROTEASE WITH UNLIGANDED ACTIVE SITE           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER                                               
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) : 1.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50331                          
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)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.178                          
REMARK   3   FREE R VALUE                      : 0.200                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.960                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2498                           
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               : 51                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.39                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.40                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 77.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1007                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2107                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 941                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2109                   
REMARK   3   BIN FREE R VALUE                        : 0.2075                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.55                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 66                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2347                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 391                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.78090                                             
REMARK   3    B22 (A**2) : 0.69780                                              
REMARK   3    B33 (A**2) : 3.08310                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04220                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.190               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.074               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.071               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.069               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.068               
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      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2628   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3595   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 909    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 466    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2628   ; 10.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 340    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3017   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.64                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   11.7561    0.8392    4.6891           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0121 T22:   -0.0177                                    
REMARK   3     T33:   -0.0441 T12:   -0.0060                                    
REMARK   3     T13:   -0.0248 T23:   -0.0095                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3373 L22:    0.9615                                    
REMARK   3     L33:    0.4899 L12:    0.1417                                    
REMARK   3     L13:   -0.0841 L23:   -0.7793                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0543 S12:    0.0192 S13:   -0.0247                     
REMARK   3     S21:   -0.0315 S22:    0.0611 S23:   -0.0331                     
REMARK   3     S31:    0.0069 S32:   -0.0231 S33:   -0.0068                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6Y84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292107053.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9126                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS, XIA2                        
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50348                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 6LU7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 5% DMSO, 0.1M MES PH       
REMARK 280  6.5. 0.15 MICROLITRE PROTEIN + 0.3 MICROLITRE RESERVOIR + 0.05      
REMARK 280  MICROLITRE SEED STOCK, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       56.40600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.47450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.40600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.47450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 774  LIES ON A SPECIAL POSITION.                          
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     PHE A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33     -132.67     57.52                                   
REMARK 500    ASN A  51       69.76   -154.49                                   
REMARK 500    ASN A  84     -119.94     56.10                                   
REMARK 500    TYR A 154      -89.93     58.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 889        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A 890        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 891        DISTANCE =  7.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404                 
DBREF  6Y84 A    1   306  PDB    6Y84     6Y84             1    306             
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL          
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR          
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO          
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO          
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN          
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE          
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL          
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL          
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS          
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET          
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY          
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS          
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR          
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR          
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY          
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU          
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN          
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA          
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL          
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA          
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN          
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU          
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN          
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN                                  
HET    DMS  A 401       4                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    DMS  A 404       4                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  DMS    4(C2 H6 O S)                                                 
FORMUL   6  HOH   *391(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLY A   15  1                                   6    
HELIX    2 AA2 HIS A   41  CYS A   44  5                                   4    
HELIX    3 AA3 GLU A   47  ASN A   51  5                                   5    
HELIX    4 AA4 ASN A   53  ARG A   60  1                                   8    
HELIX    5 AA5 LYS A   61  HIS A   64  5                                   4    
HELIX    6 AA6 ILE A  200  ASN A  214  1                                  15    
HELIX    7 AA7 THR A  226  TYR A  237  1                                  12    
HELIX    8 AA8 THR A  243  LEU A  250  1                                   8    
HELIX    9 AA9 LEU A  250  GLY A  258  1                                   9    
HELIX   10 AB1 ALA A  260  GLY A  275  1                                  16    
HELIX   11 AB2 THR A  292  GLY A  302  1                                  11    
SHEET    1 AA1 7 VAL A  73  LEU A  75  0                                        
SHEET    2 AA1 7 PHE A  66  ALA A  70 -1  N  VAL A  68   O  LEU A  75           
SHEET    3 AA1 7 MET A  17  CYS A  22 -1  N  GLN A  19   O  GLN A  69           
SHEET    4 AA1 7 THR A  25  LEU A  32 -1  O  LEU A  27   N  VAL A  20           
SHEET    5 AA1 7 VAL A  35  PRO A  39 -1  O  TYR A  37   N  LEU A  30           
SHEET    6 AA1 7 VAL A  86  VAL A  91 -1  O  LEU A  87   N  CYS A  38           
SHEET    7 AA1 7 VAL A  77  GLN A  83 -1  N  SER A  81   O  LYS A  88           
SHEET    1 AA2 5 LYS A 100  PHE A 103  0                                        
SHEET    2 AA2 5 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA2 5 VAL A 148  ASP A 153 -1  N  ASN A 151   O  SER A 158           
SHEET    4 AA2 5 THR A 111  TYR A 118 -1  N  SER A 113   O  PHE A 150           
SHEET    5 AA2 5 SER A 121  ALA A 129 -1  O  SER A 123   N  ALA A 116           
SHEET    1 AA3 3 LYS A 100  PHE A 103  0                                        
SHEET    2 AA3 3 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA3 3 HIS A 172  THR A 175 -1  O  ALA A 173   N  MET A 165           
SITE     1 AC1  8 GLN A  74  LEU A  75  ARG A  76  PHE A 223                    
SITE     2 AC1  8 THR A 224  ASP A 263  HOH A 570  HOH A 579                    
SITE     1 AC2  2 HIS A  64  ASN A  65                                          
SITE     1 AC3  6 MET A   6  PHE A   8  SER A 123  GLN A 127                    
SITE     2 AC3  6 ASP A 295  ARG A 298                                          
SITE     1 AC4  5 GLY A  15  MET A  17  LYS A  97  HOH A 620                    
SITE     2 AC4  5 HOH A 654                                                     
CRYST1  112.812   52.949   44.631  90.00 103.16  90.00 C 1 2 1       4          
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      0.008864  0.000000  0.002073        0.00000                         
SCALE2      0.000000  0.018886  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023010        0.00000                         
ATOM      1  N  ASER A   1      -2.185   4.397 -17.079  0.50 26.55           N  
ANISOU    1  N  ASER A   1     3790   3658   2638  -1331  -1030    674       N  
ATOM      2  N  BSER A   1      -2.224   4.310 -17.137  0.50 25.36           N  
ANISOU    2  N  BSER A   1     3647   3506   2482  -1342  -1039    678       N  
ATOM      3  CA ASER A   1      -2.021   5.695 -16.438  0.50 26.71           C  
ANISOU    3  CA ASER A   1     3697   3711   2741  -1239   -975    694       C  
ATOM      4  CA BSER A   1      -1.882   5.526 -16.417  0.50 25.40           C  
ANISOU    4  CA BSER A   1     3548   3538   2566  -1238   -970    677       C  
ATOM      5  C  ASER A   1      -2.350   5.650 -14.945  0.50 25.98           C  
ANISOU    5  C  ASER A   1     3512   3620   2738  -1150   -937    712       C  
ATOM      6  C  BSER A   1      -2.298   5.476 -14.933  0.50 24.98           C  
ANISOU    6  C  BSER A   1     3399   3488   2604  -1153   -938    702       C  
ATOM      7  O  ASER A   1      -2.957   4.696 -14.446  0.50 25.86           O  
ANISOU    7  O  ASER A   1     3500   3592   2735  -1169   -968    737       O  
ATOM      8  O  BSER A   1      -2.988   4.551 -14.492  0.50 24.74           O  
ANISOU    8  O  BSER A   1     3368   3447   2586  -1178   -975    736       O  
ATOM      9  CB ASER A   1      -2.819   6.777 -17.164  0.50 28.89           C  
ANISOU    9  CB ASER A   1     3908   4027   3042  -1293  -1027    802       C  
ATOM     10  CB BSER A   1      -2.440   6.757 -17.134  0.50 27.08           C  
ANISOU   10  CB BSER A   1     3697   3791   2803  -1274  -1004    766       C  
ATOM     11  OG ASER A   1      -2.052   7.417 -18.170  0.50 31.95           O  
ANISOU   11  OG ASER A   1     4343   4421   3375  -1310  -1009    760       O  
ATOM     12  OG BSER A   1      -3.797   7.000 -16.801  0.50 29.72           O  
ANISOU   12  OG BSER A   1     3934   4150   3207  -1305  -1062    898       O  
ATOM     13  N  AGLY A   2      -1.917   6.679 -14.240  0.50 25.04           N  
ANISOU   13  N  AGLY A   2     3321   3515   2678  -1055   -870    696       N  
ATOM     14  N  BGLY A   2      -1.852   6.467 -14.178  0.50 24.37           N  
ANISOU   14  N  BGLY A   2     3248   3424   2586  -1055   -869    684       N  
ATOM     15  CA AGLY A   2      -2.078   6.745 -12.803  0.50 24.62           C  
ANISOU   15  CA AGLY A   2     3196   3459   2699   -962   -822    700       C  
ATOM     16  CA BGLY A   2      -2.122   6.541 -12.756  0.50 24.27           C  
ANISOU   16  CA BGLY A   2     3159   3411   2651   -967   -827    698       C  
ATOM     17  C  AGLY A   2      -0.786   6.340 -12.129  0.50 23.89           C  
ANISOU   17  C  AGLY A   2     3152   3338   2586   -888   -752    577       C  
ATOM     18  C  BGLY A   2      -0.877   6.134 -12.010  0.50 23.87           C  
ANISOU   18  C  BGLY A   2     3152   3333   2584   -889   -756    578       C  
ATOM     19  O  AGLY A   2      -0.004   5.553 -12.671  0.50 24.05           O  
ANISOU   19  O  AGLY A   2     3266   3335   2538   -916   -748    500       O  
ATOM     20  O  BGLY A   2      -0.206   5.169 -12.398  0.50 24.00           O  
ANISOU   20  O  BGLY A   2     3260   3323   2536   -917   -755    505       O  
ATOM     21  N   PHE A   3      -0.560   6.863 -10.941  1.00 22.93           N  
ANISOU   21  N   PHE A   3     2972   3216   2523   -793   -695    563       N  
ATOM     22  CA  PHE A   3       0.639   6.585 -10.184  1.00 22.04           C  
ANISOU   22  CA  PHE A   3     2893   3080   2403   -721   -633    461       C  
ATOM     23  C   PHE A   3       0.290   6.604  -8.729  1.00 21.78           C  
ANISOU   23  C   PHE A   3     2801   3044   2431   -646   -601    477       C  
ATOM     24  O   PHE A   3      -0.157   7.619  -8.198  1.00 23.62           O  
ANISOU   24  O   PHE A   3     2968   3290   2718   -601   -580    527       O  
ATOM     25  CB  PHE A   3       1.732   7.609 -10.538  1.00 21.01           C  
ANISOU   25  CB  PHE A   3     2768   2952   2263   -688   -591    409       C  
ATOM     26  CG  PHE A   3       3.117   7.084 -10.258  1.00 21.05           C  
ANISOU   26  CG  PHE A   3     2827   2930   2240   -645   -542    307       C  
ATOM     27  CD1 PHE A   3       3.724   6.190 -11.120  1.00 21.40           C  
ANISOU   27  CD1 PHE A   3     2957   2956   2219   -689   -544    255       C  
ATOM     28  CD2 PHE A   3       3.799   7.464  -9.122  1.00 21.44           C  
ANISOU   28  CD2 PHE A   3     2846   2969   2329   -562   -493    269       C  
ATOM     29  CE1 PHE A   3       4.993   5.696 -10.852  1.00 22.14           C  
ANISOU   29  CE1 PHE A   3     3093   3023   2298   -646   -492    174       C  
ATOM     30  CE2 PHE A   3       5.075   6.985  -8.870  1.00 21.61           C  
ANISOU   30  CE2 PHE A   3     2909   2968   2333   -528   -452    189       C  
ATOM     31  CZ  PHE A   3       5.652   6.081  -9.717  1.00 21.71           C  
ANISOU   31  CZ  PHE A   3     2995   2964   2291   -566   -449    146       C  
ATOM     32  N   ARG A   4       0.443   5.457  -8.087  1.00 19.43           N  
ANISOU   32  N   ARG A   4     2533   2727   2124   -633   -595    440       N  
ATOM     33  CA  ARG A   4       0.091   5.280  -6.693  1.00 18.12           C  
ANISOU   33  CA  ARG A   4     2321   2556   2008   -566   -566    454       C  
ATOM     34  C   ARG A   4       1.257   4.818  -5.846  1.00 17.46           C  
ANISOU   34  C   ARG A   4     2271   2449   1914   -506   -517    360       C  
ATOM     35  O   ARG A   4       2.173   4.183  -6.358  1.00 18.03           O  
ANISOU   35  O   ARG A   4     2404   2504   1940   -527   -512    292       O  
ATOM     36  CB  ARG A   4      -0.984   4.179  -6.615  1.00 19.34           C  
ANISOU   36  CB  ARG A   4     2469   2710   2168   -613   -615    515       C  
ATOM     37  CG  ARG A   4      -2.389   4.693  -6.846  1.00 22.46           C  
ANISOU   37  CG  ARG A   4     2796   3131   2608   -646   -656    640       C  
ATOM     38  CD  ARG A   4      -2.962   5.187  -5.525  1.00 25.30           C  
ANISOU   38  CD  ARG A   4     3081   3495   3037   -561   -610    691       C  
ATOM     39  NE  ARG A   4      -4.352   5.630  -5.666  1.00 28.96           N  
ANISOU   39  NE  ARG A   4     3468   3979   3555   -584   -639    826       N  
ATOM     40  CZ  ARG A   4      -5.041   6.254  -4.713  1.00 31.07           C  
ANISOU   40  CZ  ARG A   4     3666   4250   3888   -513   -594    896       C  
ATOM     41  NH1 ARG A   4      -4.479   6.508  -3.538  1.00 31.07           N  
ANISOU   41  NH1 ARG A   4     3673   4234   3900   -420   -523    836       N  
ATOM     42  NH2 ARG A   4      -6.295   6.632  -4.932  1.00 28.97           N  
ANISOU   42  NH2 ARG A   4     3326   4003   3678   -535   -618   1030       N  
ATOM     43  N  ALYS A   5       1.185   5.069  -4.531  0.50 16.58           N  
ANISOU   43  N  ALYS A   5     2120   2334   1844   -433   -480    363       N  
ATOM     44  N  BLYS A   5       1.202   5.059  -4.523  0.50 16.76           N  
ANISOU   44  N  BLYS A   5     2144   2357   1867   -432   -480    362       N  
ATOM     45  CA ALYS A   5       2.185   4.556  -3.613  0.50 16.63           C  
ANISOU   45  CA ALYS A   5     2153   2320   1845   -381   -442    287       C  
ATOM     46  CA BLYS A   5       2.235   4.584  -3.597  0.50 16.99           C  
ANISOU   46  CA BLYS A   5     2199   2365   1890   -379   -441    285       C  
ATOM     47  C  ALYS A   5       1.841   3.080  -3.508  0.50 17.04           C  
ANISOU   47  C  ALYS A   5     2227   2362   1884   -413   -467    289       C  
ATOM     48  C  BLYS A   5       1.980   3.098  -3.369  0.50 17.63           C  
ANISOU   48  C  BLYS A   5     2302   2435   1960   -403   -460    280       C  
ATOM     49  O  ALYS A   5       0.747   2.726  -3.077  0.50 17.39           O  
ANISOU   49  O  ALYS A   5     2236   2416   1956   -420   -489    356       O  
ATOM     50  O  BLYS A   5       1.203   2.711  -2.496  0.50 18.57           O  
ANISOU   50  O  BLYS A   5     2387   2557   2110   -380   -461    322       O  
ATOM     51  CB ALYS A   5       2.120   5.253  -2.246  0.50 17.92           C  
ANISOU   51  CB ALYS A   5     2280   2480   2048   -301   -401    295       C  
ATOM     52  CB BLYS A   5       2.196   5.363  -2.273  0.50 18.19           C  
ANISOU   52  CB BLYS A   5     2315   2515   2083   -300   -399    293       C  
ATOM     53  CG ALYS A   5       3.300   4.911  -1.342  0.50 21.29           C  
ANISOU   53  CG ALYS A   5     2735   2887   2467   -254   -368    217       C  
ATOM     54  CG BLYS A   5       3.332   5.005  -1.326  0.50 21.43           C  
ANISOU   54  CG BLYS A   5     2752   2905   2486   -252   -367    218       C  
ATOM     55  CD ALYS A   5       4.637   5.388  -1.894  0.50 24.62           C  
ANISOU   55  CD ALYS A   5     3187   3300   2866   -257   -355    155       C  
ATOM     56  CD BLYS A   5       4.694   5.391  -1.868  0.50 24.70           C  
ANISOU   56  CD BLYS A   5     3199   3310   2877   -255   -354    153       C  
ATOM     57  CE ALYS A   5       4.810   6.884  -1.795  0.50 27.77           C  
ANISOU   57  CE ALYS A   5     3569   3701   3282   -227   -339    162       C  
ATOM     58  CE BLYS A   5       4.925   6.879  -1.800  0.50 27.68           C  
ANISOU   58  CE BLYS A   5     3559   3690   3270   -227   -339    160       C  
ATOM     59  NZ ALYS A   5       4.611   7.386  -0.415  0.50 29.14           N  
ANISOU   59  NZ ALYS A   5     3728   3864   3481   -165   -312    172       N  
ATOM     60  NZ BLYS A   5       4.633   7.433  -0.457  0.50 28.93           N  
ANISOU   60  NZ BLYS A   5     3701   3837   3454   -165   -312    172       N  
ATOM     61  N   MET A   6       2.663   2.273  -4.148  1.00 17.01           N  
ANISOU   61  N   MET A   6     2284   2341   1838   -444   -468    227       N  
ATOM     62  CA  MET A   6       2.427   0.855  -4.239  1.00 17.12           C  
ANISOU   62  CA  MET A   6     2335   2339   1832   -482   -492    221       C  
ATOM     63  C   MET A   6       3.367   0.015  -3.454  1.00 15.93           C  
ANISOU   63  C   MET A   6     2208   2164   1681   -440   -454    155       C  
ATOM     64  O   MET A   6       4.570   0.202  -3.547  1.00 16.36           O  
ANISOU   64  O   MET A   6     2287   2206   1722   -415   -417     95       O  
ATOM     65  CB  MET A   6       2.580   0.517  -5.725  1.00 19.42           C  
ANISOU   65  CB  MET A   6     2693   2619   2066   -561   -522    206       C  
ATOM     66  CG  MET A   6       2.137  -0.836  -6.077  1.00 24.58           C  
ANISOU   66  CG  MET A   6     3399   3251   2691   -619   -558    208       C  
ATOM     67  SD  MET A   6       2.195  -0.979  -7.868  1.00 31.98           S  
ANISOU   67  SD  MET A   6     4425   4174   3551   -716   -596    200       S  
ATOM     68  CE  MET A   6       0.949   0.182  -8.339  1.00 27.76           C  
ANISOU   68  CE  MET A   6     3824   3682   3041   -757   -652    303       C  
ATOM     69  N   ALA A   7       2.820  -0.956  -2.733  1.00 14.89           N  
ANISOU   69  N   ALA A   7     2066   2027   1567   -436   -466    174       N  
ATOM     70  CA  ALA A   7       3.639  -1.900  -1.989  1.00 15.29           C  
ANISOU   70  CA  ALA A   7     2137   2054   1620   -401   -434    119       C  
ATOM     71  C   ALA A   7       3.744  -3.190  -2.803  1.00 15.57           C  
ANISOU   71  C   ALA A   7     2240   2060   1616   -459   -451     93       C  
ATOM     72  O   ALA A   7       2.963  -3.405  -3.734  1.00 16.04           O  
ANISOU   72  O   ALA A   7     2328   2119   1649   -528   -498    128       O  
ATOM     73  CB  ALA A   7       3.006  -2.185  -0.630  1.00 15.59           C  
ANISOU   73  CB  ALA A   7     2122   2101   1700   -356   -430    154       C  
ATOM     74  N   PHE A   8       4.742  -4.010  -2.521  1.00 15.58           N  
ANISOU   74  N   PHE A   8     2275   2033   1611   -435   -413     35       N  
ATOM     75  CA  PHE A   8       4.868  -5.305  -3.172  1.00 16.87           C  
ANISOU   75  CA  PHE A   8     2512   2159   1740   -482   -419      8       C  
ATOM     76  C   PHE A   8       3.750  -6.202  -2.661  1.00 16.69           C  
ANISOU   76  C   PHE A   8     2471   2136   1735   -506   -463     55       C  
ATOM     77  O   PHE A   8       3.298  -6.088  -1.511  1.00 16.04           O  
ANISOU   77  O   PHE A   8     2320   2076   1699   -462   -464     90       O  
ATOM     78  CB  PHE A   8       6.222  -5.940  -2.834  1.00 17.33           C  
ANISOU   78  CB  PHE A   8     2598   2187   1802   -438   -357    -56       C  
ATOM     79  CG  PHE A   8       7.358  -5.313  -3.588  1.00 19.06           C  
ANISOU   79  CG  PHE A   8     2847   2396   1998   -426   -313    -96       C  
ATOM     80  CD1 PHE A   8       7.607  -5.651  -4.907  1.00 20.90           C  
ANISOU   80  CD1 PHE A   8     3166   2600   2176   -474   -304   -122       C  
ATOM     81  CD2 PHE A   8       8.164  -4.366  -2.990  1.00 20.60           C  
ANISOU   81  CD2 PHE A   8     2990   2610   2225   -369   -282   -105       C  
ATOM     82  CE1 PHE A   8       8.640  -5.049  -5.607  1.00 22.00           C  
ANISOU   82  CE1 PHE A   8     3331   2732   2298   -458   -259   -152       C  
ATOM     83  CE2 PHE A   8       9.209  -3.787  -3.685  1.00 21.94           C  
ANISOU   83  CE2 PHE A   8     3182   2773   2381   -358   -244   -134       C  
ATOM     84  CZ  PHE A   8       9.433  -4.123  -4.991  1.00 22.08           C  
ANISOU   84  CZ  PHE A   8     3277   2764   2349   -400   -230   -155       C  
ATOM     85  N   PRO A   9       3.322  -7.176  -3.489  1.00 17.15           N  
ANISOU   85  N   PRO A   9     2598   2165   1755   -577   -500     58       N  
ATOM     86  CA  PRO A   9       2.348  -8.173  -3.002  1.00 17.33           C  
ANISOU   86  CA  PRO A   9     2606   2180   1797   -604   -544    103       C  
ATOM     87  C   PRO A   9       2.939  -8.881  -1.771  1.00 17.30           C  
ANISOU   87  C   PRO A   9     2575   2167   1833   -537   -498     72       C  
ATOM     88  O   PRO A   9       4.125  -9.203  -1.771  1.00 19.22           O  
ANISOU   88  O   PRO A   9     2854   2383   2066   -505   -442      8       O  
ATOM     89  CB  PRO A   9       2.198  -9.124  -4.195  1.00 19.02           C  
ANISOU   89  CB  PRO A   9     2926   2349   1951   -690   -579     86       C  
ATOM     90  CG  PRO A   9       2.667  -8.338  -5.372  1.00 19.72           C  
ANISOU   90  CG  PRO A   9     3068   2437   1989   -719   -570     60       C  
ATOM     91  CD  PRO A   9       3.768  -7.478  -4.860  1.00 17.41           C  
ANISOU   91  CD  PRO A   9     2731   2162   1721   -635   -498     18       C  
ATOM     92  N   SER A  10       2.170  -8.982  -0.714  1.00 15.92           N  
ANISOU   92  N   SER A  10     2329   2016   1705   -510   -516    125       N  
ATOM     93  CA  SER A  10       2.701  -9.448   0.569  1.00 15.16           C  
ANISOU   93  CA  SER A  10     2194   1919   1648   -441   -474    103       C  
ATOM     94  C   SER A  10       2.612 -10.944   0.842  1.00 15.12           C  
ANISOU   94  C   SER A  10     2215   1881   1649   -458   -482     97       C  
ATOM     95  O   SER A  10       3.100 -11.378   1.869  1.00 14.73           O  
ANISOU   95  O   SER A  10     2135   1831   1632   -404   -448     80       O  
ATOM     96  CB  SER A  10       2.029  -8.690   1.705  1.00 15.91           C  
ANISOU   96  CB  SER A  10     2200   2056   1788   -388   -475    160       C  
ATOM     97  OG  SER A  10       0.623  -8.864   1.658  1.00 17.96           O  
ANISOU   97  OG  SER A  10     2428   2330   2066   -426   -530    242       O  
ATOM     98  N   GLY A  11       2.001 -11.708  -0.041  1.00 15.29           N  
ANISOU   98  N   GLY A  11     2295   1874   1641   -534   -530    111       N  
ATOM     99  CA  GLY A  11       1.797 -13.135   0.179  1.00 15.09           C  
ANISOU   99  CA  GLY A  11     2298   1812   1622   -558   -546    111       C  
ATOM    100  C   GLY A  11       3.008 -13.943   0.596  1.00 14.62           C  
ANISOU  100  C   GLY A  11     2268   1718   1570   -512   -480     44       C  
ATOM    101  O   GLY A  11       2.943 -14.731   1.548  1.00 15.34           O  
ANISOU  101  O   GLY A  11     2323   1805   1699   -483   -473     55       O  
ATOM    102  N   LYS A  12       4.126 -13.735  -0.106  1.00 13.99           N  
ANISOU  102  N   LYS A  12     2248   1612   1455   -504   -428    -20       N  
ATOM    103  CA  LYS A  12       5.345 -14.487   0.193  1.00 14.02           C  
ANISOU  103  CA  LYS A  12     2278   1579   1471   -461   -359    -75       C  
ATOM    104  C   LYS A  12       5.831 -14.217   1.613  1.00 14.16           C  
ANISOU  104  C   LYS A  12     2202   1631   1547   -382   -326    -68       C  
ATOM    105  O   LYS A  12       6.375 -15.110   2.261  1.00 14.81           O  
ANISOU  105  O   LYS A  12     2276   1691   1658   -351   -292    -82       O  
ATOM    106  CB  LYS A  12       6.449 -14.195  -0.821  1.00 15.54           C  
ANISOU  106  CB  LYS A  12     2543   1739   1622   -460   -303   -132       C  
ATOM    107  CG  LYS A  12       6.209 -14.833  -2.180  1.00 19.84           C  
ANISOU  107  CG  LYS A  12     3209   2229   2099   -536   -318   -155       C  
ATOM    108  CD  LYS A  12       7.166 -14.268  -3.223  1.00 25.38           C  
ANISOU  108  CD  LYS A  12     3976   2910   2756   -533   -264   -200       C  
ATOM    109  CE  LYS A  12       6.905 -14.864  -4.589  1.00 30.94           C  
ANISOU  109  CE  LYS A  12     4817   3558   3382   -610   -278   -224       C  
ATOM    110  NZ  LYS A  12       7.019 -16.342  -4.559  1.00 34.47           N  
ANISOU  110  NZ  LYS A  12     5337   3937   3822   -623   -255   -248       N  
ATOM    111  N   VAL A  13       5.605 -12.996   2.114  1.00 13.22           N  
ANISOU  111  N   VAL A  13     2016   1563   1443   -351   -337    -41       N  
ATOM    112  CA  VAL A  13       6.032 -12.646   3.468  1.00 12.21           C  
ANISOU  112  CA  VAL A  13     1813   1466   1360   -282   -311    -33       C  
ATOM    113  C   VAL A  13       5.000 -13.074   4.500  1.00 11.66           C  
ANISOU  113  C   VAL A  13     1687   1420   1324   -272   -345     20       C  
ATOM    114  O   VAL A  13       5.364 -13.520   5.588  1.00 11.73           O  
ANISOU  114  O   VAL A  13     1657   1433   1367   -227   -324     21       O  
ATOM    115  CB  VAL A  13       6.355 -11.145   3.551  1.00 13.09           C  
ANISOU  115  CB  VAL A  13     1893   1613   1468   -253   -301    -35       C  
ATOM    116  CG1 VAL A  13       6.822 -10.761   4.950  1.00 14.14           C  
ANISOU  116  CG1 VAL A  13     1965   1771   1637   -189   -280    -28       C  
ATOM    117  CG2 VAL A  13       7.411 -10.784   2.519  1.00 14.34           C  
ANISOU  117  CG2 VAL A  13     2103   1748   1597   -262   -265    -82       C  
ATOM    118  N   GLU A  14       3.701 -13.021   4.159  1.00 11.62           N  
ANISOU  118  N   GLU A  14     1675   1426   1312   -315   -400     72       N  
ATOM    119  CA  GLU A  14       2.641 -13.473   5.068  1.00 11.63           C  
ANISOU  119  CA  GLU A  14     1621   1448   1350   -306   -432    135       C  
ATOM    120  C   GLU A  14       2.876 -14.916   5.521  1.00 12.71           C  
ANISOU  120  C   GLU A  14     1768   1554   1508   -305   -424    123       C  
ATOM    121  O   GLU A  14       2.716 -15.224   6.703  1.00 13.03           O  
ANISOU  121  O   GLU A  14     1752   1613   1585   -261   -416    149       O  
ATOM    122  CB  GLU A  14       1.275 -13.399   4.373  1.00 12.59           C  
ANISOU  122  CB  GLU A  14     1742   1577   1464   -368   -496    200       C  
ATOM    123  CG  GLU A  14       0.756 -11.988   4.211  1.00 15.46           C  
ANISOU  123  CG  GLU A  14     2071   1980   1825   -359   -505    238       C  
ATOM    124  CD  GLU A  14      -0.445 -11.950   3.292  1.00 18.75           C  
ANISOU  124  CD  GLU A  14     2494   2399   2232   -433   -572    303       C  
ATOM    125  OE1 GLU A  14      -1.417 -12.694   3.553  1.00 21.44           O  
ANISOU  125  OE1 GLU A  14     2807   2738   2599   -459   -616    368       O  
ATOM    126  OE2 GLU A  14      -0.390 -11.204   2.289  1.00 19.65           O  
ANISOU  126  OE2 GLU A  14     2641   2514   2313   -469   -584    294       O  
ATOM    127  N   GLY A  15       3.357 -15.745   4.598  1.00 12.90           N  
ANISOU  127  N   GLY A  15     1868   1528   1505   -348   -418     79       N  
ATOM    128  CA  GLY A  15       3.649 -17.145   4.878  1.00 12.73           C  
ANISOU  128  CA  GLY A  15     1869   1467   1502   -351   -405     63       C  
ATOM    129  C   GLY A  15       4.818 -17.392   5.810  1.00 12.45           C  
ANISOU  129  C   GLY A  15     1802   1431   1499   -284   -343     31       C  
ATOM    130  O   GLY A  15       5.068 -18.532   6.200  1.00 13.52           O  
ANISOU  130  O   GLY A  15     1941   1536   1659   -278   -328     25       O  
ATOM    131  N   CYS A  16       5.547 -16.341   6.161  1.00 11.59           N  
ANISOU  131  N   CYS A  16     1662   1350   1391   -239   -310     14       N  
ATOM    132  CA  CYS A  16       6.690 -16.411   7.064  1.00 11.47           C  
ANISOU  132  CA  CYS A  16     1612   1338   1407   -181   -261     -7       C  
ATOM    133  C   CYS A  16       6.412 -15.838   8.439  1.00 11.91           C  
ANISOU  133  C   CYS A  16     1592   1443   1489   -133   -270     29       C  
ATOM    134  O   CYS A  16       7.299 -15.910   9.283  1.00 12.77           O  
ANISOU  134  O   CYS A  16     1672   1557   1622    -92   -239     20       O  
ATOM    135  CB  CYS A  16       7.899 -15.722   6.446  1.00 12.44           C  
ANISOU  135  CB  CYS A  16     1764   1450   1513   -169   -216    -51       C  
ATOM    136  SG  CYS A  16       8.356 -16.342   4.810  1.00 15.98           S  
ANISOU  136  SG  CYS A  16     2316   1834   1921   -216   -188    -97       S  
ATOM    137  N   MET A  17       5.240 -15.226   8.673  1.00 11.61           N  
ANISOU  137  N   MET A  17     1526   1440   1446   -137   -308     74       N  
ATOM    138  CA  MET A  17       5.017 -14.567   9.953  1.00 12.03           C  
ANISOU  138  CA  MET A  17     1522   1534   1515    -85   -305    105       C  
ATOM    139  C   MET A  17       4.535 -15.499  11.022  1.00 12.33           C  
ANISOU  139  C   MET A  17     1518   1579   1587    -65   -311    143       C  
ATOM    140  O   MET A  17       3.618 -16.266  10.806  1.00 12.97           O  
ANISOU  140  O   MET A  17     1596   1653   1680    -94   -341    178       O  
ATOM    141  CB  MET A  17       4.077 -13.372   9.816  1.00 12.21           C  
ANISOU  141  CB  MET A  17     1531   1588   1521    -85   -326    140       C  
ATOM    142  CG  MET A  17       4.535 -12.353   8.787  1.00 13.24           C  
ANISOU  142  CG  MET A  17     1697   1714   1618   -104   -321    106       C  
ATOM    143  SD  MET A  17       6.217 -11.703   9.005  1.00 14.39           S  
ANISOU  143  SD  MET A  17     1856   1854   1757    -71   -278     48       S  
ATOM    144  CE  MET A  17       6.158 -11.181  10.754  1.00 15.96           C  
ANISOU  144  CE  MET A  17     2009   2086   1971    -10   -269     74       C  
ATOM    145  N   VAL A  18       5.186 -15.438  12.176  1.00 11.86           N  
ANISOU  145  N   VAL A  18     1429   1536   1543    -18   -287    140       N  
ATOM    146  CA  VAL A  18       4.849 -16.234  13.343  1.00 12.74           C  
ANISOU  146  CA  VAL A  18     1498   1659   1684      9   -289    176       C  
ATOM    147  C   VAL A  18       4.775 -15.312  14.559  1.00 12.62           C  
ANISOU  147  C   VAL A  18     1456   1680   1660     60   -278    197       C  
ATOM    148  O   VAL A  18       5.220 -14.160  14.518  1.00 12.38           O  
ANISOU  148  O   VAL A  18     1443   1657   1602     72   -267    174       O  
ATOM    149  CB  VAL A  18       5.882 -17.373  13.576  1.00 13.97           C  
ANISOU  149  CB  VAL A  18     1652   1787   1868     11   -267    150       C  
ATOM    150  CG1 VAL A  18       5.917 -18.341  12.404  1.00 14.87           C  
ANISOU  150  CG1 VAL A  18     1808   1855   1986    -36   -270    128       C  
ATOM    151  CG2 VAL A  18       7.262 -16.802  13.868  1.00 13.93           C  
ANISOU  151  CG2 VAL A  18     1651   1782   1858     34   -238    115       C  
ATOM    152  N   GLN A  19       4.185 -15.818  15.633  1.00 12.65           N  
ANISOU  152  N   GLN A  19     1422   1701   1683     88   -280    241       N  
ATOM    153  CA  GLN A  19       4.107 -15.113  16.896  1.00 13.10           C  
ANISOU  153  CA  GLN A  19     1465   1786   1726    138   -264    262       C  
ATOM    154  C   GLN A  19       5.221 -15.641  17.802  1.00 12.93           C  
ANISOU  154  C   GLN A  19     1436   1763   1715    154   -252    242       C  
ATOM    155  O   GLN A  19       5.433 -16.850  17.868  1.00 12.86           O  
ANISOU  155  O   GLN A  19     1405   1740   1740    142   -255    247       O  
ATOM    156  CB  GLN A  19       2.735 -15.376  17.520  1.00 14.90           C  
ANISOU  156  CB  GLN A  19     1656   2034   1970    161   -268    332       C  
ATOM    157  CG  GLN A  19       2.552 -14.741  18.881  1.00 18.61           C  
ANISOU  157  CG  GLN A  19     2122   2528   2420    218   -243    357       C  
ATOM    158  CD  GLN A  19       1.293 -15.237  19.530  1.00 24.25           C  
ANISOU  158  CD  GLN A  19     2795   3260   3160    245   -240    433       C  
ATOM    159  OE1 GLN A  19       1.285 -16.257  20.224  1.00 26.10           O  
ANISOU  159  OE1 GLN A  19     2999   3499   3420    254   -242    455       O  
ATOM    160  NE2 GLN A  19       0.206 -14.527  19.326  1.00 25.55           N  
ANISOU  160  NE2 GLN A  19     2951   3434   3321    261   -232    481       N  
ATOM    161  N   VAL A  20       5.940 -14.742  18.500  1.00 12.43           N  
ANISOU  161  N   VAL A  20     1391   1710   1624    177   -242    225       N  
ATOM    162  CA  VAL A  20       6.962 -15.171  19.450  1.00 13.22           C  
ANISOU  162  CA  VAL A  20     1480   1811   1733    187   -239    219       C  
ATOM    163  C   VAL A  20       6.631 -14.580  20.807  1.00 13.82           C  
ANISOU  163  C   VAL A  20     1564   1910   1775    226   -234    245       C  
ATOM    164  O   VAL A  20       6.435 -13.367  20.921  1.00 14.21           O  
ANISOU  164  O   VAL A  20     1651   1964   1783    241   -228    238       O  
ATOM    165  CB  VAL A  20       8.405 -14.806  19.036  1.00 13.47           C  
ANISOU  165  CB  VAL A  20     1530   1826   1763    167   -238    177       C  
ATOM    166  CG1 VAL A  20       9.408 -15.330  20.066  1.00 14.22           C  
ANISOU  166  CG1 VAL A  20     1603   1924   1876    173   -241    188       C  
ATOM    167  CG2 VAL A  20       8.731 -15.348  17.650  1.00 13.91           C  
ANISOU  167  CG2 VAL A  20     1588   1853   1843    134   -231    150       C  
ATOM    168  N   THR A  21       6.537 -15.429  21.823  1.00 14.34           N  
ANISOU  168  N   THR A  21     1601   1987   1858    244   -234    277       N  
ATOM    169  CA  THR A  21       6.264 -14.970  23.174  1.00 15.62           C  
ANISOU  169  CA  THR A  21     1782   2169   1984    281   -225    302       C  
ATOM    170  C   THR A  21       7.382 -15.417  24.085  1.00 16.58           C  
ANISOU  170  C   THR A  21     1897   2293   2108    274   -239    300       C  
ATOM    171  O   THR A  21       7.797 -16.567  24.035  1.00 16.63           O  
ANISOU  171  O   THR A  21     1860   2296   2163    258   -245    309       O  
ATOM    172  CB  THR A  21       4.920 -15.534  23.681  1.00 18.06           C  
ANISOU  172  CB  THR A  21     2060   2495   2307    314   -211    358       C  
ATOM    173  OG1 THR A  21       3.855 -15.130  22.823  1.00 19.40           O  
ANISOU  173  OG1 THR A  21     2226   2663   2481    316   -204    375       O  
ATOM    174  CG2 THR A  21       4.614 -15.109  25.110  1.00 19.50           C  
ANISOU  174  CG2 THR A  21     2269   2694   2447    358   -192    387       C  
ATOM    175  N   CYS A  22       7.882 -14.511  24.909  1.00 17.62           N  
ANISOU  175  N   CYS A  22     2077   2429   2189    281   -245    292       N  
ATOM    176  CA  CYS A  22       8.866 -14.862  25.915  1.00 19.68           C  
ANISOU  176  CA  CYS A  22     2335   2695   2447    270   -266    302       C  
ATOM    177  C   CYS A  22       8.353 -14.192  27.181  1.00 22.21           C  
ANISOU  177  C   CYS A  22     2710   3026   2700    302   -258    320       C  
ATOM    178  O   CYS A  22       8.185 -12.976  27.221  1.00 22.29           O  
ANISOU  178  O   CYS A  22     2785   3027   2655    312   -250    301       O  
ATOM    179  CB  CYS A  22      10.273 -14.403  25.535  1.00 19.81           C  
ANISOU  179  CB  CYS A  22     2364   2697   2468    230   -292    274       C  
ATOM    180  SG  CYS A  22      11.574 -15.049  26.614  1.00 26.04           S  
ANISOU  180  SG  CYS A  22     3129   3491   3273    205   -326    304       S  
ATOM    181  N   GLY A  23       7.977 -15.014  28.151  1.00 24.20           N  
ANISOU  181  N   GLY A  23     2938   3296   2959    323   -252    360       N  
ATOM    182  CA  GLY A  23       7.401 -14.541  29.403  1.00 25.86           C  
ANISOU  182  CA  GLY A  23     3204   3516   3105    360   -235    383       C  
ATOM    183  C   GLY A  23       6.078 -13.859  29.141  1.00 27.25           C  
ANISOU  183  C   GLY A  23     3405   3689   3258    405   -191    393       C  
ATOM    184  O   GLY A  23       5.164 -14.465  28.577  1.00 28.42           O  
ANISOU  184  O   GLY A  23     3496   3845   3455    421   -173    419       O  
ATOM    185  N   THR A  24       6.013 -12.564  29.424  1.00 27.33           N  
ANISOU  185  N   THR A  24     3500   3684   3199    420   -176    372       N  
ATOM    186  CA  THR A  24       4.800 -11.787  29.185  1.00 27.90           C  
ANISOU  186  CA  THR A  24     3600   3750   3251    468   -126    387       C  
ATOM    187  C   THR A  24       4.849 -10.946  27.898  1.00 26.48           C  
ANISOU  187  C   THR A  24     3425   3554   3082    448   -129    352       C  
ATOM    188  O   THR A  24       3.899 -10.223  27.618  1.00 27.56           O  
ANISOU  188  O   THR A  24     3580   3683   3207    484    -90    367       O  
ATOM    189  CB  THR A  24       4.514 -10.899  30.395  1.00 31.42           C  
ANISOU  189  CB  THR A  24     4144   4183   3611    508    -92    394       C  
ATOM    190  OG1 THR A  24       5.534  -9.903  30.499  1.00 33.89           O  
ANISOU  190  OG1 THR A  24     4539   4472   3867    473   -122    343       O  
ATOM    191  CG2 THR A  24       4.440 -11.691  31.681  1.00 32.45           C  
ANISOU  191  CG2 THR A  24     4277   4329   3722    528    -86    431       C  
ATOM    192  N   THR A  25       5.938 -11.023  27.128  1.00 24.11           N  
ANISOU  192  N   THR A  25     3104   3248   2808    395   -172    312       N  
ATOM    193  CA  THR A  25       6.082 -10.214  25.922  1.00 22.53           C  
ANISOU  193  CA  THR A  25     2916   3033   2612    375   -177    277       C  
ATOM    194  C   THR A  25       5.755 -11.009  24.671  1.00 21.00           C  
ANISOU  194  C   THR A  25     2647   2846   2487    354   -183    281       C  
ATOM    195  O   THR A  25       6.304 -12.083  24.490  1.00 21.49           O  
ANISOU  195  O   THR A  25     2662   2913   2590    329   -204    281       O  
ATOM    196  CB  THR A  25       7.503  -9.662  25.850  1.00 23.52           C  
ANISOU  196  CB  THR A  25     3080   3144   2715    330   -217    233       C  
ATOM    197  OG1 THR A  25       7.752  -8.858  27.011  1.00 24.80           O  
ANISOU  197  OG1 THR A  25     3325   3293   2804    341   -218    229       O  
ATOM    198  CG2 THR A  25       7.756  -8.862  24.584  1.00 23.98           C  
ANISOU  198  CG2 THR A  25     3143   3188   2782    307   -223    198       C  
ATOM    199  N   THR A  26       4.880 -10.486  23.817  1.00 19.91           N  
ANISOU  199  N   THR A  26     2504   2704   2356    365   -163    289       N  
ATOM    200  CA  THR A  26       4.539 -11.124  22.554  1.00 19.02           C  
ANISOU  200  CA  THR A  26     2337   2594   2297    337   -176    293       C  
ATOM    201  C   THR A  26       4.814 -10.164  21.401  1.00 17.49           C  
ANISOU  201  C   THR A  26     2166   2386   2093    312   -182    256       C  
ATOM    202  O   THR A  26       4.376  -9.013  21.413  1.00 18.04           O  
ANISOU  202  O   THR A  26     2275   2450   2130    334   -162    257       O  
ATOM    203  CB  THR A  26       3.074 -11.584  22.541  1.00 20.95           C  
ANISOU  203  CB  THR A  26     2539   2850   2569    365   -155    355       C  
ATOM    204  OG1 THR A  26       2.900 -12.636  23.488  1.00 22.53           O  
ANISOU  204  OG1 THR A  26     2709   3065   2788    383   -153    390       O  
ATOM    205  CG2 THR A  26       2.634 -12.069  21.182  1.00 21.72           C  
ANISOU  205  CG2 THR A  26     2595   2945   2711    327   -176    361       C  
ATOM    206  N   LEU A  27       5.539 -10.637  20.411  1.00 15.55           N  
ANISOU  206  N   LEU A  27     1900   2133   1877    268   -206    225       N  
ATOM    207  CA  LEU A  27       5.787  -9.858  19.200  1.00 14.34           C  
ANISOU  207  CA  LEU A  27     1763   1967   1717    241   -212    193       C  
ATOM    208  C   LEU A  27       5.841 -10.794  17.990  1.00 13.54           C  
ANISOU  208  C   LEU A  27     1629   1858   1657    201   -227    183       C  
ATOM    209  O   LEU A  27       5.400 -11.943  18.087  1.00 13.86           O  
ANISOU  209  O   LEU A  27     1637   1902   1728    199   -230    208       O  
ATOM    210  CB  LEU A  27       7.007  -8.909  19.344  1.00 13.99           C  
ANISOU  210  CB  LEU A  27     1762   1911   1642    230   -222    151       C  
ATOM    211  CG  LEU A  27       8.263  -9.503  19.968  1.00 14.11           C  
ANISOU  211  CG  LEU A  27     1771   1923   1666    215   -240    137       C  
ATOM    212  CD1 LEU A  27       8.801 -10.671  19.161  1.00 14.29           C  
ANISOU  212  CD1 LEU A  27     1749   1939   1740    186   -246    130       C  
ATOM    213  CD2 LEU A  27       9.349  -8.450  20.127  1.00 14.70           C  
ANISOU  213  CD2 LEU A  27     1888   1986   1711    199   -258    109       C  
ATOM    214  N   ASN A  28       6.313 -10.302  16.845  1.00 12.24           N  
ANISOU  214  N   ASN A  28     1481   1682   1488    171   -233    150       N  
ATOM    215  CA  ASN A  28       6.346 -11.091  15.631  1.00 11.92           C  
ANISOU  215  CA  ASN A  28     1428   1628   1474    132   -242    138       C  
ATOM    216  C   ASN A  28       7.714 -11.653  15.355  1.00 11.52           C  
ANISOU  216  C   ASN A  28     1380   1558   1440    112   -240    101       C  
ATOM    217  O   ASN A  28       8.725 -11.066  15.710  1.00 11.85           O  
ANISOU  217  O   ASN A  28     1433   1598   1471    117   -238     82       O  
ATOM    218  CB  ASN A  28       5.884 -10.259  14.427  1.00 13.05           C  
ANISOU  218  CB  ASN A  28     1590   1768   1601    110   -247    131       C  
ATOM    219  CG  ASN A  28       4.569  -9.595  14.702  1.00 15.18           C  
ANISOU  219  CG  ASN A  28     1851   2055   1862    134   -244    178       C  
ATOM    220  OD1 ASN A  28       3.512 -10.223  14.621  1.00 15.52           O  
ANISOU  220  OD1 ASN A  28     1866   2104   1926    130   -252    224       O  
ATOM    221  ND2 ASN A  28       4.620  -8.331  15.068  1.00 15.66           N  
ANISOU  221  ND2 ASN A  28     1936   2120   1895    160   -230    173       N  
ATOM    222  N   GLY A  29       7.713 -12.775  14.686  1.00 11.02           N  
ANISOU  222  N   GLY A  29     1306   1477   1402     88   -239     97       N  
ATOM    223  CA  GLY A  29       8.925 -13.411  14.219  1.00 11.06           C  
ANISOU  223  CA  GLY A  29     1316   1457   1430     71   -224     68       C  
ATOM    224  C   GLY A  29       8.812 -13.718  12.738  1.00 11.20           C  
ANISOU  224  C   GLY A  29     1363   1448   1445     35   -219     46       C  
ATOM    225  O   GLY A  29       7.714 -13.803  12.179  1.00 11.95           O  
ANISOU  225  O   GLY A  29     1468   1545   1528     15   -237     59       O  
ATOM    226  N   LEU A  30       9.956 -13.877  12.090  1.00 10.90           N  
ANISOU  226  N   LEU A  30     1341   1384   1416     24   -195     16       N  
ATOM    227  CA  LEU A  30      10.046 -14.190  10.667  1.00 10.82           C  
ANISOU  227  CA  LEU A  30     1373   1342   1396     -8   -180    -11       C  
ATOM    228  C   LEU A  30      10.616 -15.606  10.560  1.00 10.79           C  
ANISOU  228  C   LEU A  30     1373   1300   1426    -11   -150    -17       C  
ATOM    229  O   LEU A  30      11.740 -15.840  11.002  1.00 11.77           O  
ANISOU  229  O   LEU A  30     1475   1416   1582     10   -121    -15       O  
ATOM    230  CB  LEU A  30      10.994 -13.195   9.995  1.00 10.42           C  
ANISOU  230  CB  LEU A  30     1341   1286   1331    -10   -162    -37       C  
ATOM    231  CG  LEU A  30      11.086 -13.328   8.477  1.00 11.21           C  
ANISOU  231  CG  LEU A  30     1495   1355   1410    -42   -143    -65       C  
ATOM    232  CD1 LEU A  30       9.784 -12.894   7.816  1.00 12.16           C  
ANISOU  232  CD1 LEU A  30     1640   1487   1493    -73   -180    -60       C  
ATOM    233  CD2 LEU A  30      12.245 -12.507   7.952  1.00 12.12           C  
ANISOU  233  CD2 LEU A  30     1619   1464   1524    -34   -116    -84       C  
ATOM    234  N   TRP A  31       9.866 -16.535   9.979  1.00 10.46           N  
ANISOU  234  N   TRP A  31     1360   1233   1380    -39   -156    -18       N  
ATOM    235  CA  TRP A  31      10.255 -17.943   9.908  1.00 10.74           C  
ANISOU  235  CA  TRP A  31     1406   1227   1448    -42   -127    -22       C  
ATOM    236  C   TRP A  31      10.711 -18.287   8.502  1.00 11.18           C  
ANISOU  236  C   TRP A  31     1535   1230   1484    -69    -91    -60       C  
ATOM    237  O   TRP A  31       9.923 -18.273   7.553  1.00 11.15           O  
ANISOU  237  O   TRP A  31     1585   1212   1440   -111   -114    -72       O  
ATOM    238  CB  TRP A  31       9.054 -18.777  10.353  1.00 11.08           C  
ANISOU  238  CB  TRP A  31     1435   1275   1500    -56   -164      7       C  
ATOM    239  CG  TRP A  31       9.218 -20.262  10.334  1.00 11.19           C  
ANISOU  239  CG  TRP A  31     1463   1244   1545    -63   -142      6       C  
ATOM    240  CD1 TRP A  31      10.371 -20.974  10.511  1.00 11.87           C  
ANISOU  240  CD1 TRP A  31     1544   1298   1669    -40    -90     -3       C  
ATOM    241  CD2 TRP A  31       8.153 -21.221  10.295  1.00 11.18           C  
ANISOU  241  CD2 TRP A  31     1473   1227   1548    -93   -176     27       C  
ATOM    242  NE1 TRP A  31      10.090 -22.323  10.513  1.00 11.94           N  
ANISOU  242  NE1 TRP A  31     1567   1268   1702    -52    -83      3       N  
ATOM    243  CE2 TRP A  31       8.734 -22.499  10.412  1.00 11.98           C  
ANISOU  243  CE2 TRP A  31     1583   1284   1687    -86   -139     21       C  
ATOM    244  CE3 TRP A  31       6.763 -21.123  10.121  1.00 11.96           C  
ANISOU  244  CE3 TRP A  31     1574   1343   1627   -126   -234     56       C  
ATOM    245  CZ2 TRP A  31       7.976 -23.673  10.353  1.00 12.16           C  
ANISOU  245  CZ2 TRP A  31     1623   1274   1721   -115   -162     35       C  
ATOM    246  CZ3 TRP A  31       6.013 -22.284  10.075  1.00 12.27           C  
ANISOU  246  CZ3 TRP A  31     1626   1355   1682   -157   -261     78       C  
ATOM    247  CH2 TRP A  31       6.621 -23.544  10.169  1.00 12.25           C  
ANISOU  247  CH2 TRP A  31     1640   1305   1711   -153   -226     63       C  
ATOM    248  N   LEU A  32      12.025 -18.505   8.356  1.00 11.11           N  
ANISOU  248  N   LEU A  32     1528   1193   1501    -46    -33    -72       N  
ATOM    249  CA  LEU A  32      12.646 -18.808   7.060  1.00 12.05           C  
ANISOU  249  CA  LEU A  32     1720   1257   1602    -59     20   -106       C  
ATOM    250  C   LEU A  32      13.464 -20.041   7.259  1.00 12.52           C  
ANISOU  250  C   LEU A  32     1779   1269   1710    -36     80   -101       C  
ATOM    251  O   LEU A  32      14.277 -20.097   8.192  1.00 12.39           O  
ANISOU  251  O   LEU A  32     1695   1268   1746      1     99    -72       O  
ATOM    252  CB  LEU A  32      13.563 -17.678   6.627  1.00 12.45           C  
ANISOU  252  CB  LEU A  32     1767   1319   1644    -44     45   -115       C  
ATOM    253  CG  LEU A  32      12.892 -16.342   6.393  1.00 13.71           C  
ANISOU  253  CG  LEU A  32     1925   1523   1759    -62     -6   -120       C  
ATOM    254  CD1 LEU A  32      13.907 -15.285   6.173  1.00 13.62           C  
ANISOU  254  CD1 LEU A  32     1900   1524   1752    -43     18   -122       C  
ATOM    255  CD2 LEU A  32      11.959 -16.400   5.210  1.00 14.51           C  
ANISOU  255  CD2 LEU A  32     2102   1605   1805   -111    -28   -142       C  
ATOM    256  N   ASP A  33      13.193 -21.093   6.468  1.00 12.93           N  
ANISOU  256  N   ASP A  33     1908   1261   1746    -61    105   -124       N  
ATOM    257  CA  ASP A  33      13.854 -22.381   6.675  1.00 13.70           C  
ANISOU  257  CA  ASP A  33     2009   1304   1891    -38    166   -117       C  
ATOM    258  C   ASP A  33      13.561 -22.852   8.132  1.00 13.91           C  
ANISOU  258  C   ASP A  33     1946   1369   1970    -19    130    -76       C  
ATOM    259  O   ASP A  33      12.412 -22.706   8.557  1.00 14.60           O  
ANISOU  259  O   ASP A  33     2016   1493   2037    -42     60    -65       O  
ATOM    260  CB  ASP A  33      15.356 -22.306   6.311  1.00 16.27           C  
ANISOU  260  CB  ASP A  33     2335   1598   2250      3    255   -115       C  
ATOM    261  CG  ASP A  33      15.597 -21.887   4.883  1.00 21.63           C  
ANISOU  261  CG  ASP A  33     3105   2238   2874    -13    295   -153       C  
ATOM    262  OD1 ASP A  33      14.817 -22.304   4.008  1.00 23.84           O  
ANISOU  262  OD1 ASP A  33     3480   2480   3097    -56    283   -188       O  
ATOM    263  OD2 ASP A  33      16.574 -21.142   4.642  1.00 23.06           O  
ANISOU  263  OD2 ASP A  33     3265   2427   3068     15    337   -145       O  
ATOM    264  N   ASP A  34      14.549 -23.299   8.901  1.00 12.95           N  
ANISOU  264  N   ASP A  34     1764   1244   1914     22    173    -46       N  
ATOM    265  CA  ASP A  34      14.306 -23.727  10.265  1.00 12.62           C  
ANISOU  265  CA  ASP A  34     1641   1238   1917     38    139     -5       C  
ATOM    266  C   ASP A  34      14.745 -22.702  11.278  1.00 12.42           C  
ANISOU  266  C   ASP A  34     1535   1277   1907     61    110     26       C  
ATOM    267  O   ASP A  34      15.104 -23.073  12.395  1.00 13.06           O  
ANISOU  267  O   ASP A  34     1547   1379   2036     83    105     66       O  
ATOM    268  CB  ASP A  34      14.988 -25.077  10.522  1.00 13.51           C  
ANISOU  268  CB  ASP A  34     1742   1298   2092     61    201     14       C  
ATOM    269  CG  ASP A  34      16.497 -25.078  10.331  1.00 17.85           C  
ANISOU  269  CG  ASP A  34     2272   1819   2691     99    282     33       C  
ATOM    270  OD1 ASP A  34      17.037 -24.076   9.798  1.00 17.68           O  
ANISOU  270  OD1 ASP A  34     2261   1809   2648    103    295     23       O  
ATOM    271  OD2 ASP A  34      17.138 -26.087  10.709  1.00 20.21           O  
ANISOU  271  OD2 ASP A  34     2542   2083   3054    125    334     63       O  
ATOM    272  N   VAL A  35      14.689 -21.404  10.928  1.00 11.43           N  
ANISOU  272  N   VAL A  35     1421   1184   1739     53     84     10       N  
ATOM    273  CA  VAL A  35      15.074 -20.358  11.868  1.00 12.04           C  
ANISOU  273  CA  VAL A  35     1436   1316   1821     69     51     37       C  
ATOM    274  C   VAL A  35      13.987 -19.307  11.950  1.00 11.65           C  
ANISOU  274  C   VAL A  35     1399   1313   1715     51    -11     23       C  
ATOM    275  O   VAL A  35      13.400 -18.939  10.930  1.00 12.01           O  
ANISOU  275  O   VAL A  35     1499   1347   1716     27    -17     -8       O  
ATOM    276  CB  VAL A  35      16.424 -19.702  11.481  1.00 13.42           C  
ANISOU  276  CB  VAL A  35     1601   1481   2015     84     91     44       C  
ATOM    277  CG1 VAL A  35      16.824 -18.604  12.473  1.00 13.93           C  
ANISOU  277  CG1 VAL A  35     1611   1599   2082     91     45     72       C  
ATOM    278  CG2 VAL A  35      17.519 -20.750  11.384  1.00 14.17           C  
ANISOU  278  CG2 VAL A  35     1679   1529   2177    107    163     69       C  
ATOM    279  N   VAL A  36      13.699 -18.861  13.164  1.00 11.24           N  
ANISOU  279  N   VAL A  36     1299   1308   1664     64    -53     50       N  
ATOM    280  CA  VAL A  36      12.775 -17.774  13.408  1.00 11.41           C  
ANISOU  280  CA  VAL A  36     1327   1371   1637     58   -101     46       C  
ATOM    281  C   VAL A  36      13.589 -16.584  13.895  1.00 11.05           C  
ANISOU  281  C   VAL A  36     1263   1352   1584     70   -112     53       C  
ATOM    282  O   VAL A  36      14.339 -16.704  14.855  1.00 10.78           O  
ANISOU  282  O   VAL A  36     1188   1327   1579     84   -115     82       O  
ATOM    283  CB  VAL A  36      11.676 -18.169  14.404  1.00 12.20           C  
ANISOU  283  CB  VAL A  36     1401   1500   1736     65   -136     73       C  
ATOM    284  CG1 VAL A  36      10.833 -16.957  14.781  1.00 12.52           C  
ANISOU  284  CG1 VAL A  36     1445   1580   1732     70   -172     78       C  
ATOM    285  CG2 VAL A  36      10.810 -19.281  13.826  1.00 12.70           C  
ANISOU  285  CG2 VAL A  36     1485   1535   1807     45   -135     70       C  
ATOM    286  N   TYR A  37      13.465 -15.444  13.220  1.00 11.02           N  
ANISOU  286  N   TYR A  37     1289   1355   1541     60   -122     30       N  
ATOM    287  CA  TYR A  37      14.205 -14.229  13.566  1.00 10.75           C  
ANISOU  287  CA  TYR A  37     1248   1341   1497     65   -137     34       C  
ATOM    288  C   TYR A  37      13.256 -13.286  14.257  1.00 11.13           C  
ANISOU  288  C   TYR A  37     1305   1425   1501     71   -177     37       C  
ATOM    289  O   TYR A  37      12.130 -13.095  13.787  1.00 11.97           O  
ANISOU  289  O   TYR A  37     1433   1537   1579     64   -186     27       O  
ATOM    290  CB  TYR A  37      14.693 -13.529  12.285  1.00 10.59           C  
ANISOU  290  CB  TYR A  37     1259   1303   1462     52   -117      8       C  
ATOM    291  CG  TYR A  37      15.597 -14.400  11.453  1.00 11.51           C  
ANISOU  291  CG  TYR A  37     1381   1378   1616     52    -62      5       C  
ATOM    292  CD1 TYR A  37      15.076 -15.318  10.558  1.00 12.49           C  
ANISOU  292  CD1 TYR A  37     1543   1469   1734     41    -34    -17       C  
ATOM    293  CD2 TYR A  37      16.974 -14.306  11.565  1.00 12.68           C  
ANISOU  293  CD2 TYR A  37     1499   1515   1806     63    -38     29       C  
ATOM    294  CE1 TYR A  37      15.904 -16.163   9.830  1.00 13.67           C  
ANISOU  294  CE1 TYR A  37     1709   1572   1914     46     27    -21       C  
ATOM    295  CE2 TYR A  37      17.814 -15.115  10.809  1.00 13.61           C  
ANISOU  295  CE2 TYR A  37     1620   1589   1962     72     26     34       C  
ATOM    296  CZ  TYR A  37      17.275 -16.032   9.932  1.00 14.78           C  
ANISOU  296  CZ  TYR A  37     1816   1701   2098     66     62      5       C  
ATOM    297  OH  TYR A  37      18.101 -16.885   9.229  1.00 17.25           O  
ANISOU  297  OH  TYR A  37     2143   1962   2448     79    135     10       O  
ATOM    298  N   CYS A  38      13.677 -12.713  15.375  1.00 10.69           N  
ANISOU  298  N   CYS A  38     1233   1388   1439     81   -201     56       N  
ATOM    299  CA  CYS A  38      12.825 -11.757  16.071  1.00 10.98           C  
ANISOU  299  CA  CYS A  38     1292   1452   1430     92   -229     58       C  
ATOM    300  C   CYS A  38      13.672 -10.755  16.841  1.00 11.25           C  
ANISOU  300  C   CYS A  38     1335   1493   1447     91   -254     65       C  
ATOM    301  O   CYS A  38      14.846 -11.012  17.094  1.00 11.69           O  
ANISOU  301  O   CYS A  38     1367   1541   1535     81   -258     82       O  
ATOM    302  CB  CYS A  38      11.815 -12.484  16.958  1.00 11.60           C  
ANISOU  302  CB  CYS A  38     1355   1545   1507    110   -234     81       C  
ATOM    303  SG  CYS A  38      12.515 -13.143  18.487  1.00 13.48           S  
ANISOU  303  SG  CYS A  38     1562   1794   1768    121   -247    115       S  
ATOM    304  N   PRO A  39      13.111  -9.604  17.244  1.00 10.96           N  
ANISOU  304  N   PRO A  39     1337   1469   1360     98   -274     58       N  
ATOM    305  CA  PRO A  39      13.899  -8.651  18.033  1.00 10.74           C  
ANISOU  305  CA  PRO A  39     1342   1442   1298     92   -309     63       C  
ATOM    306  C   PRO A  39      14.331  -9.281  19.350  1.00 11.52           C  
ANISOU  306  C   PRO A  39     1415   1548   1415     92   -323     95       C  
ATOM    307  O   PRO A  39      13.544  -9.987  19.992  1.00 12.03           O  
ANISOU  307  O   PRO A  39     1469   1622   1478    111   -313    107       O  
ATOM    308  CB  PRO A  39      12.903  -7.512  18.282  1.00 11.14           C  
ANISOU  308  CB  PRO A  39     1438   1499   1296    112   -305     50       C  
ATOM    309  CG  PRO A  39      11.956  -7.602  17.126  1.00 11.48           C  
ANISOU  309  CG  PRO A  39     1467   1541   1352    113   -279     37       C  
ATOM    310  CD  PRO A  39      11.753  -9.084  16.998  1.00 10.66           C  
ANISOU  310  CD  PRO A  39     1321   1439   1290    113   -265     50       C  
ATOM    311  N   ARG A  40      15.581  -9.024  19.762  1.00 11.03           N  
ANISOU  311  N   ARG A  40     1347   1480   1365     68   -353    114       N  
ATOM    312  CA  ARG A  40      16.049  -9.593  21.020  1.00 11.30           C  
ANISOU  312  CA  ARG A  40     1363   1522   1409     61   -378    151       C  
ATOM    313  C   ARG A  40      15.284  -9.013  22.218  1.00 12.95           C  
ANISOU  313  C   ARG A  40     1631   1740   1549     73   -400    150       C  
ATOM    314  O   ARG A  40      15.228  -9.680  23.250  1.00 13.60           O  
ANISOU  314  O   ARG A  40     1704   1833   1629     78   -407    175       O  
ATOM    315  CB  ARG A  40      17.549  -9.444  21.184  1.00 11.64           C  
ANISOU  315  CB  ARG A  40     1380   1555   1486     25   -411    184       C  
ATOM    316  CG  ARG A  40      17.977  -8.012  21.332  1.00 12.88           C  
ANISOU  316  CG  ARG A  40     1592   1704   1596      1   -455    177       C  
ATOM    317  CD  ARG A  40      19.457  -7.968  21.572  1.00 13.12           C  
ANISOU  317  CD  ARG A  40     1588   1727   1669    -40   -497    227       C  
ATOM    318  NE  ARG A  40      19.935  -6.599  21.666  1.00 14.21           N  
ANISOU  318  NE  ARG A  40     1780   1853   1766    -69   -543    221       N  
ATOM    319  CZ  ARG A  40      21.174  -6.261  21.996  1.00 15.68           C  
ANISOU  319  CZ  ARG A  40     1952   2032   1976   -113   -597    268       C  
ATOM    320  NH1 ARG A  40      22.082  -7.197  22.248  1.00 15.22           N  
ANISOU  320  NH1 ARG A  40     1822   1977   1982   -129   -605    328       N  
ATOM    321  NH2 ARG A  40      21.519  -4.983  22.070  1.00 15.20           N  
ANISOU  321  NH2 ARG A  40     1947   1956   1873   -143   -643    261       N  
ATOM    322  N   HIS A  41      14.628  -7.836  22.073  1.00 13.07           N  
ANISOU  322  N   HIS A  41     1708   1750   1508     84   -397    121       N  
ATOM    323  CA  HIS A  41      13.892  -7.269  23.196  1.00 13.76           C  
ANISOU  323  CA  HIS A  41     1863   1838   1525    106   -399    119       C  
ATOM    324  C   HIS A  41      12.612  -8.048  23.529  1.00 14.57           C  
ANISOU  324  C   HIS A  41     1951   1958   1627    149   -359    129       C  
ATOM    325  O   HIS A  41      11.970  -7.700  24.519  1.00 14.99           O  
ANISOU  325  O   HIS A  41     2054   2012   1629    172   -354    136       O  
ATOM    326  CB  HIS A  41      13.651  -5.754  23.097  1.00 14.02           C  
ANISOU  326  CB  HIS A  41     1972   1853   1502    106   -406     91       C  
ATOM    327  CG  HIS A  41      12.654  -5.295  22.083  1.00 16.36           C  
ANISOU  327  CG  HIS A  41     2270   2150   1798    134   -364     69       C  
ATOM    328  ND1 HIS A  41      11.296  -5.507  22.253  1.00 19.44           N  
ANISOU  328  ND1 HIS A  41     2661   2548   2175    176   -323     76       N  
ATOM    329  CD2 HIS A  41      12.838  -4.516  20.993  1.00 17.15           C  
ANISOU  329  CD2 HIS A  41     2370   2239   1905    124   -360     46       C  
ATOM    330  CE1 HIS A  41      10.708  -4.914  21.223  1.00 19.39           C  
ANISOU  330  CE1 HIS A  41     2654   2539   2173    188   -298     62       C  
ATOM    331  NE2 HIS A  41      11.596  -4.303  20.441  1.00 18.52           N  
ANISOU  331  NE2 HIS A  41     2544   2419   2074    157   -320     41       N  
ATOM    332  N   VAL A  42      12.320  -9.175  22.827  1.00 14.08           N  
ANISOU  332  N   VAL A  42     1822   1906   1623    156   -336    136       N  
ATOM    333  CA  VAL A  42      11.239 -10.064  23.272  1.00 14.58           C  
ANISOU  333  CA  VAL A  42     1859   1985   1696    188   -310    159       C  
ATOM    334  C   VAL A  42      11.547 -10.606  24.697  1.00 15.27           C  
ANISOU  334  C   VAL A  42     1949   2082   1770    189   -329    189       C  
ATOM    335  O   VAL A  42      10.628 -10.903  25.447  1.00 16.44           O  
ANISOU  335  O   VAL A  42     2105   2241   1898    221   -310    207       O  
ATOM    336  CB  VAL A  42      10.982 -11.221  22.276  1.00 14.96           C  
ANISOU  336  CB  VAL A  42     1841   2034   1807    184   -292    161       C  
ATOM    337  CG1 VAL A  42      12.125 -12.225  22.274  1.00 14.97           C  
ANISOU  337  CG1 VAL A  42     1795   2032   1863    160   -303    173       C  
ATOM    338  CG2 VAL A  42       9.651 -11.914  22.559  1.00 15.69           C  
ANISOU  338  CG2 VAL A  42     1914   2140   1907    215   -268    185       C  
ATOM    339  N   ILE A  43      12.839 -10.667  25.091  1.00 14.68           N  
ANISOU  339  N   ILE A  43     1867   2004   1707    153   -367    199       N  
ATOM    340  CA  ILE A  43      13.211 -11.149  26.424  1.00 15.70           C  
ANISOU  340  CA  ILE A  43     2001   2144   1822    145   -394    234       C  
ATOM    341  C   ILE A  43      13.082 -10.078  27.518  1.00 18.13           C  
ANISOU  341  C   ILE A  43     2405   2444   2041    146   -414    228       C  
ATOM    342  O   ILE A  43      13.347 -10.366  28.682  1.00 18.87           O  
ANISOU  342  O   ILE A  43     2518   2544   2107    138   -437    255       O  
ATOM    343  CB  ILE A  43      14.635 -11.767  26.406  1.00 15.42           C  
ANISOU  343  CB  ILE A  43     1911   2105   1842    102   -429    260       C  
ATOM    344  CG1 ILE A  43      15.718 -10.687  26.276  1.00 15.89           C  
ANISOU  344  CG1 ILE A  43     2007   2149   1882     61   -472    255       C  
ATOM    345  CG2 ILE A  43      14.757 -12.817  25.294  1.00 15.89           C  
ANISOU  345  CG2 ILE A  43     1891   2162   1985    106   -396    261       C  
ATOM    346  CD1 ILE A  43      17.155 -11.214  26.301  1.00 17.16           C  
ANISOU  346  CD1 ILE A  43     2105   2308   2108     20   -504    297       C  
ATOM    347  N   CYS A  44      12.700  -8.851  27.161  1.00 19.70           N  
ANISOU  347  N   CYS A  44     2667   2625   2191    156   -403    196       N  
ATOM    348  CA  CYS A  44      12.587  -7.761  28.109  1.00 22.56           C  
ANISOU  348  CA  CYS A  44     3137   2971   2464    156   -418    188       C  
ATOM    349  C   CYS A  44      11.166  -7.545  28.562  1.00 26.82           C  
ANISOU  349  C   CYS A  44     3723   3510   2957    217   -360    186       C  
ATOM    350  O   CYS A  44      10.221  -7.737  27.806  1.00 27.66           O  
ANISOU  350  O   CYS A  44     3787   3624   3097    251   -317    185       O  
ATOM    351  CB  CYS A  44      13.121  -6.476  27.485  1.00 22.30           C  
ANISOU  351  CB  CYS A  44     3157   2911   2403    133   -436    155       C  
ATOM    352  SG  CYS A  44      14.871  -6.530  27.050  1.00 22.16           S  
ANISOU  352  SG  CYS A  44     3091   2889   2438     63   -504    168       S  
ATOM    353  N   THR A  45      11.039  -7.011  29.755  1.00 29.51           N  
ANISOU  353  N   THR A  45     4158   3836   3217    226   -363    189       N  
ATOM    354  CA  THR A  45       9.787  -6.494  30.270  1.00 32.18           C  
ANISOU  354  CA  THR A  45     4565   4164   3498    287   -301    190       C  
ATOM    355  C   THR A  45       9.827  -4.970  29.895  1.00 34.36           C  
ANISOU  355  C   THR A  45     4930   4402   3723    283   -296    152       C  
ATOM    356  O   THR A  45      10.846  -4.488  29.368  1.00 34.59           O  
ANISOU  356  O   THR A  45     4961   4420   3762    231   -348    130       O  
ATOM    357  CB  THR A  45       9.740  -6.707  31.794  1.00 34.04           C  
ANISOU  357  CB  THR A  45     4873   4397   3665    295   -304    212       C  
ATOM    358  OG1 THR A  45      10.699  -5.849  32.419  1.00 35.60           O  
ANISOU  358  OG1 THR A  45     5172   4565   3790    245   -359    193       O  
ATOM    359  CG2 THR A  45      10.010  -8.155  32.194  1.00 34.58           C  
ANISOU  359  CG2 THR A  45     4854   4501   3785    283   -326    250       C  
ATOM    360  N   SER A  46       8.754  -4.205  30.188  1.00 35.48           N  
ANISOU  360  N   SER A  46     5146   4523   3813    340   -232    150       N  
ATOM    361  CA  SER A  46       8.778  -2.760  29.936  1.00 36.69           C  
ANISOU  361  CA  SER A  46     5392   4636   3915    340   -223    116       C  
ATOM    362  C   SER A  46       9.855  -2.090  30.824  1.00 37.23           C  
ANISOU  362  C   SER A  46     5572   4670   3904    286   -286     95       C  
ATOM    363  O   SER A  46      10.511  -1.144  30.383  1.00 37.54           O  
ANISOU  363  O   SER A  46     5653   4683   3928    247   -323     65       O  
ATOM    364  CB  SER A  46       7.409  -2.137  30.185  1.00 38.60           C  
ANISOU  364  CB  SER A  46     5692   4857   4118    418   -133    128       C  
ATOM    365  OG  SER A  46       7.293  -0.915  29.474  1.00 42.31           O  
ANISOU  365  OG  SER A  46     6206   5295   4576    423   -115    101       O  
ATOM    366  N   GLU A  47      10.064  -2.620  32.051  1.00 37.15           N  
ANISOU  366  N   GLU A  47     5606   4662   3845    278   -303    114       N  
ATOM    367  CA  GLU A  47      11.067  -2.151  33.007  1.00 37.30           C  
ANISOU  367  CA  GLU A  47     5733   4653   3785    217   -373    104       C  
ATOM    368  C   GLU A  47      12.485  -2.408  32.486  1.00 36.61           C  
ANISOU  368  C   GLU A  47     5575   4580   3755    133   -468    109       C  
ATOM    369  O   GLU A  47      13.323  -1.506  32.541  1.00 37.19           O  
ANISOU  369  O   GLU A  47     5721   4620   3788     78   -527     91       O  
ATOM    370  CB  GLU A  47      10.871  -2.832  34.379  1.00 40.16           C  
ANISOU  370  CB  GLU A  47     6141   5023   4093    228   -369    133       C  
ATOM    371  CG  GLU A  47      11.899  -2.401  35.412  1.00 46.08           C  
ANISOU  371  CG  GLU A  47     7008   5744   4757    154   -451    130       C  
ATOM    372  CD  GLU A  47      11.871  -3.137  36.739  1.00 53.53           C  
ANISOU  372  CD  GLU A  47     7996   6698   5645    150   -462    161       C  
ATOM    373  OE1 GLU A  47      11.167  -4.168  36.840  1.00 55.04           O  
ANISOU  373  OE1 GLU A  47     8102   6928   5882    202   -412    191       O  
ATOM    374  OE2 GLU A  47      12.559  -2.680  37.681  1.00 56.09           O  
ANISOU  374  OE2 GLU A  47     8443   6991   5879     92   -525    159       O  
ATOM    375  N   ASP A  48      12.752  -3.629  31.971  1.00 35.12           N  
ANISOU  375  N   ASP A  48     5245   4437   3662    125   -481    136       N  
ATOM    376  CA  ASP A  48      14.071  -3.994  31.442  1.00 34.07           C  
ANISOU  376  CA  ASP A  48     5032   4319   3596     56   -555    152       C  
ATOM    377  C   ASP A  48      14.517  -3.050  30.338  1.00 32.73           C  
ANISOU  377  C   ASP A  48     4859   4129   3449     34   -570    124       C  
ATOM    378  O   ASP A  48      15.695  -2.736  30.268  1.00 32.68           O  
ANISOU  378  O   ASP A  48     4853   4111   3451    -31   -643    134       O  
ATOM    379  CB  ASP A  48      14.089  -5.430  30.884  1.00 35.22           C  
ANISOU  379  CB  ASP A  48     5029   4508   3845     67   -541    181       C  
ATOM    380  CG  ASP A  48      14.024  -6.544  31.907  1.00 39.53           C  
ANISOU  380  CG  ASP A  48     5549   5080   4393     72   -546    220       C  
ATOM    381  OD1 ASP A  48      14.540  -6.353  33.029  1.00 39.78           O  
ANISOU  381  OD1 ASP A  48     5653   5100   4362     33   -596    238       O  
ATOM    382  OD2 ASP A  48      13.467  -7.614  31.581  1.00 41.68           O  
ANISOU  382  OD2 ASP A  48     5728   5380   4728    109   -503    236       O  
ATOM    383  N   MET A  49      13.587  -2.587  29.486  1.00 31.75           N  
ANISOU  383  N   MET A  49     4729   4001   3335     86   -505     95       N  
ATOM    384  CA  MET A  49      13.915  -1.698  28.369  1.00 31.02           C  
ANISOU  384  CA  MET A  49     4625   3892   3268     69   -514     69       C  
ATOM    385  C   MET A  49      14.627  -0.405  28.761  1.00 30.28           C  
ANISOU  385  C   MET A  49     4647   3753   3103     22   -568     51       C  
ATOM    386  O   MET A  49      15.313   0.164  27.924  1.00 29.65           O  
ANISOU  386  O   MET A  49     4547   3665   3055    -11   -601     43       O  
ATOM    387  CB  MET A  49      12.679  -1.384  27.513  1.00 31.35           C  
ANISOU  387  CB  MET A  49     4649   3936   3326    132   -435     48       C  
ATOM    388  CG  MET A  49      12.174  -2.572  26.724  1.00 32.65           C  
ANISOU  388  CG  MET A  49     4693   4140   3572    161   -398     65       C  
ATOM    389  SD  MET A  49      13.436  -3.315  25.650  1.00 33.34           S  
ANISOU  389  SD  MET A  49     4666   4249   3751    107   -446     75       S  
ATOM    390  CE  MET A  49      13.560  -2.060  24.368  1.00 27.71           C  
ANISOU  390  CE  MET A  49     3963   3518   3049     97   -444     42       C  
ATOM    391  N   LEU A  50      14.493   0.050  30.009  1.00 30.11           N  
ANISOU  391  N   LEU A  50     4750   3702   2988     18   -579     48       N  
ATOM    392  CA  LEU A  50      15.162   1.274  30.453  1.00 30.70           C  
ANISOU  392  CA  LEU A  50     4951   3727   2988    -35   -638     31       C  
ATOM    393  C   LEU A  50      16.689   1.159  30.403  1.00 30.56           C  
ANISOU  393  C   LEU A  50     4892   3714   3007   -125   -744     62       C  
ATOM    394  O   LEU A  50      17.345   2.089  29.955  1.00 31.26           O  
ANISOU  394  O   LEU A  50     5008   3775   3094   -168   -790     53       O  
ATOM    395  CB  LEU A  50      14.682   1.683  31.851  1.00 31.34           C  
ANISOU  395  CB  LEU A  50     5188   3769   2950    -22   -625     21       C  
ATOM    396  CG  LEU A  50      13.191   1.988  31.949  1.00 33.68           C  
ANISOU  396  CG  LEU A  50     5538   4051   3208     72   -512     -2       C  
ATOM    397  CD1 LEU A  50      12.778   2.229  33.387  1.00 34.43           C  
ANISOU  397  CD1 LEU A  50     5787   4107   3185     88   -492     -5       C  
ATOM    398  CD2 LEU A  50      12.806   3.173  31.059  1.00 34.52           C  
ANISOU  398  CD2 LEU A  50     5675   4125   3316     97   -473    -35       C  
ATOM    399  N   ASN A  51      17.251   0.022  30.820  1.00 29.29           N  
ANISOU  399  N   ASN A  51     4655   3587   2886   -153   -781    107       N  
ATOM    400  CA  ASN A  51      18.701  -0.204  30.771  1.00 28.56           C  
ANISOU  400  CA  ASN A  51     4505   3502   2843   -236   -877    154       C  
ATOM    401  C   ASN A  51      18.964  -1.718  30.692  1.00 26.51           C  
ANISOU  401  C   ASN A  51     4106   3292   2674   -231   -871    201       C  
ATOM    402  O   ASN A  51      19.400  -2.327  31.674  1.00 26.96           O  
ANISOU  402  O   ASN A  51     4166   3359   2718   -268   -920    243       O  
ATOM    403  CB  ASN A  51      19.381   0.398  32.009  1.00 30.92           C  
ANISOU  403  CB  ASN A  51     4934   3764   3050   -310   -968    172       C  
ATOM    404  CG  ASN A  51      20.892   0.388  31.942  1.00 35.07           C  
ANISOU  404  CG  ASN A  51     5408   4292   3627   -404  -1077    232       C  
ATOM    405  OD1 ASN A  51      21.493   0.225  30.873  1.00 36.86           O  
ANISOU  405  OD1 ASN A  51     5517   4536   3951   -411  -1081    253       O  
ATOM    406  ND2 ASN A  51      21.539   0.567  33.085  1.00 36.16           N  
ANISOU  406  ND2 ASN A  51     5631   4408   3698   -478  -1167    266       N  
ATOM    407  N   PRO A  52      18.640  -2.362  29.557  1.00 23.74           N  
ANISOU  407  N   PRO A  52     3637   2970   2411   -183   -808    193       N  
ATOM    408  CA  PRO A  52      18.791  -3.824  29.494  1.00 22.58           C  
ANISOU  408  CA  PRO A  52     3370   2864   2345   -171   -792    233       C  
ATOM    409  C   PRO A  52      20.203  -4.339  29.261  1.00 21.84           C  
ANISOU  409  C   PRO A  52     3183   2781   2333   -231   -854    295       C  
ATOM    410  O   PRO A  52      20.938  -3.775  28.461  1.00 23.02           O  
ANISOU  410  O   PRO A  52     3308   2919   2521   -260   -879    301       O  
ATOM    411  CB  PRO A  52      17.858  -4.228  28.347  1.00 23.00           C  
ANISOU  411  CB  PRO A  52     3352   2934   2451   -104   -704    200       C  
ATOM    412  CG  PRO A  52      17.799  -3.012  27.462  1.00 23.84           C  
ANISOU  412  CG  PRO A  52     3498   3017   2544   -104   -698    161       C  
ATOM    413  CD  PRO A  52      18.087  -1.804  28.306  1.00 23.00           C  
ANISOU  413  CD  PRO A  52     3524   2872   2342   -139   -749    150       C  
ATOM    414  N   ASN A  53      20.579  -5.426  29.948  1.00 20.08           N  
ANISOU  414  N   ASN A  53     2904   2581   2144   -247   -874    346       N  
ATOM    415  CA  ASN A  53      21.843  -6.098  29.676  1.00 19.44           C  
ANISOU  415  CA  ASN A  53     2714   2513   2160   -292   -915    417       C  
ATOM    416  C   ASN A  53      21.378  -7.382  29.004  1.00 19.09           C  
ANISOU  416  C   ASN A  53     2561   2495   2199   -233   -835    415       C  
ATOM    417  O   ASN A  53      20.976  -8.328  29.682  1.00 19.86           O  
ANISOU  417  O   ASN A  53     2636   2611   2298   -214   -818    432       O  
ATOM    418  CB  ASN A  53      22.650  -6.418  30.934  1.00 20.41           C  
ANISOU  418  CB  ASN A  53     2848   2640   2268   -357   -999    486       C  
ATOM    419  CG  ASN A  53      24.001  -6.990  30.569  1.00 23.36           C  
ANISOU  419  CG  ASN A  53     3101   3024   2753   -401  -1038    571       C  
ATOM    420  OD1 ASN A  53      24.112  -7.970  29.818  1.00 24.42           O  
ANISOU  420  OD1 ASN A  53     3120   3174   2984   -364   -978    589       O  
ATOM    421  ND2 ASN A  53      25.063  -6.397  31.086  1.00 23.75           N  
ANISOU  421  ND2 ASN A  53     3174   3058   2792   -483  -1136    631       N  
ATOM    422  N   TYR A  54      21.348  -7.382  27.684  1.00 18.47           N  
ANISOU  422  N   TYR A  54     2424   2414   2180   -206   -786    394       N  
ATOM    423  CA  TYR A  54      20.814  -8.489  26.923  1.00 17.26           C  
ANISOU  423  CA  TYR A  54     2190   2277   2090   -151   -706    380       C  
ATOM    424  C   TYR A  54      21.500  -9.801  27.153  1.00 17.52           C  
ANISOU  424  C   TYR A  54     2126   2325   2207   -161   -708    446       C  
ATOM    425  O   TYR A  54      20.800 -10.791  27.331  1.00 17.53           O  
ANISOU  425  O   TYR A  54     2098   2340   2224   -125   -664    439       O  
ATOM    426  CB  TYR A  54      20.781  -8.147  25.448  1.00 15.88           C  
ANISOU  426  CB  TYR A  54     1991   2092   1952   -128   -659    343       C  
ATOM    427  CG  TYR A  54      19.666  -7.180  25.141  1.00 15.71           C  
ANISOU  427  CG  TYR A  54     2051   2062   1857    -98   -634    275       C  
ATOM    428  CD1 TYR A  54      18.353  -7.614  25.039  1.00 16.04           C  
ANISOU  428  CD1 TYR A  54     2100   2115   1881    -46   -576    238       C  
ATOM    429  CD2 TYR A  54      19.916  -5.823  25.004  1.00 15.93           C  
ANISOU  429  CD2 TYR A  54     2146   2070   1837   -123   -670    256       C  
ATOM    430  CE1 TYR A  54      17.320  -6.725  24.759  1.00 16.34           C  
ANISOU  430  CE1 TYR A  54     2203   2145   1861    -17   -549    189       C  
ATOM    431  CE2 TYR A  54      18.897  -4.929  24.714  1.00 16.57           C  
ANISOU  431  CE2 TYR A  54     2297   2141   1858    -93   -641    200       C  
ATOM    432  CZ  TYR A  54      17.596  -5.382  24.598  1.00 17.28           C  
ANISOU  432  CZ  TYR A  54     2388   2243   1935    -39   -578    169       C  
ATOM    433  OH  TYR A  54      16.582  -4.489  24.330  1.00 18.46           O  
ANISOU  433  OH  TYR A  54     2600   2383   2033     -7   -547    126       O  
ATOM    434  N   GLU A  55      22.849  -9.837  27.217  1.00 18.17           N  
ANISOU  434  N   GLU A  55     2157   2401   2346   -210   -755    513       N  
ATOM    435  CA  GLU A  55      23.536 -11.110  27.478  1.00 18.88           C  
ANISOU  435  CA  GLU A  55     2147   2503   2523   -216   -749    585       C  
ATOM    436  C   GLU A  55      23.132 -11.677  28.833  1.00 19.05           C  
ANISOU  436  C   GLU A  55     2191   2544   2503   -224   -778    605       C  
ATOM    437  O   GLU A  55      22.911 -12.883  28.953  1.00 19.30           O  
ANISOU  437  O   GLU A  55     2158   2588   2585   -196   -739    625       O  
ATOM    438  CB  GLU A  55      25.069 -10.991  27.409  1.00 22.09           C  
ANISOU  438  CB  GLU A  55     2489   2902   3003   -271   -801    674       C  
ATOM    439  CG  GLU A  55      25.638 -10.894  26.003  1.00 27.99           C  
ANISOU  439  CG  GLU A  55     3177   3632   3827   -252   -751    679       C  
ATOM    440  CD  GLU A  55      25.669 -12.141  25.133  1.00 34.81           C  
ANISOU  440  CD  GLU A  55     3953   4491   4783   -201   -658    687       C  
ATOM    441  OE1 GLU A  55      25.127 -13.194  25.538  1.00 33.74           O  
ANISOU  441  OE1 GLU A  55     3796   4366   4658   -173   -623    681       O  
ATOM    442  OE2 GLU A  55      26.209 -12.043  24.007  1.00 39.00           O  
ANISOU  442  OE2 GLU A  55     4443   5004   5372   -188   -615    697       O  
ATOM    443  N   ASP A  56      22.991 -10.802  29.841  1.00 18.58           N  
ANISOU  443  N   ASP A  56     2230   2482   2347   -260   -845    597       N  
ATOM    444  CA  ASP A  56      22.594 -11.263  31.171  1.00 18.89           C  
ANISOU  444  CA  ASP A  56     2304   2538   2334   -269   -872    616       C  
ATOM    445  C   ASP A  56      21.151 -11.742  31.203  1.00 19.04           C  
ANISOU  445  C   ASP A  56     2346   2569   2318   -198   -798    556       C  
ATOM    446  O   ASP A  56      20.872 -12.782  31.794  1.00 20.06           O  
ANISOU  446  O   ASP A  56     2434   2719   2470   -182   -783    583       O  
ATOM    447  CB  ASP A  56      22.838 -10.181  32.232  1.00 20.13           C  
ANISOU  447  CB  ASP A  56     2578   2683   2388   -329   -960    623       C  
ATOM    448  CG  ASP A  56      24.304  -9.937  32.525  1.00 23.92           C  
ANISOU  448  CG  ASP A  56     3026   3156   2907   -413  -1053    708       C  
ATOM    449  OD1 ASP A  56      25.133 -10.830  32.216  1.00 23.66           O  
ANISOU  449  OD1 ASP A  56     2869   3134   2985   -422  -1049    781       O  
ATOM    450  OD2 ASP A  56      24.630  -8.853  33.067  1.00 25.46           O  
ANISOU  450  OD2 ASP A  56     3320   3330   3023   -470  -1130    709       O  
ATOM    451  N   LEU A  57      20.235 -11.002  30.566  1.00 18.53           N  
ANISOU  451  N   LEU A  57     2342   2493   2205   -158   -754    482       N  
ATOM    452  CA  LEU A  57      18.835 -11.405  30.531  1.00 18.71           C  
ANISOU  452  CA  LEU A  57     2381   2527   2202    -93   -686    437       C  
ATOM    453  C   LEU A  57      18.663 -12.733  29.781  1.00 18.63           C  
ANISOU  453  C   LEU A  57     2260   2529   2289    -57   -628    448       C  
ATOM    454  O   LEU A  57      17.847 -13.565  30.166  1.00 18.76           O  
ANISOU  454  O   LEU A  57     2258   2561   2308    -21   -595    449       O  
ATOM    455  CB  LEU A  57      17.989 -10.323  29.851  1.00 19.11           C  
ANISOU  455  CB  LEU A  57     2503   2561   2198    -60   -651    369       C  
ATOM    456  CG  LEU A  57      17.861  -9.013  30.615  1.00 21.19           C  
ANISOU  456  CG  LEU A  57     2895   2804   2353    -81   -690    346       C  
ATOM    457  CD1 LEU A  57      17.170  -7.968  29.770  1.00 22.03           C  
ANISOU  457  CD1 LEU A  57     3054   2892   2426    -49   -650    287       C  
ATOM    458  CD2 LEU A  57      17.084  -9.216  31.913  1.00 22.04           C  
ANISOU  458  CD2 LEU A  57     3070   2920   2385    -60   -683    350       C  
ATOM    459  N   LEU A  58      19.446 -12.932  28.724  1.00 17.87           N  
ANISOU  459  N   LEU A  58     2097   2422   2272    -68   -616    459       N  
ATOM    460  CA  LEU A  58      19.353 -14.126  27.908  1.00 18.31           C  
ANISOU  460  CA  LEU A  58     2064   2478   2414    -36   -557    464       C  
ATOM    461  C   LEU A  58      19.824 -15.379  28.634  1.00 18.99           C  
ANISOU  461  C   LEU A  58     2077   2577   2561    -45   -564    529       C  
ATOM    462  O   LEU A  58      19.291 -16.458  28.361  1.00 19.97           O  
ANISOU  462  O   LEU A  58     2154   2705   2731    -10   -514    525       O  
ATOM    463  CB  LEU A  58      20.098 -13.912  26.579  1.00 18.33           C  
ANISOU  463  CB  LEU A  58     2030   2459   2476    -42   -534    458       C  
ATOM    464  CG  LEU A  58      19.768 -14.878  25.447  1.00 19.20           C  
ANISOU  464  CG  LEU A  58     2085   2557   2651     -5   -460    438       C  
ATOM    465  CD1 LEU A  58      18.284 -14.903  25.133  1.00 18.38           C  
ANISOU  465  CD1 LEU A  58     2022   2459   2502     35   -423    379       C  
ATOM    466  CD2 LEU A  58      20.620 -14.581  24.225  1.00 20.01           C  
ANISOU  466  CD2 LEU A  58     2163   2637   2805    -13   -438    438       C  
ATOM    467  N   ILE A  59      20.748 -15.251  29.613  1.00 18.93           N  
ANISOU  467  N   ILE A  59     2065   2578   2550    -94   -630    590       N  
ATOM    468  CA  ILE A  59      21.213 -16.402  30.410  1.00 20.28           C  
ANISOU  468  CA  ILE A  59     2165   2764   2778   -106   -643    661       C  
ATOM    469  C   ILE A  59      20.039 -17.065  31.138  1.00 20.86           C  
ANISOU  469  C   ILE A  59     2255   2857   2813    -69   -619    643       C  
ATOM    470  O   ILE A  59      20.042 -18.276  31.340  1.00 21.11           O  
ANISOU  470  O   ILE A  59     2214   2898   2908    -55   -597    681       O  
ATOM    471  CB  ILE A  59      22.308 -15.997  31.439  1.00 22.03           C  
ANISOU  471  CB  ILE A  59     2392   2992   2986   -174   -732    734       C  
ATOM    472  CG1 ILE A  59      23.587 -15.552  30.751  1.00 24.25           C  
ANISOU  472  CG1 ILE A  59     2630   3255   3329   -213   -757    777       C  
ATOM    473  CG2 ILE A  59      22.606 -17.132  32.438  1.00 23.10           C  
ANISOU  473  CG2 ILE A  59     2463   3149   3164   -188   -750    808       C  
ATOM    474  CD1 ILE A  59      24.600 -14.933  31.734  1.00 26.45           C  
ANISOU  474  CD1 ILE A  59     2926   3538   3584   -292   -861    852       C  
ATOM    475  N   ARG A  60      19.043 -16.267  31.544  1.00 21.21           N  
ANISOU  475  N   ARG A  60     2395   2907   2757    -51   -622    591       N  
ATOM    476  CA  ARG A  60      17.885 -16.790  32.250  1.00 22.07           C  
ANISOU  476  CA  ARG A  60     2522   3034   2828    -12   -596    581       C  
ATOM    477  C   ARG A  60      16.844 -17.440  31.336  1.00 21.30           C  
ANISOU  477  C   ARG A  60     2388   2934   2769     44   -524    543       C  
ATOM    478  O   ARG A  60      15.812 -17.882  31.826  1.00 22.28           O  
ANISOU  478  O   ARG A  60     2522   3074   2870     80   -500    539       O  
ATOM    479  CB  ARG A  60      17.247 -15.694  33.120  1.00 24.65           C  
ANISOU  479  CB  ARG A  60     2970   3364   3034    -11   -620    552       C  
ATOM    480  CG  ARG A  60      18.246 -14.947  33.999  1.00 29.44           C  
ANISOU  480  CG  ARG A  60     3633   3965   3587    -77   -701    585       C  
ATOM    481  CD  ARG A  60      18.917 -15.852  35.008  1.00 33.62           C  
ANISOU  481  CD  ARG A  60     4112   4515   4147   -112   -745    661       C  
ATOM    482  NE  ARG A  60      20.227 -15.335  35.399  1.00 37.98           N  
ANISOU  482  NE  ARG A  60     4675   5059   4695   -189   -830    711       N  
ATOM    483  CZ  ARG A  60      21.142 -16.030  36.067  1.00 40.16           C  
ANISOU  483  CZ  ARG A  60     4890   5351   5020   -237   -881    793       C  
ATOM    484  NH1 ARG A  60      22.307 -15.479  36.372  1.00 39.79           N  
ANISOU  484  NH1 ARG A  60     4853   5294   4970   -313   -964    846       N  
ATOM    485  NH2 ARG A  60      20.898 -17.284  36.432  1.00 40.17           N  
ANISOU  485  NH2 ARG A  60     4813   5375   5075   -212   -853    830       N  
ATOM    486  N   LYS A  61      17.089 -17.491  30.014  1.00 19.36           N  
ANISOU  486  N   LYS A  61     2107   2668   2580     50   -491    517       N  
ATOM    487  CA  LYS A  61      16.134 -18.067  29.078  1.00 18.81           C  
ANISOU  487  CA  LYS A  61     2015   2591   2540     92   -432    481       C  
ATOM    488  C   LYS A  61      16.645 -19.373  28.501  1.00 19.17           C  
ANISOU  488  C   LYS A  61     1973   2624   2687     94   -401    509       C  
ATOM    489  O   LYS A  61      17.832 -19.513  28.216  1.00 20.35           O  
ANISOU  489  O   LYS A  61     2081   2760   2892     68   -408    540       O  
ATOM    490  CB  LYS A  61      15.853 -17.072  27.936  1.00 19.82           C  
ANISOU  490  CB  LYS A  61     2188   2701   2642     98   -414    424       C  
ATOM    491  CG  LYS A  61      15.324 -15.717  28.401  1.00 22.51           C  
ANISOU  491  CG  LYS A  61     2620   3046   2885    101   -435    394       C  
ATOM    492  CD  LYS A  61      14.023 -15.821  29.196  1.00 26.00           C  
ANISOU  492  CD  LYS A  61     3096   3507   3275    139   -418    394       C  
ATOM    493  CE  LYS A  61      13.493 -14.456  29.568  1.00 29.36           C  
ANISOU  493  CE  LYS A  61     3620   3928   3608    150   -423    363       C  
ATOM    494  NZ  LYS A  61      12.260 -14.538  30.405  1.00 32.04           N  
ANISOU  494  NZ  LYS A  61     3994   4282   3897    193   -397    373       N  
ATOM    495  N   SER A  62      15.745 -20.338  28.359  1.00 17.84           N  
ANISOU  495  N   SER A  62     1776   2457   2545    125   -365    504       N  
ATOM    496  CA  SER A  62      16.030 -21.625  27.751  1.00 17.70           C  
ANISOU  496  CA  SER A  62     1690   2418   2617    132   -327    521       C  
ATOM    497  C   SER A  62      15.168 -21.747  26.476  1.00 16.11           C  
ANISOU  497  C   SER A  62     1510   2194   2419    152   -285    468       C  
ATOM    498  O   SER A  62      14.219 -20.985  26.286  1.00 15.44           O  
ANISOU  498  O   SER A  62     1477   2118   2273    164   -288    431       O  
ATOM    499  CB  SER A  62      15.673 -22.756  28.709  1.00 20.52           C  
ANISOU  499  CB  SER A  62     2000   2793   3004    144   -328    566       C  
ATOM    500  OG  SER A  62      16.454 -22.685  29.891  1.00 23.82           O  
ANISOU  500  OG  SER A  62     2401   3234   3417    120   -372    620       O  
ATOM    501  N   ASN A  63      15.466 -22.730  25.611  1.00 15.74           N  
ANISOU  501  N   ASN A  63     1426   2113   2442    155   -244    467       N  
ATOM    502  CA  ASN A  63      14.663 -22.963  24.399  1.00 15.24           C  
ANISOU  502  CA  ASN A  63     1389   2022   2378    164   -210    420       C  
ATOM    503  C   ASN A  63      13.166 -23.023  24.663  1.00 15.14           C  
ANISOU  503  C   ASN A  63     1396   2029   2325    181   -221    410       C  
ATOM    504  O   ASN A  63      12.399 -22.427  23.914  1.00 15.00           O  
ANISOU  504  O   ASN A  63     1422   2008   2270    182   -218    372       O  
ATOM    505  CB  ASN A  63      15.077 -24.261  23.732  1.00 15.61           C  
ANISOU  505  CB  ASN A  63     1400   2028   2503    167   -165    429       C  
ATOM    506  CG  ASN A  63      16.449 -24.203  23.162  1.00 17.36           C  
ANISOU  506  CG  ASN A  63     1606   2220   2770    158   -136    440       C  
ATOM    507  OD1 ASN A  63      16.926 -23.144  22.757  1.00 17.17           O  
ANISOU  507  OD1 ASN A  63     1610   2198   2717    147   -145    422       O  
ATOM    508  ND2 ASN A  63      17.110 -25.341  23.087  1.00 17.34           N  
ANISOU  508  ND2 ASN A  63     1556   2186   2845    164    -96    474       N  
ATOM    509  N   HIS A  64      12.750 -23.729  25.736  1.00 15.18           N  
ANISOU  509  N   HIS A  64     1366   2058   2344    194   -233    450       N  
ATOM    510  CA  HIS A  64      11.332 -23.876  26.064  1.00 15.34           C  
ANISOU  510  CA  HIS A  64     1395   2098   2337    214   -239    456       C  
ATOM    511  C   HIS A  64      10.643 -22.586  26.518  1.00 15.59           C  
ANISOU  511  C   HIS A  64     1476   2159   2288    228   -257    445       C  
ATOM    512  O   HIS A  64       9.414 -22.564  26.635  1.00 16.33           O  
ANISOU  512  O   HIS A  64     1578   2267   2361    249   -255    453       O  
ATOM    513  CB  HIS A  64      11.090 -25.001  27.087  1.00 16.13           C  
ANISOU  513  CB  HIS A  64     1440   2214   2474    228   -243    507       C  
ATOM    514  CG  HIS A  64      11.550 -24.698  28.481  1.00 17.26           C  
ANISOU  514  CG  HIS A  64     1574   2393   2592    231   -269    545       C  
ATOM    515  ND1 HIS A  64      12.805 -25.063  28.912  1.00 18.51           N  
ANISOU  515  ND1 HIS A  64     1694   2548   2790    213   -277    575       N  
ATOM    516  CD2 HIS A  64      10.890 -24.109  29.506  1.00 18.35           C  
ANISOU  516  CD2 HIS A  64     1738   2566   2667    250   -286    562       C  
ATOM    517  CE1 HIS A  64      12.887 -24.663  30.171  1.00 18.91           C  
ANISOU  517  CE1 HIS A  64     1754   2634   2797    213   -308    606       C  
ATOM    518  NE2 HIS A  64      11.768 -24.069  30.566  1.00 19.00           N  
ANISOU  518  NE2 HIS A  64     1810   2667   2742    237   -311    595       N  
ATOM    519  N   ASN A  65      11.413 -21.525  26.808  1.00 14.89           N  
ANISOU  519  N   ASN A  65     1421   2078   2157    217   -274    433       N  
ATOM    520  CA  ASN A  65      10.825 -20.244  27.197  1.00 15.45           C  
ANISOU  520  CA  ASN A  65     1553   2168   2150    231   -285    418       C  
ATOM    521  C   ASN A  65      10.364 -19.437  25.979  1.00 15.62           C  
ANISOU  521  C   ASN A  65     1613   2173   2150    229   -272    373       C  
ATOM    522  O   ASN A  65       9.615 -18.487  26.144  1.00 16.44           O  
ANISOU  522  O   ASN A  65     1761   2288   2198    247   -271    365       O  
ATOM    523  CB  ASN A  65      11.814 -19.399  27.993  1.00 16.32           C  
ANISOU  523  CB  ASN A  65     1695   2287   2218    213   -315    422       C  
ATOM    524  CG  ASN A  65      12.130 -19.936  29.354  1.00 20.06           C  
ANISOU  524  CG  ASN A  65     2148   2782   2691    212   -336    470       C  
ATOM    525  OD1 ASN A  65      13.288 -19.972  29.757  1.00 21.53           O  
ANISOU  525  OD1 ASN A  65     2319   2968   2893    182   -363    491       O  
ATOM    526  ND2 ASN A  65      11.113 -20.354  30.094  1.00 20.32           N  
ANISOU  526  ND2 ASN A  65     2177   2836   2708    243   -325    495       N  
ATOM    527  N   PHE A  66      10.834 -19.782  24.766  1.00 14.81           N  
ANISOU  527  N   PHE A  66     1497   2042   2089    208   -259    348       N  
ATOM    528  CA  PHE A  66      10.445 -19.072  23.556  1.00 14.55           C  
ANISOU  528  CA  PHE A  66     1500   1993   2036    201   -250    308       C  
ATOM    529  C   PHE A  66       9.285 -19.790  22.901  1.00 15.70           C  
ANISOU  529  C   PHE A  66     1633   2130   2202    205   -239    311       C  
ATOM    530  O   PHE A  66       9.473 -20.833  22.284  1.00 17.06           O  
ANISOU  530  O   PHE A  66     1783   2277   2423    190   -227    309       O  
ATOM    531  CB  PHE A  66      11.624 -18.973  22.581  1.00 13.81           C  
ANISOU  531  CB  PHE A  66     1409   1871   1969    175   -240    280       C  
ATOM    532  CG  PHE A  66      12.755 -18.158  23.140  1.00 14.30           C  
ANISOU  532  CG  PHE A  66     1481   1940   2013    164   -260    284       C  
ATOM    533  CD1 PHE A  66      12.739 -16.779  23.058  1.00 15.07           C  
ANISOU  533  CD1 PHE A  66     1628   2043   2053    161   -275    261       C  
ATOM    534  CD2 PHE A  66      13.840 -18.771  23.734  1.00 14.97           C  
ANISOU  534  CD2 PHE A  66     1524   2022   2140    153   -266    318       C  
ATOM    535  CE1 PHE A  66      13.791 -16.027  23.574  1.00 15.66           C  
ANISOU  535  CE1 PHE A  66     1717   2122   2112    143   -302    269       C  
ATOM    536  CE2 PHE A  66      14.884 -18.017  24.257  1.00 15.64           C  
ANISOU  536  CE2 PHE A  66     1617   2114   2212    134   -295    333       C  
ATOM    537  CZ  PHE A  66      14.840 -16.648  24.190  1.00 15.18           C  
ANISOU  537  CZ  PHE A  66     1615   2061   2093    127   -316    307       C  
ATOM    538  N   LEU A  67       8.095 -19.249  23.059  1.00 14.73           N  
ANISOU  538  N   LEU A  67     1528   2026   2045    223   -242    323       N  
ATOM    539  CA  LEU A  67       6.890 -19.851  22.496  1.00 15.02           C  
ANISOU  539  CA  LEU A  67     1549   2058   2102    223   -241    341       C  
ATOM    540  C   LEU A  67       6.660 -19.315  21.087  1.00 14.82           C  
ANISOU  540  C   LEU A  67     1556   2011   2063    197   -242    307       C  
ATOM    541  O   LEU A  67       6.407 -18.125  20.903  1.00 14.57           O  
ANISOU  541  O   LEU A  67     1556   1989   1989    204   -242    295       O  
ATOM    542  CB  LEU A  67       5.687 -19.563  23.389  1.00 16.22           C  
ANISOU  542  CB  LEU A  67     1694   2240   2231    259   -240    387       C  
ATOM    543  CG  LEU A  67       5.825 -20.012  24.845  1.00 19.15           C  
ANISOU  543  CG  LEU A  67     2040   2634   2603    286   -238    424       C  
ATOM    544  CD1 LEU A  67       4.603 -19.600  25.664  1.00 20.19           C  
ANISOU  544  CD1 LEU A  67     2174   2792   2706    330   -225    471       C  
ATOM    545  CD2 LEU A  67       6.082 -21.512  24.947  1.00 20.70           C  
ANISOU  545  CD2 LEU A  67     2184   2820   2861    273   -243    444       C  
ATOM    546  N   VAL A  68       6.797 -20.185  20.094  1.00 13.69           N  
ANISOU  546  N   VAL A  68     1411   1836   1954    166   -241    291       N  
ATOM    547  CA  VAL A  68       6.672 -19.779  18.702  1.00 13.84           C  
ANISOU  547  CA  VAL A  68     1470   1832   1958    135   -243    257       C  
ATOM    548  C   VAL A  68       5.478 -20.455  18.106  1.00 14.57           C  
ANISOU  548  C   VAL A  68     1559   1913   2065    113   -262    282       C  
ATOM    549  O   VAL A  68       5.380 -21.671  18.188  1.00 14.93           O  
ANISOU  549  O   VAL A  68     1585   1941   2148    103   -265    298       O  
ATOM    550  CB  VAL A  68       7.958 -20.136  17.936  1.00 14.82           C  
ANISOU  550  CB  VAL A  68     1612   1918   2099    114   -221    215       C  
ATOM    551  CG1 VAL A  68       7.847 -19.711  16.467  1.00 14.89           C  
ANISOU  551  CG1 VAL A  68     1670   1902   2084     82   -220    178       C  
ATOM    552  CG2 VAL A  68       9.173 -19.485  18.597  1.00 15.58           C  
ANISOU  552  CG2 VAL A  68     1702   2028   2190    132   -210    205       C  
ATOM    553  N   GLN A  69       4.540 -19.672  17.571  1.00 14.79           N  
ANISOU  553  N   GLN A  69     1602   1952   2065    104   -278    294       N  
ATOM    554  CA  GLN A  69       3.320 -20.238  17.038  1.00 16.19           C  
ANISOU  554  CA  GLN A  69     1772   2122   2259     77   -307    333       C  
ATOM    555  C   GLN A  69       3.083 -19.685  15.636  1.00 17.21           C  
ANISOU  555  C   GLN A  69     1946   2232   2361     33   -323    309       C  
ATOM    556  O   GLN A  69       3.122 -18.475  15.425  1.00 16.72           O  
ANISOU  556  O   GLN A  69     1901   2187   2267     43   -316    296       O  
ATOM    557  CB  GLN A  69       2.170 -19.888  17.999  1.00 18.04           C  
ANISOU  557  CB  GLN A  69     1963   2396   2497    114   -313    402       C  
ATOM    558  CG  GLN A  69       0.888 -20.656  17.771  1.00 21.51           C  
ANISOU  558  CG  GLN A  69     2373   2833   2968     91   -347    466       C  
ATOM    559  CD  GLN A  69      -0.161 -20.174  18.731  1.00 25.03           C  
ANISOU  559  CD  GLN A  69     2773   3317   3418    139   -339    540       C  
ATOM    560  OE1 GLN A  69       0.106 -19.927  19.909  1.00 25.84           O  
ANISOU  560  OE1 GLN A  69     2862   3444   3514    190   -309    547       O  
ATOM    561  NE2 GLN A  69      -1.385 -20.021  18.241  1.00 26.21           N  
ANISOU  561  NE2 GLN A  69     2905   3473   3582    121   -365    602       N  
ATOM    562  N   ALA A  70       2.875 -20.594  14.677  1.00 19.00           N  
ANISOU  562  N   ALA A  70     2201   2421   2599    -17   -344    301       N  
ATOM    563  CA  ALA A  70       2.620 -20.293  13.267  1.00 20.96           C  
ANISOU  563  CA  ALA A  70     2502   2644   2818    -71   -366    280       C  
ATOM    564  C   ALA A  70       1.139 -20.600  13.043  1.00 23.17           C  
ANISOU  564  C   ALA A  70     2762   2930   3110   -104   -418    350       C  
ATOM    565  O   ALA A  70       0.751 -21.762  13.002  1.00 23.52           O  
ANISOU  565  O   ALA A  70     2803   2952   3183   -131   -442    374       O  
ATOM    566  CB  ALA A  70       3.471 -21.204  12.398  1.00 20.97           C  
ANISOU  566  CB  ALA A  70     2561   2590   2818   -106   -351    226       C  
ATOM    567  N   GLY A  71       0.297 -19.573  13.046  1.00 24.68           N  
ANISOU  567  N   GLY A  71     2932   3155   3291    -97   -433    393       N  
ATOM    568  CA  GLY A  71      -1.148 -19.764  12.969  1.00 25.82           C  
ANISOU  568  CA  GLY A  71     3039   3312   3459   -122   -480    480       C  
ATOM    569  C   GLY A  71      -1.586 -20.403  14.272  1.00 26.30           C  
ANISOU  569  C   GLY A  71     3035   3394   3562    -76   -472    536       C  
ATOM    570  O   GLY A  71      -1.283 -19.875  15.340  1.00 27.29           O  
ANISOU  570  O   GLY A  71     3133   3550   3687    -11   -430    534       O  
ATOM    571  N  AASN A  72      -2.203 -21.577  14.195  0.50 25.88           N  
ANISOU  571  N  AASN A  72     2967   3324   3544   -112   -512    581       N  
ATOM    572  N  BASN A  72      -2.232 -21.574  14.208  0.50 26.13           N  
ANISOU  572  N  BASN A  72     2996   3356   3576   -112   -512    583       N  
ATOM    573  CA AASN A  72      -2.607 -22.309  15.390  0.50 25.81           C  
ANISOU  573  CA AASN A  72     2894   3333   3579    -72   -506    637       C  
ATOM    574  CA BASN A  72      -2.637 -22.282  15.426  0.50 26.29           C  
ANISOU  574  CA BASN A  72     2953   3396   3641    -70   -505    639       C  
ATOM    575  C  AASN A  72      -1.585 -23.402  15.775  0.50 25.30           C  
ANISOU  575  C  AASN A  72     2844   3241   3527    -65   -484    581       C  
ATOM    576  C  BASN A  72      -1.713 -23.458  15.794  0.50 25.45           C  
ANISOU  576  C  BASN A  72     2858   3261   3550    -67   -489    590       C  
ATOM    577  O  AASN A  72      -1.765 -24.044  16.810  0.50 25.73           O  
ANISOU  577  O  AASN A  72     2848   3311   3618    -30   -476    620       O  
ATOM    578  O  BASN A  72      -2.036 -24.222  16.705  0.50 25.81           O  
ANISOU  578  O  BASN A  72     2853   3318   3635    -41   -489    637       O  
ATOM    579  CB AASN A  72      -3.990 -22.935  15.174  0.50 27.13           C  
ANISOU  579  CB AASN A  72     3023   3498   3786   -113   -566    734       C  
ATOM    580  CB BASN A  72      -4.102 -22.729  15.351  0.50 28.37           C  
ANISOU  580  CB BASN A  72     3169   3666   3945   -100   -560    746       C  
ATOM    581  CG AASN A  72      -4.706 -23.325  16.447  0.50 29.97           C  
ANISOU  581  CG AASN A  72     3301   3891   4194    -61   -557    819       C  
ATOM    582  CG BASN A  72      -4.444 -23.658  14.208  0.50 32.49           C  
ANISOU  582  CG BASN A  72     3733   4141   4471   -192   -627    749       C  
ATOM    583  OD1AASN A  72      -4.849 -22.526  17.378  0.50 30.90           O  
ANISOU  583  OD1AASN A  72     3382   4048   4309     10   -511    846       O  
ATOM    584  OD1BASN A  72      -3.749 -24.647  13.927  0.50 34.05           O  
ANISOU  584  OD1BASN A  72     3977   4295   4666   -221   -629    691       O  
ATOM    585  ND2AASN A  72      -5.171 -24.566  16.514  0.50 30.55           N  
ANISOU  585  ND2AASN A  72     3352   3945   4310    -93   -598    863       N  
ATOM    586  ND2BASN A  72      -5.547 -23.372  13.532  0.50 33.10           N  
ANISOU  586  ND2BASN A  72     3798   4222   4556   -241   -683    824       N  
ATOM    587  N  AVAL A  73      -0.530 -23.633  14.956  0.75 24.08           N  
ANISOU  587  N  AVAL A  73     2756   3045   3347    -96   -471    497       N  
ATOM    588  N  BVAL A  73      -0.584 -23.618  15.080  0.25 23.95           N  
ANISOU  588  N  BVAL A  73     2733   3034   3335    -91   -471    504       N  
ATOM    589  CA AVAL A  73       0.414 -24.705  15.245  0.75 23.44           C  
ANISOU  589  CA AVAL A  73     2687   2933   3288    -90   -446    455       C  
ATOM    590  CA BVAL A  73       0.344 -24.718  15.304  0.25 22.97           C  
ANISOU  590  CA BVAL A  73     2623   2875   3231    -89   -448    461       C  
ATOM    591  C  AVAL A  73       1.668 -24.214  15.976  0.75 21.47           C  
ANISOU  591  C  AVAL A  73     2429   2701   3030    -34   -389    407       C  
ATOM    592  C  BVAL A  73       1.640 -24.244  15.966  0.25 21.72           C  
ANISOU  592  C  BVAL A  73     2460   2730   3061    -36   -390    408       C  
ATOM    593  O  AVAL A  73       2.283 -23.222  15.597  0.75 20.54           O  
ANISOU  593  O  AVAL A  73     2341   2588   2876    -27   -367    363       O  
ATOM    594  O  BVAL A  73       2.279 -23.304  15.502  0.25 21.51           O  
ANISOU  594  O  BVAL A  73     2468   2705   2999    -32   -369    361       O  
ATOM    595  CB AVAL A  73       0.763 -25.565  14.001  0.75 24.81           C  
ANISOU  595  CB AVAL A  73     2938   3038   3449   -155   -460    407       C  
ATOM    596  CB BVAL A  73       0.577 -25.518  13.997  0.25 23.51           C  
ANISOU  596  CB BVAL A  73     2769   2878   3287   -159   -468    418       C  
ATOM    597  CG1AVAL A  73       1.636 -24.807  13.009  0.75 25.84           C  
ANISOU  597  CG1AVAL A  73     3138   3149   3532   -169   -432    334       C  
ATOM    598  CG1BVAL A  73       1.798 -26.431  14.097  0.25 24.00           C  
ANISOU  598  CG1BVAL A  73     2857   2897   3364   -147   -422    361       C  
ATOM    599  CG2AVAL A  73       1.436 -26.868  14.414  0.75 25.38           C  
ANISOU  599  CG2AVAL A  73     3009   3074   3558   -147   -435    388       C  
ATOM    600  CG2BVAL A  73      -0.667 -26.320  13.638  0.25 23.85           C  
ANISOU  600  CG2BVAL A  73     2809   2903   3351   -215   -535    482       C  
ATOM    601  N   GLN A  74       2.014 -24.909  17.059  1.00 20.75           N  
ANISOU  601  N   GLN A  74     2292   2618   2972      2   -370    423       N  
ATOM    602  CA  GLN A  74       3.186 -24.589  17.836  1.00 19.17           C  
ANISOU  602  CA  GLN A  74     2079   2433   2770     46   -327    391       C  
ATOM    603  C   GLN A  74       4.454 -25.134  17.203  1.00 18.22           C  
ANISOU  603  C   GLN A  74     2000   2265   2658     28   -296    331       C  
ATOM    604  O   GLN A  74       4.478 -26.264  16.693  1.00 18.47           O  
ANISOU  604  O   GLN A  74     2053   2250   2715     -2   -298    324       O  
ATOM    605  CB  GLN A  74       3.034 -25.162  19.243  1.00 19.18           C  
ANISOU  605  CB  GLN A  74     2017   2464   2807     86   -322    440       C  
ATOM    606  CG  GLN A  74       3.779 -24.366  20.307  1.00 19.39           C  
ANISOU  606  CG  GLN A  74     2025   2529   2815    135   -293    433       C  
ATOM    607  CD  GLN A  74       3.183 -23.013  20.563  1.00 21.32           C  
ANISOU  607  CD  GLN A  74     2277   2810   3015    159   -294    447       C  
ATOM    608  OE1 GLN A  74       2.013 -22.747  20.265  1.00 21.97           O  
ANISOU  608  OE1 GLN A  74     2352   2901   3093    154   -314    487       O  
ATOM    609  NE2 GLN A  74       3.972 -22.133  21.159  1.00 21.51           N  
ANISOU  609  NE2 GLN A  74     2313   2853   3008    187   -273    422       N  
ATOM    610  N   LEU A  75       5.519 -24.334  17.242  1.00 17.05           N  
ANISOU  610  N   LEU A  75     1864   2124   2489     49   -264    291       N  
ATOM    611  CA  LEU A  75       6.809 -24.770  16.729  1.00 17.04           C  
ANISOU  611  CA  LEU A  75     1892   2081   2503     42   -224    246       C  
ATOM    612  C   LEU A  75       7.735 -25.145  17.865  1.00 16.56           C  
ANISOU  612  C   LEU A  75     1778   2034   2479     79   -199    263       C  
ATOM    613  O   LEU A  75       7.725 -24.505  18.912  1.00 17.40           O  
ANISOU  613  O   LEU A  75     1848   2187   2575    108   -208    287       O  
ATOM    614  CB  LEU A  75       7.454 -23.702  15.837  1.00 17.69           C  
ANISOU  614  CB  LEU A  75     2020   2155   2545     34   -207    199       C  
ATOM    615  CG  LEU A  75       6.621 -23.233  14.636  1.00 19.89           C  
ANISOU  615  CG  LEU A  75     2354   2421   2782     -7   -233    183       C  
ATOM    616  CD1 LEU A  75       7.402 -22.256  13.792  1.00 20.45           C  
ANISOU  616  CD1 LEU A  75     2468   2484   2818    -12   -210    136       C  
ATOM    617  CD2 LEU A  75       6.150 -24.405  13.778  1.00 21.66           C  
ANISOU  617  CD2 LEU A  75     2622   2593   3016    -52   -245    178       C  
ATOM    618  N   ARG A  76       8.516 -26.197  17.669  1.00 14.98           N  
ANISOU  618  N   ARG A  76     1580   1790   2321     75   -166    253       N  
ATOM    619  CA  ARG A  76       9.440 -26.670  18.686  1.00 14.65           C  
ANISOU  619  CA  ARG A  76     1483   1758   2325    104   -142    278       C  
ATOM    620  C   ARG A  76      10.784 -25.974  18.535  1.00 15.18           C  
ANISOU  620  C   ARG A  76     1556   1822   2391    115   -110    257       C  
ATOM    621  O   ARG A  76      11.405 -26.099  17.487  1.00 16.02           O  
ANISOU  621  O   ARG A  76     1705   1882   2501    103    -73    224       O  
ATOM    622  CB  ARG A  76       9.611 -28.184  18.570  1.00 15.16           C  
ANISOU  622  CB  ARG A  76     1542   1774   2447     98   -118    289       C  
ATOM    623  CG  ARG A  76      10.429 -28.788  19.702  1.00 15.73           C  
ANISOU  623  CG  ARG A  76     1544   1859   2574    127    -99    329       C  
ATOM    624  CD  ARG A  76      10.493 -30.311  19.588  1.00 16.39           C  
ANISOU  624  CD  ARG A  76     1620   1890   2716    122    -73    342       C  
ATOM    625  NE  ARG A  76       9.152 -30.898  19.628  1.00 17.45           N  
ANISOU  625  NE  ARG A  76     1758   2025   2848    104   -115    359       N  
ATOM    626  CZ  ARG A  76       8.486 -31.179  20.744  1.00 18.47           C  
ANISOU  626  CZ  ARG A  76     1826   2198   2994    120   -148    409       C  
ATOM    627  NH1 ARG A  76       9.049 -30.980  21.932  1.00 17.24           N  
ANISOU  627  NH1 ARG A  76     1608   2087   2855    151   -144    443       N  
ATOM    628  NH2 ARG A  76       7.256 -31.675  20.681  1.00 18.11           N  
ANISOU  628  NH2 ARG A  76     1781   2151   2948    101   -186    432       N  
ATOM    629  N   VAL A  77      11.234 -25.254  19.574  1.00 14.60           N  
ANISOU  629  N   VAL A  77     1442   1795   2310    136   -124    281       N  
ATOM    630  CA  VAL A  77      12.504 -24.530  19.581  1.00 14.79           C  
ANISOU  630  CA  VAL A  77     1462   1822   2336    142   -106    274       C  
ATOM    631  C   VAL A  77      13.634 -25.433  20.060  1.00 15.27           C  
ANISOU  631  C   VAL A  77     1473   1863   2465    153    -74    309       C  
ATOM    632  O   VAL A  77      13.610 -25.910  21.200  1.00 15.58           O  
ANISOU  632  O   VAL A  77     1462   1929   2530    164    -91    352       O  
ATOM    633  CB  VAL A  77      12.396 -23.241  20.417  1.00 14.63           C  
ANISOU  633  CB  VAL A  77     1438   1855   2267    150   -144    283       C  
ATOM    634  CG1 VAL A  77      13.738 -22.496  20.457  1.00 15.23           C  
ANISOU  634  CG1 VAL A  77     1508   1931   2347    148   -136    284       C  
ATOM    635  CG2 VAL A  77      11.286 -22.353  19.859  1.00 15.19           C  
ANISOU  635  CG2 VAL A  77     1555   1939   2278    143   -166    254       C  
ATOM    636  N   ILE A  78      14.606 -25.704  19.183  1.00 14.95           N  
ANISOU  636  N   ILE A  78     1447   1776   2457    151    -24    296       N  
ATOM    637  CA  ILE A  78      15.726 -26.579  19.519  1.00 15.44           C  
ANISOU  637  CA  ILE A  78     1458   1813   2595    165     18    339       C  
ATOM    638  C   ILE A  78      17.072 -25.865  19.681  1.00 15.44           C  
ANISOU  638  C   ILE A  78     1428   1822   2617    169     29    366       C  
ATOM    639  O   ILE A  78      18.089 -26.513  19.933  1.00 16.12           O  
ANISOU  639  O   ILE A  78     1463   1887   2773    181     65    414       O  
ATOM    640  CB  ILE A  78      15.821 -27.724  18.493  1.00 16.42           C  
ANISOU  640  CB  ILE A  78     1617   1865   2757    167     81    319       C  
ATOM    641  CG1 ILE A  78      16.122 -27.179  17.085  1.00 17.67           C  
ANISOU  641  CG1 ILE A  78     1846   1983   2883    159    119    270       C  
ATOM    642  CG2 ILE A  78      14.532 -28.525  18.490  1.00 16.90           C  
ANISOU  642  CG2 ILE A  78     1700   1918   2805    156     57    305       C  
ATOM    643  CD1 ILE A  78      16.430 -28.295  16.044  1.00 18.94           C  
ANISOU  643  CD1 ILE A  78     2057   2061   3078    164    196    251       C  
ATOM    644  N   GLY A  79      17.071 -24.547  19.607  1.00 15.03           N  
ANISOU  644  N   GLY A  79     1401   1801   2510    159     -6    346       N  
ATOM    645  CA  GLY A  79      18.273 -23.758  19.811  1.00 15.04           C  
ANISOU  645  CA  GLY A  79     1374   1814   2527    155    -10    377       C  
ATOM    646  C   GLY A  79      17.946 -22.286  19.759  1.00 15.10           C  
ANISOU  646  C   GLY A  79     1422   1855   2460    141    -57    345       C  
ATOM    647  O   GLY A  79      16.938 -21.896  19.168  1.00 14.94           O  
ANISOU  647  O   GLY A  79     1454   1836   2384    138    -65    295       O  
ATOM    648  N   HIS A  80      18.773 -21.465  20.388  1.00 14.85           N  
ANISOU  648  N   HIS A  80     1366   1849   2427    130    -91    379       N  
ATOM    649  CA  HIS A  80      18.582 -20.020  20.321  1.00 14.66           C  
ANISOU  649  CA  HIS A  80     1385   1849   2335    116   -132    350       C  
ATOM    650  C   HIS A  80      19.904 -19.333  20.423  1.00 15.30           C  
ANISOU  650  C   HIS A  80     1440   1931   2443    101   -145    390       C  
ATOM    651  O   HIS A  80      20.814 -19.802  21.123  1.00 15.86           O  
ANISOU  651  O   HIS A  80     1452   2003   2570     95   -151    455       O  
ATOM    652  CB  HIS A  80      17.588 -19.490  21.366  1.00 14.91           C  
ANISOU  652  CB  HIS A  80     1439   1924   2301    114   -188    341       C  
ATOM    653  CG  HIS A  80      18.070 -19.617  22.771  1.00 16.66           C  
ANISOU  653  CG  HIS A  80     1623   2172   2534    105   -229    397       C  
ATOM    654  ND1 HIS A  80      17.910 -20.787  23.482  1.00 17.48           N  
ANISOU  654  ND1 HIS A  80     1682   2281   2678    115   -222    432       N  
ATOM    655  CD2 HIS A  80      18.705 -18.716  23.556  1.00 17.84           C  
ANISOU  655  CD2 HIS A  80     1778   2344   2659     82   -280    424       C  
ATOM    656  CE1 HIS A  80      18.440 -20.563  24.674  1.00 18.30           C  
ANISOU  656  CE1 HIS A  80     1764   2412   2779     98   -268    480       C  
ATOM    657  NE2 HIS A  80      18.929 -19.326  24.760  1.00 18.47           N  
ANISOU  657  NE2 HIS A  80     1818   2442   2758     76   -306    477       N  
ATOM    658  N   SER A  81      20.031 -18.237  19.705  1.00 14.84           N  
ANISOU  658  N   SER A  81     1420   1870   2347     92   -151    359       N  
ATOM    659  CA  SER A  81      21.265 -17.465  19.755  1.00 14.86           C  
ANISOU  659  CA  SER A  81     1398   1873   2373     74   -171    401       C  
ATOM    660  C   SER A  81      20.972 -16.018  19.462  1.00 14.66           C  
ANISOU  660  C   SER A  81     1430   1863   2279     59   -208    359       C  
ATOM    661  O   SER A  81      19.970 -15.697  18.822  1.00 15.19           O  
ANISOU  661  O   SER A  81     1548   1929   2294     69   -196    299       O  
ATOM    662  CB  SER A  81      22.291 -18.011  18.768  1.00 16.73           C  
ANISOU  662  CB  SER A  81     1600   2070   2686     87   -103    429       C  
ATOM    663  OG  SER A  81      21.809 -17.919  17.441  1.00 20.31           O  
ANISOU  663  OG  SER A  81     2105   2497   3114    102    -53    368       O  
ATOM    664  N  AMET A  82      21.828 -15.125  19.951  0.50 14.30           N  
ANISOU  664  N  AMET A  82     1375   1829   2230     32   -258    397       N  
ATOM    665  N  BMET A  82      21.839 -15.141  19.938  0.50 14.04           N  
ANISOU  665  N  BMET A  82     1341   1796   2199     33   -256    397       N  
ATOM    666  CA AMET A  82      21.664 -13.700  19.723  0.50 14.74           C  
ANISOU  666  CA AMET A  82     1484   1893   2223     16   -295    362       C  
ATOM    667  CA BMET A  82      21.699 -13.721  19.712  0.50 14.21           C  
ANISOU  667  CA BMET A  82     1415   1826   2160     16   -294    364       C  
ATOM    668  C  AMET A  82      22.712 -13.224  18.723  0.50 15.23           C  
ANISOU  668  C  AMET A  82     1526   1934   2328     10   -272    382       C  
ATOM    669  C  BMET A  82      22.718 -13.294  18.664  0.50 14.88           C  
ANISOU  669  C  BMET A  82     1480   1888   2288     12   -266    382       C  
ATOM    670  O  AMET A  82      23.905 -13.470  18.919  0.50 16.17           O  
ANISOU  670  O  AMET A  82     1586   2045   2514     -2   -274    453       O  
ATOM    671  O  BMET A  82      23.890 -13.665  18.753  0.50 15.61           O  
ANISOU  671  O  BMET A  82     1511   1969   2453      5   -257    451       O  
ATOM    672  CB AMET A  82      21.801 -12.929  21.041  0.50 15.23           C  
ANISOU  672  CB AMET A  82     1567   1980   2242    -15   -375    388       C  
ATOM    673  CB BMET A  82      21.937 -12.966  21.026  0.50 14.18           C  
ANISOU  673  CB BMET A  82     1426   1844   2116    -17   -375    395       C  
ATOM    674  CG AMET A  82      21.614 -11.442  20.874  0.50 17.47           C  
ANISOU  674  CG AMET A  82     1915   2267   2458    -31   -413    351       C  
ATOM    675  CG BMET A  82      21.759 -11.474  20.898  0.50 15.64           C  
ANISOU  675  CG BMET A  82     1675   2033   2234    -34   -415    359       C  
ATOM    676  SD AMET A  82      21.828 -10.548  22.424  0.50 20.86           S  
ANISOU  676  SD AMET A  82     2388   2711   2825    -73   -506    379       S  
ATOM    677  SD BMET A  82      21.374 -10.707  22.484  0.50 15.97           S  
ANISOU  677  SD BMET A  82     1780   2095   2192    -61   -495    362       S  
ATOM    678  CE AMET A  82      20.402 -11.108  23.302  0.50 20.46           C  
ANISOU  678  CE AMET A  82     2376   2679   2717    -43   -496    344       C  
ATOM    679  CE BMET A  82      22.877 -11.090  23.413  0.50 12.42           C  
ANISOU  679  CE BMET A  82     1267   1648   1803   -108   -552    463       C  
ATOM    680  N   GLN A  83      22.270 -12.561  17.647  1.00 15.01           N  
ANISOU  680  N   GLN A  83     1542   1897   2265     19   -248    327       N  
ATOM    681  CA  GLN A  83      23.164 -12.017  16.627  1.00 15.04           C  
ANISOU  681  CA  GLN A  83     1533   1881   2299     16   -223    341       C  
ATOM    682  C   GLN A  83      22.849 -10.536  16.608  1.00 13.84           C  
ANISOU  682  C   GLN A  83     1433   1744   2080     -4   -275    308       C  
ATOM    683  O   GLN A  83      21.761 -10.157  16.187  1.00 14.15           O  
ANISOU  683  O   GLN A  83     1526   1789   2062      6   -269    245       O  
ATOM    684  CB  GLN A  83      22.915 -12.619  15.247  1.00 17.78           C  
ANISOU  684  CB  GLN A  83     1894   2200   2662     45   -140    304       C  
ATOM    685  CG  GLN A  83      23.871 -12.027  14.206  1.00 22.38           C  
ANISOU  685  CG  GLN A  83     2466   2763   3275     46   -109    324       C  
ATOM    686  CD  GLN A  83      23.630 -12.527  12.802  1.00 27.19           C  
ANISOU  686  CD  GLN A  83     3106   3341   3886     72    -26    284       C  
ATOM    687  OE1 GLN A  83      22.667 -13.246  12.515  1.00 27.58           O  
ANISOU  687  OE1 GLN A  83     3192   3381   3906     83      1    235       O  
ATOM    688  NE2 GLN A  83      24.504 -12.142  11.883  1.00 28.65           N  
ANISOU  688  NE2 GLN A  83     3279   3504   4102     79     15    307       N  
ATOM    689  N   ASN A  84      23.741  -9.705  17.152  1.00 13.13           N  
ANISOU  689  N   ASN A  84     1329   1659   1999    -36   -333    354       N  
ATOM    690  CA  ASN A  84      23.516  -8.266  17.264  1.00 12.86           C  
ANISOU  690  CA  ASN A  84     1351   1634   1902    -59   -388    327       C  
ATOM    691  C   ASN A  84      22.187  -8.003  18.043  1.00 12.30           C  
ANISOU  691  C   ASN A  84     1344   1580   1748    -53   -415    273       C  
ATOM    692  O   ASN A  84      22.073  -8.505  19.170  1.00 13.18           O  
ANISOU  692  O   ASN A  84     1453   1703   1853    -60   -442    295       O  
ATOM    693  CB  ASN A  84      23.643  -7.595  15.893  1.00 13.60           C  
ANISOU  693  CB  ASN A  84     1455   1714   1997    -50   -352    300       C  
ATOM    694  CG  ASN A  84      24.979  -7.902  15.287  1.00 16.97           C  
ANISOU  694  CG  ASN A  84     1817   2124   2509    -50   -321    365       C  
ATOM    695  OD1 ASN A  84      26.030  -7.659  15.897  1.00 18.65           O  
ANISOU  695  OD1 ASN A  84     1987   2336   2761    -80   -368    437       O  
ATOM    696  ND2 ASN A  84      24.965  -8.478  14.103  1.00 17.35           N  
ANISOU  696  ND2 ASN A  84     1855   2154   2584    -19   -241    348       N  
ATOM    697  N   CYS A  85      21.183  -7.327  17.448  1.00 11.65           N  
ANISOU  697  N   CYS A  85     1317   1500   1611    -38   -400    211       N  
ATOM    698  CA  CYS A  85      19.935  -7.077  18.150  1.00 11.74           C  
ANISOU  698  CA  CYS A  85     1382   1524   1553    -26   -414    172       C  
ATOM    699  C   CYS A  85      18.805  -8.021  17.785  1.00 11.93           C  
ANISOU  699  C   CYS A  85     1403   1555   1577      7   -364    141       C  
ATOM    700  O   CYS A  85      17.658  -7.743  18.135  1.00 12.25           O  
ANISOU  700  O   CYS A  85     1484   1605   1564     22   -366    113       O  
ATOM    701  CB  CYS A  85      19.518  -5.626  17.998  1.00 12.25           C  
ANISOU  701  CB  CYS A  85     1510   1586   1558    -33   -439    138       C  
ATOM    702  SG  CYS A  85      20.771  -4.475  18.599  1.00 14.49           S  
ANISOU  702  SG  CYS A  85     1812   1858   1834    -81   -513    176       S  
ATOM    703  N   VAL A  86      19.106  -9.142  17.124  1.00 11.92           N  
ANISOU  703  N   VAL A  86     1354   1543   1631     17   -318    152       N  
ATOM    704  CA AVAL A  86      18.063 -10.123  16.816  0.80 12.69           C  
ANISOU  704  CA AVAL A  86     1452   1642   1728     40   -279    128       C  
ATOM    705  CA BVAL A  86      18.084 -10.108  16.770  0.20 12.62           C  
ANISOU  705  CA BVAL A  86     1442   1632   1719     40   -279    127       C  
ATOM    706  C   VAL A  86      18.368 -11.466  17.447  1.00 13.31           C  
ANISOU  706  C   VAL A  86     1483   1718   1854     47   -267    163       C  
ATOM    707  O   VAL A  86      19.522 -11.792  17.744  1.00 13.89           O  
ANISOU  707  O   VAL A  86     1515   1785   1978     36   -272    209       O  
ATOM    708  CB AVAL A  86      17.715 -10.290  15.315  0.80 13.96           C  
ANISOU  708  CB AVAL A  86     1624   1787   1895     47   -232     93       C  
ATOM    709  CB BVAL A  86      17.964 -10.163  15.216  0.20 13.40           C  
ANISOU  709  CB BVAL A  86     1550   1713   1828     44   -232     96       C  
ATOM    710  CG1AVAL A  86      17.232  -8.980  14.704  0.80 14.98           C  
ANISOU  710  CG1AVAL A  86     1797   1922   1975     41   -245     60       C  
ATOM    711  CG1BVAL A  86      17.427 -11.492  14.704  0.20 13.91           C  
ANISOU  711  CG1BVAL A  86     1607   1764   1916     57   -188     85       C  
ATOM    712  CG2AVAL A  86      18.874 -10.884  14.538  0.80 14.71           C  
ANISOU  712  CG2AVAL A  86     1683   1855   2049     46   -191    115       C  
ATOM    713  CG2BVAL A  86      17.115  -9.007  14.699  0.20 14.01           C  
ANISOU  713  CG2BVAL A  86     1676   1800   1849     42   -245     58       C  
ATOM    714  N   LEU A  87      17.311 -12.214  17.743  1.00 12.95           N  
ANISOU  714  N   LEU A  87     1444   1682   1797     63   -256    150       N  
ATOM    715  CA  LEU A  87      17.437 -13.555  18.248  1.00 13.45           C  
ANISOU  715  CA  LEU A  87     1464   1742   1906     72   -239    179       C  
ATOM    716  C   LEU A  87      17.087 -14.460  17.060  1.00 12.81           C  
ANISOU  716  C   LEU A  87     1383   1635   1851     82   -185    155       C  
ATOM    717  O   LEU A  87      16.214 -14.148  16.232  1.00 12.84           O  
ANISOU  717  O   LEU A  87     1425   1635   1819     82   -176    116       O  
ATOM    718  CB  LEU A  87      16.456 -13.848  19.385  1.00 14.73           C  
ANISOU  718  CB  LEU A  87     1632   1927   2037     84   -262    185       C  
ATOM    719  CG  LEU A  87      16.676 -13.104  20.677  1.00 17.21           C  
ANISOU  719  CG  LEU A  87     1963   2262   2314     75   -312    207       C  
ATOM    720  CD1 LEU A  87      15.555 -13.409  21.659  1.00 17.72           C  
ANISOU  720  CD1 LEU A  87     2043   2347   2342     95   -320    209       C  
ATOM    721  CD2 LEU A  87      18.026 -13.431  21.279  1.00 19.12           C  
ANISOU  721  CD2 LEU A  87     2162   2502   2602     53   -333    259       C  
ATOM    722  N   LYS A  88      17.808 -15.569  16.962  1.00 12.70           N  
ANISOU  722  N   LYS A  88     1328   1598   1898     87   -150    182       N  
ATOM    723  CA  LYS A  88      17.600 -16.588  15.957  1.00 12.67           C  
ANISOU  723  CA  LYS A  88     1334   1560   1921     95    -95    163       C  
ATOM    724  C   LYS A  88      17.188 -17.806  16.736  1.00 12.90           C  
ANISOU  724  C   LYS A  88     1333   1590   1978    105    -93    185       C  
ATOM    725  O   LYS A  88      17.975 -18.321  17.525  1.00 13.84           O  
ANISOU  725  O   LYS A  88     1402   1711   2146    109    -93    232       O  
ATOM    726  CB  LYS A  88      18.899 -16.875  15.190  1.00 13.93           C  
ANISOU  726  CB  LYS A  88     1473   1683   2136    100    -42    184       C  
ATOM    727  CG  LYS A  88      19.258 -15.755  14.219  1.00 17.96           C  
ANISOU  727  CG  LYS A  88     2015   2189   2621     92    -36    161       C  
ATOM    728  CD  LYS A  88      20.490 -16.070  13.376  1.00 22.34           C  
ANISOU  728  CD  LYS A  88     2553   2703   3230    103     28    185       C  
ATOM    729  CE  LYS A  88      21.738 -16.137  14.208  1.00 26.94           C  
ANISOU  729  CE  LYS A  88     3066   3292   3880    106     21    258       C  
ATOM    730  NZ  LYS A  88      22.952 -15.999  13.363  1.00 28.94           N  
ANISOU  730  NZ  LYS A  88     3299   3515   4180    116     74    291       N  
ATOM    731  N   LEU A  89      15.950 -18.220  16.574  1.00 12.44           N  
ANISOU  731  N   LEU A  89     1301   1534   1893    106    -97    159       N  
ATOM    732  CA  LEU A  89      15.403 -19.373  17.256  1.00 12.59           C  
ANISOU  732  CA  LEU A  89     1294   1554   1937    114    -98    179       C  
ATOM    733  C   LEU A  89      15.367 -20.511  16.264  1.00 12.94           C  
ANISOU  733  C   LEU A  89     1356   1549   2012    113    -48    163       C  
ATOM    734  O   LEU A  89      14.620 -20.459  15.287  1.00 13.54           O  
ANISOU  734  O   LEU A  89     1483   1607   2054    100    -42    125       O  
ATOM    735  CB  LEU A  89      13.982 -19.063  17.753  1.00 12.75           C  
ANISOU  735  CB  LEU A  89     1331   1607   1908    116   -137    171       C  
ATOM    736  CG  LEU A  89      13.831 -17.772  18.569  1.00 13.26           C  
ANISOU  736  CG  LEU A  89     1403   1710   1923    120   -178    176       C  
ATOM    737  CD1 LEU A  89      12.360 -17.539  18.932  1.00 14.00           C  
ANISOU  737  CD1 LEU A  89     1515   1830   1976    129   -200    174       C  
ATOM    738  CD2 LEU A  89      14.701 -17.814  19.810  1.00 14.04           C  
ANISOU  738  CD2 LEU A  89     1466   1827   2044    123   -197    217       C  
ATOM    739  N   LYS A  90      16.203 -21.522  16.472  1.00 12.58           N  
ANISOU  739  N   LYS A  90     1274   1477   2030    124    -10    194       N  
ATOM    740  CA  LYS A  90      16.232 -22.674  15.595  1.00 13.10           C  
ANISOU  740  CA  LYS A  90     1365   1485   2125    126     46    179       C  
ATOM    741  C   LYS A  90      15.051 -23.539  15.962  1.00 13.08           C  
ANISOU  741  C   LYS A  90     1366   1485   2118    120     22    178       C  
ATOM    742  O   LYS A  90      14.830 -23.805  17.137  1.00 13.52           O  
ANISOU  742  O   LYS A  90     1371   1575   2191    129     -8    213       O  
ATOM    743  CB  LYS A  90      17.536 -23.458  15.769  1.00 15.25           C  
ANISOU  743  CB  LYS A  90     1591   1726   2476    146    101    223       C  
ATOM    744  CG  LYS A  90      17.687 -24.519  14.697  1.00 19.98           C  
ANISOU  744  CG  LYS A  90     2237   2255   3100    152    174    202       C  
ATOM    745  CD  LYS A  90      18.937 -25.357  14.862  1.00 26.70           C  
ANISOU  745  CD  LYS A  90     3041   3069   4037    179    242    252       C  
ATOM    746  CE  LYS A  90      18.950 -26.460  13.827  1.00 31.95           C  
ANISOU  746  CE  LYS A  90     3769   3655   4717    188    320    225       C  
ATOM    747  NZ  LYS A  90      20.250 -27.184  13.784  1.00 34.61           N  
ANISOU  747  NZ  LYS A  90     4068   3943   5138    222    407    276       N  
ATOM    748  N   VAL A  91      14.239 -23.892  14.982  1.00 13.01           N  
ANISOU  748  N   VAL A  91     1419   1445   2081    102     29    140       N  
ATOM    749  CA  VAL A  91      13.080 -24.738  15.204  1.00 13.59           C  
ANISOU  749  CA  VAL A  91     1498   1516   2152     89      1    144       C  
ATOM    750  C   VAL A  91      13.290 -26.080  14.510  1.00 13.94           C  
ANISOU  750  C   VAL A  91     1577   1489   2230     84     52    133       C  
ATOM    751  O   VAL A  91      14.153 -26.193  13.635  1.00 14.24           O  
ANISOU  751  O   VAL A  91     1654   1478   2276     88    111    113       O  
ATOM    752  CB  VAL A  91      11.760 -24.046  14.810  1.00 13.54           C  
ANISOU  752  CB  VAL A  91     1528   1533   2083     64    -51    124       C  
ATOM    753  CG1 VAL A  91      11.470 -22.870  15.748  1.00 13.86           C  
ANISOU  753  CG1 VAL A  91     1531   1640   2097     79    -93    143       C  
ATOM    754  CG2 VAL A  91      11.792 -23.576  13.358  1.00 13.61           C  
ANISOU  754  CG2 VAL A  91     1613   1508   2049     39    -33     78       C  
ATOM    755  N   ASP A  92      12.510 -27.098  14.887  1.00 14.52           N  
ANISOU  755  N   ASP A  92     1643   1553   2322     75     33    149       N  
ATOM    756  CA  ASP A  92      12.713 -28.432  14.308  1.00 15.39           C  
ANISOU  756  CA  ASP A  92     1792   1588   2466     69     81    140       C  
ATOM    757  C   ASP A  92      12.040 -28.640  12.940  1.00 16.15           C  
ANISOU  757  C   ASP A  92     1994   1631   2511     28     81     92       C  
ATOM    758  O   ASP A  92      12.151 -29.724  12.366  1.00 17.58           O  
ANISOU  758  O   ASP A  92     2231   1741   2708     18    121     77       O  
ATOM    759  CB  ASP A  92      12.298 -29.535  15.300  1.00 16.92           C  
ANISOU  759  CB  ASP A  92     1931   1787   2710     77     64    181       C  
ATOM    760  CG  ASP A  92      10.803 -29.782  15.434  1.00 21.75           C  
ANISOU  760  CG  ASP A  92     2553   2417   3296     47     -3    188       C  
ATOM    761  OD1 ASP A  92      10.011 -28.950  14.931  1.00 21.92           O  
ANISOU  761  OD1 ASP A  92     2611   2460   3260     22    -45    169       O  
ATOM    762  OD2 ASP A  92      10.423 -30.804  16.052  1.00 24.89           O  
ANISOU  762  OD2 ASP A  92     2915   2806   3734     49    -14    220       O  
ATOM    763  N   THR A  93      11.319 -27.629  12.442  1.00 15.46           N  
ANISOU  763  N   THR A  93     1939   1574   2361      1     33     71       N  
ATOM    764  CA  THR A  93      10.601 -27.740  11.184  1.00 15.98           C  
ANISOU  764  CA  THR A  93     2104   1596   2373    -47     18     33       C  
ATOM    765  C   THR A  93      10.936 -26.576  10.273  1.00 15.60           C  
ANISOU  765  C   THR A  93     2101   1555   2272    -55     29     -2       C  
ATOM    766  O   THR A  93      10.857 -25.414  10.682  1.00 15.87           O  
ANISOU  766  O   THR A  93     2088   1651   2291    -43     -1      9       O  
ATOM    767  CB  THR A  93       9.091 -27.772  11.474  1.00 18.02           C  
ANISOU  767  CB  THR A  93     2348   1888   2611    -82    -67     59       C  
ATOM    768  OG1 THR A  93       8.807 -28.909  12.282  1.00 19.65           O  
ANISOU  768  OG1 THR A  93     2512   2085   2869    -75    -75     93       O  
ATOM    769  CG2 THR A  93       8.231 -27.818  10.214  1.00 18.56           C  
ANISOU  769  CG2 THR A  93     2512   1918   2621   -145   -103     33       C  
ATOM    770  N   ALA A  94      11.321 -26.885   9.036  1.00 15.11           N  
ANISOU  770  N   ALA A  94     2136   1424   2181    -75     76    -44       N  
ATOM    771  CA  ALA A  94      11.580 -25.846   8.051  1.00 15.27           C  
ANISOU  771  CA  ALA A  94     2209   1446   2147    -87     87    -77       C  
ATOM    772  C   ALA A  94      10.227 -25.287   7.629  1.00 14.37           C  
ANISOU  772  C   ALA A  94     2124   1362   1976   -140      3    -79       C  
ATOM    773  O   ALA A  94       9.266 -26.049   7.472  1.00 14.40           O  
ANISOU  773  O   ALA A  94     2162   1342   1968   -183    -41    -72       O  
ATOM    774  CB  ALA A  94      12.280 -26.436   6.838  1.00 15.99           C  
ANISOU  774  CB  ALA A  94     2408   1451   2218    -95    164   -119       C  
ATOM    775  N   ASN A  95      10.133 -23.953   7.445  1.00 13.14           N  
ANISOU  775  N   ASN A  95     1950   1255   1786   -141    -22    -83       N  
ATOM    776  CA  ASN A  95       8.883 -23.366   6.989  1.00 12.83           C  
ANISOU  776  CA  ASN A  95     1934   1243   1698   -190    -96    -76       C  
ATOM    777  C   ASN A  95       8.594 -23.845   5.583  1.00 14.44           C  
ANISOU  777  C   ASN A  95     2259   1381   1848   -249    -97   -111       C  
ATOM    778  O   ASN A  95       9.373 -23.554   4.678  1.00 15.01           O  
ANISOU  778  O   ASN A  95     2395   1421   1889   -248    -45   -150       O  
ATOM    779  CB  ASN A  95       8.974 -21.836   7.015  1.00 11.70           C  
ANISOU  779  CB  ASN A  95     1754   1158   1533   -175   -111    -75       C  
ATOM    780  CG  ASN A  95       7.671 -21.166   6.662  1.00 12.68           C  
ANISOU  780  CG  ASN A  95     1885   1314   1617   -219   -184    -54       C  
ATOM    781  OD1 ASN A  95       6.665 -21.818   6.312  1.00 12.65           O  
ANISOU  781  OD1 ASN A  95     1915   1291   1601   -268   -232    -37       O  
ATOM    782  ND2 ASN A  95       7.654 -19.854   6.755  1.00 13.33           N  
ANISOU  782  ND2 ASN A  95     1933   1446   1685   -204   -197    -48       N  
ATOM    783  N   PRO A  96       7.498 -24.592   5.381  1.00 15.09           N  
ANISOU  783  N   PRO A  96     2378   1442   1916   -304   -156    -95       N  
ATOM    784  CA  PRO A  96       7.194 -25.071   4.022  1.00 15.91           C  
ANISOU  784  CA  PRO A  96     2611   1476   1956   -371   -165   -128       C  
ATOM    785  C   PRO A  96       6.869 -23.969   3.029  1.00 16.81           C  
ANISOU  785  C   PRO A  96     2771   1609   2007   -411   -196   -140       C  
ATOM    786  O   PRO A  96       6.955 -24.177   1.819  1.00 18.67           O  
ANISOU  786  O   PRO A  96     3125   1787   2182   -458   -185   -178       O  
ATOM    787  CB  PRO A  96       6.007 -26.020   4.234  1.00 16.85           C  
ANISOU  787  CB  PRO A  96     2739   1579   2084   -424   -239    -91       C  
ATOM    788  CG  PRO A  96       5.365 -25.537   5.452  1.00 17.21           C  
ANISOU  788  CG  PRO A  96     2656   1705   2179   -394   -285    -32       C  
ATOM    789  CD  PRO A  96       6.454 -24.999   6.343  1.00 15.27           C  
ANISOU  789  CD  PRO A  96     2328   1500   1975   -311   -220    -40       C  
ATOM    790  N  ALYS A  97       6.497 -22.792   3.536  0.50 16.18           N  
ANISOU  790  N  ALYS A  97     2603   1608   1938   -391   -232   -109       N  
ATOM    791  N  BLYS A  97       6.498 -22.794   3.526  0.50 15.87           N  
ANISOU  791  N  BLYS A  97     2564   1568   1898   -392   -232   -109       N  
ATOM    792  CA ALYS A  97       6.197 -21.633   2.715  0.50 16.25           C  
ANISOU  792  CA ALYS A  97     2636   1643   1896   -422   -261   -113       C  
ATOM    793  CA BLYS A  97       6.186 -21.657   2.678  0.50 15.62           C  
ANISOU  793  CA BLYS A  97     2560   1561   1815   -424   -262   -113       C  
ATOM    794  C  ALYS A  97       7.398 -20.685   2.599  0.50 16.20           C  
ANISOU  794  C  ALYS A  97     2614   1653   1889   -368   -193   -146       C  
ATOM    795  C  BLYS A  97       7.397 -20.733   2.479  0.50 15.87           C  
ANISOU  795  C  BLYS A  97     2585   1605   1841   -374   -192   -149       C  
ATOM    796  O  ALYS A  97       7.196 -19.507   2.312  0.50 16.30           O  
ANISOU  796  O  ALYS A  97     2606   1709   1879   -373   -216   -138       O  
ATOM    797  O  BLYS A  97       7.210 -19.616   1.997  0.50 15.98           O  
ANISOU  797  O  BLYS A  97     2598   1652   1823   -387   -213   -148       O  
ATOM    798  CB ALYS A  97       4.997 -20.876   3.290  0.50 17.71           C  
ANISOU  798  CB ALYS A  97     2736   1897   2095   -434   -339    -50       C  
ATOM    799  CB BLYS A  97       5.028 -20.859   3.292  0.50 16.13           C  
ANISOU  799  CB BLYS A  97     2533   1698   1896   -431   -337    -51       C  
ATOM    800  CG ALYS A  97       3.707 -21.681   3.258  0.50 21.36           C  
ANISOU  800  CG ALYS A  97     3212   2347   2559   -497   -418     -3       C  
ATOM    801  CG BLYS A  97       3.787 -21.702   3.563  0.50 18.13           C  
ANISOU  801  CG BLYS A  97     2776   1946   2165   -478   -409      2       C  
ATOM    802  CD ALYS A  97       2.514 -20.817   3.626  0.50 25.21           C  
ANISOU  802  CD ALYS A  97     3618   2900   3060   -508   -487     69       C  
ATOM    803  CD BLYS A  97       2.659 -20.874   4.168  0.50 20.47           C  
ANISOU  803  CD BLYS A  97     2981   2314   2485   -476   -472     74       C  
ATOM    804  CE ALYS A  97       1.247 -21.628   3.735  0.50 28.84           C  
ANISOU  804  CE ALYS A  97     4069   3352   3536   -564   -565    134       C  
ATOM    805  CE BLYS A  97       1.497 -21.748   4.586  0.50 23.28           C  
ANISOU  805  CE BLYS A  97     3308   2666   2870   -513   -538    139       C  
ATOM    806  NZ ALYS A  97       1.311 -22.583   4.872  0.50 31.00           N  
ANISOU  806  NZ ALYS A  97     4286   3624   3867   -522   -549    151       N  
ATOM    807  NZ BLYS A  97       0.450 -20.970   5.306  0.50 24.86           N  
ANISOU  807  NZ BLYS A  97     3407   2934   3103   -497   -582    220       N  
ATOM    808  N   THR A  98       8.635 -21.173   2.838  1.00 15.64           N  
ANISOU  808  N   THR A  98     2547   1549   1848   -317   -110   -174       N  
ATOM    809  CA  THR A  98       9.819 -20.315   2.707  1.00 15.75           C  
ANISOU  809  CA  THR A  98     2542   1576   1867   -270    -48   -195       C  
ATOM    810  C   THR A  98      10.036 -19.955   1.256  1.00 17.30           C  
ANISOU  810  C   THR A  98     2842   1736   1997   -305    -26   -232       C  
ATOM    811  O   THR A  98      10.207 -20.836   0.419  1.00 18.89           O  
ANISOU  811  O   THR A  98     3148   1866   2165   -332      9   -263       O  
ATOM    812  CB  THR A  98      11.098 -20.973   3.223  1.00 15.79           C  
ANISOU  812  CB  THR A  98     2523   1549   1925   -210     37   -202       C  
ATOM    813  OG1 THR A  98      10.913 -21.371   4.576  1.00 14.95           O  
ANISOU  813  OG1 THR A  98     2326   1476   1878   -181     15   -166       O  
ATOM    814  CG2 THR A  98      12.291 -20.020   3.161  1.00 16.33           C  
ANISOU  814  CG2 THR A  98     2558   1638   2009   -164     90   -207       C  
ATOM    815  N   PRO A  99       9.971 -18.662   0.943  1.00 17.35           N  
ANISOU  815  N   PRO A  99     2825   1788   1980   -308    -48   -229       N  
ATOM    816  CA  PRO A  99      10.220 -18.251  -0.440  1.00 17.36           C  
ANISOU  816  CA  PRO A  99     2921   1759   1916   -340    -26   -262       C  
ATOM    817  C   PRO A  99      11.719 -18.183  -0.682  1.00 17.89           C  
ANISOU  817  C   PRO A  99     3000   1796   2001   -284     75   -286       C  
ATOM    818  O   PRO A  99      12.539 -18.301   0.246  1.00 18.10           O  
ANISOU  818  O   PRO A  99     2949   1834   2093   -225    117   -271       O  
ATOM    819  CB  PRO A  99       9.616 -16.844  -0.472  1.00 17.74           C  
ANISOU  819  CB  PRO A  99     2916   1876   1950   -354    -86   -239       C  
ATOM    820  CG  PRO A  99       9.944 -16.303   0.908  1.00 18.63           C  
ANISOU  820  CG  PRO A  99     2906   2044   2130   -291    -83   -211       C  
ATOM    821  CD  PRO A  99       9.806 -17.493   1.835  1.00 16.90           C  
ANISOU  821  CD  PRO A  99     2660   1807   1953   -276    -83   -197       C  
ATOM    822  N   LYS A 100      12.124 -17.929  -1.950  1.00 18.01           N  
ANISOU  822  N   LYS A 100     3110   1775   1960   -303    116   -318       N  
ATOM    823  CA  LYS A 100      13.535 -17.625  -2.236  1.00 17.86           C  
ANISOU  823  CA  LYS A 100     3088   1736   1961   -246    211   -328       C  
ATOM    824  C   LYS A 100      13.794 -16.281  -1.557  1.00 16.86           C  
ANISOU  824  C   LYS A 100     2847   1688   1873   -214    182   -300       C  
ATOM    825  O   LYS A 100      12.915 -15.410  -1.609  1.00 17.12           O  
ANISOU  825  O   LYS A 100     2856   1769   1878   -249    106   -290       O  
ATOM    826  CB  LYS A 100      13.781 -17.459  -3.727  1.00 20.30           C  
ANISOU  826  CB  LYS A 100     3518   2000   2196   -274    254   -363       C  
ATOM    827  CG  LYS A 100      13.806 -18.781  -4.460  1.00 25.36           C  
ANISOU  827  CG  LYS A 100     4294   2549   2793   -297    305   -396       C  
ATOM    828  CD  LYS A 100      13.957 -18.552  -5.942  1.00 30.62           C  
ANISOU  828  CD  LYS A 100     5093   3170   3371   -332    340   -431       C  
ATOM    829  CE  LYS A 100      13.870 -19.846  -6.690  1.00 34.80           C  
ANISOU  829  CE  LYS A 100     5777   3601   3843   -365    383   -468       C  
ATOM    830  NZ  LYS A 100      13.923 -19.616  -8.154  1.00 37.87           N  
ANISOU  830  NZ  LYS A 100     6311   3946   4134   -404    413   -503       N  
ATOM    831  N   TYR A 101      14.880 -16.181  -0.805  1.00 16.48           N  
ANISOU  831  N   TYR A 101     2722   1649   1891   -152    233   -279       N  
ATOM    832  CA  TYR A 101      15.128 -14.952  -0.066  1.00 16.55           C  
ANISOU  832  CA  TYR A 101     2629   1725   1935   -127    198   -252       C  
ATOM    833  C   TYR A 101      16.581 -14.602   0.070  1.00 17.45           C  
ANISOU  833  C   TYR A 101     2697   1834   2099    -73    267   -232       C  
ATOM    834  O   TYR A 101      17.465 -15.432  -0.117  1.00 18.21           O  
ANISOU  834  O   TYR A 101     2816   1879   2224    -42    348   -229       O  
ATOM    835  CB  TYR A 101      14.446 -14.990   1.329  1.00 15.77           C  
ANISOU  835  CB  TYR A 101     2444   1674   1873   -121    131   -225       C  
ATOM    836  CG  TYR A 101      15.146 -15.902   2.316  1.00 15.73           C  
ANISOU  836  CG  TYR A 101     2390   1652   1934    -80    170   -204       C  
ATOM    837  CD1 TYR A 101      14.886 -17.261   2.336  1.00 15.94           C  
ANISOU  837  CD1 TYR A 101     2457   1632   1967    -88    191   -212       C  
ATOM    838  CD2 TYR A 101      16.069 -15.402   3.228  1.00 16.30           C  
ANISOU  838  CD2 TYR A 101     2376   1754   2064    -37    181   -172       C  
ATOM    839  CE1 TYR A 101      15.528 -18.107   3.223  1.00 17.03           C  
ANISOU  839  CE1 TYR A 101     2546   1755   2170    -49    228   -188       C  
ATOM    840  CE2 TYR A 101      16.721 -16.242   4.126  1.00 16.87           C  
ANISOU  840  CE2 TYR A 101     2398   1813   2199     -3    212   -144       C  
ATOM    841  CZ  TYR A 101      16.426 -17.592   4.137  1.00 18.00           C  
ANISOU  841  CZ  TYR A 101     2577   1913   2351     -8    236   -152       C  
ATOM    842  OH  TYR A 101      17.050 -18.451   5.005  1.00 19.69           O  
ANISOU  842  OH  TYR A 101     2740   2112   2629     25    269   -122       O  
ATOM    843  N   LYS A 102      16.813 -13.342   0.419  1.00 17.07           N  
ANISOU  843  N   LYS A 102     2583   1839   2065    -62    232   -213       N  
ATOM    844  CA  LYS A 102      18.117 -12.782   0.702  1.00 17.29           C  
ANISOU  844  CA  LYS A 102     2549   1875   2147    -18    273   -181       C  
ATOM    845  C   LYS A 102      17.931 -11.785   1.830  1.00 17.01           C  
ANISOU  845  C   LYS A 102     2427   1902   2135    -15    200   -157       C  
ATOM    846  O   LYS A 102      16.841 -11.228   2.005  1.00 17.36           O  
ANISOU  846  O   LYS A 102     2472   1982   2143    -44    132   -169       O  
ATOM    847  CB  LYS A 102      18.666 -12.018  -0.521  1.00 19.57           C  
ANISOU  847  CB  LYS A 102     2879   2152   2405    -19    314   -190       C  
ATOM    848  CG  LYS A 102      19.172 -12.891  -1.652  1.00 25.57           C  
ANISOU  848  CG  LYS A 102     3730   2843   3144     -9    408   -209       C  
ATOM    849  CD  LYS A 102      19.560 -12.019  -2.838  1.00 30.51           C  
ANISOU  849  CD  LYS A 102     4398   3464   3730    -13    439   -217       C  
ATOM    850  CE  LYS A 102      19.942 -12.850  -4.039  1.00 34.71           C  
ANISOU  850  CE  LYS A 102     5043   3923   4223     -8    534   -241       C  
ATOM    851  NZ  LYS A 102      20.222 -11.998  -5.223  1.00 37.67           N  
ANISOU  851  NZ  LYS A 102     5466   4297   4550    -15    561   -250       N  
ATOM    852  N   PHE A 103      18.997 -11.533   2.573  1.00 16.41           N  
ANISOU  852  N   PHE A 103     2279   1836   2119     18    214   -118       N  
ATOM    853  CA  PHE A 103      18.994 -10.484   3.584  1.00 16.22           C  
ANISOU  853  CA  PHE A 103     2188   1863   2111     19    147    -95       C  
ATOM    854  C   PHE A 103      19.847  -9.382   3.004  1.00 16.98           C  
ANISOU  854  C   PHE A 103     2271   1966   2214     25    161    -80       C  
ATOM    855  O   PHE A 103      20.994  -9.634   2.601  1.00 18.29           O  
ANISOU  855  O   PHE A 103     2426   2103   2420     50    225    -52       O  
ATOM    856  CB  PHE A 103      19.613 -10.957   4.902  1.00 15.69           C  
ANISOU  856  CB  PHE A 103     2052   1803   2106     41    140    -53       C  
ATOM    857  CG  PHE A 103      18.795 -11.943   5.708  1.00 15.24           C  
ANISOU  857  CG  PHE A 103     1993   1748   2051     38    119    -60       C  
ATOM    858  CD1 PHE A 103      17.445 -12.132   5.446  1.00 15.08           C  
ANISOU  858  CD1 PHE A 103     2018   1733   1978     12     87    -95       C  
ATOM    859  CD2 PHE A 103      19.352 -12.609   6.784  1.00 15.50           C  
ANISOU  859  CD2 PHE A 103     1970   1780   2139     57    123    -22       C  
ATOM    860  CE1 PHE A 103      16.690 -13.014   6.217  1.00 15.35           C  
ANISOU  860  CE1 PHE A 103     2043   1770   2018     10     65    -93       C  
ATOM    861  CE2 PHE A 103      18.597 -13.493   7.545  1.00 15.76           C  
ANISOU  861  CE2 PHE A 103     1998   1817   2174     55    102    -25       C  
ATOM    862  CZ  PHE A 103      17.267 -13.671   7.274  1.00 15.43           C  
ANISOU  862  CZ  PHE A 103     2000   1780   2082     33     73    -60       C  
ATOM    863  N   VAL A 104      19.279  -8.182   2.889  1.00 16.37           N  
ANISOU  863  N   VAL A 104     2197   1924   2100      5    107    -93       N  
ATOM    864  CA  VAL A 104      20.033  -7.044   2.376  1.00 17.50           C  
ANISOU  864  CA  VAL A 104     2324   2076   2249      8    110    -77       C  
ATOM    865  C   VAL A 104      19.980  -5.887   3.348  1.00 17.45           C  
ANISOU  865  C   VAL A 104     2271   2109   2250      2     39    -60       C  
ATOM    866  O   VAL A 104      18.977  -5.694   4.025  1.00 18.38           O  
ANISOU  866  O   VAL A 104     2392   2249   2341    -10    -12    -76       O  
ATOM    867  CB  VAL A 104      19.568  -6.605   0.972  1.00 19.51           C  
ANISOU  867  CB  VAL A 104     2641   2325   2449    -12    127   -110       C  
ATOM    868  CG1 VAL A 104      19.602  -7.772  -0.011  1.00 20.51           C  
ANISOU  868  CG1 VAL A 104     2834   2403   2554    -11    197   -131       C  
ATOM    869  CG2 VAL A 104      18.188  -5.980   1.030  1.00 21.03           C  
ANISOU  869  CG2 VAL A 104     2852   2550   2590    -44     60   -136       C  
ATOM    870  N   ARG A 105      21.056  -5.114   3.423  1.00 15.80           N  
ANISOU  870  N   ARG A 105     2023   1904   2078     10     37    -24       N  
ATOM    871  CA  ARG A 105      21.085  -3.918   4.245  1.00 15.43           C  
ANISOU  871  CA  ARG A 105     1946   1886   2031     -1    -31     -9       C  
ATOM    872  C   ARG A 105      20.948  -2.766   3.265  1.00 16.07           C  
ANISOU  872  C   ARG A 105     2048   1975   2081    -13    -37    -24       C  
ATOM    873  O   ARG A 105      21.814  -2.585   2.403  1.00 16.45           O  
ANISOU  873  O   ARG A 105     2089   2009   2150     -6      4     -4       O  
ATOM    874  CB  ARG A 105      22.391  -3.812   5.050  1.00 15.61           C  
ANISOU  874  CB  ARG A 105     1910   1905   2118      7    -42     50       C  
ATOM    875  CG  ARG A 105      22.422  -2.551   5.896  1.00 16.10           C  
ANISOU  875  CG  ARG A 105     1958   1989   2171    -12   -119     62       C  
ATOM    876  CD  ARG A 105      23.630  -2.518   6.815  1.00 16.65           C  
ANISOU  876  CD  ARG A 105     1972   2054   2298    -16   -147    126       C  
ATOM    877  NE  ARG A 105      23.615  -1.344   7.690  1.00 16.81           N  
ANISOU  877  NE  ARG A 105     1998   2089   2299    -42   -226    133       N  
ATOM    878  CZ  ARG A 105      22.963  -1.276   8.847  1.00 17.76           C  
ANISOU  878  CZ  ARG A 105     2140   2221   2387    -51   -276    117       C  
ATOM    879  NH1 ARG A 105      22.257  -2.313   9.283  1.00 15.50           N  
ANISOU  879  NH1 ARG A 105     1863   1938   2090    -38   -257     96       N  
ATOM    880  NH2 ARG A 105      23.019  -0.174   9.580  1.00 16.68           N  
ANISOU  880  NH2 ARG A 105     2021   2088   2227    -74   -342    122       N  
ATOM    881  N   ILE A 106      19.843  -2.020   3.359  1.00 16.34           N  
ANISOU  881  N   ILE A 106     2107   2033   2069    -30    -83    -53       N  
ATOM    882  CA  ILE A 106      19.591  -0.952   2.403  1.00 17.54           C  
ANISOU  882  CA  ILE A 106     2279   2195   2192    -43    -89    -66       C  
ATOM    883  C   ILE A 106      20.273   0.351   2.775  1.00 18.38           C  
ANISOU  883  C   ILE A 106     2356   2311   2318    -47   -128    -40       C  
ATOM    884  O   ILE A 106      20.686   0.548   3.914  1.00 18.30           O  
ANISOU  884  O   ILE A 106     2320   2302   2331    -46   -166    -18       O  
ATOM    885  CB  ILE A 106      18.079  -0.754   2.154  1.00 18.39           C  
ANISOU  885  CB  ILE A 106     2423   2319   2246    -60   -113    -99       C  
ATOM    886  CG1 ILE A 106      17.349  -0.412   3.456  1.00 18.46           C  
ANISOU  886  CG1 ILE A 106     2423   2345   2247    -57   -162    -99       C  
ATOM    887  CG2 ILE A 106      17.482  -1.941   1.420  1.00 19.36           C  
ANISOU  887  CG2 ILE A 106     2585   2427   2345    -68    -76   -122       C  
ATOM    888  CD1 ILE A 106      15.965   0.091   3.254  1.00 19.73           C  
ANISOU  888  CD1 ILE A 106     2607   2523   2368    -69   -185   -114       C  
ATOM    889  N   GLN A 107      20.428   1.226   1.782  1.00 19.23           N  
ANISOU  889  N   GLN A 107     2470   2421   2414    -55   -122    -41       N  
ATOM    890  CA  GLN A 107      20.997   2.545   1.964  1.00 19.73           C  
ANISOU  890  CA  GLN A 107     2511   2492   2493    -62   -161    -18       C  
ATOM    891  C   GLN A 107      19.865   3.537   2.207  1.00 18.47           C  
ANISOU  891  C   GLN A 107     2377   2349   2291    -75   -206    -44       C  
ATOM    892  O   GLN A 107      18.742   3.340   1.721  1.00 17.38           O  
ANISOU  892  O   GLN A 107     2268   2221   2116    -80   -196    -72       O  
ATOM    893  CB  GLN A 107      21.745   2.950   0.676  1.00 23.23           C  
ANISOU  893  CB  GLN A 107     2947   2930   2949    -61   -123     -1       C  
ATOM    894  CG  GLN A 107      22.876   1.997   0.305  1.00 29.27           C  
ANISOU  894  CG  GLN A 107     3689   3673   3760    -41    -61     33       C  
ATOM    895  CD  GLN A 107      24.026   2.049   1.285  1.00 36.32           C  
ANISOU  895  CD  GLN A 107     4527   4559   4716    -36    -86     88       C  
ATOM    896  OE1 GLN A 107      24.225   3.026   2.019  1.00 38.70           O  
ANISOU  896  OE1 GLN A 107     4809   4869   5026    -53   -152    106       O  
ATOM    897  NE2 GLN A 107      24.829   0.996   1.300  1.00 37.97           N  
ANISOU  897  NE2 GLN A 107     4710   4747   4969    -14    -34    122       N  
ATOM    898  N   PRO A 108      20.146   4.681   2.862  1.00 18.14           N  
ANISOU  898  N   PRO A 108     2328   2308   2256    -82   -254    -30       N  
ATOM    899  CA  PRO A 108      19.108   5.716   2.987  1.00 17.93           C  
ANISOU  899  CA  PRO A 108     2328   2291   2193    -88   -285    -51       C  
ATOM    900  C   PRO A 108      18.660   6.165   1.590  1.00 17.22           C  
ANISOU  900  C   PRO A 108     2246   2212   2084    -96   -261    -61       C  
ATOM    901  O   PRO A 108      19.462   6.189   0.647  1.00 17.68           O  
ANISOU  901  O   PRO A 108     2289   2269   2161    -99   -235    -46       O  
ATOM    902  CB  PRO A 108      19.811   6.845   3.755  1.00 19.73           C  
ANISOU  902  CB  PRO A 108     2553   2507   2435    -98   -334    -30       C  
ATOM    903  CG  PRO A 108      21.269   6.568   3.594  1.00 21.30           C  
ANISOU  903  CG  PRO A 108     2711   2697   2685   -102   -330     10       C  
ATOM    904  CD  PRO A 108      21.423   5.100   3.467  1.00 19.01           C  
ANISOU  904  CD  PRO A 108     2406   2406   2409    -88   -284     11       C  
ATOM    905  N   GLY A 109      17.382   6.434   1.449  1.00 15.99           N  
ANISOU  905  N   GLY A 109     2113   2069   1895    -99   -266    -79       N  
ATOM    906  CA  GLY A 109      16.807   6.791   0.158  1.00 16.21           C  
ANISOU  906  CA  GLY A 109     2149   2110   1901   -113   -251    -83       C  
ATOM    907  C   GLY A 109      16.074   5.638  -0.506  1.00 16.96           C  
ANISOU  907  C   GLY A 109     2262   2210   1971   -123   -223    -97       C  
ATOM    908  O   GLY A 109      15.191   5.862  -1.338  1.00 18.41           O  
ANISOU  908  O   GLY A 109     2460   2407   2128   -141   -223    -99       O  
ATOM    909  N  AGLN A 110      16.422   4.397  -0.138  0.75 16.76           N  
ANISOU  909  N  AGLN A 110     2239   2173   1955   -114   -202   -104       N  
ATOM    910  N  BGLN A 110      16.445   4.390  -0.161  0.25 16.16           N  
ANISOU  910  N  BGLN A 110     2164   2097   1880   -114   -201   -104       N  
ATOM    911  CA AGLN A 110      15.768   3.237  -0.714  0.75 16.95           C  
ANISOU  911  CA AGLN A 110     2291   2196   1955   -126   -179   -118       C  
ATOM    912  CA BGLN A 110      15.829   3.187  -0.717  0.25 15.84           C  
ANISOU  912  CA BGLN A 110     2150   2054   1816   -125   -177   -118       C  
ATOM    913  C  AGLN A 110      14.440   2.952  -0.068  0.75 16.11           C  
ANISOU  913  C  AGLN A 110     2190   2100   1832   -129   -203   -120       C  
ATOM    914  C  BGLN A 110      14.470   2.926  -0.075  0.25 15.71           C  
ANISOU  914  C  BGLN A 110     2140   2049   1782   -129   -202   -120       C  
ATOM    915  O  AGLN A 110      14.240   3.191   1.125  0.75 16.11           O  
ANISOU  915  O  AGLN A 110     2176   2103   1844   -110   -224   -114       O  
ATOM    916  O  BGLN A 110      14.293   3.143   1.123  0.25 15.80           O  
ANISOU  916  O  BGLN A 110     2136   2063   1806   -110   -223   -114       O  
ATOM    917  CB AGLN A 110      16.693   2.020  -0.709  0.75 19.14           C  
ANISOU  917  CB AGLN A 110     2570   2450   2251   -114   -138   -121       C  
ATOM    918  CB BGLN A 110      16.764   1.974  -0.537  0.25 16.49           C  
ANISOU  918  CB BGLN A 110     2230   2113   1920   -111   -139   -120       C  
ATOM    919  CG AGLN A 110      17.940   2.248  -1.555  0.75 23.45           C  
ANISOU  919  CG AGLN A 110     3110   2983   2815   -108   -101   -110       C  
ATOM    920  CG BGLN A 110      16.218   0.644  -1.057  0.25 17.81           C  
ANISOU  920  CG BGLN A 110     2436   2268   2063   -123   -112   -138       C  
ATOM    921  CD AGLN A 110      17.625   2.582  -2.992  0.75 30.28           C  
ANISOU  921  CD AGLN A 110     4009   3852   3643   -131    -84   -118       C  
ATOM    922  CD BGLN A 110      15.922   0.672  -2.535  0.25 19.23           C  
ANISOU  922  CD BGLN A 110     2659   2445   2201   -152    -94   -149       C  
ATOM    923  OE1AGLN A 110      17.015   1.792  -3.727  0.75 33.04           O  
ANISOU  923  OE1AGLN A 110     4405   4194   3954   -150    -65   -137       O  
ATOM    924  OE1BGLN A 110      16.709   1.161  -3.348  0.25 20.49           O  
ANISOU  924  OE1BGLN A 110     2822   2600   2362   -150    -68   -144       O  
ATOM    925  NE2AGLN A 110      18.015   3.774  -3.418  0.75 30.91           N  
ANISOU  925  NE2AGLN A 110     4069   3944   3730   -133    -95   -103       N  
ATOM    926  NE2BGLN A 110      14.760   0.153  -2.910  0.25 17.17           N  
ANISOU  926  NE2BGLN A 110     2433   2187   1903   -181   -110   -158       N  
ATOM    927  N   THR A 111      13.508   2.467  -0.876  1.00 15.42           N  
ANISOU  927  N   THR A 111     2128   2018   1715   -155   -202   -122       N  
ATOM    928  CA  THR A 111      12.177   2.177  -0.420  1.00 15.01           C  
ANISOU  928  CA  THR A 111     2075   1977   1651   -162   -225   -111       C  
ATOM    929  C   THR A 111      12.007   0.676  -0.190  1.00 14.44           C  
ANISOU  929  C   THR A 111     2020   1891   1577   -166   -214   -120       C  
ATOM    930  O   THR A 111      12.800  -0.137  -0.654  1.00 15.56           O  
ANISOU  930  O   THR A 111     2183   2012   1718   -169   -183   -138       O  
ATOM    931  CB  THR A 111      11.189   2.708  -1.461  1.00 15.57           C  
ANISOU  931  CB  THR A 111     2156   2063   1695   -197   -243    -94       C  
ATOM    932  OG1 THR A 111      11.488   2.051  -2.697  1.00 16.40           O  
ANISOU  932  OG1 THR A 111     2302   2157   1773   -229   -226   -109       O  
ATOM    933  CG2 THR A 111      11.297   4.211  -1.623  1.00 15.53           C  
ANISOU  933  CG2 THR A 111     2132   2071   1698   -190   -254    -81       C  
ATOM    934  N   PHE A 112      10.950   0.319   0.518  1.00 13.51           N  
ANISOU  934  N   PHE A 112     1891   1782   1460   -163   -234   -104       N  
ATOM    935  CA  PHE A 112      10.598  -1.063   0.784  1.00 13.06           C  
ANISOU  935  CA  PHE A 112     1846   1713   1403   -170   -231   -107       C  
ATOM    936  C   PHE A 112       9.173  -1.129   1.275  1.00 12.87           C  
ANISOU  936  C   PHE A 112     1805   1706   1378   -175   -261    -74       C  
ATOM    937  O   PHE A 112       8.617  -0.121   1.728  1.00 12.86           O  
ANISOU  937  O   PHE A 112     1779   1722   1383   -158   -274    -50       O  
ATOM    938  CB  PHE A 112      11.550  -1.690   1.813  1.00 13.30           C  
ANISOU  938  CB  PHE A 112     1862   1730   1462   -136   -210   -121       C  
ATOM    939  CG  PHE A 112      11.648  -0.996   3.149  1.00 13.25           C  
ANISOU  939  CG  PHE A 112     1824   1736   1476   -101   -224   -109       C  
ATOM    940  CD1 PHE A 112      12.527   0.058   3.340  1.00 14.26           C  
ANISOU  940  CD1 PHE A 112     1942   1864   1613    -87   -225   -112       C  
ATOM    941  CD2 PHE A 112      10.881  -1.409   4.218  1.00 13.58           C  
ANISOU  941  CD2 PHE A 112     1852   1784   1524    -84   -236    -94       C  
ATOM    942  CE1 PHE A 112      12.649   0.667   4.581  1.00 14.94           C  
ANISOU  942  CE1 PHE A 112     2015   1953   1709    -61   -241   -105       C  
ATOM    943  CE2 PHE A 112      11.024  -0.820   5.466  1.00 14.05           C  
ANISOU  943  CE2 PHE A 112     1897   1848   1592    -52   -244    -86       C  
ATOM    944  CZ  PHE A 112      11.895   0.226   5.637  1.00 14.59           C  
ANISOU  944  CZ  PHE A 112     1967   1914   1664    -43   -248    -94       C  
ATOM    945  N   SER A 113       8.584  -2.325   1.254  1.00 12.27           N  
ANISOU  945  N   SER A 113     1742   1622   1298   -194   -268    -68       N  
ATOM    946  CA  SER A 113       7.231  -2.520   1.754  1.00 12.47           C  
ANISOU  946  CA  SER A 113     1744   1662   1331   -198   -296    -25       C  
ATOM    947  C   SER A 113       7.324  -3.072   3.152  1.00 12.94           C  
ANISOU  947  C   SER A 113     1779   1720   1416   -156   -286    -23       C  
ATOM    948  O   SER A 113       8.199  -3.891   3.424  1.00 13.55           O  
ANISOU  948  O   SER A 113     1868   1781   1502   -147   -266    -53       O  
ATOM    949  CB  SER A 113       6.494  -3.535   0.894  1.00 13.09           C  
ANISOU  949  CB  SER A 113     1853   1730   1390   -252   -320    -12       C  
ATOM    950  OG  SER A 113       6.426  -3.026  -0.426  1.00 14.30           O  
ANISOU  950  OG  SER A 113     2038   1885   1513   -296   -333    -13       O  
ATOM    951  N   VAL A 114       6.388  -2.710   4.000  1.00 12.29           N  
ANISOU  951  N   VAL A 114     1666   1656   1348   -132   -296     16       N  
ATOM    952  CA  VAL A 114       6.309  -3.243   5.354  1.00 12.81           C  
ANISOU  952  CA  VAL A 114     1711   1722   1433    -93   -287     25       C  
ATOM    953  C   VAL A 114       5.016  -4.014   5.481  1.00 13.03           C  
ANISOU  953  C   VAL A 114     1720   1758   1472   -107   -308     73       C  
ATOM    954  O   VAL A 114       3.956  -3.520   5.093  1.00 13.21           O  
ANISOU  954  O   VAL A 114     1727   1794   1497   -122   -325    121       O  
ATOM    955  CB  VAL A 114       6.321  -2.096   6.393  1.00 12.98           C  
ANISOU  955  CB  VAL A 114     1719   1753   1458    -46   -275     34       C  
ATOM    956  CG1 VAL A 114       5.995  -2.605   7.800  1.00 13.23           C  
ANISOU  956  CG1 VAL A 114     1736   1787   1503     -6   -266     52       C  
ATOM    957  CG2 VAL A 114       7.642  -1.359   6.377  1.00 13.58           C  
ANISOU  957  CG2 VAL A 114     1813   1819   1527    -37   -264     -7       C  
ATOM    958  N   LEU A 115       5.084  -5.218   6.060  1.00 12.47           N  
ANISOU  958  N   LEU A 115     1646   1679   1415   -102   -306     70       N  
ATOM    959  CA  LEU A 115       3.894  -5.974   6.346  1.00 12.54           C  
ANISOU  959  CA  LEU A 115     1630   1694   1439   -111   -327    122       C  
ATOM    960  C   LEU A 115       3.703  -5.818   7.851  1.00 12.81           C  
ANISOU  960  C   LEU A 115     1635   1741   1492    -51   -306    143       C  
ATOM    961  O   LEU A 115       4.403  -6.474   8.629  1.00 13.18           O  
ANISOU  961  O   LEU A 115     1683   1779   1546    -29   -292    116       O  
ATOM    962  CB  LEU A 115       4.037  -7.458   5.964  1.00 12.90           C  
ANISOU  962  CB  LEU A 115     1697   1718   1487   -147   -340    106       C  
ATOM    963  CG  LEU A 115       2.822  -8.307   6.284  1.00 14.50           C  
ANISOU  963  CG  LEU A 115     1872   1925   1710   -160   -368    165       C  
ATOM    964  CD1 LEU A 115       1.620  -7.870   5.469  1.00 15.37           C  
ANISOU  964  CD1 LEU A 115     1973   2049   1819   -202   -406    224       C  
ATOM    965  CD2 LEU A 115       3.100  -9.764   6.033  1.00 14.68           C  
ANISOU  965  CD2 LEU A 115     1923   1921   1735   -192   -377    142       C  
ATOM    966  N  AALA A 116       2.831  -4.892   8.282  0.50 12.53           N  
ANISOU  966  N  AALA A 116     1576   1721   1462    -22   -299    190       N  
ATOM    967  N  BALA A 116       2.781  -4.931   8.250  0.50 12.98           N  
ANISOU  967  N  BALA A 116     1632   1778   1520    -24   -300    193       N  
ATOM    968  CA AALA A 116       2.624  -4.675   9.718  0.50 13.17           C  
ANISOU  968  CA AALA A 116     1643   1809   1552     39   -271    210       C  
ATOM    969  CA BALA A 116       2.439  -4.683   9.648  0.50 14.18           C  
ANISOU  969  CA BALA A 116     1766   1938   1682     36   -274    220       C  
ATOM    970  C  AALA A 116       1.810  -5.835  10.275  0.50 13.37           C  
ANISOU  970  C  AALA A 116     1638   1840   1603     43   -280    257       C  
ATOM    971  C  BALA A 116       1.816  -5.963  10.194  0.50 14.72           C  
ANISOU  971  C  BALA A 116     1808   2010   1775     37   -283    256       C  
ATOM    972  O  AALA A 116       0.739  -6.137   9.755  0.50 13.60           O  
ANISOU  972  O  AALA A 116     1640   1877   1651     17   -302    314       O  
ATOM    973  O  BALA A 116       0.984  -6.577   9.520  0.50 15.10           O  
ANISOU  973  O  BALA A 116     1837   2061   1839     -2   -313    298       O  
ATOM    974  CB AALA A 116       1.907  -3.354   9.963  0.50 13.83           C  
ANISOU  974  CB AALA A 116     1721   1901   1635     74   -249    250       C  
ATOM    975  CB BALA A 116       1.442  -3.535   9.736  0.50 14.78           C  
ANISOU  975  CB BALA A 116     1826   2025   1765     62   -258    276       C  
ATOM    976  N  ACYS A 117       2.327  -6.495  11.304  0.75 13.30           N  
ANISOU  976  N  ACYS A 117     1629   1828   1597     71   -266    237       N  
ATOM    977  N  BCYS A 117       2.247  -6.387  11.372  0.25 14.79           N  
ANISOU  977  N  BCYS A 117     1817   2018   1786     76   -264    241       N  
ATOM    978  CA ACYS A 117       1.697  -7.643  11.954  0.75 13.87           C  
ANISOU  978  CA ACYS A 117     1670   1905   1694     80   -272    278       C  
ATOM    979  CA BCYS A 117       1.815  -7.651  11.942  0.25 15.40           C  
ANISOU  979  CA BCYS A 117     1867   2097   1886     78   -272    270       C  
ATOM    980  C  ACYS A 117       1.506  -7.426  13.414  0.75 14.56           C  
ANISOU  980  C  ACYS A 117     1750   2001   1782    142   -240    300       C  
ATOM    981  C  BCYS A 117       1.597  -7.519  13.450  0.25 15.40           C  
ANISOU  981  C  BCYS A 117     1857   2107   1888    141   -240    295       C  
ATOM    982  O  ACYS A 117       2.265  -6.683  14.028  0.75 14.38           O  
ANISOU  982  O  ACYS A 117     1758   1973   1732    170   -218    262       O  
ATOM    983  O  BCYS A 117       2.357  -6.821  14.110  0.25 15.48           O  
ANISOU  983  O  BCYS A 117     1897   2112   1872    170   -219    258       O  
ATOM    984  CB ACYS A 117       2.543  -8.892  11.752  0.75 14.43           C  
ANISOU  984  CB ACYS A 117     1751   1960   1771     49   -287    233       C  
ATOM    985  CB BCYS A 117       2.882  -8.701  11.636  0.25 16.62           C  
ANISOU  985  CB BCYS A 117     2039   2234   2040     47   -284    214       C  
ATOM    986  SG ACYS A 117       2.803  -9.323  10.034  0.75 14.59           S  
ANISOU  986  SG ACYS A 117     1800   1960   1782    -24   -317    203       S  
ATOM    987  SG BCYS A 117       2.292 -10.412  11.656  0.25 20.52           S  
ANISOU  987  SG BCYS A 117     2509   2722   2567     20   -309    245       S  
ATOM    988  N   TYR A 118       0.570  -8.188  13.997  1.00 15.18           N  
ANISOU  988  N   TYR A 118     1791   2090   1887    158   -239    360       N  
ATOM    989  CA  TYR A 118       0.296  -8.220  15.447  1.00 16.61           C  
ANISOU  989  CA  TYR A 118     1964   2278   2067    219   -205    388       C  
ATOM    990  C   TYR A 118      -0.002  -9.668  15.797  1.00 18.17           C  
ANISOU  990  C   TYR A 118     2126   2481   2297    210   -223    416       C  
ATOM    991  O   TYR A 118      -0.763 -10.310  15.085  1.00 18.33           O  
ANISOU  991  O   TYR A 118     2115   2504   2348    173   -253    459       O  
ATOM    992  CB  TYR A 118      -0.905  -7.330  15.835  1.00 17.19           C  
ANISOU  992  CB  TYR A 118     2023   2361   2148    267   -169    462       C  
ATOM    993  CG  TYR A 118      -0.613  -5.889  15.531  1.00 17.88           C  
ANISOU  993  CG  TYR A 118     2149   2438   2205    279   -148    434       C  
ATOM    994  CD1 TYR A 118       0.120  -5.113  16.416  1.00 18.60           C  
ANISOU  994  CD1 TYR A 118     2294   2518   2255    318   -117    390       C  
ATOM    995  CD2 TYR A 118      -0.904  -5.351  14.286  1.00 18.85           C  
ANISOU  995  CD2 TYR A 118     2263   2562   2337    240   -169    444       C  
ATOM    996  CE1 TYR A 118       0.471  -3.810  16.108  1.00 19.34           C  
ANISOU  996  CE1 TYR A 118     2428   2598   2321    323   -102    360       C  
ATOM    997  CE2 TYR A 118      -0.509  -4.069  13.946  1.00 19.60           C  
ANISOU  997  CE2 TYR A 118     2393   2647   2406    246   -153    412       C  
ATOM    998  CZ  TYR A 118       0.167  -3.297  14.865  1.00 20.22           C  
ANISOU  998  CZ  TYR A 118     2523   2712   2448    289   -119    371       C  
ATOM    999  OH  TYR A 118       0.539  -2.027  14.526  1.00 21.79           O  
ANISOU  999  OH  TYR A 118     2759   2898   2623    292   -107    342       O  
ATOM   1000  N   ASN A 119       0.643 -10.210  16.842  1.00 18.87           N  
ANISOU 1000  N   ASN A 119     2222   2571   2379    235   -211    393       N  
ATOM   1001  CA  ASN A 119       0.439 -11.600  17.254  1.00 20.10           C  
ANISOU 1001  CA  ASN A 119     2341   2729   2567    229   -226    418       C  
ATOM   1002  C   ASN A 119       0.702 -12.594  16.117  1.00 19.55           C  
ANISOU 1002  C   ASN A 119     2266   2644   2519    164   -266    395       C  
ATOM   1003  O   ASN A 119      -0.008 -13.593  15.977  1.00 20.20           O  
ANISOU 1003  O   ASN A 119     2314   2726   2635    144   -290    439       O  
ATOM   1004  CB  ASN A 119      -0.981 -11.790  17.805  1.00 22.64           C  
ANISOU 1004  CB  ASN A 119     2617   3068   2918    263   -213    512       C  
ATOM   1005  CG  ASN A 119      -1.294 -10.896  18.970  1.00 27.97           C  
ANISOU 1005  CG  ASN A 119     3308   3751   3568    333   -160    538       C  
ATOM   1006  OD1 ASN A 119      -2.158 -10.021  18.891  1.00 30.85           O  
ANISOU 1006  OD1 ASN A 119     3668   4120   3934    362   -133    588       O  
ATOM   1007  ND2 ASN A 119      -0.591 -11.091  20.070  1.00 29.18           N  
ANISOU 1007  ND2 ASN A 119     3485   3905   3698    362   -143    508       N  
ATOM   1008  N   GLY A 120       1.679 -12.285  15.272  1.00 18.20           N  
ANISOU 1008  N   GLY A 120     2131   2457   2328    131   -274    329       N  
ATOM   1009  CA  GLY A 120       2.021 -13.141  14.143  1.00 17.98           C  
ANISOU 1009  CA  GLY A 120     2116   2406   2310     73   -301    300       C  
ATOM   1010  C   GLY A 120       1.039 -13.089  12.987  1.00 18.05           C  
ANISOU 1010  C   GLY A 120     2124   2411   2323     27   -334    335       C  
ATOM   1011  O   GLY A 120       1.168 -13.860  12.037  1.00 18.15           O  
ANISOU 1011  O   GLY A 120     2158   2400   2337    -27   -360    316       O  
ATOM   1012  N   SER A 121       0.031 -12.200  13.059  1.00 17.88           N  
ANISOU 1012  N   SER A 121     2081   2410   2303     45   -332    393       N  
ATOM   1013  CA  SER A 121      -0.988 -12.098  12.025  1.00 19.05           C  
ANISOU 1013  CA  SER A 121     2219   2559   2461     -2   -369    444       C  
ATOM   1014  C   SER A 121      -0.884 -10.784  11.263  1.00 19.31           C  
ANISOU 1014  C   SER A 121     2273   2595   2467    -10   -363    428       C  
ATOM   1015  O   SER A 121      -0.858  -9.709  11.855  1.00 18.83           O  
ANISOU 1015  O   SER A 121     2210   2548   2397     40   -327    432       O  
ATOM   1016  CB  SER A 121      -2.379 -12.227  12.637  1.00 21.46           C  
ANISOU 1016  CB  SER A 121     2465   2885   2805     22   -374    548       C  
ATOM   1017  OG  SER A 121      -2.553 -13.527  13.175  1.00 25.54           O  
ANISOU 1017  OG  SER A 121     2958   3397   3349     18   -389    568       O  
ATOM   1018  N   PRO A 122      -0.842 -10.855   9.929  1.00 20.18           N  
ANISOU 1018  N   PRO A 122     2413   2691   2563    -75   -399    411       N  
ATOM   1019  CA  PRO A 122      -0.716  -9.623   9.136  1.00 20.36           C  
ANISOU 1019  CA  PRO A 122     2456   2719   2562    -87   -395    397       C  
ATOM   1020  C   PRO A 122      -1.952  -8.725   9.210  1.00 20.01           C  
ANISOU 1020  C   PRO A 122     2367   2697   2538    -69   -395    485       C  
ATOM   1021  O   PRO A 122      -3.095  -9.193   9.177  1.00 20.24           O  
ANISOU 1021  O   PRO A 122     2354   2734   2600    -88   -424    570       O  
ATOM   1022  CB  PRO A 122      -0.453 -10.148   7.715  1.00 22.14           C  
ANISOU 1022  CB  PRO A 122     2727   2920   2764   -165   -436    364       C  
ATOM   1023  CG  PRO A 122       0.095 -11.574   7.925  1.00 22.93           C  
ANISOU 1023  CG  PRO A 122     2849   2995   2868   -178   -438    324       C  
ATOM   1024  CD  PRO A 122      -0.761 -12.055   9.076  1.00 20.91           C  
ANISOU 1024  CD  PRO A 122     2534   2757   2652   -142   -439    393       C  
ATOM   1025  N   SER A 123      -1.723  -7.421   9.339  1.00 19.28           N  
ANISOU 1025  N   SER A 123     2282   2613   2432    -32   -360    472       N  
ATOM   1026  CA  SER A 123      -2.812  -6.455   9.398  1.00 19.98           C  
ANISOU 1026  CA  SER A 123     2331   2718   2542     -8   -348    555       C  
ATOM   1027  C   SER A 123      -2.866  -5.587   8.166  1.00 19.22           C  
ANISOU 1027  C   SER A 123     2247   2623   2433    -52   -369    555       C  
ATOM   1028  O   SER A 123      -3.958  -5.209   7.743  1.00 19.82           O  
ANISOU 1028  O   SER A 123     2283   2711   2537    -68   -386    643       O  
ATOM   1029  CB  SER A 123      -2.716  -5.583  10.640  1.00 23.07           C  
ANISOU 1029  CB  SER A 123     2721   3113   2931     77   -283    556       C  
ATOM   1030  OG  SER A 123      -1.507  -4.852  10.632  1.00 27.68           O  
ANISOU 1030  OG  SER A 123     3356   3686   3475     89   -263    467       O  
ATOM   1031  N   GLY A 124      -1.705  -5.226   7.622  1.00 17.37           N  
ANISOU 1031  N   GLY A 124     2063   2377   2159    -69   -366    466       N  
ATOM   1032  CA  GLY A 124      -1.677  -4.368   6.453  1.00 16.81           C  
ANISOU 1032  CA  GLY A 124     2006   2308   2073   -109   -383    464       C  
ATOM   1033  C   GLY A 124      -0.319  -4.237   5.824  1.00 15.64           C  
ANISOU 1033  C   GLY A 124     1914   2145   1884   -130   -381    366       C  
ATOM   1034  O   GLY A 124       0.683  -4.635   6.408  1.00 14.83           O  
ANISOU 1034  O   GLY A 124     1835   2030   1769   -105   -358    302       O  
ATOM   1035  N   VAL A 125      -0.281  -3.697   4.620  1.00 15.52           N  
ANISOU 1035  N   VAL A 125     1915   2130   1850   -177   -403    362       N  
ATOM   1036  CA  VAL A 125       0.955  -3.526   3.900  1.00 16.15           C  
ANISOU 1036  CA  VAL A 125     2046   2196   1894   -198   -398    280       C  
ATOM   1037  C   VAL A 125       1.037  -2.116   3.362  1.00 16.23           C  
ANISOU 1037  C   VAL A 125     2054   2216   1896   -194   -388    283       C  
ATOM   1038  O   VAL A 125       0.028  -1.552   2.933  1.00 16.69           O  
ANISOU 1038  O   VAL A 125     2082   2289   1970   -211   -406    352       O  
ATOM   1039  CB  VAL A 125       1.136  -4.627   2.825  1.00 18.52           C  
ANISOU 1039  CB  VAL A 125     2389   2477   2169   -270   -434    256       C  
ATOM   1040  CG1 VAL A 125       0.022  -4.589   1.791  1.00 20.02           C  
ANISOU 1040  CG1 VAL A 125     2575   2676   2356   -337   -487    322       C  
ATOM   1041  CG2 VAL A 125       2.511  -4.563   2.175  1.00 19.01           C  
ANISOU 1041  CG2 VAL A 125     2505   2520   2196   -278   -413    171       C  
ATOM   1042  N   TYR A 126       2.205  -1.514   3.481  1.00 16.20           N  
ANISOU 1042  N   TYR A 126     2076   2204   1874   -167   -359    217       N  
ATOM   1043  CA  TYR A 126       2.408  -0.148   3.015  1.00 16.17           C  
ANISOU 1043  CA  TYR A 126     2073   2207   1864   -161   -349    215       C  
ATOM   1044  C   TYR A 126       3.842   0.066   2.588  1.00 15.60           C  
ANISOU 1044  C   TYR A 126     2039   2122   1767   -165   -336    139       C  
ATOM   1045  O   TYR A 126       4.736  -0.688   2.960  1.00 15.94           O  
ANISOU 1045  O   TYR A 126     2102   2149   1804   -156   -324     92       O  
ATOM   1046  CB  TYR A 126       1.958   0.884   4.064  1.00 16.49           C  
ANISOU 1046  CB  TYR A 126     2086   2252   1926    -98   -316    249       C  
ATOM   1047  CG  TYR A 126       2.669   0.757   5.389  1.00 17.12           C  
ANISOU 1047  CG  TYR A 126     2180   2320   2004    -43   -285    209       C  
ATOM   1048  CD1 TYR A 126       3.901   1.356   5.601  1.00 17.77           C  
ANISOU 1048  CD1 TYR A 126     2293   2390   2069    -27   -271    147       C  
ATOM   1049  CD2 TYR A 126       2.115   0.027   6.430  1.00 18.46           C  
ANISOU 1049  CD2 TYR A 126     2334   2491   2190    -13   -275    237       C  
ATOM   1050  CE1 TYR A 126       4.560   1.241   6.817  1.00 18.59           C  
ANISOU 1050  CE1 TYR A 126     2413   2482   2168     14   -252    117       C  
ATOM   1051  CE2 TYR A 126       2.758  -0.085   7.654  1.00 19.26           C  
ANISOU 1051  CE2 TYR A 126     2452   2581   2283     33   -250    202       C  
ATOM   1052  CZ  TYR A 126       3.979   0.529   7.845  1.00 19.71           C  
ANISOU 1052  CZ  TYR A 126     2542   2625   2320     43   -241    143       C  
ATOM   1053  OH  TYR A 126       4.608   0.427   9.064  1.00 22.38           O  
ANISOU 1053  OH  TYR A 126     2901   2953   2649     80   -226    116       O  
ATOM   1054  N  AGLN A 127       4.050   1.061   1.748  0.50 15.62           N  
ANISOU 1054  N  AGLN A 127     2048   2129   1759   -181   -338    136       N  
ATOM   1055  N  BGLN A 127       4.090   1.164   1.886  0.50 15.49           N  
ANISOU 1055  N  BGLN A 127     2029   2111   1743   -174   -334    134       N  
ATOM   1056  CA AGLN A 127       5.336   1.360   1.175  0.50 15.80           C  
ANISOU 1056  CA AGLN A 127     2100   2140   1761   -189   -326     78       C  
ATOM   1057  CA BGLN A 127       5.413   1.506   1.423  0.50 15.72           C  
ANISOU 1057  CA BGLN A 127     2088   2131   1755   -177   -321     75       C  
ATOM   1058  C  AGLN A 127       5.965   2.540   1.890  0.50 16.49           C  
ANISOU 1058  C  AGLN A 127     2180   2225   1858   -142   -304     61       C  
ATOM   1059  C  BGLN A 127       6.095   2.480   2.372  0.50 16.20           C  
ANISOU 1059  C  BGLN A 127     2144   2186   1826   -125   -297     55       C  
ATOM   1060  O  AGLN A 127       5.306   3.560   2.092  0.50 16.63           O  
ANISOU 1060  O  AGLN A 127     2180   2252   1888   -123   -300     97       O  
ATOM   1061  O  BGLN A 127       5.462   3.402   2.878  0.50 16.36           O  
ANISOU 1061  O  BGLN A 127     2147   2211   1858    -97   -289     88       O  
ATOM   1062  CB AGLN A 127       5.117   1.674  -0.313  0.50 16.38           C  
ANISOU 1062  CB AGLN A 127     2189   2223   1814   -245   -349     91       C  
ATOM   1063  CB BGLN A 127       5.315   2.096   0.015  0.50 17.00           C  
ANISOU 1063  CB BGLN A 127     2260   2301   1899   -223   -338     85       C  
ATOM   1064  CG AGLN A 127       6.368   1.792  -1.131  0.50 18.09           C  
ANISOU 1064  CG AGLN A 127     2441   2428   2006   -261   -336     39       C  
ATOM   1065  CG BGLN A 127       6.631   2.112  -0.715  0.50 19.17           C  
ANISOU 1065  CG BGLN A 127     2569   2563   2152   -236   -324     30       C  
ATOM   1066  CD AGLN A 127       7.089   0.490  -1.349  0.50 18.85           C  
ANISOU 1066  CD AGLN A 127     2576   2501   2085   -274   -323     -4       C  
ATOM   1067  CD BGLN A 127       7.033   0.761  -1.249  0.50 19.69           C  
ANISOU 1067  CD BGLN A 127     2674   2610   2195   -268   -323      0       C  
ATOM   1068  OE1AGLN A 127       6.666  -0.598  -0.912  0.50 18.45           O  
ANISOU 1068  OE1AGLN A 127     2529   2441   2039   -277   -329      1       O  
ATOM   1069  OE1BGLN A 127       6.501  -0.300  -0.868  0.50 20.09           O  
ANISOU 1069  OE1BGLN A 127     2729   2655   2250   -275   -333     10       O  
ATOM   1070  NE2AGLN A 127       8.210   0.583  -2.023  0.50 19.51           N  
ANISOU 1070  NE2AGLN A 127     2689   2572   2154   -278   -299    -43       N  
ATOM   1071  NE2BGLN A 127       8.008   0.774  -2.125  0.50 19.03           N  
ANISOU 1071  NE2BGLN A 127     2625   2514   2090   -283   -305    -36       N  
ATOM   1072  N  ACYS A 128       7.225   2.400   2.294  0.50 16.47           N  
ANISOU 1072  N  ACYS A 128     2195   2209   1853   -124   -288     13       N  
ATOM   1073  N  BCYS A 128       7.382   2.261   2.606  0.50 16.43           N  
ANISOU 1073  N  BCYS A 128     2191   2201   1851   -114   -285      6       N  
ATOM   1074  CA ACYS A 128       7.942   3.478   2.975  0.50 16.78           C  
ANISOU 1074  CA ACYS A 128     2236   2241   1898    -89   -277     -4       C  
ATOM   1075  CA BCYS A 128       8.255   3.071   3.448  0.50 17.09           C  
ANISOU 1075  CA BCYS A 128     2279   2275   1941    -78   -273    -16       C  
ATOM   1076  C  ACYS A 128       9.416   3.592   2.486  0.50 16.85           C  
ANISOU 1076  C  ACYS A 128     2259   2239   1904    -99   -272    -44       C  
ATOM   1077  C  BCYS A 128       9.557   3.356   2.718  0.50 17.04           C  
ANISOU 1077  C  BCYS A 128     2284   2260   1930    -94   -270    -49       C  
ATOM   1078  O  ACYS A 128       9.746   3.008   1.463  0.50 16.70           O  
ANISOU 1078  O  ACYS A 128     2252   2219   1876   -130   -269    -57       O  
ATOM   1079  O  BCYS A 128       9.936   2.632   1.810  0.50 16.87           O  
ANISOU 1079  O  BCYS A 128     2274   2236   1902   -123   -266    -63       O  
ATOM   1080  CB ACYS A 128       7.831   3.331   4.489  0.50 17.30           C  
ANISOU 1080  CB ACYS A 128     2301   2299   1972    -46   -267     -1       C  
ATOM   1081  CB BCYS A 128       8.549   2.332   4.751  0.50 18.43           C  
ANISOU 1081  CB BCYS A 128     2450   2435   2118    -49   -266    -27       C  
ATOM   1082  SG ACYS A 128       8.691   1.883   5.141  0.50 19.72           S  
ANISOU 1082  SG ACYS A 128     2613   2596   2283    -42   -265    -31       S  
ATOM   1083  SG BCYS A 128       7.272   2.509   6.011  0.50 23.03           S  
ANISOU 1083  SG BCYS A 128     3024   3023   2705     -8   -258     13       S  
ATOM   1084  N   ALA A 129      10.286   4.364   3.171  1.00 17.09           N  
ANISOU 1084  N   ALA A 129     2293   2258   1942    -75   -270    -59       N  
ATOM   1085  CA  ALA A 129      11.650   4.578   2.712  1.00 17.20           C  
ANISOU 1085  CA  ALA A 129     2310   2263   1962    -84   -268    -82       C  
ATOM   1086  C   ALA A 129      12.538   4.679   3.922  1.00 16.36           C  
ANISOU 1086  C   ALA A 129     2206   2142   1869    -61   -274    -91       C  
ATOM   1087  O   ALA A 129      12.115   5.142   4.987  1.00 17.23           O  
ANISOU 1087  O   ALA A 129     2327   2246   1972    -39   -283    -85       O  
ATOM   1088  CB  ALA A 129      11.767   5.848   1.894  1.00 17.51           C  
ANISOU 1088  CB  ALA A 129     2348   2306   1999    -96   -273    -76       C  
ATOM   1089  N   MET A 130      13.787   4.272   3.753  1.00 14.85           N  
ANISOU 1089  N   MET A 130     2008   1942   1694    -68   -270   -101       N  
ATOM   1090  CA  MET A 130      14.793   4.474   4.787  1.00 14.43           C  
ANISOU 1090  CA  MET A 130     1952   1873   1656    -57   -286    -99       C  
ATOM   1091  C   MET A 130      15.149   5.964   4.667  1.00 14.95           C  
ANISOU 1091  C   MET A 130     2025   1933   1720    -61   -307    -95       C  
ATOM   1092  O   MET A 130      15.626   6.382   3.618  1.00 15.32           O  
ANISOU 1092  O   MET A 130     2061   1984   1776    -75   -301    -92       O  
ATOM   1093  CB  MET A 130      16.023   3.600   4.511  1.00 14.88           C  
ANISOU 1093  CB  MET A 130     1989   1922   1742    -63   -271    -96       C  
ATOM   1094  CG  MET A 130      17.144   3.773   5.526  1.00 16.66           C  
ANISOU 1094  CG  MET A 130     2203   2135   1991    -60   -295    -81       C  
ATOM   1095  SD  MET A 130      16.663   3.502   7.255  1.00 17.10           S  
ANISOU 1095  SD  MET A 130     2278   2187   2031    -45   -322    -81       S  
ATOM   1096  CE  MET A 130      15.931   1.868   7.146  1.00 15.89           C  
ANISOU 1096  CE  MET A 130     2113   2043   1880    -35   -287    -88       C  
ATOM   1097  N   ARG A 131      14.805   6.763   5.672  1.00 14.67           N  
ANISOU 1097  N   ARG A 131     2015   1887   1670    -48   -327    -94       N  
ATOM   1098  CA  ARG A 131      15.075   8.199   5.615  1.00 14.63           C  
ANISOU 1098  CA  ARG A 131     2027   1870   1662    -53   -347    -91       C  
ATOM   1099  C   ARG A 131      16.579   8.470   5.700  1.00 15.11           C  
ANISOU 1099  C   ARG A 131     2077   1917   1747    -72   -374    -82       C  
ATOM   1100  O   ARG A 131      17.321   7.663   6.261  1.00 15.31           O  
ANISOU 1100  O   ARG A 131     2090   1938   1788    -75   -383    -74       O  
ATOM   1101  CB  ARG A 131      14.359   8.906   6.784  1.00 14.75           C  
ANISOU 1101  CB  ARG A 131     2088   1867   1650    -32   -355    -94       C  
ATOM   1102  CG  ARG A 131      12.853   8.693   6.868  1.00 15.21           C  
ANISOU 1102  CG  ARG A 131     2152   1936   1693     -8   -325    -88       C  
ATOM   1103  CD  ARG A 131      12.112   9.087   5.600  1.00 15.22           C  
ANISOU 1103  CD  ARG A 131     2128   1956   1700    -15   -307    -75       C  
ATOM   1104  NE  ARG A 131      12.512  10.422   5.144  1.00 14.93           N  
ANISOU 1104  NE  ARG A 131     2100   1907   1667    -24   -319    -75       N  
ATOM   1105  CZ  ARG A 131      12.205  10.925   3.951  1.00 14.97           C  
ANISOU 1105  CZ  ARG A 131     2081   1926   1680    -38   -312    -63       C  
ATOM   1106  NH1 ARG A 131      11.460  10.230   3.101  1.00 14.04           N  
ANISOU 1106  NH1 ARG A 131     1936   1834   1563    -48   -297    -50       N  
ATOM   1107  NH2 ARG A 131      12.629  12.136   3.606  1.00 14.38           N  
ANISOU 1107  NH2 ARG A 131     2013   1839   1611    -45   -325    -61       N  
ATOM   1108  N   PRO A 132      17.057   9.636   5.226  1.00 15.38           N  
ANISOU 1108  N   PRO A 132     2112   1942   1788    -85   -393    -75       N  
ATOM   1109  CA  PRO A 132      18.491   9.948   5.366  1.00 15.82           C  
ANISOU 1109  CA  PRO A 132     2154   1985   1874   -105   -426    -54       C  
ATOM   1110  C   PRO A 132      18.982   9.985   6.832  1.00 16.21           C  
ANISOU 1110  C   PRO A 132     2233   2010   1915   -113   -469    -47       C  
ATOM   1111  O   PRO A 132      20.180   9.803   7.070  1.00 17.50           O  
ANISOU 1111  O   PRO A 132     2373   2166   2109   -134   -498    -19       O  
ATOM   1112  CB  PRO A 132      18.614  11.299   4.676  1.00 16.65           C  
ANISOU 1112  CB  PRO A 132     2262   2083   1981   -116   -440    -48       C  
ATOM   1113  CG  PRO A 132      17.506  11.284   3.656  1.00 16.44           C  
ANISOU 1113  CG  PRO A 132     2227   2079   1941   -105   -399    -61       C  
ATOM   1114  CD  PRO A 132      16.361  10.665   4.424  1.00 15.17           C  
ANISOU 1114  CD  PRO A 132     2092   1921   1752    -84   -383    -77       C  
ATOM   1115  N   ASN A 133      18.087  10.206   7.816  1.00 14.91           N  
ANISOU 1115  N   ASN A 133     2123   1833   1710    -98   -473    -67       N  
ATOM   1116  CA  ASN A 133      18.488  10.161   9.234  1.00 14.67           C  
ANISOU 1116  CA  ASN A 133     2134   1779   1661   -109   -513    -62       C  
ATOM   1117  C   ASN A 133      18.338   8.731   9.835  1.00 14.76           C  
ANISOU 1117  C   ASN A 133     2127   1806   1674    -96   -496    -62       C  
ATOM   1118  O   ASN A 133      18.393   8.562  11.050  1.00 14.97           O  
ANISOU 1118  O   ASN A 133     2193   1818   1678    -99   -521    -61       O  
ATOM   1119  CB  ASN A 133      17.697  11.176  10.071  1.00 15.33           C  
ANISOU 1119  CB  ASN A 133     2299   1833   1694    -97   -521    -83       C  
ATOM   1120  CG  ASN A 133      16.214  10.909  10.098  1.00 15.79           C  
ANISOU 1120  CG  ASN A 133     2370   1903   1728    -56   -467   -100       C  
ATOM   1121  OD1 ASN A 133      15.728   9.883   9.605  1.00 15.06           O  
ANISOU 1121  OD1 ASN A 133     2231   1841   1651    -41   -433    -99       O  
ATOM   1122  ND2 ASN A 133      15.454  11.831  10.669  1.00 16.61           N  
ANISOU 1122  ND2 ASN A 133     2540   1978   1793    -36   -456   -112       N  
ATOM   1123  N   PHE A 134      18.104   7.718   8.982  1.00 14.43           N  
ANISOU 1123  N   PHE A 134     2034   1791   1657    -83   -454    -63       N  
ATOM   1124  CA  PHE A 134      18.012   6.312   9.351  1.00 15.16           C  
ANISOU 1124  CA  PHE A 134     2103   1897   1760    -72   -434    -60       C  
ATOM   1125  C   PHE A 134      16.803   5.931  10.198  1.00 15.02           C  
ANISOU 1125  C   PHE A 134     2120   1882   1706    -47   -419    -77       C  
ATOM   1126  O   PHE A 134      16.792   4.877  10.839  1.00 15.26           O  
ANISOU 1126  O   PHE A 134     2138   1918   1740    -40   -414    -72       O  
ATOM   1127  CB  PHE A 134      19.291   5.830  10.006  1.00 15.66           C  
ANISOU 1127  CB  PHE A 134     2145   1952   1854    -93   -468    -29       C  
ATOM   1128  CG  PHE A 134      20.480   5.964   9.086  1.00 17.62           C  
ANISOU 1128  CG  PHE A 134     2344   2200   2151   -112   -470      0       C  
ATOM   1129  CD1 PHE A 134      20.732   5.016   8.114  1.00 19.31           C  
ANISOU 1129  CD1 PHE A 134     2511   2428   2400   -101   -422      8       C  
ATOM   1130  CD2 PHE A 134      21.369   7.012   9.226  1.00 19.06           C  
ANISOU 1130  CD2 PHE A 134     2532   2365   2344   -140   -520     26       C  
ATOM   1131  CE1 PHE A 134      21.843   5.131   7.281  1.00 20.53           C  
ANISOU 1131  CE1 PHE A 134     2621   2578   2600   -110   -413     42       C  
ATOM   1132  CE2 PHE A 134      22.476   7.120   8.396  1.00 20.32           C  
ANISOU 1132  CE2 PHE A 134     2640   2525   2556   -153   -519     64       C  
ATOM   1133  CZ  PHE A 134      22.710   6.176   7.437  1.00 20.35           C  
ANISOU 1133  CZ  PHE A 134     2594   2543   2595   -135   -462     73       C  
ATOM   1134  N   THR A 135      15.760   6.743  10.140  1.00 14.48           N  
ANISOU 1134  N   THR A 135     2087   1810   1607    -29   -404    -91       N  
ATOM   1135  CA  THR A 135      14.475   6.389  10.724  1.00 14.62           C  
ANISOU 1135  CA  THR A 135     2126   1833   1598      2   -376    -96       C  
ATOM   1136  C   THR A 135      13.558   5.992   9.541  1.00 14.74           C  
ANISOU 1136  C   THR A 135     2102   1872   1627     10   -340    -95       C  
ATOM   1137  O   THR A 135      13.902   6.189   8.367  1.00 14.52           O  
ANISOU 1137  O   THR A 135     2047   1852   1617     -8   -337    -95       O  
ATOM   1138  CB  THR A 135      13.860   7.611  11.436  1.00 15.36           C  
ANISOU 1138  CB  THR A 135     2285   1900   1652     20   -376   -102       C  
ATOM   1139  OG1 THR A 135      13.529   8.620  10.477  1.00 16.63           O  
ANISOU 1139  OG1 THR A 135     2442   2059   1817     19   -365   -103       O  
ATOM   1140  CG2 THR A 135      14.745   8.161  12.529  1.00 15.23           C  
ANISOU 1140  CG2 THR A 135     2325   1852   1610      2   -420   -105       C  
ATOM   1141  N   ILE A 136      12.395   5.430   9.852  1.00 14.48           N  
ANISOU 1141  N   ILE A 136     2069   1849   1584     34   -314    -87       N  
ATOM   1142  CA  ILE A 136      11.362   5.231   8.863  1.00 15.24           C  
ANISOU 1142  CA  ILE A 136     2138   1964   1688     36   -290    -76       C  
ATOM   1143  C   ILE A 136      10.103   5.840   9.436  1.00 15.66           C  
ANISOU 1143  C   ILE A 136     2215   2012   1722     69   -267    -57       C  
ATOM   1144  O   ILE A 136       9.949   5.927  10.654  1.00 15.42           O  
ANISOU 1144  O   ILE A 136     2221   1966   1672     95   -262    -57       O  
ATOM   1145  CB  ILE A 136      11.154   3.773   8.380  1.00 16.56           C  
ANISOU 1145  CB  ILE A 136     2269   2151   1873     25   -280    -73       C  
ATOM   1146  CG1 ILE A 136      10.532   2.890   9.459  1.00 17.44           C  
ANISOU 1146  CG1 ILE A 136     2382   2265   1980     48   -272    -61       C  
ATOM   1147  CG2 ILE A 136      12.448   3.165   7.826  1.00 17.63           C  
ANISOU 1147  CG2 ILE A 136     2386   2284   2029      0   -288    -88       C  
ATOM   1148  CD1 ILE A 136       9.987   1.590   8.900  1.00 18.35           C  
ANISOU 1148  CD1 ILE A 136     2465   2396   2111     37   -262    -52       C  
ATOM   1149  N  ALYS A 137       9.196   6.293   8.569  0.50 16.39           N  
ANISOU 1149  N  ALYS A 137     2290   2116   1822     70   -251    -36       N  
ATOM   1150  N  BLYS A 137       9.209   6.274   8.558  0.50 16.47           N  
ANISOU 1150  N  BLYS A 137     2299   2126   1832     69   -252    -37       N  
ATOM   1151  CA ALYS A 137       7.929   6.844   9.037  0.50 17.56           C  
ANISOU 1151  CA ALYS A 137     2450   2258   1963    107   -221     -4       C  
ATOM   1152  CA BLYS A 137       7.936   6.833   8.974  0.50 17.72           C  
ANISOU 1152  CA BLYS A 137     2468   2279   1985    105   -222     -4       C  
ATOM   1153  C  ALYS A 137       6.887   5.782   8.750  0.50 17.91           C  
ANISOU 1153  C  ALYS A 137     2452   2327   2025    107   -210     30       C  
ATOM   1154  C  BLYS A 137       6.920   5.736   8.717  0.50 17.94           C  
ANISOU 1154  C  BLYS A 137     2455   2332   2030    105   -211     29       C  
ATOM   1155  O  ALYS A 137       6.343   5.738   7.658  0.50 18.13           O  
ANISOU 1155  O  ALYS A 137     2446   2372   2069     83   -214     52       O  
ATOM   1156  O  BLYS A 137       6.413   5.631   7.608  0.50 18.10           O  
ANISOU 1156  O  BLYS A 137     2441   2371   2066     80   -216     50       O  
ATOM   1157  CB ALYS A 137       7.610   8.173   8.334  0.50 20.10           C  
ANISOU 1157  CB ALYS A 137     2776   2572   2288    108   -211      9       C  
ATOM   1158  CB BLYS A 137       7.601   8.067   8.115  0.50 20.49           C  
ANISOU 1158  CB BLYS A 137     2817   2627   2342    101   -214     10       C  
ATOM   1159  CG ALYS A 137       8.672   9.240   8.580  0.50 24.65           C  
ANISOU 1159  CG ALYS A 137     3396   3121   2850    101   -229    -23       C  
ATOM   1160  CG BLYS A 137       8.547   9.239   8.322  0.50 25.54           C  
ANISOU 1160  CG BLYS A 137     3499   3238   2966     98   -227    -18       C  
ATOM   1161  CD ALYS A 137       8.340  10.542   7.865  0.50 28.93           C  
ANISOU 1161  CD ALYS A 137     3939   3654   3399    102   -218     -8       C  
ATOM   1162  CD BLYS A 137       8.454  10.239   7.173  0.50 29.94           C  
ANISOU 1162  CD BLYS A 137     4039   3799   3538     82   -228     -7       C  
ATOM   1163  CE ALYS A 137       7.600  11.508   8.754  0.50 32.40           C  
ANISOU 1163  CE ALYS A 137     4429   4061   3822    148   -181      8       C  
ATOM   1164  CE BLYS A 137       8.724  11.649   7.635  0.50 33.45           C  
ANISOU 1164  CE BLYS A 137     4534   4206   3967     98   -225    -17       C  
ATOM   1165  NZ ALYS A 137       8.483  12.051   9.819  0.50 34.48           N  
ANISOU 1165  NZ ALYS A 137     4766   4283   4051    152   -197    -28       N  
ATOM   1166  NZ BLYS A 137       9.352  12.475   6.565  0.50 34.98           N  
ANISOU 1166  NZ BLYS A 137     4711   4404   4176     67   -246    -24       N  
ATOM   1167  N   GLY A 138       6.673   4.891   9.709  1.00 17.84           N  
ANISOU 1167  N   GLY A 138     2446   2319   2013    127   -202     35       N  
ATOM   1168  CA  GLY A 138       5.745   3.780   9.550  1.00 18.27           C  
ANISOU 1168  CA  GLY A 138     2460   2394   2086    125   -198     70       C  
ATOM   1169  C   GLY A 138       4.449   3.921  10.307  1.00 17.75           C  
ANISOU 1169  C   GLY A 138     2391   2328   2027    170   -163    123       C  
ATOM   1170  O   GLY A 138       4.066   5.022  10.697  1.00 18.35           O  
ANISOU 1170  O   GLY A 138     2492   2386   2092    205   -133    139       O  
ATOM   1171  N   SER A 139       3.747   2.813  10.483  1.00 16.95           N  
ANISOU 1171  N   SER A 139     2255   2242   1942    172   -163    156       N  
ATOM   1172  CA  SER A 139       2.511   2.779  11.237  1.00 17.34           C  
ANISOU 1172  CA  SER A 139     2291   2292   2003    218   -127    217       C  
ATOM   1173  C   SER A 139       2.627   1.538  12.081  1.00 18.01           C  
ANISOU 1173  C   SER A 139     2372   2384   2089    226   -132    213       C  
ATOM   1174  O   SER A 139       2.438   0.427  11.594  1.00 18.46           O  
ANISOU 1174  O   SER A 139     2391   2458   2167    194   -158    224       O  
ATOM   1175  CB  SER A 139       1.310   2.717  10.300  1.00 18.70           C  
ANISOU 1175  CB  SER A 139     2409   2483   2211    202   -129    287       C  
ATOM   1176  OG  SER A 139       0.131   2.477  11.049  1.00 23.01           O  
ANISOU 1176  OG  SER A 139     2930   3033   2779    245    -96    358       O  
ATOM   1177  N   PHE A 140       3.090   1.719  13.311  1.00 17.22           N  
ANISOU 1177  N   PHE A 140     2317   2266   1959    262   -113    188       N  
ATOM   1178  CA  PHE A 140       3.374   0.600  14.192  1.00 17.88           C  
ANISOU 1178  CA  PHE A 140     2400   2355   2040    268   -120    179       C  
ATOM   1179  C   PHE A 140       2.824   0.838  15.576  1.00 20.15           C  
ANISOU 1179  C   PHE A 140     2721   2629   2306    328    -76    206       C  
ATOM   1180  O   PHE A 140       3.184   1.818  16.205  1.00 21.50           O  
ANISOU 1180  O   PHE A 140     2955   2774   2439    353    -56    183       O  
ATOM   1181  CB  PHE A 140       4.896   0.431  14.317  1.00 16.98           C  
ANISOU 1181  CB  PHE A 140     2313   2232   1906    238   -153    113       C  
ATOM   1182  CG  PHE A 140       5.648   0.038  13.067  1.00 16.74           C  
ANISOU 1182  CG  PHE A 140     2256   2211   1894    184   -188     83       C  
ATOM   1183  CD1 PHE A 140       5.592  -1.254  12.584  1.00 17.75           C  
ANISOU 1183  CD1 PHE A 140     2344   2352   2047    157   -205     88       C  
ATOM   1184  CD2 PHE A 140       6.484   0.939  12.430  1.00 16.89           C  
ANISOU 1184  CD2 PHE A 140     2295   2219   1902    162   -202     49       C  
ATOM   1185  CE1 PHE A 140       6.315  -1.619  11.454  1.00 17.58           C  
ANISOU 1185  CE1 PHE A 140     2311   2331   2036    112   -227     59       C  
ATOM   1186  CE2 PHE A 140       7.224   0.564  11.320  1.00 17.58           C  
ANISOU 1186  CE2 PHE A 140     2363   2312   2005    118   -225     24       C  
ATOM   1187  CZ  PHE A 140       7.144  -0.713  10.843  1.00 17.08           C  
ANISOU 1187  CZ  PHE A 140     2268   2259   1962     95   -234     27       C  
ATOM   1188  N   LEU A 141       2.006  -0.071  16.069  1.00 20.53           N  
ANISOU 1188  N   LEU A 141     2734   2692   2374    351    -61    253       N  
ATOM   1189  CA  LEU A 141       1.467   0.022  17.427  1.00 22.25           C  
ANISOU 1189  CA  LEU A 141     2985   2898   2571    412    -13    283       C  
ATOM   1190  C   LEU A 141       2.194  -0.996  18.303  1.00 22.71           C  
ANISOU 1190  C   LEU A 141     3053   2961   2613    405    -35    254       C  
ATOM   1191  O   LEU A 141       3.009  -1.765  17.799  1.00 22.61           O  
ANISOU 1191  O   LEU A 141     3014   2961   2616    356    -82    219       O  
ATOM   1192  CB  LEU A 141      -0.022  -0.321  17.412  1.00 23.61           C  
ANISOU 1192  CB  LEU A 141     3101   3085   2785    446     22    372       C  
ATOM   1193  CG  LEU A 141      -0.880   0.558  16.561  1.00 26.86           C  
ANISOU 1193  CG  LEU A 141     3488   3495   3224    453     44    422       C  
ATOM   1194  CD1 LEU A 141      -2.217  -0.070  16.370  1.00 28.11           C  
ANISOU 1194  CD1 LEU A 141     3570   3675   3437    466     57    518       C  
ATOM   1195  CD2 LEU A 141      -1.000   1.953  17.161  1.00 27.94           C  
ANISOU 1195  CD2 LEU A 141     3693   3596   3325    508    105    421       C  
ATOM   1196  N   ASN A 142       1.876  -1.054  19.615  1.00 23.13           N  
ANISOU 1196  N   ASN A 142     3145   3005   2638    455      3    273       N  
ATOM   1197  CA  ASN A 142       2.473  -2.056  20.495  1.00 23.46           C  
ANISOU 1197  CA  ASN A 142     3191   3055   2668    448    -19    255       C  
ATOM   1198  C   ASN A 142       2.080  -3.453  20.002  1.00 21.95           C  
ANISOU 1198  C   ASN A 142     2914   2895   2533    425    -43    287       C  
ATOM   1199  O   ASN A 142       0.950  -3.667  19.566  1.00 22.17           O  
ANISOU 1199  O   ASN A 142     2891   2935   2599    439    -25    346       O  
ATOM   1200  CB  ASN A 142       2.077  -1.814  21.953  1.00 26.50           C  
ANISOU 1200  CB  ASN A 142     3638   3423   3007    507     31    276       C  
ATOM   1201  CG  ASN A 142       2.744  -0.586  22.522  1.00 33.37           C  
ANISOU 1201  CG  ASN A 142     4614   4256   3811    514     40    230       C  
ATOM   1202  OD1 ASN A 142       3.924  -0.317  22.266  1.00 35.67           O  
ANISOU 1202  OD1 ASN A 142     4930   4539   4085    465    -11    174       O  
ATOM   1203  ND2 ASN A 142       2.005   0.198  23.302  1.00 35.11           N  
ANISOU 1203  ND2 ASN A 142     4901   4448   3992    576    107    256       N  
ATOM   1204  N   GLY A 143       3.065  -4.323  19.913  1.00 20.23           N  
ANISOU 1204  N   GLY A 143     2679   2684   2323    383    -87    248       N  
ATOM   1205  CA  GLY A 143       2.872  -5.658  19.374  1.00 18.71           C  
ANISOU 1205  CA  GLY A 143     2418   2512   2180    354   -114    266       C  
ATOM   1206  C   GLY A 143       3.365  -5.788  17.939  1.00 16.65           C  
ANISOU 1206  C   GLY A 143     2132   2251   1943    298   -149    234       C  
ATOM   1207  O   GLY A 143       3.442  -6.903  17.428  1.00 16.13           O  
ANISOU 1207  O   GLY A 143     2026   2193   1911    266   -173    235       O  
ATOM   1208  N   SER A 144       3.691  -4.663  17.268  1.00 15.41           N  
ANISOU 1208  N   SER A 144     2005   2082   1767    286   -150    207       N  
ATOM   1209  CA  SER A 144       4.151  -4.716  15.875  1.00 14.02           C  
ANISOU 1209  CA  SER A 144     1811   1906   1609    235   -179    178       C  
ATOM   1210  C   SER A 144       5.623  -5.030  15.716  1.00 13.25           C  
ANISOU 1210  C   SER A 144     1726   1799   1508    202   -204    123       C  
ATOM   1211  O   SER A 144       6.059  -5.283  14.594  1.00 12.34           O  
ANISOU 1211  O   SER A 144     1598   1682   1408    163   -220    101       O  
ATOM   1212  CB  SER A 144       3.856  -3.411  15.150  1.00 14.75           C  
ANISOU 1212  CB  SER A 144     1922   1992   1689    234   -170    179       C  
ATOM   1213  OG  SER A 144       4.555  -2.361  15.795  1.00 16.91           O  
ANISOU 1213  OG  SER A 144     2250   2249   1925    253   -159    147       O  
ATOM   1214  N   CYS A 145       6.413  -5.035  16.803  1.00 13.27           N  
ANISOU 1214  N   CYS A 145     1754   1797   1493    216   -206    107       N  
ATOM   1215  CA  CYS A 145       7.837  -5.364  16.678  1.00 13.16           C  
ANISOU 1215  CA  CYS A 145     1740   1774   1484    185   -230     69       C  
ATOM   1216  C   CYS A 145       8.043  -6.722  16.046  1.00 12.44           C  
ANISOU 1216  C   CYS A 145     1604   1686   1434    158   -237     69       C  
ATOM   1217  O   CYS A 145       7.218  -7.618  16.221  1.00 12.76           O  
ANISOU 1217  O   CYS A 145     1619   1736   1494    167   -232     96       O  
ATOM   1218  CB  CYS A 145       8.549  -5.254  18.016  1.00 14.52           C  
ANISOU 1218  CB  CYS A 145     1941   1942   1633    197   -239     66       C  
ATOM   1219  SG  CYS A 145       8.542  -3.580  18.699  1.00 19.18           S  
ANISOU 1219  SG  CYS A 145     2609   2515   2164    219   -233     55       S  
ATOM   1220  N   GLY A 146       9.054  -6.812  15.211  1.00 11.62           N  
ANISOU 1220  N   GLY A 146     1498   1572   1345    128   -246     39       N  
ATOM   1221  CA  GLY A 146       9.297  -8.040  14.474  1.00 11.65           C  
ANISOU 1221  CA  GLY A 146     1474   1568   1383    104   -244     34       C  
ATOM   1222  C   GLY A 146       8.639  -8.028  13.111  1.00 11.50           C  
ANISOU 1222  C   GLY A 146     1458   1546   1365     80   -242     30       C  
ATOM   1223  O   GLY A 146       8.938  -8.880  12.282  1.00 12.48           O  
ANISOU 1223  O   GLY A 146     1578   1655   1507     55   -237     17       O  
ATOM   1224  N   SER A 147       7.753  -7.040  12.831  1.00 11.19           N  
ANISOU 1224  N   SER A 147     1431   1517   1305     86   -243     43       N  
ATOM   1225  CA  SER A 147       7.204  -6.880  11.475  1.00 11.25           C  
ANISOU 1225  CA  SER A 147     1443   1522   1310     55   -249     43       C  
ATOM   1226  C   SER A 147       8.385  -6.510  10.565  1.00 11.68           C  
ANISOU 1226  C   SER A 147     1516   1561   1359     31   -246      2       C  
ATOM   1227  O   SER A 147       9.322  -5.827  11.010  1.00 11.33           O  
ANISOU 1227  O   SER A 147     1480   1514   1310     44   -243    -15       O  
ATOM   1228  CB  SER A 147       6.210  -5.723  11.428  1.00 12.25           C  
ANISOU 1228  CB  SER A 147     1573   1662   1420     69   -249     71       C  
ATOM   1229  OG  SER A 147       5.054  -6.012  12.198  1.00 13.30           O  
ANISOU 1229  OG  SER A 147     1685   1807   1562     96   -244    120       O  
ATOM   1230  N   VAL A 148       8.354  -6.970   9.308  1.00 11.17           N  
ANISOU 1230  N   VAL A 148     1463   1485   1295     -4   -246    -10       N  
ATOM   1231  CA  VAL A 148       9.493  -6.779   8.444  1.00 11.78           C  
ANISOU 1231  CA  VAL A 148     1560   1546   1370    -22   -233    -44       C  
ATOM   1232  C   VAL A 148       9.223  -5.923   7.220  1.00 12.04           C  
ANISOU 1232  C   VAL A 148     1614   1581   1381    -47   -239    -51       C  
ATOM   1233  O   VAL A 148       8.088  -5.781   6.767  1.00 11.94           O  
ANISOU 1233  O   VAL A 148     1603   1578   1356    -65   -256    -28       O  
ATOM   1234  CB  VAL A 148      10.129  -8.138   8.036  1.00 12.63           C  
ANISOU 1234  CB  VAL A 148     1675   1627   1497    -36   -213    -60       C  
ATOM   1235  CG1 VAL A 148      10.607  -8.914   9.260  1.00 12.66           C  
ANISOU 1235  CG1 VAL A 148     1651   1630   1529    -10   -206    -50       C  
ATOM   1236  CG2 VAL A 148       9.180  -8.973   7.195  1.00 13.55           C  
ANISOU 1236  CG2 VAL A 148     1812   1732   1603    -71   -223    -55       C  
ATOM   1237  N   GLY A 149      10.312  -5.371   6.699  1.00 12.16           N  
ANISOU 1237  N   GLY A 149     1641   1587   1394    -51   -225    -76       N  
ATOM   1238  CA  GLY A 149      10.362  -4.619   5.460  1.00 12.30           C  
ANISOU 1238  CA  GLY A 149     1680   1602   1390    -76   -224    -87       C  
ATOM   1239  C   GLY A 149      11.095  -5.441   4.419  1.00 12.43           C  
ANISOU 1239  C   GLY A 149     1725   1592   1405    -98   -198   -111       C  
ATOM   1240  O   GLY A 149      12.033  -6.187   4.731  1.00 12.20           O  
ANISOU 1240  O   GLY A 149     1692   1545   1400    -84   -172   -121       O  
ATOM   1241  N   PHE A 150      10.650  -5.327   3.175  1.00 12.00           N  
ANISOU 1241  N   PHE A 150     1703   1533   1322   -134   -202   -117       N  
ATOM   1242  CA  PHE A 150      11.198  -6.146   2.114  1.00 13.19           C  
ANISOU 1242  CA  PHE A 150     1901   1652   1460   -157   -172   -141       C  
ATOM   1243  C   PHE A 150      10.981  -5.537   0.748  1.00 14.59           C  
ANISOU 1243  C   PHE A 150     2117   1828   1599   -193   -176   -148       C  
ATOM   1244  O   PHE A 150      10.124  -4.675   0.576  1.00 14.07           O  
ANISOU 1244  O   PHE A 150     2039   1788   1519   -209   -211   -128       O  
ATOM   1245  CB  PHE A 150      10.498  -7.529   2.164  1.00 13.42           C  
ANISOU 1245  CB  PHE A 150     1951   1662   1486   -177   -178   -138       C  
ATOM   1246  CG  PHE A 150       8.997  -7.465   1.967  1.00 14.35           C  
ANISOU 1246  CG  PHE A 150     2071   1797   1583   -212   -228   -110       C  
ATOM   1247  CD1 PHE A 150       8.154  -7.170   3.021  1.00 15.42           C  
ANISOU 1247  CD1 PHE A 150     2157   1963   1740   -192   -256    -74       C  
ATOM   1248  CD2 PHE A 150       8.432  -7.691   0.721  1.00 15.45           C  
ANISOU 1248  CD2 PHE A 150     2264   1922   1683   -267   -246   -111       C  
ATOM   1249  CE1 PHE A 150       6.783  -7.040   2.825  1.00 16.35           C  
ANISOU 1249  CE1 PHE A 150     2266   2097   1848   -220   -297    -33       C  
ATOM   1250  CE2 PHE A 150       7.052  -7.611   0.541  1.00 16.30           C  
ANISOU 1250  CE2 PHE A 150     2366   2048   1780   -305   -299    -70       C  
ATOM   1251  CZ  PHE A 150       6.239  -7.292   1.593  1.00 15.96           C  
ANISOU 1251  CZ  PHE A 150     2261   2036   1767   -279   -322    -28       C  
ATOM   1252  N   ASN A 151      11.734  -6.041  -0.222  1.00 15.13           N  
ANISOU 1252  N   ASN A 151     2234   1864   1650   -206   -137   -174       N  
ATOM   1253  CA  ASN A 151      11.561  -5.768  -1.644  1.00 16.70           C  
ANISOU 1253  CA  ASN A 151     2490   2054   1802   -247   -136   -185       C  
ATOM   1254  C   ASN A 151      11.469  -7.132  -2.334  1.00 18.24           C  
ANISOU 1254  C   ASN A 151     2759   2203   1967   -277   -115   -205       C  
ATOM   1255  O   ASN A 151      11.926  -8.137  -1.785  1.00 17.68           O  
ANISOU 1255  O   ASN A 151     2690   2107   1922   -254    -83   -215       O  
ATOM   1256  CB  ASN A 151      12.736  -4.982  -2.203  1.00 17.55           C  
ANISOU 1256  CB  ASN A 151     2598   2158   1913   -227    -96   -196       C  
ATOM   1257  CG  ASN A 151      12.678  -3.526  -1.848  1.00 21.16           C  
ANISOU 1257  CG  ASN A 151     3002   2653   2385   -214   -125   -177       C  
ATOM   1258  OD1 ASN A 151      12.018  -2.729  -2.525  1.00 23.71           O  
ANISOU 1258  OD1 ASN A 151     3333   2995   2679   -243   -154   -168       O  
ATOM   1259  ND2 ASN A 151      13.342  -3.149  -0.770  1.00 19.82           N  
ANISOU 1259  ND2 ASN A 151     2779   2494   2257   -172   -122   -169       N  
ATOM   1260  N   ILE A 152      10.860  -7.188  -3.527  1.00 19.82           N  
ANISOU 1260  N   ILE A 152     3027   2392   2112   -333   -133   -211       N  
ATOM   1261  CA  ILE A 152      10.779  -8.458  -4.255  1.00 22.59           C  
ANISOU 1261  CA  ILE A 152     3469   2691   2424   -368   -114   -235       C  
ATOM   1262  C   ILE A 152      11.333  -8.271  -5.655  1.00 25.21           C  
ANISOU 1262  C   ILE A 152     3883   2993   2701   -391    -75   -260       C  
ATOM   1263  O   ILE A 152      11.049  -7.265  -6.296  1.00 25.64           O  
ANISOU 1263  O   ILE A 152     3936   3075   2730   -415   -102   -249       O  
ATOM   1264  CB  ILE A 152       9.350  -9.069  -4.286  1.00 23.47           C  
ANISOU 1264  CB  ILE A 152     3603   2802   2511   -428   -184   -213       C  
ATOM   1265  CG1 ILE A 152       8.720  -9.144  -2.884  1.00 24.58           C  
ANISOU 1265  CG1 ILE A 152     3656   2977   2707   -401   -221   -178       C  
ATOM   1266  CG2 ILE A 152       9.360 -10.453  -4.972  1.00 24.13           C  
ANISOU 1266  CG2 ILE A 152     3794   2822   2552   -466   -163   -242       C  
ATOM   1267  CD1 ILE A 152       7.304  -9.608  -2.866  1.00 25.76           C  
ANISOU 1267  CD1 ILE A 152     3812   3132   2845   -455   -290   -141       C  
ATOM   1268  N   ASP A 153      12.157  -9.211  -6.114  1.00 26.83           N  
ANISOU 1268  N   ASP A 153     4161   3142   2891   -379     -5   -292       N  
ATOM   1269  CA  ASP A 153      12.655  -9.198  -7.484  1.00 28.74           C  
ANISOU 1269  CA  ASP A 153     4501   3347   3071   -400     42   -317       C  
ATOM   1270  C   ASP A 153      12.170 -10.512  -8.056  1.00 29.83           C  
ANISOU 1270  C   ASP A 153     4755   3426   3155   -448     44   -342       C  
ATOM   1271  O   ASP A 153      12.773 -11.548  -7.779  1.00 30.55           O  
ANISOU 1271  O   ASP A 153     4875   3468   3264   -416    105   -360       O  
ATOM   1272  CB  ASP A 153      14.184  -9.123  -7.546  1.00 31.89           C  
ANISOU 1272  CB  ASP A 153     4891   3723   3503   -332    141   -327       C  
ATOM   1273  CG  ASP A 153      14.688  -8.981  -8.971  1.00 40.02           C  
ANISOU 1273  CG  ASP A 153     6021   4717   4468   -348    196   -349       C  
ATOM   1274  OD1 ASP A 153      13.977  -8.356  -9.795  1.00 41.47           O  
ANISOU 1274  OD1 ASP A 153     6244   4920   4593   -404    145   -348       O  
ATOM   1275  OD2 ASP A 153      15.789  -9.501  -9.268  1.00 43.80           O  
ANISOU 1275  OD2 ASP A 153     6541   5147   4955   -303    293   -361       O  
ATOM   1276  N   TYR A 154      11.037 -10.469  -8.789  1.00 29.57           N  
ANISOU 1276  N   TYR A 154     4783   3395   3057   -529    -29   -336       N  
ATOM   1277  CA  TYR A 154      10.327 -11.603  -9.381  1.00 30.13           C  
ANISOU 1277  CA  TYR A 154     4970   3411   3065   -599    -57   -351       C  
ATOM   1278  C   TYR A 154       9.896 -12.627  -8.298  1.00 29.86           C  
ANISOU 1278  C   TYR A 154     4899   3367   3080   -589    -80   -341       C  
ATOM   1279  O   TYR A 154       8.809 -12.476  -7.736  1.00 30.57           O  
ANISOU 1279  O   TYR A 154     4925   3498   3191   -620   -165   -302       O  
ATOM   1280  CB  TYR A 154      11.081 -12.243 -10.574  0.50 30.31           C  
ANISOU 1280  CB  TYR A 154     5145   3358   3015   -610     24   -398       C  
ATOM   1281  CG  TYR A 154      10.357 -13.446 -11.143  0.50 31.41           C  
ANISOU 1281  CG  TYR A 154     5418   3431   3083   -686     -9   -418       C  
ATOM   1282  CD1 TYR A 154       9.054 -13.341 -11.609  0.50 32.51           C  
ANISOU 1282  CD1 TYR A 154     5593   3587   3171   -784   -120   -392       C  
ATOM   1283  CD2 TYR A 154      10.964 -14.693 -11.188  0.50 32.38           C  
ANISOU 1283  CD2 TYR A 154     5632   3475   3196   -663     70   -455       C  
ATOM   1284  CE1 TYR A 154       8.372 -14.447 -12.100  0.50 33.48           C  
ANISOU 1284  CE1 TYR A 154     5842   3648   3230   -863   -162   -403       C  
ATOM   1285  CE2 TYR A 154      10.290 -15.808 -11.669  0.50 33.42           C  
ANISOU 1285  CE2 TYR A 154     5893   3541   3262   -736     36   -474       C  
ATOM   1286  CZ  TYR A 154       8.994 -15.680 -12.131  0.50 34.48           C  
ANISOU 1286  CZ  TYR A 154     6066   3693   3342   -840    -84   -449       C  
ATOM   1287  OH  TYR A 154       8.328 -16.774 -12.627  0.50 36.31           O  
ANISOU 1287  OH  TYR A 154     6433   3857   3507   -922   -128   -463       O  
ATOM   1288  N   ASP A 155      10.732 -13.629  -7.970  1.00 28.99           N  
ANISOU 1288  N   ASP A 155     4819   3204   2992   -543     -1   -370       N  
ATOM   1289  CA  ASP A 155      10.368 -14.624  -6.961  1.00 28.27           C  
ANISOU 1289  CA  ASP A 155     4692   3101   2947   -533    -20   -360       C  
ATOM   1290  C   ASP A 155      11.249 -14.600  -5.720  1.00 26.66           C  
ANISOU 1290  C   ASP A 155     4375   2920   2834   -445     33   -350       C  
ATOM   1291  O   ASP A 155      11.085 -15.455  -4.854  1.00 27.06           O  
ANISOU 1291  O   ASP A 155     4396   2961   2927   -429     28   -342       O  
ATOM   1292  CB  ASP A 155      10.346 -16.038  -7.566  1.00 30.93           C  
ANISOU 1292  CB  ASP A 155     5167   3350   3233   -570     10   -394       C  
ATOM   1293  CG  ASP A 155      11.673 -16.511  -8.140  1.00 36.67           C  
ANISOU 1293  CG  ASP A 155     5979   4010   3946   -521    136   -436       C  
ATOM   1294  OD1 ASP A 155      12.607 -15.683  -8.250  1.00 37.43           O  
ANISOU 1294  OD1 ASP A 155     6029   4128   4064   -465    196   -435       O  
ATOM   1295  OD2 ASP A 155      11.772 -17.708  -8.495  1.00 39.58           O  
ANISOU 1295  OD2 ASP A 155     6460   4298   4281   -537    176   -465       O  
ATOM   1296  N   CYS A 156      12.175 -13.637  -5.622  1.00 24.66           N  
ANISOU 1296  N   CYS A 156     4061   2698   2611   -390     78   -346       N  
ATOM   1297  CA  CYS A 156      13.076 -13.566  -4.484  1.00 23.25           C  
ANISOU 1297  CA  CYS A 156     3780   2540   2516   -314    122   -330       C  
ATOM   1298  C   CYS A 156      12.758 -12.398  -3.587  1.00 20.76           C  
ANISOU 1298  C   CYS A 156     3346   2300   2241   -297     62   -297       C  
ATOM   1299  O   CYS A 156      12.827 -11.248  -4.023  1.00 20.48           O  
ANISOU 1299  O   CYS A 156     3294   2298   2191   -301     50   -292       O  
ATOM   1300  CB  CYS A 156      14.525 -13.518  -4.955  1.00 24.48           C  
ANISOU 1300  CB  CYS A 156     3957   2659   2683   -262    226   -343       C  
ATOM   1301  SG  CYS A 156      15.738 -13.478  -3.610  1.00 27.04           S  
ANISOU 1301  SG  CYS A 156     4155   3003   3114   -177    276   -310       S  
ATOM   1302  N   VAL A 157      12.484 -12.680  -2.310  1.00 18.60           N  
ANISOU 1302  N   VAL A 157     2993   2052   2021   -273     34   -275       N  
ATOM   1303  CA  VAL A 157      12.218 -11.620  -1.344  1.00 17.05           C  
ANISOU 1303  CA  VAL A 157     2695   1921   1862   -250    -13   -245       C  
ATOM   1304  C   VAL A 157      13.514 -11.180  -0.700  1.00 15.71           C  
ANISOU 1304  C   VAL A 157     2462   1761   1745   -190     35   -237       C  
ATOM   1305  O   VAL A 157      14.196 -11.995  -0.084  1.00 15.50           O  
ANISOU 1305  O   VAL A 157     2416   1712   1762   -156     77   -233       O  
ATOM   1306  CB  VAL A 157      11.247 -12.102  -0.243  1.00 17.28           C  
ANISOU 1306  CB  VAL A 157     2674   1973   1918   -254    -67   -219       C  
ATOM   1307  CG1 VAL A 157      10.950 -10.990   0.757  1.00 17.60           C  
ANISOU 1307  CG1 VAL A 157     2624   2074   1989   -227   -108   -189       C  
ATOM   1308  CG2 VAL A 157       9.958 -12.653  -0.847  1.00 18.06           C  
ANISOU 1308  CG2 VAL A 157     2831   2058   1974   -319   -121   -214       C  
ATOM   1309  N   SER A 158      13.840  -9.894  -0.794  1.00 15.06           N  
ANISOU 1309  N   SER A 158     2344   1714   1665   -178     25   -229       N  
ATOM   1310  CA  SER A 158      15.008  -9.358  -0.111  1.00 14.90           C  
ANISOU 1310  CA  SER A 158     2258   1707   1698   -129     54   -212       C  
ATOM   1311  C   SER A 158      14.517  -8.654   1.138  1.00 14.32           C  
ANISOU 1311  C   SER A 158     2111   1683   1649   -118     -5   -189       C  
ATOM   1312  O   SER A 158      13.944  -7.567   1.050  1.00 14.24           O  
ANISOU 1312  O   SER A 158     2087   1705   1618   -132    -47   -183       O  
ATOM   1313  CB  SER A 158      15.755  -8.366  -0.997  1.00 17.17           C  
ANISOU 1313  CB  SER A 158     2555   1997   1973   -125     81   -214       C  
ATOM   1314  OG  SER A 158      16.436  -9.063  -2.024  1.00 20.62           O  
ANISOU 1314  OG  SER A 158     3059   2382   2392   -122    154   -230       O  
ATOM   1315  N   PHE A 159      14.725  -9.276   2.299  1.00 13.50           N  
ANISOU 1315  N   PHE A 159     1963   1580   1587    -92     -6   -174       N  
ATOM   1316  CA  PHE A 159      14.327  -8.676   3.565  1.00 13.12           C  
ANISOU 1316  CA  PHE A 159     1856   1572   1557    -78    -55   -152       C  
ATOM   1317  C   PHE A 159      15.366  -7.649   3.959  1.00 12.99           C  
ANISOU 1317  C   PHE A 159     1799   1570   1566    -54    -52   -138       C  
ATOM   1318  O   PHE A 159      16.559  -7.954   3.983  1.00 13.40           O  
ANISOU 1318  O   PHE A 159     1835   1603   1655    -34    -12   -127       O  
ATOM   1319  CB  PHE A 159      14.245  -9.749   4.654  1.00 12.61           C  
ANISOU 1319  CB  PHE A 159     1763   1503   1525    -61    -55   -139       C  
ATOM   1320  CG  PHE A 159      13.131 -10.726   4.411  1.00 11.64           C  
ANISOU 1320  CG  PHE A 159     1674   1367   1381    -86    -69   -146       C  
ATOM   1321  CD1 PHE A 159      11.819 -10.392   4.702  1.00 12.23           C  
ANISOU 1321  CD1 PHE A 159     1742   1471   1436   -104   -121   -133       C  
ATOM   1322  CD2 PHE A 159      13.391 -11.978   3.887  1.00 11.94           C  
ANISOU 1322  CD2 PHE A 159     1754   1360   1424    -94    -28   -160       C  
ATOM   1323  CE1 PHE A 159      10.793 -11.300   4.508  1.00 12.59           C  
ANISOU 1323  CE1 PHE A 159     1811   1504   1468   -132   -142   -128       C  
ATOM   1324  CE2 PHE A 159      12.357 -12.881   3.669  1.00 12.59           C  
ANISOU 1324  CE2 PHE A 159     1872   1425   1485   -125    -50   -164       C  
ATOM   1325  CZ  PHE A 159      11.064 -12.538   3.991  1.00 12.27           C  
ANISOU 1325  CZ  PHE A 159     1816   1420   1428   -146   -111   -145       C  
ATOM   1326  N   CYS A 160      14.918  -6.444   4.317  1.00 12.93           N  
ANISOU 1326  N   CYS A 160     1774   1596   1544    -56    -96   -132       N  
ATOM   1327  CA  CYS A 160      15.839  -5.365   4.668  1.00 13.50           C  
ANISOU 1327  CA  CYS A 160     1816   1679   1634    -42   -104   -118       C  
ATOM   1328  C   CYS A 160      15.596  -4.739   6.011  1.00 13.22           C  
ANISOU 1328  C   CYS A 160     1752   1668   1604    -30   -148   -103       C  
ATOM   1329  O   CYS A 160      16.451  -3.984   6.456  1.00 13.85           O  
ANISOU 1329  O   CYS A 160     1811   1751   1700    -23   -161    -89       O  
ATOM   1330  CB  CYS A 160      15.838  -4.296   3.580  1.00 14.93           C  
ANISOU 1330  CB  CYS A 160     2017   1866   1789    -58   -105   -128       C  
ATOM   1331  SG  CYS A 160      14.213  -3.572   3.272  1.00 15.19           S  
ANISOU 1331  SG  CYS A 160     2072   1925   1776    -81   -147   -136       S  
ATOM   1332  N   TYR A 161      14.433  -4.952   6.614  1.00 12.04           N  
ANISOU 1332  N   TYR A 161     1606   1533   1436    -29   -171   -103       N  
ATOM   1333  CA  TYR A 161      14.112  -4.270   7.849  1.00 11.92           C  
ANISOU 1333  CA  TYR A 161     1578   1535   1414    -14   -205    -90       C  
ATOM   1334  C   TYR A 161      13.335  -5.134   8.797  1.00 11.21           C  
ANISOU 1334  C   TYR A 161     1479   1452   1326     -1   -212    -80       C  
ATOM   1335  O   TYR A 161      12.520  -5.929   8.377  1.00 11.05           O  
ANISOU 1335  O   TYR A 161     1466   1431   1302    -10   -204    -81       O  
ATOM   1336  CB  TYR A 161      13.272  -3.020   7.497  1.00 11.04           C  
ANISOU 1336  CB  TYR A 161     1484   1439   1270    -19   -224    -94       C  
ATOM   1337  CG  TYR A 161      12.873  -2.174   8.686  1.00 11.13           C  
ANISOU 1337  CG  TYR A 161     1499   1462   1268      1   -248    -83       C  
ATOM   1338  CD1 TYR A 161      13.734  -1.221   9.206  1.00 12.22           C  
ANISOU 1338  CD1 TYR A 161     1642   1594   1405      4   -266    -82       C  
ATOM   1339  CD2 TYR A 161      11.614  -2.292   9.256  1.00 11.72           C  
ANISOU 1339  CD2 TYR A 161     1577   1549   1328     15   -253    -70       C  
ATOM   1340  CE1 TYR A 161      13.370  -0.445  10.303  1.00 12.77           C  
ANISOU 1340  CE1 TYR A 161     1733   1666   1453     20   -286    -76       C  
ATOM   1341  CE2 TYR A 161      11.245  -1.535  10.356  1.00 12.42           C  
ANISOU 1341  CE2 TYR A 161     1680   1641   1399     39   -263    -60       C  
ATOM   1342  CZ  TYR A 161      12.120  -0.604  10.873  1.00 12.57           C  
ANISOU 1342  CZ  TYR A 161     1717   1649   1409     41   -279    -67       C  
ATOM   1343  OH  TYR A 161      11.751   0.138  11.977  1.00 12.95           O  
ANISOU 1343  OH  TYR A 161     1797   1693   1430     63   -287    -61       O  
ATOM   1344  N   MET A 162      13.585  -4.974  10.085  1.00 10.28           N  
ANISOU 1344  N   MET A 162     1349   1341   1214     16   -230    -66       N  
ATOM   1345  CA  MET A 162      12.783  -5.594  11.126  1.00 10.68           C  
ANISOU 1345  CA  MET A 162     1393   1402   1261     32   -238    -51       C  
ATOM   1346  C   MET A 162      12.509  -4.476  12.131  1.00 10.72           C  
ANISOU 1346  C   MET A 162     1416   1418   1238     49   -260    -44       C  
ATOM   1347  O   MET A 162      13.429  -3.757  12.531  1.00 10.71           O  
ANISOU 1347  O   MET A 162     1424   1411   1235     45   -277    -45       O  
ATOM   1348  CB  MET A 162      13.469  -6.782  11.785  1.00 11.91           C  
ANISOU 1348  CB  MET A 162     1523   1551   1451     37   -230    -39       C  
ATOM   1349  CG  MET A 162      12.631  -7.332  12.936  1.00 12.92           C  
ANISOU 1349  CG  MET A 162     1644   1693   1574     56   -240    -21       C  
ATOM   1350  SD  MET A 162      13.162  -8.961  13.503  1.00 15.17           S  
ANISOU 1350  SD  MET A 162     1893   1969   1903     60   -227     -4       S  
ATOM   1351  CE  MET A 162      12.432  -9.997  12.218  1.00 16.30           C  
ANISOU 1351  CE  MET A 162     2042   2095   2055     44   -201    -18       C  
ATOM   1352  N   HIS A 163      11.245  -4.306  12.496  1.00 10.85           N  
ANISOU 1352  N   HIS A 163     1442   1446   1233     66   -259    -33       N  
ATOM   1353  CA  HIS A 163      10.862  -3.230  13.394  1.00 10.78           C  
ANISOU 1353  CA  HIS A 163     1463   1439   1192     88   -267    -27       C  
ATOM   1354  C   HIS A 163      11.218  -3.501  14.829  1.00 10.88           C  
ANISOU 1354  C   HIS A 163     1486   1451   1197    103   -278    -17       C  
ATOM   1355  O   HIS A 163      10.858  -4.554  15.333  1.00 11.36           O  
ANISOU 1355  O   HIS A 163     1525   1519   1271    113   -271     -1       O  
ATOM   1356  CB  HIS A 163       9.363  -2.967  13.299  1.00 11.80           C  
ANISOU 1356  CB  HIS A 163     1596   1579   1309    107   -252     -6       C  
ATOM   1357  CG  HIS A 163       8.995  -1.754  14.072  1.00 12.60           C  
ANISOU 1357  CG  HIS A 163     1737   1674   1376    134   -246     -1       C  
ATOM   1358  ND1 HIS A 163       9.637  -0.545  13.857  1.00 13.89           N  
ANISOU 1358  ND1 HIS A 163     1932   1824   1522    125   -257    -21       N  
ATOM   1359  CD2 HIS A 163       8.139  -1.619  15.105  1.00 13.61           C  
ANISOU 1359  CD2 HIS A 163     1884   1803   1484    172   -229     23       C  
ATOM   1360  CE1 HIS A 163       9.124   0.289  14.740  1.00 14.58           C  
ANISOU 1360  CE1 HIS A 163     2062   1900   1576    155   -245    -12       C  
ATOM   1361  NE2 HIS A 163       8.222  -0.307  15.514  1.00 14.16           N  
ANISOU 1361  NE2 HIS A 163     2005   1855   1519    186   -224     14       N  
ATOM   1362  N   HIS A 164      11.850  -2.524  15.504  1.00 10.72           N  
ANISOU 1362  N   HIS A 164     1504   1420   1151    102   -297    -23       N  
ATOM   1363  CA  HIS A 164      12.191  -2.691  16.911  1.00 12.02           C  
ANISOU 1363  CA  HIS A 164     1691   1581   1297    109   -315    -12       C  
ATOM   1364  C   HIS A 164      11.654  -1.626  17.827  1.00 13.54           C  
ANISOU 1364  C   HIS A 164     1951   1761   1434    131   -314    -13       C  
ATOM   1365  O   HIS A 164      11.296  -1.961  18.960  1.00 14.57           O  
ANISOU 1365  O   HIS A 164     2104   1892   1541    150   -310     -1       O  
ATOM   1366  CB  HIS A 164      13.720  -2.699  17.140  1.00 12.32           C  
ANISOU 1366  CB  HIS A 164     1722   1610   1352     75   -351    -10       C  
ATOM   1367  CG  HIS A 164      14.408  -3.927  16.654  1.00 11.31           C  
ANISOU 1367  CG  HIS A 164     1532   1487   1278     62   -345      1       C  
ATOM   1368  ND1 HIS A 164      15.090  -4.762  17.524  1.00 11.61           N  
ANISOU 1368  ND1 HIS A 164     1547   1526   1337     53   -361     25       N  
ATOM   1369  CD2 HIS A 164      14.549  -4.392  15.393  1.00 11.50           C  
ANISOU 1369  CD2 HIS A 164     1520   1510   1338     54   -321     -6       C  
ATOM   1370  CE1 HIS A 164      15.623  -5.706  16.765  1.00 11.94           C  
ANISOU 1370  CE1 HIS A 164     1538   1568   1431     46   -342     33       C  
ATOM   1371  NE2 HIS A 164      15.308  -5.537  15.478  1.00 12.33           N  
ANISOU 1371  NE2 HIS A 164     1584   1614   1487     47   -316     11       N  
ATOM   1372  N  AMET A 165      11.586  -0.360  17.376  0.50 14.49           N  
ANISOU 1372  N  AMET A 165     2107   1865   1532    126   -317    -29       N  
ATOM   1373  N  BMET A 165      11.783  -0.326  17.439  0.50 13.59           N  
ANISOU 1373  N  BMET A 165     1993   1751   1418    126   -317    -29       N  
ATOM   1374  CA AMET A 165      11.139   0.666  18.305  0.50 16.09           C  
ANISOU 1374  CA AMET A 165     2385   2048   1679    154   -305    -30       C  
ATOM   1375  CA BMET A 165      11.504   0.797  18.336  0.50 14.00           C  
ANISOU 1375  CA BMET A 165     2125   1782   1414    148   -313    -32       C  
ATOM   1376  C  AMET A 165      10.595   1.912  17.722  0.50 15.90           C  
ANISOU 1376  C  AMET A 165     2389   2011   1640    169   -281    -37       C  
ATOM   1377  C  BMET A 165      10.702   1.944  17.739  0.50 14.88           C  
ANISOU 1377  C  BMET A 165     2261   1882   1511    168   -283    -38       C  
ATOM   1378  O  AMET A 165      10.776   2.215  16.550  0.50 15.72           O  
ANISOU 1378  O  AMET A 165     2340   1991   1642    146   -292    -48       O  
ATOM   1379  O  BMET A 165      10.842   2.241  16.560  0.50 14.65           O  
ANISOU 1379  O  BMET A 165     2205   1856   1506    147   -292    -48       O  
ATOM   1380  CB AMET A 165      12.260   1.033  19.260  0.50 18.07           C  
ANISOU 1380  CB AMET A 165     2700   2275   1892    129   -348    -39       C  
ATOM   1381  CB BMET A 165      12.844   1.448  18.767  0.50 13.85           C  
ANISOU 1381  CB BMET A 165     2153   1739   1371    111   -364    -44       C  
ATOM   1382  CG AMET A 165      13.510   1.441  18.567  0.50 21.85           C  
ANISOU 1382  CG AMET A 165     3156   2749   2397     85   -389    -47       C  
ATOM   1383  CG BMET A 165      13.883   0.481  19.312  0.50 14.29           C  
ANISOU 1383  CG BMET A 165     2179   1802   1450     75   -407    -30       C  
ATOM   1384  SD AMET A 165      14.871   1.411  19.737  0.50 29.90           S  
ANISOU 1384  SD AMET A 165     4189   3763   3410     48   -446    -30       S  
ATOM   1385  SD BMET A 165      13.470  -0.155  20.945  0.50 15.29           S  
ANISOU 1385  SD BMET A 165     2343   1928   1536     91   -411    -13       S  
ATOM   1386  CE AMET A 165      14.286   0.130  20.907  0.50 30.34           C  
ANISOU 1386  CE AMET A 165     4248   3833   3446     84   -417    -14       C  
ATOM   1387  CE BMET A 165      13.829   1.249  21.920  0.50 19.00           C  
ANISOU 1387  CE BMET A 165     2937   2357   1926     73   -447    -26       C  
ATOM   1388  N   GLU A 166       9.962   2.669  18.591  1.00 16.13           N  
ANISOU 1388  N   GLU A 166     2493   2015   1619    199   -262    -36       N  
ATOM   1389  CA  GLU A 166       9.355   3.908  18.240  1.00 17.53           C  
ANISOU 1389  CA  GLU A 166     2711   2172   1777    221   -233    -39       C  
ATOM   1390  C   GLU A 166      10.049   4.945  19.115  1.00 19.53           C  
ANISOU 1390  C   GLU A 166     3063   2383   1974    209   -257    -62       C  
ATOM   1391  O   GLU A 166      10.099   4.793  20.337  1.00 20.14           O  
ANISOU 1391  O   GLU A 166     3201   2445   2007    219   -259    -61       O  
ATOM   1392  CB  GLU A 166       7.885   3.883  18.595  1.00 19.56           C  
ANISOU 1392  CB  GLU A 166     2977   2430   2027    279   -169     -7       C  
ATOM   1393  CG  GLU A 166       7.200   5.177  18.243  1.00 23.51           C  
ANISOU 1393  CG  GLU A 166     3512   2905   2515    306   -131     -1       C  
ATOM   1394  CD  GLU A 166       5.719   4.914  18.267  1.00 27.84           C  
ANISOU 1394  CD  GLU A 166     4030   3466   3083    360    -68     49       C  
ATOM   1395  OE1 GLU A 166       5.148   4.841  19.378  1.00 29.33           O  
ANISOU 1395  OE1 GLU A 166     4265   3640   3240    405    -28     68       O  
ATOM   1396  OE2 GLU A 166       5.144   4.697  17.176  1.00 27.18           O  
ANISOU 1396  OE2 GLU A 166     3872   3407   3047    354    -62     75       O  
ATOM   1397  N   LEU A 167      10.596   5.973  18.494  1.00 20.80           N  
ANISOU 1397  N   LEU A 167     3244   2526   2134    184   -279    -79       N  
ATOM   1398  CA  LEU A 167      11.246   7.053  19.220  1.00 23.30           C  
ANISOU 1398  CA  LEU A 167     3661   2796   2395    166   -309   -100       C  
ATOM   1399  C   LEU A 167      10.170   7.948  19.834  1.00 25.62           C  
ANISOU 1399  C   LEU A 167     4043   3052   2639    220   -247    -99       C  
ATOM   1400  O   LEU A 167       9.054   8.016  19.312  1.00 25.54           O  
ANISOU 1400  O   LEU A 167     3997   3053   2653    264   -187    -78       O  
ATOM   1401  CB  LEU A 167      12.109   7.853  18.227  1.00 24.19           C  
ANISOU 1401  CB  LEU A 167     3754   2902   2534    124   -348   -113       C  
ATOM   1402  CG  LEU A 167      13.150   7.045  17.422  1.00 26.98           C  
ANISOU 1402  CG  LEU A 167     4016   3291   2946     79   -394   -107       C  
ATOM   1403  CD1 LEU A 167      14.029   7.967  16.621  1.00 28.28           C  
ANISOU 1403  CD1 LEU A 167     4176   3442   3127     40   -432   -114       C  
ATOM   1404  CD2 LEU A 167      14.022   6.155  18.327  1.00 27.79           C  
ANISOU 1404  CD2 LEU A 167     4117   3399   3045     50   -439    -97       C  
ATOM   1405  N   PRO A 168      10.502   8.716  20.885  1.00 27.44           N  
ANISOU 1405  N   PRO A 168     4393   3232   2800    214   -261   -117       N  
ATOM   1406  CA  PRO A 168       9.495   9.604  21.486  1.00 28.84           C  
ANISOU 1406  CA  PRO A 168     4669   3364   2926    271   -190   -117       C  
ATOM   1407  C   PRO A 168       8.854  10.601  20.525  1.00 30.15           C  
ANISOU 1407  C   PRO A 168     4820   3517   3119    298   -144   -111       C  
ATOM   1408  O   PRO A 168       7.806  11.147  20.853  1.00 31.65           O  
ANISOU 1408  O   PRO A 168     5059   3678   3287    360    -67    -95       O  
ATOM   1409  CB  PRO A 168      10.264  10.307  22.605  1.00 29.60           C  
ANISOU 1409  CB  PRO A 168     4906   3403   2940    240   -231   -145       C  
ATOM   1410  CG  PRO A 168      11.376   9.380  22.945  1.00 29.87           C  
ANISOU 1410  CG  PRO A 168     4903   3464   2981    179   -313   -145       C  
ATOM   1411  CD  PRO A 168      11.767   8.736  21.646  1.00 27.74           C  
ANISOU 1411  CD  PRO A 168     4489   3251   2801    155   -339   -133       C  
ATOM   1412  N   THR A 169       9.448  10.838  19.342  1.00 29.64           N  
ANISOU 1412  N   THR A 169     4686   3473   3103    257   -187   -118       N  
ATOM   1413  CA  THR A 169       8.869  11.743  18.351  1.00 29.70           C  
ANISOU 1413  CA  THR A 169     4668   3475   3142    278   -149   -108       C  
ATOM   1414  C   THR A 169       7.931  11.078  17.330  1.00 29.13           C  
ANISOU 1414  C   THR A 169     4478   3455   3136    302   -111    -70       C  
ATOM   1415  O   THR A 169       7.497  11.738  16.388  1.00 29.33           O  
ANISOU 1415  O   THR A 169     4469   3484   3194    311    -89    -55       O  
ATOM   1416  CB  THR A 169       9.946  12.533  17.623  1.00 31.65           C  
ANISOU 1416  CB  THR A 169     4914   3711   3402    222   -211   -131       C  
ATOM   1417  OG1 THR A 169      10.933  11.626  17.118  1.00 32.87           O  
ANISOU 1417  OG1 THR A 169     4986   3909   3595    169   -276   -134       O  
ATOM   1418  CG2 THR A 169      10.574  13.602  18.502  1.00 32.20           C  
ANISOU 1418  CG2 THR A 169     5117   3714   3405    203   -239   -159       C  
ATOM   1419  N   GLY A 170       7.618   9.799  17.517  1.00 28.09           N  
ANISOU 1419  N   GLY A 170     4288   3363   3024    310   -107    -52       N  
ATOM   1420  CA  GLY A 170       6.690   9.104  16.634  1.00 27.29           C  
ANISOU 1420  CA  GLY A 170     4084   3306   2979    327    -78    -12       C  
ATOM   1421  C   GLY A 170       7.276   8.478  15.392  1.00 25.98           C  
ANISOU 1421  C   GLY A 170     3825   3184   2863    276   -126    -18       C  
ATOM   1422  O   GLY A 170       6.531   7.969  14.548  1.00 26.76           O  
ANISOU 1422  O   GLY A 170     3849   3314   3003    280   -110     14       O  
ATOM   1423  N   VAL A 171       8.602   8.553  15.235  1.00 23.64           N  
ANISOU 1423  N   VAL A 171     3537   2884   2562    226   -185    -54       N  
ATOM   1424  CA  VAL A 171       9.262   7.930  14.096  1.00 21.19           C  
ANISOU 1424  CA  VAL A 171     3148   2609   2295    182   -223    -60       C  
ATOM   1425  C   VAL A 171       9.803   6.561  14.543  1.00 17.38           C  
ANISOU 1425  C   VAL A 171     2636   2147   1821    166   -248    -64       C  
ATOM   1426  O   VAL A 171       9.847   6.266  15.735  1.00 17.18           O  
ANISOU 1426  O   VAL A 171     2655   2109   1765    180   -248    -66       O  
ATOM   1427  CB  VAL A 171      10.323   8.817  13.418  1.00 22.74           C  
ANISOU 1427  CB  VAL A 171     3351   2792   2497    143   -262    -82       C  
ATOM   1428  CG1 VAL A 171       9.690  10.084  12.853  1.00 23.85           C  
ANISOU 1428  CG1 VAL A 171     3511   2915   2636    161   -234    -74       C  
ATOM   1429  CG2 VAL A 171      11.443   9.141  14.386  1.00 23.08           C  
ANISOU 1429  CG2 VAL A 171     3457   2805   2507    118   -307   -104       C  
ATOM   1430  N   HIS A 172      10.166   5.722  13.586  1.00 15.44           N  
ANISOU 1430  N   HIS A 172     2320   1932   1615    137   -265    -64       N  
ATOM   1431  CA  HIS A 172      10.508   4.343  13.854  1.00 13.98           C  
ANISOU 1431  CA  HIS A 172     2098   1766   1447    127   -277    -62       C  
ATOM   1432  C   HIS A 172      11.940   3.965  13.543  1.00 13.47           C  
ANISOU 1432  C   HIS A 172     2010   1704   1405     86   -317    -76       C  
ATOM   1433  O   HIS A 172      12.551   4.481  12.612  1.00 13.64           O  
ANISOU 1433  O   HIS A 172     2016   1725   1443     62   -330    -84       O  
ATOM   1434  CB  HIS A 172       9.512   3.472  13.081  1.00 13.55           C  
ANISOU 1434  CB  HIS A 172     1986   1740   1423    134   -251    -41       C  
ATOM   1435  CG  HIS A 172       8.096   3.784  13.471  1.00 13.40           C  
ANISOU 1435  CG  HIS A 172     1979   1719   1392    177   -211    -10       C  
ATOM   1436  ND1 HIS A 172       7.228   4.426  12.601  1.00 14.72           N  
ANISOU 1436  ND1 HIS A 172     2129   1892   1572    184   -190     13       N  
ATOM   1437  CD2 HIS A 172       7.501   3.693  14.686  1.00 14.40           C  
ANISOU 1437  CD2 HIS A 172     2140   1836   1495    216   -186      6       C  
ATOM   1438  CE1 HIS A 172       6.107   4.609  13.283  1.00 15.27           C  
ANISOU 1438  CE1 HIS A 172     2212   1955   1633    229   -150     48       C  
ATOM   1439  NE2 HIS A 172       6.228   4.194  14.544  1.00 15.66           N  
ANISOU 1439  NE2 HIS A 172     2297   1995   1659    252   -143     44       N  
ATOM   1440  N   ALA A 173      12.452   3.012  14.322  1.00 12.95           N  
ANISOU 1440  N   ALA A 173     1934   1642   1343     80   -331    -72       N  
ATOM   1441  CA  ALA A 173      13.821   2.530  14.168  1.00 12.79           C  
ANISOU 1441  CA  ALA A 173     1885   1623   1353     46   -364    -72       C  
ATOM   1442  C   ALA A 173      13.843   1.028  14.231  1.00 12.27           C  
ANISOU 1442  C   ALA A 173     1771   1575   1317     48   -352    -61       C  
ATOM   1443  O   ALA A 173      13.033   0.406  14.916  1.00 12.33           O  
ANISOU 1443  O   ALA A 173     1781   1590   1312     72   -336    -53       O  
ATOM   1444  CB  ALA A 173      14.713   3.092  15.263  1.00 13.06           C  
ANISOU 1444  CB  ALA A 173     1967   1635   1362     27   -408    -69       C  
ATOM   1445  N   GLY A 174      14.761   0.447  13.481  1.00 11.78           N  
ANISOU 1445  N   GLY A 174     1663   1516   1295     26   -356    -57       N  
ATOM   1446  CA  GLY A 174      14.888  -0.994  13.445  1.00 11.54           C  
ANISOU 1446  CA  GLY A 174     1590   1496   1298     28   -340    -47       C  
ATOM   1447  C   GLY A 174      16.188  -1.435  12.847  1.00 11.18           C  
ANISOU 1447  C   GLY A 174     1505   1445   1298      6   -341    -36       C  
ATOM   1448  O   GLY A 174      17.097  -0.636  12.618  1.00 11.32           O  
ANISOU 1448  O   GLY A 174     1524   1453   1323    -12   -363    -29       O  
ATOM   1449  N   THR A 175      16.261  -2.716  12.564  1.00 10.81           N  
ANISOU 1449  N   THR A 175     1423   1401   1283     10   -314    -30       N  
ATOM   1450  CA  THR A 175      17.491  -3.329  12.129  1.00 10.66           C  
ANISOU 1450  CA  THR A 175     1365   1372   1314     -1   -302    -10       C  
ATOM   1451  C   THR A 175      17.367  -3.974  10.774  1.00 10.85           C  
ANISOU 1451  C   THR A 175     1378   1390   1355      1   -256    -25       C  
ATOM   1452  O   THR A 175      16.261  -4.147  10.274  1.00 11.09           O  
ANISOU 1452  O   THR A 175     1427   1426   1360      6   -241    -47       O  
ATOM   1453  CB  THR A 175      17.861  -4.455  13.166  1.00 11.46           C  
ANISOU 1453  CB  THR A 175     1438   1473   1442      3   -307     17       C  
ATOM   1454  OG1 THR A 175      16.924  -5.534  13.087  1.00 11.86           O  
ANISOU 1454  OG1 THR A 175     1485   1530   1492     19   -277      4       O  
ATOM   1455  CG2 THR A 175      17.958  -3.963  14.586  1.00 10.45           C  
ANISOU 1455  CG2 THR A 175     1331   1350   1289     -4   -355     32       C  
ATOM   1456  N   ASP A 176      18.499  -4.410  10.211  1.00 10.92           N  
ANISOU 1456  N   ASP A 176     1357   1384   1409     -3   -231     -6       N  
ATOM   1457  CA  ASP A 176      18.444  -5.296   9.071  1.00 11.27           C  
ANISOU 1457  CA  ASP A 176     1402   1414   1467      2   -177    -19       C  
ATOM   1458  C   ASP A 176      18.223  -6.736   9.677  1.00 12.10           C  
ANISOU 1458  C   ASP A 176     1491   1512   1593     14   -159    -11       C  
ATOM   1459  O   ASP A 176      18.096  -6.893  10.907  1.00 12.09           O  
ANISOU 1459  O   ASP A 176     1476   1524   1594     17   -190      5       O  
ATOM   1460  CB  ASP A 176      19.709  -5.176   8.218  1.00 12.43           C  
ANISOU 1460  CB  ASP A 176     1529   1542   1652      2   -144      2       C  
ATOM   1461  CG  ASP A 176      20.997  -5.503   8.928  1.00 14.28           C  
ANISOU 1461  CG  ASP A 176     1714   1768   1944      5   -146     55       C  
ATOM   1462  OD1 ASP A 176      20.945  -6.153  10.000  1.00 12.59           O  
ANISOU 1462  OD1 ASP A 176     1481   1558   1743      8   -165     72       O  
ATOM   1463  OD2 ASP A 176      22.059  -5.109   8.421  1.00 16.57           O  
ANISOU 1463  OD2 ASP A 176     1979   2047   2269      4   -132     86       O  
ATOM   1464  N   LEU A 177      18.214  -7.776   8.839  1.00 12.56           N  
ANISOU 1464  N   LEU A 177     1557   1549   1667     18   -108    -21       N  
ATOM   1465  CA  LEU A 177      17.977  -9.134   9.340  1.00 13.37           C  
ANISOU 1465  CA  LEU A 177     1647   1641   1791     28    -91    -14       C  
ATOM   1466  C   LEU A 177      19.229  -9.788   9.950  1.00 14.68           C  
ANISOU 1466  C   LEU A 177     1765   1794   2020     40    -71     31       C  
ATOM   1467  O   LEU A 177      19.141 -10.901  10.466  1.00 15.23           O  
ANISOU 1467  O   LEU A 177     1817   1855   2115     49    -57     43       O  
ATOM   1468  CB  LEU A 177      17.292 -10.027   8.318  1.00 13.37           C  
ANISOU 1468  CB  LEU A 177     1687   1618   1774     23    -52    -44       C  
ATOM   1469  CG  LEU A 177      15.764  -9.973   8.325  1.00 14.51           C  
ANISOU 1469  CG  LEU A 177     1860   1781   1872      9    -85    -67       C  
ATOM   1470  CD1 LEU A 177      15.215 -10.582   9.597  1.00 15.35           C  
ANISOU 1470  CD1 LEU A 177     1940   1903   1990     20   -110    -50       C  
ATOM   1471  CD2 LEU A 177      15.227  -8.547   8.101  1.00 15.65           C  
ANISOU 1471  CD2 LEU A 177     2019   1950   1976     -1   -120    -78       C  
ATOM   1472  N   GLU A 178      20.370  -9.083   9.938  1.00 14.29           N  
ANISOU 1472  N   GLU A 178     1687   1743   1999     38    -76     64       N  
ATOM   1473  CA  GLU A 178      21.541  -9.484  10.702  1.00 13.76           C  
ANISOU 1473  CA  GLU A 178     1564   1671   1995     43    -76    123       C  
ATOM   1474  C   GLU A 178      21.486  -8.861  12.125  1.00 13.43           C  
ANISOU 1474  C   GLU A 178     1508   1657   1938     26   -152    143       C  
ATOM   1475  O   GLU A 178      22.376  -9.100  12.928  1.00 13.86           O  
ANISOU 1475  O   GLU A 178     1516   1712   2037     20   -171    198       O  
ATOM   1476  CB  GLU A 178      22.832  -9.097   9.978  1.00 15.67           C  
ANISOU 1476  CB  GLU A 178     1777   1894   2282     47    -44    162       C  
ATOM   1477  CG  GLU A 178      22.961  -9.834   8.661  1.00 20.95           C  
ANISOU 1477  CG  GLU A 178     2469   2527   2963     68     43    145       C  
ATOM   1478  CD  GLU A 178      24.223  -9.546   7.877  1.00 29.38           C  
ANISOU 1478  CD  GLU A 178     3511   3573   4079     81     92    189       C  
ATOM   1479  OE1 GLU A 178      24.984  -8.632   8.273  1.00 29.50           O  
ANISOU 1479  OE1 GLU A 178     3485   3603   4119     68     49    235       O  
ATOM   1480  OE2 GLU A 178      24.452 -10.242   6.861  1.00 33.24           O  
ANISOU 1480  OE2 GLU A 178     4024   4025   4580    103    175    182       O  
ATOM   1481  N   GLY A 179      20.467  -8.044  12.419  1.00 13.13           N  
ANISOU 1481  N   GLY A 179     1512   1640   1836     18   -194    105       N  
ATOM   1482  CA  GLY A 179      20.307  -7.465  13.737  1.00 12.66           C  
ANISOU 1482  CA  GLY A 179     1460   1601   1751      6   -257    117       C  
ATOM   1483  C   GLY A 179      21.024  -6.160  13.973  1.00 12.23           C  
ANISOU 1483  C   GLY A 179     1411   1548   1686    -18   -306    136       C  
ATOM   1484  O   GLY A 179      21.067  -5.710  15.109  1.00 12.53           O  
ANISOU 1484  O   GLY A 179     1464   1596   1702    -34   -361    151       O  
ATOM   1485  N   ASN A 180      21.583  -5.550  12.928  1.00 11.78           N  
ANISOU 1485  N   ASN A 180     1351   1482   1645    -22   -289    137       N  
ATOM   1486  CA  ASN A 180      22.268  -4.273  13.077  1.00 12.01           C  
ANISOU 1486  CA  ASN A 180     1386   1510   1668    -47   -339    158       C  
ATOM   1487  C   ASN A 180      21.296  -3.149  12.821  1.00 11.40           C  
ANISOU 1487  C   ASN A 180     1367   1440   1525    -48   -357    106       C  
ATOM   1488  O   ASN A 180      20.701  -3.072  11.748  1.00 10.73           O  
ANISOU 1488  O   ASN A 180     1297   1355   1425    -35   -318     71       O  
ATOM   1489  CB  ASN A 180      23.447  -4.180  12.113  1.00 13.42           C  
ANISOU 1489  CB  ASN A 180     1521   1674   1905    -49   -310    197       C  
ATOM   1490  CG  ASN A 180      24.560  -5.117  12.483  1.00 16.66           C  
ANISOU 1490  CG  ASN A 180     1866   2074   2390    -49   -296    267       C  
ATOM   1491  OD1 ASN A 180      25.033  -5.908  11.663  1.00 18.84           O  
ANISOU 1491  OD1 ASN A 180     2108   2333   2715    -25   -227    285       O  
ATOM   1492  ND2 ASN A 180      24.992  -5.054  13.726  1.00 16.09           N  
ANISOU 1492  ND2 ASN A 180     1778   2009   2326    -74   -358    310       N  
ATOM   1493  N   PHE A 181      21.136  -2.246  13.795  1.00 11.37           N  
ANISOU 1493  N   PHE A 181     1401   1438   1479    -66   -415    105       N  
ATOM   1494  CA  PHE A 181      20.248  -1.104  13.610  1.00 11.91           C  
ANISOU 1494  CA  PHE A 181     1528   1509   1490    -63   -427     62       C  
ATOM   1495  C   PHE A 181      20.686  -0.235  12.452  1.00 12.38           C  
ANISOU 1495  C   PHE A 181     1580   1562   1561    -71   -419     60       C  
ATOM   1496  O   PHE A 181      21.881  -0.094  12.176  1.00 12.34           O  
ANISOU 1496  O   PHE A 181     1538   1548   1602    -89   -430    100       O  
ATOM   1497  CB  PHE A 181      20.201  -0.235  14.871  1.00 12.24           C  
ANISOU 1497  CB  PHE A 181     1623   1544   1484    -81   -487     65       C  
ATOM   1498  CG  PHE A 181      19.085  -0.590  15.813  1.00 12.39           C  
ANISOU 1498  CG  PHE A 181     1681   1570   1456    -60   -481     43       C  
ATOM   1499  CD1 PHE A 181      19.280  -1.514  16.825  1.00 12.74           C  
ANISOU 1499  CD1 PHE A 181     1711   1620   1510    -62   -494     68       C  
ATOM   1500  CD2 PHE A 181      17.854   0.039  15.721  1.00 12.69           C  
ANISOU 1500  CD2 PHE A 181     1768   1609   1444    -36   -461      5       C  
ATOM   1501  CE1 PHE A 181      18.258  -1.822  17.714  1.00 12.99           C  
ANISOU 1501  CE1 PHE A 181     1778   1658   1498    -40   -486     52       C  
ATOM   1502  CE2 PHE A 181      16.828  -0.277  16.600  1.00 13.19           C  
ANISOU 1502  CE2 PHE A 181     1865   1678   1470    -11   -449     -5       C  
ATOM   1503  CZ  PHE A 181      17.031  -1.207  17.593  1.00 13.05           C  
ANISOU 1503  CZ  PHE A 181     1834   1666   1458    -12   -461     17       C  
ATOM   1504  N   TYR A 182      19.702   0.341  11.784  1.00 11.78           N  
ANISOU 1504  N   TYR A 182     1537   1491   1449    -58   -398     19       N  
ATOM   1505  CA  TYR A 182      19.973   1.380  10.817  1.00 12.63           C  
ANISOU 1505  CA  TYR A 182     1648   1594   1557    -67   -400     14       C  
ATOM   1506  C   TYR A 182      20.218   2.634  11.653  1.00 13.60           C  
ANISOU 1506  C   TYR A 182     1812   1704   1651    -89   -460     20       C  
ATOM   1507  O   TYR A 182      19.486   2.909  12.615  1.00 14.08           O  
ANISOU 1507  O   TYR A 182     1923   1761   1665    -83   -478      2       O  
ATOM   1508  CB  TYR A 182      18.765   1.574   9.929  1.00 12.36           C  
ANISOU 1508  CB  TYR A 182     1636   1569   1491    -50   -364    -26       C  
ATOM   1509  CG  TYR A 182      18.689   0.495   8.878  1.00 12.38           C  
ANISOU 1509  CG  TYR A 182     1610   1576   1518    -41   -312    -31       C  
ATOM   1510  CD1 TYR A 182      19.511   0.528   7.766  1.00 12.83           C  
ANISOU 1510  CD1 TYR A 182     1643   1626   1605    -46   -286    -20       C  
ATOM   1511  CD2 TYR A 182      17.862  -0.604   9.045  1.00 12.57           C  
ANISOU 1511  CD2 TYR A 182     1635   1606   1534    -27   -287    -44       C  
ATOM   1512  CE1 TYR A 182      19.456  -0.465   6.802  1.00 12.90           C  
ANISOU 1512  CE1 TYR A 182     1644   1631   1626    -38   -232    -28       C  
ATOM   1513  CE2 TYR A 182      17.792  -1.601   8.089  1.00 12.93           C  
ANISOU 1513  CE2 TYR A 182     1670   1648   1595    -23   -242    -52       C  
ATOM   1514  CZ  TYR A 182      18.601  -1.534   6.970  1.00 13.28           C  
ANISOU 1514  CZ  TYR A 182     1702   1681   1661    -29   -212    -46       C  
ATOM   1515  OH  TYR A 182      18.538  -2.508   5.998  1.00 13.15           O  
ANISOU 1515  OH  TYR A 182     1692   1653   1651    -25   -162    -57       O  
ATOM   1516  N   GLY A 183      21.282   3.338  11.320  1.00 13.88           N  
ANISOU 1516  N   GLY A 183     1830   1729   1714   -113   -488     49       N  
ATOM   1517  CA  GLY A 183      21.632   4.549  12.030  1.00 15.00           C  
ANISOU 1517  CA  GLY A 183     2017   1853   1830   -142   -551     58       C  
ATOM   1518  C   GLY A 183      22.167   4.279  13.408  1.00 15.58           C  
ANISOU 1518  C   GLY A 183     2106   1916   1898   -167   -605     87       C  
ATOM   1519  O   GLY A 183      22.626   3.178  13.716  1.00 15.49           O  
ANISOU 1519  O   GLY A 183     2050   1914   1923   -166   -597    118       O  
ATOM   1520  N   PRO A 184      22.081   5.295  14.261  1.00 15.71           N  
ANISOU 1520  N   PRO A 184     2194   1910   1864   -190   -659     79       N  
ATOM   1521  CA  PRO A 184      22.700   5.199  15.592  1.00 15.80           C  
ANISOU 1521  CA  PRO A 184     2234   1908   1861   -227   -724    112       C  
ATOM   1522  C   PRO A 184      21.818   4.666  16.712  1.00 15.71           C  
ANISOU 1522  C   PRO A 184     2274   1897   1796   -209   -716     86       C  
ATOM   1523  O   PRO A 184      22.202   4.708  17.880  1.00 16.85           O  
ANISOU 1523  O   PRO A 184     2463   2028   1912   -241   -773    107       O  
ATOM   1524  CB  PRO A 184      23.004   6.662  15.886  1.00 16.92           C  
ANISOU 1524  CB  PRO A 184     2447   2017   1965   -264   -787    110       C  
ATOM   1525  CG  PRO A 184      21.820   7.366  15.282  1.00 17.42           C  
ANISOU 1525  CG  PRO A 184     2552   2077   1988   -224   -734     51       C  
ATOM   1526  CD  PRO A 184      21.576   6.658  13.991  1.00 15.87           C  
ANISOU 1526  CD  PRO A 184     2274   1912   1842   -190   -667     46       C  
ATOM   1527  N   PHE A 185      20.626   4.205  16.356  1.00 15.02           N  
ANISOU 1527  N   PHE A 185     2187   1827   1693   -159   -649     45       N  
ATOM   1528  CA  PHE A 185      19.631   3.816  17.322  1.00 15.08           C  
ANISOU 1528  CA  PHE A 185     2245   1836   1649   -134   -632     22       C  
ATOM   1529  C   PHE A 185      19.972   2.543  18.048  1.00 15.67           C  
ANISOU 1529  C   PHE A 185     2280   1925   1746   -138   -639     52       C  
ATOM   1530  O   PHE A 185      20.717   1.701  17.548  1.00 15.41           O  
ANISOU 1530  O   PHE A 185     2167   1908   1780   -146   -631     84       O  
ATOM   1531  CB  PHE A 185      18.245   3.763  16.665  1.00 14.67           C  
ANISOU 1531  CB  PHE A 185     2196   1798   1582    -83   -562    -17       C  
ATOM   1532  CG  PHE A 185      17.918   5.097  16.038  1.00 14.96           C  
ANISOU 1532  CG  PHE A 185     2271   1816   1595    -80   -557    -41       C  
ATOM   1533  CD1 PHE A 185      17.777   6.231  16.819  1.00 15.71           C  
ANISOU 1533  CD1 PHE A 185     2458   1877   1632    -89   -586    -54       C  
ATOM   1534  CD2 PHE A 185      17.856   5.235  14.665  1.00 15.58           C  
ANISOU 1534  CD2 PHE A 185     2299   1909   1710    -72   -527    -47       C  
ATOM   1535  CE1 PHE A 185      17.550   7.473  16.232  1.00 15.86           C  
ANISOU 1535  CE1 PHE A 185     2512   1878   1637    -87   -581    -71       C  
ATOM   1536  CE2 PHE A 185      17.627   6.471  14.088  1.00 15.63           C  
ANISOU 1536  CE2 PHE A 185     2336   1901   1701    -73   -526    -62       C  
ATOM   1537  CZ  PHE A 185      17.450   7.580  14.874  1.00 15.37           C  
ANISOU 1537  CZ  PHE A 185     2389   1835   1617    -78   -552    -74       C  
ATOM   1538  N   VAL A 186      19.484   2.448  19.269  1.00 16.07           N  
ANISOU 1538  N   VAL A 186     2393   1970   1744   -134   -652     45       N  
ATOM   1539  CA  VAL A 186      19.714   1.295  20.124  1.00 16.52           C  
ANISOU 1539  CA  VAL A 186     2422   2041   1814   -139   -663     74       C  
ATOM   1540  C   VAL A 186      18.408   0.767  20.679  1.00 16.78           C  
ANISOU 1540  C   VAL A 186     2486   2085   1806    -92   -614     47       C  
ATOM   1541  O   VAL A 186      17.436   1.513  20.778  1.00 17.71           O  
ANISOU 1541  O   VAL A 186     2669   2189   1870    -63   -588     13       O  
ATOM   1542  CB  VAL A 186      20.699   1.623  21.273  1.00 17.66           C  
ANISOU 1542  CB  VAL A 186     2610   2167   1934   -196   -747    112       C  
ATOM   1543  CG1 VAL A 186      22.088   1.924  20.725  1.00 18.92           C  
ANISOU 1543  CG1 VAL A 186     2715   2320   2153   -245   -797    160       C  
ATOM   1544  CG2 VAL A 186      20.188   2.782  22.130  1.00 18.38           C  
ANISOU 1544  CG2 VAL A 186     2830   2224   1930   -204   -773     80       C  
ATOM   1545  N   ASP A 187      18.386  -0.515  21.077  1.00 15.60           N  
ANISOU 1545  N   ASP A 187     2285   1956   1684    -81   -601     69       N  
ATOM   1546  CA  ASP A 187      17.180  -1.106  21.642  1.00 15.58           C  
ANISOU 1546  CA  ASP A 187     2303   1966   1651    -37   -557     53       C  
ATOM   1547  C   ASP A 187      17.101  -0.911  23.133  1.00 16.90           C  
ANISOU 1547  C   ASP A 187     2549   2120   1752    -47   -590     61       C  
ATOM   1548  O   ASP A 187      17.132  -1.857  23.916  1.00 16.91           O  
ANISOU 1548  O   ASP A 187     2531   2136   1759    -47   -597     85       O  
ATOM   1549  CB  ASP A 187      16.973  -2.565  21.246  1.00 15.08           C  
ANISOU 1549  CB  ASP A 187     2152   1930   1649    -16   -519     67       C  
ATOM   1550  CG  ASP A 187      18.169  -3.478  21.361  1.00 15.13           C  
ANISOU 1550  CG  ASP A 187     2089   1944   1717    -48   -548    111       C  
ATOM   1551  OD1 ASP A 187      19.244  -3.005  21.797  1.00 15.07           O  
ANISOU 1551  OD1 ASP A 187     2092   1923   1709    -92   -606    141       O  
ATOM   1552  OD2 ASP A 187      18.030  -4.666  21.026  1.00 14.64           O  
ANISOU 1552  OD2 ASP A 187     1961   1897   1704    -29   -512    121       O  
ATOM   1553  N   ARG A 188      16.993   0.352  23.513  1.00 18.27           N  
ANISOU 1553  N   ARG A 188     2821   2263   1859    -57   -611     40       N  
ATOM   1554  CA  ARG A 188      16.915   0.803  24.882  1.00 20.54           C  
ANISOU 1554  CA  ARG A 188     3215   2525   2064    -70   -642     40       C  
ATOM   1555  C   ARG A 188      15.979   2.000  24.892  1.00 22.19           C  
ANISOU 1555  C   ARG A 188     3521   2702   2206    -35   -603      0       C  
ATOM   1556  O   ARG A 188      16.006   2.826  23.979  1.00 21.85           O  
ANISOU 1556  O   ARG A 188     3475   2648   2178    -36   -596    -19       O  
ATOM   1557  CB  ARG A 188      18.315   1.222  25.371  1.00 23.06           C  
ANISOU 1557  CB  ARG A 188     3562   2825   2376   -146   -735     70       C  
ATOM   1558  CG  ARG A 188      18.378   1.486  26.858  1.00 28.82           C  
ANISOU 1558  CG  ARG A 188     4405   3529   3017   -173   -780     76       C  
ATOM   1559  CD  ARG A 188      19.755   1.913  27.332  1.00 34.58           C  
ANISOU 1559  CD  ARG A 188     5164   4237   3738   -260   -885    114       C  
ATOM   1560  NE  ARG A 188      19.637   2.726  28.541  1.00 39.48           N  
ANISOU 1560  NE  ARG A 188     5940   4813   4246   -288   -924     99       N  
ATOM   1561  CZ  ARG A 188      20.650   3.073  29.325  1.00 42.92           C  
ANISOU 1561  CZ  ARG A 188     6437   5225   4646   -369  -1024    134       C  
ATOM   1562  NH1 ARG A 188      21.884   2.678  29.040  1.00 43.29           N  
ANISOU 1562  NH1 ARG A 188     6388   5290   4771   -431  -1096    195       N  
ATOM   1563  NH2 ARG A 188      20.434   3.803  30.412  1.00 43.34           N  
ANISOU 1563  NH2 ARG A 188     6649   5232   4584   -392  -1053    113       N  
ATOM   1564  N   GLN A 189      15.143   2.089  25.912  1.00 24.10           N  
ANISOU 1564  N   GLN A 189     3850   2930   2379     -2   -573     -9       N  
ATOM   1565  CA  GLN A 189      14.193   3.177  26.044  1.00 26.30           C  
ANISOU 1565  CA  GLN A 189     4227   3172   2593     41   -522    -40       C  
ATOM   1566  C   GLN A 189      14.930   4.350  26.661  1.00 28.13           C  
ANISOU 1566  C   GLN A 189     4583   3352   2753    -10   -582    -54       C  
ATOM   1567  O   GLN A 189      14.955   4.501  27.883  1.00 28.84           O  
ANISOU 1567  O   GLN A 189     4780   3414   2765    -22   -601    -54       O  
ATOM   1568  CB  GLN A 189      13.013   2.731  26.905  1.00 28.62           C  
ANISOU 1568  CB  GLN A 189     4560   3469   2846    103   -454    -36       C  
ATOM   1569  CG  GLN A 189      11.848   3.700  26.891  1.00 33.55           C  
ANISOU 1569  CG  GLN A 189     5266   4059   3421    164   -378    -56       C  
ATOM   1570  CD  GLN A 189      10.793   3.236  27.855  1.00 39.90           C  
ANISOU 1570  CD  GLN A 189     6110   4864   4185    225   -312    -40       C  
ATOM   1571  OE1 GLN A 189      10.375   2.071  27.855  1.00 41.94           O  
ANISOU 1571  OE1 GLN A 189     6280   5166   4490    248   -292    -13       O  
ATOM   1572  NE2 GLN A 189      10.354   4.137  28.711  1.00 40.98           N  
ANISOU 1572  NE2 GLN A 189     6387   4950   4234    254   -275    -54       N  
ATOM   1573  N   THR A 190      15.597   5.137  25.811  1.00 29.21           N  
ANISOU 1573  N   THR A 190     4705   3476   2918    -45   -618    -63       N  
ATOM   1574  CA  THR A 190      16.412   6.287  26.208  1.00 30.97           C  
ANISOU 1574  CA  THR A 190     5034   3648   3086   -104   -687    -71       C  
ATOM   1575  C   THR A 190      16.145   7.506  25.303  1.00 31.77           C  
ANISOU 1575  C   THR A 190     5160   3722   3190    -89   -662   -100       C  
ATOM   1576  O   THR A 190      15.420   7.392  24.308  1.00 32.40           O  
ANISOU 1576  O   THR A 190     5161   3828   3322    -39   -597   -107       O  
ATOM   1577  CB  THR A 190      17.915   5.902  26.162  1.00 33.71           C  
ANISOU 1577  CB  THR A 190     5318   4010   3480   -186   -788    -31       C  
ATOM   1578  OG1 THR A 190      18.225   5.263  24.922  1.00 35.59           O  
ANISOU 1578  OG1 THR A 190     5408   4293   3822   -179   -774    -14       O  
ATOM   1579  CG2 THR A 190      18.348   5.087  27.338  1.00 34.74           C  
ANISOU 1579  CG2 THR A 190     5465   4150   3586   -220   -835      1       C  
ATOM   1580  N   ALA A 191      16.753   8.667  25.625  1.00 31.73           N  
ANISOU 1580  N   ALA A 191     5262   3663   3131   -138   -719   -112       N  
ATOM   1581  CA  ALA A 191      16.636   9.844  24.794  1.00 32.04           C  
ANISOU 1581  CA  ALA A 191     5322   3675   3178   -132   -705   -134       C  
ATOM   1582  C   ALA A 191      17.438   9.584  23.530  1.00 32.03           C  
ANISOU 1582  C   ALA A 191     5178   3715   3276   -162   -740   -110       C  
ATOM   1583  O   ALA A 191      18.667   9.639  23.539  1.00 33.57           O  
ANISOU 1583  O   ALA A 191     5351   3910   3496   -232   -828    -80       O  
ATOM   1584  CB  ALA A 191      17.189  11.058  25.515  1.00 32.37           C  
ANISOU 1584  CB  ALA A 191     5515   3644   3138   -185   -768   -149       C  
ATOM   1585  N   GLN A 192      16.744   9.214  22.473  1.00 30.11           N  
ANISOU 1585  N   GLN A 192     4838   3510   3093   -110   -671   -115       N  
ATOM   1586  CA  GLN A 192      17.362   8.979  21.185  1.00 28.86           C  
ANISOU 1586  CA  GLN A 192     4556   3388   3022   -128   -686    -98       C  
ATOM   1587  C   GLN A 192      16.641   9.910  20.261  1.00 28.78           C  
ANISOU 1587  C   GLN A 192     4553   3366   3017    -92   -634   -122       C  
ATOM   1588  O   GLN A 192      15.459   9.689  19.992  1.00 30.27           O  
ANISOU 1588  O   GLN A 192     4729   3568   3204    -31   -556   -134       O  
ATOM   1589  CB  GLN A 192      17.121   7.544  20.715  1.00 28.03           C  
ANISOU 1589  CB  GLN A 192     4330   3339   2979   -100   -647    -81       C  
ATOM   1590  CG  GLN A 192      17.466   6.488  21.725  1.00 27.39           C  
ANISOU 1590  CG  GLN A 192     4245   3272   2891   -117   -676    -57       C  
ATOM   1591  CD  GLN A 192      17.504   5.185  21.001  1.00 24.21           C  
ANISOU 1591  CD  GLN A 192     3715   2920   2566   -101   -647    -38       C  
ATOM   1592  OE1 GLN A 192      18.318   5.000  20.097  1.00 22.45           O  
ANISOU 1592  OE1 GLN A 192     3411   2712   2406   -125   -666    -19       O  
ATOM   1593  NE2 GLN A 192      16.608   4.276  21.359  1.00 23.00           N  
ANISOU 1593  NE2 GLN A 192     3545   2788   2407    -57   -597    -41       N  
ATOM   1594  N   ALA A 193      17.306  10.977  19.816  1.00 27.11           N  
ANISOU 1594  N   ALA A 193     4362   3127   2810   -129   -677   -124       N  
ATOM   1595  CA  ALA A 193      16.657  11.916  18.912  1.00 26.29           C  
ANISOU 1595  CA  ALA A 193     4262   3013   2715    -96   -629   -143       C  
ATOM   1596  C   ALA A 193      17.154  11.718  17.499  1.00 25.22           C  
ANISOU 1596  C   ALA A 193     4005   2918   2661   -109   -634   -126       C  
ATOM   1597  O   ALA A 193      18.320  11.376  17.282  1.00 25.57           O  
ANISOU 1597  O   ALA A 193     3993   2976   2745   -157   -693    -99       O  
ATOM   1598  CB  ALA A 193      16.894  13.340  19.361  1.00 26.29           C  
ANISOU 1598  CB  ALA A 193     4384   2947   2658   -122   -662   -160       C  
ATOM   1599  N   ALA A 194      16.261  11.895  16.535  1.00 23.81           N  
ANISOU 1599  N   ALA A 194     3784   2757   2506    -66   -571   -136       N  
ATOM   1600  CA  ALA A 194      16.617  11.758  15.133  1.00 22.55           C  
ANISOU 1600  CA  ALA A 194     3522   2633   2414    -76   -568   -123       C  
ATOM   1601  C   ALA A 194      17.257  13.041  14.614  1.00 20.69           C  
ANISOU 1601  C   ALA A 194     3308   2368   2184   -108   -606   -122       C  
ATOM   1602  O   ALA A 194      16.939  14.141  15.065  1.00 20.78           O  
ANISOU 1602  O   ALA A 194     3411   2333   2150   -104   -607   -139       O  
ATOM   1603  CB  ALA A 194      15.384  11.422  14.309  1.00 22.80           C  
ANISOU 1603  CB  ALA A 194     3502   2696   2465    -25   -493   -129       C  
ATOM   1604  N   GLY A 195      18.140  12.891  13.641  1.00 18.81           N  
ANISOU 1604  N   GLY A 195     2987   2156   2004   -136   -632   -100       N  
ATOM   1605  CA  GLY A 195      18.752  14.027  12.981  1.00 18.20           C  
ANISOU 1605  CA  GLY A 195     2911   2060   1945   -164   -665    -92       C  
ATOM   1606  C   GLY A 195      17.782  14.641  11.989  1.00 17.45           C  
ANISOU 1606  C   GLY A 195     2800   1973   1857   -127   -606   -108       C  
ATOM   1607  O   GLY A 195      16.600  14.274  11.937  1.00 17.25           O  
ANISOU 1607  O   GLY A 195     2772   1964   1819    -82   -544   -122       O  
ATOM   1608  N   THR A 196      18.293  15.530  11.144  1.00 16.59           N  
ANISOU 1608  N   THR A 196     2668   1859   1776   -148   -627    -97       N  
ATOM   1609  CA  THR A 196      17.483  16.239  10.165  1.00 16.96           C  
ANISOU 1609  CA  THR A 196     2699   1913   1834   -121   -581   -105       C  
ATOM   1610  C   THR A 196      16.846  15.288   9.210  1.00 17.50           C  
ANISOU 1610  C   THR A 196     2685   2034   1931    -95   -527   -101       C  
ATOM   1611  O   THR A 196      17.541  14.425   8.663  1.00 17.04           O  
ANISOU 1611  O   THR A 196     2559   2007   1909   -111   -536    -87       O  
ATOM   1612  CB  THR A 196      18.339  17.238   9.386  1.00 18.41           C  
ANISOU 1612  CB  THR A 196     2861   2086   2049   -155   -621    -88       C  
ATOM   1613  OG1 THR A 196      19.041  18.066  10.303  1.00 19.49           O  
ANISOU 1613  OG1 THR A 196     3079   2169   2157   -191   -684    -87       O  
ATOM   1614  CG2 THR A 196      17.516  18.113   8.465  1.00 19.24           C  
ANISOU 1614  CG2 THR A 196     2955   2193   2161   -131   -578    -92       C  
ATOM   1615  N   ASP A 197      15.517  15.412   9.024  1.00 17.89           N  
ANISOU 1615  N   ASP A 197     2743   2089   1966    -54   -470   -110       N  
ATOM   1616  CA  ASP A 197      14.850  14.565   8.047  1.00 18.28           C  
ANISOU 1616  CA  ASP A 197     2719   2186   2041    -38   -428   -102       C  
ATOM   1617  C   ASP A 197      14.922  15.240   6.692  1.00 17.83           C  
ANISOU 1617  C   ASP A 197     2617   2144   2013    -50   -423    -90       C  
ATOM   1618  O   ASP A 197      13.995  15.929   6.257  1.00 20.27           O  
ANISOU 1618  O   ASP A 197     2930   2452   2321    -30   -392    -83       O  
ATOM   1619  CB  ASP A 197      13.431  14.139   8.441  1.00 20.37           C  
ANISOU 1619  CB  ASP A 197     2997   2457   2285      4   -377   -102       C  
ATOM   1620  CG  ASP A 197      12.899  12.932   7.682  1.00 23.82           C  
ANISOU 1620  CG  ASP A 197     3365   2940   2744      8   -350    -91       C  
ATOM   1621  OD1 ASP A 197      13.654  12.353   6.864  1.00 20.44           O  
ANISOU 1621  OD1 ASP A 197     2888   2537   2342    -18   -366    -90       O  
ATOM   1622  OD2 ASP A 197      11.747  12.542   7.934  1.00 28.73           O  
ANISOU 1622  OD2 ASP A 197     3987   3570   3357     38   -313    -81       O  
ATOM   1623  N  ATHR A 198      16.073  15.084   6.036  0.50 16.35           N  
ANISOU 1623  N  ATHR A 198     2387   1970   1855    -81   -454    -81       N  
ATOM   1624  N  BTHR A 198      16.027  14.973   6.021  0.50 16.18           N  
ANISOU 1624  N  BTHR A 198     2362   1952   1834    -80   -451    -81       N  
ATOM   1625  CA ATHR A 198      16.273  15.688   4.726  0.50 15.97           C  
ANISOU 1625  CA ATHR A 198     2296   1938   1834    -94   -450    -68       C  
ATOM   1626  CA BTHR A 198      16.431  15.485   4.722  0.50 15.73           C  
ANISOU 1626  CA BTHR A 198     2258   1911   1806    -97   -452    -67       C  
ATOM   1627  C  ATHR A 198      15.435  14.991   3.669  0.50 15.27           C  
ANISOU 1627  C  ATHR A 198     2161   1890   1751    -84   -407    -63       C  
ATOM   1628  C  BTHR A 198      15.577  14.886   3.597  0.50 15.16           C  
ANISOU 1628  C  BTHR A 198     2140   1880   1741    -88   -409    -63       C  
ATOM   1629  O  ATHR A 198      14.972  13.861   3.855  0.50 15.28           O  
ANISOU 1629  O  ATHR A 198     2153   1908   1743    -73   -386    -69       O  
ATOM   1630  O  BTHR A 198      15.248  13.702   3.663  0.50 15.19           O  
ANISOU 1630  O  BTHR A 198     2128   1903   1740    -81   -390    -68       O  
ATOM   1631  CB ATHR A 198      17.753  15.778   4.371  0.50 17.51           C  
ANISOU 1631  CB ATHR A 198     2460   2133   2061   -126   -489    -51       C  
ATOM   1632  CB BTHR A 198      17.918  15.133   4.570  0.50 16.74           C  
ANISOU 1632  CB BTHR A 198     2355   2043   1965   -126   -488    -51       C  
ATOM   1633  OG1ATHR A 198      18.310  14.471   4.399  0.50 18.42           O  
ANISOU 1633  OG1ATHR A 198     2540   2270   2191   -130   -483    -46       O  
ATOM   1634  OG1BTHR A 198      18.659  15.683   5.672  0.50 17.41           O  
ANISOU 1634  OG1BTHR A 198     2486   2088   2041   -145   -540    -48       O  
ATOM   1635  CG2ATHR A 198      18.524  16.703   5.296  0.50 17.78           C  
ANISOU 1635  CG2ATHR A 198     2543   2123   2089   -148   -545    -46       C  
ATOM   1636  CG2BTHR A 198      18.499  15.622   3.285  0.50 17.17           C  
ANISOU 1636  CG2BTHR A 198     2360   2113   2051   -142   -487    -32       C  
ATOM   1637  N   THR A 199      15.201  15.692   2.578  1.00 14.19           N  
ANISOU 1637  N   THR A 199     1998   1767   1627    -91   -398    -51       N  
ATOM   1638  CA  THR A 199      14.404  15.175   1.472  1.00 13.47           C  
ANISOU 1638  CA  THR A 199     1870   1712   1538    -93   -367    -41       C  
ATOM   1639  C   THR A 199      15.302  14.448   0.475  1.00 12.86           C  
ANISOU 1639  C   THR A 199     1754   1658   1475   -115   -366    -39       C  
ATOM   1640  O   THR A 199      16.404  14.913   0.194  1.00 13.34           O  
ANISOU 1640  O   THR A 199     1801   1711   1555   -128   -384    -31       O  
ATOM   1641  CB  THR A 199      13.546  16.279   0.859  1.00 14.60           C  
ANISOU 1641  CB  THR A 199     2008   1857   1684    -89   -355    -22       C  
ATOM   1642  OG1 THR A 199      12.711  16.839   1.874  1.00 15.22           O  
ANISOU 1642  OG1 THR A 199     2126   1907   1749    -59   -342    -21       O  
ATOM   1643  CG2 THR A 199      12.667  15.765  -0.281  1.00 15.03           C  
ANISOU 1643  CG2 THR A 199     2025   1949   1736   -100   -333     -4       C  
ATOM   1644  N   ILE A 200      14.861  13.264  -0.011  1.00 12.06           N  
ANISOU 1644  N   ILE A 200     1639   1580   1363   -118   -342    -43       N  
ATOM   1645  CA  ILE A 200      15.633  12.442  -0.950  1.00 12.31           C  
ANISOU 1645  CA  ILE A 200     1650   1627   1402   -134   -327    -44       C  
ATOM   1646  C   ILE A 200      15.432  12.991  -2.363  1.00 11.85           C  
ANISOU 1646  C   ILE A 200     1575   1587   1338   -153   -318    -30       C  
ATOM   1647  O   ILE A 200      14.510  12.616  -3.089  1.00 11.58           O  
ANISOU 1647  O   ILE A 200     1543   1573   1284   -166   -304    -27       O  
ATOM   1648  CB  ILE A 200      15.218  10.951  -0.852  1.00 12.52           C  
ANISOU 1648  CB  ILE A 200     1682   1662   1412   -132   -306    -57       C  
ATOM   1649  CG1 ILE A 200      15.204  10.474   0.626  1.00 12.89           C  
ANISOU 1649  CG1 ILE A 200     1744   1693   1460   -112   -317    -67       C  
ATOM   1650  CG2 ILE A 200      16.162  10.099  -1.689  1.00 12.93           C  
ANISOU 1650  CG2 ILE A 200     1724   1717   1471   -142   -282    -59       C  
ATOM   1651  CD1 ILE A 200      14.183   9.365   0.910  1.00 14.24           C  
ANISOU 1651  CD1 ILE A 200     1923   1873   1614   -105   -302    -73       C  
ATOM   1652  N   THR A 201      16.317  13.911  -2.732  1.00 11.75           N  
ANISOU 1652  N   THR A 201     1548   1570   1348   -158   -329    -18       N  
ATOM   1653  CA  THR A 201      16.264  14.631  -3.995  1.00 12.03           C  
ANISOU 1653  CA  THR A 201     1566   1622   1383   -175   -324     -1       C  
ATOM   1654  C   THR A 201      16.083  13.743  -5.217  1.00 12.46           C  
ANISOU 1654  C   THR A 201     1622   1698   1412   -193   -294     -2       C  
ATOM   1655  O   THR A 201      15.218  14.024  -6.052  1.00 13.25           O  
ANISOU 1655  O   THR A 201     1723   1817   1493   -212   -293      8       O  
ATOM   1656  CB  THR A 201      17.526  15.476  -4.150  1.00 13.15           C  
ANISOU 1656  CB  THR A 201     1688   1753   1557   -177   -339     16       C  
ATOM   1657  OG1 THR A 201      17.749  16.207  -2.951  1.00 13.77           O  
ANISOU 1657  OG1 THR A 201     1778   1802   1650   -168   -373     15       O  
ATOM   1658  CG2 THR A 201      17.479  16.386  -5.360  1.00 14.00           C  
ANISOU 1658  CG2 THR A 201     1775   1876   1668   -192   -336     37       C  
ATOM   1659  N   VAL A 202      16.888  12.675  -5.341  1.00 11.54           N  
ANISOU 1659  N   VAL A 202     1512   1577   1297   -189   -270    -12       N  
ATOM   1660  CA  VAL A 202      16.798  11.804  -6.519  1.00 12.15           C  
ANISOU 1660  CA  VAL A 202     1608   1665   1342   -206   -235    -18       C  
ATOM   1661  C   VAL A 202      15.402  11.170  -6.634  1.00 12.21           C  
ANISOU 1661  C   VAL A 202     1642   1685   1313   -225   -241    -28       C  
ATOM   1662  O   VAL A 202      14.899  10.999  -7.736  1.00 12.15           O  
ANISOU 1662  O   VAL A 202     1653   1690   1273   -253   -233    -23       O  
ATOM   1663  CB  VAL A 202      17.929  10.751  -6.579  1.00 13.19           C  
ANISOU 1663  CB  VAL A 202     1747   1781   1485   -192   -197    -24       C  
ATOM   1664  CG1 VAL A 202      17.770   9.698  -5.480  1.00 14.16           C  
ANISOU 1664  CG1 VAL A 202     1879   1889   1611   -177   -196    -42       C  
ATOM   1665  CG2 VAL A 202      18.012  10.102  -7.959  1.00 14.05           C  
ANISOU 1665  CG2 VAL A 202     1887   1892   1558   -207   -153    -28       C  
ATOM   1666  N   ASN A 203      14.756  10.889  -5.487  1.00 12.28           N  
ANISOU 1666  N   ASN A 203     1651   1688   1328   -211   -257    -35       N  
ATOM   1667  CA  ASN A 203      13.419  10.315  -5.495  1.00 12.14           C  
ANISOU 1667  CA  ASN A 203     1648   1681   1284   -228   -266    -32       C  
ATOM   1668  C   ASN A 203      12.385  11.343  -5.906  1.00 12.09           C  
ANISOU 1668  C   ASN A 203     1626   1693   1276   -244   -287     -2       C  
ATOM   1669  O   ASN A 203      11.470  11.014  -6.664  1.00 12.27           O  
ANISOU 1669  O   ASN A 203     1657   1731   1272   -277   -295     15       O  
ATOM   1670  CB  ASN A 203      13.086   9.747  -4.116  1.00 12.23           C  
ANISOU 1670  CB  ASN A 203     1660   1681   1308   -203   -272    -42       C  
ATOM   1671  CG  ASN A 203      13.839   8.482  -3.781  1.00 12.94           C  
ANISOU 1671  CG  ASN A 203     1764   1755   1397   -193   -251    -65       C  
ATOM   1672  OD1 ASN A 203      14.704   8.031  -4.528  1.00 12.49           O  
ANISOU 1672  OD1 ASN A 203     1717   1691   1335   -200   -225    -74       O  
ATOM   1673  ND2 ASN A 203      13.543   7.903  -2.603  1.00 12.93           N  
ANISOU 1673  ND2 ASN A 203     1763   1746   1404   -173   -256    -72       N  
ATOM   1674  N   VAL A 204      12.549  12.612  -5.486  1.00 11.53           N  
ANISOU 1674  N   VAL A 204     1532   1617   1232   -225   -298     10       N  
ATOM   1675  CA  VAL A 204      11.614  13.665  -5.908  1.00 11.74           C  
ANISOU 1675  CA  VAL A 204     1539   1657   1264   -236   -311     45       C  
ATOM   1676  C   VAL A 204      11.696  13.853  -7.408  1.00 12.06           C  
ANISOU 1676  C   VAL A 204     1578   1719   1285   -274   -312     60       C  
ATOM   1677  O   VAL A 204      10.667  13.959  -8.069  1.00 12.65           O  
ANISOU 1677  O   VAL A 204     1647   1814   1347   -304   -325     92       O  
ATOM   1678  CB  VAL A 204      11.899  14.998  -5.193  1.00 12.37           C  
ANISOU 1678  CB  VAL A 204     1605   1719   1374   -207   -318     51       C  
ATOM   1679  CG1 VAL A 204      10.971  16.096  -5.711  1.00 12.86           C  
ANISOU 1679  CG1 VAL A 204     1644   1793   1447   -216   -324     92       C  
ATOM   1680  CG2 VAL A 204      11.731  14.836  -3.687  1.00 11.91           C  
ANISOU 1680  CG2 VAL A 204     1563   1636   1325   -172   -317     37       C  
ATOM   1681  N   LEU A 205      12.920  13.831  -7.961  1.00 11.62           N  
ANISOU 1681  N   LEU A 205     1529   1659   1227   -275   -297     42       N  
ATOM   1682  CA  LEU A 205      13.080  13.980  -9.409  1.00 11.61           C  
ANISOU 1682  CA  LEU A 205     1534   1676   1201   -309   -291     55       C  
ATOM   1683  C   LEU A 205      12.439  12.817 -10.129  1.00 12.03           C  
ANISOU 1683  C   LEU A 205     1627   1739   1206   -346   -288     51       C  
ATOM   1684  O   LEU A 205      11.742  13.024 -11.120  1.00 11.50           O  
ANISOU 1684  O   LEU A 205     1567   1691   1112   -388   -304     76       O  
ATOM   1685  CB  LEU A 205      14.560  14.080  -9.785  1.00 11.82           C  
ANISOU 1685  CB  LEU A 205     1561   1693   1238   -295   -266     43       C  
ATOM   1686  CG  LEU A 205      15.223  15.375  -9.349  1.00 12.51           C  
ANISOU 1686  CG  LEU A 205     1609   1772   1370   -272   -280     57       C  
ATOM   1687  CD1 LEU A 205      16.733  15.246  -9.360  1.00 13.36           C  
ANISOU 1687  CD1 LEU A 205     1710   1866   1501   -253   -259     52       C  
ATOM   1688  CD2 LEU A 205      14.733  16.542 -10.186  1.00 13.75           C  
ANISOU 1688  CD2 LEU A 205     1744   1949   1530   -293   -295     89       C  
ATOM   1689  N   ALA A 206      12.630  11.587  -9.620  1.00 12.01           N  
ANISOU 1689  N   ALA A 206     1654   1719   1192   -337   -273     21       N  
ATOM   1690  CA  ALA A 206      12.019  10.411 -10.254  1.00 12.58           C  
ANISOU 1690  CA  ALA A 206     1774   1791   1214   -376   -273     15       C  
ATOM   1691  C   ALA A 206      10.483  10.546 -10.260  1.00 13.06           C  
ANISOU 1691  C   ALA A 206     1821   1871   1269   -409   -315     53       C  
ATOM   1692  O   ALA A 206       9.841  10.284 -11.270  1.00 12.97           O  
ANISOU 1692  O   ALA A 206     1838   1872   1217   -462   -334     73       O  
ATOM   1693  CB  ALA A 206      12.426   9.154  -9.509  1.00 13.02           C  
ANISOU 1693  CB  ALA A 206     1854   1822   1269   -354   -251    -19       C  
ATOM   1694  N   TRP A 207       9.924  11.046  -9.151  1.00 12.31           N  
ANISOU 1694  N   TRP A 207     1684   1778   1215   -378   -327     70       N  
ATOM   1695  CA  TRP A 207       8.484  11.237  -9.044  1.00 12.72           C  
ANISOU 1695  CA  TRP A 207     1712   1846   1275   -399   -358    120       C  
ATOM   1696  C   TRP A 207       7.993  12.353  -9.993  1.00 12.88           C  
ANISOU 1696  C   TRP A 207     1705   1890   1298   -430   -378    168       C  
ATOM   1697  O   TRP A 207       6.919  12.226 -10.565  1.00 13.64           O  
ANISOU 1697  O   TRP A 207     1798   2004   1382   -476   -409    215       O  
ATOM   1698  CB  TRP A 207       8.134  11.468  -7.574  1.00 13.10           C  
ANISOU 1698  CB  TRP A 207     1730   1883   1366   -347   -352    125       C  
ATOM   1699  CG  TRP A 207       6.764  11.990  -7.302  1.00 13.61           C  
ANISOU 1699  CG  TRP A 207     1756   1960   1455   -349   -368    187       C  
ATOM   1700  CD1 TRP A 207       5.613  11.271  -7.141  1.00 14.89           C  
ANISOU 1700  CD1 TRP A 207     1911   2131   1617   -369   -387    226       C  
ATOM   1701  CD2 TRP A 207       6.432  13.349  -7.037  1.00 13.53           C  
ANISOU 1701  CD2 TRP A 207     1708   1951   1482   -323   -362    222       C  
ATOM   1702  NE1 TRP A 207       4.581  12.114  -6.796  1.00 15.38           N  
ANISOU 1702  NE1 TRP A 207     1926   2200   1718   -353   -388    290       N  
ATOM   1703  CE2 TRP A 207       5.061  13.396  -6.721  1.00 14.69           C  
ANISOU 1703  CE2 TRP A 207     1823   2106   1652   -322   -369    286       C  
ATOM   1704  CE3 TRP A 207       7.177  14.530  -6.990  1.00 14.59           C  
ANISOU 1704  CE3 TRP A 207     1833   2076   1635   -297   -349    208       C  
ATOM   1705  CZ2 TRP A 207       4.421  14.585  -6.382  1.00 15.53           C  
ANISOU 1705  CZ2 TRP A 207     1891   2210   1800   -292   -355    335       C  
ATOM   1706  CZ3 TRP A 207       6.536  15.709  -6.670  1.00 15.61           C  
ANISOU 1706  CZ3 TRP A 207     1929   2200   1800   -272   -341    251       C  
ATOM   1707  CH2 TRP A 207       5.175  15.729  -6.384  1.00 15.54           C  
ANISOU 1707  CH2 TRP A 207     1892   2198   1814   -268   -340    314       C  
ATOM   1708  N   LEU A 208       8.814  13.381 -10.235  1.00 12.37           N  
ANISOU 1708  N   LEU A 208     1624   1825   1250   -411   -364    160       N  
ATOM   1709  CA  LEU A 208       8.452  14.412 -11.218  1.00 12.13           C  
ANISOU 1709  CA  LEU A 208     1569   1818   1222   -441   -381    204       C  
ATOM   1710  C   LEU A 208       8.433  13.799 -12.619  1.00 12.89           C  
ANISOU 1710  C   LEU A 208     1709   1928   1260   -504   -394    206       C  
ATOM   1711  O   LEU A 208       7.538  14.110 -13.409  1.00 13.49           O  
ANISOU 1711  O   LEU A 208     1774   2027   1324   -554   -427    258       O  
ATOM   1712  CB  LEU A 208       9.446  15.566 -11.142  1.00 11.68           C  
ANISOU 1712  CB  LEU A 208     1490   1754   1195   -407   -363    191       C  
ATOM   1713  CG  LEU A 208       9.330  16.445  -9.891  1.00 13.13           C  
ANISOU 1713  CG  LEU A 208     1641   1919   1430   -354   -357    196       C  
ATOM   1714  CD1 LEU A 208      10.419  17.506  -9.884  1.00 13.35           C  
ANISOU 1714  CD1 LEU A 208     1654   1935   1482   -330   -348    182       C  
ATOM   1715  CD2 LEU A 208       7.956  17.130  -9.824  1.00 13.49           C  
ANISOU 1715  CD2 LEU A 208     1647   1975   1502   -360   -369    260       C  
ATOM   1716  N   TYR A 209       9.367  12.870 -12.916  1.00 12.85           N  
ANISOU 1716  N   TYR A 209     1759   1907   1216   -505   -369    155       N  
ATOM   1717  CA  TYR A 209       9.341  12.143 -14.193  1.00 13.30           C  
ANISOU 1717  CA  TYR A 209     1880   1968   1206   -564   -375    150       C  
ATOM   1718  C   TYR A 209       8.069  11.310 -14.283  1.00 14.51           C  
ANISOU 1718  C   TYR A 209     2056   2126   1332   -617   -417    179       C  
ATOM   1719  O   TYR A 209       7.423  11.315 -15.316  1.00 15.06           O  
ANISOU 1719  O   TYR A 209     2150   2212   1362   -682   -452    215       O  
ATOM   1720  CB  TYR A 209      10.556  11.234 -14.364  1.00 12.99           C  
ANISOU 1720  CB  TYR A 209     1901   1901   1135   -545   -327     93       C  
ATOM   1721  CG  TYR A 209      11.758  11.992 -14.871  1.00 13.05           C  
ANISOU 1721  CG  TYR A 209     1898   1909   1153   -518   -291     83       C  
ATOM   1722  CD1 TYR A 209      11.814  12.446 -16.178  1.00 13.88           C  
ANISOU 1722  CD1 TYR A 209     2026   2029   1217   -557   -292    102       C  
ATOM   1723  CD2 TYR A 209      12.843  12.240 -14.048  1.00 13.62           C  
ANISOU 1723  CD2 TYR A 209     1937   1964   1272   -457   -258     60       C  
ATOM   1724  CE1 TYR A 209      12.907  13.155 -16.649  1.00 14.59           C  
ANISOU 1724  CE1 TYR A 209     2103   2121   1321   -531   -257    100       C  
ATOM   1725  CE2 TYR A 209      13.943  12.953 -14.506  1.00 14.55           C  
ANISOU 1725  CE2 TYR A 209     2039   2083   1406   -434   -229     63       C  
ATOM   1726  CZ  TYR A 209      13.975  13.397 -15.814  1.00 14.96           C  
ANISOU 1726  CZ  TYR A 209     2111   2151   1421   -469   -226     82       C  
ATOM   1727  OH  TYR A 209      15.049  14.115 -16.279  1.00 16.11           O  
ANISOU 1727  OH  TYR A 209     2235   2299   1587   -445   -196     92       O  
ATOM   1728  N   ALA A 210       7.680  10.629 -13.183  1.00 14.89           N  
ANISOU 1728  N   ALA A 210     2094   2161   1404   -591   -418    170       N  
ATOM   1729  CA  ALA A 210       6.429   9.851 -13.171  1.00 15.35           C  
ANISOU 1729  CA  ALA A 210     2163   2224   1447   -640   -463    208       C  
ATOM   1730  C   ALA A 210       5.231  10.755 -13.445  1.00 16.18           C  
ANISOU 1730  C   ALA A 210     2209   2359   1579   -673   -507    291       C  
ATOM   1731  O   ALA A 210       4.309  10.368 -14.163  1.00 16.64           O  
ANISOU 1731  O   ALA A 210     2286   2430   1608   -745   -557    340       O  
ATOM   1732  CB  ALA A 210       6.246   9.164 -11.820  1.00 15.41           C  
ANISOU 1732  CB  ALA A 210     2153   2215   1488   -595   -452    192       C  
ATOM   1733  N   ALA A 211       5.247  11.971 -12.900  1.00 15.83           N  
ANISOU 1733  N   ALA A 211     2098   2324   1593   -624   -491    314       N  
ATOM   1734  CA  ALA A 211       4.178  12.927 -13.105  1.00 15.93           C  
ANISOU 1734  CA  ALA A 211     2048   2362   1643   -643   -520    398       C  
ATOM   1735  C   ALA A 211       4.077  13.306 -14.578  1.00 16.27           C  
ANISOU 1735  C   ALA A 211     2108   2428   1647   -714   -553    430       C  
ATOM   1736  O   ALA A 211       2.978  13.279 -15.138  1.00 17.39           O  
ANISOU 1736  O   ALA A 211     2234   2590   1784   -777   -603    504       O  
ATOM   1737  CB  ALA A 211       4.407  14.152 -12.240  1.00 16.23           C  
ANISOU 1737  CB  ALA A 211     2027   2395   1745   -571   -485    402       C  
ATOM   1738  N   VAL A 212       5.210  13.588 -15.237  1.00 15.64           N  
ANISOU 1738  N   VAL A 212     2063   2345   1535   -709   -527    380       N  
ATOM   1739  CA  VAL A 212       5.187  13.927 -16.663  1.00 16.48           C  
ANISOU 1739  CA  VAL A 212     2194   2472   1595   -775   -554    407       C  
ATOM   1740  C   VAL A 212       4.654  12.777 -17.487  1.00 18.29           C  
ANISOU 1740  C   VAL A 212     2499   2699   1751   -858   -596    415       C  
ATOM   1741  O   VAL A 212       3.796  12.996 -18.351  1.00 19.31           O  
ANISOU 1741  O   VAL A 212     2625   2852   1860   -933   -650    483       O  
ATOM   1742  CB  VAL A 212       6.574  14.389 -17.150  1.00 16.59           C  
ANISOU 1742  CB  VAL A 212     2233   2480   1591   -745   -509    353       C  
ATOM   1743  CG1 VAL A 212       6.583  14.581 -18.668  1.00 16.85           C  
ANISOU 1743  CG1 VAL A 212     2307   2533   1563   -815   -532    376       C  
ATOM   1744  CG2 VAL A 212       6.969  15.674 -16.451  1.00 17.06           C  
ANISOU 1744  CG2 VAL A 212     2217   2542   1723   -679   -483    360       C  
ATOM   1745  N   ILE A 213       5.112  11.552 -17.202  1.00 19.03           N  
ANISOU 1745  N   ILE A 213     2661   2762   1805   -851   -576    352       N  
ATOM   1746  CA  ILE A 213       4.654  10.357 -17.930  1.00 20.91           C  
ANISOU 1746  CA  ILE A 213     2989   2988   1967   -932   -615    351       C  
ATOM   1747  C   ILE A 213       3.142  10.195 -17.791  1.00 23.56           C  
ANISOU 1747  C   ILE A 213     3284   3341   2324   -989   -688    438       C  
ATOM   1748  O   ILE A 213       2.457   9.941 -18.777  1.00 24.76           O  
ANISOU 1748  O   ILE A 213     3478   3505   2427  -1081   -749    486       O  
ATOM   1749  CB  ILE A 213       5.416   9.109 -17.418  1.00 21.25           C  
ANISOU 1749  CB  ILE A 213     3102   2991   1982   -898   -572    270       C  
ATOM   1750  CG1 ILE A 213       6.904   9.189 -17.803  1.00 21.73           C  
ANISOU 1750  CG1 ILE A 213     3208   3032   2015   -853   -501    200       C  
ATOM   1751  CG2 ILE A 213       4.783   7.803 -17.918  1.00 21.99           C  
ANISOU 1751  CG2 ILE A 213     3287   3063   2006   -978   -616    272       C  
ATOM   1752  CD1 ILE A 213       7.788   8.246 -17.083  1.00 22.87           C  
ANISOU 1752  CD1 ILE A 213     3387   3140   2162   -797   -445    132       C  
ATOM   1753  N   ASN A 214       2.620  10.439 -16.588  1.00 24.22           N  
ANISOU 1753  N   ASN A 214     3286   3431   2488   -934   -681    468       N  
ATOM   1754  CA  ASN A 214       1.204  10.282 -16.300  1.00 26.05           C  
ANISOU 1754  CA  ASN A 214     3465   3677   2756   -973   -738    560       C  
ATOM   1755  C   ASN A 214       0.343  11.544 -16.522  1.00 27.69           C  
ANISOU 1755  C   ASN A 214     3578   3920   3022   -985   -764    662       C  
ATOM   1756  O   ASN A 214      -0.799  11.581 -16.055  1.00 29.91           O  
ANISOU 1756  O   ASN A 214     3792   4213   3358   -992   -794    750       O  
ATOM   1757  CB  ASN A 214       1.016   9.716 -14.899  1.00 27.31           C  
ANISOU 1757  CB  ASN A 214     3592   3819   2964   -909   -712    545       C  
ATOM   1758  CG  ASN A 214       1.479   8.279 -14.822  1.00 30.24           C  
ANISOU 1758  CG  ASN A 214     4054   4159   3279   -923   -708    474       C  
ATOM   1759  OD1 ASN A 214       0.744   7.346 -15.163  1.00 32.47           O  
ANISOU 1759  OD1 ASN A 214     4375   4434   3529   -994   -763    505       O  
ATOM   1760  ND2 ASN A 214       2.714   8.047 -14.430  1.00 29.78           N  
ANISOU 1760  ND2 ASN A 214     4032   4076   3206   -863   -645    381       N  
ATOM   1761  N   GLY A 215       0.848  12.529 -17.260  1.00 26.51           N  
ANISOU 1761  N   GLY A 215     3423   3787   2864   -988   -753    660       N  
ATOM   1762  CA  GLY A 215       0.065  13.709 -17.623  1.00 26.05           C  
ANISOU 1762  CA  GLY A 215     3281   3761   2856  -1007   -778    759       C  
ATOM   1763  C   GLY A 215       0.186  15.021 -16.870  1.00 24.55           C  
ANISOU 1763  C   GLY A 215     3001   3575   2753   -920   -726    778       C  
ATOM   1764  O   GLY A 215      -0.239  16.059 -17.380  1.00 25.20           O  
ANISOU 1764  O   GLY A 215     3024   3681   2871   -937   -741    852       O  
ATOM   1765  N  AASP A 216       0.744  14.999 -15.654  0.50 23.04           N  
ANISOU 1765  N  AASP A 216     2803   3359   2594   -829   -667    714       N  
ATOM   1766  N  BASP A 216       0.748  14.992 -15.660  0.50 23.39           N  
ANISOU 1766  N  BASP A 216     2847   3402   2637   -830   -668    714       N  
ATOM   1767  CA AASP A 216       0.891  16.222 -14.868  0.50 22.25           C  
ANISOU 1767  CA AASP A 216     2635   3253   2567   -747   -618    725       C  
ATOM   1768  CA BASP A 216       0.909  16.203 -14.862  0.50 22.94           C  
ANISOU 1768  CA BASP A 216     2724   3339   2653   -747   -617    722       C  
ATOM   1769  C  AASP A 216       2.182  16.909 -15.280  0.50 22.70           C  
ANISOU 1769  C  AASP A 216     2716   3305   2605   -722   -585    655       C  
ATOM   1770  C  BASP A 216       2.192  16.893 -15.307  0.50 23.02           C  
ANISOU 1770  C  BASP A 216     2758   3346   2642   -724   -587    654       C  
ATOM   1771  O  AASP A 216       3.265  16.409 -14.988  0.50 23.46           O  
ANISOU 1771  O  AASP A 216     2864   3380   2669   -689   -555    565       O  
ATOM   1772  O  BASP A 216       3.280  16.379 -15.060  0.50 23.77           O  
ANISOU 1772  O  BASP A 216     2909   3421   2703   -696   -558    564       O  
ATOM   1773  CB AASP A 216       0.863  15.910 -13.369  0.50 22.37           C  
ANISOU 1773  CB AASP A 216     2639   3240   2621   -669   -575    695       C  
ATOM   1774  CB BASP A 216       0.959  15.849 -13.368  0.50 24.09           C  
ANISOU 1774  CB BASP A 216     2863   3457   2833   -669   -574    686       C  
ATOM   1775  CG AASP A 216      -0.442  15.298 -12.907  0.50 24.19           C  
ANISOU 1775  CG AASP A 216     2835   3475   2882   -685   -600    774       C  
ATOM   1776  CG BASP A 216      -0.170  16.456 -12.563  0.50 27.89           C  
ANISOU 1776  CG BASP A 216     3267   3938   3393   -629   -559    775       C  
ATOM   1777  OD1AASP A 216      -1.477  15.540 -13.561  0.50 24.19           O  
ANISOU 1777  OD1AASP A 216     2790   3500   2902   -743   -644    877       O  
ATOM   1778  OD1BASP A 216      -0.595  17.580 -12.895  0.50 28.66           O  
ANISOU 1778  OD1BASP A 216     3309   4047   3535   -626   -554    842       O  
ATOM   1779  OD2AASP A 216      -0.430  14.579 -11.889  0.50 25.07           O  
ANISOU 1779  OD2AASP A 216     2960   3567   3001   -642   -577    741       O  
ATOM   1780  OD2BASP A 216      -0.618  15.812 -11.589  0.50 29.52           O  
ANISOU 1780  OD2BASP A 216     3469   4129   3618   -597   -546    781       O  
ATOM   1781  N   ARG A 217       2.073  18.016 -16.019  1.00 21.99           N  
ANISOU 1781  N   ARG A 217     2585   3236   2534   -740   -594    705       N  
ATOM   1782  CA  ARG A 217       3.233  18.713 -16.564  1.00 20.81           C  
ANISOU 1782  CA  ARG A 217     2453   3087   2367   -726   -572    655       C  
ATOM   1783  C   ARG A 217       3.263  20.218 -16.299  1.00 19.92           C  
ANISOU 1783  C   ARG A 217     2271   2973   2323   -678   -545    689       C  
ATOM   1784  O   ARG A 217       4.105  20.898 -16.881  1.00 19.51           O  
ANISOU 1784  O   ARG A 217     2224   2927   2263   -675   -535    665       O  
ATOM   1785  CB  ARG A 217       3.252  18.535 -18.107  0.50 21.37           C  
ANISOU 1785  CB  ARG A 217     2559   3186   2373   -814   -615    677       C  
ATOM   1786  CG  ARG A 217       2.978  17.127 -18.645  0.50 23.57           C  
ANISOU 1786  CG  ARG A 217     2916   3465   2575   -885   -654    663       C  
ATOM   1787  CD  ARG A 217       2.523  17.152 -20.100  0.50 25.14           C  
ANISOU 1787  CD  ARG A 217     3143   3693   2718   -984   -710    717       C  
ATOM   1788  NE  ARG A 217       3.525  17.746 -20.981  0.50 25.70           N  
ANISOU 1788  NE  ARG A 217     3240   3770   2753   -983   -686    679       N  
ATOM   1789  CZ  ARG A 217       4.427  17.041 -21.650  0.50 25.29           C  
ANISOU 1789  CZ  ARG A 217     3284   3705   2620  -1002   -669    609       C  
ATOM   1790  NH1 ARG A 217       5.318  17.652 -22.418  0.50 24.48           N  
ANISOU 1790  NH1 ARG A 217     3197   3610   2493   -996   -642    587       N  
ATOM   1791  NH2 ARG A 217       4.448  15.719 -21.555  0.50 23.66           N  
ANISOU 1791  NH2 ARG A 217     3159   3476   2355  -1029   -676    567       N  
ATOM   1792  N   TRP A 218       2.347  20.759 -15.483  1.00 19.50           N  
ANISOU 1792  N   TRP A 218     2159   2912   2339   -640   -532    750       N  
ATOM   1793  CA  TRP A 218       2.290  22.214 -15.276  1.00 19.27           C  
ANISOU 1793  CA  TRP A 218     2071   2875   2374   -597   -503    788       C  
ATOM   1794  C   TRP A 218       3.589  22.829 -14.740  1.00 19.18           C  
ANISOU 1794  C   TRP A 218     2084   2834   2369   -535   -463    704       C  
ATOM   1795  O   TRP A 218       3.833  24.006 -14.958  1.00 19.69           O  
ANISOU 1795  O   TRP A 218     2116   2896   2469   -518   -450    724       O  
ATOM   1796  CB  TRP A 218       1.102  22.617 -14.384  1.00 19.08           C  
ANISOU 1796  CB  TRP A 218     1990   2837   2422   -556   -480    866       C  
ATOM   1797  CG  TRP A 218       1.172  22.070 -12.987  1.00 18.92           C  
ANISOU 1797  CG  TRP A 218     1998   2781   2409   -491   -442    816       C  
ATOM   1798  CD1 TRP A 218       0.547  20.956 -12.513  1.00 19.63           C  
ANISOU 1798  CD1 TRP A 218     2098   2871   2488   -499   -453    828       C  
ATOM   1799  CD2 TRP A 218       1.858  22.655 -11.864  1.00 19.21           C  
ANISOU 1799  CD2 TRP A 218     2055   2774   2468   -410   -390    754       C  
ATOM   1800  NE1 TRP A 218       0.866  20.766 -11.187  1.00 19.83           N  
ANISOU 1800  NE1 TRP A 218     2152   2860   2523   -426   -408    770       N  
ATOM   1801  CE2 TRP A 218       1.651  21.805 -10.761  1.00 19.68           C  
ANISOU 1801  CE2 TRP A 218     2142   2813   2523   -373   -370    726       C  
ATOM   1802  CE3 TRP A 218       2.647  23.803 -11.692  1.00 19.71           C  
ANISOU 1802  CE3 TRP A 218     2123   2814   2553   -370   -363    720       C  
ATOM   1803  CZ2 TRP A 218       2.230  22.048  -9.514  1.00 19.83           C  
ANISOU 1803  CZ2 TRP A 218     2196   2788   2549   -302   -327    663       C  
ATOM   1804  CZ3 TRP A 218       3.229  24.034 -10.460  1.00 20.19           C  
ANISOU 1804  CZ3 TRP A 218     2220   2828   2621   -302   -323    658       C  
ATOM   1805  CH2 TRP A 218       3.000  23.174  -9.383  1.00 20.04           C  
ANISOU 1805  CH2 TRP A 218     2233   2790   2592   -270   -306    631       C  
ATOM   1806  N   PHE A 219       4.383  22.040 -14.003  1.00 18.30           N  
ANISOU 1806  N   PHE A 219     2026   2700   2228   -503   -446    619       N  
ATOM   1807  CA  PHE A 219       5.624  22.483 -13.356  1.00 17.79           C  
ANISOU 1807  CA  PHE A 219     1985   2603   2170   -448   -415    545       C  
ATOM   1808  C   PHE A 219       6.842  22.530 -14.276  1.00 18.51           C  
ANISOU 1808  C   PHE A 219     2102   2707   2225   -472   -423    502       C  
ATOM   1809  O   PHE A 219       7.911  22.994 -13.861  1.00 18.69           O  
ANISOU 1809  O   PHE A 219     2134   2706   2260   -434   -405    455       O  
ATOM   1810  CB  PHE A 219       5.920  21.590 -12.136  1.00 16.65           C  
ANISOU 1810  CB  PHE A 219     1881   2429   2014   -407   -396    485       C  
ATOM   1811  CG  PHE A 219       5.997  20.133 -12.506  1.00 15.65           C  
ANISOU 1811  CG  PHE A 219     1796   2318   1831   -447   -415    455       C  
ATOM   1812  CD1 PHE A 219       7.163  19.591 -13.018  1.00 15.83           C  
ANISOU 1812  CD1 PHE A 219     1862   2342   1810   -461   -414    395       C  
ATOM   1813  CD2 PHE A 219       4.885  19.316 -12.400  1.00 15.39           C  
ANISOU 1813  CD2 PHE A 219     1759   2296   1791   -472   -432    495       C  
ATOM   1814  CE1 PHE A 219       7.210  18.266 -13.417  1.00 15.82           C  
ANISOU 1814  CE1 PHE A 219     1908   2348   1755   -497   -425    369       C  
ATOM   1815  CE2 PHE A 219       4.956  17.985 -12.749  1.00 15.80           C  
ANISOU 1815  CE2 PHE A 219     1857   2356   1790   -512   -452    467       C  
ATOM   1816  CZ  PHE A 219       6.103  17.475 -13.293  1.00 15.51           C  
ANISOU 1816  CZ  PHE A 219     1871   2316   1705   -526   -447    402       C  
ATOM   1817  N   LEU A 220       6.703  22.044 -15.520  1.00 18.09           N  
ANISOU 1817  N   LEU A 220     2060   2687   2125   -536   -450    522       N  
ATOM   1818  CA  LEU A 220       7.800  22.117 -16.472  1.00 19.03           C  
ANISOU 1818  CA  LEU A 220     2204   2817   2208   -556   -448    490       C  
ATOM   1819  C   LEU A 220       7.971  23.571 -16.859  1.00 20.12           C  
ANISOU 1819  C   LEU A 220     2291   2963   2392   -547   -447    528       C  
ATOM   1820  O   LEU A 220       6.988  24.309 -16.991  1.00 20.85           O  
ANISOU 1820  O   LEU A 220     2333   3066   2522   -558   -460    597       O  
ATOM   1821  CB  LEU A 220       7.525  21.266 -17.709  1.00 19.05           C  
ANISOU 1821  CB  LEU A 220     2247   2850   2142   -629   -475    503       C  
ATOM   1822  CG  LEU A 220       7.424  19.768 -17.467  1.00 19.56           C  
ANISOU 1822  CG  LEU A 220     2373   2904   2156   -645   -477    463       C  
ATOM   1823  CD1 LEU A 220       7.122  19.044 -18.764  1.00 19.47           C  
ANISOU 1823  CD1 LEU A 220     2414   2915   2069   -725   -507    479       C  
ATOM   1824  CD2 LEU A 220       8.694  19.212 -16.777  1.00 20.00           C  
ANISOU 1824  CD2 LEU A 220     2467   2928   2205   -591   -436    381       C  
ATOM   1825  N   ASN A 221       9.214  23.996 -16.965  1.00 20.10           N  
ANISOU 1825  N   ASN A 221     2295   2950   2392   -523   -430    490       N  
ATOM   1826  CA  ASN A 221       9.510  25.383 -17.252  1.00 20.10           C  
ANISOU 1826  CA  ASN A 221     2248   2950   2438   -510   -429    521       C  
ATOM   1827  C   ASN A 221      10.545  25.542 -18.362  1.00 19.74           C  
ANISOU 1827  C   ASN A 221     2211   2925   2365   -531   -427    511       C  
ATOM   1828  O   ASN A 221      11.001  24.563 -18.944  1.00 20.14           O  
ANISOU 1828  O   ASN A 221     2310   2986   2357   -554   -421    482       O  
ATOM   1829  CB  ASN A 221       9.905  26.097 -15.960  1.00 20.92           C  
ANISOU 1829  CB  ASN A 221     2341   3011   2598   -448   -412    496       C  
ATOM   1830  CG  ASN A 221      11.146  25.546 -15.329  1.00 23.14           C  
ANISOU 1830  CG  ASN A 221     2661   3267   2866   -417   -398    428       C  
ATOM   1831  OD1 ASN A 221      12.101  25.106 -15.998  1.00 22.57           O  
ANISOU 1831  OD1 ASN A 221     2607   3206   2763   -430   -393    405       O  
ATOM   1832  ND2 ASN A 221      11.167  25.582 -14.017  1.00 23.81           N  
ANISOU 1832  ND2 ASN A 221     2758   3312   2975   -375   -390    400       N  
ATOM   1833  N   ARG A 222      10.877  26.784 -18.683  1.00 18.88           N  
ANISOU 1833  N   ARG A 222     2057   2819   2299   -522   -429    542       N  
ATOM   1834  CA  ARG A 222      11.832  27.102 -19.726  1.00 18.93           C  
ANISOU 1834  CA  ARG A 222     2060   2843   2288   -537   -424    545       C  
ATOM   1835  C   ARG A 222      13.271  27.127 -19.238  1.00 18.41           C  
ANISOU 1835  C   ARG A 222     2006   2750   2238   -493   -403    498       C  
ATOM   1836  O   ARG A 222      14.134  27.579 -19.982  1.00 18.72           O  
ANISOU 1836  O   ARG A 222     2032   2802   2280   -496   -395    510       O  
ATOM   1837  CB  ARG A 222      11.491  28.498 -20.253  1.00 20.02           C  
ANISOU 1837  CB  ARG A 222     2137   2997   2475   -546   -439    607       C  
ATOM   1838  CG  ARG A 222      10.094  28.584 -20.823  1.00 23.44           C  
ANISOU 1838  CG  ARG A 222     2546   3462   2899   -595   -463    672       C  
ATOM   1839  CD  ARG A 222       9.746  29.989 -21.277  1.00 26.45           C  
ANISOU 1839  CD  ARG A 222     2858   3854   3336   -601   -474    740       C  
ATOM   1840  NE  ARG A 222       8.499  29.999 -22.037  1.00 28.59           N  
ANISOU 1840  NE  ARG A 222     3103   4163   3597   -658   -502    815       N  
ATOM   1841  CZ  ARG A 222       8.402  29.730 -23.335  1.00 31.63           C  
ANISOU 1841  CZ  ARG A 222     3500   4591   3926   -722   -526    845       C  
ATOM   1842  NH1 ARG A 222       9.488  29.449 -24.047  1.00 31.12           N  
ANISOU 1842  NH1 ARG A 222     3476   4538   3813   -730   -515    807       N  
ATOM   1843  NH2 ARG A 222       7.218  29.741 -23.933  1.00 31.84           N  
ANISOU 1843  NH2 ARG A 222     3501   4649   3946   -780   -560    921       N  
ATOM   1844  N   PHE A 223      13.552  26.663 -18.016  1.00 17.24           N  
ANISOU 1844  N   PHE A 223     1880   2567   2104   -456   -395    453       N  
ATOM   1845  CA  PHE A 223      14.877  26.810 -17.437  1.00 17.43           C  
ANISOU 1845  CA  PHE A 223     1905   2561   2156   -418   -384    423       C  
ATOM   1846  C   PHE A 223      15.704  25.551 -17.362  1.00 15.35           C  
ANISOU 1846  C   PHE A 223     1685   2292   1855   -409   -360    381       C  
ATOM   1847  O   PHE A 223      15.192  24.438 -17.466  1.00 15.55           O  
ANISOU 1847  O   PHE A 223     1751   2326   1831   -425   -350    360       O  
ATOM   1848  CB  PHE A 223      14.761  27.413 -16.009  1.00 18.71           C  
ANISOU 1848  CB  PHE A 223     2060   2680   2368   -381   -397    409       C  
ATOM   1849  CG  PHE A 223      13.758  28.531 -15.821  1.00 20.74           C  
ANISOU 1849  CG  PHE A 223     2286   2930   2664   -380   -409    447       C  
ATOM   1850  CD1 PHE A 223      13.624  29.530 -16.768  1.00 22.13           C  
ANISOU 1850  CD1 PHE A 223     2419   3129   2861   -400   -417    496       C  
ATOM   1851  CD2 PHE A 223      12.977  28.595 -14.684  1.00 22.23           C  
ANISOU 1851  CD2 PHE A 223     2490   3088   2870   -355   -406    437       C  
ATOM   1852  CE1 PHE A 223      12.696  30.547 -16.598  1.00 23.38           C  
ANISOU 1852  CE1 PHE A 223     2545   3277   3060   -396   -421    538       C  
ATOM   1853  CE2 PHE A 223      12.071  29.627 -14.501  1.00 23.56           C  
ANISOU 1853  CE2 PHE A 223     2631   3243   3077   -346   -405    478       C  
ATOM   1854  CZ  PHE A 223      11.935  30.596 -15.459  1.00 23.59           C  
ANISOU 1854  CZ  PHE A 223     2589   3269   3106   -367   -412    529       C  
ATOM   1855  N   THR A 224      17.002  25.743 -17.157  1.00 14.22           N  
ANISOU 1855  N   THR A 224     1530   2131   1741   -383   -350    374       N  
ATOM   1856  CA  THR A 224      17.923  24.681 -16.819  1.00 13.87           C  
ANISOU 1856  CA  THR A 224     1516   2071   1683   -362   -324    342       C  
ATOM   1857  C   THR A 224      18.777  25.156 -15.619  1.00 14.09           C  
ANISOU 1857  C   THR A 224     1523   2060   1769   -330   -344    335       C  
ATOM   1858  O   THR A 224      18.645  26.293 -15.133  1.00 14.76           O  
ANISOU 1858  O   THR A 224     1582   2130   1898   -326   -376    351       O  
ATOM   1859  CB  THR A 224      18.695  24.154 -18.032  1.00 14.52           C  
ANISOU 1859  CB  THR A 224     1613   2174   1731   -369   -284    352       C  
ATOM   1860  OG1 THR A 224      19.214  22.865 -17.666  1.00 14.05           O  
ANISOU 1860  OG1 THR A 224     1594   2096   1648   -351   -251    318       O  
ATOM   1861  CG2 THR A 224      19.849  25.052 -18.412  1.00 14.98           C  
ANISOU 1861  CG2 THR A 224     1625   2231   1837   -353   -280    390       C  
ATOM   1862  N   THR A 225      19.601  24.275 -15.099  1.00 13.19           N  
ANISOU 1862  N   THR A 225     1427   1930   1656   -310   -327    314       N  
ATOM   1863  CA  THR A 225      20.500  24.563 -14.003  1.00 13.50           C  
ANISOU 1863  CA  THR A 225     1450   1933   1745   -289   -350    314       C  
ATOM   1864  C   THR A 225      21.729  23.647 -14.160  1.00 13.55           C  
ANISOU 1864  C   THR A 225     1455   1935   1756   -272   -316    321       C  
ATOM   1865  O   THR A 225      21.844  22.918 -15.145  1.00 13.01           O  
ANISOU 1865  O   THR A 225     1403   1888   1651   -273   -269    323       O  
ATOM   1866  CB  THR A 225      19.759  24.407 -12.648  1.00 15.53           C  
ANISOU 1866  CB  THR A 225     1737   2164   2000   -281   -375    279       C  
ATOM   1867  OG1 THR A 225      20.659  24.812 -11.628  1.00 17.08           O  
ANISOU 1867  OG1 THR A 225     1926   2324   2239   -269   -407    283       O  
ATOM   1868  CG2 THR A 225      19.333  22.975 -12.374  1.00 16.36           C  
ANISOU 1868  CG2 THR A 225     1881   2273   2060   -277   -349    242       C  
ATOM   1869  N   THR A 226      22.671  23.746 -13.226  1.00 13.79           N  
ANISOU 1869  N   THR A 226     1469   1936   1834   -257   -339    332       N  
ATOM   1870  CA  THR A 226      23.834  22.885 -13.142  1.00 13.97           C  
ANISOU 1870  CA  THR A 226     1483   1950   1876   -238   -308    348       C  
ATOM   1871  C   THR A 226      23.718  22.116 -11.827  1.00 14.17           C  
ANISOU 1871  C   THR A 226     1535   1950   1898   -231   -325    314       C  
ATOM   1872  O   THR A 226      22.936  22.501 -10.957  1.00 13.64           O  
ANISOU 1872  O   THR A 226     1489   1869   1823   -239   -365    286       O  
ATOM   1873  CB  THR A 226      25.130  23.738 -13.146  1.00 16.08           C  
ANISOU 1873  CB  THR A 226     1692   2204   2212   -234   -332    409       C  
ATOM   1874  OG1 THR A 226      25.192  24.499 -11.938  1.00 16.64           O  
ANISOU 1874  OG1 THR A 226     1760   2243   2318   -246   -401    409       O  
ATOM   1875  CG2 THR A 226      25.245  24.618 -14.361  1.00 17.33           C  
ANISOU 1875  CG2 THR A 226     1819   2387   2379   -240   -320    448       C  
ATOM   1876  N  ALEU A 227      24.519  21.061 -11.653  0.50 14.30           N  
ANISOU 1876  N  ALEU A 227     1551   1958   1924   -213   -291    321       N  
ATOM   1877  N  BLEU A 227      24.524  21.056 -11.640  0.50 14.01           N  
ANISOU 1877  N  BLEU A 227     1515   1922   1888   -213   -291    321       N  
ATOM   1878  CA ALEU A 227      24.520  20.302 -10.408  0.50 15.27           C  
ANISOU 1878  CA ALEU A 227     1694   2059   2049   -206   -308    296       C  
ATOM   1879  CA BLEU A 227      24.508  20.322 -10.373  0.50 14.69           C  
ANISOU 1879  CA BLEU A 227     1621   1985   1977   -207   -310    295       C  
ATOM   1880  C  ALEU A 227      24.897  21.190  -9.216  0.50 15.82           C  
ANISOU 1880  C  ALEU A 227     1749   2099   2162   -218   -380    311       C  
ATOM   1881  C  BLEU A 227      24.873  21.224  -9.206  0.50 15.51           C  
ANISOU 1881  C  BLEU A 227     1711   2060   2123   -219   -382    311       C  
ATOM   1882  O  ALEU A 227      24.223  21.149  -8.192  0.50 16.27           O  
ANISOU 1882  O  ALEU A 227     1842   2140   2200   -224   -412    274       O  
ATOM   1883  O  BLEU A 227      24.172  21.226  -8.197  0.50 15.90           O  
ANISOU 1883  O  BLEU A 227     1795   2093   2152   -225   -414    273       O  
ATOM   1884  CB ALEU A 227      25.476  19.108 -10.535  0.50 15.64           C  
ANISOU 1884  CB ALEU A 227     1732   2100   2112   -183   -254    317       C  
ATOM   1885  CB BLEU A 227      25.440  19.112 -10.410  0.50 14.62           C  
ANISOU 1885  CB BLEU A 227     1603   1969   1982   -184   -260    314       C  
ATOM   1886  CG ALEU A 227      25.138  17.847  -9.735  0.50 17.11           C  
ANISOU 1886  CG ALEU A 227     1952   2274   2273   -174   -240    278       C  
ATOM   1887  CG BLEU A 227      24.906  17.875 -11.109  0.50 15.35           C  
ANISOU 1887  CG BLEU A 227     1740   2074   2019   -174   -192    279       C  
ATOM   1888  CD1ALEU A 227      23.676  17.439  -9.907  0.50 17.60           C  
ANISOU 1888  CD1ALEU A 227     2069   2351   2268   -185   -232    217       C  
ATOM   1889  CD1BLEU A 227      25.881  16.725 -10.955  0.50 15.25           C  
ANISOU 1889  CD1BLEU A 227     1720   2045   2030   -146   -141    300       C  
ATOM   1890  CD2ALEU A 227      26.019  16.702 -10.161  0.50 17.33           C  
ANISOU 1890  CD2ALEU A 227     1975   2297   2314   -147   -170    301       C  
ATOM   1891  CD2BLEU A 227      23.531  17.463 -10.562  0.50 15.94           C  
ANISOU 1891  CD2BLEU A 227     1864   2153   2040   -187   -211    218       C  
ATOM   1892  N   ASN A 228      25.916  22.051  -9.374  1.00 15.51           N  
ANISOU 1892  N   ASN A 228     1664   2052   2179   -225   -408    368       N  
ATOM   1893  CA  ASN A 228      26.326  22.950  -8.300  1.00 15.00           C  
ANISOU 1893  CA  ASN A 228     1596   1953   2151   -245   -486    386       C  
ATOM   1894  C   ASN A 228      25.286  24.033  -7.986  1.00 14.90           C  
ANISOU 1894  C   ASN A 228     1620   1930   2114   -260   -525    350       C  
ATOM   1895  O   ASN A 228      25.056  24.317  -6.813  1.00 15.98           O  
ANISOU 1895  O   ASN A 228     1794   2032   2243   -271   -572    328       O  
ATOM   1896  CB  ASN A 228      27.700  23.551  -8.581  1.00 15.85           C  
ANISOU 1896  CB  ASN A 228     1641   2053   2327   -253   -510    464       C  
ATOM   1897  CG  ASN A 228      28.840  22.550  -8.522  1.00 19.59           C  
ANISOU 1897  CG  ASN A 228     2077   2526   2841   -237   -480    514       C  
ATOM   1898  OD1 ASN A 228      29.929  22.794  -9.060  1.00 21.73           O  
ANISOU 1898  OD1 ASN A 228     2288   2799   3169   -233   -473    588       O  
ATOM   1899  ND2 ASN A 228      28.635  21.411  -7.881  1.00 20.10           N  
ANISOU 1899  ND2 ASN A 228     2169   2585   2882   -226   -459    482       N  
ATOM   1900  N   ASP A 229      24.638  24.604  -9.002  1.00 14.47           N  
ANISOU 1900  N   ASP A 229     1556   1898   2042   -260   -501    347       N  
ATOM   1901  CA  ASP A 229      23.626  25.638  -8.756  1.00 14.83           C  
ANISOU 1901  CA  ASP A 229     1631   1932   2073   -269   -529    323       C  
ATOM   1902  C   ASP A 229      22.417  25.008  -8.087  1.00 15.00           C  
ANISOU 1902  C   ASP A 229     1704   1950   2044   -259   -513    267       C  
ATOM   1903  O   ASP A 229      21.915  25.535  -7.090  1.00 15.74           O  
ANISOU 1903  O   ASP A 229     1840   2011   2132   -261   -544    245       O  
ATOM   1904  CB  ASP A 229      23.213  26.348 -10.049  1.00 17.00           C  
ANISOU 1904  CB  ASP A 229     1876   2237   2347   -273   -507    342       C  
ATOM   1905  CG  ASP A 229      22.101  27.337  -9.811  1.00 23.28           C  
ANISOU 1905  CG  ASP A 229     2696   3018   3131   -278   -525    323       C  
ATOM   1906  OD1 ASP A 229      22.347  28.337  -9.109  1.00 25.03           O  
ANISOU 1906  OD1 ASP A 229     2930   3199   3380   -287   -572    331       O  
ATOM   1907  OD2 ASP A 229      20.957  27.068 -10.265  1.00 24.97           O  
ANISOU 1907  OD2 ASP A 229     2923   3257   3308   -273   -492    302       O  
ATOM   1908  N   PHE A 230      21.979  23.838  -8.584  1.00 14.41           N  
ANISOU 1908  N   PHE A 230     1635   1907   1935   -249   -463    247       N  
ATOM   1909  CA  PHE A 230      20.850  23.142  -7.980  1.00 14.40           C  
ANISOU 1909  CA  PHE A 230     1676   1905   1891   -240   -449    203       C  
ATOM   1910  C   PHE A 230      21.151  22.818  -6.516  1.00 15.23           C  
ANISOU 1910  C   PHE A 230     1813   1975   2000   -235   -479    184       C  
ATOM   1911  O   PHE A 230      20.308  23.067  -5.661  1.00 16.01           O  
ANISOU 1911  O   PHE A 230     1952   2052   2080   -229   -491    157       O  
ATOM   1912  CB  PHE A 230      20.527  21.845  -8.745  1.00 13.67           C  
ANISOU 1912  CB  PHE A 230     1586   1845   1762   -236   -398    189       C  
ATOM   1913  CG  PHE A 230      19.422  21.092  -8.049  1.00 14.69           C  
ANISOU 1913  CG  PHE A 230     1754   1973   1855   -229   -389    150       C  
ATOM   1914  CD1 PHE A 230      18.100  21.467  -8.213  1.00 15.26           C  
ANISOU 1914  CD1 PHE A 230     1837   2056   1905   -233   -387    144       C  
ATOM   1915  CD2 PHE A 230      19.715  20.119  -7.106  1.00 15.80           C  
ANISOU 1915  CD2 PHE A 230     1914   2097   1991   -218   -389    129       C  
ATOM   1916  CE1 PHE A 230      17.088  20.834  -7.504  1.00 16.46           C  
ANISOU 1916  CE1 PHE A 230     2018   2204   2030   -225   -380    119       C  
ATOM   1917  CE2 PHE A 230      18.704  19.520  -6.370  1.00 16.25           C  
ANISOU 1917  CE2 PHE A 230     2005   2151   2019   -210   -385     99       C  
ATOM   1918  CZ  PHE A 230      17.399  19.868  -6.589  1.00 16.71           C  
ANISOU 1918  CZ  PHE A 230     2073   2221   2056   -212   -379     95       C  
ATOM   1919  N   ASN A 231      22.374  22.361  -6.232  1.00 15.00           N  
ANISOU 1919  N   ASN A 231     1764   1935   1998   -237   -491    205       N  
ATOM   1920  CA  ASN A 231      22.758  22.003  -4.873  1.00 15.46           C  
ANISOU 1920  CA  ASN A 231     1851   1963   2061   -239   -525    195       C  
ATOM   1921  C   ASN A 231      22.802  23.158  -3.914  1.00 16.96           C  
ANISOU 1921  C   ASN A 231     2076   2110   2259   -255   -585    195       C  
ATOM   1922  O   ASN A 231      22.591  22.932  -2.725  1.00 17.72           O  
ANISOU 1922  O   ASN A 231     2219   2178   2334   -255   -607    170       O  
ATOM   1923  CB  ASN A 231      24.050  21.215  -4.849  1.00 16.36           C  
ANISOU 1923  CB  ASN A 231     1929   2078   2210   -240   -523    231       C  
ATOM   1924  CG  ASN A 231      23.829  19.796  -5.314  1.00 18.15           C  
ANISOU 1924  CG  ASN A 231     2152   2331   2414   -220   -461    213       C  
ATOM   1925  OD1 ASN A 231      22.721  19.254  -5.242  1.00 18.68           O  
ANISOU 1925  OD1 ASN A 231     2253   2409   2436   -211   -436    169       O  
ATOM   1926  ND2 ASN A 231      24.868  19.145  -5.804  1.00 19.47           N  
ANISOU 1926  ND2 ASN A 231     2279   2506   2612   -211   -431    250       N  
ATOM   1927  N   LEU A 232      22.976  24.394  -4.396  1.00 17.68           N  
ANISOU 1927  N   LEU A 232     2152   2191   2374   -267   -609    220       N  
ATOM   1928  CA  LEU A 232      22.885  25.567  -3.519  1.00 19.22           C  
ANISOU 1928  CA  LEU A 232     2396   2337   2569   -283   -662    214       C  
ATOM   1929  C   LEU A 232      21.437  25.670  -3.002  1.00 19.67           C  
ANISOU 1929  C   LEU A 232     2511   2382   2580   -261   -634    166       C  
ATOM   1930  O   LEU A 232      21.223  25.880  -1.806  1.00 20.80           O  
ANISOU 1930  O   LEU A 232     2721   2482   2700   -262   -658    142       O  
ATOM   1931  CB  LEU A 232      23.257  26.842  -4.289  1.00 20.79           C  
ANISOU 1931  CB  LEU A 232     2564   2531   2805   -298   -684    250       C  
ATOM   1932  CG  LEU A 232      24.717  26.974  -4.677  1.00 23.66           C  
ANISOU 1932  CG  LEU A 232     2869   2897   3222   -320   -719    310       C  
ATOM   1933  CD1 LEU A 232      24.933  28.250  -5.452  1.00 24.78           C  
ANISOU 1933  CD1 LEU A 232     2982   3035   3398   -333   -739    345       C  
ATOM   1934  CD2 LEU A 232      25.615  26.984  -3.447  1.00 24.66           C  
ANISOU 1934  CD2 LEU A 232     3027   2980   3364   -349   -789    327       C  
ATOM   1935  N   VAL A 233      20.459  25.417  -3.886  1.00 18.99           N  
ANISOU 1935  N   VAL A 233     2402   2334   2479   -243   -580    157       N  
ATOM   1936  CA  VAL A 233      19.045  25.406  -3.533  1.00 18.83           C  
ANISOU 1936  CA  VAL A 233     2420   2309   2424   -220   -547    128       C  
ATOM   1937  C   VAL A 233      18.700  24.193  -2.684  1.00 18.78           C  
ANISOU 1937  C   VAL A 233     2444   2304   2386   -206   -531     97       C  
ATOM   1938  O   VAL A 233      18.008  24.331  -1.675  1.00 19.12           O  
ANISOU 1938  O   VAL A 233     2544   2316   2405   -190   -528     74       O  
ATOM   1939  CB  VAL A 233      18.177  25.464  -4.804  1.00 20.10           C  
ANISOU 1939  CB  VAL A 233     2538   2514   2584   -214   -505    142       C  
ATOM   1940  CG1 VAL A 233      16.694  25.454  -4.446  1.00 20.95           C  
ANISOU 1940  CG1 VAL A 233     2676   2618   2668   -191   -471    128       C  
ATOM   1941  CG2 VAL A 233      18.525  26.699  -5.624  1.00 20.92           C  
ANISOU 1941  CG2 VAL A 233     2610   2616   2722   -228   -521    175       C  
ATOM   1942  N   ALA A 234      19.239  23.018  -3.016  1.00 18.51           N  
ANISOU 1942  N   ALA A 234     2379   2302   2354   -209   -520     99       N  
ATOM   1943  CA  ALA A 234      18.996  21.802  -2.227  1.00 19.45           C  
ANISOU 1943  CA  ALA A 234     2521   2423   2446   -197   -506     73       C  
ATOM   1944  C   ALA A 234      19.449  22.000  -0.771  1.00 20.44           C  
ANISOU 1944  C   ALA A 234     2700   2501   2564   -201   -549     61       C  
ATOM   1945  O   ALA A 234      18.700  21.699   0.153  1.00 20.35           O  
ANISOU 1945  O   ALA A 234     2737   2472   2521   -185   -538     34       O  
ATOM   1946  CB  ALA A 234      19.732  20.621  -2.849  1.00 19.88           C  
ANISOU 1946  CB  ALA A 234     2534   2510   2511   -201   -488     82       C  
ATOM   1947  N   MET A 235      20.620  22.616  -0.569  1.00 20.53           N  
ANISOU 1947  N   MET A 235     2708   2489   2605   -227   -599     85       N  
ATOM   1948  CA  MET A 235      21.139  22.894   0.770  1.00 21.06           C  
ANISOU 1948  CA  MET A 235     2833   2506   2661   -244   -653     80       C  
ATOM   1949  C   MET A 235      20.163  23.771   1.556  1.00 19.75           C  
ANISOU 1949  C   MET A 235     2748   2297   2458   -231   -651     50       C  
ATOM   1950  O   MET A 235      19.813  23.447   2.691  1.00 19.72           O  
ANISOU 1950  O   MET A 235     2808   2267   2418   -223   -654     24       O  
ATOM   1951  CB  MET A 235      22.522  23.574   0.668  1.00 23.60           C  
ANISOU 1951  CB  MET A 235     3132   2810   3027   -282   -716    124       C  
ATOM   1952  CG  MET A 235      23.037  24.121   1.984  1.00 29.30           C  
ANISOU 1952  CG  MET A 235     3926   3474   3734   -313   -786    124       C  
ATOM   1953  SD  MET A 235      24.257  23.025   2.705  1.00 42.88           S  
ANISOU 1953  SD  MET A 235     5622   5196   5473   -340   -831    157       S  
ATOM   1954  CE  MET A 235      25.589  23.247   1.552  1.00 39.42           C  
ANISOU 1954  CE  MET A 235     5082   4783   5112   -362   -851    231       C  
ATOM   1955  N   LYS A 236      19.700  24.853   0.927  1.00 18.47           N  
ANISOU 1955  N   LYS A 236     2583   2127   2306   -226   -639     57       N  
ATOM   1956  CA  LYS A 236      18.792  25.785   1.563  1.00 17.97           C  
ANISOU 1956  CA  LYS A 236     2595   2016   2215   -208   -625     36       C  
ATOM   1957  C   LYS A 236      17.493  25.121   2.014  1.00 17.43           C  
ANISOU 1957  C   LYS A 236     2555   1957   2112   -167   -566     10       C  
ATOM   1958  O   LYS A 236      16.951  25.470   3.058  1.00 18.51           O  
ANISOU 1958  O   LYS A 236     2773   2045   2214   -149   -556    -12       O  
ATOM   1959  CB  LYS A 236      18.530  26.978   0.623  1.00 20.89           C  
ANISOU 1959  CB  LYS A 236     2939   2384   2613   -207   -616     56       C  
ATOM   1960  CG  LYS A 236      17.528  27.986   1.164  1.00 26.53           C  
ANISOU 1960  CG  LYS A 236     3727   3048   3307   -180   -586     42       C  
ATOM   1961  CD  LYS A 236      17.172  29.030   0.127  1.00 33.01           C  
ANISOU 1961  CD  LYS A 236     4508   3874   4161   -177   -569     68       C  
ATOM   1962  CE  LYS A 236      15.990  29.854   0.572  1.00 37.50           C  
ANISOU 1962  CE  LYS A 236     5137   4397   4715   -139   -519     61       C  
ATOM   1963  NZ  LYS A 236      16.358  30.835   1.631  1.00 40.05           N  
ANISOU 1963  NZ  LYS A 236     5567   4634   5015   -148   -550     42       N  
ATOM   1964  N   TYR A 237      17.020  24.124   1.260  1.00 15.66           N  
ANISOU 1964  N   TYR A 237     2267   1790   1895   -153   -527     15       N  
ATOM   1965  CA  TYR A 237      15.746  23.472   1.564  1.00 14.78           C  
ANISOU 1965  CA  TYR A 237     2168   1692   1758   -118   -474      2       C  
ATOM   1966  C   TYR A 237      15.852  22.109   2.238  1.00 14.96           C  
ANISOU 1966  C   TYR A 237     2196   1729   1759   -114   -473    -16       C  
ATOM   1967  O   TYR A 237      14.861  21.366   2.262  1.00 15.72           O  
ANISOU 1967  O   TYR A 237     2282   1848   1841    -89   -431    -19       O  
ATOM   1968  CB  TYR A 237      14.899  23.373   0.286  1.00 14.56           C  
ANISOU 1968  CB  TYR A 237     2073   1712   1748   -110   -433     26       C  
ATOM   1969  CG  TYR A 237      14.367  24.728  -0.118  1.00 15.63           C  
ANISOU 1969  CG  TYR A 237     2211   1826   1900   -101   -420     47       C  
ATOM   1970  CD1 TYR A 237      13.223  25.245   0.467  1.00 16.68           C  
ANISOU 1970  CD1 TYR A 237     2387   1928   2023    -65   -377     51       C  
ATOM   1971  CD2 TYR A 237      15.067  25.534  -1.005  1.00 16.39           C  
ANISOU 1971  CD2 TYR A 237     2272   1928   2027   -126   -446     66       C  
ATOM   1972  CE1 TYR A 237      12.778  26.527   0.169  1.00 17.54           C  
ANISOU 1972  CE1 TYR A 237     2503   2010   2152    -53   -360     73       C  
ATOM   1973  CE2 TYR A 237      14.617  26.808  -1.333  1.00 16.88           C  
ANISOU 1973  CE2 TYR A 237     2339   1968   2108   -118   -434     86       C  
ATOM   1974  CZ  TYR A 237      13.486  27.312  -0.721  1.00 18.39           C  
ANISOU 1974  CZ  TYR A 237     2574   2123   2289    -82   -391     89       C  
ATOM   1975  OH  TYR A 237      13.013  28.560  -1.046  1.00 19.90           O  
ANISOU 1975  OH  TYR A 237     2769   2289   2504    -70   -372    114       O  
ATOM   1976  N  AASN A 238      17.029  21.783   2.777  0.50 14.71           N  
ANISOU 1976  N  AASN A 238     2175   1685   1729   -140   -520    -21       N  
ATOM   1977  N  BASN A 238      17.031  21.780   2.788  0.50 14.49           N  
ANISOU 1977  N  BASN A 238     2148   1657   1700   -140   -520    -21       N  
ATOM   1978  CA AASN A 238      17.254  20.514   3.458  0.50 15.20           C  
ANISOU 1978  CA AASN A 238     2240   1759   1775   -138   -523    -33       C  
ATOM   1979  CA BASN A 238      17.284  20.504   3.467  0.50 14.74           C  
ANISOU 1979  CA BASN A 238     2182   1701   1718   -139   -524    -33       C  
ATOM   1980  C  AASN A 238      16.986  19.323   2.549  0.50 14.96           C  
ANISOU 1980  C  AASN A 238     2143   1785   1758   -131   -487    -28       C  
ATOM   1981  C  BASN A 238      17.054  19.295   2.568  0.50 14.80           C  
ANISOU 1981  C  BASN A 238     2122   1765   1739   -133   -489    -28       C  
ATOM   1982  O  AASN A 238      16.317  18.373   2.941  0.50 15.04           O  
ANISOU 1982  O  AASN A 238     2159   1809   1749   -112   -459    -41       O  
ATOM   1983  O  BASN A 238      16.509  18.281   3.000  0.50 14.95           O  
ANISOU 1983  O  BASN A 238     2144   1796   1739   -117   -466    -41       O  
ATOM   1984  CB AASN A 238      16.460  20.437   4.761  0.50 17.13           C  
ANISOU 1984  CB AASN A 238     2562   1969   1976   -112   -506    -57       C  
ATOM   1985  CB BASN A 238      16.506  20.379   4.782  0.50 15.99           C  
ANISOU 1985  CB BASN A 238     2416   1827   1832   -114   -508    -57       C  
ATOM   1986  CG AASN A 238      16.882  21.508   5.733  0.50 21.05           C  
ANISOU 1986  CG AASN A 238     3145   2403   2451   -126   -546    -66       C  
ATOM   1987  CG BASN A 238      17.068  21.220   5.903  0.50 18.49           C  
ANISOU 1987  CG BASN A 238     2820   2082   2124   -131   -554    -67       C  
ATOM   1988  OD1AASN A 238      16.104  22.393   6.115  0.50 22.39           O  
ANISOU 1988  OD1AASN A 238     3377   2533   2598   -103   -521    -75       O  
ATOM   1989  OD1BASN A 238      18.118  21.861   5.772  0.50 18.96           O  
ANISOU 1989  OD1BASN A 238     2879   2122   2202   -168   -609    -53       O  
ATOM   1990  ND2AASN A 238      18.142  21.469   6.126  0.50 21.55           N  
ANISOU 1990  ND2AASN A 238     3215   2452   2521   -167   -611    -58       N  
ATOM   1991  ND2BASN A 238      16.368  21.244   7.026  0.50 19.10           N  
ANISOU 1991  ND2BASN A 238     2978   2124   2157   -105   -534    -89       N  
ATOM   1992  N   TYR A 239      17.462  19.417   1.309  1.00 14.63           N  
ANISOU 1992  N   TYR A 239     2042   1771   1744   -147   -485     -8       N  
ATOM   1993  CA  TYR A 239      17.378  18.342   0.336  1.00 14.81           C  
ANISOU 1993  CA  TYR A 239     2014   1840   1775   -147   -454     -4       C  
ATOM   1994  C   TYR A 239      18.779  17.746   0.260  1.00 15.52           C  
ANISOU 1994  C   TYR A 239     2074   1933   1890   -165   -474     10       C  
ATOM   1995  O   TYR A 239      19.769  18.452   0.460  1.00 16.11           O  
ANISOU 1995  O   TYR A 239     2147   1986   1987   -183   -514     29       O  
ATOM   1996  CB  TYR A 239      17.039  18.905  -1.050  1.00 14.64           C  
ANISOU 1996  CB  TYR A 239     1953   1844   1764   -154   -435     14       C  
ATOM   1997  CG  TYR A 239      15.569  18.840  -1.373  1.00 14.52           C  
ANISOU 1997  CG  TYR A 239     1940   1846   1730   -140   -401     13       C  
ATOM   1998  CD1 TYR A 239      14.637  19.491  -0.584  1.00 14.91           C  
ANISOU 1998  CD1 TYR A 239     2026   1870   1769   -118   -394     12       C  
ATOM   1999  CD2 TYR A 239      15.115  18.175  -2.502  1.00 14.55           C  
ANISOU 1999  CD2 TYR A 239     1911   1889   1728   -151   -376     22       C  
ATOM   2000  CE1 TYR A 239      13.281  19.426  -0.871  1.00 15.52           C  
ANISOU 2000  CE1 TYR A 239     2095   1964   1839   -104   -361     26       C  
ATOM   2001  CE2 TYR A 239      13.766  18.114  -2.809  1.00 15.01           C  
ANISOU 2001  CE2 TYR A 239     1965   1964   1773   -146   -355     34       C  
ATOM   2002  CZ  TYR A 239      12.850  18.743  -1.992  1.00 15.84           C  
ANISOU 2002  CZ  TYR A 239     2094   2047   1877   -121   -347     41       C  
ATOM   2003  OH  TYR A 239      11.509  18.631  -2.269  1.00 16.32           O  
ANISOU 2003  OH  TYR A 239     2142   2126   1936   -115   -324     67       O  
ATOM   2004  N  AGLU A 240      18.870  16.448  -0.030  0.50 15.37           N  
ANISOU 2004  N  AGLU A 240     2031   1938   1870   -160   -446      6       N  
ATOM   2005  N  BGLU A 240      18.868  16.461  -0.067  0.50 15.60           N  
ANISOU 2005  N  BGLU A 240     2060   1969   1900   -160   -446      6       N  
ATOM   2006  CA AGLU A 240      20.154  15.777  -0.186  0.50 16.23           C  
ANISOU 2006  CA AGLU A 240     2106   2050   2009   -169   -451     28       C  
ATOM   2007  CA BGLU A 240      20.151  15.796  -0.223  0.50 16.61           C  
ANISOU 2007  CA BGLU A 240     2154   2099   2058   -169   -450     28       C  
ATOM   2008  C  AGLU A 240      20.879  16.322  -1.420  0.50 16.43           C  
ANISOU 2008  C  AGLU A 240     2090   2088   2064   -180   -444     58       C  
ATOM   2009  C  BGLU A 240      20.878  16.350  -1.428  0.50 16.61           C  
ANISOU 2009  C  BGLU A 240     2113   2111   2087   -180   -444     58       C  
ATOM   2010  O  AGLU A 240      20.244  16.585  -2.438  0.50 15.69           O  
ANISOU 2010  O  AGLU A 240     1989   2015   1956   -179   -417     53       O  
ATOM   2011  O  BGLU A 240      20.249  16.611  -2.453  0.50 15.86           O  
ANISOU 2011  O  BGLU A 240     2011   2037   1979   -179   -417     53       O  
ATOM   2012  CB AGLU A 240      19.925  14.265  -0.355  0.50 18.78           C  
ANISOU 2012  CB AGLU A 240     2421   2394   2322   -157   -409     14       C  
ATOM   2013  CB BGLU A 240      19.929  14.302  -0.446  0.50 19.82           C  
ANISOU 2013  CB BGLU A 240     2550   2526   2454   -157   -408     15       C  
ATOM   2014  CG AGLU A 240      19.511  13.580   0.931  0.50 23.01           C  
ANISOU 2014  CG AGLU A 240     2988   2918   2839   -147   -418     -6       C  
ATOM   2015  CG BGLU A 240      19.757  13.549   0.847  0.50 25.74           C  
ANISOU 2015  CG BGLU A 240     3326   3262   3190   -149   -418     -1       C  
ATOM   2016  CD AGLU A 240      20.607  13.558   1.976  0.50 27.97           C  
ANISOU 2016  CD AGLU A 240     3616   3521   3489   -158   -460     13       C  
ATOM   2017  CD BGLU A 240      19.839  12.057   0.654  0.50 32.83           C  
ANISOU 2017  CD BGLU A 240     4209   4175   4091   -139   -381     -6       C  
ATOM   2018  OE1AGLU A 240      21.558  12.757   1.825  0.50 28.30           O  
ANISOU 2018  OE1AGLU A 240     3622   3567   3563   -160   -451     38       O  
ATOM   2019  OE1BGLU A 240      19.029  11.520  -0.134  0.50 34.72           O  
ANISOU 2019  OE1BGLU A 240     4450   4433   4308   -135   -343    -22       O  
ATOM   2020  OE2AGLU A 240      20.521  14.346   2.943  0.50 29.56           O  
ANISOU 2020  OE2AGLU A 240     3858   3697   3677   -165   -502      8       O  
ATOM   2021  OE2BGLU A 240      20.715  11.421   1.281  0.50 35.82           O  
ANISOU 2021  OE2BGLU A 240     4574   4543   4493   -140   -390     10       O  
ATOM   2022  N   PRO A 241      22.205  16.501  -1.358  1.00 17.14           N  
ANISOU 2022  N   PRO A 241     2153   2168   2193   -191   -466     92       N  
ATOM   2023  CA  PRO A 241      22.942  16.989  -2.541  1.00 18.08           C  
ANISOU 2023  CA  PRO A 241     2227   2298   2344   -196   -454    129       C  
ATOM   2024  C   PRO A 241      22.812  15.998  -3.698  1.00 17.98           C  
ANISOU 2024  C   PRO A 241     2198   2315   2320   -182   -387    124       C  
ATOM   2025  O   PRO A 241      22.874  14.796  -3.468  1.00 18.99           O  
ANISOU 2025  O   PRO A 241     2329   2443   2441   -171   -359    115       O  
ATOM   2026  CB  PRO A 241      24.400  17.037  -2.063  1.00 19.59           C  
ANISOU 2026  CB  PRO A 241     2383   2473   2589   -208   -485    182       C  
ATOM   2027  CG  PRO A 241      24.323  17.034  -0.568  1.00 19.93           C  
ANISOU 2027  CG  PRO A 241     2465   2487   2620   -222   -542    169       C  
ATOM   2028  CD  PRO A 241      23.111  16.247  -0.217  1.00 17.24           C  
ANISOU 2028  CD  PRO A 241     2168   2155   2229   -203   -511    114       C  
ATOM   2029  N   LEU A 242      22.540  16.485  -4.895  1.00 17.16           N  
ANISOU 2029  N   LEU A 242     2081   2229   2211   -185   -365    132       N  
ATOM   2030  CA  LEU A 242      22.418  15.624  -6.060  1.00 17.79           C  
ANISOU 2030  CA  LEU A 242     2160   2329   2268   -176   -302    127       C  
ATOM   2031  C   LEU A 242      23.822  15.392  -6.612  1.00 17.81           C  
ANISOU 2031  C   LEU A 242     2124   2329   2316   -165   -271    175       C  
ATOM   2032  O   LEU A 242      24.618  16.325  -6.735  1.00 17.96           O  
ANISOU 2032  O   LEU A 242     2108   2343   2374   -171   -297    215       O  
ATOM   2033  CB  LEU A 242      21.514  16.262  -7.115  1.00 18.10           C  
ANISOU 2033  CB  LEU A 242     2211   2391   2274   -188   -292    115       C  
ATOM   2034  CG  LEU A 242      20.945  15.279  -8.128  1.00 19.57           C  
ANISOU 2034  CG  LEU A 242     2425   2597   2415   -191   -240     96       C  
ATOM   2035  CD1 LEU A 242      19.885  14.396  -7.492  1.00 20.27           C  
ANISOU 2035  CD1 LEU A 242     2550   2685   2468   -192   -238     58       C  
ATOM   2036  CD2 LEU A 242      20.350  16.000  -9.280  1.00 19.83           C  
ANISOU 2036  CD2 LEU A 242     2458   2652   2423   -210   -238    103       C  
ATOM   2037  N   THR A 243      24.131  14.138  -6.881  1.00 18.16           N  
ANISOU 2037  N   THR A 243     2176   2371   2353   -148   -216    171       N  
ATOM   2038  CA  THR A 243      25.435  13.756  -7.399  1.00 18.67           C  
ANISOU 2038  CA  THR A 243     2205   2427   2461   -129   -169    223       C  
ATOM   2039  C   THR A 243      25.333  13.318  -8.861  1.00 19.12           C  
ANISOU 2039  C   THR A 243     2288   2496   2482   -118    -94    215       C  
ATOM   2040  O   THR A 243      24.223  13.074  -9.370  1.00 18.82           O  
ANISOU 2040  O   THR A 243     2298   2470   2382   -132    -85    168       O  
ATOM   2041  CB  THR A 243      26.018  12.618  -6.543  1.00 19.51           C  
ANISOU 2041  CB  THR A 243     2302   2515   2595   -111   -150    234       C  
ATOM   2042  OG1 THR A 243      25.257  11.425  -6.756  1.00 19.15           O  
ANISOU 2042  OG1 THR A 243     2306   2470   2500   -103   -103    186       O  
ATOM   2043  CG2 THR A 243      26.099  12.973  -5.073  1.00 20.65           C  
ANISOU 2043  CG2 THR A 243     2434   2647   2764   -127   -225    239       C  
ATOM   2044  N   GLN A 244      26.491  13.150  -9.526  1.00 19.36           N  
ANISOU 2044  N   GLN A 244     2287   2517   2550    -95    -42    267       N  
ATOM   2045  CA  GLN A 244      26.496  12.626 -10.886  1.00 19.60           C  
ANISOU 2045  CA  GLN A 244     2356   2551   2540    -81     41    261       C  
ATOM   2046  C   GLN A 244      25.936  11.192 -10.896  1.00 19.31           C  
ANISOU 2046  C   GLN A 244     2382   2500   2454    -73     89    213       C  
ATOM   2047  O   GLN A 244      25.228  10.841 -11.832  1.00 19.52           O  
ANISOU 2047  O   GLN A 244     2468   2530   2417    -83    125    179       O  
ATOM   2048  CB  GLN A 244      27.908  12.662 -11.481  1.00 21.32           C  
ANISOU 2048  CB  GLN A 244     2529   2757   2816    -48    101    335       C  
ATOM   2049  CG  GLN A 244      27.948  12.291 -12.963  1.00 24.67           C  
ANISOU 2049  CG  GLN A 244     3001   3180   3193    -31    191    332       C  
ATOM   2050  CD  GLN A 244      27.099  13.215 -13.796  1.00 27.50           C  
ANISOU 2050  CD  GLN A 244     3381   3566   3501    -62    161    309       C  
ATOM   2051  OE1 GLN A 244      27.194  14.445 -13.689  1.00 28.95           O  
ANISOU 2051  OE1 GLN A 244     3514   3767   3719    -76    105    337       O  
ATOM   2052  NE2 GLN A 244      26.239  12.644 -14.629  1.00 26.25           N  
ANISOU 2052  NE2 GLN A 244     3302   3412   3261    -76    196    259       N  
ATOM   2053  N   ASP A 245      26.150  10.409  -9.818  1.00 18.53           N  
ANISOU 2053  N   ASP A 245     2271   2384   2386    -60     86    214       N  
ATOM   2054  CA  ASP A 245      25.574   9.066  -9.707  1.00 18.09           C  
ANISOU 2054  CA  ASP A 245     2274   2313   2287    -56    124    166       C  
ATOM   2055  C   ASP A 245      24.045   9.134  -9.768  1.00 16.92           C  
ANISOU 2055  C   ASP A 245     2178   2185   2068    -93     79    104       C  
ATOM   2056  O   ASP A 245      23.437   8.335 -10.466  1.00 17.01           O  
ANISOU 2056  O   ASP A 245     2251   2189   2021   -101    116     70       O  
ATOM   2057  CB  ASP A 245      26.001   8.387  -8.399  1.00 20.87           C  
ANISOU 2057  CB  ASP A 245     2592   2649   2687    -42    107    180       C  
ATOM   2058  CG  ASP A 245      27.274   7.574  -8.483  1.00 27.71           C  
ANISOU 2058  CG  ASP A 245     3428   3489   3613     -2    180    237       C  
ATOM   2059  OD1 ASP A 245      28.003   7.709  -9.493  1.00 28.66           O  
ANISOU 2059  OD1 ASP A 245     3544   3601   3744     20    244    273       O  
ATOM   2060  OD2 ASP A 245      27.551   6.809  -7.530  1.00 30.69           O  
ANISOU 2060  OD2 ASP A 245     3785   3852   4024      8    174    248       O  
ATOM   2061  N   HIS A 246      23.429  10.114  -9.083  1.00 15.98           N  
ANISOU 2061  N   HIS A 246     2032   2084   1955   -114      0     96       N  
ATOM   2062  CA  HIS A 246      21.969  10.269  -9.127  1.00 15.49           C  
ANISOU 2062  CA  HIS A 246     2009   2041   1837   -146    -39     52       C  
ATOM   2063  C   HIS A 246      21.504  10.639 -10.533  1.00 15.40           C  
ANISOU 2063  C   HIS A 246     2030   2044   1775   -167    -19     47       C  
ATOM   2064  O   HIS A 246      20.479  10.138 -10.994  1.00 15.05           O  
ANISOU 2064  O   HIS A 246     2037   2007   1676   -192    -20     17       O  
ATOM   2065  CB  HIS A 246      21.508  11.368  -8.176  1.00 15.78           C  
ANISOU 2065  CB  HIS A 246     2012   2089   1896   -157   -114     55       C  
ATOM   2066  CG  HIS A 246      21.770  11.078  -6.743  1.00 17.82           C  
ANISOU 2066  CG  HIS A 246     2251   2332   2186   -144   -143     54       C  
ATOM   2067  ND1 HIS A 246      22.203  12.070  -5.882  1.00 19.11           N  
ANISOU 2067  ND1 HIS A 246     2381   2491   2389   -146   -197     75       N  
ATOM   2068  CD2 HIS A 246      21.645   9.920  -6.061  1.00 19.14           C  
ANISOU 2068  CD2 HIS A 246     2434   2488   2352   -134   -129     37       C  
ATOM   2069  CE1 HIS A 246      22.337  11.483  -4.706  1.00 19.83           C  
ANISOU 2069  CE1 HIS A 246     2470   2568   2495   -138   -215     70       C  
ATOM   2070  NE2 HIS A 246      21.998  10.194  -4.760  1.00 20.16           N  
ANISOU 2070  NE2 HIS A 246     2537   2608   2516   -129   -174     48       N  
ATOM   2071  N   VAL A 247      22.246  11.522 -11.204  1.00 15.42           N  
ANISOU 2071  N   VAL A 247     2002   2054   1801   -161    -10     83       N  
ATOM   2072  CA  VAL A 247      21.930  11.926 -12.569  1.00 15.51           C  
ANISOU 2072  CA  VAL A 247     2044   2082   1767   -182     10     85       C  
ATOM   2073  C   VAL A 247      21.958  10.715 -13.495  1.00 16.08           C  
ANISOU 2073  C   VAL A 247     2190   2136   1784   -181     82     65       C  
ATOM   2074  O   VAL A 247      21.051  10.539 -14.308  1.00 16.35           O  
ANISOU 2074  O   VAL A 247     2279   2181   1753   -215     78     42       O  
ATOM   2075  CB  VAL A 247      22.896  13.023 -13.073  1.00 16.23           C  
ANISOU 2075  CB  VAL A 247     2085   2181   1902   -168     18    134       C  
ATOM   2076  CG1 VAL A 247      22.681  13.298 -14.560  1.00 17.00           C  
ANISOU 2076  CG1 VAL A 247     2220   2293   1947   -186     50    137       C  
ATOM   2077  CG2 VAL A 247      22.733  14.297 -12.255  1.00 17.00           C  
ANISOU 2077  CG2 VAL A 247     2124   2290   2044   -177    -57    150       C  
ATOM   2078  N   ASP A 248      22.964   9.855 -13.327  1.00 16.47           N  
ANISOU 2078  N   ASP A 248     2240   2157   1861   -143    144     78       N  
ATOM   2079  CA  ASP A 248      23.084   8.653 -14.146  1.00 17.07           C  
ANISOU 2079  CA  ASP A 248     2398   2205   1885   -134    226     58       C  
ATOM   2080  C   ASP A 248      21.953   7.675 -13.877  1.00 17.14           C  
ANISOU 2080  C   ASP A 248     2470   2205   1838   -164    205      6       C  
ATOM   2081  O   ASP A 248      21.438   7.067 -14.812  1.00 17.79           O  
ANISOU 2081  O   ASP A 248     2636   2275   1848   -189    234    -21       O  
ATOM   2082  CB  ASP A 248      24.433   7.972 -13.911  1.00 18.42           C  
ANISOU 2082  CB  ASP A 248     2546   2342   2111    -81    302     92       C  
ATOM   2083  CG  ASP A 248      25.621   8.798 -14.361  1.00 21.95           C  
ANISOU 2083  CG  ASP A 248     2938   2793   2610    -51    336    155       C  
ATOM   2084  OD1 ASP A 248      25.426   9.733 -15.170  1.00 22.47           O  
ANISOU 2084  OD1 ASP A 248     3003   2881   2652    -70    318    162       O  
ATOM   2085  OD2 ASP A 248      26.742   8.511 -13.904  1.00 24.76           O  
ANISOU 2085  OD2 ASP A 248     3247   3128   3031    -10    376    200       O  
ATOM   2086  N   ILE A 249      21.549   7.528 -12.614  1.00 16.87           N  
ANISOU 2086  N   ILE A 249     2398   2176   1835   -165    152     -6       N  
ATOM   2087  CA  ILE A 249      20.432   6.648 -12.257  1.00 17.46           C  
ANISOU 2087  CA  ILE A 249     2522   2245   1865   -193    126    -48       C  
ATOM   2088  C   ILE A 249      19.119   7.132 -12.904  1.00 16.76           C  
ANISOU 2088  C   ILE A 249     2467   2183   1717   -247     74    -62       C  
ATOM   2089  O   ILE A 249      18.263   6.320 -13.253  1.00 17.06           O  
ANISOU 2089  O   ILE A 249     2569   2212   1701   -279     69    -89       O  
ATOM   2090  CB  ILE A 249      20.323   6.530 -10.715  1.00 19.59           C  
ANISOU 2090  CB  ILE A 249     2738   2517   2187   -177     83    -49       C  
ATOM   2091  CG1 ILE A 249      21.526   5.765 -10.147  1.00 20.92           C  
ANISOU 2091  CG1 ILE A 249     2886   2655   2407   -132    136    -33       C  
ATOM   2092  CG2 ILE A 249      19.034   5.855 -10.297  1.00 21.07           C  
ANISOU 2092  CG2 ILE A 249     2960   2709   2335   -209     42    -82       C  
ATOM   2093  CD1 ILE A 249      21.709   5.942  -8.653  1.00 22.51           C  
ANISOU 2093  CD1 ILE A 249     3018   2864   2672   -115     89    -17       C  
ATOM   2094  N   LEU A 250      18.972   8.455 -13.087  1.00 15.50           N  
ANISOU 2094  N   LEU A 250     2261   2054   1573   -259     32    -39       N  
ATOM   2095  CA  LEU A 250      17.794   9.034 -13.730  1.00 15.60           C  
ANISOU 2095  CA  LEU A 250     2291   2096   1540   -310    -18    -37       C  
ATOM   2096  C   LEU A 250      17.834   8.995 -15.268  1.00 16.87           C  
ANISOU 2096  C   LEU A 250     2518   2255   1636   -339     17    -36       C  
ATOM   2097  O   LEU A 250      16.844   9.354 -15.898  1.00 17.10           O  
ANISOU 2097  O   LEU A 250     2569   2306   1623   -388    -24    -30       O  
ATOM   2098  CB  LEU A 250      17.591  10.474 -13.267  1.00 14.27           C  
ANISOU 2098  CB  LEU A 250     2045   1956   1420   -306    -71    -10       C  
ATOM   2099  CG  LEU A 250      17.215  10.646 -11.808  1.00 14.27           C  
ANISOU 2099  CG  LEU A 250     1998   1957   1467   -288   -113    -14       C  
ATOM   2100  CD1 LEU A 250      17.430  12.094 -11.372  1.00 14.67           C  
ANISOU 2100  CD1 LEU A 250     1986   2022   1567   -275   -148     13       C  
ATOM   2101  CD2 LEU A 250      15.762  10.236 -11.577  1.00 14.78           C  
ANISOU 2101  CD2 LEU A 250     2085   2031   1500   -320   -152    -24       C  
ATOM   2102  N   GLY A 251      18.940   8.525 -15.843  1.00 17.02           N  
ANISOU 2102  N   GLY A 251     2570   2248   1650   -307     94    -36       N  
ATOM   2103  CA  GLY A 251      19.134   8.385 -17.284  1.00 18.15           C  
ANISOU 2103  CA  GLY A 251     2790   2382   1725   -327    142    -36       C  
ATOM   2104  C   GLY A 251      17.975   7.739 -18.021  1.00 19.09           C  
ANISOU 2104  C   GLY A 251     3006   2497   1753   -393    116    -62       C  
ATOM   2105  O   GLY A 251      17.410   8.357 -18.923  1.00 19.38           O  
ANISOU 2105  O   GLY A 251     3064   2557   1743   -440     85    -49       O  
ATOM   2106  N   PRO A 252      17.540   6.528 -17.623  1.00 19.11           N  
ANISOU 2106  N   PRO A 252     3063   2471   1729   -404    118    -95       N  
ATOM   2107  CA  PRO A 252      16.394   5.908 -18.309  1.00 19.24           C  
ANISOU 2107  CA  PRO A 252     3173   2481   1658   -477     81   -113       C  
ATOM   2108  C   PRO A 252      15.110   6.745 -18.294  1.00 18.83           C  
ANISOU 2108  C   PRO A 252     3076   2475   1604   -534    -17    -86       C  
ATOM   2109  O   PRO A 252      14.431   6.798 -19.315  1.00 19.47           O  
ANISOU 2109  O   PRO A 252     3219   2563   1613   -599    -47    -78       O  
ATOM   2110  CB  PRO A 252      16.246   4.562 -17.589  1.00 20.19           C  
ANISOU 2110  CB  PRO A 252     3331   2562   1776   -468     95   -146       C  
ATOM   2111  CG  PRO A 252      17.626   4.268 -17.093  1.00 20.99           C  
ANISOU 2111  CG  PRO A 252     3405   2637   1935   -389    180   -148       C  
ATOM   2112  CD  PRO A 252      18.109   5.617 -16.617  1.00 19.33           C  
ANISOU 2112  CD  PRO A 252     3076   2467   1802   -356    156   -111       C  
ATOM   2113  N   LEU A 253      14.785   7.429 -17.181  1.00 18.06           N  
ANISOU 2113  N   LEU A 253     2874   2407   1582   -512    -65    -66       N  
ATOM   2114  CA  LEU A 253      13.586   8.275 -17.140  1.00 17.83           C  
ANISOU 2114  CA  LEU A 253     2797   2418   1560   -557   -145    -31       C  
ATOM   2115  C   LEU A 253      13.741   9.519 -18.012  1.00 18.44           C  
ANISOU 2115  C   LEU A 253     2847   2525   1635   -570   -153      1       C  
ATOM   2116  O   LEU A 253      12.785   9.977 -18.635  1.00 19.17           O  
ANISOU 2116  O   LEU A 253     2944   2644   1698   -629   -206     32       O  
ATOM   2117  CB  LEU A 253      13.221   8.666 -15.706  1.00 17.36           C  
ANISOU 2117  CB  LEU A 253     2645   2373   1577   -522   -181    -20       C  
ATOM   2118  CG  LEU A 253      12.642   7.523 -14.882  1.00 18.39           C  
ANISOU 2118  CG  LEU A 253     2797   2484   1705   -525   -193    -40       C  
ATOM   2119  CD1 LEU A 253      12.522   7.914 -13.415  1.00 18.47           C  
ANISOU 2119  CD1 LEU A 253     2723   2503   1790   -479   -212    -33       C  
ATOM   2120  CD2 LEU A 253      11.285   7.102 -15.419  1.00 19.76           C  
ANISOU 2120  CD2 LEU A 253     3014   2666   1826   -600   -251    -21       C  
ATOM   2121  N   SER A 254      14.956  10.052 -18.077  1.00 18.35           N  
ANISOU 2121  N   SER A 254     2804   2509   1657   -518   -101      1       N  
ATOM   2122  CA  SER A 254      15.269  11.190 -18.918  1.00 18.83           C  
ANISOU 2122  CA  SER A 254     2840   2596   1720   -525   -100     32       C  
ATOM   2123  C   SER A 254      15.130  10.789 -20.399  1.00 19.74           C  
ANISOU 2123  C   SER A 254     3057   2704   1738   -578    -82     29       C  
ATOM   2124  O   SER A 254      14.617  11.567 -21.210  1.00 20.29           O  
ANISOU 2124  O   SER A 254     3123   2805   1782   -624   -119     61       O  
ATOM   2125  CB  SER A 254      16.703  11.640 -18.638  1.00 19.93           C  
ANISOU 2125  CB  SER A 254     2930   2724   1917   -456    -43     35       C  
ATOM   2126  OG  SER A 254      17.063  12.706 -19.494  1.00 22.09           O  
ANISOU 2126  OG  SER A 254     3179   3022   2193   -461    -39     68       O  
ATOM   2127  N   ALA A 255      15.585   9.585 -20.748  1.00 19.75           N  
ANISOU 2127  N   ALA A 255     3155   2664   1685   -573    -23     -8       N  
ATOM   2128  CA  ALA A 255      15.515   9.100 -22.123  1.00 20.73           C  
ANISOU 2128  CA  ALA A 255     3400   2771   1707   -623      2    -17       C  
ATOM   2129  C   ALA A 255      14.080   8.868 -22.550  1.00 22.35           C  
ANISOU 2129  C   ALA A 255     3655   2991   1848   -715    -82     -7       C  
ATOM   2130  O   ALA A 255      13.724   9.175 -23.692  1.00 22.53           O  
ANISOU 2130  O   ALA A 255     3732   3025   1802   -774   -103     12       O  
ATOM   2131  CB  ALA A 255      16.321   7.819 -22.267  1.00 20.66           C  
ANISOU 2131  CB  ALA A 255     3488   2704   1658   -590     91    -60       C  
ATOM   2132  N   GLN A 256      13.260   8.330 -21.643  1.00 22.99           N  
ANISOU 2132  N   GLN A 256     3714   3069   1952   -729   -131    -13       N  
ATOM   2133  CA  GLN A 256      11.861   8.039 -21.931  1.00 24.03           C  
ANISOU 2133  CA  GLN A 256     3882   3212   2036   -818   -217      9       C  
ATOM   2134  C   GLN A 256      11.033   9.298 -22.174  1.00 23.74           C  
ANISOU 2134  C   GLN A 256     3764   3230   2027   -857   -289     71       C  
ATOM   2135  O   GLN A 256      10.254   9.350 -23.132  1.00 24.91           O  
ANISOU 2135  O   GLN A 256     3964   3390   2109   -941   -342    102       O  
ATOM   2136  CB  GLN A 256      11.252   7.200 -20.805  1.00 26.63           C  
ANISOU 2136  CB  GLN A 256     4192   3527   2398   -813   -246     -4       C  
ATOM   2137  CG  GLN A 256       9.818   6.770 -21.073  1.00 31.24           C  
ANISOU 2137  CG  GLN A 256     4812   4119   2938   -905   -335     28       C  
ATOM   2138  CD  GLN A 256       9.199   6.054 -19.898  1.00 36.62           C  
ANISOU 2138  CD  GLN A 256     5459   4792   3663   -894   -364     25       C  
ATOM   2139  OE1 GLN A 256       9.885   5.560 -18.983  1.00 38.38           O  
ANISOU 2139  OE1 GLN A 256     5664   4991   3928   -825   -312    -15       O  
ATOM   2140  NE2 GLN A 256       7.876   5.983 -19.902  1.00 37.67           N  
ANISOU 2140  NE2 GLN A 256     5577   4944   3791   -964   -450     75       N  
ATOM   2141  N   THR A 257      11.226  10.325 -21.350  1.00 21.63           N  
ANISOU 2141  N   THR A 257     3374   2991   1853   -801   -291     93       N  
ATOM   2142  CA  THR A 257      10.447  11.552 -21.456  1.00 20.74           C  
ANISOU 2142  CA  THR A 257     3177   2924   1780   -828   -352    154       C  
ATOM   2143  C   THR A 257      11.055  12.627 -22.354  1.00 20.66           C  
ANISOU 2143  C   THR A 257     3148   2937   1766   -824   -332    176       C  
ATOM   2144  O   THR A 257      10.367  13.578 -22.708  1.00 21.25           O  
ANISOU 2144  O   THR A 257     3169   3048   1857   -860   -382    231       O  
ATOM   2145  CB  THR A 257      10.244  12.132 -20.061  1.00 21.06           C  
ANISOU 2145  CB  THR A 257     3105   2976   1920   -770   -364    167       C  
ATOM   2146  OG1 THR A 257      11.535  12.470 -19.536  1.00 21.29           O  
ANISOU 2146  OG1 THR A 257     3100   2992   1997   -691   -302    135       O  
ATOM   2147  CG2 THR A 257       9.565  11.151 -19.127  1.00 21.27           C  
ANISOU 2147  CG2 THR A 257     3140   2985   1956   -772   -386    155       C  
ATOM   2148  N   GLY A 258      12.336  12.508 -22.660  1.00 19.65           N  
ANISOU 2148  N   GLY A 258     3055   2787   1625   -777   -256    140       N  
ATOM   2149  CA  GLY A 258      13.033  13.522 -23.440  1.00 19.47           C  
ANISOU 2149  CA  GLY A 258     3007   2784   1606   -763   -230    162       C  
ATOM   2150  C   GLY A 258      13.360  14.765 -22.637  1.00 18.75           C  
ANISOU 2150  C   GLY A 258     2790   2716   1619   -707   -237    188       C  
ATOM   2151  O   GLY A 258      13.782  15.770 -23.207  1.00 18.83           O  
ANISOU 2151  O   GLY A 258     2760   2747   1645   -699   -229    217       O  
ATOM   2152  N   ILE A 259      13.206  14.712 -21.284  1.00 17.30           N  
ANISOU 2152  N   ILE A 259     2544   2524   1504   -664   -249    176       N  
ATOM   2153  CA  ILE A 259      13.516  15.858 -20.450  1.00 17.01           C  
ANISOU 2153  CA  ILE A 259     2404   2499   1558   -614   -257    196       C  
ATOM   2154  C   ILE A 259      14.840  15.605 -19.784  1.00 16.46           C  
ANISOU 2154  C   ILE A 259     2324   2402   1529   -544   -200    163       C  
ATOM   2155  O   ILE A 259      14.980  14.653 -19.015  1.00 16.95           O  
ANISOU 2155  O   ILE A 259     2410   2438   1594   -521   -183    128       O  
ATOM   2156  CB  ILE A 259      12.396  16.138 -19.416  1.00 18.00           C  
ANISOU 2156  CB  ILE A 259     2472   2634   1733   -617   -310    216       C  
ATOM   2157  CG1 ILE A 259      11.064  16.389 -20.148  1.00 19.63           C  
ANISOU 2157  CG1 ILE A 259     2679   2870   1908   -690   -367    267       C  
ATOM   2158  CG2 ILE A 259      12.766  17.336 -18.557  1.00 18.35           C  
ANISOU 2158  CG2 ILE A 259     2428   2682   1863   -565   -312    231       C  
ATOM   2159  CD1 ILE A 259       9.876  16.454 -19.229  1.00 21.54           C  
ANISOU 2159  CD1 ILE A 259     2874   3119   2193   -695   -411    296       C  
ATOM   2160  N   ALA A 260      15.837  16.436 -20.095  1.00 15.60           N  
ANISOU 2160  N   ALA A 260     2177   2297   1452   -512   -172    179       N  
ATOM   2161  CA  ALA A 260      17.170  16.324 -19.512  1.00 15.26           C  
ANISOU 2161  CA  ALA A 260     2111   2229   1457   -449   -123    165       C  
ATOM   2162  C   ALA A 260      17.099  16.416 -17.996  1.00 14.60           C  
ANISOU 2162  C   ALA A 260     1974   2133   1439   -416   -150    154       C  
ATOM   2163  O   ALA A 260      16.278  17.168 -17.463  1.00 14.60           O  
ANISOU 2163  O   ALA A 260     1930   2148   1470   -426   -201    169       O  
ATOM   2164  CB  ALA A 260      18.067  17.431 -20.055  1.00 16.18           C  
ANISOU 2164  CB  ALA A 260     2178   2359   1611   -428   -106    202       C  
ATOM   2165  N   VAL A 261      17.925  15.638 -17.296  1.00 13.65           N  
ANISOU 2165  N   VAL A 261     1862   1984   1340   -375   -114    130       N  
ATOM   2166  CA  VAL A 261      17.923  15.636 -15.837  1.00 13.86           C  
ANISOU 2166  CA  VAL A 261     1849   1997   1422   -346   -140    118       C  
ATOM   2167  C   VAL A 261      18.078  17.028 -15.244  1.00 13.55           C  
ANISOU 2167  C   VAL A 261     1738   1965   1447   -331   -179    145       C  
ATOM   2168  O   VAL A 261      17.313  17.391 -14.351  1.00 14.19           O  
ANISOU 2168  O   VAL A 261     1797   2045   1548   -332   -219    141       O  
ATOM   2169  CB  VAL A 261      18.954  14.647 -15.258  1.00 15.10           C  
ANISOU 2169  CB  VAL A 261     2018   2123   1596   -306    -94     99       C  
ATOM   2170  CG1 VAL A 261      19.013  14.754 -13.744  1.00 14.97           C  
ANISOU 2170  CG1 VAL A 261     1959   2093   1635   -281   -127     92       C  
ATOM   2171  CG2 VAL A 261      18.624  13.214 -15.680  1.00 16.65           C  
ANISOU 2171  CG2 VAL A 261     2294   2303   1728   -321    -58     66       C  
ATOM   2172  N   LEU A 262      19.005  17.831 -15.794  1.00 13.28           N  
ANISOU 2172  N   LEU A 262     1670   1935   1440   -319   -165    175       N  
ATOM   2173  CA  LEU A 262      19.208  19.180 -15.273  1.00 13.56           C  
ANISOU 2173  CA  LEU A 262     1643   1971   1536   -308   -205    201       C  
ATOM   2174  C   LEU A 262      18.028  20.109 -15.552  1.00 13.51           C  
ANISOU 2174  C   LEU A 262     1622   1988   1522   -338   -245    217       C  
ATOM   2175  O   LEU A 262      17.795  21.025 -14.755  1.00 13.73           O  
ANISOU 2175  O   LEU A 262     1616   2008   1595   -329   -281    226       O  
ATOM   2176  CB  LEU A 262      20.526  19.768 -15.738  1.00 13.70           C  
ANISOU 2176  CB  LEU A 262     1625   1988   1594   -288   -184    237       C  
ATOM   2177  CG  LEU A 262      21.765  19.061 -15.162  1.00 15.11           C  
ANISOU 2177  CG  LEU A 262     1797   2140   1806   -252   -152    239       C  
ATOM   2178  CD1 LEU A 262      23.038  19.609 -15.783  1.00 15.85           C  
ANISOU 2178  CD1 LEU A 262     1849   2233   1941   -233   -126    290       C  
ATOM   2179  CD2 LEU A 262      21.832  19.171 -13.652  1.00 15.29           C  
ANISOU 2179  CD2 LEU A 262     1798   2139   1872   -239   -195    228       C  
ATOM   2180  N   ASP A 263      17.252  19.857 -16.630  1.00 13.50           N  
ANISOU 2180  N   ASP A 263     1652   2012   1467   -376   -240    223       N  
ATOM   2181  CA  ASP A 263      16.044  20.647 -16.866  1.00 13.09           C  
ANISOU 2181  CA  ASP A 263     1578   1982   1413   -407   -279    249       C  
ATOM   2182  C   ASP A 263      15.008  20.287 -15.786  1.00 14.28           C  
ANISOU 2182  C   ASP A 263     1734   2122   1570   -405   -304    233       C  
ATOM   2183  O   ASP A 263      14.352  21.181 -15.249  1.00 15.00           O  
ANISOU 2183  O   ASP A 263     1790   2213   1698   -400   -331    254       O  
ATOM   2184  CB  ASP A 263      15.460  20.397 -18.251  1.00 13.77           C  
ANISOU 2184  CB  ASP A 263     1698   2097   1437   -457   -277    267       C  
ATOM   2185  CG  ASP A 263      16.333  20.842 -19.408  1.00 14.89           C  
ANISOU 2185  CG  ASP A 263     1838   2253   1567   -461   -250    288       C  
ATOM   2186  OD1 ASP A 263      17.440  21.396 -19.156  1.00 14.07           O  
ANISOU 2186  OD1 ASP A 263     1696   2137   1512   -423   -234    296       O  
ATOM   2187  OD2 ASP A 263      15.912  20.661 -20.549  1.00 16.19           O  
ANISOU 2187  OD2 ASP A 263     2039   2440   1674   -504   -248    302       O  
ATOM   2188  N   MET A 264      14.883  18.991 -15.442  1.00 13.23           N  
ANISOU 2188  N   MET A 264     1646   1978   1403   -405   -289    199       N  
ATOM   2189  CA  MET A 264      13.973  18.598 -14.358  1.00 12.75           C  
ANISOU 2189  CA  MET A 264     1588   1907   1351   -398   -309    187       C  
ATOM   2190  C   MET A 264      14.443  19.193 -13.029  1.00 13.28           C  
ANISOU 2190  C   MET A 264     1625   1947   1475   -352   -315    177       C  
ATOM   2191  O   MET A 264      13.626  19.638 -12.230  1.00 14.09           O  
ANISOU 2191  O   MET A 264     1712   2041   1599   -342   -334    186       O  
ATOM   2192  CB  MET A 264      13.808  17.085 -14.252  1.00 13.83           C  
ANISOU 2192  CB  MET A 264     1777   2035   1444   -407   -293    155       C  
ATOM   2193  CG  MET A 264      12.620  16.710 -13.385  1.00 14.70           C  
ANISOU 2193  CG  MET A 264     1885   2142   1558   -409   -317    157       C  
ATOM   2194  SD  MET A 264      11.043  17.204 -14.145  1.00 16.49           S  
ANISOU 2194  SD  MET A 264     2095   2401   1771   -463   -356    214       S  
ATOM   2195  CE  MET A 264      10.741  15.784 -15.174  1.00 18.99           C  
ANISOU 2195  CE  MET A 264     2483   2724   2007   -520   -357    202       C  
ATOM   2196  N   CYS A 265      15.767  19.296 -12.823  1.00 12.88           N  
ANISOU 2196  N   CYS A 265     1567   1879   1448   -327   -301    165       N  
ATOM   2197  CA  CYS A 265      16.310  19.936 -11.623  1.00 13.13           C  
ANISOU 2197  CA  CYS A 265     1578   1883   1529   -294   -318    160       C  
ATOM   2198  C   CYS A 265      15.888  21.399 -11.572  1.00 13.37           C  
ANISOU 2198  C   CYS A 265     1576   1912   1591   -295   -343    189       C  
ATOM   2199  O   CYS A 265      15.599  21.895 -10.489  1.00 13.84           O  
ANISOU 2199  O   CYS A 265     1637   1946   1675   -276   -360    183       O  
ATOM   2200  CB  CYS A 265      17.828  19.815 -11.597  1.00 13.18           C  
ANISOU 2200  CB  CYS A 265     1574   1875   1559   -276   -304    160       C  
ATOM   2201  SG  CYS A 265      18.430  18.150 -11.239  1.00 13.95           S  
ANISOU 2201  SG  CYS A 265     1704   1959   1636   -262   -268    129       S  
ATOM   2202  N   ALA A 266      15.814  22.076 -12.734  1.00 13.18           N  
ANISOU 2202  N   ALA A 266     1530   1913   1565   -317   -343    220       N  
ATOM   2203  CA  ALA A 266      15.388  23.477 -12.773  1.00 14.34           C  
ANISOU 2203  CA  ALA A 266     1644   2059   1747   -318   -364    252       C  
ATOM   2204  C   ALA A 266      13.907  23.600 -12.453  1.00 15.13           C  
ANISOU 2204  C   ALA A 266     1744   2162   1842   -323   -370    266       C  
ATOM   2205  O   ALA A 266      13.510  24.582 -11.826  1.00 16.07           O  
ANISOU 2205  O   ALA A 266     1850   2259   1996   -305   -379    280       O  
ATOM   2206  CB  ALA A 266      15.692  24.101 -14.119  1.00 15.34           C  
ANISOU 2206  CB  ALA A 266     1742   2213   1873   -342   -362    287       C  
ATOM   2207  N   SER A 267      13.093  22.600 -12.841  1.00 14.73           N  
ANISOU 2207  N   SER A 267     1711   2133   1750   -346   -364    266       N  
ATOM   2208  CA  SER A 267      11.680  22.574 -12.475  1.00 15.16           C  
ANISOU 2208  CA  SER A 267     1762   2192   1808   -350   -370    290       C  
ATOM   2209  C   SER A 267      11.573  22.402 -10.957  1.00 14.35           C  
ANISOU 2209  C   SER A 267     1678   2053   1723   -308   -364    261       C  
ATOM   2210  O   SER A 267      10.788  23.086 -10.302  1.00 14.65           O  
ANISOU 2210  O   SER A 267     1705   2073   1788   -287   -360    283       O  
ATOM   2211  CB  SER A 267      10.953  21.421 -13.163  1.00 17.63           C  
ANISOU 2211  CB  SER A 267     2095   2533   2072   -390   -373    297       C  
ATOM   2212  OG  SER A 267      10.610  21.744 -14.499  1.00 21.64           O  
ANISOU 2212  OG  SER A 267     2588   3075   2561   -436   -386    337       O  
ATOM   2213  N   LEU A 268      12.371  21.488 -10.401  1.00 13.19           N  
ANISOU 2213  N   LEU A 268     1561   1892   1560   -295   -358    216       N  
ATOM   2214  CA  LEU A 268      12.359  21.248  -8.965  1.00 13.02           C  
ANISOU 2214  CA  LEU A 268     1563   1837   1548   -260   -354    188       C  
ATOM   2215  C   LEU A 268      12.836  22.482  -8.205  1.00 13.76           C  
ANISOU 2215  C   LEU A 268     1657   1895   1678   -233   -363    187       C  
ATOM   2216  O   LEU A 268      12.237  22.854  -7.203  1.00 13.46           O  
ANISOU 2216  O   LEU A 268     1637   1828   1651   -206   -357    187       O  
ATOM   2217  CB  LEU A 268      13.191  20.007  -8.611  1.00 12.54           C  
ANISOU 2217  CB  LEU A 268     1529   1770   1465   -255   -348    147       C  
ATOM   2218  CG  LEU A 268      13.338  19.701  -7.124  1.00 13.38           C  
ANISOU 2218  CG  LEU A 268     1661   1844   1579   -223   -349    118       C  
ATOM   2219  CD1 LEU A 268      11.961  19.546  -6.450  1.00 14.09           C  
ANISOU 2219  CD1 LEU A 268     1760   1930   1665   -209   -341    130       C  
ATOM   2220  CD2 LEU A 268      14.098  18.421  -6.934  1.00 13.76           C  
ANISOU 2220  CD2 LEU A 268     1727   1891   1609   -223   -341     87       C  
ATOM   2221  N   LYS A 269      13.869  23.160  -8.705  1.00 12.82           N  
ANISOU 2221  N   LYS A 269     1523   1773   1577   -241   -375    191       N  
ATOM   2222  CA  LYS A 269      14.363  24.389  -8.097  1.00 12.60           C  
ANISOU 2222  CA  LYS A 269     1498   1707   1582   -225   -392    194       C  
ATOM   2223  C   LYS A 269      13.255  25.446  -8.026  1.00 13.34           C  
ANISOU 2223  C   LYS A 269     1584   1790   1695   -214   -383    224       C  
ATOM   2224  O   LYS A 269      13.062  26.038  -6.976  1.00 13.99           O  
ANISOU 2224  O   LYS A 269     1699   1828   1789   -188   -381    215       O  
ATOM   2225  CB  LYS A 269      15.546  24.917  -8.911  1.00 13.63           C  
ANISOU 2225  CB  LYS A 269     1600   1846   1732   -242   -407    208       C  
ATOM   2226  CG  LYS A 269      16.062  26.292  -8.492  1.00 17.21           C  
ANISOU 2226  CG  LYS A 269     2053   2261   2223   -235   -433    219       C  
ATOM   2227  CD  LYS A 269      17.254  26.664  -9.357  1.00 20.23           C  
ANISOU 2227  CD  LYS A 269     2400   2659   2629   -252   -448    241       C  
ATOM   2228  CE  LYS A 269      17.557  28.150  -9.315  1.00 23.68           C  
ANISOU 2228  CE  LYS A 269     2824   3067   3105   -255   -474    265       C  
ATOM   2229  NZ  LYS A 269      18.553  28.518 -10.362  1.00 25.16           N  
ANISOU 2229  NZ  LYS A 269     2965   3278   3318   -272   -484    298       N  
ATOM   2230  N   GLU A 270      12.479  25.616  -9.107  1.00 13.60           N  
ANISOU 2230  N   GLU A 270     1579   1859   1729   -234   -374    264       N  
ATOM   2231  CA  GLU A 270      11.380  26.581  -9.098  1.00 14.67           C  
ANISOU 2231  CA  GLU A 270     1697   1985   1891   -223   -360    306       C  
ATOM   2232  C   GLU A 270      10.288  26.174  -8.115  1.00 15.62           C  
ANISOU 2232  C   GLU A 270     1841   2088   2007   -194   -335    309       C  
ATOM   2233  O   GLU A 270       9.749  27.026  -7.415  1.00 16.25           O  
ANISOU 2233  O   GLU A 270     1935   2128   2111   -162   -315    324       O  
ATOM   2234  CB  GLU A 270      10.813  26.806 -10.505  1.00 17.51           C  
ANISOU 2234  CB  GLU A 270     2006   2393   2255   -258   -363    358       C  
ATOM   2235  CG  GLU A 270      11.804  27.456 -11.453  1.00 24.81           C  
ANISOU 2235  CG  GLU A 270     2905   3331   3190   -280   -381    365       C  
ATOM   2236  CD  GLU A 270      12.368  28.793 -11.016  1.00 32.43           C  
ANISOU 2236  CD  GLU A 270     3871   4255   4198   -259   -388    367       C  
ATOM   2237  OE1 GLU A 270      11.568  29.730 -10.794  1.00 33.99           O  
ANISOU 2237  OE1 GLU A 270     4059   4431   4426   -243   -375    400       O  
ATOM   2238  OE2 GLU A 270      13.611  28.907 -10.900  1.00 33.71           O  
ANISOU 2238  OE2 GLU A 270     4043   4403   4364   -260   -407    342       O  
ATOM   2239  N   LEU A 271       9.974  24.877  -8.043  1.00 15.19           N  
ANISOU 2239  N   LEU A 271     1794   2056   1921   -203   -333    295       N  
ATOM   2240  CA  LEU A 271       8.984  24.384  -7.082  1.00 15.27           C  
ANISOU 2240  CA  LEU A 271     1824   2050   1928   -174   -309    300       C  
ATOM   2241  C   LEU A 271       9.434  24.628  -5.646  1.00 15.62           C  
ANISOU 2241  C   LEU A 271     1924   2041   1972   -133   -299    258       C  
ATOM   2242  O   LEU A 271       8.598  24.933  -4.792  1.00 17.11           O  
ANISOU 2242  O   LEU A 271     2133   2197   2169    -95   -268    273       O  
ATOM   2243  CB  LEU A 271       8.749  22.894  -7.289  1.00 15.27           C  
ANISOU 2243  CB  LEU A 271     1825   2083   1894   -196   -316    289       C  
ATOM   2244  CG  LEU A 271       7.915  22.555  -8.510  1.00 16.49           C  
ANISOU 2244  CG  LEU A 271     1939   2284   2042   -240   -327    340       C  
ATOM   2245  CD1 LEU A 271       7.962  21.084  -8.777  1.00 16.95           C  
ANISOU 2245  CD1 LEU A 271     2015   2366   2060   -269   -339    316       C  
ATOM   2246  CD2 LEU A 271       6.477  23.030  -8.321  1.00 17.56           C  
ANISOU 2246  CD2 LEU A 271     2042   2418   2211   -226   -308    409       C  
ATOM   2247  N   LEU A 272      10.737  24.490  -5.367  1.00 14.10           N  
ANISOU 2247  N   LEU A 272     1758   1833   1766   -139   -325    211       N  
ATOM   2248  CA  LEU A 272      11.233  24.723  -4.011  1.00 14.76           C  
ANISOU 2248  CA  LEU A 272     1901   1864   1843   -111   -327    173       C  
ATOM   2249  C   LEU A 272      11.164  26.195  -3.655  1.00 16.26           C  
ANISOU 2249  C   LEU A 272     2116   2007   2057    -91   -319    186       C  
ATOM   2250  O   LEU A 272      10.760  26.536  -2.543  1.00 17.01           O  
ANISOU 2250  O   LEU A 272     2267   2053   2144    -57   -297    175       O  
ATOM   2251  CB  LEU A 272      12.669  24.214  -3.869  1.00 14.74           C  
ANISOU 2251  CB  LEU A 272     1912   1860   1829   -130   -362    135       C  
ATOM   2252  CG  LEU A 272      12.797  22.705  -3.843  1.00 16.78           C  
ANISOU 2252  CG  LEU A 272     2166   2148   2063   -139   -361    114       C  
ATOM   2253  CD1 LEU A 272      14.257  22.274  -3.868  1.00 17.63           C  
ANISOU 2253  CD1 LEU A 272     2272   2256   2170   -157   -389     91       C  
ATOM   2254  CD2 LEU A 272      12.062  22.119  -2.657  1.00 18.76           C  
ANISOU 2254  CD2 LEU A 272     2454   2379   2294   -109   -341     99       C  
ATOM   2255  N   GLN A 273      11.531  27.061  -4.599  1.00 16.06           N  
ANISOU 2255  N   GLN A 273     2054   1992   2057   -112   -335    209       N  
ATOM   2256  CA  GLN A 273      11.587  28.499  -4.374  1.00 17.33           C  
ANISOU 2256  CA  GLN A 273     2237   2105   2243    -99   -332    221       C  
ATOM   2257  C   GLN A 273      10.240  29.180  -4.375  1.00 19.69           C  
ANISOU 2257  C   GLN A 273     2527   2390   2565    -68   -283    266       C  
ATOM   2258  O   GLN A 273      10.080  30.197  -3.708  1.00 20.97           O  
ANISOU 2258  O   GLN A 273     2737   2493   2739    -40   -263    267       O  
ATOM   2259  CB  GLN A 273      12.515  29.162  -5.409  1.00 17.71           C  
ANISOU 2259  CB  GLN A 273     2243   2171   2315   -133   -367    234       C  
ATOM   2260  CG  GLN A 273      13.968  28.758  -5.252  1.00 19.36           C  
ANISOU 2260  CG  GLN A 273     2464   2378   2515   -156   -413    202       C  
ATOM   2261  CD  GLN A 273      14.860  29.396  -6.286  1.00 22.80           C  
ANISOU 2261  CD  GLN A 273     2852   2832   2979   -185   -442    225       C  
ATOM   2262  OE1 GLN A 273      14.437  29.745  -7.391  1.00 24.43           O  
ANISOU 2262  OE1 GLN A 273     3006   3075   3202   -196   -430    261       O  
ATOM   2263  NE2 GLN A 273      16.125  29.546  -5.950  1.00 23.28           N  
ANISOU 2263  NE2 GLN A 273     2929   2871   3048   -200   -483    211       N  
ATOM   2264  N   ASN A 274       9.280  28.656  -5.133  1.00 20.29           N  
ANISOU 2264  N   ASN A 274     2545   2516   2649    -75   -264    309       N  
ATOM   2265  CA  ASN A 274       7.976  29.304  -5.249  1.00 21.83           C  
ANISOU 2265  CA  ASN A 274     2714   2704   2878    -49   -218    371       C  
ATOM   2266  C   ASN A 274       6.801  28.527  -4.690  1.00 22.69           C  
ANISOU 2266  C   ASN A 274     2823   2817   2981    -20   -178    397       C  
ATOM   2267  O   ASN A 274       5.697  29.063  -4.637  1.00 23.59           O  
ANISOU 2267  O   ASN A 274     2916   2917   3129     10   -132    457       O  
ATOM   2268  CB  ASN A 274       7.716  29.658  -6.695  1.00 23.76           C  
ANISOU 2268  CB  ASN A 274     2879   2999   3149    -86   -232    426       C  
ATOM   2269  CG  ASN A 274       8.780  30.577  -7.217  1.00 29.54           C  
ANISOU 2269  CG  ASN A 274     3608   3720   3895   -106   -263    411       C  
ATOM   2270  OD1 ASN A 274       8.793  31.778  -6.927  1.00 32.28           O  
ANISOU 2270  OD1 ASN A 274     3974   4019   4271    -83   -247    422       O  
ATOM   2271  ND2 ASN A 274       9.721  30.023  -7.954  1.00 30.78           N  
ANISOU 2271  ND2 ASN A 274     3745   3917   4032   -146   -305    387       N  
ATOM   2272  N   GLY A 275       7.023  27.287  -4.285  1.00 22.59           N  
ANISOU 2272  N   GLY A 275     2828   2823   2932    -28   -193    359       N  
ATOM   2273  CA  GLY A 275       5.948  26.444  -3.791  1.00 22.92           C  
ANISOU 2273  CA  GLY A 275     2865   2874   2970     -5   -161    386       C  
ATOM   2274  C   GLY A 275       5.080  25.943  -4.929  1.00 23.41           C  
ANISOU 2274  C   GLY A 275     2849   2996   3049    -41   -171    452       C  
ATOM   2275  O   GLY A 275       5.379  26.177  -6.111  1.00 23.66           O  
ANISOU 2275  O   GLY A 275     2838   3064   3087    -85   -203    469       O  
ATOM   2276  N  AMET A 276       3.995  25.255  -4.586  0.75 23.76           N  
ANISOU 2276  N  AMET A 276     2877   3051   3100    -24   -146    494       N  
ATOM   2277  N  BMET A 276       3.999  25.241  -4.587  0.25 23.17           N  
ANISOU 2277  N  BMET A 276     2802   2977   3025    -25   -147    494       N  
ATOM   2278  CA AMET A 276       3.106  24.713  -5.607  0.75 24.64           C  
ANISOU 2278  CA AMET A 276     2918   3217   3226    -67   -165    565       C  
ATOM   2279  CA BMET A 276       3.087  24.717  -5.599  0.25 23.44           C  
ANISOU 2279  CA BMET A 276     2766   3065   3075    -66   -165    566       C  
ATOM   2280  C  AMET A 276       1.887  25.618  -5.902  0.75 25.05           C  
ANISOU 2280  C  AMET A 276     2913   3266   3338    -49   -128    668       C  
ATOM   2281  C  BMET A 276       1.968  25.686  -5.984  0.25 24.43           C  
ANISOU 2281  C  BMET A 276     2834   3188   3259    -52   -132    666       C  
ATOM   2282  O  AMET A 276       1.113  25.299  -6.801  0.75 25.20           O  
ANISOU 2282  O  AMET A 276     2868   3330   3374    -92   -151    741       O  
ATOM   2283  O  BMET A 276       1.294  25.437  -6.974  0.25 24.50           O  
ANISOU 2283  O  BMET A 276     2781   3245   3285    -99   -158    734       O  
ATOM   2284  CB AMET A 276       2.723  23.269  -5.272  0.75 25.92           C  
ANISOU 2284  CB AMET A 276     3085   3402   3362    -77   -176    558       C  
ATOM   2285  CB BMET A 276       2.506  23.358  -5.181  0.25 23.19           C  
ANISOU 2285  CB BMET A 276     2735   3053   3025    -70   -168    572       C  
ATOM   2286  CG AMET A 276       3.943  22.341  -5.362  0.75 28.07           C  
ANISOU 2286  CG AMET A 276     3395   3688   3581   -109   -218    471       C  
ATOM   2287  CG BMET A 276       3.463  22.203  -5.391  0.25 23.17           C  
ANISOU 2287  CG BMET A 276     2760   3074   2968   -110   -214    498       C  
ATOM   2288  SD AMET A 276       3.789  20.735  -4.570  0.75 35.78           S  
ANISOU 2288  SD AMET A 276     4400   4671   4525   -105   -223    438       S  
ATOM   2289  SD BMET A 276       2.590  20.634  -5.587  0.25 19.97           S  
ANISOU 2289  SD BMET A 276     2332   2709   2548   -145   -237    531       S  
ATOM   2290  CE AMET A 276       2.500  20.047  -5.545  0.75 30.19           C  
ANISOU 2290  CE AMET A 276     3629   4010   3831   -152   -244    528       C  
ATOM   2291  CE BMET A 276       3.918  19.512  -5.312  0.25 18.54           C  
ANISOU 2291  CE BMET A 276     2208   2526   2310   -159   -263    426       C  
ATOM   2292  N   ASN A 277       1.774  26.783  -5.227  1.00 24.94           N  
ANISOU 2292  N   ASN A 277     2923   3197   3354      8    -75    678       N  
ATOM   2293  CA  ASN A 277       0.711  27.772  -5.473  1.00 25.60           C  
ANISOU 2293  CA  ASN A 277     2954   3270   3503     34    -29    778       C  
ATOM   2294  C   ASN A 277      -0.709  27.189  -5.412  1.00 25.41           C  
ANISOU 2294  C   ASN A 277     2873   3268   3515     43     -4    878       C  
ATOM   2295  O   ASN A 277      -1.567  27.570  -6.209  1.00 26.11           O  
ANISOU 2295  O   ASN A 277     2883   3383   3654     22     -4    980       O  
ATOM   2296  CB  ASN A 277       0.942  28.527  -6.787  1.00 27.55           C  
ANISOU 2296  CB  ASN A 277     3146   3549   3771    -16    -66    811       C  
ATOM   2297  CG  ASN A 277       2.030  29.565  -6.712  1.00 32.36           C  
ANISOU 2297  CG  ASN A 277     3801   4120   4375     -4    -67    749       C  
ATOM   2298  OD1 ASN A 277       3.087  29.452  -7.353  1.00 34.44           O  
ANISOU 2298  OD1 ASN A 277     4070   4407   4607    -50   -120    694       O  
ATOM   2299  ND2 ASN A 277       1.795  30.607  -5.933  1.00 32.85           N  
ANISOU 2299  ND2 ASN A 277     3897   4116   4467     58     -5    760       N  
ATOM   2300  N   GLY A 278      -0.939  26.258  -4.495  1.00 24.04           N  
ANISOU 2300  N   GLY A 278     2732   3084   3318     70     13    856       N  
ATOM   2301  CA  GLY A 278      -2.250  25.630  -4.362  1.00 23.26           C  
ANISOU 2301  CA  GLY A 278     2576   3004   3255     80     34    955       C  
ATOM   2302  C   GLY A 278      -2.558  24.555  -5.391  1.00 22.48           C  
ANISOU 2302  C   GLY A 278     2420   2976   3147     -3    -42    992       C  
ATOM   2303  O   GLY A 278      -3.689  24.070  -5.468  1.00 22.88           O  
ANISOU 2303  O   GLY A 278     2411   3048   3234    -11    -39   1091       O  
ATOM   2304  N  AARG A 279      -1.553  24.151  -6.167  0.50 21.95           N  
ANISOU 2304  N  AARG A 279     2374   2940   3026    -66   -109    916       N  
ATOM   2305  N  BARG A 279      -1.550  24.164  -6.183  0.50 21.71           N  
ANISOU 2305  N  BARG A 279     2343   2909   2996    -67   -110    916       N  
ATOM   2306  CA AARG A 279      -1.722  23.116  -7.173  0.50 21.79           C  
ANISOU 2306  CA AARG A 279     2322   2977   2981   -149   -181    936       C  
ATOM   2307  CA BARG A 279      -1.691  23.135  -7.207  0.50 21.30           C  
ANISOU 2307  CA BARG A 279     2260   2915   2918   -151   -183    935       C  
ATOM   2308  C  AARG A 279      -1.216  21.759  -6.668  0.50 21.02           C  
ANISOU 2308  C  AARG A 279     2276   2883   2826   -159   -206    856       C  
ATOM   2309  C  BARG A 279      -1.203  21.769  -6.683  0.50 20.81           C  
ANISOU 2309  C  BARG A 279     2250   2857   2799   -160   -206    856       C  
ATOM   2310  O  AARG A 279      -0.595  21.677  -5.602  0.50 20.83           O  
ANISOU 2310  O  AARG A 279     2311   2822   2782   -106   -172    780       O  
ATOM   2311  O  BARG A 279      -0.560  21.694  -5.629  0.50 20.66           O  
ANISOU 2311  O  BARG A 279     2290   2801   2759   -107   -173    778       O  
ATOM   2312  CB AARG A 279      -1.035  23.533  -8.485  0.50 23.35           C  
ANISOU 2312  CB AARG A 279     2510   3206   3158   -214   -232    918       C  
ATOM   2313  CB BARG A 279      -0.911  23.540  -8.475  0.50 22.14           C  
ANISOU 2313  CB BARG A 279     2362   3051   2999   -213   -233    907       C  
ATOM   2314  CG AARG A 279      -1.623  24.814  -9.067  0.50 27.22           C  
ANISOU 2314  CG AARG A 279     2938   3698   3709   -211   -214   1010       C  
ATOM   2315  CG BARG A 279      -1.238  24.939  -9.002  0.50 24.89           C  
ANISOU 2315  CG BARG A 279     2661   3395   3403   -205   -212    976       C  
ATOM   2316  CD AARG A 279      -1.199  25.050 -10.505  0.50 31.04           C  
ANISOU 2316  CD AARG A 279     3399   4224   4173   -287   -273   1016       C  
ATOM   2317  CD BARG A 279      -0.110  25.483  -9.868  0.50 27.42           C  
ANISOU 2317  CD BARG A 279     2998   3726   3693   -240   -245    916       C  
ATOM   2318  NE AARG A 279      -1.606  23.954 -11.383  0.50 34.59           N  
ANISOU 2318  NE AARG A 279     3833   4723   4588   -371   -340   1049       N  
ATOM   2319  NE BARG A 279      -0.302  26.894 -10.206  0.50 30.09           N  
ANISOU 2319  NE BARG A 279     3295   4052   4085   -223   -219    973       N  
ATOM   2320  CZ AARG A 279      -2.790  23.867 -11.981  0.50 37.85           C  
ANISOU 2320  CZ AARG A 279     4179   5167   5037   -417   -368   1170       C  
ATOM   2321  CZ BARG A 279       0.680  27.785 -10.306  0.50 31.90           C  
ANISOU 2321  CZ BARG A 279     3550   4260   4310   -209   -213    917       C  
ATOM   2322  NH1AARG A 279      -3.697  24.824 -11.819  0.50 37.97           N  
ANISOU 2322  NH1AARG A 279     4125   5171   5131   -382   -327   1276       N  
ATOM   2323  NH1BARG A 279       1.940  27.424 -10.088  0.50 31.04           N  
ANISOU 2323  NH1BARG A 279     3504   4141   4149   -210   -232    809       N  
ATOM   2324  NH2AARG A 279      -3.068  22.834 -12.764  0.50 38.37           N  
ANISOU 2324  NH2AARG A 279     4248   5272   5060   -501   -437   1190       N  
ATOM   2325  NH2BARG A 279       0.413  29.041 -10.636  0.50 31.90           N  
ANISOU 2325  NH2BARG A 279     3509   4248   4364   -195   -189    976       N  
ATOM   2326  N   THR A 280      -1.531  20.684  -7.398  1.00 20.29           N  
ANISOU 2326  N   THR A 280     2166   2832   2709   -228   -264    879       N  
ATOM   2327  CA  THR A 280      -1.107  19.344  -7.010  1.00 19.70           C  
ANISOU 2327  CA  THR A 280     2139   2762   2585   -242   -287    810       C  
ATOM   2328  C   THR A 280      -0.346  18.658  -8.148  1.00 18.60           C  
ANISOU 2328  C   THR A 280     2026   2653   2386   -320   -349    758       C  
ATOM   2329  O   THR A 280      -0.473  19.032  -9.320  1.00 18.37           O  
ANISOU 2329  O   THR A 280     1972   2652   2356   -377   -384    798       O  
ATOM   2330  CB  THR A 280      -2.305  18.475  -6.574  1.00 21.75           C  
ANISOU 2330  CB  THR A 280     2364   3030   2869   -242   -288    887       C  
ATOM   2331  OG1 THR A 280      -3.207  18.341  -7.675  1.00 22.42           O  
ANISOU 2331  OG1 THR A 280     2391   3154   2973   -315   -340    988       O  
ATOM   2332  CG2 THR A 280      -3.016  19.017  -5.348  1.00 22.81           C  
ANISOU 2332  CG2 THR A 280     2482   3129   3057   -154   -213    936       C  
ATOM   2333  N   ILE A 281       0.475  17.669  -7.786  1.00 17.32           N  
ANISOU 2333  N   ILE A 281     1921   2483   2175   -321   -358    669       N  
ATOM   2334  CA  ILE A 281       1.241  16.844  -8.713  1.00 17.17           C  
ANISOU 2334  CA  ILE A 281     1942   2484   2097   -384   -402    613       C  
ATOM   2335  C   ILE A 281       0.971  15.413  -8.307  1.00 17.06           C  
ANISOU 2335  C   ILE A 281     1954   2471   2059   -398   -418    598       C  
ATOM   2336  O   ILE A 281       1.194  15.057  -7.152  1.00 16.72           O  
ANISOU 2336  O   ILE A 281     1929   2404   2021   -344   -387    558       O  
ATOM   2337  CB  ILE A 281       2.749  17.150  -8.631  1.00 17.81           C  
ANISOU 2337  CB  ILE A 281     2069   2547   2150   -359   -385    514       C  
ATOM   2338  CG1 ILE A 281       3.047  18.602  -9.014  1.00 18.05           C  
ANISOU 2338  CG1 ILE A 281     2075   2576   2209   -346   -371    531       C  
ATOM   2339  CG2 ILE A 281       3.527  16.160  -9.502  1.00 18.38           C  
ANISOU 2339  CG2 ILE A 281     2187   2634   2162   -414   -415    459       C  
ATOM   2340  CD1 ILE A 281       4.518  19.020  -8.861  1.00 18.34           C  
ANISOU 2340  CD1 ILE A 281     2148   2592   2228   -321   -358    447       C  
ATOM   2341  N   LEU A 282       0.390  14.603  -9.206  1.00 17.24           N  
ANISOU 2341  N   LEU A 282     1976   2518   2056   -474   -470    638       N  
ATOM   2342  CA  LEU A 282       0.041  13.212  -8.889  1.00 17.35           C  
ANISOU 2342  CA  LEU A 282     2014   2530   2048   -495   -492    632       C  
ATOM   2343  C   LEU A 282      -0.763  13.066  -7.587  1.00 18.42           C  
ANISOU 2343  C   LEU A 282     2114   2652   2233   -435   -461    674       C  
ATOM   2344  O   LEU A 282      -0.449  12.228  -6.754  1.00 19.49           O  
ANISOU 2344  O   LEU A 282     2279   2771   2354   -406   -446    622       O  
ATOM   2345  CB  LEU A 282       1.267  12.292  -8.890  1.00 16.82           C  
ANISOU 2345  CB  LEU A 282     2020   2448   1923   -498   -488    523       C  
ATOM   2346  CG  LEU A 282       1.936  12.047 -10.240  1.00 17.52           C  
ANISOU 2346  CG  LEU A 282     2157   2547   1952   -564   -518    488       C  
ATOM   2347  CD1 LEU A 282       3.136  11.159 -10.080  1.00 17.37           C  
ANISOU 2347  CD1 LEU A 282     2203   2506   1889   -551   -497    390       C  
ATOM   2348  CD2 LEU A 282       0.969  11.447 -11.235  1.00 18.50           C  
ANISOU 2348  CD2 LEU A 282     2288   2691   2051   -654   -580    555       C  
ATOM   2349  N   GLY A 283      -1.725  13.970  -7.411  1.00 19.57           N  
ANISOU 2349  N   GLY A 283     2195   2802   2437   -412   -443    767       N  
ATOM   2350  CA  GLY A 283      -2.606  13.998  -6.248  1.00 20.20           C  
ANISOU 2350  CA  GLY A 283     2237   2868   2570   -349   -402    826       C  
ATOM   2351  C   GLY A 283      -1.975  14.425  -4.940  1.00 20.33           C  
ANISOU 2351  C   GLY A 283     2283   2848   2593   -257   -334    759       C  
ATOM   2352  O   GLY A 283      -2.567  14.232  -3.877  1.00 21.64           O  
ANISOU 2352  O   GLY A 283     2436   2998   2788   -202   -296    791       O  
ATOM   2353  N  ASER A 284      -0.758  14.973  -4.996  0.75 19.07           N  
ANISOU 2353  N  ASER A 284     2168   2675   2403   -242   -321    668       N  
ATOM   2354  N  BSER A 284      -0.757  14.979  -4.998  0.25 19.33           N  
ANISOU 2354  N  BSER A 284     2200   2707   2436   -242   -321    669       N  
ATOM   2355  CA ASER A 284      -0.061  15.413  -3.798  0.75 18.29           C  
ANISOU 2355  CA ASER A 284     2108   2539   2303   -166   -269    603       C  
ATOM   2356  CA BSER A 284      -0.033  15.409  -3.809  0.25 18.82           C  
ANISOU 2356  CA BSER A 284     2176   2606   2369   -167   -270    601       C  
ATOM   2357  C  ASER A 284       0.123  16.915  -3.823  0.75 18.11           C  
ANISOU 2357  C  ASER A 284     2077   2497   2305   -132   -236    613       C  
ATOM   2358  C  BSER A 284       0.197  16.911  -3.813  0.25 18.48           C  
ANISOU 2358  C  BSER A 284     2128   2543   2350   -132   -236    607       C  
ATOM   2359  O  ASER A 284       0.390  17.488  -4.872  0.75 17.64           O  
ANISOU 2359  O  ASER A 284     2003   2455   2245   -173   -261    621       O  
ATOM   2360  O  BSER A 284       0.554  17.481  -4.841  0.25 18.38           O  
ANISOU 2360  O  BSER A 284     2104   2546   2333   -172   -261    607       O  
ATOM   2361  CB ASER A 284       1.311  14.752  -3.713  0.75 18.83           C  
ANISOU 2361  CB ASER A 284     2234   2600   2319   -177   -285    493       C  
ATOM   2362  CB BSER A 284       1.319  14.705  -3.725  0.25 19.61           C  
ANISOU 2362  CB BSER A 284     2334   2699   2416   -179   -287    492       C  
ATOM   2363  OG ASER A 284       2.022  15.192  -2.566  0.75 20.77           O  
ANISOU 2363  OG ASER A 284     2520   2810   2562   -114   -246    435       O  
ATOM   2364  OG BSER A 284       1.181  13.310  -3.519  0.25 21.27           O  
ANISOU 2364  OG BSER A 284     2558   2918   2605   -199   -308    477       O  
ATOM   2365  N   ALA A 285       0.040  17.547  -2.650  1.00 18.03           N  
ANISOU 2365  N   ALA A 285     2088   2447   2314    -58   -178    607       N  
ATOM   2366  CA  ALA A 285       0.290  18.982  -2.522  1.00 18.74           C  
ANISOU 2366  CA  ALA A 285     2189   2508   2425    -20   -141    606       C  
ATOM   2367  C   ALA A 285       1.728  19.259  -1.985  1.00 18.86           C  
ANISOU 2367  C   ALA A 285     2274   2492   2400     -3   -142    498       C  
ATOM   2368  O   ALA A 285       2.067  20.400  -1.676  1.00 20.19           O  
ANISOU 2368  O   ALA A 285     2469   2625   2578     30   -114    483       O  
ATOM   2369  CB  ALA A 285      -0.755  19.620  -1.623  1.00 19.27           C  
ANISOU 2369  CB  ALA A 285     2244   2542   2537     51    -71    676       C  
ATOM   2370  N   LEU A 286       2.561  18.233  -1.874  1.00 17.88           N  
ANISOU 2370  N   LEU A 286     2180   2377   2235    -26   -174    429       N  
ATOM   2371  CA  LEU A 286       3.951  18.373  -1.497  1.00 18.08           C  
ANISOU 2371  CA  LEU A 286     2259   2381   2229    -22   -186    342       C  
ATOM   2372  C   LEU A 286       4.832  17.526  -2.431  1.00 17.12           C  
ANISOU 2372  C   LEU A 286     2134   2293   2079    -80   -234    299       C  
ATOM   2373  O   LEU A 286       4.316  16.735  -3.234  1.00 17.43           O  
ANISOU 2373  O   LEU A 286     2143   2366   2113   -123   -257    329       O  
ATOM   2374  CB  LEU A 286       4.191  18.099  -0.005  1.00 19.14           C  
ANISOU 2374  CB  LEU A 286     2449   2477   2345     28   -159    300       C  
ATOM   2375  CG  LEU A 286       3.662  16.806   0.562  1.00 21.28           C  
ANISOU 2375  CG  LEU A 286     2717   2762   2607     35   -156    307       C  
ATOM   2376  CD1 LEU A 286       4.491  15.630   0.105  1.00 22.70           C  
ANISOU 2376  CD1 LEU A 286     2898   2969   2759    -12   -201    258       C  
ATOM   2377  CD2 LEU A 286       3.721  16.839   2.088  1.00 22.17           C  
ANISOU 2377  CD2 LEU A 286     2887   2833   2704     92   -120    279       C  
ATOM   2378  N   LEU A 287       6.135  17.757  -2.402  1.00 15.55           N  
ANISOU 2378  N   LEU A 287     1966   2080   1863    -85   -248    238       N  
ATOM   2379  CA  LEU A 287       7.059  17.031  -3.258  1.00 15.39           C  
ANISOU 2379  CA  LEU A 287     1945   2084   1818   -129   -280    201       C  
ATOM   2380  C   LEU A 287       7.339  15.664  -2.641  1.00 15.22           C  
ANISOU 2380  C   LEU A 287     1947   2063   1774   -127   -283    165       C  
ATOM   2381  O   LEU A 287       7.958  15.571  -1.591  1.00 16.81           O  
ANISOU 2381  O   LEU A 287     2180   2238   1970    -98   -277    127       O  
ATOM   2382  CB  LEU A 287       8.323  17.863  -3.459  1.00 16.06           C  
ANISOU 2382  CB  LEU A 287     2044   2153   1904   -131   -290    166       C  
ATOM   2383  CG  LEU A 287       8.026  19.223  -4.104  1.00 18.18           C  
ANISOU 2383  CG  LEU A 287     2287   2422   2198   -134   -287    204       C  
ATOM   2384  CD1 LEU A 287       9.204  20.138  -3.991  1.00 18.93           C  
ANISOU 2384  CD1 LEU A 287     2400   2492   2299   -128   -297    172       C  
ATOM   2385  CD2 LEU A 287       7.575  19.068  -5.566  1.00 19.33           C  
ANISOU 2385  CD2 LEU A 287     2392   2611   2341   -183   -304    244       C  
ATOM   2386  N  AGLU A 288       6.855  14.602  -3.286  0.50 13.98           N  
ANISOU 2386  N  AGLU A 288     1777   1933   1603   -162   -297    179       N  
ATOM   2387  N  BGLU A 288       6.866  14.610  -3.293  0.50 14.00           N  
ANISOU 2387  N  BGLU A 288     1778   1935   1605   -162   -297    179       N  
ATOM   2388  CA AGLU A 288       6.993  13.231  -2.776  0.50 13.48           C  
ANISOU 2388  CA AGLU A 288     1732   1869   1521   -162   -299    150       C  
ATOM   2389  CA BGLU A 288       6.991  13.233  -2.807  0.50 13.54           C  
ANISOU 2389  CA BGLU A 288     1739   1877   1528   -164   -299    151       C  
ATOM   2390  C  AGLU A 288       8.376  12.638  -2.986  0.50 13.16           C  
ANISOU 2390  C  AGLU A 288     1716   1824   1461   -175   -305     93       C  
ATOM   2391  C  BGLU A 288       8.390  12.654  -2.992  0.50 13.22           C  
ANISOU 2391  C  BGLU A 288     1723   1831   1468   -175   -305     93       C  
ATOM   2392  O  AGLU A 288       8.883  12.653  -4.105  0.50 13.26           O  
ANISOU 2392  O  AGLU A 288     1728   1850   1461   -209   -314     87       O  
ATOM   2393  O  BGLU A 288       8.917  12.689  -4.102  0.50 13.37           O  
ANISOU 2393  O  BGLU A 288     1742   1863   1476   -208   -314     86       O  
ATOM   2394  CB AGLU A 288       5.916  12.318  -3.382  0.50 14.44           C  
ANISOU 2394  CB AGLU A 288     1836   2015   1635   -199   -314    192       C  
ATOM   2395  CB BGLU A 288       5.938  12.358  -3.504  0.50 14.59           C  
ANISOU 2395  CB BGLU A 288     1855   2036   1653   -203   -316    192       C  
ATOM   2396  CG AGLU A 288       4.495  12.789  -3.115  0.50 16.46           C  
ANISOU 2396  CG AGLU A 288     2056   2277   1921   -185   -306    266       C  
ATOM   2397  CG BGLU A 288       6.026  10.881  -3.187  0.50 16.96           C  
ANISOU 2397  CG BGLU A 288     2176   2336   1934   -213   -322    166       C  
ATOM   2398  CD AGLU A 288       3.946  12.471  -1.736  0.50 20.85           C  
ANISOU 2398  CD AGLU A 288     2616   2815   2492   -134   -280    276       C  
ATOM   2399  CD BGLU A 288       5.638  10.508  -1.773  0.50 19.50           C  
ANISOU 2399  CD BGLU A 288     2499   2642   2269   -166   -304    167       C  
ATOM   2400  OE1AGLU A 288       4.624  11.747  -0.972  0.50 22.15           O  
ANISOU 2400  OE1AGLU A 288     2810   2966   2640   -115   -275    224       O  
ATOM   2401  OE1BGLU A 288       6.458   9.855  -1.089  0.50 16.00           O  
ANISOU 2401  OE1BGLU A 288     2080   2184   1815   -149   -297    118       O  
ATOM   2402  OE2AGLU A 288       2.824  12.931  -1.426  0.50 21.03           O  
ANISOU 2402  OE2AGLU A 288     2609   2838   2546   -111   -261    343       O  
ATOM   2403  OE2BGLU A 288       4.514  10.867  -1.350  0.50 22.07           O  
ANISOU 2403  OE2BGLU A 288     2800   2969   2618   -145   -293    222       O  
ATOM   2404  N   ASP A 289       8.971  12.078  -1.927  1.00 12.93           N  
ANISOU 2404  N   ASP A 289     1707   1775   1429   -148   -298     58       N  
ATOM   2405  CA  ASP A 289      10.310  11.516  -2.024  1.00 12.60           C  
ANISOU 2405  CA  ASP A 289     1681   1727   1380   -155   -300     16       C  
ATOM   2406  C   ASP A 289      10.423  10.047  -1.666  1.00 13.43           C  
ANISOU 2406  C   ASP A 289     1799   1831   1473   -156   -295     -4       C  
ATOM   2407  O   ASP A 289      11.543   9.594  -1.414  1.00 13.88           O  
ANISOU 2407  O   ASP A 289     1866   1876   1533   -150   -290    -33       O  
ATOM   2408  CB  ASP A 289      11.323  12.330  -1.215  1.00 12.56           C  
ANISOU 2408  CB  ASP A 289     1686   1696   1389   -129   -303     -4       C  
ATOM   2409  CG  ASP A 289      11.288  12.143   0.274  1.00 14.92           C  
ANISOU 2409  CG  ASP A 289     2007   1974   1689    -96   -302    -16       C  
ATOM   2410  OD1 ASP A 289      10.301  11.554   0.778  1.00 14.82           O  
ANISOU 2410  OD1 ASP A 289     1995   1965   1670    -83   -291     -4       O  
ATOM   2411  OD2 ASP A 289      12.243  12.583   0.934  1.00 15.48           O  
ANISOU 2411  OD2 ASP A 289     2094   2023   1766    -86   -313    -34       O  
ATOM   2412  N   GLU A 290       9.296   9.306  -1.633  1.00 13.33           N  
ANISOU 2412  N   GLU A 290     1783   1828   1452   -165   -297     17       N  
ATOM   2413  CA  GLU A 290       9.409   7.892  -1.299  1.00 13.90           C  
ANISOU 2413  CA  GLU A 290     1869   1897   1516   -168   -293     -2       C  
ATOM   2414  C   GLU A 290       9.082   6.995  -2.504  1.00 14.27           C  
ANISOU 2414  C   GLU A 290     1929   1955   1537   -215   -299      2       C  
ATOM   2415  O   GLU A 290       8.544   5.902  -2.363  1.00 14.58           O  
ANISOU 2415  O   GLU A 290     1977   1993   1568   -227   -304      5       O  
ATOM   2416  CB  GLU A 290       8.658   7.524  -0.006  1.00 14.67           C  
ANISOU 2416  CB  GLU A 290     1961   1989   1623   -136   -289     10       C  
ATOM   2417  CG  GLU A 290       9.218   8.275   1.202  1.00 16.76           C  
ANISOU 2417  CG  GLU A 290     2235   2234   1899    -94   -282     -5       C  
ATOM   2418  CD  GLU A 290       8.875   7.717   2.576  1.00 18.56           C  
ANISOU 2418  CD  GLU A 290     2471   2452   2128    -61   -274     -5       C  
ATOM   2419  OE1 GLU A 290       7.986   6.840   2.655  1.00 16.60           O  
ANISOU 2419  OE1 GLU A 290     2213   2215   1880    -64   -272     16       O  
ATOM   2420  OE2 GLU A 290       9.511   8.133   3.572  1.00 19.92           O  
ANISOU 2420  OE2 GLU A 290     2664   2605   2300    -35   -273    -23       O  
ATOM   2421  N   PHE A 291       9.510   7.433  -3.696  1.00 13.63           N  
ANISOU 2421  N   PHE A 291     1857   1881   1443   -244   -300     -1       N  
ATOM   2422  CA  PHE A 291       9.546   6.589  -4.879  1.00 14.24           C  
ANISOU 2422  CA  PHE A 291     1967   1958   1484   -288   -300    -10       C  
ATOM   2423  C   PHE A 291      10.925   6.730  -5.436  1.00 14.69           C  
ANISOU 2423  C   PHE A 291     2040   2004   1537   -282   -273    -41       C  
ATOM   2424  O   PHE A 291      11.307   7.844  -5.781  1.00 15.37           O  
ANISOU 2424  O   PHE A 291     2109   2098   1633   -278   -274    -32       O  
ATOM   2425  CB  PHE A 291       8.614   7.038  -5.997  1.00 14.36           C  
ANISOU 2425  CB  PHE A 291     1984   1994   1479   -337   -326     28       C  
ATOM   2426  CG  PHE A 291       7.153   6.969  -5.703  1.00 15.75           C  
ANISOU 2426  CG  PHE A 291     2136   2184   1665   -352   -355     79       C  
ATOM   2427  CD1 PHE A 291       6.458   5.787  -5.858  1.00 16.87           C  
ANISOU 2427  CD1 PHE A 291     2299   2323   1787   -387   -375     90       C  
ATOM   2428  CD2 PHE A 291       6.457   8.100  -5.333  1.00 17.27           C  
ANISOU 2428  CD2 PHE A 291     2284   2390   1890   -331   -361    122       C  
ATOM   2429  CE1 PHE A 291       5.089   5.746  -5.646  1.00 18.29           C  
ANISOU 2429  CE1 PHE A 291     2449   2518   1984   -404   -406    152       C  
ATOM   2430  CE2 PHE A 291       5.090   8.060  -5.145  1.00 18.48           C  
ANISOU 2430  CE2 PHE A 291     2408   2556   2059   -343   -383    184       C  
ATOM   2431  CZ  PHE A 291       4.414   6.885  -5.307  1.00 18.11           C  
ANISOU 2431  CZ  PHE A 291     2375   2511   1997   -380   -407    202       C  
ATOM   2432  N   THR A 292      11.657   5.637  -5.560  1.00 14.58           N  
ANISOU 2432  N   THR A 292     2058   1971   1510   -281   -247    -71       N  
ATOM   2433  CA  THR A 292      12.980   5.663  -6.157  1.00 14.64           C  
ANISOU 2433  CA  THR A 292     2080   1966   1518   -272   -211    -90       C  
ATOM   2434  C   THR A 292      12.849   5.681  -7.683  1.00 14.39           C  
ANISOU 2434  C   THR A 292     2090   1937   1441   -315   -204    -88       C  
ATOM   2435  O   THR A 292      11.814   5.278  -8.228  1.00 14.19           O  
ANISOU 2435  O   THR A 292     2094   1919   1380   -358   -229    -77       O  
ATOM   2436  CB  THR A 292      13.753   4.380  -5.771  1.00 15.84           C  
ANISOU 2436  CB  THR A 292     2254   2090   1675   -252   -175   -115       C  
ATOM   2437  OG1 THR A 292      13.148   3.243  -6.396  1.00 17.07           O  
ANISOU 2437  OG1 THR A 292     2463   2233   1789   -286   -170   -126       O  
ATOM   2438  CG2 THR A 292      13.836   4.168  -4.275  1.00 15.86           C  
ANISOU 2438  CG2 THR A 292     2222   2088   1715   -217   -184   -116       C  
ATOM   2439  N   PRO A 293      13.938   5.984  -8.406  1.00 14.84           N  
ANISOU 2439  N   PRO A 293     2156   1986   1496   -306   -169    -94       N  
ATOM   2440  CA  PRO A 293      13.897   5.872  -9.875  1.00 14.67           C  
ANISOU 2440  CA  PRO A 293     2189   1964   1422   -345   -154    -96       C  
ATOM   2441  C   PRO A 293      13.499   4.455 -10.322  1.00 15.65           C  
ANISOU 2441  C   PRO A 293     2387   2063   1496   -376   -141   -118       C  
ATOM   2442  O   PRO A 293      12.761   4.300 -11.296  1.00 16.06           O  
ANISOU 2442  O   PRO A 293     2490   2119   1493   -430   -162   -112       O  
ATOM   2443  CB  PRO A 293      15.339   6.206 -10.275  1.00 15.78           C  
ANISOU 2443  CB  PRO A 293     2324   2092   1581   -312   -103    -99       C  
ATOM   2444  CG  PRO A 293      15.801   7.141  -9.190  1.00 16.06           C  
ANISOU 2444  CG  PRO A 293     2285   2138   1679   -274   -122    -83       C  
ATOM   2445  CD  PRO A 293      15.229   6.536  -7.942  1.00 14.54           C  
ANISOU 2445  CD  PRO A 293     2079   1941   1504   -263   -145    -92       C  
ATOM   2446  N   PHE A 294      13.961   3.420  -9.593  1.00 16.05           N  
ANISOU 2446  N   PHE A 294     2447   2087   1564   -347   -111   -139       N  
ATOM   2447  CA APHE A 294      13.614   2.037  -9.947  0.60 17.63           C  
ANISOU 2447  CA APHE A 294     2722   2257   1719   -374    -97   -162       C  
ATOM   2448  CA BPHE A 294      13.625   2.042  -9.943  0.40 17.39           C  
ANISOU 2448  CA BPHE A 294     2692   2227   1690   -374    -96   -162       C  
ATOM   2449  C   PHE A 294      12.129   1.806  -9.755  1.00 17.49           C  
ANISOU 2449  C   PHE A 294     2707   2255   1683   -420   -162   -146       C  
ATOM   2450  O   PHE A 294      11.509   1.147 -10.587  1.00 18.53           O  
ANISOU 2450  O   PHE A 294     2910   2372   1757   -475   -177   -150       O  
ATOM   2451  CB APHE A 294      14.414   1.007  -9.126  0.60 18.71           C  
ANISOU 2451  CB APHE A 294     2858   2362   1888   -329    -50   -182       C  
ATOM   2452  CB BPHE A 294      14.457   1.057  -9.109  0.40 18.14           C  
ANISOU 2452  CB BPHE A 294     2783   2291   1819   -327    -49   -181       C  
ATOM   2453  CG APHE A 294      15.839   0.729  -9.559  0.60 20.73           C  
ANISOU 2453  CG APHE A 294     3135   2587   2155   -291     29   -192       C  
ATOM   2454  CG BPHE A 294      14.453  -0.377  -9.584  0.40 19.78           C  
ANISOU 2454  CG BPHE A 294     3077   2455   1983   -345    -13   -209       C  
ATOM   2455  CD1APHE A 294      16.370   1.325 -10.689  0.60 22.07           C  
ANISOU 2455  CD1APHE A 294     3332   2756   2298   -297     61   -187       C  
ATOM   2456  CD1BPHE A 294      14.237  -0.685 -10.916  0.40 21.21           C  
ANISOU 2456  CD1BPHE A 294     3351   2616   2092   -392      0   -222       C  
ATOM   2457  CD2APHE A 294      16.668  -0.076  -8.794  0.60 22.36           C  
ANISOU 2457  CD2APHE A 294     3325   2768   2404   -247     74   -197       C  
ATOM   2458  CD2BPHE A 294      14.733  -1.411  -8.711  0.40 21.02           C  
ANISOU 2458  CD2BPHE A 294     3229   2587   2170   -316     11   -221       C  
ATOM   2459  CE1APHE A 294      17.685   1.092 -11.061  0.60 23.04           C  
ANISOU 2459  CE1APHE A 294     3467   2849   2437   -255    141   -185       C  
ATOM   2460  CE1BPHE A 294      14.239  -2.002 -11.348  0.40 22.18           C  
ANISOU 2460  CE1BPHE A 294     3569   2690   2170   -411     34   -250       C  
ATOM   2461  CE2APHE A 294      17.988  -0.290  -9.162  0.60 23.26           C  
ANISOU 2461  CE2APHE A 294     3446   2853   2539   -207    151   -191       C  
ATOM   2462  CE2BPHE A 294      14.734  -2.729  -9.147  0.40 21.90           C  
ANISOU 2462  CE2BPHE A 294     3424   2652   2243   -331     47   -246       C  
ATOM   2463  CZ APHE A 294      18.485   0.292 -10.294  0.60 23.11           C  
ANISOU 2463  CZ APHE A 294     3455   2831   2493   -209    187   -184       C  
ATOM   2464  CZ BPHE A 294      14.485  -3.015 -10.461  0.40 21.80           C  
ANISOU 2464  CZ BPHE A 294     3512   2615   2156   -379     59   -263       C  
ATOM   2465  N   ASP A 295      11.540   2.357  -8.678  1.00 16.66           N  
ANISOU 2465  N   ASP A 295     2529   2177   1624   -401   -201   -122       N  
ATOM   2466  CA  ASP A 295      10.103   2.218  -8.410  1.00 16.33           C  
ANISOU 2466  CA  ASP A 295     2476   2153   1577   -437   -259    -92       C  
ATOM   2467  C   ASP A 295       9.308   2.848  -9.537  1.00 17.17           C  
ANISOU 2467  C   ASP A 295     2600   2280   1646   -496   -298    -60       C  
ATOM   2468  O   ASP A 295       8.307   2.286  -9.970  1.00 18.29           O  
ANISOU 2468  O   ASP A 295     2774   2420   1754   -553   -340    -39       O  
ATOM   2469  CB  ASP A 295       9.693   2.913  -7.106  1.00 17.12           C  
ANISOU 2469  CB  ASP A 295     2495   2275   1733   -396   -279    -67       C  
ATOM   2470  CG  ASP A 295      10.224   2.304  -5.838  1.00 18.41           C  
ANISOU 2470  CG  ASP A 295     2638   2425   1933   -346   -256    -88       C  
ATOM   2471  OD1 ASP A 295      10.556   1.095  -5.850  1.00 19.16           O  
ANISOU 2471  OD1 ASP A 295     2773   2493   2015   -349   -234   -113       O  
ATOM   2472  OD2 ASP A 295      10.319   3.037  -4.827  1.00 18.01           O  
ANISOU 2472  OD2 ASP A 295     2535   2386   1922   -306   -260    -78       O  
ATOM   2473  N   VAL A 296       9.741   4.040  -9.998  1.00 16.16           N  
ANISOU 2473  N   VAL A 296     2445   2169   1525   -487   -290    -51       N  
ATOM   2474  CA  VAL A 296       9.047   4.738 -11.073  1.00 16.40           C  
ANISOU 2474  CA  VAL A 296     2485   2222   1524   -542   -327    -16       C  
ATOM   2475  C   VAL A 296       9.068   3.925 -12.358  1.00 18.06           C  
ANISOU 2475  C   VAL A 296     2792   2410   1658   -602   -325    -33       C  
ATOM   2476  O   VAL A 296       8.017   3.731 -12.959  1.00 19.14           O  
ANISOU 2476  O   VAL A 296     2957   2555   1759   -670   -378      0       O  
ATOM   2477  CB  VAL A 296       9.581   6.179 -11.258  1.00 16.18           C  
ANISOU 2477  CB  VAL A 296     2406   2216   1524   -515   -316     -3       C  
ATOM   2478  CG1 VAL A 296       8.940   6.830 -12.468  1.00 16.59           C  
ANISOU 2478  CG1 VAL A 296     2471   2291   1541   -575   -351     35       C  
ATOM   2479  CG2 VAL A 296       9.293   7.003 -10.012  1.00 16.05           C  
ANISOU 2479  CG2 VAL A 296     2309   2216   1572   -468   -328     19       C  
ATOM   2480  N   VAL A 297      10.238   3.395 -12.748  1.00 18.39           N  
ANISOU 2480  N   VAL A 297     2892   2421   1676   -579   -263    -80       N  
ATOM   2481  CA  VAL A 297      10.337   2.563 -13.952  1.00 19.89           C  
ANISOU 2481  CA  VAL A 297     3194   2578   1784   -631   -248   -103       C  
ATOM   2482  C   VAL A 297       9.473   1.298 -13.807  1.00 20.88           C  
ANISOU 2482  C   VAL A 297     3375   2679   1878   -677   -283   -106       C  
ATOM   2483  O   VAL A 297       8.737   0.942 -14.739  1.00 21.36           O  
ANISOU 2483  O   VAL A 297     3512   2732   1873   -755   -325    -93       O  
ATOM   2484  CB  VAL A 297      11.811   2.192 -14.251  1.00 21.55           C  
ANISOU 2484  CB  VAL A 297     3451   2753   1985   -581   -158   -147       C  
ATOM   2485  CG1 VAL A 297      11.910   1.180 -15.391  1.00 22.49           C  
ANISOU 2485  CG1 VAL A 297     3705   2827   2015   -628   -129   -176       C  
ATOM   2486  CG2 VAL A 297      12.640   3.438 -14.563  1.00 22.68           C  
ANISOU 2486  CG2 VAL A 297     3543   2919   2157   -545   -128   -135       C  
ATOM   2487  N   ARG A 298       9.549   0.644 -12.641  1.00 21.24           N  
ANISOU 2487  N   ARG A 298     3385   2714   1970   -634   -271   -119       N  
ATOM   2488  CA  ARG A 298       8.807  -0.585 -12.372  1.00 22.55           C  
ANISOU 2488  CA  ARG A 298     3595   2855   2117   -670   -301   -122       C  
ATOM   2489  C   ARG A 298       7.308  -0.361 -12.501  1.00 22.93           C  
ANISOU 2489  C   ARG A 298     3621   2932   2158   -738   -391    -63       C  
ATOM   2490  O   ARG A 298       6.636  -1.115 -13.208  1.00 22.97           O  
ANISOU 2490  O   ARG A 298     3706   2916   2105   -814   -433    -54       O  
ATOM   2491  CB  ARG A 298       9.156  -1.144 -10.976  1.00 25.03           C  
ANISOU 2491  CB  ARG A 298     3855   3161   2494   -605   -274   -137       C  
ATOM   2492  CG  ARG A 298       8.689  -2.583 -10.744  1.00 29.79           C  
ANISOU 2492  CG  ARG A 298     4514   3728   3077   -632   -286   -150       C  
ATOM   2493  CD  ARG A 298       8.979  -3.085  -9.331  1.00 34.67           C  
ANISOU 2493  CD  ARG A 298     5071   4343   3760   -568   -263   -159       C  
ATOM   2494  NE  ARG A 298      10.404  -3.075  -8.999  1.00 39.16           N  
ANISOU 2494  NE  ARG A 298     5627   4894   4357   -499   -184   -195       N  
ATOM   2495  CZ  ARG A 298      10.970  -2.244  -8.127  1.00 42.47           C  
ANISOU 2495  CZ  ARG A 298     5959   5340   4836   -439   -169   -186       C  
ATOM   2496  NH1 ARG A 298      12.272  -2.306  -7.894  1.00 43.09           N  
ANISOU 2496  NH1 ARG A 298     6028   5401   4942   -386   -104   -208       N  
ATOM   2497  NH2 ARG A 298      10.237  -1.347  -7.482  1.00 42.21           N  
ANISOU 2497  NH2 ARG A 298     5851   5349   4837   -434   -218   -151       N  
ATOM   2498  N   GLN A 299       6.784   0.674 -11.846  1.00 23.07           N  
ANISOU 2498  N   GLN A 299     3535   2995   2235   -715   -421    -16       N  
ATOM   2499  CA  GLN A 299       5.354   0.958 -11.884  1.00 23.81           C  
ANISOU 2499  CA  GLN A 299     3590   3118   2339   -770   -499     56       C  
ATOM   2500  C   GLN A 299       4.900   1.427 -13.238  1.00 25.68           C  
ANISOU 2500  C   GLN A 299     3870   3366   2520   -848   -542     88       C  
ATOM   2501  O   GLN A 299       3.853   0.988 -13.714  1.00 26.69           O  
ANISOU 2501  O   GLN A 299     4029   3494   2619   -928   -611    134       O  
ATOM   2502  CB  GLN A 299       4.957   1.970 -10.809  1.00 23.65           C  
ANISOU 2502  CB  GLN A 299     3452   3136   2398   -713   -503     98       C  
ATOM   2503  CG  GLN A 299       3.447   2.122 -10.708  1.00 23.14           C  
ANISOU 2503  CG  GLN A 299     3338   3097   2356   -760   -573    184       C  
ATOM   2504  CD  GLN A 299       2.957   2.977  -9.576  1.00 22.18           C  
ANISOU 2504  CD  GLN A 299     3113   3003   2311   -699   -567    229       C  
ATOM   2505  OE1 GLN A 299       1.844   3.497  -9.627  1.00 22.38           O  
ANISOU 2505  OE1 GLN A 299     3085   3054   2364   -726   -610    310       O  
ATOM   2506  NE2 GLN A 299       3.758   3.156  -8.534  1.00 20.10           N  
ANISOU 2506  NE2 GLN A 299     2821   2734   2084   -618   -513    185       N  
ATOM   2507  N   CYS A 300       5.691   2.286 -13.886  1.00 26.06           N  
ANISOU 2507  N   CYS A 300     3924   3424   2554   -831   -507     68       N  
ATOM   2508  CA  CYS A 300       5.337   2.786 -15.204  1.00 27.01           C  
ANISOU 2508  CA  CYS A 300     4087   3556   2619   -905   -545     98       C  
ATOM   2509  C   CYS A 300       5.445   1.714 -16.315  1.00 28.98           C  
ANISOU 2509  C   CYS A 300     4480   3763   2769   -979   -552     65       C  
ATOM   2510  O   CYS A 300       4.855   1.899 -17.375  1.00 29.26           O  
ANISOU 2510  O   CYS A 300     4564   3806   2748  -1063   -607    101       O  
ATOM   2511  CB  CYS A 300       6.127   4.045 -15.545  1.00 26.34           C  
ANISOU 2511  CB  CYS A 300     3963   3494   2550   -864   -505     91       C  
ATOM   2512  SG  CYS A 300       5.721   5.471 -14.500  1.00 27.90           S  
ANISOU 2512  SG  CYS A 300     4013   3739   2849   -804   -515    145       S  
ATOM   2513  N   SER A 301       6.132   0.583 -16.063  1.00 30.28           N  
ANISOU 2513  N   SER A 301     4716   3880   2911   -951   -500      1       N  
ATOM   2514  CA  SER A 301       6.245  -0.481 -17.069  1.00 32.04           C  
ANISOU 2514  CA  SER A 301     5089   4050   3035  -1017   -498    -35       C  
ATOM   2515  C   SER A 301       5.465  -1.768 -16.734  1.00 33.71           C  
ANISOU 2515  C   SER A 301     5350   4229   3229  -1066   -546    -31       C  
ATOM   2516  O   SER A 301       5.292  -2.617 -17.604  1.00 34.43           O  
ANISOU 2516  O   SER A 301     5574   4275   3234  -1139   -565    -50       O  
ATOM   2517  CB  SER A 301       7.705  -0.806 -17.369  1.00 33.84           C  
ANISOU 2517  CB  SER A 301     5388   4236   3234   -957   -391   -109       C  
ATOM   2518  OG  SER A 301       8.315  -1.500 -16.296  1.00 36.40           O  
ANISOU 2518  OG  SER A 301     5687   4535   3609   -883   -335   -146       O  
ATOM   2519  N   GLY A 302       5.019  -1.910 -15.491  1.00 34.12           N  
ANISOU 2519  N   GLY A 302     5305   4300   3361  -1026   -563     -6       N  
ATOM   2520  CA  GLY A 302       4.222  -3.058 -15.071  1.00 35.05           C  
ANISOU 2520  CA  GLY A 302     5449   4392   3475  -1069   -613     10       C  
ATOM   2521  C   GLY A 302       4.997  -4.334 -14.820  1.00 35.61           C  
ANISOU 2521  C   GLY A 302     5606   4402   3523  -1038   -550    -62       C  
ATOM   2522  O   GLY A 302       4.571  -5.413 -15.243  1.00 36.15           O  
ANISOU 2522  O   GLY A 302     5777   4425   3534  -1106   -585    -70       O  
ATOM   2523  N   VAL A 303       6.128  -4.228 -14.109  1.00 35.32           N  
ANISOU 2523  N   VAL A 303     5526   4361   3534   -937   -459   -110       N  
ATOM   2524  CA  VAL A 303       6.954  -5.389 -13.780  1.00 35.32           C  
ANISOU 2524  CA  VAL A 303     5589   4304   3526   -896   -389   -171       C  
ATOM   2525  C   VAL A 303       6.215  -6.275 -12.784  1.00 34.93           C  
ANISOU 2525  C   VAL A 303     5504   4249   3518   -901   -431   -151       C  
ATOM   2526  O   VAL A 303       5.658  -5.767 -11.815  1.00 34.71           O  
ANISOU 2526  O   VAL A 303     5357   4270   3563   -873   -466   -105       O  
ATOM   2527  CB  VAL A 303       8.320  -4.942 -13.211  1.00 36.13           C  
ANISOU 2527  CB  VAL A 303     5633   4412   3684   -789   -291   -207       C  
ATOM   2528  CG1 VAL A 303       9.179  -6.136 -12.804  1.00 36.86           C  
ANISOU 2528  CG1 VAL A 303     5777   4448   3782   -742   -215   -257       C  
ATOM   2529  CG2 VAL A 303       9.059  -4.069 -14.209  1.00 36.62           C  
ANISOU 2529  CG2 VAL A 303     5724   4479   3709   -782   -248   -220       C  
ATOM   2530  N  ATHR A 304       6.200  -7.599 -13.004  0.50 34.73           N  
ANISOU 2530  N  ATHR A 304     5584   4163   3449   -934   -424   -183       N  
ATOM   2531  N  BTHR A 304       6.201  -7.585 -13.044  0.50 34.72           N  
ANISOU 2531  N  BTHR A 304     5585   4161   3445   -936   -424   -183       N  
ATOM   2532  CA ATHR A 304       5.514  -8.516 -12.093  0.50 34.97           C  
ANISOU 2532  CA ATHR A 304     5583   4185   3519   -940   -464   -162       C  
ATOM   2533  CA BTHR A 304       5.553  -8.566 -12.184  0.50 34.96           C  
ANISOU 2533  CA BTHR A 304     5595   4178   3510   -944   -461   -167       C  
ATOM   2534  C  ATHR A 304       6.476  -9.352 -11.246  0.50 35.09           C  
ANISOU 2534  C  ATHR A 304     5592   4165   3575   -859   -379   -212       C  
ATOM   2535  C  BTHR A 304       6.556  -9.620 -11.706  0.50 35.18           C  
ANISOU 2535  C  BTHR A 304     5665   4152   3551   -881   -372   -228       C  
ATOM   2536  O  ATHR A 304       6.038 -10.116 -10.384  0.50 34.91           O  
ANISOU 2536  O  ATHR A 304     5537   4136   3592   -853   -403   -199       O  
ATOM   2537  O  BTHR A 304       7.751  -9.347 -11.597  0.50 35.09           O  
ANISOU 2537  O  BTHR A 304     5641   4134   3558   -806   -281   -266       O  
ATOM   2538  CB ATHR A 304       4.532  -9.384 -12.868  0.50 36.14           C  
ANISOU 2538  CB ATHR A 304     5841   4294   3596  -1053   -545   -143       C  
ATOM   2539  CB BTHR A 304       4.394  -9.205 -12.939  0.50 35.98           C  
ANISOU 2539  CB BTHR A 304     5814   4283   3575  -1062   -558   -133       C  
ATOM   2540  OG1ATHR A 304       5.255 -10.142 -13.839  0.50 37.13           O  
ANISOU 2540  OG1ATHR A 304     6127   4346   3633  -1078   -490   -209       O  
ATOM   2541  OG1BTHR A 304       4.903  -9.804 -14.134  0.50 36.92           O  
ANISOU 2541  OG1BTHR A 304     6100   4336   3593  -1110   -526   -187       O  
ATOM   2542  CG2ATHR A 304       3.471  -8.559 -13.555  0.50 36.53           C  
ANISOU 2542  CG2ATHR A 304     5871   4386   3622  -1137   -643    -73       C  
ATOM   2543  CG2BTHR A 304       3.329  -8.196 -13.297  0.50 36.25           C  
ANISOU 2543  CG2BTHR A 304     5784   4376   3615  -1123   -651    -54       C  
TER    2544      THR A 304                                                      
HETATM 2545  S   DMS A 401       6.882 -28.125  21.472  1.00 20.06           S  
ANISOU 2545  S   DMS A 401     2030   2530   3059    142   -223    422       S  
HETATM 2546  O   DMS A 401       7.674 -27.206  22.316  1.00 20.48           O  
ANISOU 2546  O   DMS A 401     2067   2623   3090    170   -213    422       O  
HETATM 2547  C1  DMS A 401       5.955 -27.138  20.370  1.00 19.79           C  
ANISOU 2547  C1  DMS A 401     2054   2497   2971    117   -247    398       C  
HETATM 2548  C2  DMS A 401       5.581 -28.752  22.497  1.00 19.86           C  
ANISOU 2548  C2  DMS A 401     1948   2540   3057    159   -255    493       C  
HETATM 2549  S   DMS A 402       7.044 -21.256  28.847  1.00 48.64           S  
ANISOU 2549  S   DMS A 402     5726   6429   6328    331   -250    516       S  
HETATM 2550  O   DMS A 402       6.922 -22.717  28.688  1.00 48.54           O  
ANISOU 2550  O   DMS A 402     5645   6411   6389    324   -251    544       O  
HETATM 2551  C1  DMS A 402       5.390 -20.729  29.206  1.00 48.61           C  
ANISOU 2551  C1  DMS A 402     5741   6444   6284    381   -224    551       C  
HETATM 2552  C2  DMS A 402       7.732 -21.050  30.463  1.00 48.75           C  
ANISOU 2552  C2  DMS A 402     5761   6466   6296    338   -265    540       C  
HETATM 2553  S   DMS A 403       6.261  -1.076  -6.323  1.00 29.95           S  
ANISOU 2553  S   DMS A 403     4191   3868   3321   -512   -390    -11       S  
HETATM 2554  O   DMS A 403       5.958  -2.533  -6.360  1.00 30.71           O  
ANISOU 2554  O   DMS A 403     4341   3934   3396   -547   -404    -21       O  
HETATM 2555  C1  DMS A 403       7.022  -0.725  -7.858  1.00 30.37           C  
ANISOU 2555  C1  DMS A 403     4314   3907   3317   -546   -369    -43       C  
HETATM 2556  C2  DMS A 403       7.596  -0.894  -5.175  1.00 30.14           C  
ANISOU 2556  C2  DMS A 403     4176   3886   3391   -424   -329    -54       C  
HETATM 2557  S   DMS A 404       2.371 -18.855   7.984  1.00 36.23           S  
ANISOU 2557  S   DMS A 404     4677   4488   4601   -274   -432    179       S  
HETATM 2558  O   DMS A 404       1.975 -20.201   7.546  1.00 36.88           O  
ANISOU 2558  O   DMS A 404     4800   4523   4688   -326   -462    186       O  
HETATM 2559  C1  DMS A 404       3.628 -19.160   9.196  1.00 36.02           C  
ANISOU 2559  C1  DMS A 404     4613   4467   4607   -200   -367    144       C  
HETATM 2560  C2  DMS A 404       1.058 -18.333   9.062  1.00 36.25           C  
ANISOU 2560  C2  DMS A 404     4585   4549   4639   -243   -465    272       C  
HETATM 2561  O   HOH A 501      16.168   1.473  -5.859  1.00 46.52           O  
HETATM 2562  O   HOH A 502      14.078 -19.491  32.277  1.00 41.46           O  
HETATM 2563  O   HOH A 503       6.880  13.380  21.324  1.00 29.25           O  
HETATM 2564  O   HOH A 504      13.998 -10.881  31.006  1.00 35.36           O  
HETATM 2565  O   HOH A 505      -0.912  17.057 -19.539  1.00 38.93           O  
HETATM 2566  O   HOH A 506      -3.061  10.895 -16.794  1.00 40.86           O  
HETATM 2567  O   HOH A 507       6.044   5.803   1.306  1.00 24.97           O  
HETATM 2568  O   HOH A 508       2.799   4.893  20.226  1.00 34.61           O  
HETATM 2569  O   HOH A 509      24.406  -5.758   8.993  1.00 17.99           O  
HETATM 2570  O   HOH A 510      21.426 -20.287  30.771  1.00 23.30           O  
HETATM 2571  O   HOH A 511      11.397  31.677  -2.156  1.00 25.90           O  
HETATM 2572  O   HOH A 512      12.195 -27.051  22.943  1.00 19.83           O  
HETATM 2573  O   HOH A 513      19.756  10.134  -2.112  1.00 30.96           O  
HETATM 2574  O   HOH A 514       5.478 -17.689   1.918  1.00 19.67           O  
HETATM 2575  O   HOH A 515       8.621  24.377 -11.854  1.00 26.34           O  
HETATM 2576  O   HOH A 516       0.090 -17.755  15.613  1.00 35.61           O  
HETATM 2577  O   HOH A 517       9.022 -26.606  14.754  1.00 40.22           O  
HETATM 2578  O   HOH A 518       9.601 -23.263  23.053  1.00 21.34           O  
HETATM 2579  O   HOH A 519       7.168 -26.153   0.208  1.00 33.81           O  
HETATM 2580  O   HOH A 520      16.939  -5.562  33.520  1.00 37.83           O  
HETATM 2581  O   HOH A 521       8.175 -31.641  17.026  1.00 31.45           O  
HETATM 2582  O   HOH A 522      20.485   8.740  25.153  1.00 39.46           O  
HETATM 2583  O   HOH A 523       6.032  -8.497   8.633  1.00 14.96           O  
HETATM 2584  O   HOH A 524      13.232  10.946  19.529  1.00 48.19           O  
HETATM 2585  O   HOH A 525       3.638  22.182  -0.621  1.00 34.15           O  
HETATM 2586  O   HOH A 526       6.136   4.320  21.727  1.00 40.25           O  
HETATM 2587  O   HOH A 527      24.549   4.929  18.980  1.00 27.73           O  
HETATM 2588  O   HOH A 528      21.248 -12.985  34.361  1.00 37.99           O  
HETATM 2589  O   HOH A 529       4.472  26.774  -8.479  1.00 30.69           O  
HETATM 2590  O   HOH A 530      16.252  12.230   7.025  1.00 30.97           O  
HETATM 2591  O   HOH A 531       6.267   8.345  11.973  1.00 33.79           O  
HETATM 2592  O   HOH A 532      14.837  -9.578  -4.136  1.00 34.69           O  
HETATM 2593  O   HOH A 533      23.775 -14.714  27.189  1.00 19.51           O  
HETATM 2594  O   HOH A 534      12.117  31.027  -8.579  1.00 28.22           O  
HETATM 2595  O   HOH A 535      10.798 -24.784   2.844  1.00 18.90           O  
HETATM 2596  O   HOH A 536      18.416 -28.970  20.813  1.00 44.66           O  
HETATM 2597  O   HOH A 537      13.207  23.157 -18.628  1.00 23.28           O  
HETATM 2598  O   HOH A 538       1.305  22.918  -1.525  1.00 39.57           O  
HETATM 2599  O   HOH A 539      13.733 -16.538  32.742  1.00 42.72           O  
HETATM 2600  O   HOH A 540      20.769 -13.106  10.684  1.00 24.31           O  
HETATM 2601  O   HOH A 541       8.621   5.486  22.418  1.00 37.97           O  
HETATM 2602  O   HOH A 542      19.369   9.113   0.911  0.50 21.92           O  
HETATM 2603  O   HOH A 543      20.059  10.278  15.617  1.00 20.33           O  
HETATM 2604  O   HOH A 544      13.595   0.797  -5.476  1.00 24.59           O  
HETATM 2605  O   HOH A 545      15.233  18.533 -21.978  1.00 20.38           O  
HETATM 2606  O   HOH A 546       4.305   7.616  10.196  1.00 32.91           O  
HETATM 2607  O   HOH A 547      28.704   8.986 -11.711  1.00 37.15           O  
HETATM 2608  O   HOH A 548      20.309 -18.432  26.843  1.00 19.13           O  
HETATM 2609  O   HOH A 549      -0.916   1.911  13.421  1.00 31.81           O  
HETATM 2610  O   HOH A 550      22.855  27.060  -0.065  1.00 31.20           O  
HETATM 2611  O   HOH A 551      14.655  26.081   4.261  1.00 21.96           O  
HETATM 2612  O   HOH A 552       3.751   4.190 -18.169  1.00 34.28           O  
HETATM 2613  O   HOH A 553      13.326 -24.508   3.825  1.00 22.78           O  
HETATM 2614  O   HOH A 554      27.169  26.220 -11.432  1.00 21.90           O  
HETATM 2615  O   HOH A 555       9.882  19.723  -0.456  1.00 21.00           O  
HETATM 2616  O   HOH A 556      -3.265  28.392  -8.099  1.00 21.52           O  
HETATM 2617  O   HOH A 557      20.738  21.420   4.165  1.00 27.07           O  
HETATM 2618  O   HOH A 558       6.867 -23.050  20.986  1.00 15.42           O  
HETATM 2619  O   HOH A 559       8.877  28.045  -1.387  1.00 22.94           O  
HETATM 2620  O   HOH A 560       0.113  -1.132  12.039  1.00 27.87           O  
HETATM 2621  O   HOH A 561       2.365  -8.994  18.707  1.00 22.91           O  
HETATM 2622  O   HOH A 562       4.775  24.485 -18.488  1.00 38.08           O  
HETATM 2623  O   HOH A 563      11.512  21.778 -17.020  1.00 21.35           O  
HETATM 2624  O   HOH A 564      -1.260 -19.317  22.131  1.00 37.41           O  
HETATM 2625  O   HOH A 565      23.016   1.706  15.920  1.00 19.55           O  
HETATM 2626  O   HOH A 566      22.194  19.573   0.676  1.00 26.37           O  
HETATM 2627  O   HOH A 567       8.161 -17.907  28.320  1.00 34.19           O  
HETATM 2628  O   HOH A 568       7.958   3.525  -3.456  1.00 17.12           O  
HETATM 2629  O   HOH A 569      15.855 -27.834  12.287  1.00 23.48           O  
HETATM 2630  O   HOH A 570      16.709  28.254 -20.308  1.00 19.84           O  
HETATM 2631  O   HOH A 571       8.450  15.959   1.017  1.00 29.83           O  
HETATM 2632  O   HOH A 572       9.777   6.249   5.698  1.00 15.43           O  
HETATM 2633  O   HOH A 573      17.679 -25.053  30.209  1.00 30.30           O  
HETATM 2634  O   HOH A 574      -5.912  -4.357   9.377  1.00 39.55           O  
HETATM 2635  O   HOH A 575      25.363   9.442  -4.945  1.00 28.46           O  
HETATM 2636  O   HOH A 576      16.878   6.559  -3.938  1.00 17.95           O  
HETATM 2637  O   HOH A 577      12.105 -32.691  16.980  1.00 31.58           O  
HETATM 2638  O   HOH A 578      12.237  21.928   2.499  1.00 20.92           O  
HETATM 2639  O   HOH A 579       9.918 -25.725  22.117  1.00 14.76           O  
HETATM 2640  O   HOH A 580      21.216  28.768  -6.698  1.00 41.88           O  
HETATM 2641  O   HOH A 581      10.267  17.926   1.520  1.00 26.08           O  
HETATM 2642  O   HOH A 582      24.873  29.260  -8.891  1.00 23.50           O  
HETATM 2643  O   HOH A 583      18.869  10.206  13.140  1.00 19.66           O  
HETATM 2644  O   HOH A 584      -1.740 -15.236   2.695  1.00 33.35           O  
HETATM 2645  O   HOH A 585      10.507  -0.544  -3.024  1.00 21.42           O  
HETATM 2646  O   HOH A 586      23.489  22.748 -17.286  1.00 16.05           O  
HETATM 2647  O   HOH A 587      13.322  21.382 -20.851  1.00 26.01           O  
HETATM 2648  O   HOH A 588      18.541  -8.076  -3.408  1.00 40.63           O  
HETATM 2649  O   HOH A 589       8.071   3.586  30.056  1.00 37.79           O  
HETATM 2650  O   HOH A 590      -1.477   3.593  -1.801  1.00 42.67           O  
HETATM 2651  O   HOH A 591       3.602  22.218 -19.191  1.00 32.60           O  
HETATM 2652  O   HOH A 592       9.993 -17.767  -3.963  1.00 21.80           O  
HETATM 2653  O   HOH A 593      22.259  16.293   3.670  1.00 37.29           O  
HETATM 2654  O   HOH A 594      10.599  32.889  -5.240  1.00 50.44           O  
HETATM 2655  O   HOH A 595      13.521  12.427  17.221  1.00 36.62           O  
HETATM 2656  O   HOH A 596      -3.864 -12.103   2.544  1.00 20.32           O  
HETATM 2657  O   HOH A 597      26.359  -5.686  17.729  1.00 34.04           O  
HETATM 2658  O   HOH A 598       0.896 -16.433   2.082  1.00 39.32           O  
HETATM 2659  O   HOH A 599      28.921   9.379 -15.273  1.00 32.13           O  
HETATM 2660  O   HOH A 600      24.011  13.123  -1.655  1.00 31.18           O  
HETATM 2661  O   HOH A 601      21.433  21.717 -18.735  1.00 17.60           O  
HETATM 2662  O   HOH A 602       1.773   1.863   0.024  1.00 26.63           O  
HETATM 2663  O   HOH A 603       7.494 -28.340  15.770  1.00 33.19           O  
HETATM 2664  O   HOH A 604      15.633  -5.640  20.179  1.00 12.60           O  
HETATM 2665  O   HOH A 605      22.115   9.845   5.153  1.00 29.86           O  
HETATM 2666  O   HOH A 606      24.327  -8.927  20.642  1.00 20.53           O  
HETATM 2667  O   HOH A 607      16.826 -18.849   7.693  1.00 18.59           O  
HETATM 2668  O   HOH A 608      28.679  18.724  -8.356  1.00 35.42           O  
HETATM 2669  O   HOH A 609      24.424  -0.652  12.999  1.00 27.63           O  
HETATM 2670  O   HOH A 610      -0.724  22.828  -3.129  1.00 39.81           O  
HETATM 2671  O   HOH A 611      19.959   5.204  -1.851  1.00 27.89           O  
HETATM 2672  O   HOH A 612      15.062  26.996 -12.204  1.00 18.02           O  
HETATM 2673  O   HOH A 613       8.199 -28.395   6.565  1.00 25.90           O  
HETATM 2674  O   HOH A 614       7.788 -24.522  25.639  1.00 18.95           O  
HETATM 2675  O   HOH A 615      10.042  -5.817  25.008  1.00 36.65           O  
HETATM 2676  O   HOH A 616      22.116   2.055   5.700  1.00 36.41           O  
HETATM 2677  O   HOH A 617       3.693 -17.399  20.860  1.00 18.97           O  
HETATM 2678  O   HOH A 618      26.732  23.577  -4.772  1.00 19.11           O  
HETATM 2679  O   HOH A 619       9.585  10.091  -4.896  1.00 12.16           O  
HETATM 2680  O   HOH A 620       1.295 -21.833   9.645  1.00 55.13           O  
HETATM 2681  O   HOH A 621      22.839  -7.292  34.441  1.00 27.63           O  
HETATM 2682  O   HOH A 622      18.961 -27.689   9.426  1.00 43.04           O  
HETATM 2683  O   HOH A 623      21.521  10.599 -17.013  1.00 25.46           O  
HETATM 2684  O   HOH A 624      13.990  14.918  12.502  1.00 32.85           O  
HETATM 2685  O   HOH A 625       1.918 -11.990  25.974  1.00 35.35           O  
HETATM 2686  O   HOH A 626      -4.038  -9.431  16.969  1.00 48.81           O  
HETATM 2687  O   HOH A 627      13.366  19.059   3.371  1.00 28.20           O  
HETATM 2688  O   HOH A 628      24.678   1.909  12.377  1.00 46.47           O  
HETATM 2689  O   HOH A 629      14.580 -25.790  26.928  1.00 17.27           O  
HETATM 2690  O   HOH A 630      15.757 -12.840  31.816  1.00 22.74           O  
HETATM 2691  O   HOH A 631      14.529 -20.206   0.077  1.00 29.75           O  
HETATM 2692  O   HOH A 632      10.744 -23.544   0.343  1.00 18.47           O  
HETATM 2693  O   HOH A 633       2.570  13.675 -20.732  1.00 43.65           O  
HETATM 2694  O   HOH A 634       5.372  -6.477  21.881  1.00 27.60           O  
HETATM 2695  O   HOH A 635       3.140   9.142 -21.338  1.00 30.01           O  
HETATM 2696  O   HOH A 636      19.977 -21.182  28.743  1.00 32.10           O  
HETATM 2697  O   HOH A 637       7.570  12.013   0.722  1.00 33.53           O  
HETATM 2698  O   HOH A 638      12.447  11.173  10.477  1.00 26.80           O  
HETATM 2699  O   HOH A 639      15.757   6.369 -14.440  1.00 24.76           O  
HETATM 2700  O   HOH A 640      17.547  27.500 -12.889  1.00 19.19           O  
HETATM 2701  O   HOH A 641       5.057 -17.229  28.359  1.00 47.39           O  
HETATM 2702  O   HOH A 642      -2.486  12.802 -14.220  1.00 42.13           O  
HETATM 2703  O   HOH A 643      -4.994  23.645  -3.052  1.00 32.21           O  
HETATM 2704  O   HOH A 644      -0.389 -15.332  10.266  1.00 36.06           O  
HETATM 2705  O   HOH A 645       5.665   2.461  -4.750  1.00 17.90           O  
HETATM 2706  O   HOH A 646       5.266 -27.778  14.491  1.00 36.75           O  
HETATM 2707  O   HOH A 647       2.594  25.678 -16.824  1.00 30.95           O  
HETATM 2708  O   HOH A 648      22.547   8.950  -2.317  1.00 43.74           O  
HETATM 2709  O   HOH A 649      15.056  -5.071   0.319  1.00 20.13           O  
HETATM 2710  O   HOH A 650      18.804  -7.696   6.107  1.00 16.54           O  
HETATM 2711  O   HOH A 651       6.258   2.386  -7.542  1.00 22.14           O  
HETATM 2712  O   HOH A 652      25.440 -15.867  12.089  1.00 45.56           O  
HETATM 2713  O   HOH A 653      13.858  31.054  -2.000  1.00 31.40           O  
HETATM 2714  O   HOH A 654       3.992 -22.184   7.072  1.00 17.77           O  
HETATM 2715  O   HOH A 655      16.781   4.789  30.472  1.00 57.67           O  
HETATM 2716  O   HOH A 656      14.653 -22.055  31.952  1.00 32.65           O  
HETATM 2717  O   HOH A 657      13.879   4.396 -20.671  1.00 28.86           O  
HETATM 2718  O   HOH A 658      27.708  -4.709  14.373  1.00 45.60           O  
HETATM 2719  O   HOH A 659      -2.375  19.163 -11.398  1.00 31.14           O  
HETATM 2720  O   HOH A 660       9.946 -10.999  28.175  1.00 34.34           O  
HETATM 2721  O   HOH A 661      16.584   2.526  12.374  1.00 14.44           O  
HETATM 2722  O   HOH A 662       7.870  23.887  -2.281  1.00 26.01           O  
HETATM 2723  O   HOH A 663      15.076  11.269 -25.013  1.00 30.97           O  
HETATM 2724  O   HOH A 664      12.776  -3.174  -5.257  1.00 33.42           O  
HETATM 2725  O   HOH A 665      17.673  16.856  14.835  1.00 35.96           O  
HETATM 2726  O   HOH A 666      -5.618  24.316  -7.513  1.00 20.87           O  
HETATM 2727  O   HOH A 667      29.467  15.778 -12.676  1.00 32.03           O  
HETATM 2728  O   HOH A 668      -2.615  16.225  -9.453  1.00 26.89           O  
HETATM 2729  O   HOH A 669      20.970   6.298  19.867  1.00 27.96           O  
HETATM 2730  O   HOH A 670      22.051 -18.298  38.812  1.00 31.27           O  
HETATM 2731  O   HOH A 671      22.550   7.382 -17.399  1.00 24.21           O  
HETATM 2732  O   HOH A 672      20.505  18.890   3.164  1.00 33.29           O  
HETATM 2733  O   HOH A 673      21.340  -1.629  20.448  1.00 16.34           O  
HETATM 2734  O   HOH A 674      -0.741 -15.736  14.250  1.00 30.76           O  
HETATM 2735  O   HOH A 675      23.323  20.417  -1.600  1.00 29.58           O  
HETATM 2736  O   HOH A 676       1.456   8.663  -6.092  1.00 38.82           O  
HETATM 2737  O   HOH A 677      17.887   4.741  -6.103  1.00 34.71           O  
HETATM 2738  O   HOH A 678      14.269   5.280  22.766  1.00 24.58           O  
HETATM 2739  O   HOH A 679      27.355  20.815  -5.391  1.00 24.25           O  
HETATM 2740  O   HOH A 680       9.720  -1.209  21.229  1.00 30.93           O  
HETATM 2741  O   HOH A 681       2.024  11.322  -5.624  1.00 22.74           O  
HETATM 2742  O   HOH A 682       9.861  24.688  -0.545  1.00 22.75           O  
HETATM 2743  O   HOH A 683      20.486  -1.656  24.001  1.00 24.64           O  
HETATM 2744  O   HOH A 684      23.225   2.694   9.309  1.00 22.82           O  
HETATM 2745  O   HOH A 685      27.418  16.923  -6.933  1.00 31.40           O  
HETATM 2746  O   HOH A 686      16.157 -27.895  23.992  1.00 21.03           O  
HETATM 2747  O   HOH A 687      18.371 -16.308  -2.702  1.00 39.26           O  
HETATM 2748  O   HOH A 688      25.461 -11.702  20.577  1.00 40.43           O  
HETATM 2749  O   HOH A 689      22.395  -0.560  18.161  1.00 15.98           O  
HETATM 2750  O   HOH A 690      11.106 -22.190  32.650  1.00 28.72           O  
HETATM 2751  O   HOH A 691      13.906  15.879 -26.087  1.00 40.25           O  
HETATM 2752  O   HOH A 692       3.233  28.434  -3.275  1.00 28.74           O  
HETATM 2753  O   HOH A 693      22.874  -2.369  16.096  1.00 16.71           O  
HETATM 2754  O   HOH A 694       5.924  -4.719  19.944  1.00 29.98           O  
HETATM 2755  O   HOH A 695      13.872  17.335  10.417  1.00 36.01           O  
HETATM 2756  O   HOH A 696      -3.730  23.139 -15.560  1.00 97.94           O  
HETATM 2757  O   HOH A 697       8.299 -10.717  30.288  1.00 47.50           O  
HETATM 2758  O   HOH A 698      21.543  -1.801  26.438  1.00 47.98           O  
HETATM 2759  O   HOH A 699      18.028 -23.973  26.108  1.00 19.47           O  
HETATM 2760  O   HOH A 700      12.908  18.528 -23.180  1.00 41.68           O  
HETATM 2761  O   HOH A 701       2.949  30.284 -11.274  1.00 37.62           O  
HETATM 2762  O   HOH A 702      20.081 -20.090  16.613  1.00 22.76           O  
HETATM 2763  O   HOH A 703      18.378  30.888  -7.178  1.00 34.12           O  
HETATM 2764  O   HOH A 704       5.351 -31.635  18.500  1.00 40.71           O  
HETATM 2765  O   HOH A 705       0.701  25.514  -2.225  1.00 36.15           O  
HETATM 2766  O   HOH A 706      25.191  16.426 -14.367  1.00 24.82           O  
HETATM 2767  O   HOH A 707      21.234 -13.358   2.280  1.00 27.41           O  
HETATM 2768  O   HOH A 708       7.239  19.679  -0.526  1.00 19.53           O  
HETATM 2769  O   HOH A 709      26.231 -10.821  18.148  1.00 29.32           O  
HETATM 2770  O   HOH A 710      18.272  24.759   5.918  1.00 42.75           O  
HETATM 2771  O   HOH A 711      23.954 -16.170  21.645  1.00 23.30           O  
HETATM 2772  O   HOH A 712      10.555 -16.892  30.368  1.00 33.54           O  
HETATM 2773  O   HOH A 713      -3.214  21.063  -9.741  1.00 34.02           O  
HETATM 2774  O   HOH A 714      -2.136   9.260 -10.450  1.00 40.46           O  
HETATM 2775  O   HOH A 715      11.910 -29.685   8.498  1.00 34.74           O  
HETATM 2776  O   HOH A 716       1.343 -16.891  12.512  1.00 27.31           O  
HETATM 2777  O   HOH A 717      13.914  19.690   7.284  1.00 37.82           O  
HETATM 2778  O   HOH A 718      -0.234  16.076  -0.146  0.50 11.47           O  
HETATM 2779  O   HOH A 719      24.548  -7.687  26.198  1.00 36.32           O  
HETATM 2780  O   HOH A 720      18.171  27.334   4.952  1.00 53.03           O  
HETATM 2781  O   HOH A 721      11.863  12.861  14.635  1.00 54.98           O  
HETATM 2782  O   HOH A 722      19.214  -6.192  32.419  1.00 25.40           O  
HETATM 2783  O   HOH A 723      -0.227   7.570  -3.969  1.00 37.09           O  
HETATM 2784  O   HOH A 724      19.243  12.398  -3.622  1.00 19.12           O  
HETATM 2785  O   HOH A 725      23.410  -6.008   1.926  1.00 25.91           O  
HETATM 2786  O   HOH A 726       7.624  -8.536 -15.424  1.00 46.55           O  
HETATM 2787  O   HOH A 727      23.169  -8.425   4.161  1.00 50.23           O  
HETATM 2788  O   HOH A 728      20.967  16.913 -17.778  1.00 17.97           O  
HETATM 2789  O   HOH A 729       3.435  -8.065  24.643  1.00 37.20           O  
HETATM 2790  O   HOH A 730       2.421 -19.701  21.721  1.00 19.80           O  
HETATM 2791  O   HOH A 731      20.354 -26.799  18.082  1.00 35.93           O  
HETATM 2792  O   HOH A 732      26.885  -9.220  10.443  1.00 44.15           O  
HETATM 2793  O   HOH A 733       1.564  -8.119  21.531  1.00 37.29           O  
HETATM 2794  O   HOH A 734      15.456  24.744   7.786  1.00 37.81           O  
HETATM 2795  O   HOH A 735      27.760  21.772 -11.674  1.00 17.55           O  
HETATM 2796  O   HOH A 736      -5.506  20.181  -8.002  1.00 40.32           O  
HETATM 2797  O   HOH A 737      11.915  15.221   4.229  1.00 32.50           O  
HETATM 2798  O   HOH A 738      30.151  25.265 -10.687  1.00 30.25           O  
HETATM 2799  O   HOH A 739      20.827 -22.801  22.064  1.00 21.95           O  
HETATM 2800  O   HOH A 740      13.583 -14.012  33.010  1.00 38.07           O  
HETATM 2801  O   HOH A 741       0.455   1.284  20.771  1.00 47.74           O  
HETATM 2802  O   HOH A 742      -0.514  19.449 -15.740  1.00 36.34           O  
HETATM 2803  O   HOH A 743      23.836  -4.507  23.876  1.00 50.45           O  
HETATM 2804  O   HOH A 744       3.878  20.684 -21.337  1.00 32.39           O  
HETATM 2805  O   HOH A 745      24.290 -15.929  16.833  1.00 38.93           O  
HETATM 2806  O   HOH A 746      23.201  -5.397  26.412  1.00 24.88           O  
HETATM 2807  O   HOH A 747      26.273  20.548 -14.032  1.00 22.96           O  
HETATM 2808  O   HOH A 748       2.975   2.530  24.921  1.00 30.68           O  
HETATM 2809  O   HOH A 749      10.919 -11.853  30.486  1.00 37.95           O  
HETATM 2810  O   HOH A 750      20.396  13.586   9.082  1.00 33.87           O  
HETATM 2811  O   HOH A 751      11.865   4.048  22.653  1.00 33.22           O  
HETATM 2812  O   HOH A 752      27.729  -7.194  12.023  1.00 36.54           O  
HETATM 2813  O   HOH A 753      17.618  22.329   9.554  1.00 40.97           O  
HETATM 2814  O   HOH A 754       8.941  -7.897  -8.369  1.00 32.94           O  
HETATM 2815  O   HOH A 755      11.761 -29.800  22.589  1.00 19.37           O  
HETATM 2816  O   HOH A 756      28.635  10.717  -8.101  1.00 30.16           O  
HETATM 2817  O   HOH A 757       9.498   1.361  21.295  1.00 24.46           O  
HETATM 2818  O   HOH A 758       9.182  28.999 -17.474  1.00 26.72           O  
HETATM 2819  O   HOH A 759      16.203  30.204  -2.976  1.00 42.95           O  
HETATM 2820  O   HOH A 760      11.088 -31.620  10.226  1.00 43.15           O  
HETATM 2821  O   HOH A 761      20.093 -25.462  22.433  1.00 26.03           O  
HETATM 2822  O   HOH A 762      28.829  14.538  -8.128  1.00 34.41           O  
HETATM 2823  O   HOH A 763       3.441  24.795  -1.613  1.00 34.84           O  
HETATM 2824  O   HOH A 764      20.202  14.527 -19.039  1.00 33.34           O  
HETATM 2825  O   HOH A 765       0.115 -27.182  17.907  1.00 30.24           O  
HETATM 2826  O   HOH A 766       1.044 -16.222  23.465  1.00 44.28           O  
HETATM 2827  O   HOH A 767      -2.627  17.627 -15.519  1.00 60.97           O  
HETATM 2828  O   HOH A 768      16.474   3.496  -7.806  1.00 29.34           O  
HETATM 2829  O   HOH A 769      24.409  -4.330  16.668  1.00 28.43           O  
HETATM 2830  O   HOH A 770      16.789 -18.630  -0.780  1.00 27.06           O  
HETATM 2831  O   HOH A 771      25.012  13.875 -17.225  1.00 25.24           O  
HETATM 2832  O   HOH A 772       6.492  -8.329  -7.853  1.00 39.75           O  
HETATM 2833  O   HOH A 773      20.068  -0.155  -1.012  1.00 35.16           O  
HETATM 2834  O   HOH A 774       0.000  -0.407   0.000  0.50 24.99           O  
HETATM 2835  O   HOH A 775      11.274  -2.559 -16.545  1.00 43.12           O  
HETATM 2836  O   HOH A 776      -1.568   6.148  -2.378  1.00 39.83           O  
HETATM 2837  O   HOH A 777      -4.782  26.408  -9.310  1.00 22.16           O  
HETATM 2838  O   HOH A 778      16.309  -2.605  -2.855  1.00 41.31           O  
HETATM 2839  O   HOH A 779      30.825  20.967  -5.604  1.00 39.69           O  
HETATM 2840  O   HOH A 780      15.578 -19.046  34.790  1.00 41.80           O  
HETATM 2841  O   HOH A 781      -2.125  -3.200  18.826  1.00 41.36           O  
HETATM 2842  O   HOH A 782      23.956 -20.421  20.945  1.00 45.16           O  
HETATM 2843  O   HOH A 783      12.859  22.637   6.077  1.00 35.21           O  
HETATM 2844  O   HOH A 784      25.214  -7.886  22.805  1.00 37.18           O  
HETATM 2845  O   HOH A 785       6.955 -15.138  -8.159  1.00 53.30           O  
HETATM 2846  O   HOH A 786      26.675  27.198  -8.963  1.00 30.23           O  
HETATM 2847  O   HOH A 787       5.969   2.060  28.913  1.00 39.92           O  
HETATM 2848  O   HOH A 788       3.824 -29.082  18.300  1.00 39.98           O  
HETATM 2849  O   HOH A 789       5.982 -23.035  -1.144  1.00 38.34           O  
HETATM 2850  O   HOH A 790       2.922 -18.050   1.197  1.00 32.81           O  
HETATM 2851  O   HOH A 791      21.637  -7.541   6.163  1.00 28.51           O  
HETATM 2852  O   HOH A 792      20.695  25.668   5.052  1.00 48.77           O  
HETATM 2853  O   HOH A 793      21.965 -17.907  23.656  1.00 32.28           O  
HETATM 2854  O   HOH A 794       3.738   9.887  14.440  1.00 38.47           O  
HETATM 2855  O   HOH A 795       7.546 -34.937  19.762  1.00 35.53           O  
HETATM 2856  O   HOH A 796      19.252 -11.117  34.347  1.00 37.85           O  
HETATM 2857  O   HOH A 797      17.203  15.425 -23.516  1.00 36.42           O  
HETATM 2858  O   HOH A 798      25.973  23.296  -2.028  1.00 29.90           O  
HETATM 2859  O   HOH A 799      17.194 -10.402  -5.842  1.00 42.68           O  
HETATM 2860  O   HOH A 800       8.784  -4.353  26.547  1.00 44.39           O  
HETATM 2861  O   HOH A 801      17.638 -17.925  37.524  1.00 49.93           O  
HETATM 2862  O   HOH A 802      12.370  32.802 -12.287  1.00 44.37           O  
HETATM 2863  O   HOH A 803       2.872  -1.757 -11.757  1.00 38.02           O  
HETATM 2864  O   HOH A 804      20.613   4.079  -5.766  1.00 40.55           O  
HETATM 2865  O   HOH A 805      14.640 -29.204   9.936  1.00 30.84           O  
HETATM 2866  O   HOH A 806      17.978 -19.808  33.834  1.00 31.41           O  
HETATM 2867  O   HOH A 807      15.789 -25.802   6.748  1.00 34.39           O  
HETATM 2868  O   HOH A 808       5.765  11.051  11.864  1.00 47.77           O  
HETATM 2869  O   HOH A 809      20.630   8.871  18.299  1.00 34.56           O  
HETATM 2870  O   HOH A 810      28.704  24.207 -12.425  1.00 28.48           O  
HETATM 2871  O   HOH A 811       0.105 -17.197   4.667  1.00 37.28           O  
HETATM 2872  O   HOH A 812      22.401 -22.767  19.930  1.00 34.52           O  
HETATM 2873  O   HOH A 813      18.717 -18.428   1.379  1.00 41.70           O  
HETATM 2874  O   HOH A 814      17.792 -22.269  33.181  1.00 42.81           O  
HETATM 2875  O   HOH A 815      20.668 -22.530  17.546  1.00 24.89           O  
HETATM 2876  O   HOH A 816       7.721  -5.547  22.694  1.00 46.81           O  
HETATM 2877  O   HOH A 817      20.766   5.826 -19.089  1.00 39.70           O  
HETATM 2878  O   HOH A 818      28.111   9.358  -5.026  1.00 37.59           O  
HETATM 2879  O   HOH A 819      25.908 -14.886  15.182  1.00 37.07           O  
HETATM 2880  O   HOH A 820      14.701  -6.924  -4.448  1.00 39.83           O  
HETATM 2881  O   HOH A 821      21.178   6.636  -5.226  1.00 32.30           O  
HETATM 2882  O   HOH A 822      24.874  10.464  -2.477  1.00 28.16           O  
HETATM 2883  O   HOH A 823      -2.947  28.034  -1.971  1.00 40.10           O  
HETATM 2884  O   HOH A 824      14.364  20.232   9.961  1.00 64.02           O  
HETATM 2885  O   HOH A 825       1.998   9.130  -3.466  1.00 43.88           O  
HETATM 2886  O   HOH A 826      11.115  20.848 -19.436  1.00 28.04           O  
HETATM 2887  O   HOH A 827      10.569 -34.359  21.224  1.00 30.05           O  
HETATM 2888  O   HOH A 828       7.992   2.820  22.784  1.00 30.45           O  
HETATM 2889  O   HOH A 829      23.890   6.960  -5.408  1.00 41.41           O  
HETATM 2890  O   HOH A 830      -4.860 -11.927   5.027  1.00 34.53           O  
HETATM 2891  O   HOH A 831      -5.504  22.417  -9.461  1.00 35.31           O  
HETATM 2892  O   HOH A 832      21.823 -25.766  20.312  1.00 35.08           O  
HETATM 2893  O   HOH A 833      24.913   4.376  10.687  1.00 37.92           O  
HETATM 2894  O   HOH A 834       1.269  20.703 -21.897  1.00 32.97           O  
HETATM 2895  O   HOH A 835       3.771  11.637 -21.977  1.00 31.92           O  
HETATM 2896  O   HOH A 836      12.626  24.742 -22.470  1.00 40.86           O  
HETATM 2897  O   HOH A 837      16.595  -4.924  -1.942  1.00 35.09           O  
HETATM 2898  O   HOH A 838      11.940  -2.105 -13.997  1.00 81.21           O  
HETATM 2899  O   HOH A 839      22.261 -14.167   8.754  1.00 42.15           O  
HETATM 2900  O   HOH A 840      25.901   3.885  16.892  1.00 35.17           O  
HETATM 2901  O   HOH A 841       6.955   0.869  24.448  1.00 37.90           O  
HETATM 2902  O   HOH A 842      19.400   7.494  -3.277  1.00 24.50           O  
HETATM 2903  O   HOH A 843      22.943  -1.301  22.523  1.00 28.74           O  
HETATM 2904  O   HOH A 844      -4.289   9.192  -7.451  1.00 33.71           O  
HETATM 2905  O   HOH A 845      24.338   2.535   6.965  1.00 50.58           O  
HETATM 2906  O   HOH A 846      12.482  24.156   3.931  1.00 27.61           O  
HETATM 2907  O   HOH A 847      13.627 -27.685  25.198  1.00 17.11           O  
HETATM 2908  O   HOH A 848      21.105 -20.304  14.193  1.00 35.35           O  
HETATM 2909  O   HOH A 849      22.677 -16.948  26.065  1.00 22.28           O  
HETATM 2910  O   HOH A 850       8.193   2.892 -22.627  1.00 55.19           O  
HETATM 2911  O   HOH A 851      17.203 -26.064  27.384  1.00 25.61           O  
HETATM 2912  O   HOH A 852       6.147  21.871  -1.733  1.00 31.41           O  
HETATM 2913  O   HOH A 853      20.037  -8.416  33.885  1.00 27.89           O  
HETATM 2914  O   HOH A 854      15.046  17.762  14.001  1.00 56.06           O  
HETATM 2915  O   HOH A 855      25.051  -3.698  20.136  1.00 53.04           O  
HETATM 2916  O   HOH A 856      10.109  25.184 -23.031  1.00 38.82           O  
HETATM 2917  O   HOH A 857      27.648  -2.076  15.145  1.00 34.17           O  
HETATM 2918  O   HOH A 858      19.976  14.798 -21.747  1.00 35.44           O  
HETATM 2919  O   HOH A 859      11.374 -33.896  23.985  1.00 24.95           O  
HETATM 2920  O   HOH A 860      25.999  20.692  -1.475  1.00 31.16           O  
HETATM 2921  O   HOH A 861       8.111  -2.686  22.688  1.00 44.34           O  
HETATM 2922  O   HOH A 862      10.912   0.306  23.988  1.00 62.89           O  
HETATM 2923  O   HOH A 863       0.810  22.459 -19.140  1.00 42.26           O  
HETATM 2924  O   HOH A 864       9.569  31.573 -18.134  1.00 44.74           O  
HETATM 2925  O   HOH A 865       4.943   1.282  26.322  1.00 29.80           O  
HETATM 2926  O   HOH A 866       8.400 -28.634   3.942  1.00 32.60           O  
HETATM 2927  O   HOH A 867      13.703  12.434  22.929  1.00 44.31           O  
HETATM 2928  O   HOH A 868      10.378 -27.381   2.773  1.00 30.68           O  
HETATM 2929  O   HOH A 869      28.747  25.438  -4.710  1.00 33.95           O  
HETATM 2930  O   HOH A 870      16.308 -29.927  22.132  1.00 41.46           O  
HETATM 2931  O   HOH A 871      20.530 -15.652   4.907  1.00 37.96           O  
HETATM 2932  O   HOH A 872       1.363 -29.462  16.883  1.00 43.05           O  
HETATM 2933  O   HOH A 873      28.290  -3.921  16.901  1.00 33.06           O  
HETATM 2934  O   HOH A 874      21.119 -26.362  24.834  1.00 28.95           O  
HETATM 2935  O   HOH A 875      27.101  14.413  -1.879  1.00 33.91           O  
HETATM 2936  O   HOH A 876      25.873  21.448 -16.628  1.00 22.36           O  
HETATM 2937  O   HOH A 877      25.161  31.405  -7.246  1.00 39.01           O  
HETATM 2938  O   HOH A 878      25.157  -0.742  15.399  1.00 32.15           O  
HETATM 2939  O   HOH A 879      18.090  -7.289  35.812  1.00 56.43           O  
HETATM 2940  O   HOH A 880      16.073  13.714  23.421  1.00 31.52           O  
HETATM 2941  O   HOH A 881      21.892   0.520  24.913  1.00 47.37           O  
HETATM 2942  O   HOH A 882      10.432  22.183   0.548  1.00 21.18           O  
HETATM 2943  O   HOH A 883      16.365 -11.946  34.322  1.00 44.91           O  
HETATM 2944  O   HOH A 884      14.946 -32.152  15.788  1.00 37.75           O  
HETATM 2945  O   HOH A 885      21.901  12.848 -18.345  1.00 27.03           O  
HETATM 2946  O   HOH A 886      23.819  16.236 -16.712  1.00 22.25           O  
HETATM 2947  O   HOH A 887      24.099  18.963   2.615  1.00 30.17           O  
HETATM 2948  O   HOH A 888      13.977 -31.276  21.409  1.00 26.57           O  
HETATM 2949  O   HOH A 889      24.747  17.900 -18.867  1.00 37.61           O  
HETATM 2950  O   HOH A 890      26.570  31.349  -4.896  1.00 34.25           O  
HETATM 2951  O   HOH A 891      25.523  16.140 -20.792  1.00 39.96           O  
CONECT 2545 2546 2547 2548                                                      
CONECT 2546 2545                                                                
CONECT 2547 2545                                                                
CONECT 2548 2545                                                                
CONECT 2549 2550 2551 2552                                                      
CONECT 2550 2549                                                                
CONECT 2551 2549                                                                
CONECT 2552 2549                                                                
CONECT 2553 2554 2555 2556                                                      
CONECT 2554 2553                                                                
CONECT 2555 2553                                                                
CONECT 2556 2553                                                                
CONECT 2557 2558 2559 2560                                                      
CONECT 2558 2557                                                                
CONECT 2559 2557                                                                
CONECT 2560 2557                                                                
MASTER      307    0    4   11   15    0    7    6 2754    1   16   24          
END