HEADER    MEMBRANE PROTEIN                        11-MAY-20   6Z10              
TITLE     CRYSTAL STRUCTURE OF A HUMANIZED (K18E, K269N) RAT SUCCINATE RECEPTOR 
TITLE    2 SUCNR1 (GPR91) IN COMPLEX WITH A NANOBODY AND ANTAGONIST             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE RECEPTOR 1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 91;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NANOBODY6;                                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: SUCNR1, GPR91;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: VICUGNA PACOS;                                  
SOURCE  10 ORGANISM_TAXID: 30538;                                               
SOURCE  11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    G PROTEIN-COUPLED RECEPTOR GPCR SUCCINATE RECEPTOR, MEMBRANE PROTEIN  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HAFFKE,F.VILLARD                                                    
REVDAT   2   23-SEP-20 6Z10    1       JRNL                                     
REVDAT   1   16-SEP-20 6Z10    0                                                
JRNL        AUTH   J.VELCICKY,R.WILCKEN,S.COTESTA,P.JANSER,A.SCHLAPBACH,        
JRNL        AUTH 2 T.WAGNER,P.PIECHON,F.VILLARD,R.BOUHELAL,F.PILLER,            
JRNL        AUTH 3 S.HARLFINGER,R.STRINGER,D.FEHLMANN,K.KAUPMANN,               
JRNL        AUTH 4 A.LITTLEWOOD-EVANS,M.HAFFKE,N.GOMMERMANN                     
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF NOVEL SUCNR1 INHIBITORS:       
JRNL        TITL 2 DESIGN OF ZWITTERIONIC DERIVATIVES WITH A SALT BRIDGE FOR    
JRNL        TITL 3 THE IMPROVEMENT OF ORAL EXPOSURE.                            
JRNL        REF    J.MED.CHEM.                   V.  63  9856 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   32856916                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.0C01020                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7 (19-MAR-2020)                          
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) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 25647                          
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)  : 0.205                          
REMARK   3   R VALUE            (WORKING SET)  : 0.204                          
REMARK   3   FREE R VALUE                      : 0.223                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.160                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1323                           
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               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.27                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.37                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 12.55                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 487                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2035                   
REMARK   3   BIN FREE R VALUE                        : 0.2071                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.07                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 26                       
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            : 3268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 255                                     
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.76                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.98840                                              
REMARK   3    B22 (A**2) : -5.84560                                             
REMARK   3    B33 (A**2) : 3.85730                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.72540                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.340               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.285               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.204               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.292               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.208               
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      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3594   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4820   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1278   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 566    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3594   ; 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   : 447    ; 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   : 2772   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 12.54                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.2191   23.0206   18.3267           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0281 T22:   -0.1399                                    
REMARK   3     T33:   -0.0125 T12:    0.0054                                    
REMARK   3     T13:    0.0765 T23:    0.0101                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5739 L22:    2.2281                                    
REMARK   3     L33:    0.6897 L12:   -0.3115                                    
REMARK   3     L13:   -0.0784 L23:    0.4213                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0163 S12:    0.0241 S13:    0.0324                     
REMARK   3     S21:   -0.2209 S22:    0.0178 S23:   -0.0417                     
REMARK   3     S31:    0.0079 S32:    0.0514 S33:   -0.0015                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    2.8018   63.9049   24.9163           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0869 T22:   -0.2516                                    
REMARK   3     T33:    0.0080 T12:   -0.0613                                    
REMARK   3     T13:    0.0751 T23:    0.0410                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8416 L22:    6.9541                                    
REMARK   3     L33:    2.3300 L12:    0.0694                                    
REMARK   3     L13:   -0.9349 L23:    2.6162                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0383 S12:    0.0264 S13:    0.1103                     
REMARK   3     S21:   -0.2485 S22:    0.0081 S23:   -0.0995                     
REMARK   3     S31:   -0.1650 S32:    0.1253 S33:    0.0303                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6Z10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292108668.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AUTOPROC                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.269                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.17200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 19.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.27400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6RNK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ADA PH 7.0, 28% (W/V) PEG MME      
REMARK 280  550, 0.55 M (NH4)2SO4, 200 MICROM RAW241, 2% (V/V) DMSO, LIPIDIC    
REMARK 280  CUBIC PHASE, TEMPERATURE 293.15K                                    
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       38.41950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.50150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.41950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       75.50150            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 S    SO4 A 414  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     ASP A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLN A   215                                                      
REMARK 465     GLN A   216                                                      
REMARK 465     GLN A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     THR A   219                                                      
REMARK 465     VAL A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     SER A   258                                                      
REMARK 465     TRP A   259                                                      
REMARK 465     PRO A   260                                                      
REMARK 465     GLN A   261                                                      
REMARK 465     LEU A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     TYR A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     SER A   314                                                      
REMARK 465     PHE A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     LEU A   318                                                      
REMARK 465     GLU A   319                                                      
REMARK 465     VAL A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     PHE A   322                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     PRO A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     HIS A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     HIS A   331                                                      
REMARK 465     HIS A   332                                                      
REMARK 465     HIS A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     TYR B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     TYR B    35                                                      
REMARK 465     GLU B   138                                                      
REMARK 465     VAL B   139                                                      
REMARK 465     LEU B   140                                                      
REMARK 465     PHE B   141                                                      
REMARK 465     GLN B   142                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 214    OG                                                  
REMARK 470     GLU B   9    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 137    CG   CD1  CD2                                       
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    CYS A 168       82.18   -156.65                                   
REMARK 500    ARG B 111      -62.48    -90.71                                   
REMARK 500    ASP B 115       73.42   -151.08                                   
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 609        DISTANCE =  6.05 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A  402                                                       
REMARK 610     OLC A  403                                                       
REMARK 610     OLC A  404                                                       
REMARK 610     OLC A  405                                                       
REMARK 610     OLC A  406                                                       
REMARK 610     OLC A  408                                                       
REMARK 610     OLC A  409                                                       
REMARK 610     OLC A  410                                                       
REMARK 610     OLC A  412                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue Q4T A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 415                  
DBREF  6Z10 A    2   317  UNP    Q6IYF9   SUCR1_RAT        2    317             
DBREF  6Z10 B    1   142  PDB    6Z10     6Z10             1    142             
SEQADV 6Z10 ASP A   -6  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 TYR A   -5  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 LYS A   -4  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 ASP A   -3  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 ASP A   -2  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 ASP A   -1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 ASP A    0  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 LYS A    1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 GLU A   18  UNP  Q6IYF9    LYS    18 ENGINEERED MUTATION            
SEQADV 6Z10 ASN A  269  UNP  Q6IYF9    LYS   269 ENGINEERED MUTATION            
SEQADV 6Z10 LEU A  318  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 GLU A  319  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 VAL A  320  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 LEU A  321  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 PHE A  322  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 GLN A  323  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 GLY A  324  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 PRO A  325  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  326  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  327  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  328  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  329  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  330  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  331  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  332  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  333  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  334  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6Z10 HIS A  335  UNP  Q6IYF9              EXPRESSION TAG                 
SEQRES   1 A  342  ASP TYR LYS ASP ASP ASP ASP LYS ALA GLN ASN LEU SER          
SEQRES   2 A  342  CYS GLU ASN TRP LEU ALA LEU GLU ASN ILE LEU GLU LYS          
SEQRES   3 A  342  TYR TYR LEU SER ALA PHE TYR GLY ILE GLU PHE ILE VAL          
SEQRES   4 A  342  GLY MET LEU GLY ASN PHE THR VAL VAL PHE GLY TYR LEU          
SEQRES   5 A  342  PHE CYS MET LYS ASN TRP ASN SER SER ASN VAL TYR LEU          
SEQRES   6 A  342  PHE ASN LEU SER ILE SER ASP LEU ALA PHE LEU CYS THR          
SEQRES   7 A  342  LEU PRO MET LEU ILE ARG SER TYR ALA THR GLY ASN TRP          
SEQRES   8 A  342  THR TYR GLY ASP VAL LEU CYS ILE SER ASN ARG TYR VAL          
SEQRES   9 A  342  LEU HIS ALA ASN LEU TYR THR SER ILE LEU PHE LEU THR          
SEQRES  10 A  342  PHE ILE SER ILE ASP ARG TYR LEU LEU MET LYS PHE PRO          
SEQRES  11 A  342  PHE ARG GLU HIS ILE LEU GLN LYS LYS GLU PHE ALA ILE          
SEQRES  12 A  342  LEU ILE SER LEU ALA VAL TRP VAL LEU VAL THR LEU GLU          
SEQRES  13 A  342  VAL LEU PRO MET LEU THR PHE ILE THR SER THR PRO ILE          
SEQRES  14 A  342  GLU LYS GLY ASP SER CYS VAL ASP TYR ALA SER SER GLY          
SEQRES  15 A  342  ASN PRO LYS TYR SER LEU ILE TYR SER LEU CYS LEU THR          
SEQRES  16 A  342  LEU LEU GLY PHE LEU ILE PRO LEU SER VAL MET CYS PHE          
SEQRES  17 A  342  PHE TYR TYR LYS MET VAL VAL PHE LEU LYS LYS ARG SER          
SEQRES  18 A  342  GLN GLN GLN ALA THR VAL LEU SER LEU ASN LYS PRO LEU          
SEQRES  19 A  342  ARG LEU VAL VAL LEU ALA VAL VAL ILE PHE SER VAL LEU          
SEQRES  20 A  342  PHE THR PRO TYR HIS ILE MET ARG ASN VAL ARG ILE ALA          
SEQRES  21 A  342  SER ARG LEU ASP SER TRP PRO GLN GLY CYS SER GLN LYS          
SEQRES  22 A  342  ALA ILE ASN CYS LEU TYR ILE LEU THR ARG PRO LEU ALA          
SEQRES  23 A  342  PHE LEU ASN SER ALA VAL ASN PRO ILE PHE TYR PHE LEU          
SEQRES  24 A  342  VAL GLY ASP HIS PHE ARG ASP MET LEU PHE SER LYS LEU          
SEQRES  25 A  342  ARG GLN TYR PHE LYS SER LEU THR SER PHE ARG LEU LEU          
SEQRES  26 A  342  GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS          
SEQRES  27 A  342  HIS HIS HIS HIS                                              
SEQRES   1 B  142  ASP TYR LYS ASP ASP ASP ASP LYS GLU VAL GLN LEU VAL          
SEQRES   2 B  142  GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU          
SEQRES   3 B  142  ARG LEU SER CYS GLU ALA SER GLY TYR THR LEU ALA ASN          
SEQRES   4 B  142  TYR ALA ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU          
SEQRES   5 B  142  ARG GLU GLY VAL SER CYS ILE SER SER GLY GLY SER THR          
SEQRES   6 B  142  VAL TYR SER GLU SER VAL LYS ASP ARG PHE THR ILE SER          
SEQRES   7 B  142  ARG ASP ASN ALA LYS LYS ILE VAL TYR LEU GLN MET ASN          
SEQRES   8 B  142  SER LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA          
SEQRES   9 B  142  ALA ASP PRO PHE GLY GLU ARG LEU CYS ILE ASP PRO ASN          
SEQRES  10 B  142  THR PHE ALA GLY TYR LEU GLU THR TRP GLY GLN GLY THR          
SEQRES  11 B  142  GLN VAL THR VAL SER SER LEU GLU VAL LEU PHE GLN              
HET    Q4T  A 401      36                                                       
HET    OLC  A 402      19                                                       
HET    OLC  A 403      19                                                       
HET    OLC  A 404      15                                                       
HET    OLC  A 405      21                                                       
HET    OLC  A 406      14                                                       
HET    OLC  A 407      25                                                       
HET    OLC  A 408      10                                                       
HET    OLC  A 409      12                                                       
HET    OLC  A 410      11                                                       
HET    OLC  A 411      25                                                       
HET    OLC  A 412      17                                                       
HET    OLC  A 413      25                                                       
HET    SO4  A 414       5                                                       
HET     CL  A 415       1                                                       
HETNAM     Q4T 2-[2-[[3-[4-CHLORANYL-2-FLUORANYL-5-[(3~{R})-PIPERIDIN-          
HETNAM   2 Q4T  3-YL]OXY-PHENYL]-2-FLUORANYL-PHENYL]CARBONYLAMINO]-5-           
HETNAM   3 Q4T  FLUORANYL-PHENYL]ETHANOIC ACID                                  
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  Q4T    C26 H22 CL F3 N2 O4                                          
FORMUL   4  OLC    12(C21 H40 O4)                                               
FORMUL  16  SO4    O4 S 2-                                                      
FORMUL  17   CL    CL 1-                                                        
FORMUL  18  HOH   *154(H2 O)                                                    
HELIX    1 AA1 CYS A    7  TYR A   20  1                                  14    
HELIX    2 AA2 TYR A   20  MET A   48  1                                  29    
HELIX    3 AA3 ASN A   52  GLY A   82  1                                  31    
HELIX    4 AA4 GLY A   87  PHE A  122  1                                  36    
HELIX    5 AA5 HIS A  127  GLN A  130  5                                   4    
HELIX    6 AA6 LYS A  131  THR A  160  1                                  30    
HELIX    7 AA7 PRO A  161  GLY A  165  5                                   5    
HELIX    8 AA8 ASN A  176  PHE A  192  1                                  17    
HELIX    9 AA9 PHE A  192  SER A  214  1                                  23    
HELIX   10 AB1 LYS A  225  SER A  254  1                                  30    
HELIX   11 AB2 CYS A  263  LEU A  281  1                                  19    
HELIX   12 AB3 LEU A  281  ASN A  286  1                                   6    
HELIX   13 AB4 PRO A  287  LEU A  292  5                                   6    
HELIX   14 AB5 HIS A  296  LYS A  304  1                                   9    
HELIX   15 AB6 GLN B   94  THR B   98  5                                   5    
HELIX   16 AB7 ARG B  111  ILE B  114  5                                   4    
HELIX   17 AB8 ASP B  115  ALA B  120  1                                   6    
HELIX   18 AB9 GLY B  121  LEU B  123  5                                   3    
SHEET    1 AA1 4 GLN B  11  SER B  15  0                                        
SHEET    2 AA1 4 LEU B  26  SER B  33 -1  O  GLU B  31   N  VAL B  13           
SHEET    3 AA1 4 ILE B  85  MET B  90 -1  O  MET B  90   N  LEU B  26           
SHEET    4 AA1 4 PHE B  75  ASP B  80 -1  N  THR B  76   O  GLN B  89           
SHEET    1 AA2 6 LEU B  19  VAL B  20  0                                        
SHEET    2 AA2 6 THR B 130  VAL B 134  1  O  THR B 133   N  VAL B  20           
SHEET    3 AA2 6 ALA B  99  ASP B 106 -1  N  TYR B 101   O  THR B 130           
SHEET    4 AA2 6 ALA B  41  GLN B  47 -1  N  PHE B  45   O  TYR B 102           
SHEET    5 AA2 6 GLU B  54  ILE B  59 -1  O  SER B  57   N  TRP B  44           
SHEET    6 AA2 6 THR B  65  TYR B  67 -1  O  VAL B  66   N  CYS B  58           
SHEET    1 AA3 4 LEU B  19  VAL B  20  0                                        
SHEET    2 AA3 4 THR B 130  VAL B 134  1  O  THR B 133   N  VAL B  20           
SHEET    3 AA3 4 ALA B  99  ASP B 106 -1  N  TYR B 101   O  THR B 130           
SHEET    4 AA3 4 THR B 125  TRP B 126 -1  O  THR B 125   N  ALA B 105           
SSBOND   1 CYS A    7    CYS A  263                          1555   1555  2.04  
SSBOND   2 CYS A   91    CYS A  168                          1555   1555  2.05  
SSBOND   3 CYS B   30    CYS B  103                          1555   1555  2.04  
SSBOND   4 CYS B   58    CYS B  113                          1555   1555  2.07  
SITE     1 AC1 13 TYR A  26  LEU A  75  SER A  78  TYR A  79                    
SITE     2 AC1 13 TRP A  84  ASN A  94  ARG A  95  LEU A  98                    
SITE     3 AC1 13 CYS A 168  TYR A 244  ARG A 276  PHE A 280                    
SITE     4 AC1 13 HOH A 523                                                     
SITE     1 AC2  9 TYR A  57  PHE A 111  ASP A 115  LEU A 118                    
SITE     2 AC2  9 LEU A 129  PHE A 134  ILE A 138  OLC A 403                    
SITE     3 AC2  9 OLC A 407                                                     
SITE     1 AC3  8 TYR A 117  LEU A 118  LYS A 121  LEU A 137                    
SITE     2 AC3  8 PHE A 202  OLC A 402  OLC A 407  HOH A 527                    
SITE     1 AC4  6 PHE A 156  THR A 158  ASN A 176  TYR A 179                    
SITE     2 AC4  6 SER A 180  TYR A 183                                          
SITE     1 AC5  6 LYS A  49  TRP A  51  ASN A  60  LYS A 132                    
SITE     2 AC5  6 TRP A 143  OLC A 408                                          
SITE     1 AC6  5 ILE A  63  CYS A  70  SER A  93  ASN A  94                    
SITE     2 AC6  5 OLC A 413                                                     
SITE     1 AC7  8 VAL A 144  LEU A 145  ILE A 194  SER A 197                    
SITE     2 AC7  8 VAL A 198  TYR A 204  OLC A 402  OLC A 403                    
SITE     1 AC8  4 LEU A  45  MET A  48  TRP A  51  OLC A 405                    
SITE     1 AC9  5 LEU A 185  THR A 188  HIS A 245  ASN A 249                    
SITE     2 AC9  5 ALA A 253                                                     
SITE     1 AD1  4 LYS A 178  LEU A 181  ILE A 182  LEU A 185                    
SITE     1 AD2  7 TYR A  21  PHE A  25  MET A 247  ILE A 268                    
SITE     2 AD2  7 LEU A 271  THR A 275  OLC A 412                               
SITE     1 AD3  6 TRP A  10  TYR A  20  CYS A 263  ALA A 267                    
SITE     2 AD3  6 OLC A 411  HOH A 533                                          
SITE     1 AD4  9 TYR A  86  GLY A  87  ASP A  88  VAL A  89                    
SITE     2 AD4  9 LEU A  90  TYR A  96  VAL A  97  OLC A 406                    
SITE     3 AD4  9 GLY B  17                                                     
SITE     1 AD5  3 HIS A 127  ILE A 128  LEU A 129                               
SITE     1 AD6  1 SER A 174                                                     
CRYST1   76.839  151.003   68.211  90.00 112.29  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      0.013014  0.000000  0.005335        0.00000                         
SCALE2      0.000000  0.006622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015844        0.00000                         
ATOM      1  N   CYS A   7      -8.297  -7.465   2.989  1.00 83.54           N  
ANISOU    1  N   CYS A   7    12577   8378  10785    117    205   -887       N  
ATOM      2  CA  CYS A   7      -7.875  -6.087   2.736  1.00 83.94           C  
ANISOU    2  CA  CYS A   7    12639   8524  10733    148    226   -841       C  
ATOM      3  C   CYS A   7      -6.379  -5.925   2.976  1.00 83.11           C  
ANISOU    3  C   CYS A   7    12549   8476  10554    206    396   -782       C  
ATOM      4  O   CYS A   7      -5.943  -4.947   3.582  1.00 83.17           O  
ANISOU    4  O   CYS A   7    12472   8569  10559    213    460   -712       O  
ATOM      5  CB  CYS A   7      -8.686  -5.119   3.588  1.00 85.65           C  
ANISOU    5  CB  CYS A   7    12698   8798  11047     99    179   -793       C  
ATOM      6  SG  CYS A   7     -10.475  -5.289   3.382  1.00 92.24           S  
ANISOU    6  SG  CYS A   7    13478   9562  12009     28    -17   -870       S  
ATOM      7  N   GLU A   8      -5.601  -6.896   2.484  1.00 82.18           N  
ANISOU    7  N   GLU A   8    12536   8305  10385    249    465   -817       N  
ATOM      8  CA  GLU A   8      -4.145  -6.991   2.590  1.00 81.59           C  
ANISOU    8  CA  GLU A   8    12479   8262  10259    312    625   -781       C  
ATOM      9  C   GLU A   8      -3.437  -5.786   1.944  1.00 79.78           C  
ANISOU    9  C   GLU A   8    12310   8100   9903    349    684   -757       C  
ATOM     10  O   GLU A   8      -2.365  -5.376   2.404  1.00 79.42           O  
ANISOU   10  O   GLU A   8    12203   8113   9859    382    812   -704       O  
ATOM     11  CB  GLU A   8      -3.662  -8.305   1.932  1.00 85.16           C  
ANISOU   11  CB  GLU A   8    13055   8624  10676    350    665   -845       C  
ATOM     12  CG  GLU A   8      -4.454  -9.560   2.299  1.00 92.33           C  
ANISOU   12  CG  GLU A   8    13945   9441  11696    310    593   -886       C  
ATOM     13  CD  GLU A   8      -5.775  -9.787   1.575  1.00101.16           C  
ANISOU   13  CD  GLU A   8    15126  10491  12821    259    425   -964       C  
ATOM     14  OE1 GLU A   8      -5.814  -9.636   0.332  1.00103.45           O  
ANISOU   14  OE1 GLU A   8    15571  10754  12983    285    368  -1026       O  
ATOM     15  OE2 GLU A   8      -6.781 -10.090   2.259  1.00103.48           O  
ANISOU   15  OE2 GLU A   8    15313  10754  13249    195    349   -964       O  
ATOM     16  N   ASN A   9      -4.038  -5.238   0.863  1.00 78.26           N  
ANISOU   16  N   ASN A   9    12241   7891   9604    344    588   -800       N  
ATOM     17  CA  ASN A   9      -3.507  -4.087   0.132  1.00 77.04           C  
ANISOU   17  CA  ASN A   9    12174   7781   9315    376    637   -779       C  
ATOM     18  C   ASN A   9      -3.621  -2.822   0.948  1.00 74.74           C  
ANISOU   18  C   ASN A   9    11742   7582   9076    349    641   -703       C  
ATOM     19  O   ASN A   9      -2.686  -2.027   0.975  1.00 74.77           O  
ANISOU   19  O   ASN A   9    11734   7641   9035    375    759   -657       O  
ATOM     20  CB  ASN A   9      -4.181  -3.910  -1.246  1.00 78.71           C  
ANISOU   20  CB  ASN A   9    12582   7936   9388    385    517   -846       C  
ATOM     21  CG  ASN A   9      -5.694  -3.804  -1.250  1.00 82.73           C  
ANISOU   21  CG  ASN A   9    13060   8420   9955    336    310   -882       C  
ATOM     22  OD1 ASN A   9      -6.402  -4.351  -0.391  1.00 84.21           O  
ANISOU   22  OD1 ASN A   9    13104   8595  10296    287    249   -884       O  
ATOM     23  ND2 ASN A   9      -6.228  -3.120  -2.250  1.00 83.83           N  
ANISOU   23  ND2 ASN A   9    13339   8538   9974    349    196   -915       N  
ATOM     24  N   TRP A  10      -4.758  -2.641   1.625  1.00 72.72           N  
ANISOU   24  N   TRP A  10    11373   7337   8923    296    520   -694       N  
ATOM     25  CA  TRP A  10      -4.997  -1.482   2.481  1.00 71.34           C  
ANISOU   25  CA  TRP A  10    11058   7242   8806    268    514   -627       C  
ATOM     26  C   TRP A  10      -4.154  -1.538   3.751  1.00 70.55           C  
ANISOU   26  C   TRP A  10    10811   7197   8798    272    639   -563       C  
ATOM     27  O   TRP A  10      -3.715  -0.498   4.242  1.00 70.62           O  
ANISOU   27  O   TRP A  10    10745   7278   8810    275    694   -506       O  
ATOM     28  CB  TRP A  10      -6.489  -1.332   2.784  1.00 70.82           C  
ANISOU   28  CB  TRP A  10    10917   7160   8831    213    354   -646       C  
ATOM     29  CG  TRP A  10      -7.282  -0.950   1.571  1.00 70.82           C  
ANISOU   29  CG  TRP A  10    11051   7119   8738    217    211   -703       C  
ATOM     30  CD1 TRP A  10      -8.038  -1.775   0.792  1.00 71.62           C  
ANISOU   30  CD1 TRP A  10    11248   7135   8830    211     84   -787       C  
ATOM     31  CD2 TRP A  10      -7.322   0.341   0.944  1.00 70.60           C  
ANISOU   31  CD2 TRP A  10    11095   7126   8604    237    176   -683       C  
ATOM     32  NE1 TRP A  10      -8.573  -1.071  -0.264  1.00 71.85           N  
ANISOU   32  NE1 TRP A  10    11406   7145   8751    230    -41   -823       N  
ATOM     33  CE2 TRP A  10      -8.163   0.235  -0.183  1.00 71.34           C  
ANISOU   33  CE2 TRP A  10    11331   7152   8622    247     15   -756       C  
ATOM     34  CE3 TRP A  10      -6.754   1.586   1.246  1.00 70.89           C  
ANISOU   34  CE3 TRP A  10    11092   7238   8606    248    258   -613       C  
ATOM     35  CZ2 TRP A  10      -8.451   1.325  -1.003  1.00 71.68           C  
ANISOU   35  CZ2 TRP A  10    11486   7199   8549    272    -67   -755       C  
ATOM     36  CZ3 TRP A  10      -7.042   2.661   0.433  1.00 71.58           C  
ANISOU   36  CZ3 TRP A  10    11285   7329   8584    266    189   -610       C  
ATOM     37  CH2 TRP A  10      -7.869   2.523  -0.686  1.00 71.76           C  
ANISOU   37  CH2 TRP A  10    11460   7282   8523    282     29   -678       C  
ATOM     38  N   LEU A  11      -3.856  -2.751   4.235  1.00 69.64           N  
ANISOU   38  N   LEU A  11    10669   7041   8751    280    683   -574       N  
ATOM     39  CA  LEU A  11      -2.980  -2.956   5.379  1.00 69.36           C  
ANISOU   39  CA  LEU A  11    10518   7043   8791    298    790   -520       C  
ATOM     40  C   LEU A  11      -1.525  -2.594   4.987  1.00 68.22           C  
ANISOU   40  C   LEU A  11    10410   6934   8578    356    923   -507       C  
ATOM     41  O   LEU A  11      -0.808  -2.007   5.786  1.00 68.48           O  
ANISOU   41  O   LEU A  11    10338   7028   8653    370    992   -455       O  
ATOM     42  CB  LEU A  11      -3.106  -4.409   5.871  1.00 69.99           C  
ANISOU   42  CB  LEU A  11    10587   7055   8953    297    792   -540       C  
ATOM     43  CG  LEU A  11      -2.347  -4.813   7.137  1.00 72.18           C  
ANISOU   43  CG  LEU A  11    10761   7353   9312    322    877   -486       C  
ATOM     44  CD1 LEU A  11      -2.608  -3.855   8.299  1.00 72.75           C  
ANISOU   44  CD1 LEU A  11    10701   7498   9441    295    869   -419       C  
ATOM     45  CD2 LEU A  11      -2.715  -6.227   7.535  1.00 73.01           C  
ANISOU   45  CD2 LEU A  11    10877   7373   9490    314    864   -506       C  
ATOM     46  N   ALA A  12      -1.121  -2.873   3.741  1.00 66.91           N  
ANISOU   46  N   ALA A  12    10393   6723   8307    389    958   -557       N  
ATOM     47  CA  ALA A  12       0.188  -2.498   3.219  1.00 65.93           C  
ANISOU   47  CA  ALA A  12    10312   6619   8120    439   1099   -552       C  
ATOM     48  C   ALA A  12       0.288  -0.961   3.161  1.00 65.38           C  
ANISOU   48  C   ALA A  12    10214   6619   8009    424   1117   -507       C  
ATOM     49  O   ALA A  12       1.336  -0.411   3.489  1.00 65.96           O  
ANISOU   49  O   ALA A  12    10216   6738   8109    446   1231   -474       O  
ATOM     50  CB  ALA A  12       0.384  -3.090   1.831  1.00 65.54           C  
ANISOU   50  CB  ALA A  12    10454   6497   7952    472   1128   -619       C  
ATOM     51  N   LEU A  13      -0.806  -0.271   2.768  1.00 63.96           N  
ANISOU   51  N   LEU A  13    10083   6441   7777    387    999   -509       N  
ATOM     52  CA  LEU A  13      -0.846   1.189   2.713  1.00 62.88           C  
ANISOU   52  CA  LEU A  13     9929   6361   7602    372   1001   -467       C  
ATOM     53  C   LEU A  13      -0.767   1.756   4.122  1.00 62.70           C  
ANISOU   53  C   LEU A  13     9713   6410   7700    348   1008   -407       C  
ATOM     54  O   LEU A  13       0.036   2.649   4.336  1.00 63.31           O  
ANISOU   54  O   LEU A  13     9739   6536   7780    357   1097   -370       O  
ATOM     55  CB  LEU A  13      -2.098   1.709   1.978  1.00 62.21           C  
ANISOU   55  CB  LEU A  13     9943   6252   7440    347    853   -488       C  
ATOM     56  CG  LEU A  13      -2.326   3.234   1.982  1.00 62.11           C  
ANISOU   56  CG  LEU A  13     9912   6291   7395    330    832   -441       C  
ATOM     57  CD1 LEU A  13      -1.223   3.947   1.314  1.00 62.37           C  
ANISOU   57  CD1 LEU A  13    10032   6332   7333    360    975   -421       C  
ATOM     58  CD2 LEU A  13      -3.618   3.597   1.305  1.00 61.95           C  
ANISOU   58  CD2 LEU A  13     9984   6238   7316    315    663   -470       C  
ATOM     59  N   GLU A  14      -1.544   1.215   5.094  1.00 61.72           N  
ANISOU   59  N   GLU A  14     9487   6286   7676    319    925   -400       N  
ATOM     60  CA  GLU A  14      -1.524   1.670   6.495  1.00 60.99           C  
ANISOU   60  CA  GLU A  14     9230   6254   7688    301    930   -346       C  
ATOM     61  C   GLU A  14      -0.113   1.587   7.061  1.00 60.31           C  
ANISOU   61  C   GLU A  14     9074   6198   7641    342   1055   -322       C  
ATOM     62  O   GLU A  14       0.338   2.540   7.681  1.00 60.47           O  
ANISOU   62  O   GLU A  14     9004   6278   7693    340   1090   -282       O  
ATOM     63  CB  GLU A  14      -2.443   0.808   7.388  1.00 63.11           C  
ANISOU   63  CB  GLU A  14     9431   6496   8052    271    855   -347       C  
ATOM     64  CG  GLU A  14      -3.926   1.122   7.370  1.00 68.65           C  
ANISOU   64  CG  GLU A  14    10119   7185   8779    219    729   -358       C  
ATOM     65  CD  GLU A  14      -4.804   0.158   8.154  1.00 76.91           C  
ANISOU   65  CD  GLU A  14    11104   8188   9929    184    679   -366       C  
ATOM     66  OE1 GLU A  14      -4.447  -1.036   8.257  1.00 78.62           O  
ANISOU   66  OE1 GLU A  14    11348   8356  10169    201    716   -383       O  
ATOM     67  OE2 GLU A  14      -5.859   0.598   8.663  1.00 80.49           O  
ANISOU   67  OE2 GLU A  14    11483   8650  10447    140    609   -356       O  
ATOM     68  N   ASN A  15       0.586   0.455   6.829  1.00 59.75           N  
ANISOU   68  N   ASN A  15     9043   6082   7576    382   1116   -352       N  
ATOM     69  CA  ASN A  15       1.936   0.228   7.336  1.00 59.96           C  
ANISOU   69  CA  ASN A  15     8997   6126   7658    430   1223   -341       C  
ATOM     70  C   ASN A  15       2.937   1.202   6.742  1.00 59.11           C  
ANISOU   70  C   ASN A  15     8895   6050   7513    447   1329   -337       C  
ATOM     71  O   ASN A  15       3.722   1.782   7.488  1.00 59.16           O  
ANISOU   71  O   ASN A  15     8785   6104   7589    460   1378   -309       O  
ATOM     72  CB  ASN A  15       2.380  -1.231   7.124  1.00 62.35           C  
ANISOU   72  CB  ASN A  15     9351   6363   7977    472   1260   -380       C  
ATOM     73  CG  ASN A  15       1.630  -2.255   7.961  1.00 67.63           C  
ANISOU   73  CG  ASN A  15     9993   6994   8709    459   1180   -375       C  
ATOM     74  OD1 ASN A  15       1.099  -1.962   9.040  1.00 70.18           O  
ANISOU   74  OD1 ASN A  15    10228   7348   9089    430   1125   -333       O  
ATOM     75  ND2 ASN A  15       1.548  -3.484   7.475  1.00 68.71           N  
ANISOU   75  ND2 ASN A  15    10216   7056   8836    477   1180   -419       N  
ATOM     76  N   ILE A  16       2.883   1.411   5.410  1.00 58.27           N  
ANISOU   76  N   ILE A  16     8931   5911   7297    447   1362   -368       N  
ATOM     77  CA  ILE A  16       3.745   2.345   4.679  1.00 58.02           C  
ANISOU   77  CA  ILE A  16     8937   5893   7216    458   1481   -364       C  
ATOM     78  C   ILE A  16       3.490   3.796   5.120  1.00 58.48           C  
ANISOU   78  C   ILE A  16     8921   6012   7285    420   1453   -315       C  
ATOM     79  O   ILE A  16       4.447   4.556   5.280  1.00 59.26           O  
ANISOU   79  O   ILE A  16     8949   6143   7426    426   1553   -297       O  
ATOM     80  CB  ILE A  16       3.628   2.139   3.135  1.00 58.11           C  
ANISOU   80  CB  ILE A  16     9153   5841   7084    470   1517   -406       C  
ATOM     81  CG1 ILE A  16       4.491   0.955   2.678  1.00 59.40           C  
ANISOU   81  CG1 ILE A  16     9370   5949   7251    522   1619   -455       C  
ATOM     82  CG2 ILE A  16       4.038   3.363   2.357  1.00 58.46           C  
ANISOU   82  CG2 ILE A  16     9269   5895   7048    463   1609   -389       C  
ATOM     83  CD1 ILE A  16       4.037   0.275   1.359  1.00 60.46           C  
ANISOU   83  CD1 ILE A  16     9720   6007   7248    536   1604   -509       C  
ATOM     84  N   LEU A  17       2.215   4.186   5.309  1.00 57.45           N  
ANISOU   84  N   LEU A  17     8804   5896   7130    380   1319   -298       N  
ATOM     85  CA  LEU A  17       1.882   5.542   5.730  1.00 56.87           C  
ANISOU   85  CA  LEU A  17     8666   5874   7068    346   1284   -255       C  
ATOM     86  C   LEU A  17       2.458   5.831   7.111  1.00 58.37           C  
ANISOU   86  C   LEU A  17     8677   6121   7380    346   1305   -222       C  
ATOM     87  O   LEU A  17       2.982   6.920   7.339  1.00 58.76           O  
ANISOU   87  O   LEU A  17     8665   6209   7453    337   1354   -196       O  
ATOM     88  CB  LEU A  17       0.359   5.783   5.738  1.00 55.37           C  
ANISOU   88  CB  LEU A  17     8506   5681   6849    309   1131   -251       C  
ATOM     89  CG  LEU A  17      -0.336   5.882   4.406  1.00 54.05           C  
ANISOU   89  CG  LEU A  17     8516   5464   6557    308   1074   -280       C  
ATOM     90  CD1 LEU A  17      -1.807   6.111   4.592  1.00 53.24           C  
ANISOU   90  CD1 LEU A  17     8401   5360   6466    275    912   -282       C  
ATOM     91  CD2 LEU A  17       0.300   6.948   3.526  1.00 54.45           C  
ANISOU   91  CD2 LEU A  17     8663   5512   6512    318   1166   -264       C  
ATOM     92  N   GLU A  18       2.381   4.854   8.032  1.00 58.82           N  
ANISOU   92  N   GLU A  18     8660   6177   7513    360   1265   -225       N  
ATOM     93  CA  GLU A  18       2.913   5.042   9.381  1.00 59.52           C  
ANISOU   93  CA  GLU A  18     8599   6311   7704    370   1268   -196       C  
ATOM     94  C   GLU A  18       4.426   5.064   9.395  1.00 60.32           C  
ANISOU   94  C   GLU A  18     8640   6419   7860    411   1383   -208       C  
ATOM     95  O   GLU A  18       5.021   5.984   9.952  1.00 61.02           O  
ANISOU   95  O   GLU A  18     8630   6551   8004    408   1410   -189       O  
ATOM     96  CB  GLU A  18       2.381   3.970  10.323  1.00 61.64           C  
ANISOU   96  CB  GLU A  18     8831   6563   8024    376   1197   -192       C  
ATOM     97  CG  GLU A  18       0.896   4.103  10.580  1.00 67.26           C  
ANISOU   97  CG  GLU A  18     9559   7274   8723    328   1091   -178       C  
ATOM     98  CD  GLU A  18       0.291   3.037  11.469  1.00 76.44           C  
ANISOU   98  CD  GLU A  18    10699   8408   9938    326   1040   -173       C  
ATOM     99  OE1 GLU A  18       1.035   2.136  11.923  1.00 80.07           O  
ANISOU   99  OE1 GLU A  18    11140   8846  10436    368   1077   -176       O  
ATOM    100  OE2 GLU A  18      -0.936   3.104  11.707  1.00 78.14           O  
ANISOU  100  OE2 GLU A  18    10914   8614  10162    283    966   -166       O  
ATOM    101  N   LYS A  19       5.051   4.087   8.740  1.00 60.15           N  
ANISOU  101  N   LYS A  19     8674   6350   7829    450   1453   -245       N  
ATOM    102  CA  LYS A  19       6.497   3.965   8.702  1.00 60.68           C  
ANISOU  102  CA  LYS A  19     8676   6414   7967    495   1569   -267       C  
ATOM    103  C   LYS A  19       7.208   5.078   7.915  1.00 60.98           C  
ANISOU  103  C   LYS A  19     8721   6460   7988    480   1686   -270       C  
ATOM    104  O   LYS A  19       8.248   5.561   8.362  1.00 61.46           O  
ANISOU  104  O   LYS A  19     8661   6544   8149    494   1751   -272       O  
ATOM    105  CB  LYS A  19       6.875   2.570   8.170  1.00 62.74           C  
ANISOU  105  CB  LYS A  19     9003   6612   8221    542   1615   -309       C  
ATOM    106  CG  LYS A  19       8.350   2.238   8.227  1.00 68.14           C  
ANISOU  106  CG  LYS A  19     9604   7285   9003    599   1726   -339       C  
ATOM    107  CD  LYS A  19       8.553   0.715   8.198  1.00 74.82           C  
ANISOU  107  CD  LYS A  19    10487   8074   9868    652   1726   -373       C  
ATOM    108  CE  LYS A  19      10.001   0.286   8.006  1.00 79.97           C  
ANISOU  108  CE  LYS A  19    11072   8699  10615    716   1848   -415       C  
ATOM    109  NZ  LYS A  19      10.871   0.644   9.166  1.00 83.15           N  
ANISOU  109  NZ  LYS A  19    11294   9141  11160    748   1827   -405       N  
ATOM    110  N   TYR A  20       6.664   5.485   6.755  1.00 60.46           N  
ANISOU  110  N   TYR A  20     8801   6369   7801    453   1710   -271       N  
ATOM    111  CA  TYR A  20       7.324   6.448   5.878  1.00 60.42           C  
ANISOU  111  CA  TYR A  20     8840   6354   7762    440   1841   -271       C  
ATOM    112  C   TYR A  20       6.673   7.830   5.770  1.00 59.13           C  
ANISOU  112  C   TYR A  20     8705   6219   7543    390   1801   -231       C  
ATOM    113  O   TYR A  20       7.395   8.828   5.816  1.00 59.58           O  
ANISOU  113  O   TYR A  20     8699   6292   7649    374   1889   -217       O  
ATOM    114  CB  TYR A  20       7.495   5.845   4.479  1.00 61.49           C  
ANISOU  114  CB  TYR A  20     9151   6422   7790    462   1938   -308       C  
ATOM    115  CG  TYR A  20       8.353   4.594   4.474  1.00 63.47           C  
ANISOU  115  CG  TYR A  20     9372   6639   8107    517   2012   -353       C  
ATOM    116  CD1 TYR A  20       9.739   4.677   4.468  1.00 64.54           C  
ANISOU  116  CD1 TYR A  20     9409   6766   8346    545   2166   -375       C  
ATOM    117  CD2 TYR A  20       7.775   3.330   4.481  1.00 64.99           C  
ANISOU  117  CD2 TYR A  20     9624   6799   8268    540   1929   -377       C  
ATOM    118  CE1 TYR A  20      10.528   3.538   4.480  1.00 65.85           C  
ANISOU  118  CE1 TYR A  20     9539   6897   8584    602   2229   -419       C  
ATOM    119  CE2 TYR A  20       8.553   2.183   4.496  1.00 66.15           C  
ANISOU  119  CE2 TYR A  20     9745   6909   8478    594   1993   -417       C  
ATOM    120  CZ  TYR A  20       9.932   2.291   4.484  1.00 67.61           C  
ANISOU  120  CZ  TYR A  20     9835   7089   8764    628   2142   -438       C  
ATOM    121  OH  TYR A  20      10.713   1.155   4.489  1.00 70.40           O  
ANISOU  121  OH  TYR A  20    10157   7401   9190    689   2204   -483       O  
ATOM    122  N   TYR A  21       5.349   7.911   5.603  1.00 57.44           N  
ANISOU  122  N   TYR A  21     8583   6005   7239    366   1672   -216       N  
ATOM    123  CA  TYR A  21       4.690   9.211   5.490  1.00 56.67           C  
ANISOU  123  CA  TYR A  21     8514   5926   7090    326   1625   -179       C  
ATOM    124  C   TYR A  21       4.744   9.993   6.809  1.00 55.65           C  
ANISOU  124  C   TYR A  21     8212   5861   7073    304   1577   -148       C  
ATOM    125  O   TYR A  21       5.161  11.139   6.795  1.00 55.10           O  
ANISOU  125  O   TYR A  21     8110   5805   7020    283   1634   -127       O  
ATOM    126  CB  TYR A  21       3.257   9.077   4.930  1.00 56.64           C  
ANISOU  126  CB  TYR A  21     8646   5900   6975    313   1490   -181       C  
ATOM    127  CG  TYR A  21       2.401  10.330   5.042  1.00 57.14           C  
ANISOU  127  CG  TYR A  21     8716   5988   7009    278   1404   -144       C  
ATOM    128  CD1 TYR A  21       2.450  11.316   4.070  1.00 57.43           C  
ANISOU  128  CD1 TYR A  21     8878   5996   6946    271   1455   -128       C  
ATOM    129  CD2 TYR A  21       1.482  10.481   6.073  1.00 57.70           C  
ANISOU  129  CD2 TYR A  21     8681   6098   7143    256   1274   -127       C  
ATOM    130  CE1 TYR A  21       1.642  12.439   4.142  1.00 58.16           C  
ANISOU  130  CE1 TYR A  21     8984   6102   7011    246   1369    -95       C  
ATOM    131  CE2 TYR A  21       0.689  11.611   6.169  1.00 58.57           C  
ANISOU  131  CE2 TYR A  21     8793   6226   7234    230   1198    -98       C  
ATOM    132  CZ  TYR A  21       0.769  12.592   5.199  1.00 59.23           C  
ANISOU  132  CZ  TYR A  21     8997   6283   7224    226   1239    -83       C  
ATOM    133  OH  TYR A  21      -0.032  13.711   5.274  1.00 60.05           O  
ANISOU  133  OH  TYR A  21     9107   6397   7311    206   1156    -55       O  
ATOM    134  N   LEU A  22       4.330   9.374   7.941  1.00 55.38           N  
ANISOU  134  N   LEU A  22     8077   5855   7109    310   1477   -146       N  
ATOM    135  CA  LEU A  22       4.331  10.011   9.264  1.00 55.08           C  
ANISOU  135  CA  LEU A  22     7892   5872   7164    296   1423   -119       C  
ATOM    136  C   LEU A  22       5.752  10.345   9.735  1.00 56.13           C  
ANISOU  136  C   LEU A  22     7902   6023   7402    314   1519   -128       C  
ATOM    137  O   LEU A  22       5.982  11.450  10.198  1.00 56.42           O  
ANISOU  137  O   LEU A  22     7862   6090   7483    291   1523   -110       O  
ATOM    138  CB  LEU A  22       3.564   9.172  10.315  1.00 54.48           C  
ANISOU  138  CB  LEU A  22     7765   5811   7125    302   1310   -114       C  
ATOM    139  CG  LEU A  22       2.046   8.985  10.096  1.00 54.64           C  
ANISOU  139  CG  LEU A  22     7864   5816   7081    275   1201   -109       C  
ATOM    140  CD1 LEU A  22       1.402   8.275  11.252  1.00 54.10           C  
ANISOU  140  CD1 LEU A  22     7730   5757   7068    275   1120   -100       C  
ATOM    141  CD2 LEU A  22       1.335  10.311   9.893  1.00 55.02           C  
ANISOU  141  CD2 LEU A  22     7930   5883   7091    239   1158    -84       C  
ATOM    142  N   SER A  23       6.719   9.428   9.547  1.00 56.77           N  
ANISOU  142  N   SER A  23     7963   6079   7529    354   1598   -161       N  
ATOM    143  CA  SER A  23       8.126   9.650   9.896  1.00 57.70           C  
ANISOU  143  CA  SER A  23     7953   6204   7768    376   1689   -182       C  
ATOM    144  C   SER A  23       8.717  10.874   9.202  1.00 58.44           C  
ANISOU  144  C   SER A  23     8050   6288   7865    343   1807   -178       C  
ATOM    145  O   SER A  23       9.389  11.677   9.852  1.00 59.32           O  
ANISOU  145  O   SER A  23     8032   6425   8081    331   1824   -178       O  
ATOM    146  CB  SER A  23       8.959   8.429   9.536  1.00 59.95           C  
ANISOU  146  CB  SER A  23     8239   6450   8091    429   1765   -223       C  
ATOM    147  OG  SER A  23       8.555   7.312  10.311  1.00 64.62           O  
ANISOU  147  OG  SER A  23     8815   7042   8695    463   1661   -225       O  
ATOM    148  N   ALA A  24       8.478  11.019   7.878  1.00 57.60           N  
ANISOU  148  N   ALA A  24     8100   6139   7645    328   1889   -176       N  
ATOM    149  CA  ALA A  24       8.977  12.146   7.090  1.00 56.54           C  
ANISOU  149  CA  ALA A  24     8007   5982   7495    296   2018   -166       C  
ATOM    150  C   ALA A  24       8.277  13.477   7.447  1.00 55.33           C  
ANISOU  150  C   ALA A  24     7847   5858   7317    249   1944   -123       C  
ATOM    151  O   ALA A  24       8.965  14.462   7.715  1.00 55.83           O  
ANISOU  151  O   ALA A  24     7818   5928   7466    223   2009   -118       O  
ATOM    152  CB  ALA A  24       8.835  11.848   5.602  1.00 56.60           C  
ANISOU  152  CB  ALA A  24     8215   5928   7362    302   2115   -173       C  
ATOM    153  N   PHE A  25       6.925  13.499   7.486  1.00 53.42           N  
ANISOU  153  N   PHE A  25     7691   5630   6976    238   1806    -98       N  
ATOM    154  CA  PHE A  25       6.149  14.696   7.797  1.00 51.93           C  
ANISOU  154  CA  PHE A  25     7503   5465   6762    201   1727    -60       C  
ATOM    155  C   PHE A  25       6.442  15.182   9.234  1.00 50.88           C  
ANISOU  155  C   PHE A  25     7185   5386   6761    192   1670    -57       C  
ATOM    156  O   PHE A  25       6.701  16.370   9.424  1.00 50.66           O  
ANISOU  156  O   PHE A  25     7111   5365   6773    161   1698    -41       O  
ATOM    157  CB  PHE A  25       4.646  14.441   7.550  1.00 51.27           C  
ANISOU  157  CB  PHE A  25     7534   5380   6568    199   1587    -46       C  
ATOM    158  CG  PHE A  25       3.800  15.609   7.059  1.00 51.17           C  
ANISOU  158  CG  PHE A  25     7617   5356   6471    172   1540    -12       C  
ATOM    159  CD1 PHE A  25       4.011  16.894   7.532  1.00 51.57           C  
ANISOU  159  CD1 PHE A  25     7595   5425   6574    143   1557     13       C  
ATOM    160  CD2 PHE A  25       2.724  15.400   6.217  1.00 51.31           C  
ANISOU  160  CD2 PHE A  25     7789   5341   6366    179   1458    -11       C  
ATOM    161  CE1 PHE A  25       3.193  17.959   7.127  1.00 51.59           C  
ANISOU  161  CE1 PHE A  25     7687   5412   6504    124   1505     45       C  
ATOM    162  CE2 PHE A  25       1.914  16.464   5.815  1.00 51.52           C  
ANISOU  162  CE2 PHE A  25     7900   5353   6322    163   1395     18       C  
ATOM    163  CZ  PHE A  25       2.145  17.733   6.286  1.00 51.03           C  
ANISOU  163  CZ  PHE A  25     7769   5310   6312    137   1421     48       C  
ATOM    164  N   TYR A  26       6.451  14.280  10.225  1.00 49.93           N  
ANISOU  164  N   TYR A  26     6970   5295   6704    221   1593    -72       N  
ATOM    165  CA  TYR A  26       6.794  14.664  11.592  1.00 49.71           C  
ANISOU  165  CA  TYR A  26     6788   5312   6787    222   1535    -73       C  
ATOM    166  C   TYR A  26       8.259  15.040  11.724  1.00 51.55           C  
ANISOU  166  C   TYR A  26     6904   5539   7144    227   1638   -102       C  
ATOM    167  O   TYR A  26       8.580  15.890  12.532  1.00 52.91           O  
ANISOU  167  O   TYR A  26     6971   5737   7397    211   1609   -102       O  
ATOM    168  CB  TYR A  26       6.384  13.605  12.647  1.00 48.57           C  
ANISOU  168  CB  TYR A  26     6598   5193   6666    256   1425    -78       C  
ATOM    169  CG  TYR A  26       4.885  13.545  12.893  1.00 47.02           C  
ANISOU  169  CG  TYR A  26     6467   5007   6389    239   1314    -50       C  
ATOM    170  CD1 TYR A  26       4.153  14.701  13.160  1.00 46.38           C  
ANISOU  170  CD1 TYR A  26     6385   4948   6291    204   1264    -24       C  
ATOM    171  CD2 TYR A  26       4.202  12.335  12.860  1.00 46.32           C  
ANISOU  171  CD2 TYR A  26     6437   4903   6260    257   1264    -54       C  
ATOM    172  CE1 TYR A  26       2.776  14.658  13.340  1.00 46.35           C  
ANISOU  172  CE1 TYR A  26     6429   4949   6233    189   1169     -5       C  
ATOM    173  CE2 TYR A  26       2.826  12.282  13.029  1.00 46.60           C  
ANISOU  173  CE2 TYR A  26     6520   4941   6244    236   1172    -36       C  
ATOM    174  CZ  TYR A  26       2.116  13.446  13.273  1.00 46.95           C  
ANISOU  174  CZ  TYR A  26     6553   5007   6278    203   1125    -12       C  
ATOM    175  OH  TYR A  26       0.755  13.380  13.424  1.00 47.40           O  
ANISOU  175  OH  TYR A  26     6643   5062   6304    184   1039     -1       O  
ATOM    176  N   GLY A  27       9.139  14.426  10.946  1.00 52.27           N  
ANISOU  176  N   GLY A  27     7009   5593   7258    247   1757   -131       N  
ATOM    177  CA  GLY A  27      10.564  14.745  10.966  1.00 53.30           C  
ANISOU  177  CA  GLY A  27     7016   5708   7527    250   1872   -166       C  
ATOM    178  C   GLY A  27      10.808  16.173  10.512  1.00 54.69           C  
ANISOU  178  C   GLY A  27     7195   5866   7717    195   1961   -151       C  
ATOM    179  O   GLY A  27      11.548  16.919  11.161  1.00 55.21           O  
ANISOU  179  O   GLY A  27     7121   5942   7914    179   1972   -169       O  
ATOM    180  N   ILE A  28      10.135  16.590   9.410  1.00 55.00           N  
ANISOU  180  N   ILE A  28     7404   5874   7618    167   2014   -117       N  
ATOM    181  CA  ILE A  28      10.218  17.948   8.853  1.00 55.19           C  
ANISOU  181  CA  ILE A  28     7475   5869   7626    116   2102    -91       C  
ATOM    182  C   ILE A  28       9.637  18.978   9.819  1.00 54.37           C  
ANISOU  182  C   ILE A  28     7304   5806   7549     87   1980    -68       C  
ATOM    183  O   ILE A  28      10.240  20.023  10.029  1.00 54.64           O  
ANISOU  183  O   ILE A  28     7259   5829   7675     51   2037    -71       O  
ATOM    184  CB  ILE A  28       9.554  17.991   7.452  1.00 56.45           C  
ANISOU  184  CB  ILE A  28     7861   5979   7607    109   2163    -60       C  
ATOM    185  CG1 ILE A  28      10.406  17.203   6.457  1.00 58.42           C  
ANISOU  185  CG1 ILE A  28     8172   6177   7848    131   2330    -89       C  
ATOM    186  CG2 ILE A  28       9.354  19.426   6.954  1.00 56.67           C  
ANISOU  186  CG2 ILE A  28     7970   5975   7588     61   2216    -20       C  
ATOM    187  CD1 ILE A  28       9.673  16.782   5.222  1.00 60.76           C  
ANISOU  187  CD1 ILE A  28     8702   6429   7953    146   2348    -72       C  
ATOM    188  N   GLU A  29       8.497  18.655  10.447  1.00 53.36           N  
ANISOU  188  N   GLU A  29     7202   5720   7353    103   1818    -49       N  
ATOM    189  CA  GLU A  29       7.858  19.512  11.447  1.00 52.55           C  
ANISOU  189  CA  GLU A  29     7040   5656   7272     83   1699    -31       C  
ATOM    190  C   GLU A  29       8.756  19.674  12.676  1.00 52.28           C  
ANISOU  190  C   GLU A  29     6820   5652   7392     90   1669    -65       C  
ATOM    191  O   GLU A  29       8.811  20.758  13.239  1.00 51.84           O  
ANISOU  191  O   GLU A  29     6701   5606   7390     61   1643    -62       O  
ATOM    192  CB  GLU A  29       6.504  18.926  11.874  1.00 52.94           C  
ANISOU  192  CB  GLU A  29     7145   5738   7232    103   1551    -11       C  
ATOM    193  CG  GLU A  29       5.433  19.075  10.814  1.00 53.60           C  
ANISOU  193  CG  GLU A  29     7399   5793   7176     92   1536     19       C  
ATOM    194  CD  GLU A  29       4.094  18.453  11.162  1.00 54.32           C  
ANISOU  194  CD  GLU A  29     7531   5907   7203    107   1398     29       C  
ATOM    195  OE1 GLU A  29       3.944  17.951  12.297  1.00 53.52           O  
ANISOU  195  OE1 GLU A  29     7334   5843   7158    122   1322     20       O  
ATOM    196  OE2 GLU A  29       3.179  18.494  10.310  1.00 54.34           O  
ANISOU  196  OE2 GLU A  29     7663   5883   7101    103   1363     45       O  
ATOM    197  N   PHE A  30       9.445  18.597  13.099  1.00 52.11           N  
ANISOU  197  N   PHE A  30     6717   5641   7441    134   1663   -101       N  
ATOM    198  CA  PHE A  30      10.366  18.654  14.227  1.00 52.71           C  
ANISOU  198  CA  PHE A  30     6623   5738   7664    153   1619   -141       C  
ATOM    199  C   PHE A  30      11.499  19.639  13.929  1.00 54.15           C  
ANISOU  199  C   PHE A  30     6712   5888   7974    115   1737   -169       C  
ATOM    200  O   PHE A  30      11.823  20.442  14.786  1.00 55.31           O  
ANISOU  200  O   PHE A  30     6752   6049   8216    100   1682   -187       O  
ATOM    201  CB  PHE A  30      10.963  17.271  14.532  1.00 52.35           C  
ANISOU  201  CB  PHE A  30     6525   5695   7669    213   1602   -175       C  
ATOM    202  CG  PHE A  30      11.983  17.280  15.652  1.00 52.39           C  
ANISOU  202  CG  PHE A  30     6360   5715   7831    245   1542   -223       C  
ATOM    203  CD1 PHE A  30      13.339  17.327  15.380  1.00 52.88           C  
ANISOU  203  CD1 PHE A  30     6302   5746   8044    251   1641   -275       C  
ATOM    204  CD2 PHE A  30      11.582  17.286  16.974  1.00 52.68           C  
ANISOU  204  CD2 PHE A  30     6359   5790   7866    270   1388   -221       C  
ATOM    205  CE1 PHE A  30      14.266  17.374  16.412  1.00 53.29           C  
ANISOU  205  CE1 PHE A  30     6191   5807   8251    283   1565   -327       C  
ATOM    206  CE2 PHE A  30      12.514  17.284  18.001  1.00 52.98           C  
ANISOU  206  CE2 PHE A  30     6258   5836   8037    308   1314   -269       C  
ATOM    207  CZ  PHE A  30      13.846  17.341  17.715  1.00 52.79           C  
ANISOU  207  CZ  PHE A  30     6107   5782   8169    315   1393   -324       C  
ATOM    208  N   ILE A  31      12.098  19.584  12.733  1.00 53.98           N  
ANISOU  208  N   ILE A  31     6735   5817   7959     99   1903   -174       N  
ATOM    209  CA  ILE A  31      13.192  20.488  12.375  1.00 54.26           C  
ANISOU  209  CA  ILE A  31     6682   5808   8126     56   2044   -201       C  
ATOM    210  C   ILE A  31      12.745  21.960  12.277  1.00 55.07           C  
ANISOU  210  C   ILE A  31     6829   5896   8199     -5   2055   -166       C  
ATOM    211  O   ILE A  31      13.315  22.812  12.958  1.00 55.60           O  
ANISOU  211  O   ILE A  31     6764   5962   8398    -33   2039   -193       O  
ATOM    212  CB  ILE A  31      13.903  19.998  11.074  1.00 53.89           C  
ANISOU  212  CB  ILE A  31     6692   5702   8081     56   2243   -213       C  
ATOM    213  CG1 ILE A  31      14.547  18.611  11.270  1.00 53.76           C  
ANISOU  213  CG1 ILE A  31     6599   5694   8135    120   2238   -259       C  
ATOM    214  CG2 ILE A  31      14.919  21.032  10.580  1.00 54.01           C  
ANISOU  214  CG2 ILE A  31     6638   5658   8223      0   2420   -232       C  
ATOM    215  CD1 ILE A  31      14.897  17.927   9.978  1.00 54.41           C  
ANISOU  215  CD1 ILE A  31     6784   5723   8165    132   2411   -265       C  
ATOM    216  N   VAL A  32      11.736  22.252  11.419  1.00 55.13           N  
ANISOU  216  N   VAL A  32     7023   5888   8037    -24   2075   -109       N  
ATOM    217  CA  VAL A  32      11.175  23.591  11.173  1.00 55.22           C  
ANISOU  217  CA  VAL A  32     7110   5876   7994    -73   2084    -68       C  
ATOM    218  C   VAL A  32      10.567  24.212  12.446  1.00 55.69           C  
ANISOU  218  C   VAL A  32     7093   5986   8080    -76   1915    -66       C  
ATOM    219  O   VAL A  32      10.779  25.397  12.729  1.00 55.87           O  
ANISOU  219  O   VAL A  32     7066   5991   8172   -118   1928    -67       O  
ATOM    220  CB  VAL A  32      10.168  23.560   9.990  1.00 55.07           C  
ANISOU  220  CB  VAL A  32     7317   5828   7778    -73   2111    -13       C  
ATOM    221  CG1 VAL A  32       9.452  24.895   9.831  1.00 54.93           C  
ANISOU  221  CG1 VAL A  32     7384   5789   7698   -111   2087     32       C  
ATOM    222  CG2 VAL A  32      10.861  23.154   8.688  1.00 54.90           C  
ANISOU  222  CG2 VAL A  32     7393   5744   7725    -74   2302    -15       C  
ATOM    223  N   GLY A  33       9.887  23.382  13.231  1.00 55.60           N  
ANISOU  223  N   GLY A  33     7071   6032   8023    -32   1768    -68       N  
ATOM    224  CA  GLY A  33       9.253  23.778  14.481  1.00 56.02           C  
ANISOU  224  CA  GLY A  33     7068   6132   8085    -25   1613    -68       C  
ATOM    225  C   GLY A  33      10.239  24.136  15.569  1.00 56.67           C  
ANISOU  225  C   GLY A  33     6976   6226   8328    -25   1576   -120       C  
ATOM    226  O   GLY A  33      10.060  25.150  16.243  1.00 57.01           O  
ANISOU  226  O   GLY A  33     6979   6276   8406    -49   1516   -122       O  
ATOM    227  N   MET A  34      11.279  23.313  15.768  1.00 56.72           N  
ANISOU  227  N   MET A  34     6878   6233   8439      6   1600   -167       N  
ATOM    228  CA  MET A  34      12.289  23.595  16.788  1.00 57.58           C  
ANISOU  228  CA  MET A  34     6813   6348   8715     14   1548   -227       C  
ATOM    229  C   MET A  34      13.078  24.877  16.463  1.00 59.05           C  
ANISOU  229  C   MET A  34     6925   6486   9026    -49   1651   -249       C  
ATOM    230  O   MET A  34      13.254  25.720  17.341  1.00 58.99           O  
ANISOU  230  O   MET A  34     6831   6484   9099    -66   1572   -277       O  
ATOM    231  CB  MET A  34      13.241  22.403  16.981  1.00 57.91           C  
ANISOU  231  CB  MET A  34     6759   6393   8852     69   1548   -275       C  
ATOM    232  CG  MET A  34      12.632  21.247  17.747  1.00 59.60           C  
ANISOU  232  CG  MET A  34     7012   6651   8981    136   1411   -266       C  
ATOM    233  SD  MET A  34      12.456  21.631  19.500  1.00 65.92           S  
ANISOU  233  SD  MET A  34     7743   7493   9810    166   1214   -289       S  
ATOM    234  CE  MET A  34      12.009  20.064  20.145  1.00 59.21           C  
ANISOU  234  CE  MET A  34     6949   6673   8876    247   1108   -277       C  
ATOM    235  N   LEU A  35      13.542  25.036  15.200  1.00 59.82           N  
ANISOU  235  N   LEU A  35     7064   6528   9137    -87   1835   -237       N  
ATOM    236  CA  LEU A  35      14.293  26.224  14.796  1.00 60.37           C  
ANISOU  236  CA  LEU A  35     7074   6537   9327   -154   1963   -253       C  
ATOM    237  C   LEU A  35      13.443  27.468  14.928  1.00 59.72           C  
ANISOU  237  C   LEU A  35     7072   6448   9171   -197   1920   -211       C  
ATOM    238  O   LEU A  35      13.897  28.469  15.480  1.00 60.51           O  
ANISOU  238  O   LEU A  35     7071   6527   9393   -235   1905   -243       O  
ATOM    239  CB  LEU A  35      14.817  26.090  13.354  1.00 61.69           C  
ANISOU  239  CB  LEU A  35     7312   6640   9490   -182   2185   -237       C  
ATOM    240  CG  LEU A  35      15.929  25.058  13.127  1.00 64.80           C  
ANISOU  240  CG  LEU A  35     7598   7019  10003   -150   2272   -292       C  
ATOM    241  CD1 LEU A  35      16.216  24.878  11.625  1.00 65.48           C  
ANISOU  241  CD1 LEU A  35     7804   7041  10036   -172   2500   -266       C  
ATOM    242  CD2 LEU A  35      17.223  25.466  13.850  1.00 65.78           C  
ANISOU  242  CD2 LEU A  35     7485   7123  10385   -166   2277   -374       C  
ATOM    243  N   GLY A  36      12.212  27.398  14.446  1.00 58.35           N  
ANISOU  243  N   GLY A  36     7074   6289   8808   -187   1891   -146       N  
ATOM    244  CA  GLY A  36      11.304  28.531  14.519  1.00 57.95           C  
ANISOU  244  CA  GLY A  36     7108   6230   8680   -218   1844   -104       C  
ATOM    245  C   GLY A  36      10.931  28.940  15.931  1.00 57.46           C  
ANISOU  245  C   GLY A  36     6963   6216   8654   -204   1672   -129       C  
ATOM    246  O   GLY A  36      10.969  30.121  16.269  1.00 57.58           O  
ANISOU  246  O   GLY A  36     6947   6205   8724   -244   1662   -135       O  
ATOM    247  N   ASN A  37      10.568  27.973  16.764  1.00 57.16           N  
ANISOU  247  N   ASN A  37     6899   6240   8580   -147   1543   -142       N  
ATOM    248  CA  ASN A  37      10.157  28.253  18.125  1.00 57.57           C  
ANISOU  248  CA  ASN A  37     6897   6334   8641   -126   1384   -163       C  
ATOM    249  C   ASN A  37      11.303  28.666  19.024  1.00 58.17           C  
ANISOU  249  C   ASN A  37     6808   6403   8892   -132   1346   -235       C  
ATOM    250  O   ASN A  37      11.084  29.538  19.840  1.00 58.77           O  
ANISOU  250  O   ASN A  37     6857   6482   8990   -144   1262   -251       O  
ATOM    251  CB  ASN A  37       9.347  27.110  18.718  1.00 58.34           C  
ANISOU  251  CB  ASN A  37     7041   6489   8635    -64   1271   -149       C  
ATOM    252  CG  ASN A  37       7.935  27.144  18.203  1.00 60.27           C  
ANISOU  252  CG  ASN A  37     7432   6742   8725    -66   1258    -88       C  
ATOM    253  OD1 ASN A  37       7.117  27.939  18.663  1.00 61.32           O  
ANISOU  253  OD1 ASN A  37     7598   6882   8818    -76   1194    -71       O  
ATOM    254  ND2 ASN A  37       7.631  26.325  17.206  1.00 60.49           N  
ANISOU  254  ND2 ASN A  37     7550   6762   8670    -56   1317    -58       N  
ATOM    255  N   PHE A  38      12.510  28.109  18.875  1.00 58.52           N  
ANISOU  255  N   PHE A  38     6739   6431   9066   -124   1401   -284       N  
ATOM    256  CA  PHE A  38      13.638  28.513  19.721  1.00 59.39           C  
ANISOU  256  CA  PHE A  38     6676   6526   9363   -128   1349   -364       C  
ATOM    257  C   PHE A  38      14.075  29.947  19.405  1.00 58.12           C  
ANISOU  257  C   PHE A  38     6469   6305   9309   -206   1437   -378       C  
ATOM    258  O   PHE A  38      14.382  30.705  20.325  1.00 57.91           O  
ANISOU  258  O   PHE A  38     6353   6272   9377   -217   1343   -428       O  
ATOM    259  CB  PHE A  38      14.807  27.495  19.698  1.00 61.02           C  
ANISOU  259  CB  PHE A  38     6757   6727   9699    -90   1373   -420       C  
ATOM    260  CG  PHE A  38      14.603  26.403  20.740  1.00 63.88           C  
ANISOU  260  CG  PHE A  38     7114   7146  10012     -5   1207   -436       C  
ATOM    261  CD1 PHE A  38      14.466  26.718  22.088  1.00 65.81           C  
ANISOU  261  CD1 PHE A  38     7326   7417  10262     26   1033   -469       C  
ATOM    262  CD2 PHE A  38      14.477  25.077  20.367  1.00 65.29           C  
ANISOU  262  CD2 PHE A  38     7342   7344  10120     45   1227   -414       C  
ATOM    263  CE1 PHE A  38      14.250  25.722  23.041  1.00 66.70           C  
ANISOU  263  CE1 PHE A  38     7460   7572  10310    107    889   -476       C  
ATOM    264  CE2 PHE A  38      14.256  24.084  21.323  1.00 66.43           C  
ANISOU  264  CE2 PHE A  38     7497   7530  10212    122   1081   -423       C  
ATOM    265  CZ  PHE A  38      14.157  24.412  22.653  1.00 66.47           C  
ANISOU  265  CZ  PHE A  38     7476   7559  10222    153    916   -452       C  
ATOM    266  N   THR A  39      14.009  30.347  18.119  1.00 56.68           N  
ANISOU  266  N   THR A  39     6368   6071   9095   -258   1612   -331       N  
ATOM    267  CA  THR A  39      14.325  31.700  17.673  1.00 55.16           C  
ANISOU  267  CA  THR A  39     6166   5809   8985   -336   1720   -329       C  
ATOM    268  C   THR A  39      13.342  32.745  18.263  1.00 54.13           C  
ANISOU  268  C   THR A  39     6108   5686   8771   -350   1615   -303       C  
ATOM    269  O   THR A  39      13.788  33.782  18.757  1.00 54.39           O  
ANISOU  269  O   THR A  39     6055   5682   8926   -392   1597   -344       O  
ATOM    270  CB  THR A  39      14.345  31.754  16.133  1.00 55.63           C  
ANISOU  270  CB  THR A  39     6343   5810   8985   -375   1930   -272       C  
ATOM    271  OG1 THR A  39      15.272  30.798  15.645  1.00 55.73           O  
ANISOU  271  OG1 THR A  39     6284   5812   9079   -359   2033   -303       O  
ATOM    272  CG2 THR A  39      14.700  33.139  15.591  1.00 55.75           C  
ANISOU  272  CG2 THR A  39     6365   5737   9081   -458   2066   -263       C  
ATOM    273  N   VAL A  40      12.026  32.482  18.223  1.00 53.07           N  
ANISOU  273  N   VAL A  40     6124   5596   8445   -315   1547   -240       N  
ATOM    274  CA  VAL A  40      11.042  33.433  18.757  1.00 53.07           C  
ANISOU  274  CA  VAL A  40     6191   5602   8370   -321   1455   -217       C  
ATOM    275  C   VAL A  40      11.022  33.444  20.303  1.00 54.26           C  
ANISOU  275  C   VAL A  40     6254   5801   8563   -284   1278   -273       C  
ATOM    276  O   VAL A  40      10.815  34.494  20.895  1.00 53.99           O  
ANISOU  276  O   VAL A  40     6209   5749   8557   -306   1223   -290       O  
ATOM    277  CB  VAL A  40       9.631  33.271  18.150  1.00 52.20           C  
ANISOU  277  CB  VAL A  40     6259   5509   8063   -300   1446   -137       C  
ATOM    278  CG1 VAL A  40       9.649  33.520  16.647  1.00 51.97           C  
ANISOU  278  CG1 VAL A  40     6344   5417   7984   -337   1609    -83       C  
ATOM    279  CG2 VAL A  40       9.037  31.912  18.478  1.00 52.31           C  
ANISOU  279  CG2 VAL A  40     6304   5595   7978   -234   1358   -127       C  
ATOM    280  N   VAL A  41      11.293  32.304  20.945  1.00 55.79           N  
ANISOU  280  N   VAL A  41     6390   6046   8762   -227   1193   -305       N  
ATOM    281  CA  VAL A  41      11.369  32.193  22.406  1.00 57.36           C  
ANISOU  281  CA  VAL A  41     6522   6283   8988   -181   1026   -360       C  
ATOM    282  C   VAL A  41      12.602  32.942  22.902  1.00 60.34           C  
ANISOU  282  C   VAL A  41     6746   6619   9563   -213   1006   -444       C  
ATOM    283  O   VAL A  41      12.470  33.777  23.791  1.00 60.71           O  
ANISOU  283  O   VAL A  41     6775   6660   9633   -218    908   -479       O  
ATOM    284  CB  VAL A  41      11.323  30.719  22.905  1.00 56.63           C  
ANISOU  284  CB  VAL A  41     6432   6248   8838   -106    945   -365       C  
ATOM    285  CG1 VAL A  41      11.797  30.591  24.346  1.00 56.68           C  
ANISOU  285  CG1 VAL A  41     6358   6275   8902    -56    783   -434       C  
ATOM    286  CG2 VAL A  41       9.929  30.160  22.777  1.00 56.84           C  
ANISOU  286  CG2 VAL A  41     6605   6314   8678    -76    926   -294       C  
ATOM    287  N   PHE A  42      13.782  32.703  22.300  1.00 62.42           N  
ANISOU  287  N   PHE A  42     6896   6845   9977   -238   1105   -480       N  
ATOM    288  CA  PHE A  42      14.987  33.432  22.713  1.00 64.80           C  
ANISOU  288  CA  PHE A  42     7030   7097  10495   -276   1092   -568       C  
ATOM    289  C   PHE A  42      14.896  34.914  22.333  1.00 65.01           C  
ANISOU  289  C   PHE A  42     7073   7057  10569   -359   1176   -558       C  
ATOM    290  O   PHE A  42      15.357  35.753  23.098  1.00 65.41           O  
ANISOU  290  O   PHE A  42     7033   7080  10742   -381   1096   -625       O  
ATOM    291  CB  PHE A  42      16.295  32.755  22.254  1.00 66.67           C  
ANISOU  291  CB  PHE A  42     7120   7307  10906   -278   1174   -620       C  
ATOM    292  CG  PHE A  42      16.556  31.416  22.933  1.00 69.46           C  
ANISOU  292  CG  PHE A  42     7428   7715  11248   -188   1048   -653       C  
ATOM    293  CD1 PHE A  42      17.218  30.397  22.266  1.00 71.51           C  
ANISOU  293  CD1 PHE A  42     7634   7971  11567   -166   1140   -659       C  
ATOM    294  CD2 PHE A  42      16.059  31.149  24.205  1.00 71.02           C  
ANISOU  294  CD2 PHE A  42     7663   7963  11357   -120    848   -670       C  
ATOM    295  CE1 PHE A  42      17.403  29.149  22.871  1.00 72.70           C  
ANISOU  295  CE1 PHE A  42     7758   8166  11699    -78   1022   -683       C  
ATOM    296  CE2 PHE A  42      16.231  29.901  24.797  1.00 72.18           C  
ANISOU  296  CE2 PHE A  42     7798   8153  11475    -33    738   -689       C  
ATOM    297  CZ  PHE A  42      16.904  28.911  24.129  1.00 72.40           C  
ANISOU  297  CZ  PHE A  42     7763   8175  11569    -12    821   -695       C  
ATOM    298  N   GLY A  43      14.193  35.237  21.250  1.00 64.60           N  
ANISOU  298  N   GLY A  43     7156   6982  10407   -395   1312   -474       N  
ATOM    299  CA  GLY A  43      13.924  36.618  20.868  1.00 64.36           C  
ANISOU  299  CA  GLY A  43     7178   6887  10389   -464   1386   -449       C  
ATOM    300  C   GLY A  43      13.119  37.342  21.939  1.00 64.22           C  
ANISOU  300  C   GLY A  43     7203   6891  10305   -445   1231   -460       C  
ATOM    301  O   GLY A  43      13.385  38.506  22.229  1.00 64.56           O  
ANISOU  301  O   GLY A  43     7204   6879  10446   -495   1227   -494       O  
ATOM    302  N   TYR A  44      12.147  36.660  22.572  1.00 63.32           N  
ANISOU  302  N   TYR A  44     7173   6854  10033   -375   1107   -434       N  
ATOM    303  CA  TYR A  44      11.367  37.252  23.652  1.00 62.79           C  
ANISOU  303  CA  TYR A  44     7150   6809   9898   -349    967   -448       C  
ATOM    304  C   TYR A  44      12.172  37.325  24.947  1.00 65.04           C  
ANISOU  304  C   TYR A  44     7309   7100  10301   -326    823   -547       C  
ATOM    305  O   TYR A  44      12.121  38.334  25.648  1.00 65.10           O  
ANISOU  305  O   TYR A  44     7305   7081  10350   -344    753   -589       O  
ATOM    306  CB  TYR A  44      10.070  36.480  23.870  1.00 61.11           C  
ANISOU  306  CB  TYR A  44     7065   6666   9489   -285    904   -389       C  
ATOM    307  CG  TYR A  44       8.891  37.070  23.130  1.00 59.84           C  
ANISOU  307  CG  TYR A  44     7041   6487   9207   -303    967   -310       C  
ATOM    308  CD1 TYR A  44       9.063  37.728  21.917  1.00 59.39           C  
ANISOU  308  CD1 TYR A  44     7022   6366   9180   -363   1109   -270       C  
ATOM    309  CD2 TYR A  44       7.599  36.957  23.633  1.00 59.35           C  
ANISOU  309  CD2 TYR A  44     7077   6469   9006   -258    888   -277       C  
ATOM    310  CE1 TYR A  44       7.988  38.292  21.246  1.00 59.48           C  
ANISOU  310  CE1 TYR A  44     7167   6354   9078   -370   1147   -201       C  
ATOM    311  CE2 TYR A  44       6.510  37.481  22.946  1.00 59.29           C  
ANISOU  311  CE2 TYR A  44     7183   6442   8903   -268    931   -212       C  
ATOM    312  CZ  TYR A  44       6.711  38.160  21.759  1.00 59.83           C  
ANISOU  312  CZ  TYR A  44     7292   6445   8997   -321   1051   -174       C  
ATOM    313  OH  TYR A  44       5.655  38.684  21.061  1.00 60.63           O  
ANISOU  313  OH  TYR A  44     7514   6520   9002   -322   1079   -111       O  
ATOM    314  N   LEU A  45      12.927  36.266  25.260  1.00 66.70           N  
ANISOU  314  N   LEU A  45     7432   7342  10568   -283    773   -590       N  
ATOM    315  CA  LEU A  45      13.745  36.220  26.468  1.00 68.82           C  
ANISOU  315  CA  LEU A  45     7586   7615  10947   -248    616   -689       C  
ATOM    316  C   LEU A  45      14.873  37.255  26.454  1.00 72.00           C  
ANISOU  316  C   LEU A  45     7841   7941  11576   -318    638   -770       C  
ATOM    317  O   LEU A  45      15.310  37.680  27.521  1.00 72.51           O  
ANISOU  317  O   LEU A  45     7837   7994  11720   -301    491   -855       O  
ATOM    318  CB  LEU A  45      14.322  34.810  26.700  1.00 68.41           C  
ANISOU  318  CB  LEU A  45     7477   7606  10911   -181    558   -713       C  
ATOM    319  CG  LEU A  45      13.324  33.680  26.941  1.00 68.92           C  
ANISOU  319  CG  LEU A  45     7674   7741  10773   -107    512   -648       C  
ATOM    320  CD1 LEU A  45      14.027  32.335  27.059  1.00 68.79           C  
ANISOU  320  CD1 LEU A  45     7593   7750  10794    -45    470   -674       C  
ATOM    321  CD2 LEU A  45      12.452  33.959  28.140  1.00 69.48           C  
ANISOU  321  CD2 LEU A  45     7844   7841  10714    -61    373   -652       C  
ATOM    322  N   PHE A  46      15.333  37.683  25.263  1.00 74.06           N  
ANISOU  322  N   PHE A  46     8059   8142  11938   -396    823   -746       N  
ATOM    323  CA  PHE A  46      16.423  38.661  25.168  1.00 76.38           C  
ANISOU  323  CA  PHE A  46     8203   8350  12466   -473    872   -822       C  
ATOM    324  C   PHE A  46      16.057  40.031  24.557  1.00 77.00           C  
ANISOU  324  C   PHE A  46     8347   8356  12555   -558    995   -782       C  
ATOM    325  O   PHE A  46      16.885  40.931  24.634  1.00 77.65           O  
ANISOU  325  O   PHE A  46     8311   8360  12831   -625   1022   -849       O  
ATOM    326  CB  PHE A  46      17.625  38.067  24.422  1.00 77.58           C  
ANISOU  326  CB  PHE A  46     8207   8470  12799   -499    992   -855       C  
ATOM    327  CG  PHE A  46      18.247  36.932  25.200  1.00 80.07           C  
ANISOU  327  CG  PHE A  46     8421   8838  13165   -416    842   -922       C  
ATOM    328  CD1 PHE A  46      18.246  35.644  24.697  1.00 81.58           C  
ANISOU  328  CD1 PHE A  46     8635   9074  13288   -366    895   -881       C  
ATOM    329  CD2 PHE A  46      18.719  37.129  26.488  1.00 81.65           C  
ANISOU  329  CD2 PHE A  46     8530   9041  13452   -377    632  -1022       C  
ATOM    330  CE1 PHE A  46      18.772  34.591  25.435  1.00 82.62           C  
ANISOU  330  CE1 PHE A  46     8688   9248  13455   -282    750   -937       C  
ATOM    331  CE2 PHE A  46      19.239  36.074  27.227  1.00 82.59           C  
ANISOU  331  CE2 PHE A  46     8579   9203  13596   -288    479  -1078       C  
ATOM    332  CZ  PHE A  46      19.258  34.813  26.697  1.00 82.54           C  
ANISOU  332  CZ  PHE A  46     8591   9239  13532   -241    541  -1033       C  
ATOM    333  N   CYS A  47      14.855  40.214  23.975  1.00 76.68           N  
ANISOU  333  N   CYS A  47     8486   8330  12318   -556   1062   -680       N  
ATOM    334  CA  CYS A  47      14.491  41.501  23.363  1.00 76.82           C  
ANISOU  334  CA  CYS A  47     8580   8271  12337   -629   1173   -637       C  
ATOM    335  C   CYS A  47      13.295  42.181  24.010  1.00 76.89           C  
ANISOU  335  C   CYS A  47     8715   8299  12201   -601   1066   -611       C  
ATOM    336  O   CYS A  47      13.234  43.410  24.016  1.00 77.50           O  
ANISOU  336  O   CYS A  47     8808   8306  12333   -654   1091   -619       O  
ATOM    337  CB  CYS A  47      14.286  41.372  21.854  1.00 77.38           C  
ANISOU  337  CB  CYS A  47     8752   8309  12342   -664   1380   -542       C  
ATOM    338  SG  CYS A  47      15.673  40.626  20.972  1.00 80.48           S  
ANISOU  338  SG  CYS A  47     9010   8666  12904   -701   1548   -569       S  
ATOM    339  N   MET A  48      12.301  41.410  24.454  1.00 76.38           N  
ANISOU  339  N   MET A  48     8746   8321  11953   -521    965   -574       N  
ATOM    340  CA  MET A  48      11.108  41.997  25.054  1.00 76.19           C  
ANISOU  340  CA  MET A  48     8839   8315  11794   -491    878   -550       C  
ATOM    341  C   MET A  48      11.344  42.330  26.520  1.00 76.40           C  
ANISOU  341  C   MET A  48     8805   8353  11870   -461    705   -644       C  
ATOM    342  O   MET A  48      11.684  41.446  27.310  1.00 77.10           O  
ANISOU  342  O   MET A  48     8842   8497  11956   -405    593   -691       O  
ATOM    343  CB  MET A  48       9.876  41.095  24.863  1.00 76.28           C  
ANISOU  343  CB  MET A  48     8982   8401  11600   -426    864   -469       C  
ATOM    344  CG  MET A  48       9.512  40.866  23.410  1.00 77.87           C  
ANISOU  344  CG  MET A  48     9270   8584  11732   -449   1015   -379       C  
ATOM    345  SD  MET A  48       9.157  42.359  22.464  1.00 79.64           S  
ANISOU  345  SD  MET A  48     9585   8707  11966   -518   1136   -326       S  
ATOM    346  CE  MET A  48       8.702  41.718  20.976  1.00 71.70           C  
ANISOU  346  CE  MET A  48     8700   7701  10840   -514   1265   -228       C  
ATOM    347  N   LYS A  49      11.189  43.612  26.889  1.00 75.75           N  
ANISOU  347  N   LYS A  49     8738   8212  11831   -496    681   -673       N  
ATOM    348  CA  LYS A  49      11.372  44.028  28.281  1.00 75.42           C  
ANISOU  348  CA  LYS A  49     8658   8172  11825   -467    514   -767       C  
ATOM    349  C   LYS A  49      10.023  44.201  29.008  1.00 73.68           C  
ANISOU  349  C   LYS A  49     8582   7993  11422   -407    435   -737       C  
ATOM    350  O   LYS A  49       9.892  43.805  30.168  1.00 73.96           O  
ANISOU  350  O   LYS A  49     8633   8074  11395   -342    296   -786       O  
ATOM    351  CB  LYS A  49      12.224  45.306  28.369  1.00 78.30           C  
ANISOU  351  CB  LYS A  49     8931   8438  12383   -546    525   -841       C  
ATOM    352  CG  LYS A  49      13.277  45.261  29.484  1.00 83.97           C  
ANISOU  352  CG  LYS A  49     9511   9148  13245   -533    369   -969       C  
ATOM    353  CD  LYS A  49      13.437  46.602  30.235  1.00 89.59           C  
ANISOU  353  CD  LYS A  49    10204   9785  14051   -569    288  -1052       C  
ATOM    354  CE  LYS A  49      14.051  47.729  29.425  1.00 93.56           C  
ANISOU  354  CE  LYS A  49    10632  10176  14739   -679    424  -1062       C  
ATOM    355  NZ  LYS A  49      13.736  49.069  30.016  1.00 95.56           N  
ANISOU  355  NZ  LYS A  49    10927  10360  15021   -706    366  -1109       N  
ATOM    356  N   ASN A  50       9.024  44.779  28.325  1.00 71.69           N  
ANISOU  356  N   ASN A  50     8436   7718  11083   -424    525   -658       N  
ATOM    357  CA  ASN A  50       7.708  44.969  28.929  1.00 70.38           C  
ANISOU  357  CA  ASN A  50     8393   7585  10764   -368    467   -631       C  
ATOM    358  C   ASN A  50       6.633  44.266  28.095  1.00 67.73           C  
ANISOU  358  C   ASN A  50     8153   7294  10286   -339    545   -527       C  
ATOM    359  O   ASN A  50       6.312  44.708  26.990  1.00 69.02           O  
ANISOU  359  O   ASN A  50     8363   7416  10446   -377    652   -462       O  
ATOM    360  CB  ASN A  50       7.402  46.459  29.174  1.00 72.30           C  
ANISOU  360  CB  ASN A  50     8672   7752  11047   -401    462   -656       C  
ATOM    361  CG  ASN A  50       7.134  47.293  27.939  1.00 77.02           C  
ANISOU  361  CG  ASN A  50     9314   8277  11671   -460    598   -587       C  
ATOM    362  OD1 ASN A  50       7.917  47.329  26.966  1.00 78.46           O  
ANISOU  362  OD1 ASN A  50     9445   8415  11951   -521    704   -566       O  
ATOM    363  ND2 ASN A  50       6.009  47.992  27.966  1.00 78.16           N  
ANISOU  363  ND2 ASN A  50     9564   8404  11729   -438    599   -549       N  
ATOM    364  N   TRP A  51       6.106  43.142  28.601  1.00 63.55           N  
ANISOU  364  N   TRP A  51     7658   6845   9643   -272    489   -513       N  
ATOM    365  CA  TRP A  51       5.147  42.337  27.849  1.00 59.76           C  
ANISOU  365  CA  TRP A  51     7253   6409   9044   -246    550   -426       C  
ATOM    366  C   TRP A  51       3.708  42.822  27.893  1.00 57.16           C  
ANISOU  366  C   TRP A  51     7027   6079   8613   -218    551   -382       C  
ATOM    367  O   TRP A  51       3.218  43.214  28.941  1.00 57.82           O  
ANISOU  367  O   TRP A  51     7140   6167   8662   -184    481   -420       O  
ATOM    368  CB  TRP A  51       5.175  40.892  28.348  1.00 58.83           C  
ANISOU  368  CB  TRP A  51     7127   6368   8858   -189    498   -428       C  
ATOM    369  CG  TRP A  51       6.442  40.145  28.069  1.00 58.03           C  
ANISOU  369  CG  TRP A  51     6928   6275   8845   -204    508   -455       C  
ATOM    370  CD1 TRP A  51       7.701  40.661  27.965  1.00 58.45           C  
ANISOU  370  CD1 TRP A  51     6876   6280   9054   -254    517   -512       C  
ATOM    371  CD2 TRP A  51       6.576  38.731  27.943  1.00 57.38           C  
ANISOU  371  CD2 TRP A  51     6838   6249   8715   -167    506   -434       C  
ATOM    372  NE1 TRP A  51       8.600  39.660  27.718  1.00 58.52           N  
ANISOU  372  NE1 TRP A  51     6806   6312   9118   -247    527   -527       N  
ATOM    373  CE2 TRP A  51       7.939  38.457  27.733  1.00 58.23           C  
ANISOU  373  CE2 TRP A  51     6831   6340   8952   -191    515   -479       C  
ATOM    374  CE3 TRP A  51       5.670  37.669  27.947  1.00 57.50           C  
ANISOU  374  CE3 TRP A  51     6927   6321   8602   -117    505   -382       C  
ATOM    375  CZ2 TRP A  51       8.414  37.163  27.533  1.00 58.49           C  
ANISOU  375  CZ2 TRP A  51     6829   6413   8982   -161    519   -473       C  
ATOM    376  CZ3 TRP A  51       6.151  36.390  27.801  1.00 58.06           C  
ANISOU  376  CZ3 TRP A  51     6967   6428   8664    -91    504   -376       C  
ATOM    377  CH2 TRP A  51       7.509  36.150  27.600  1.00 58.28           C  
ANISOU  377  CH2 TRP A  51     6887   6441   8815   -109    509   -421       C  
ATOM    378  N   ASN A  52       3.005  42.727  26.773  1.00 54.21           N  
ANISOU  378  N   ASN A  52     6711   5697   8188   -226    628   -305       N  
ATOM    379  CA  ASN A  52       1.586  43.018  26.709  1.00 51.88           C  
ANISOU  379  CA  ASN A  52     6502   5404   7807   -192    624   -263       C  
ATOM    380  C   ASN A  52       0.782  41.670  26.641  1.00 49.95           C  
ANISOU  380  C   ASN A  52     6287   5232   7461   -143    617   -222       C  
ATOM    381  O   ASN A  52       1.369  40.594  26.784  1.00 49.57           O  
ANISOU  381  O   ASN A  52     6200   5229   7406   -134    608   -231       O  
ATOM    382  CB  ASN A  52       1.258  44.022  25.561  1.00 51.74           C  
ANISOU  382  CB  ASN A  52     6538   5313   7807   -227    693   -212       C  
ATOM    383  CG  ASN A  52       1.430  43.537  24.147  1.00 52.41           C  
ANISOU  383  CG  ASN A  52     6655   5387   7873   -250    775   -147       C  
ATOM    384  OD1 ASN A  52       1.359  42.346  23.846  1.00 53.92           O  
ANISOU  384  OD1 ASN A  52     6844   5633   8011   -230    782   -123       O  
ATOM    385  ND2 ASN A  52       1.621  44.457  23.233  1.00 51.35           N  
ANISOU  385  ND2 ASN A  52     6566   5174   7772   -292    843   -115       N  
ATOM    386  N   SER A  53      -0.541  41.736  26.446  1.00 48.67           N  
ANISOU  386  N   SER A  53     6186   5073   7233   -113    617   -183       N  
ATOM    387  CA  SER A  53      -1.397  40.558  26.344  1.00 47.87           C  
ANISOU  387  CA  SER A  53     6108   5027   7055    -74    614   -149       C  
ATOM    388  C   SER A  53      -0.990  39.635  25.201  1.00 47.80           C  
ANISOU  388  C   SER A  53     6099   5032   7031    -91    659   -105       C  
ATOM    389  O   SER A  53      -0.798  38.442  25.429  1.00 48.36           O  
ANISOU  389  O   SER A  53     6149   5153   7071    -73    651   -107       O  
ATOM    390  CB  SER A  53      -2.855  40.975  26.206  1.00 47.61           C  
ANISOU  390  CB  SER A  53     6124   4978   6988    -44    607   -121       C  
ATOM    391  OG  SER A  53      -3.220  41.842  27.267  1.00 48.66           O  
ANISOU  391  OG  SER A  53     6261   5094   7136    -25    576   -165       O  
ATOM    392  N   SER A  54      -0.797  40.191  23.994  1.00 47.13           N  
ANISOU  392  N   SER A  54     6047   4896   6964   -125    711    -68       N  
ATOM    393  CA  SER A  54      -0.384  39.448  22.808  1.00 46.74           C  
ANISOU  393  CA  SER A  54     6018   4847   6893   -142    768    -27       C  
ATOM    394  C   SER A  54       0.977  38.744  22.996  1.00 46.87           C  
ANISOU  394  C   SER A  54     5962   4888   6959   -163    794    -59       C  
ATOM    395  O   SER A  54       1.140  37.620  22.531  1.00 47.82           O  
ANISOU  395  O   SER A  54     6083   5041   7045   -154    815    -41       O  
ATOM    396  CB  SER A  54      -0.352  40.364  21.595  1.00 47.41           C  
ANISOU  396  CB  SER A  54     6172   4859   6983   -174    826     15       C  
ATOM    397  OG  SER A  54      -1.663  40.659  21.148  1.00 49.05           O  
ANISOU  397  OG  SER A  54     6456   5049   7132   -141    792     53       O  
ATOM    398  N   ASN A  55       1.927  39.372  23.711  1.00 45.85           N  
ANISOU  398  N   ASN A  55     5765   4741   6916   -188    783   -113       N  
ATOM    399  CA  ASN A  55       3.221  38.764  23.990  1.00 45.46           C  
ANISOU  399  CA  ASN A  55     5629   4710   6935   -201    789   -155       C  
ATOM    400  C   ASN A  55       3.051  37.537  24.837  1.00 45.64           C  
ANISOU  400  C   ASN A  55     5632   4802   6906   -150    722   -172       C  
ATOM    401  O   ASN A  55       3.656  36.509  24.536  1.00 46.46           O  
ANISOU  401  O   ASN A  55     5705   4933   7016   -143    743   -171       O  
ATOM    402  CB  ASN A  55       4.151  39.731  24.726  1.00 45.76           C  
ANISOU  402  CB  ASN A  55     5592   4710   7085   -232    763   -221       C  
ATOM    403  CG  ASN A  55       4.522  40.962  23.974  1.00 47.17           C  
ANISOU  403  CG  ASN A  55     5779   4807   7336   -292    839   -210       C  
ATOM    404  OD1 ASN A  55       4.632  42.010  24.569  1.00 48.08           O  
ANISOU  404  OD1 ASN A  55     5877   4883   7509   -310    806   -249       O  
ATOM    405  ND2 ASN A  55       4.751  40.875  22.673  1.00 47.89           N  
ANISOU  405  ND2 ASN A  55     5907   4863   7425   -324    945   -159       N  
ATOM    406  N   VAL A  56       2.222  37.641  25.895  1.00 44.93           N  
ANISOU  406  N   VAL A  56     5569   4737   6766   -111    651   -189       N  
ATOM    407  CA  VAL A  56       1.919  36.550  26.815  1.00 44.48           C  
ANISOU  407  CA  VAL A  56     5518   4737   6647    -59    594   -201       C  
ATOM    408  C   VAL A  56       1.306  35.379  26.047  1.00 44.52           C  
ANISOU  408  C   VAL A  56     5561   4772   6584    -43    632   -146       C  
ATOM    409  O   VAL A  56       1.759  34.246  26.208  1.00 45.53           O  
ANISOU  409  O   VAL A  56     5668   4932   6698    -22    623   -151       O  
ATOM    410  CB  VAL A  56       1.017  37.025  28.001  1.00 44.64           C  
ANISOU  410  CB  VAL A  56     5579   4762   6618    -23    538   -222       C  
ATOM    411  CG1 VAL A  56       0.466  35.841  28.793  1.00 44.99           C  
ANISOU  411  CG1 VAL A  56     5658   4855   6580     29    509   -217       C  
ATOM    412  CG2 VAL A  56       1.777  37.979  28.926  1.00 44.40           C  
ANISOU  412  CG2 VAL A  56     5516   4705   6649    -30    481   -291       C  
ATOM    413  N   TYR A  57       0.325  35.646  25.179  1.00 43.47           N  
ANISOU  413  N   TYR A  57     5482   4622   6413    -52    668    -98       N  
ATOM    414  CA  TYR A  57      -0.331  34.584  24.420  1.00 43.05           C  
ANISOU  414  CA  TYR A  57     5467   4591   6300    -38    691    -54       C  
ATOM    415  C   TYR A  57       0.601  33.923  23.434  1.00 44.22           C  
ANISOU  415  C   TYR A  57     5602   4735   6463    -59    744    -40       C  
ATOM    416  O   TYR A  57       0.530  32.704  23.250  1.00 45.11           O  
ANISOU  416  O   TYR A  57     5723   4879   6539    -39    747    -27       O  
ATOM    417  CB  TYR A  57      -1.573  35.093  23.684  1.00 42.44           C  
ANISOU  417  CB  TYR A  57     5449   4487   6188    -38    697    -14       C  
ATOM    418  CG  TYR A  57      -2.625  35.688  24.582  1.00 42.53           C  
ANISOU  418  CG  TYR A  57     5470   4499   6193    -14    657    -28       C  
ATOM    419  CD1 TYR A  57      -2.906  35.129  25.821  1.00 43.49           C  
ANISOU  419  CD1 TYR A  57     5575   4655   6293     18    629    -54       C  
ATOM    420  CD2 TYR A  57      -3.342  36.815  24.197  1.00 42.97           C  
ANISOU  420  CD2 TYR A  57     5556   4511   6261    -18    653    -15       C  
ATOM    421  CE1 TYR A  57      -3.879  35.669  26.652  1.00 44.04           C  
ANISOU  421  CE1 TYR A  57     5659   4719   6356     41    611    -69       C  
ATOM    422  CE2 TYR A  57      -4.312  37.366  25.022  1.00 43.70           C  
ANISOU  422  CE2 TYR A  57     5649   4599   6356      7    625    -32       C  
ATOM    423  CZ  TYR A  57      -4.591  36.776  26.240  1.00 44.98           C  
ANISOU  423  CZ  TYR A  57     5794   4798   6499     35    610    -60       C  
ATOM    424  OH  TYR A  57      -5.536  37.318  27.070  1.00 47.55           O  
ANISOU  424  OH  TYR A  57     6125   5114   6827     61    600    -79       O  
ATOM    425  N   LEU A  58       1.458  34.714  22.771  1.00 44.13           N  
ANISOU  425  N   LEU A  58     5575   4681   6510    -99    795    -43       N  
ATOM    426  CA  LEU A  58       2.404  34.180  21.794  1.00 43.85           C  
ANISOU  426  CA  LEU A  58     5529   4634   6499   -122    869    -33       C  
ATOM    427  C   LEU A  58       3.450  33.319  22.491  1.00 44.57           C  
ANISOU  427  C   LEU A  58     5535   4758   6641   -106    850    -77       C  
ATOM    428  O   LEU A  58       3.836  32.292  21.944  1.00 44.66           O  
ANISOU  428  O   LEU A  58     5544   4783   6641    -98    886    -67       O  
ATOM    429  CB  LEU A  58       3.088  35.308  21.006  1.00 43.42           C  
ANISOU  429  CB  LEU A  58     5478   4514   6505   -173    947    -27       C  
ATOM    430  CG  LEU A  58       2.249  35.952  19.918  1.00 44.22           C  
ANISOU  430  CG  LEU A  58     5689   4570   6543   -184    983     28       C  
ATOM    431  CD1 LEU A  58       2.817  37.308  19.505  1.00 44.63           C  
ANISOU  431  CD1 LEU A  58     5750   4548   6659   -233   1048     30       C  
ATOM    432  CD2 LEU A  58       2.048  35.014  18.747  1.00 44.06           C  
ANISOU  432  CD2 LEU A  58     5743   4551   6447   -174   1030     69       C  
ATOM    433  N   PHE A  59       3.908  33.719  23.693  1.00 45.07           N  
ANISOU  433  N   PHE A  59     5535   4829   6760    -97    785   -129       N  
ATOM    434  CA  PHE A  59       4.889  32.929  24.430  1.00 46.12           C  
ANISOU  434  CA  PHE A  59     5592   4989   6943    -71    741   -176       C  
ATOM    435  C   PHE A  59       4.310  31.586  24.865  1.00 46.02           C  
ANISOU  435  C   PHE A  59     5618   5024   6843    -18    699   -158       C  
ATOM    436  O   PHE A  59       4.988  30.573  24.777  1.00 46.29           O  
ANISOU  436  O   PHE A  59     5619   5075   6896      2    704   -168       O  
ATOM    437  CB  PHE A  59       5.426  33.685  25.642  1.00 46.61           C  
ANISOU  437  CB  PHE A  59     5595   5043   7071    -66    660   -239       C  
ATOM    438  CG  PHE A  59       6.738  33.109  26.140  1.00 47.88           C  
ANISOU  438  CG  PHE A  59     5659   5211   7321    -48    617   -297       C  
ATOM    439  CD1 PHE A  59       7.926  33.360  25.468  1.00 48.48           C  
ANISOU  439  CD1 PHE A  59     5643   5251   7526    -90    679   -325       C  
ATOM    440  CD2 PHE A  59       6.787  32.356  27.303  1.00 48.87           C  
ANISOU  440  CD2 PHE A  59     5788   5371   7408     13    513   -327       C  
ATOM    441  CE1 PHE A  59       9.137  32.891  25.965  1.00 49.22           C  
ANISOU  441  CE1 PHE A  59     5630   5347   7725    -70    628   -389       C  
ATOM    442  CE2 PHE A  59       7.994  31.845  27.771  1.00 49.31           C  
ANISOU  442  CE2 PHE A  59     5756   5428   7550     40    454   -384       C  
ATOM    443  CZ  PHE A  59       9.161  32.133  27.111  1.00 49.26           C  
ANISOU  443  CZ  PHE A  59     5640   5389   7689     -1    506   -419       C  
ATOM    444  N   ASN A  60       3.040  31.574  25.262  1.00 45.67           N  
ANISOU  444  N   ASN A  60     5643   4997   6714      2    669   -132       N  
ATOM    445  CA  ASN A  60       2.319  30.361  25.633  1.00 45.65           C  
ANISOU  445  CA  ASN A  60     5685   5028   6631     44    646   -110       C  
ATOM    446  C   ASN A  60       2.137  29.447  24.436  1.00 45.04           C  
ANISOU  446  C   ASN A  60     5635   4953   6525     36    705    -70       C  
ATOM    447  O   ASN A  60       2.311  28.247  24.554  1.00 45.51           O  
ANISOU  447  O   ASN A  60     5698   5033   6562     65    699    -67       O  
ATOM    448  CB  ASN A  60       0.970  30.724  26.215  1.00 47.02           C  
ANISOU  448  CB  ASN A  60     5916   5207   6744     57    623    -93       C  
ATOM    449  CG  ASN A  60       1.036  30.919  27.688  1.00 51.20           C  
ANISOU  449  CG  ASN A  60     6448   5746   7259     91    558   -132       C  
ATOM    450  OD1 ASN A  60       0.964  29.963  28.466  1.00 52.81           O  
ANISOU  450  OD1 ASN A  60     6679   5971   7416    132    529   -134       O  
ATOM    451  ND2 ASN A  60       1.213  32.162  28.098  1.00 52.25           N  
ANISOU  451  ND2 ASN A  60     6565   5858   7431     76    535   -163       N  
ATOM    452  N   LEU A  61       1.830  30.013  23.276  1.00 44.37           N  
ANISOU  452  N   LEU A  61     5582   4842   6437      1    760    -40       N  
ATOM    453  CA  LEU A  61       1.674  29.278  22.030  1.00 44.65           C  
ANISOU  453  CA  LEU A  61     5661   4870   6436     -7    814     -6       C  
ATOM    454  C   LEU A  61       2.996  28.543  21.690  1.00 46.53           C  
ANISOU  454  C   LEU A  61     5850   5107   6721     -6    858    -26       C  
ATOM    455  O   LEU A  61       2.959  27.389  21.266  1.00 47.17           O  
ANISOU  455  O   LEU A  61     5954   5200   6767     13    874    -14       O  
ATOM    456  CB  LEU A  61       1.322  30.283  20.935  1.00 43.89           C  
ANISOU  456  CB  LEU A  61     5616   4731   6329    -41    859     22       C  
ATOM    457  CG  LEU A  61       1.118  29.770  19.528  1.00 43.90           C  
ANISOU  457  CG  LEU A  61     5691   4712   6277    -48    912     57       C  
ATOM    458  CD1 LEU A  61      -0.181  28.976  19.416  1.00 43.77           C  
ANISOU  458  CD1 LEU A  61     5728   4714   6190    -22    862     78       C  
ATOM    459  CD2 LEU A  61       1.199  30.925  18.499  1.00 43.45           C  
ANISOU  459  CD2 LEU A  61     5691   4600   6216    -82    967     81       C  
ATOM    460  N   SER A  62       4.156  29.188  21.939  1.00 46.63           N  
ANISOU  460  N   SER A  62     5786   5104   6827    -24    873    -64       N  
ATOM    461  CA  SER A  62       5.459  28.582  21.700  1.00 46.99           C  
ANISOU  461  CA  SER A  62     5763   5146   6947    -21    914    -93       C  
ATOM    462  C   SER A  62       5.760  27.483  22.686  1.00 47.07           C  
ANISOU  462  C   SER A  62     5735   5190   6958     32    840   -120       C  
ATOM    463  O   SER A  62       6.319  26.482  22.281  1.00 46.98           O  
ANISOU  463  O   SER A  62     5707   5182   6960     51    871   -124       O  
ATOM    464  CB  SER A  62       6.560  29.626  21.753  1.00 48.60           C  
ANISOU  464  CB  SER A  62     5880   5315   7271    -58    945   -133       C  
ATOM    465  OG  SER A  62       6.432  30.465  20.626  1.00 51.72           O  
ANISOU  465  OG  SER A  62     6325   5665   7661   -107   1040   -101       O  
ATOM    466  N   ILE A  63       5.392  27.639  23.967  1.00 47.51           N  
ANISOU  466  N   ILE A  63     5790   5268   6994     61    746   -137       N  
ATOM    467  CA  ILE A  63       5.581  26.571  24.955  1.00 48.83           C  
ANISOU  467  CA  ILE A  63     5953   5461   7141    119    672   -155       C  
ATOM    468  C   ILE A  63       4.709  25.338  24.576  1.00 49.10           C  
ANISOU  468  C   ILE A  63     6064   5510   7083    140    694   -109       C  
ATOM    469  O   ILE A  63       5.159  24.196  24.666  1.00 48.78           O  
ANISOU  469  O   ILE A  63     6017   5475   7043    177    685   -115       O  
ATOM    470  CB  ILE A  63       5.269  27.071  26.383  1.00 50.23           C  
ANISOU  470  CB  ILE A  63     6143   5649   7293    147    576   -179       C  
ATOM    471  CG1 ILE A  63       6.232  28.218  26.811  1.00 51.69           C  
ANISOU  471  CG1 ILE A  63     6246   5814   7580    129    537   -237       C  
ATOM    472  CG2 ILE A  63       5.265  25.913  27.395  1.00 50.91           C  
ANISOU  472  CG2 ILE A  63     6264   5753   7326    213    505   -185       C  
ATOM    473  CD1 ILE A  63       7.777  27.988  26.506  1.00 53.53           C  
ANISOU  473  CD1 ILE A  63     6364   6030   7944    128    542   -286       C  
ATOM    474  N   SER A  64       3.481  25.594  24.101  1.00 48.95           N  
ANISOU  474  N   SER A  64     6114   5489   6996    117    721    -68       N  
ATOM    475  CA  SER A  64       2.554  24.568  23.631  1.00 48.96           C  
ANISOU  475  CA  SER A  64     6182   5495   6926    125    741    -31       C  
ATOM    476  C   SER A  64       3.179  23.842  22.421  1.00 49.65           C  
ANISOU  476  C   SER A  64     6267   5569   7027    118    805    -25       C  
ATOM    477  O   SER A  64       3.116  22.618  22.364  1.00 50.61           O  
ANISOU  477  O   SER A  64     6413   5696   7121    145    805    -18       O  
ATOM    478  CB  SER A  64       1.222  25.215  23.248  1.00 48.54           C  
ANISOU  478  CB  SER A  64     6181   5435   6827     98    750      0       C  
ATOM    479  OG  SER A  64       0.290  24.295  22.716  1.00 49.30           O  
ANISOU  479  OG  SER A  64     6332   5530   6872    102    761     28       O  
ATOM    480  N   ASP A  65       3.774  24.589  21.462  1.00 48.98           N  
ANISOU  480  N   ASP A  65     6163   5462   6984     82    869    -29       N  
ATOM    481  CA  ASP A  65       4.404  24.026  20.267  1.00 48.82           C  
ANISOU  481  CA  ASP A  65     6154   5422   6973     74    950    -26       C  
ATOM    482  C   ASP A  65       5.602  23.188  20.677  1.00 49.11           C  
ANISOU  482  C   ASP A  65     6116   5465   7080    108    948    -62       C  
ATOM    483  O   ASP A  65       5.767  22.076  20.187  1.00 49.66           O  
ANISOU  483  O   ASP A  65     6208   5530   7129    129    978    -59       O  
ATOM    484  CB  ASP A  65       4.878  25.136  19.286  1.00 50.04           C  
ANISOU  484  CB  ASP A  65     6309   5541   7162     27   1033    -22       C  
ATOM    485  CG  ASP A  65       3.799  25.902  18.554  1.00 54.87           C  
ANISOU  485  CG  ASP A  65     7014   6134   7702     -1   1043     17       C  
ATOM    486  OD1 ASP A  65       2.656  25.441  18.540  1.00 55.54           O  
ANISOU  486  OD1 ASP A  65     7160   6231   7713     14    994     40       O  
ATOM    487  OD2 ASP A  65       4.104  26.978  17.999  1.00 58.24           O  
ANISOU  487  OD2 ASP A  65     7450   6526   8152    -36   1098     23       O  
ATOM    488  N   LEU A  66       6.441  23.715  21.565  1.00 49.04           N  
ANISOU  488  N   LEU A  66     6018   5461   7155    116    906   -102       N  
ATOM    489  CA  LEU A  66       7.662  23.048  21.996  1.00 49.83           C  
ANISOU  489  CA  LEU A  66     6031   5561   7342    154    887   -147       C  
ATOM    490  C   LEU A  66       7.385  21.753  22.743  1.00 50.53           C  
ANISOU  490  C   LEU A  66     6153   5668   7377    215    816   -141       C  
ATOM    491  O   LEU A  66       8.165  20.807  22.623  1.00 51.48           O  
ANISOU  491  O   LEU A  66     6238   5781   7540    251    825   -161       O  
ATOM    492  CB  LEU A  66       8.559  23.995  22.823  1.00 50.01           C  
ANISOU  492  CB  LEU A  66     5949   5578   7474    151    835   -199       C  
ATOM    493  CG  LEU A  66       9.321  25.066  22.027  1.00 51.08           C  
ANISOU  493  CG  LEU A  66     6018   5679   7712     92    928   -219       C  
ATOM    494  CD1 LEU A  66       9.836  26.162  22.938  1.00 51.34           C  
ANISOU  494  CD1 LEU A  66     5967   5705   7837     80    859   -267       C  
ATOM    495  CD2 LEU A  66      10.448  24.460  21.222  1.00 51.56           C  
ANISOU  495  CD2 LEU A  66     6009   5714   7866     94   1021   -245       C  
ATOM    496  N   ALA A  67       6.271  21.685  23.482  1.00 49.88           N  
ANISOU  496  N   ALA A  67     6143   5603   7205    226    755   -113       N  
ATOM    497  CA  ALA A  67       5.874  20.482  24.205  1.00 49.92           C  
ANISOU  497  CA  ALA A  67     6200   5616   7149    278    703    -99       C  
ATOM    498  C   ALA A  67       5.579  19.383  23.175  1.00 50.28           C  
ANISOU  498  C   ALA A  67     6296   5650   7158    277    768    -73       C  
ATOM    499  O   ALA A  67       6.101  18.264  23.304  1.00 50.73           O  
ANISOU  499  O   ALA A  67     6348   5698   7227    321    757    -83       O  
ATOM    500  CB  ALA A  67       4.642  20.765  25.074  1.00 49.74           C  
ANISOU  500  CB  ALA A  67     6250   5606   7045    278    658    -72       C  
ATOM    501  N   PHE A  68       4.825  19.732  22.106  1.00 49.70           N  
ANISOU  501  N   PHE A  68     6269   5570   7044    229    830    -46       N  
ATOM    502  CA  PHE A  68       4.514  18.805  21.028  1.00 49.96           C  
ANISOU  502  CA  PHE A  68     6360   5587   7037    224    886    -27       C  
ATOM    503  C   PHE A  68       5.795  18.355  20.313  1.00 50.32           C  
ANISOU  503  C   PHE A  68     6358   5615   7146    238    948    -56       C  
ATOM    504  O   PHE A  68       5.956  17.171  20.050  1.00 50.32           O  
ANISOU  504  O   PHE A  68     6382   5603   7134    268    962    -57       O  
ATOM    505  CB  PHE A  68       3.494  19.428  20.050  1.00 50.11           C  
ANISOU  505  CB  PHE A  68     6444   5597   7000    176    920      1       C  
ATOM    506  CG  PHE A  68       3.591  18.947  18.615  1.00 51.33           C  
ANISOU  506  CG  PHE A  68     6652   5725   7125    163    992      6       C  
ATOM    507  CD1 PHE A  68       3.167  17.679  18.261  1.00 52.06           C  
ANISOU  507  CD1 PHE A  68     6801   5805   7173    182    990     13       C  
ATOM    508  CD2 PHE A  68       4.146  19.752  17.630  1.00 52.44           C  
ANISOU  508  CD2 PHE A  68     6796   5846   7281    134   1066      3       C  
ATOM    509  CE1 PHE A  68       3.286  17.232  16.952  1.00 52.72           C  
ANISOU  509  CE1 PHE A  68     6947   5861   7222    175   1053     11       C  
ATOM    510  CE2 PHE A  68       4.268  19.297  16.319  1.00 52.95           C  
ANISOU  510  CE2 PHE A  68     6933   5882   7305    128   1140      7       C  
ATOM    511  CZ  PHE A  68       3.823  18.049  15.988  1.00 52.60           C  
ANISOU  511  CZ  PHE A  68     6947   5828   7210    150   1127      9       C  
ATOM    512  N   LEU A  69       6.687  19.302  19.965  1.00 50.40           N  
ANISOU  512  N   LEU A  69     6300   5618   7232    213    996    -80       N  
ATOM    513  CA  LEU A  69       7.921  19.003  19.233  1.00 50.08           C  
ANISOU  513  CA  LEU A  69     6203   5554   7271    220   1079   -111       C  
ATOM    514  C   LEU A  69       8.846  18.071  20.002  1.00 50.92           C  
ANISOU  514  C   LEU A  69     6234   5662   7451    282   1030   -148       C  
ATOM    515  O   LEU A  69       9.528  17.249  19.400  1.00 51.11           O  
ANISOU  515  O   LEU A  69     6241   5666   7512    305   1090   -166       O  
ATOM    516  CB  LEU A  69       8.635  20.292  18.814  1.00 49.65           C  
ANISOU  516  CB  LEU A  69     6085   5483   7297    174   1148   -129       C  
ATOM    517  CG  LEU A  69       7.863  21.202  17.871  1.00 50.24           C  
ANISOU  517  CG  LEU A  69     6247   5542   7299    119   1208    -91       C  
ATOM    518  CD1 LEU A  69       8.334  22.608  17.979  1.00 50.46           C  
ANISOU  518  CD1 LEU A  69     6214   5556   7402     77   1235   -105       C  
ATOM    519  CD2 LEU A  69       7.966  20.727  16.478  1.00 51.06           C  
ANISOU  519  CD2 LEU A  69     6428   5613   7359    109   1320    -79       C  
ATOM    520  N   CYS A  70       8.816  18.139  21.327  1.00 51.47           N  
ANISOU  520  N   CYS A  70     6272   5752   7531    314    919   -158       N  
ATOM    521  CA  CYS A  70       9.611  17.267  22.183  1.00 52.58           C  
ANISOU  521  CA  CYS A  70     6360   5890   7728    385    844   -190       C  
ATOM    522  C   CYS A  70       9.128  15.810  22.183  1.00 53.50           C  
ANISOU  522  C   CYS A  70     6561   5997   7769    428    832   -164       C  
ATOM    523  O   CYS A  70       9.919  14.926  22.470  1.00 54.24           O  
ANISOU  523  O   CYS A  70     6617   6076   7915    488    803   -190       O  
ATOM    524  CB  CYS A  70       9.698  17.835  23.594  1.00 53.41           C  
ANISOU  524  CB  CYS A  70     6434   6012   7849    411    722   -209       C  
ATOM    525  SG  CYS A  70      10.729  19.319  23.717  1.00 57.63           S  
ANISOU  525  SG  CYS A  70     6831   6542   8524    376    718   -266       S  
ATOM    526  N   THR A  71       7.853  15.552  21.834  1.00 53.39           N  
ANISOU  526  N   THR A  71     6655   5986   7644    399    854   -117       N  
ATOM    527  CA  THR A  71       7.312  14.190  21.748  1.00 53.40           C  
ANISOU  527  CA  THR A  71     6738   5970   7580    429    852    -93       C  
ATOM    528  C   THR A  71       7.681  13.498  20.443  1.00 53.05           C  
ANISOU  528  C   THR A  71     6708   5901   7549    424    945   -103       C  
ATOM    529  O   THR A  71       7.645  12.264  20.391  1.00 53.36           O  
ANISOU  529  O   THR A  71     6790   5917   7566    462    943    -99       O  
ATOM    530  CB  THR A  71       5.763  14.167  21.807  1.00 54.55           C  
ANISOU  530  CB  THR A  71     6983   6121   7622    393    842    -47       C  
ATOM    531  OG1 THR A  71       5.200  14.615  20.565  1.00 55.68           O  
ANISOU  531  OG1 THR A  71     7161   6261   7734    337    910    -35       O  
ATOM    532  CG2 THR A  71       5.196  14.931  22.973  1.00 54.72           C  
ANISOU  532  CG2 THR A  71     7009   6164   7619    389    774    -34       C  
ATOM    533  N   LEU A  72       7.921  14.284  19.363  1.00 52.12           N  
ANISOU  533  N   LEU A  72     6573   5780   7450    377   1033   -111       N  
ATOM    534  CA  LEU A  72       8.141  13.742  18.021  1.00 51.06           C  
ANISOU  534  CA  LEU A  72     6482   5617   7302    368   1135   -117       C  
ATOM    535  C   LEU A  72       9.254  12.702  17.908  1.00 51.01           C  
ANISOU  535  C   LEU A  72     6425   5585   7370    424   1167   -154       C  
ATOM    536  O   LEU A  72       8.952  11.687  17.301  1.00 51.71           O  
ANISOU  536  O   LEU A  72     6590   5649   7407    438   1199   -148       O  
ATOM    537  CB  LEU A  72       8.287  14.824  16.961  1.00 50.22           C  
ANISOU  537  CB  LEU A  72     6382   5503   7197    312   1231   -117       C  
ATOM    538  CG  LEU A  72       7.017  15.653  16.721  1.00 50.46           C  
ANISOU  538  CG  LEU A  72     6494   5545   7134    262   1207    -77       C  
ATOM    539  CD1 LEU A  72       7.223  16.658  15.587  1.00 51.34           C  
ANISOU  539  CD1 LEU A  72     6634   5636   7235    215   1305    -73       C  
ATOM    540  CD2 LEU A  72       5.782  14.785  16.480  1.00 49.68           C  
ANISOU  540  CD2 LEU A  72     6503   5439   6934    264   1166    -51       C  
ATOM    541  N   PRO A  73      10.453  12.791  18.523  1.00 50.34           N  
ANISOU  541  N   PRO A  73     6219   5501   7407    464   1146   -195       N  
ATOM    542  CA  PRO A  73      11.408  11.670  18.398  1.00 50.12           C  
ANISOU  542  CA  PRO A  73     6147   5443   7453    527   1169   -231       C  
ATOM    543  C   PRO A  73      10.831  10.326  18.880  1.00 50.78           C  
ANISOU  543  C   PRO A  73     6315   5513   7465    577   1099   -209       C  
ATOM    544  O   PRO A  73      11.105   9.321  18.260  1.00 51.78           O  
ANISOU  544  O   PRO A  73     6471   5607   7596    607   1152   -222       O  
ATOM    545  CB  PRO A  73      12.629  12.150  19.187  1.00 50.51           C  
ANISOU  545  CB  PRO A  73     6043   5497   7651    561   1121   -281       C  
ATOM    546  CG  PRO A  73      12.513  13.649  19.157  1.00 51.04           C  
ANISOU  546  CG  PRO A  73     6072   5586   7734    494   1140   -278       C  
ATOM    547  CD  PRO A  73      11.044  13.910  19.284  1.00 49.69           C  
ANISOU  547  CD  PRO A  73     6028   5439   7414    455   1100   -219       C  
ATOM    548  N   MET A  74       9.977  10.310  19.922  1.00 50.43           N  
ANISOU  548  N   MET A  74     6321   5487   7352    583    994   -174       N  
ATOM    549  CA  MET A  74       9.328   9.102  20.439  1.00 49.99           C  
ANISOU  549  CA  MET A  74     6357   5410   7227    621    939   -146       C  
ATOM    550  C   MET A  74       8.265   8.614  19.460  1.00 50.67           C  
ANISOU  550  C   MET A  74     6554   5479   7220    576   1001   -119       C  
ATOM    551  O   MET A  74       8.140   7.418  19.242  1.00 51.70           O  
ANISOU  551  O   MET A  74     6742   5572   7327    605   1010   -117       O  
ATOM    552  CB  MET A  74       8.651   9.369  21.807  1.00 49.90           C  
ANISOU  552  CB  MET A  74     6379   5417   7164    630    834   -115       C  
ATOM    553  CG  MET A  74       9.564   9.168  22.995  1.00 51.88           C  
ANISOU  553  CG  MET A  74     6575   5662   7474    709    734   -138       C  
ATOM    554  SD  MET A  74       8.833   9.516  24.613  1.00 54.55           S  
ANISOU  554  SD  MET A  74     6981   6014   7732    726    620   -103       S  
ATOM    555  CE  MET A  74       8.575  11.276  24.470  1.00 53.24           C  
ANISOU  555  CE  MET A  74     6752   5897   7580    650    637   -111       C  
ATOM    556  N   LEU A  75       7.461   9.520  18.912  1.00 50.30           N  
ANISOU  556  N   LEU A  75     6539   5454   7120    507   1031   -100       N  
ATOM    557  CA  LEU A  75       6.391   9.158  17.988  1.00 49.95           C  
ANISOU  557  CA  LEU A  75     6598   5391   6991    465   1066    -80       C  
ATOM    558  C   LEU A  75       6.962   8.649  16.660  1.00 50.84           C  
ANISOU  558  C   LEU A  75     6737   5471   7107    470   1161   -109       C  
ATOM    559  O   LEU A  75       6.479   7.628  16.158  1.00 51.85           O  
ANISOU  559  O   LEU A  75     6948   5565   7187    476   1171   -108       O  
ATOM    560  CB  LEU A  75       5.432  10.351  17.787  1.00 48.87           C  
ANISOU  560  CB  LEU A  75     6482   5281   6804    400   1058    -56       C  
ATOM    561  CG  LEU A  75       4.159  10.387  18.635  1.00 48.51           C  
ANISOU  561  CG  LEU A  75     6475   5246   6712    380    986    -22       C  
ATOM    562  CD1 LEU A  75       4.411  10.058  20.086  1.00 48.14           C  
ANISOU  562  CD1 LEU A  75     6399   5205   6689    426    923    -14       C  
ATOM    563  CD2 LEU A  75       3.473  11.713  18.506  1.00 48.83           C  
ANISOU  563  CD2 LEU A  75     6509   5314   6729    328    978     -8       C  
ATOM    564  N   ILE A  76       8.010   9.316  16.115  1.00 50.22           N  
ANISOU  564  N   ILE A  76     6592   5398   7091    468   1236   -137       N  
ATOM    565  CA  ILE A  76       8.682   8.902  14.884  1.00 50.51           C  
ANISOU  565  CA  ILE A  76     6655   5400   7137    477   1349   -167       C  
ATOM    566  C   ILE A  76       9.354   7.529  15.089  1.00 52.25           C  
ANISOU  566  C   ILE A  76     6860   5587   7408    546   1349   -194       C  
ATOM    567  O   ILE A  76       9.213   6.648  14.242  1.00 52.92           O  
ANISOU  567  O   ILE A  76     7029   5633   7447    556   1400   -206       O  
ATOM    568  CB  ILE A  76       9.688   9.968  14.391  1.00 50.48           C  
ANISOU  568  CB  ILE A  76     6572   5401   7206    457   1445   -191       C  
ATOM    569  CG1 ILE A  76       9.010  11.337  14.144  1.00 51.42           C  
ANISOU  569  CG1 ILE A  76     6722   5544   7272    391   1447   -161       C  
ATOM    570  CG2 ILE A  76      10.372   9.493  13.124  1.00 50.50           C  
ANISOU  570  CG2 ILE A  76     6613   5359   7214    468   1582   -222       C  
ATOM    571  CD1 ILE A  76      10.027  12.539  14.099  1.00 52.70           C  
ANISOU  571  CD1 ILE A  76     6778   5713   7534    368   1519   -181       C  
ATOM    572  N   ARG A  77      10.037   7.318  16.231  1.00 52.85           N  
ANISOU  572  N   ARG A  77     6839   5671   7571    599   1281   -205       N  
ATOM    573  CA  ARG A  77      10.665   6.033  16.521  1.00 54.26           C  
ANISOU  573  CA  ARG A  77     7004   5813   7800    674   1265   -228       C  
ATOM    574  C   ARG A  77       9.605   4.914  16.625  1.00 54.19           C  
ANISOU  574  C   ARG A  77     7119   5775   7695    680   1218   -198       C  
ATOM    575  O   ARG A  77       9.818   3.832  16.101  1.00 54.71           O  
ANISOU  575  O   ARG A  77     7231   5795   7761    714   1256   -217       O  
ATOM    576  CB  ARG A  77      11.539   6.114  17.794  1.00 57.51           C  
ANISOU  576  CB  ARG A  77     7298   6237   8316    735   1175   -246       C  
ATOM    577  CG  ARG A  77      12.544   4.970  17.942  1.00 64.69           C  
ANISOU  577  CG  ARG A  77     8163   7104   9314    824   1169   -284       C  
ATOM    578  CD  ARG A  77      12.270   4.080  19.147  1.00 71.23           C  
ANISOU  578  CD  ARG A  77     9035   7913  10115    887   1043   -259       C  
ATOM    579  NE  ARG A  77      12.613   2.670  18.926  1.00 77.22           N  
ANISOU  579  NE  ARG A  77     9835   8614  10892    955   1056   -274       N  
ATOM    580  CZ  ARG A  77      13.788   2.126  19.227  1.00 81.01           C  
ANISOU  580  CZ  ARG A  77    10227   9065  11488   1042   1030   -318       C  
ATOM    581  NH1 ARG A  77      14.001   0.833  19.014  1.00 81.49           N  
ANISOU  581  NH1 ARG A  77    10337   9067  11557   1103   1043   -329       N  
ATOM    582  NH2 ARG A  77      14.759   2.869  19.748  1.00 80.96           N  
ANISOU  582  NH2 ARG A  77    10080   9081  11600   1071    985   -355       N  
ATOM    583  N   SER A  78       8.454   5.186  17.245  1.00 53.66           N  
ANISOU  583  N   SER A  78     7105   5728   7556    642   1145   -155       N  
ATOM    584  CA  SER A  78       7.384   4.194  17.369  1.00 53.74           C  
ANISOU  584  CA  SER A  78     7221   5704   7493    635   1109   -127       C  
ATOM    585  C   SER A  78       6.775   3.838  16.024  1.00 54.30           C  
ANISOU  585  C   SER A  78     7384   5747   7501    594   1172   -139       C  
ATOM    586  O   SER A  78       6.622   2.662  15.742  1.00 54.58           O  
ANISOU  586  O   SER A  78     7485   5733   7520    617   1180   -148       O  
ATOM    587  CB  SER A  78       6.312   4.663  18.341  1.00 54.09           C  
ANISOU  587  CB  SER A  78     7288   5774   7491    600   1035    -83       C  
ATOM    588  OG  SER A  78       6.925   5.013  19.565  1.00 55.88           O  
ANISOU  588  OG  SER A  78     7447   6023   7763    644    972    -78       O  
ATOM    589  N   TYR A  79       6.465   4.828  15.183  1.00 54.60           N  
ANISOU  589  N   TYR A  79     7435   5809   7500    539   1213   -140       N  
ATOM    590  CA  TYR A  79       5.910   4.589  13.853  1.00 55.14           C  
ANISOU  590  CA  TYR A  79     7608   5849   7495    506   1261   -155       C  
ATOM    591  C   TYR A  79       6.919   3.893  12.941  1.00 56.94           C  
ANISOU  591  C   TYR A  79     7855   6036   7743    548   1356   -198       C  
ATOM    592  O   TYR A  79       6.542   2.999  12.194  1.00 57.44           O  
ANISOU  592  O   TYR A  79     8018   6053   7756    551   1373   -216       O  
ATOM    593  CB  TYR A  79       5.429   5.897  13.226  1.00 54.21           C  
ANISOU  593  CB  TYR A  79     7509   5762   7328    448   1276   -143       C  
ATOM    594  CG  TYR A  79       4.063   6.316  13.710  1.00 54.04           C  
ANISOU  594  CG  TYR A  79     7509   5758   7264    401   1187   -110       C  
ATOM    595  CD1 TYR A  79       2.981   5.444  13.636  1.00 54.00           C  
ANISOU  595  CD1 TYR A  79     7578   5718   7222    385   1136   -108       C  
ATOM    596  CD2 TYR A  79       3.835   7.606  14.185  1.00 54.44           C  
ANISOU  596  CD2 TYR A  79     7505   5856   7324    370   1161    -86       C  
ATOM    597  CE1 TYR A  79       1.714   5.838  14.030  1.00 54.66           C  
ANISOU  597  CE1 TYR A  79     7668   5812   7287    340   1066    -84       C  
ATOM    598  CE2 TYR A  79       2.574   8.001  14.613  1.00 54.78           C  
ANISOU  598  CE2 TYR A  79     7562   5912   7339    330   1088    -60       C  
ATOM    599  CZ  TYR A  79       1.514   7.117  14.514  1.00 55.65           C  
ANISOU  599  CZ  TYR A  79     7736   5987   7421    315   1044    -60       C  
ATOM    600  OH  TYR A  79       0.249   7.483  14.879  1.00 57.36           O  
ANISOU  600  OH  TYR A  79     7955   6210   7629    274    982    -42       O  
ATOM    601  N   ALA A  80       8.201   4.254  13.034  1.00 57.82           N  
ANISOU  601  N   ALA A  80     7869   6160   7939    582   1417   -219       N  
ATOM    602  CA  ALA A  80       9.246   3.613  12.234  1.00 59.05           C  
ANISOU  602  CA  ALA A  80     8025   6275   8135    627   1523   -265       C  
ATOM    603  C   ALA A  80       9.452   2.135  12.590  1.00 60.23           C  
ANISOU  603  C   ALA A  80     8192   6378   8315    690   1493   -281       C  
ATOM    604  O   ALA A  80       9.814   1.347  11.719  1.00 60.91           O  
ANISOU  604  O   ALA A  80     8337   6416   8391    718   1569   -316       O  
ATOM    605  CB  ALA A  80      10.559   4.376  12.356  1.00 59.13           C  
ANISOU  605  CB  ALA A  80     7901   6305   8259    646   1593   -289       C  
ATOM    606  N   THR A  81       9.231   1.749  13.856  1.00 60.67           N  
ANISOU  606  N   THR A  81     8210   6441   8402    717   1388   -255       N  
ATOM    607  CA  THR A  81       9.379   0.348  14.301  1.00 61.37           C  
ANISOU  607  CA  THR A  81     8326   6477   8515    780   1352   -261       C  
ATOM    608  C   THR A  81       8.028  -0.435  14.299  1.00 61.90           C  
ANISOU  608  C   THR A  81     8517   6509   8493    745   1299   -235       C  
ATOM    609  O   THR A  81       8.030  -1.645  14.415  1.00 62.47           O  
ANISOU  609  O   THR A  81     8638   6524   8572    786   1287   -242       O  
ATOM    610  CB  THR A  81      10.110   0.260  15.672  1.00 62.85           C  
ANISOU  610  CB  THR A  81     8412   6675   8792    845   1274   -253       C  
ATOM    611  OG1 THR A  81       9.285   0.787  16.715  1.00 64.22           O  
ANISOU  611  OG1 THR A  81     8590   6884   8926    813   1180   -204       O  
ATOM    612  CG2 THR A  81      11.475   0.977  15.673  1.00 63.27           C  
ANISOU  612  CG2 THR A  81     8324   6755   8961    880   1317   -292       C  
ATOM    613  N   GLY A  82       6.900   0.257  14.210  1.00 61.82           N  
ANISOU  613  N   GLY A  82     8547   6527   8414    672   1266   -207       N  
ATOM    614  CA  GLY A  82       5.588  -0.373  14.158  1.00 62.04           C  
ANISOU  614  CA  GLY A  82     8672   6519   8380    630   1218   -190       C  
ATOM    615  C   GLY A  82       4.885  -0.607  15.476  1.00 62.62           C  
ANISOU  615  C   GLY A  82     8738   6591   8463    625   1140   -145       C  
ATOM    616  O   GLY A  82       3.729  -1.053  15.488  1.00 63.12           O  
ANISOU  616  O   GLY A  82     8867   6621   8494    581   1109   -131       O  
ATOM    617  N   ASN A  83       5.556  -0.322  16.599  1.00 62.32           N  
ANISOU  617  N   ASN A  83     8626   6581   8473    669   1108   -124       N  
ATOM    618  CA  ASN A  83       4.952  -0.574  17.902  1.00 62.45           C  
ANISOU  618  CA  ASN A  83     8657   6587   8484    672   1044    -78       C  
ATOM    619  C   ASN A  83       5.312   0.449  18.977  1.00 61.38           C  
ANISOU  619  C   ASN A  83     8444   6509   8367    688    998    -54       C  
ATOM    620  O   ASN A  83       6.297   1.200  18.870  1.00 61.68           O  
ANISOU  620  O   ASN A  83     8398   6590   8449    712   1008    -78       O  
ATOM    621  CB  ASN A  83       5.262  -2.002  18.381  1.00 65.12           C  
ANISOU  621  CB  ASN A  83     9049   6851   8842    736   1032    -74       C  
ATOM    622  CG  ASN A  83       6.714  -2.398  18.292  1.00 70.60           C  
ANISOU  622  CG  ASN A  83     9692   7533   9598    824   1046   -107       C  
ATOM    623  OD1 ASN A  83       7.630  -1.546  18.282  1.00 72.93           O  
ANISOU  623  OD1 ASN A  83     9891   7880   9939    847   1051   -128       O  
ATOM    624  ND2 ASN A  83       6.954  -3.711  18.208  1.00 70.85           N  
ANISOU  624  ND2 ASN A  83     9783   7491   9645    875   1055   -118       N  
ATOM    625  N   TRP A  84       4.480   0.469  20.022  1.00 59.53           N  
ANISOU  625  N   TRP A  84     8245   6270   8103    670    954    -10       N  
ATOM    626  CA  TRP A  84       4.681   1.340  21.149  1.00 58.03           C  
ANISOU  626  CA  TRP A  84     8008   6124   7915    687    904     13       C  
ATOM    627  C   TRP A  84       5.480   0.552  22.159  1.00 57.47           C  
ANISOU  627  C   TRP A  84     7957   6016   7864    778    856     23       C  
ATOM    628  O   TRP A  84       5.069  -0.538  22.537  1.00 58.07           O  
ANISOU  628  O   TRP A  84     8121   6028   7917    797    854     48       O  
ATOM    629  CB  TRP A  84       3.333   1.771  21.744  1.00 56.96           C  
ANISOU  629  CB  TRP A  84     7913   5996   7732    624    893     53       C  
ATOM    630  CG  TRP A  84       3.504   2.667  22.918  1.00 56.23           C  
ANISOU  630  CG  TRP A  84     7790   5946   7631    643    846     75       C  
ATOM    631  CD1 TRP A  84       3.305   2.344  24.224  1.00 56.98           C  
ANISOU  631  CD1 TRP A  84     7944   6013   7693    679    810    112       C  
ATOM    632  CD2 TRP A  84       4.039   4.001  22.908  1.00 55.53           C  
ANISOU  632  CD2 TRP A  84     7612   5925   7563    636    826     56       C  
ATOM    633  NE1 TRP A  84       3.635   3.414  25.028  1.00 56.90           N  
ANISOU  633  NE1 TRP A  84     7892   6053   7676    695    763    115       N  
ATOM    634  CE2 TRP A  84       4.107   4.434  24.246  1.00 56.07           C  
ANISOU  634  CE2 TRP A  84     7688   6006   7610    668    770     79       C  
ATOM    635  CE3 TRP A  84       4.489   4.862  21.900  1.00 55.39           C  
ANISOU  635  CE3 TRP A  84     7519   5950   7577    607    856     22       C  
ATOM    636  CZ2 TRP A  84       4.530   5.709  24.591  1.00 56.20           C  
ANISOU  636  CZ2 TRP A  84     7631   6079   7643    665    735     65       C  
ATOM    637  CZ3 TRP A  84       4.960   6.106  22.254  1.00 55.78           C  
ANISOU  637  CZ3 TRP A  84     7492   6051   7649    603    831     12       C  
ATOM    638  CH2 TRP A  84       4.970   6.521  23.584  1.00 55.87           C  
ANISOU  638  CH2 TRP A  84     7505   6078   7647    631    766     31       C  
ATOM    639  N   THR A  85       6.666   1.042  22.524  1.00 56.19           N  
ANISOU  639  N   THR A  85     7713   5885   7752    838    815     -1       N  
ATOM    640  CA  THR A  85       7.530   0.339  23.476  1.00 55.38           C  
ANISOU  640  CA  THR A  85     7624   5744   7675    939    746      2       C  
ATOM    641  C   THR A  85       7.939   1.204  24.649  1.00 53.85           C  
ANISOU  641  C   THR A  85     7392   5588   7481    975    659      8       C  
ATOM    642  O   THR A  85       8.687   0.721  25.485  1.00 53.88           O  
ANISOU  642  O   THR A  85     7409   5560   7502   1067    581      6       O  
ATOM    643  CB  THR A  85       8.835  -0.162  22.789  1.00 57.15           C  
ANISOU  643  CB  THR A  85     7776   5949   7988   1005    760    -52       C  
ATOM    644  OG1 THR A  85       9.608   0.955  22.312  1.00 58.99           O  
ANISOU  644  OG1 THR A  85     7879   6242   8291    991    777    -96       O  
ATOM    645  CG2 THR A  85       8.575  -1.132  21.665  1.00 57.12           C  
ANISOU  645  CG2 THR A  85     7825   5899   7981    986    841    -66       C  
ATOM    646  N   TYR A  86       7.506   2.471  24.709  1.00 52.73           N  
ANISOU  646  N   TYR A  86     7206   5507   7322    912    663     11       N  
ATOM    647  CA  TYR A  86       7.923   3.397  25.750  1.00 52.07           C  
ANISOU  647  CA  TYR A  86     7083   5461   7242    942    580      8       C  
ATOM    648  C   TYR A  86       7.240   3.233  27.112  1.00 52.79           C  
ANISOU  648  C   TYR A  86     7291   5526   7240    966    525     58       C  
ATOM    649  O   TYR A  86       7.748   3.797  28.080  1.00 53.10           O  
ANISOU  649  O   TYR A  86     7319   5581   7275   1015    437     50       O  
ATOM    650  CB  TYR A  86       7.795   4.835  25.277  1.00 50.83           C  
ANISOU  650  CB  TYR A  86     6836   5372   7107    869    608    -12       C  
ATOM    651  CG  TYR A  86       8.807   5.204  24.227  1.00 50.40           C  
ANISOU  651  CG  TYR A  86     6658   5338   7152    865    651    -66       C  
ATOM    652  CD1 TYR A  86      10.081   5.616  24.580  1.00 50.86           C  
ANISOU  652  CD1 TYR A  86     6608   5410   7306    922    591   -113       C  
ATOM    653  CD2 TYR A  86       8.492   5.144  22.875  1.00 50.74           C  
ANISOU  653  CD2 TYR A  86     6699   5384   7197    805    753    -74       C  
ATOM    654  CE1 TYR A  86      11.018   5.955  23.616  1.00 51.49           C  
ANISOU  654  CE1 TYR A  86     6570   5502   7493    913    652   -165       C  
ATOM    655  CE2 TYR A  86       9.427   5.461  21.901  1.00 50.87           C  
ANISOU  655  CE2 TYR A  86     6619   5410   7297    802    813   -122       C  
ATOM    656  CZ  TYR A  86      10.689   5.870  22.277  1.00 52.05           C  
ANISOU  656  CZ  TYR A  86     6652   5571   7552    853    772   -166       C  
ATOM    657  OH  TYR A  86      11.621   6.225  21.340  1.00 54.25           O  
ANISOU  657  OH  TYR A  86     6829   5854   7929    845    851   -214       O  
ATOM    658  N   GLY A  87       6.140   2.477  27.197  1.00 52.52           N  
ANISOU  658  N   GLY A  87     7371   5447   7138    933    578    106       N  
ATOM    659  CA  GLY A  87       5.480   2.271  28.481  1.00 52.71           C  
ANISOU  659  CA  GLY A  87     7520   5435   7073    953    552    157       C  
ATOM    660  C   GLY A  87       4.242   3.102  28.739  1.00 52.72           C  
ANISOU  660  C   GLY A  87     7545   5465   7022    869    602    185       C  
ATOM    661  O   GLY A  87       3.874   3.934  27.911  1.00 53.39           O  
ANISOU  661  O   GLY A  87     7545   5601   7139    794    643    165       O  
ATOM    662  N   ASP A  88       3.600   2.898  29.908  1.00 52.05           N  
ANISOU  662  N   ASP A  88     7583   5340   6855    885    601    233       N  
ATOM    663  CA  ASP A  88       2.349   3.555  30.272  1.00 52.20           C  
ANISOU  663  CA  ASP A  88     7635   5370   6827    812    663    262       C  
ATOM    664  C   ASP A  88       2.452   5.060  30.612  1.00 51.58           C  
ANISOU  664  C   ASP A  88     7490   5365   6745    796    623    239       C  
ATOM    665  O   ASP A  88       1.617   5.823  30.139  1.00 51.43           O  
ANISOU  665  O   ASP A  88     7417   5381   6742    714    678    236       O  
ATOM    666  CB  ASP A  88       1.609   2.809  31.386  1.00 54.35           C  
ANISOU  666  CB  ASP A  88     8071   5565   7014    832    702    320       C  
ATOM    667  CG  ASP A  88       2.409   2.466  32.618  1.00 61.99           C  
ANISOU  667  CG  ASP A  88     9151   6494   7909    943    614    338       C  
ATOM    668  OD1 ASP A  88       3.507   3.036  32.790  1.00 64.34           O  
ANISOU  668  OD1 ASP A  88     9386   6835   8225   1005    505    298       O  
ATOM    669  OD2 ASP A  88       1.929   1.628  33.427  1.00 64.86           O  
ANISOU  669  OD2 ASP A  88     9670   6777   8198    970    653    391       O  
ATOM    670  N   VAL A  89       3.450   5.489  31.395  1.00 50.89           N  
ANISOU  670  N   VAL A  89     7401   5294   6641    873    521    219       N  
ATOM    671  CA  VAL A  89       3.614   6.908  31.766  1.00 50.62           C  
ANISOU  671  CA  VAL A  89     7306   5321   6608    861    474    191       C  
ATOM    672  C   VAL A  89       3.780   7.776  30.509  1.00 50.10           C  
ANISOU  672  C   VAL A  89     7084   5319   6633    792    501    150       C  
ATOM    673  O   VAL A  89       3.126   8.821  30.385  1.00 50.20           O  
ANISOU  673  O   VAL A  89     7059   5371   6644    729    533    148       O  
ATOM    674  CB  VAL A  89       4.792   7.113  32.789  1.00 51.15           C  
ANISOU  674  CB  VAL A  89     7394   5385   6656    965    337    165       C  
ATOM    675  CG1 VAL A  89       5.066   8.584  33.063  1.00 51.99           C  
ANISOU  675  CG1 VAL A  89     7420   5551   6782    949    281    124       C  
ATOM    676  CG2 VAL A  89       4.545   6.369  34.095  1.00 50.99           C  
ANISOU  676  CG2 VAL A  89     7559   5296   6519   1036    310    211       C  
ATOM    677  N   LEU A  90       4.629   7.318  29.568  1.00 49.55           N  
ANISOU  677  N   LEU A  90     6935   5251   6639    807    495    119       N  
ATOM    678  CA  LEU A  90       4.901   8.032  28.327  1.00 50.15           C  
ANISOU  678  CA  LEU A  90     6885   5376   6795    750    532     83       C  
ATOM    679  C   LEU A  90       3.741   7.951  27.324  1.00 51.53           C  
ANISOU  679  C   LEU A  90     7069   5551   6961    663    630    103       C  
ATOM    680  O   LEU A  90       3.620   8.826  26.471  1.00 52.68           O  
ANISOU  680  O   LEU A  90     7140   5736   7140    606    661     84       O  
ATOM    681  CB  LEU A  90       6.239   7.607  27.702  1.00 49.83           C  
ANISOU  681  CB  LEU A  90     6760   5331   6840    799    506     39       C  
ATOM    682  CG  LEU A  90       7.471   8.103  28.461  1.00 49.74           C  
ANISOU  682  CG  LEU A  90     6686   5334   6880    871    398     -3       C  
ATOM    683  CD1 LEU A  90       8.732   7.447  27.956  1.00 49.13           C  
ANISOU  683  CD1 LEU A  90     6530   5238   6900    931    375    -46       C  
ATOM    684  CD2 LEU A  90       7.557   9.623  28.456  1.00 49.62           C  
ANISOU  684  CD2 LEU A  90     6583   5373   6897    823    387    -31       C  
ATOM    685  N   CYS A  91       2.860   6.964  27.455  1.00 51.51           N  
ANISOU  685  N   CYS A  91     7159   5499   6915    652    673    140       N  
ATOM    686  CA  CYS A  91       1.663   6.879  26.634  1.00 52.35           C  
ANISOU  686  CA  CYS A  91     7271   5598   7020    571    747    153       C  
ATOM    687  C   CYS A  91       0.730   8.041  27.030  1.00 52.44           C  
ANISOU  687  C   CYS A  91     7272   5643   7012    518    760    164       C  
ATOM    688  O   CYS A  91       0.238   8.758  26.168  1.00 53.63           O  
ANISOU  688  O   CYS A  91     7365   5823   7188    457    785    151       O  
ATOM    689  CB  CYS A  91       0.963   5.535  26.830  1.00 54.19           C  
ANISOU  689  CB  CYS A  91     7602   5760   7229    571    788    186       C  
ATOM    690  SG  CYS A  91      -0.652   5.430  26.005  1.00 62.22           S  
ANISOU  690  SG  CYS A  91     8621   6757   8262    470    863    194       S  
ATOM    691  N   ILE A  92       0.485   8.218  28.330  1.00 51.03           N  
ANISOU  691  N   ILE A  92     7156   5453   6782    545    744    188       N  
ATOM    692  CA  ILE A  92      -0.405   9.241  28.822  1.00 50.76           C  
ANISOU  692  CA  ILE A  92     7119   5440   6726    503    765    198       C  
ATOM    693  C   ILE A  92       0.154  10.639  28.585  1.00 51.07           C  
ANISOU  693  C   ILE A  92     7068   5543   6794    494    721    164       C  
ATOM    694  O   ILE A  92      -0.581  11.513  28.129  1.00 50.91           O  
ANISOU  694  O   ILE A  92     7002   5549   6793    435    749    159       O  
ATOM    695  CB  ILE A  92      -0.747   8.978  30.319  1.00 51.41           C  
ANISOU  695  CB  ILE A  92     7316   5484   6734    543    770    232       C  
ATOM    696  CG1 ILE A  92      -1.409   7.602  30.493  1.00 52.94           C  
ANISOU  696  CG1 ILE A  92     7604   5603   6909    539    835    270       C  
ATOM    697  CG2 ILE A  92      -1.639  10.095  30.915  1.00 51.32           C  
ANISOU  697  CG2 ILE A  92     7306   5493   6701    505    800    237       C  
ATOM    698  CD1 ILE A  92      -1.510   7.207  31.972  1.00 55.67           C  
ANISOU  698  CD1 ILE A  92     8090   5898   7165    594    844    309       C  
ATOM    699  N   SER A  93       1.460  10.853  28.862  1.00 50.79           N  
ANISOU  699  N   SER A  93     7000   5526   6771    552    649    137       N  
ATOM    700  CA  SER A  93       2.056  12.173  28.675  1.00 50.36           C  
ANISOU  700  CA  SER A  93     6856   5523   6757    539    611    101       C  
ATOM    701  C   SER A  93       2.073  12.587  27.214  1.00 49.28           C  
ANISOU  701  C   SER A  93     6635   5411   6680    482    655     83       C  
ATOM    702  O   SER A  93       1.675  13.719  26.921  1.00 49.02           O  
ANISOU  702  O   SER A  93     6560   5406   6658    435    668     76       O  
ATOM    703  CB  SER A  93       3.433  12.281  29.333  1.00 51.88           C  
ANISOU  703  CB  SER A  93     7022   5721   6970    613    520     68       C  
ATOM    704  OG  SER A  93       4.405  11.455  28.722  1.00 54.78           O  
ANISOU  704  OG  SER A  93     7348   6075   7392    649    507     49       O  
ATOM    705  N   ASN A  94       2.403  11.651  26.292  1.00 48.44           N  
ANISOU  705  N   ASN A  94     6522   5285   6599    485    683     79       N  
ATOM    706  CA  ASN A  94       2.376  11.939  24.851  1.00 48.24           C  
ANISOU  706  CA  ASN A  94     6447   5272   6609    435    732     65       C  
ATOM    707  C   ASN A  94       0.963  12.148  24.337  1.00 46.57           C  
ANISOU  707  C   ASN A  94     6266   5057   6372    371    772     86       C  
ATOM    708  O   ASN A  94       0.753  13.085  23.574  1.00 46.10           O  
ANISOU  708  O   ASN A  94     6170   5020   6327    329    786     76       O  
ATOM    709  CB  ASN A  94       3.039  10.842  24.026  1.00 50.80           C  
ANISOU  709  CB  ASN A  94     6772   5571   6959    460    757     51       C  
ATOM    710  CG  ASN A  94       4.541  10.825  24.085  1.00 57.01           C  
ANISOU  710  CG  ASN A  94     7492   6363   7805    513    730     16       C  
ATOM    711  OD1 ASN A  94       5.186  11.760  24.529  1.00 59.42           O  
ANISOU  711  OD1 ASN A  94     7734   6696   8148    523    693     -6       O  
ATOM    712  ND2 ASN A  94       5.139   9.751  23.646  1.00 59.33           N  
ANISOU  712  ND2 ASN A  94     7793   6628   8123    551    747      4       N  
ATOM    713  N   ARG A  95      -0.010  11.283  24.745  1.00 45.37           N  
ANISOU  713  N   ARG A  95     6179   4869   6190    365    788    112       N  
ATOM    714  CA  ARG A  95      -1.409  11.424  24.323  1.00 44.55           C  
ANISOU  714  CA  ARG A  95     6089   4754   6084    305    818    124       C  
ATOM    715  C   ARG A  95      -1.987  12.759  24.810  1.00 44.70           C  
ANISOU  715  C   ARG A  95     6078   4803   6102    279    809    126       C  
ATOM    716  O   ARG A  95      -2.739  13.401  24.077  1.00 44.52           O  
ANISOU  716  O   ARG A  95     6031   4789   6097    233    816    121       O  
ATOM    717  CB  ARG A  95      -2.264  10.259  24.837  1.00 44.41           C  
ANISOU  717  CB  ARG A  95     6136   4684   6054    303    847    148       C  
ATOM    718  CG  ARG A  95      -2.033   8.951  24.110  1.00 44.29           C  
ANISOU  718  CG  ARG A  95     6153   4629   6048    312    861    142       C  
ATOM    719  CD  ARG A  95      -2.788   8.843  22.793  1.00 45.49           C  
ANISOU  719  CD  ARG A  95     6294   4768   6223    258    873    124       C  
ATOM    720  NE  ARG A  95      -2.445   7.574  22.141  1.00 46.78           N  
ANISOU  720  NE  ARG A  95     6497   4889   6389    273    884    114       N  
ATOM    721  CZ  ARG A  95      -2.607   7.306  20.843  1.00 46.17           C  
ANISOU  721  CZ  ARG A  95     6426   4798   6318    249    884     88       C  
ATOM    722  NH1 ARG A  95      -2.239   6.121  20.348  1.00 44.66           N  
ANISOU  722  NH1 ARG A  95     6278   4565   6126    269    897     75       N  
ATOM    723  NH2 ARG A  95      -3.145   8.213  20.031  1.00 42.77           N  
ANISOU  723  NH2 ARG A  95     5971   4391   5888    209    867     72       N  
ATOM    724  N   TYR A  96      -1.599  13.192  26.021  1.00 44.96           N  
ANISOU  724  N   TYR A  96     6119   4849   6113    314    786    131       N  
ATOM    725  CA  TYR A  96      -2.017  14.473  26.564  1.00 46.17           C  
ANISOU  725  CA  TYR A  96     6250   5029   6263    297    777    128       C  
ATOM    726  C   TYR A  96      -1.456  15.612  25.708  1.00 47.40           C  
ANISOU  726  C   TYR A  96     6337   5220   6451    276    758    104       C  
ATOM    727  O   TYR A  96      -2.221  16.406  25.184  1.00 47.73           O  
ANISOU  727  O   TYR A  96     6357   5270   6507    234    769    104       O  
ATOM    728  CB  TYR A  96      -1.605  14.640  28.060  1.00 46.25           C  
ANISOU  728  CB  TYR A  96     6303   5039   6232    347    748    132       C  
ATOM    729  CG  TYR A  96      -1.771  16.057  28.577  1.00 46.98           C  
ANISOU  729  CG  TYR A  96     6370   5160   6322    337    730    119       C  
ATOM    730  CD1 TYR A  96      -3.026  16.573  28.857  1.00 48.39           C  
ANISOU  730  CD1 TYR A  96     6559   5331   6496    302    771    130       C  
ATOM    731  CD2 TYR A  96      -0.681  16.895  28.728  1.00 47.70           C  
ANISOU  731  CD2 TYR A  96     6415   5280   6429    359    673     89       C  
ATOM    732  CE1 TYR A  96      -3.193  17.892  29.267  1.00 49.32           C  
ANISOU  732  CE1 TYR A  96     6653   5471   6615    293    757    115       C  
ATOM    733  CE2 TYR A  96      -0.835  18.217  29.131  1.00 49.00           C  
ANISOU  733  CE2 TYR A  96     6556   5465   6596    345    656     73       C  
ATOM    734  CZ  TYR A  96      -2.094  18.718  29.385  1.00 50.25           C  
ANISOU  734  CZ  TYR A  96     6735   5616   6740    314    698     87       C  
ATOM    735  OH  TYR A  96      -2.248  20.008  29.843  1.00 52.54           O  
ANISOU  735  OH  TYR A  96     7009   5922   7033    306    682     69       O  
ATOM    736  N   VAL A  97      -0.133  15.684  25.564  1.00 47.86           N  
ANISOU  736  N   VAL A  97     6361   5294   6529    306    733     83       N  
ATOM    737  CA  VAL A  97       0.538  16.777  24.864  1.00 48.70           C  
ANISOU  737  CA  VAL A  97     6404   5426   6675    286    729     60       C  
ATOM    738  C   VAL A  97       0.047  16.976  23.418  1.00 49.65           C  
ANISOU  738  C   VAL A  97     6522   5540   6801    238    769     64       C  
ATOM    739  O   VAL A  97      -0.070  18.121  22.977  1.00 50.27           O  
ANISOU  739  O   VAL A  97     6576   5631   6893    208    773     60       O  
ATOM    740  CB  VAL A  97       2.073  16.588  24.946  1.00 49.27           C  
ANISOU  740  CB  VAL A  97     6430   5503   6788    327    706     31       C  
ATOM    741  CG1 VAL A  97       2.803  17.481  23.964  1.00 49.59           C  
ANISOU  741  CG1 VAL A  97     6405   5555   6883    297    734      9       C  
ATOM    742  CG2 VAL A  97       2.573  16.834  26.363  1.00 49.65           C  
ANISOU  742  CG2 VAL A  97     6476   5557   6831    374    640     18       C  
ATOM    743  N   LEU A  98      -0.235  15.880  22.683  1.00 49.28           N  
ANISOU  743  N   LEU A  98     6512   5471   6742    235    793     71       N  
ATOM    744  CA  LEU A  98      -0.689  16.002  21.300  1.00 48.74           C  
ANISOU  744  CA  LEU A  98     6462   5390   6665    199    817     71       C  
ATOM    745  C   LEU A  98      -2.051  16.691  21.215  1.00 49.34           C  
ANISOU  745  C   LEU A  98     6548   5464   6734    162    800     82       C  
ATOM    746  O   LEU A  98      -2.170  17.679  20.497  1.00 50.12           O  
ANISOU  746  O   LEU A  98     6642   5568   6832    139    799     80       O  
ATOM    747  CB  LEU A  98      -0.648  14.672  20.549  1.00 47.69           C  
ANISOU  747  CB  LEU A  98     6373   5229   6520    208    837     68       C  
ATOM    748  CG  LEU A  98       0.678  14.291  19.826  1.00 48.45           C  
ANISOU  748  CG  LEU A  98     6460   5321   6629    231    874     48       C  
ATOM    749  CD1 LEU A  98       0.813  14.948  18.493  1.00 48.40           C  
ANISOU  749  CD1 LEU A  98     6472   5310   6609    203    911     41       C  
ATOM    750  CD2 LEU A  98       1.910  14.481  20.675  1.00 48.99           C  
ANISOU  750  CD2 LEU A  98     6467   5408   6741    270    866     34       C  
ATOM    751  N   HIS A  99      -3.037  16.249  22.000  1.00 48.85           N  
ANISOU  751  N   HIS A  99     6498   5390   6672    160    791     94       N  
ATOM    752  CA  HIS A  99      -4.342  16.909  22.021  1.00 48.76           C  
ANISOU  752  CA  HIS A  99     6479   5374   6676    128    778     98       C  
ATOM    753  C   HIS A  99      -4.244  18.307  22.639  1.00 48.21           C  
ANISOU  753  C   HIS A  99     6374   5329   6613    128    767     97       C  
ATOM    754  O   HIS A  99      -4.880  19.233  22.139  1.00 48.46           O  
ANISOU  754  O   HIS A  99     6394   5361   6658    105    751     95       O  
ATOM    755  CB  HIS A  99      -5.379  16.066  22.782  1.00 49.58           C  
ANISOU  755  CB  HIS A  99     6595   5450   6795    123    792    107       C  
ATOM    756  CG  HIS A  99      -6.271  15.243  21.900  1.00 51.68           C  
ANISOU  756  CG  HIS A  99     6875   5679   7082     96    786     99       C  
ATOM    757  ND1 HIS A  99      -5.763  14.222  21.112  1.00 52.98           N  
ANISOU  757  ND1 HIS A  99     7075   5825   7229    104    788     92       N  
ATOM    758  CD2 HIS A  99      -7.617  15.290  21.739  1.00 52.58           C  
ANISOU  758  CD2 HIS A  99     6968   5767   7243     65    775     91       C  
ATOM    759  CE1 HIS A  99      -6.806  13.695  20.490  1.00 53.22           C  
ANISOU  759  CE1 HIS A  99     7112   5819   7289     75    770     79       C  
ATOM    760  NE2 HIS A  99      -7.939  14.312  20.822  1.00 53.39           N  
ANISOU  760  NE2 HIS A  99     7095   5835   7357     51    758     76       N  
ATOM    761  N   ALA A 100      -3.465  18.468  23.716  1.00 47.42           N  
ANISOU  761  N   ALA A 100     6265   5247   6505    156    767     96       N  
ATOM    762  CA  ALA A 100      -3.354  19.762  24.381  1.00 47.27           C  
ANISOU  762  CA  ALA A 100     6219   5248   6493    157    751     88       C  
ATOM    763  C   ALA A 100      -2.739  20.825  23.476  1.00 47.59           C  
ANISOU  763  C   ALA A 100     6232   5300   6551    139    745     78       C  
ATOM    764  O   ALA A 100      -3.241  21.944  23.432  1.00 47.57           O  
ANISOU  764  O   ALA A 100     6216   5298   6560    120    736     77       O  
ATOM    765  CB  ALA A 100      -2.607  19.647  25.699  1.00 47.10           C  
ANISOU  765  CB  ALA A 100     6206   5238   6454    197    737     82       C  
ATOM    766  N   ASN A 101      -1.728  20.459  22.684  1.00 47.81           N  
ANISOU  766  N   ASN A 101     6255   5327   6582    142    760     72       N  
ATOM    767  CA  ASN A 101      -1.129  21.409  21.747  1.00 48.43           C  
ANISOU  767  CA  ASN A 101     6319   5404   6677    121    778     65       C  
ATOM    768  C   ASN A 101      -2.134  21.851  20.662  1.00 48.49           C  
ANISOU  768  C   ASN A 101     6367   5392   6664     92    777     80       C  
ATOM    769  O   ASN A 101      -2.132  23.007  20.256  1.00 49.63           O  
ANISOU  769  O   ASN A 101     6511   5531   6815     74    778     82       O  
ATOM    770  CB  ASN A 101       0.181  20.859  21.132  1.00 49.33           C  
ANISOU  770  CB  ASN A 101     6421   5515   6807    132    814     53       C  
ATOM    771  CG  ASN A 101       0.693  21.656  19.957  1.00 52.27           C  
ANISOU  771  CG  ASN A 101     6799   5872   7189    104    860     52       C  
ATOM    772  OD1 ASN A 101       0.744  21.182  18.839  1.00 53.70           O  
ANISOU  772  OD1 ASN A 101     7026   6034   7342     98    897     58       O  
ATOM    773  ND2 ASN A 101       1.017  22.906  20.164  1.00 53.37           N  
ANISOU  773  ND2 ASN A 101     6905   6013   7361     86    862     46       N  
ATOM    774  N   LEU A 102      -2.969  20.938  20.201  1.00 47.33           N  
ANISOU  774  N   LEU A 102     6256   5230   6496     91    767     87       N  
ATOM    775  CA  LEU A 102      -3.923  21.211  19.161  1.00 47.28           C  
ANISOU  775  CA  LEU A 102     6291   5200   6473     72    744     93       C  
ATOM    776  C   LEU A 102      -4.961  22.256  19.607  1.00 48.11           C  
ANISOU  776  C   LEU A 102     6374   5304   6603     63    708     96       C  
ATOM    777  O   LEU A 102      -5.149  23.272  18.926  1.00 48.64           O  
ANISOU  777  O   LEU A 102     6461   5356   6662     53    693    101       O  
ATOM    778  CB  LEU A 102      -4.577  19.886  18.785  1.00 47.63           C  
ANISOU  778  CB  LEU A 102     6366   5225   6506     74    731     89       C  
ATOM    779  CG  LEU A 102      -5.236  19.777  17.419  1.00 50.04           C  
ANISOU  779  CG  LEU A 102     6732   5498   6782     64    698     85       C  
ATOM    780  CD1 LEU A 102      -4.189  19.639  16.324  1.00 50.62           C  
ANISOU  780  CD1 LEU A 102     6866   5561   6806     69    738     85       C  
ATOM    781  CD2 LEU A 102      -6.125  18.558  17.364  1.00 50.66           C  
ANISOU  781  CD2 LEU A 102     6818   5554   6875     61    670     73       C  
ATOM    782  N   TYR A 103      -5.585  22.044  20.786  1.00 47.45           N  
ANISOU  782  N   TYR A 103     6254   5230   6547     69    703     92       N  
ATOM    783  CA  TYR A 103      -6.653  22.894  21.282  1.00 46.49           C  
ANISOU  783  CA  TYR A 103     6105   5103   6458     63    681     90       C  
ATOM    784  C   TYR A 103      -6.174  24.141  22.055  1.00 46.79           C  
ANISOU  784  C   TYR A 103     6117   5157   6503     68    688     87       C  
ATOM    785  O   TYR A 103      -6.908  25.124  22.074  1.00 46.86           O  
ANISOU  785  O   TYR A 103     6114   5155   6536     63    667     84       O  
ATOM    786  CB  TYR A 103      -7.647  22.060  22.073  1.00 45.75           C  
ANISOU  786  CB  TYR A 103     5990   5000   6395     63    691     86       C  
ATOM    787  CG  TYR A 103      -8.289  21.027  21.172  1.00 46.47           C  
ANISOU  787  CG  TYR A 103     6098   5063   6495     52    671     81       C  
ATOM    788  CD1 TYR A 103      -8.094  19.665  21.388  1.00 47.31           C  
ANISOU  788  CD1 TYR A 103     6221   5162   6594     54    698     83       C  
ATOM    789  CD2 TYR A 103      -8.946  21.406  20.009  1.00 46.93           C  
ANISOU  789  CD2 TYR A 103     6169   5098   6563     43    616     73       C  
ATOM    790  CE1 TYR A 103      -8.618  18.711  20.518  1.00 47.79           C  
ANISOU  790  CE1 TYR A 103     6300   5192   6665     41    675     73       C  
ATOM    791  CE2 TYR A 103      -9.511  20.462  19.154  1.00 47.58           C  
ANISOU  791  CE2 TYR A 103     6273   5151   6653     34    582     60       C  
ATOM    792  CZ  TYR A 103      -9.343  19.115  19.410  1.00 48.46           C  
ANISOU  792  CZ  TYR A 103     6392   5255   6764     31    614     58       C  
ATOM    793  OH  TYR A 103      -9.891  18.195  18.550  1.00 49.87           O  
ANISOU  793  OH  TYR A 103     6594   5400   6955     21    576     40       O  
ATOM    794  N   THR A 104      -4.958  24.138  22.659  1.00 46.65           N  
ANISOU  794  N   THR A 104     6091   5161   6474     79    708     82       N  
ATOM    795  CA  THR A 104      -4.438  25.364  23.300  1.00 46.40           C  
ANISOU  795  CA  THR A 104     6036   5139   6456     80    703     71       C  
ATOM    796  C   THR A 104      -4.012  26.329  22.187  1.00 46.56           C  
ANISOU  796  C   THR A 104     6066   5143   6482     59    706     76       C  
ATOM    797  O   THR A 104      -4.239  27.516  22.326  1.00 47.52           O  
ANISOU  797  O   THR A 104     6179   5254   6621     52    694     73       O  
ATOM    798  CB  THR A 104      -3.227  25.128  24.256  1.00 46.82           C  
ANISOU  798  CB  THR A 104     6071   5212   6506    101    706     54       C  
ATOM    799  OG1 THR A 104      -2.257  24.323  23.618  1.00 48.00           O  
ANISOU  799  OG1 THR A 104     6221   5365   6654    104    721     54       O  
ATOM    800  CG2 THR A 104      -3.600  24.482  25.551  1.00 46.91           C  
ANISOU  800  CG2 THR A 104     6096   5231   6497    128    702     51       C  
ATOM    801  N   SER A 105      -3.423  25.831  21.080  1.00 45.82           N  
ANISOU  801  N   SER A 105     6000   5040   6370     51    727     85       N  
ATOM    802  CA  SER A 105      -2.968  26.693  20.001  1.00 45.66           C  
ANISOU  802  CA  SER A 105     6010   4995   6345     32    749     94       C  
ATOM    803  C   SER A 105      -4.063  27.542  19.380  1.00 44.98           C  
ANISOU  803  C   SER A 105     5963   4879   6247     26    714    109       C  
ATOM    804  O   SER A 105      -3.859  28.744  19.232  1.00 45.49           O  
ANISOU  804  O   SER A 105     6035   4924   6324     14    721    114       O  
ATOM    805  CB  SER A 105      -2.224  25.906  18.933  1.00 47.52           C  
ANISOU  805  CB  SER A 105     6283   5220   6552     28    791    100       C  
ATOM    806  OG  SER A 105      -3.115  25.058  18.234  1.00 51.12           O  
ANISOU  806  OG  SER A 105     6791   5665   6969     35    765    110       O  
ATOM    807  N   ILE A 106      -5.215  26.960  19.042  1.00 44.01           N  
ANISOU  807  N   ILE A 106     5862   4748   6110     35    673    113       N  
ATOM    808  CA  ILE A 106      -6.305  27.735  18.449  1.00 44.11           C  
ANISOU  808  CA  ILE A 106     5906   4729   6124     39    621    121       C  
ATOM    809  C   ILE A 106      -6.865  28.746  19.468  1.00 45.23           C  
ANISOU  809  C   ILE A 106     5996   4874   6315     43    604    111       C  
ATOM    810  O   ILE A 106      -7.204  29.872  19.075  1.00 46.24           O  
ANISOU  810  O   ILE A 106     6147   4972   6449     45    580    119       O  
ATOM    811  CB  ILE A 106      -7.383  26.838  17.781  1.00 43.65           C  
ANISOU  811  CB  ILE A 106     5874   4655   6057     48    568    117       C  
ATOM    812  CG1 ILE A 106      -8.411  27.660  16.962  1.00 43.58           C  
ANISOU  812  CG1 ILE A 106     5906   4604   6048     61    495    121       C  
ATOM    813  CG2 ILE A 106      -8.055  25.903  18.775  1.00 43.61           C  
ANISOU  813  CG2 ILE A 106     5804   4671   6097     51    565    100       C  
ATOM    814  CD1 ILE A 106      -9.225  26.749  15.983  1.00 44.76           C  
ANISOU  814  CD1 ILE A 106     6100   4728   6180     71    428    111       C  
ATOM    815  N   LEU A 107      -6.880  28.387  20.784  1.00 44.75           N  
ANISOU  815  N   LEU A 107     5877   4844   6282     48    622     95       N  
ATOM    816  CA  LEU A 107      -7.346  29.267  21.859  1.00 44.94           C  
ANISOU  816  CA  LEU A 107     5861   4870   6343     56    618     80       C  
ATOM    817  C   LEU A 107      -6.431  30.463  22.111  1.00 46.26           C  
ANISOU  817  C   LEU A 107     6028   5033   6515     47    633     76       C  
ATOM    818  O   LEU A 107      -6.915  31.587  22.301  1.00 46.79           O  
ANISOU  818  O   LEU A 107     6091   5079   6608     51    616     71       O  
ATOM    819  CB  LEU A 107      -7.557  28.508  23.155  1.00 44.72           C  
ANISOU  819  CB  LEU A 107     5800   4868   6324     67    642     66       C  
ATOM    820  CG  LEU A 107      -8.896  27.876  23.337  1.00 45.39           C  
ANISOU  820  CG  LEU A 107     5863   4942   6442     72    637     62       C  
ATOM    821  CD1 LEU A 107      -8.919  27.160  24.611  1.00 45.91           C  
ANISOU  821  CD1 LEU A 107     5918   5024   6503     82    681     54       C  
ATOM    822  CD2 LEU A 107     -10.014  28.911  23.310  1.00 45.82           C  
ANISOU  822  CD2 LEU A 107     5892   4969   6549     79    610     51       C  
ATOM    823  N   PHE A 108      -5.114  30.254  22.070  1.00 46.54           N  
ANISOU  823  N   PHE A 108     6063   5081   6537     36    663     74       N  
ATOM    824  CA  PHE A 108      -4.165  31.369  22.192  1.00 46.82           C  
ANISOU  824  CA  PHE A 108     6089   5104   6595     20    680     65       C  
ATOM    825  C   PHE A 108      -4.332  32.315  21.016  1.00 47.31           C  
ANISOU  825  C   PHE A 108     6201   5121   6653      4    682     88       C  
ATOM    826  O   PHE A 108      -4.346  33.515  21.246  1.00 48.17           O  
ANISOU  826  O   PHE A 108     6308   5205   6789     -2    678     83       O  
ATOM    827  CB  PHE A 108      -2.707  30.890  22.356  1.00 46.40           C  
ANISOU  827  CB  PHE A 108     6008   5069   6552     11    711     51       C  
ATOM    828  CG  PHE A 108      -2.477  30.365  23.753  1.00 46.23           C  
ANISOU  828  CG  PHE A 108     5949   5081   6536     34    690     23       C  
ATOM    829  CD1 PHE A 108      -2.797  31.133  24.857  1.00 46.81           C  
ANISOU  829  CD1 PHE A 108     6009   5155   6621     45    664      0       C  
ATOM    830  CD2 PHE A 108      -1.976  29.093  23.959  1.00 46.64           C  
ANISOU  830  CD2 PHE A 108     5993   5158   6571     50    695     20       C  
ATOM    831  CE1 PHE A 108      -2.633  30.630  26.138  1.00 47.64           C  
ANISOU  831  CE1 PHE A 108     6107   5283   6710     74    643    -23       C  
ATOM    832  CE2 PHE A 108      -1.802  28.594  25.244  1.00 47.26           C  
ANISOU  832  CE2 PHE A 108     6059   5259   6640     80    669     -1       C  
ATOM    833  CZ  PHE A 108      -2.140  29.360  26.326  1.00 47.10           C  
ANISOU  833  CZ  PHE A 108     6039   5238   6620     92    644    -22       C  
ATOM    834  N   LEU A 109      -4.599  31.794  19.794  1.00 46.94           N  
ANISOU  834  N   LEU A 109     6212   5057   6566      4    683    114       N  
ATOM    835  CA  LEU A 109      -4.827  32.662  18.622  1.00 46.85           C  
ANISOU  835  CA  LEU A 109     6277   4993   6530     -1    679    141       C  
ATOM    836  C   LEU A 109      -6.177  33.386  18.668  1.00 46.72           C  
ANISOU  836  C   LEU A 109     6271   4952   6528     22    612    143       C  
ATOM    837  O   LEU A 109      -6.311  34.481  18.128  1.00 46.48           O  
ANISOU  837  O   LEU A 109     6292   4875   6494     22    602    160       O  
ATOM    838  CB  LEU A 109      -4.648  31.926  17.287  1.00 46.60           C  
ANISOU  838  CB  LEU A 109     6326   4945   6437     -2    696    164       C  
ATOM    839  CG  LEU A 109      -3.325  32.150  16.564  1.00 47.07           C  
ANISOU  839  CG  LEU A 109     6427   4979   6480    -29    782    178       C  
ATOM    840  CD1 LEU A 109      -3.057  33.655  16.304  1.00 47.06           C  
ANISOU  840  CD1 LEU A 109     6462   4923   6494    -47    810    194       C  
ATOM    841  CD2 LEU A 109      -2.200  31.507  17.297  1.00 47.65           C  
ANISOU  841  CD2 LEU A 109     6416   5092   6596    -43    833    152       C  
ATOM    842  N   THR A 110      -7.166  32.779  19.318  1.00 46.38           N  
ANISOU  842  N   THR A 110     6179   4936   6509     42    571    125       N  
ATOM    843  CA  THR A 110      -8.478  33.392  19.491  1.00 46.18           C  
ANISOU  843  CA  THR A 110     6138   4887   6521     66    513    118       C  
ATOM    844  C   THR A 110      -8.341  34.576  20.454  1.00 46.58           C  
ANISOU  844  C   THR A 110     6153   4931   6613     65    529    102       C  
ATOM    845  O   THR A 110      -8.882  35.634  20.187  1.00 47.48           O  
ANISOU  845  O   THR A 110     6290   5004   6747     79    496    107       O  
ATOM    846  CB  THR A 110      -9.458  32.354  20.061  1.00 46.22           C  
ANISOU  846  CB  THR A 110     6084   4920   6559     80    492     97       C  
ATOM    847  OG1 THR A 110      -9.501  31.215  19.188  1.00 46.60           O  
ANISOU  847  OG1 THR A 110     6165   4970   6572     78    475    106       O  
ATOM    848  CG2 THR A 110     -10.835  32.934  20.313  1.00 45.47           C  
ANISOU  848  CG2 THR A 110     5950   4799   6528    105    442     80       C  
ATOM    849  N   PHE A 111      -7.590  34.413  21.556  1.00 46.22           N  
ANISOU  849  N   PHE A 111     6062   4922   6578     53    572     81       N  
ATOM    850  CA  PHE A 111      -7.406  35.487  22.530  1.00 45.74           C  
ANISOU  850  CA  PHE A 111     5976   4853   6550     53    581     58       C  
ATOM    851  C   PHE A 111      -6.514  36.590  21.985  1.00 45.39           C  
ANISOU  851  C   PHE A 111     5968   4770   6509     29    598     70       C  
ATOM    852  O   PHE A 111      -6.795  37.750  22.251  1.00 45.65           O  
ANISOU  852  O   PHE A 111     6005   4768   6573     34    585     61       O  
ATOM    853  CB  PHE A 111      -6.951  34.947  23.894  1.00 45.81           C  
ANISOU  853  CB  PHE A 111     5940   4905   6559     56    605     28       C  
ATOM    854  CG  PHE A 111      -8.108  34.280  24.617  1.00 46.40           C  
ANISOU  854  CG  PHE A 111     5988   4997   6643     81    603     17       C  
ATOM    855  CD1 PHE A 111      -9.216  35.016  25.022  1.00 46.90           C  
ANISOU  855  CD1 PHE A 111     6036   5037   6748    101    592      2       C  
ATOM    856  CD2 PHE A 111      -8.113  32.915  24.840  1.00 47.02           C  
ANISOU  856  CD2 PHE A 111     6058   5108   6698     83    620     20       C  
ATOM    857  CE1 PHE A 111     -10.305  34.396  25.626  1.00 47.25           C  
ANISOU  857  CE1 PHE A 111     6047   5088   6816    120    609    -10       C  
ATOM    858  CE2 PHE A 111      -9.205  32.295  25.450  1.00 47.35           C  
ANISOU  858  CE2 PHE A 111     6077   5155   6758    100    634     12       C  
ATOM    859  CZ  PHE A 111     -10.287  33.041  25.848  1.00 47.16           C  
ANISOU  859  CZ  PHE A 111     6030   5107   6783    116    634     -4       C  
ATOM    860  N   ILE A 112      -5.527  36.259  21.116  1.00 45.36           N  
ANISOU  860  N   ILE A 112     5996   4761   6479      4    633     90       N  
ATOM    861  CA  ILE A 112      -4.686  37.265  20.443  1.00 45.34           C  
ANISOU  861  CA  ILE A 112     6036   4708   6485    -26    671    106       C  
ATOM    862  C   ILE A 112      -5.608  38.123  19.555  1.00 46.09           C  
ANISOU  862  C   ILE A 112     6207   4744   6563     -8    636    137       C  
ATOM    863  O   ILE A 112      -5.558  39.339  19.654  1.00 46.63           O  
ANISOU  863  O   ILE A 112     6292   4765   6660    -14    638    137       O  
ATOM    864  CB  ILE A 112      -3.501  36.650  19.619  1.00 45.10           C  
ANISOU  864  CB  ILE A 112     6027   4677   6432    -56    735    122       C  
ATOM    865  CG1 ILE A 112      -2.469  35.952  20.516  1.00 45.46           C  
ANISOU  865  CG1 ILE A 112     5991   4771   6512    -68    759     86       C  
ATOM    866  CG2 ILE A 112      -2.793  37.680  18.749  1.00 45.17           C  
ANISOU  866  CG2 ILE A 112     6095   4618   6448    -88    793    146       C  
ATOM    867  CD1 ILE A 112      -1.598  34.908  19.768  1.00 45.38           C  
ANISOU  867  CD1 ILE A 112     5988   4775   6481    -81    812     97       C  
ATOM    868  N   SER A 113      -6.522  37.493  18.793  1.00 45.70           N  
ANISOU  868  N   SER A 113     6199   4692   6472     20    590    157       N  
ATOM    869  CA  SER A 113      -7.477  38.184  17.930  1.00 46.06           C  
ANISOU  869  CA  SER A 113     6320   4680   6500     50    531    182       C  
ATOM    870  C   SER A 113      -8.386  39.169  18.703  1.00 46.79           C  
ANISOU  870  C   SER A 113     6371   4753   6654     76    484    161       C  
ATOM    871  O   SER A 113      -8.632  40.278  18.218  1.00 47.17           O  
ANISOU  871  O   SER A 113     6481   4737   6704     89    461    180       O  
ATOM    872  CB  SER A 113      -8.319  37.173  17.166  1.00 46.73           C  
ANISOU  872  CB  SER A 113     6436   4774   6545     78    471    191       C  
ATOM    873  OG  SER A 113      -7.454  36.351  16.404  1.00 49.57           O  
ANISOU  873  OG  SER A 113     6847   5143   6843     56    520    209       O  
ATOM    874  N   ILE A 114      -8.893  38.765  19.890  1.00 46.10           N  
ANISOU  874  N   ILE A 114     6190   4714   6614     88    476    123       N  
ATOM    875  CA  ILE A 114      -9.706  39.653  20.723  1.00 45.52           C  
ANISOU  875  CA  ILE A 114     6073   4622   6600    113    450     96       C  
ATOM    876  C   ILE A 114      -8.819  40.807  21.244  1.00 46.56           C  
ANISOU  876  C   ILE A 114     6213   4728   6751     89    491     86       C  
ATOM    877  O   ILE A 114      -9.275  41.946  21.325  1.00 47.32           O  
ANISOU  877  O   ILE A 114     6326   4774   6881    107    469     82       O  
ATOM    878  CB  ILE A 114     -10.370  38.861  21.885  1.00 44.86           C  
ANISOU  878  CB  ILE A 114     5901   4592   6553    128    456     58       C  
ATOM    879  CG1 ILE A 114     -11.223  37.675  21.359  1.00 44.24           C  
ANISOU  879  CG1 ILE A 114     5805   4532   6473    144    420     63       C  
ATOM    880  CG2 ILE A 114     -11.161  39.788  22.823  1.00 44.93           C  
ANISOU  880  CG2 ILE A 114     5867   4579   6624    155    450     25       C  
ATOM    881  CD1 ILE A 114     -11.712  36.753  22.428  1.00 44.61           C  
ANISOU  881  CD1 ILE A 114     5776   4624   6551    147    450     34       C  
ATOM    882  N   ASP A 115      -7.543  40.526  21.550  1.00 46.63           N  
ANISOU  882  N   ASP A 115     6208   4764   6746     48    547     79       N  
ATOM    883  CA  ASP A 115      -6.610  41.543  22.011  1.00 47.21           C  
ANISOU  883  CA  ASP A 115     6278   4808   6850     18    581     62       C  
ATOM    884  C   ASP A 115      -6.372  42.592  20.934  1.00 48.22           C  
ANISOU  884  C   ASP A 115     6489   4857   6976      4    594     99       C  
ATOM    885  O   ASP A 115      -6.326  43.785  21.253  1.00 48.72           O  
ANISOU  885  O   ASP A 115     6562   4869   7079     -1    595     87       O  
ATOM    886  CB  ASP A 115      -5.268  40.933  22.454  1.00 47.87           C  
ANISOU  886  CB  ASP A 115     6319   4932   6936    -20    627     42       C  
ATOM    887  CG  ASP A 115      -4.387  41.975  23.116  1.00 51.95           C  
ANISOU  887  CG  ASP A 115     6814   5419   7507    -49    646      7       C  
ATOM    888  OD1 ASP A 115      -4.835  42.576  24.114  1.00 52.93           O  
ANISOU  888  OD1 ASP A 115     6916   5540   7656    -30    617    -29       O  
ATOM    889  OD2 ASP A 115      -3.263  42.227  22.602  1.00 53.27           O  
ANISOU  889  OD2 ASP A 115     6987   5557   7697    -93    693     14       O  
ATOM    890  N   ARG A 116      -6.195  42.150  19.664  1.00 47.81           N  
ANISOU  890  N   ARG A 116     6508   4786   6870     -3    608    145       N  
ATOM    891  CA  ARG A 116      -5.973  43.048  18.538  1.00 47.40           C  
ANISOU  891  CA  ARG A 116     6564   4651   6795    -13    630    189       C  
ATOM    892  C   ARG A 116      -7.205  43.893  18.293  1.00 48.74           C  
ANISOU  892  C   ARG A 116     6784   4767   6969     37    555    202       C  
ATOM    893  O   ARG A 116      -7.065  45.077  18.009  1.00 49.95           O  
ANISOU  893  O   ARG A 116     6999   4844   7136     31    568    220       O  
ATOM    894  CB  ARG A 116      -5.536  42.318  17.259  1.00 47.24           C  
ANISOU  894  CB  ARG A 116     6629   4621   6701    -25    668    233       C  
ATOM    895  CG  ARG A 116      -4.410  41.280  17.398  1.00 49.21           C  
ANISOU  895  CG  ARG A 116     6822   4926   6949    -64    739    218       C  
ATOM    896  CD  ARG A 116      -3.225  41.700  18.248  1.00 52.00           C  
ANISOU  896  CD  ARG A 116     7093   5285   7379   -113    802    182       C  
ATOM    897  NE  ARG A 116      -2.544  42.896  17.733  1.00 54.44           N  
ANISOU  897  NE  ARG A 116     7460   5507   7717   -152    870    202       N  
ATOM    898  CZ  ARG A 116      -1.607  43.566  18.398  1.00 55.62           C  
ANISOU  898  CZ  ARG A 116     7542   5637   7952   -197    915    167       C  
ATOM    899  NH1 ARG A 116      -1.221  43.161  19.599  1.00 54.88           N  
ANISOU  899  NH1 ARG A 116     7331   5607   7913   -202    888    109       N  
ATOM    900  NH2 ARG A 116      -1.041  44.638  17.862  1.00 55.93           N  
ANISOU  900  NH2 ARG A 116     7639   5589   8025   -237    985    188       N  
ATOM    901  N   TYR A 117      -8.399  43.331  18.473  1.00 49.16           N  
ANISOU  901  N   TYR A 117     6801   4853   7023     86    478    189       N  
ATOM    902  CA  TYR A 117      -9.647  44.064  18.341  1.00 50.68           C  
ANISOU  902  CA  TYR A 117     7015   4998   7243    141    395    190       C  
ATOM    903  C   TYR A 117      -9.781  45.137  19.439  1.00 51.46           C  
ANISOU  903  C   TYR A 117     7059   5077   7416    145    404    153       C  
ATOM    904  O   TYR A 117     -10.130  46.279  19.124  1.00 52.55           O  
ANISOU  904  O   TYR A 117     7257   5139   7572    168    376    167       O  
ATOM    905  CB  TYR A 117     -10.856  43.104  18.361  1.00 51.34           C  
ANISOU  905  CB  TYR A 117     7044   5124   7338    186    319    171       C  
ATOM    906  CG  TYR A 117     -12.185  43.816  18.453  1.00 53.07           C  
ANISOU  906  CG  TYR A 117     7245   5299   7619    246    234    155       C  
ATOM    907  CD1 TYR A 117     -12.703  44.499  17.365  1.00 54.60           C  
ANISOU  907  CD1 TYR A 117     7542   5413   7790    289    157    189       C  
ATOM    908  CD2 TYR A 117     -12.890  43.864  19.646  1.00 54.54           C  
ANISOU  908  CD2 TYR A 117     7319   5516   7888    264    234    106       C  
ATOM    909  CE1 TYR A 117     -13.897  45.201  17.457  1.00 56.17           C  
ANISOU  909  CE1 TYR A 117     7717   5567   8060    351     71    170       C  
ATOM    910  CE2 TYR A 117     -14.110  44.519  19.737  1.00 56.00           C  
ANISOU  910  CE2 TYR A 117     7475   5656   8146    322    165     85       C  
ATOM    911  CZ  TYR A 117     -14.623  45.171  18.630  1.00 57.99           C  
ANISOU  911  CZ  TYR A 117     7815   5832   8387    367     76    115       C  
ATOM    912  OH  TYR A 117     -15.813  45.873  18.715  1.00 61.67           O  
ANISOU  912  OH  TYR A 117     8246   6247   8938    431     -2     91       O  
ATOM    913  N   LEU A 118      -9.556  44.780  20.722  1.00 50.58           N  
ANISOU  913  N   LEU A 118     6848   5028   7341    128    437    105       N  
ATOM    914  CA  LEU A 118      -9.671  45.764  21.802  1.00 49.81           C  
ANISOU  914  CA  LEU A 118     6711   4911   7304    135    445     63       C  
ATOM    915  C   LEU A 118      -8.607  46.871  21.678  1.00 49.64           C  
ANISOU  915  C   LEU A 118     6740   4828   7294     92    489     71       C  
ATOM    916  O   LEU A 118      -8.880  48.022  21.980  1.00 49.50           O  
ANISOU  916  O   LEU A 118     6738   4751   7318    106    477     57       O  
ATOM    917  CB  LEU A 118      -9.629  45.076  23.171  1.00 49.69           C  
ANISOU  917  CB  LEU A 118     6605   4971   7305    131    470     11       C  
ATOM    918  CG  LEU A 118     -10.849  44.199  23.473  1.00 50.75           C  
ANISOU  918  CG  LEU A 118     6683   5147   7453    173    441     -3       C  
ATOM    919  CD1 LEU A 118     -10.625  43.334  24.696  1.00 50.92           C  
ANISOU  919  CD1 LEU A 118     6642   5238   7466    163    483    -41       C  
ATOM    920  CD2 LEU A 118     -12.093  45.036  23.651  1.00 51.11           C  
ANISOU  920  CD2 LEU A 118     6714   5145   7562    226    401    -21       C  
ATOM    921  N   LEU A 119      -7.411  46.528  21.208  1.00 49.68           N  
ANISOU  921  N   LEU A 119     6767   4839   7270     38    545     91       N  
ATOM    922  CA  LEU A 119      -6.327  47.487  20.996  1.00 50.00           C  
ANISOU  922  CA  LEU A 119     6847   4815   7338    -13    602     98       C  
ATOM    923  C   LEU A 119      -6.642  48.452  19.840  1.00 51.67           C  
ANISOU  923  C   LEU A 119     7178   4924   7529      0    598    154       C  
ATOM    924  O   LEU A 119      -6.181  49.597  19.826  1.00 52.41           O  
ANISOU  924  O   LEU A 119     7310   4940   7662    -27    631    156       O  
ATOM    925  CB  LEU A 119      -5.026  46.740  20.708  1.00 49.06           C  
ANISOU  925  CB  LEU A 119     6709   4727   7205    -70    672    104       C  
ATOM    926  CG  LEU A 119      -3.770  47.578  20.719  1.00 48.48           C  
ANISOU  926  CG  LEU A 119     6635   4595   7189   -134    743     93       C  
ATOM    927  CD1 LEU A 119      -3.504  48.115  22.085  1.00 47.68           C  
ANISOU  927  CD1 LEU A 119     6453   4505   7159   -144    721     23       C  
ATOM    928  CD2 LEU A 119      -2.601  46.768  20.217  1.00 49.54           C  
ANISOU  928  CD2 LEU A 119     6752   4754   7319   -183    817    104       C  
ATOM    929  N   MET A 120      -7.396  47.985  18.860  1.00 52.16           N  
ANISOU  929  N   MET A 120     7308   4980   7529     41    554    198       N  
ATOM    930  CA  MET A 120      -7.833  48.797  17.744  1.00 53.49           C  
ANISOU  930  CA  MET A 120     7611   5051   7661     71    527    253       C  
ATOM    931  C   MET A 120      -8.789  49.902  18.256  1.00 53.52           C  
ANISOU  931  C   MET A 120     7609   5003   7724    121    461    232       C  
ATOM    932  O   MET A 120      -8.716  51.035  17.801  1.00 54.64           O  
ANISOU  932  O   MET A 120     7845   5047   7871    124    469    261       O  
ATOM    933  CB  MET A 120      -8.525  47.861  16.743  1.00 55.57           C  
ANISOU  933  CB  MET A 120     7935   5334   7846    114    467    288       C  
ATOM    934  CG  MET A 120      -9.265  48.541  15.649  1.00 60.61           C  
ANISOU  934  CG  MET A 120     8714   5878   8436    169    399    338       C  
ATOM    935  SD  MET A 120     -10.237  47.306  14.772  1.00 72.54           S  
ANISOU  935  SD  MET A 120    10258   7429   9876    229    293    351       S  
ATOM    936  CE  MET A 120      -9.036  46.640  13.732  1.00 67.50           C  
ANISOU  936  CE  MET A 120     9731   6784   9130    176    392    399       C  
ATOM    937  N   LYS A 121      -9.644  49.584  19.228  1.00 52.58           N  
ANISOU  937  N   LYS A 121     7382   4944   7652    159    408    180       N  
ATOM    938  CA  LYS A 121     -10.606  50.521  19.797  1.00 51.83           C  
ANISOU  938  CA  LYS A 121     7265   4806   7621    212    354    151       C  
ATOM    939  C   LYS A 121     -10.020  51.358  20.919  1.00 50.98           C  
ANISOU  939  C   LYS A 121     7112   4685   7575    178    405    103       C  
ATOM    940  O   LYS A 121     -10.442  52.488  21.107  1.00 51.31           O  
ANISOU  940  O   LYS A 121     7182   4653   7662    206    383     93       O  
ATOM    941  CB  LYS A 121     -11.812  49.749  20.355  1.00 53.46           C  
ANISOU  941  CB  LYS A 121     7372   5078   7860    266    293    112       C  
ATOM    942  CG  LYS A 121     -12.694  49.140  19.295  1.00 58.30           C  
ANISOU  942  CG  LYS A 121     8023   5685   8442    316    209    145       C  
ATOM    943  CD  LYS A 121     -13.747  48.260  19.918  1.00 64.64           C  
ANISOU  943  CD  LYS A 121     8706   6556   9297    353    169    100       C  
ATOM    944  CE  LYS A 121     -14.801  49.014  20.678  1.00 69.10           C  
ANISOU  944  CE  LYS A 121     9203   7091   9959    408    137     54       C  
ATOM    945  NZ  LYS A 121     -15.599  48.081  21.510  1.00 72.76           N  
ANISOU  945  NZ  LYS A 121     9539   7627  10480    423    145      5       N  
ATOM    946  N   PHE A 122      -9.152  50.767  21.738  1.00 50.06           N  
ANISOU  946  N   PHE A 122     6920   4638   7462    126    460     66       N  
ATOM    947  CA  PHE A 122      -8.569  51.387  22.923  1.00 49.51           C  
ANISOU  947  CA  PHE A 122     6800   4566   7445     96    493      7       C  
ATOM    948  C   PHE A 122      -7.056  51.135  22.886  1.00 50.25           C  
ANISOU  948  C   PHE A 122     6883   4674   7535     18    559      5       C  
ATOM    949  O   PHE A 122      -6.547  50.200  23.532  1.00 50.75           O  
ANISOU  949  O   PHE A 122     6875   4820   7589     -3    572    -27       O  
ATOM    950  CB  PHE A 122      -9.163  50.775  24.208  1.00 48.75           C  
ANISOU  950  CB  PHE A 122     6610   4550   7363    128    476    -54       C  
ATOM    951  CG  PHE A 122     -10.669  50.622  24.197  1.00 49.05           C  
ANISOU  951  CG  PHE A 122     6627   4592   7416    202    425    -56       C  
ATOM    952  CD1 PHE A 122     -11.493  51.728  24.263  1.00 49.47           C  
ANISOU  952  CD1 PHE A 122     6702   4572   7522    250    393    -67       C  
ATOM    953  CD2 PHE A 122     -11.259  49.374  24.063  1.00 49.51           C  
ANISOU  953  CD2 PHE A 122     6641   4722   7450    222    409    -47       C  
ATOM    954  CE1 PHE A 122     -12.868  51.587  24.201  1.00 49.69           C  
ANISOU  954  CE1 PHE A 122     6696   4599   7585    319    344    -73       C  
ATOM    955  CE2 PHE A 122     -12.634  49.237  24.040  1.00 49.62           C  
ANISOU  955  CE2 PHE A 122     6619   4733   7501    285    363    -55       C  
ATOM    956  CZ  PHE A 122     -13.426  50.343  24.106  1.00 49.36           C  
ANISOU  956  CZ  PHE A 122     6597   4628   7528    334    330    -70       C  
ATOM    957  N   PRO A 123      -6.319  51.972  22.124  1.00 49.11           N  
ANISOU  957  N   PRO A 123     6811   4442   7406    -26    604     39       N  
ATOM    958  CA  PRO A 123      -4.870  51.745  21.987  1.00 48.57           C  
ANISOU  958  CA  PRO A 123     6721   4376   7356   -104    678     36       C  
ATOM    959  C   PRO A 123      -4.062  51.835  23.291  1.00 48.63           C  
ANISOU  959  C   PRO A 123     6632   4417   7430   -141    682    -45       C  
ATOM    960  O   PRO A 123      -2.986  51.235  23.421  1.00 48.36           O  
ANISOU  960  O   PRO A 123     6540   4419   7414   -190    718    -65       O  
ATOM    961  CB  PRO A 123      -4.438  52.815  20.962  1.00 48.88           C  
ANISOU  961  CB  PRO A 123     6868   4295   7411   -139    735     88       C  
ATOM    962  CG  PRO A 123      -5.697  53.243  20.270  1.00 49.15           C  
ANISOU  962  CG  PRO A 123     7000   4278   7397    -68    677    137       C  
ATOM    963  CD  PRO A 123      -6.786  53.092  21.283  1.00 47.77           C  
ANISOU  963  CD  PRO A 123     6751   4162   7239     -4    594     86       C  
ATOM    964  N   PHE A 124      -4.583  52.586  24.263  1.00 48.72           N  
ANISOU  964  N   PHE A 124     6626   4409   7475   -111    638    -96       N  
ATOM    965  CA  PHE A 124      -3.877  52.844  25.517  1.00 48.56           C  
ANISOU  965  CA  PHE A 124     6538   4404   7510   -138    626   -179       C  
ATOM    966  C   PHE A 124      -4.059  51.737  26.569  1.00 47.69           C  
ANISOU  966  C   PHE A 124     6359   4402   7357   -105    587   -225       C  
ATOM    967  O   PHE A 124      -3.437  51.822  27.631  1.00 47.81           O  
ANISOU  967  O   PHE A 124     6330   4434   7402   -120    564   -295       O  
ATOM    968  CB  PHE A 124      -4.232  54.254  26.067  1.00 48.50           C  
ANISOU  968  CB  PHE A 124     6561   4310   7556   -125    605   -217       C  
ATOM    969  CG  PHE A 124      -3.640  55.364  25.208  1.00 48.61           C  
ANISOU  969  CG  PHE A 124     6636   4206   7627   -179    656   -184       C  
ATOM    970  CD1 PHE A 124      -4.267  55.776  24.037  1.00 48.54           C  
ANISOU  970  CD1 PHE A 124     6724   4130   7588   -156    674   -105       C  
ATOM    971  CD2 PHE A 124      -2.399  55.910  25.507  1.00 49.22           C  
ANISOU  971  CD2 PHE A 124     6676   4234   7791   -253    689   -230       C  
ATOM    972  CE1 PHE A 124      -3.680  56.740  23.210  1.00 48.65           C  
ANISOU  972  CE1 PHE A 124     6812   4027   7644   -206    736    -66       C  
ATOM    973  CE2 PHE A 124      -1.831  56.890  24.682  1.00 49.02           C  
ANISOU  973  CE2 PHE A 124     6708   4091   7826   -310    755   -196       C  
ATOM    974  CZ  PHE A 124      -2.477  57.301  23.548  1.00 48.04           C  
ANISOU  974  CZ  PHE A 124     6695   3899   7658   -286    785   -110       C  
ATOM    975  N   ARG A 125      -4.847  50.667  26.248  1.00 46.17           N  
ANISOU  975  N   ARG A 125     6166   4279   7098    -63    578   -186       N  
ATOM    976  CA  ARG A 125      -5.058  49.498  27.099  1.00 44.67           C  
ANISOU  976  CA  ARG A 125     5926   4185   6861    -34    556   -215       C  
ATOM    977  C   ARG A 125      -5.579  49.831  28.502  1.00 45.62           C  
ANISOU  977  C   ARG A 125     6035   4316   6980      7    526   -282       C  
ATOM    978  O   ARG A 125      -5.076  49.284  29.488  1.00 47.08           O  
ANISOU  978  O   ARG A 125     6191   4552   7144      7    509   -331       O  
ATOM    979  CB  ARG A 125      -3.789  48.630  27.175  1.00 42.70           C  
ANISOU  979  CB  ARG A 125     5628   3985   6612    -79    570   -228       C  
ATOM    980  CG  ARG A 125      -3.271  48.104  25.845  1.00 40.82           C  
ANISOU  980  CG  ARG A 125     5400   3745   6365   -115    616   -165       C  
ATOM    981  CD  ARG A 125      -2.157  47.115  26.136  1.00 42.54           C  
ANISOU  981  CD  ARG A 125     5555   4021   6589   -144    624   -190       C  
ATOM    982  NE  ARG A 125      -1.750  46.367  24.950  1.00 43.73           N  
ANISOU  982  NE  ARG A 125     5714   4182   6718   -168    675   -134       N  
ATOM    983  CZ  ARG A 125      -2.295  45.223  24.563  1.00 44.60           C  
ANISOU  983  CZ  ARG A 125     5835   4352   6761   -138    672    -98       C  
ATOM    984  NH1 ARG A 125      -1.888  44.634  23.451  1.00 43.83           N  
ANISOU  984  NH1 ARG A 125     5759   4254   6642   -160    721    -51       N  
ATOM    985  NH2 ARG A 125      -3.254  44.656  25.288  1.00 44.44           N  
ANISOU  985  NH2 ARG A 125     5807   4385   6695    -87    627   -111       N  
ATOM    986  N   GLU A 126      -6.597  50.675  28.594  1.00 44.84           N  
ANISOU  986  N   GLU A 126     5969   4170   6900     47    518   -285       N  
ATOM    987  CA  GLU A 126      -7.129  51.040  29.893  1.00 46.40           C  
ANISOU  987  CA  GLU A 126     6166   4368   7094     88    504   -350       C  
ATOM    988  C   GLU A 126      -7.970  49.966  30.525  1.00 48.11           C  
ANISOU  988  C   GLU A 126     6362   4659   7257    136    514   -357       C  
ATOM    989  O   GLU A 126      -8.067  49.926  31.754  1.00 49.68           O  
ANISOU  989  O   GLU A 126     6570   4878   7430    161    516   -414       O  
ATOM    990  CB  GLU A 126      -7.919  52.345  29.826  1.00 49.00           C  
ANISOU  990  CB  GLU A 126     6532   4614   7472    119    500   -358       C  
ATOM    991  CG  GLU A 126      -7.058  53.530  29.436  1.00 53.87           C  
ANISOU  991  CG  GLU A 126     7178   5142   8146     69    498   -364       C  
ATOM    992  CD  GLU A 126      -7.305  53.939  28.005  1.00 60.06           C  
ANISOU  992  CD  GLU A 126     8004   5866   8950     61    508   -287       C  
ATOM    993  OE1 GLU A 126      -7.308  55.158  27.754  1.00 59.15           O  
ANISOU  993  OE1 GLU A 126     7935   5657   8885     55    508   -287       O  
ATOM    994  OE2 GLU A 126      -7.542  53.058  27.145  1.00 64.66           O  
ANISOU  994  OE2 GLU A 126     8584   6490   9494     66    513   -228       O  
ATOM    995  N   HIS A 127      -8.618  49.121  29.715  1.00 47.36           N  
ANISOU  995  N   HIS A 127     6250   4599   7146    150    524   -301       N  
ATOM    996  CA  HIS A 127      -9.507  48.094  30.226  1.00 47.22           C  
ANISOU  996  CA  HIS A 127     6206   4641   7094    190    544   -304       C  
ATOM    997  C   HIS A 127      -8.768  46.962  30.936  1.00 48.11           C  
ANISOU  997  C   HIS A 127     6310   4825   7145    175    552   -320       C  
ATOM    998  O   HIS A 127      -7.660  46.589  30.525  1.00 48.56           O  
ANISOU  998  O   HIS A 127     6359   4901   7190    133    538   -306       O  
ATOM    999  CB  HIS A 127     -10.344  47.542  29.073  1.00 47.61           C  
ANISOU  999  CB  HIS A 127     6236   4698   7156    205    538   -245       C  
ATOM   1000  CG  HIS A 127     -11.252  48.564  28.470  1.00 49.77           C  
ANISOU 1000  CG  HIS A 127     6522   4900   7488    237    516   -232       C  
ATOM   1001  ND1 HIS A 127     -12.555  48.719  28.906  1.00 51.49           N  
ANISOU 1001  ND1 HIS A 127     6710   5104   7749    293    524   -257       N  
ATOM   1002  CD2 HIS A 127     -11.002  49.485  27.518  1.00 50.97           C  
ANISOU 1002  CD2 HIS A 127     6717   4985   7665    225    487   -199       C  
ATOM   1003  CE1 HIS A 127     -13.057  49.707  28.195  1.00 51.69           C  
ANISOU 1003  CE1 HIS A 127     6755   5058   7827    317    488   -240       C  
ATOM   1004  NE2 HIS A 127     -12.159  50.204  27.352  1.00 51.96           N  
ANISOU 1004  NE2 HIS A 127     6842   5055   7844    278    464   -203       N  
ATOM   1005  N   ILE A 128      -9.393  46.390  31.987  1.00 47.77           N  
ANISOU 1005  N   ILE A 128     6270   4816   7064    213    582   -350       N  
ATOM   1006  CA  ILE A 128      -8.871  45.237  32.727  1.00 47.86           C  
ANISOU 1006  CA  ILE A 128     6291   4890   7006    213    591   -361       C  
ATOM   1007  C   ILE A 128      -8.604  44.065  31.755  1.00 47.92           C  
ANISOU 1007  C   ILE A 128     6264   4943   7001    187    588   -304       C  
ATOM   1008  O   ILE A 128      -7.532  43.463  31.831  1.00 48.41           O  
ANISOU 1008  O   ILE A 128     6326   5038   7032    163    568   -305       O  
ATOM   1009  CB  ILE A 128      -9.820  44.813  33.891  1.00 48.12           C  
ANISOU 1009  CB  ILE A 128     6349   4937   6998    262    645   -390       C  
ATOM   1010  CG1 ILE A 128     -10.006  45.964  34.905  1.00 48.84           C  
ANISOU 1010  CG1 ILE A 128     6488   4979   7089    290    652   -454       C  
ATOM   1011  CG2 ILE A 128      -9.335  43.538  34.574  1.00 47.93           C  
ANISOU 1011  CG2 ILE A 128     6350   4969   6892    266    657   -390       C  
ATOM   1012  CD1 ILE A 128     -11.235  45.855  35.743  1.00 50.07           C  
ANISOU 1012  CD1 ILE A 128     6665   5128   7233    339    728   -476       C  
ATOM   1013  N   LEU A 129      -9.528  43.810  30.785  1.00 46.91           N  
ANISOU 1013  N   LEU A 129     6107   4810   6905    194    600   -259       N  
ATOM   1014  CA  LEU A 129      -9.381  42.766  29.759  1.00 46.39           C  
ANISOU 1014  CA  LEU A 129     6020   4779   6828    172    594   -207       C  
ATOM   1015  C   LEU A 129      -8.070  42.924  28.940  1.00 46.56           C  
ANISOU 1015  C   LEU A 129     6049   4795   6848    126    569   -187       C  
ATOM   1016  O   LEU A 129      -7.596  41.951  28.359  1.00 47.15           O  
ANISOU 1016  O   LEU A 129     6114   4906   6897    106    572   -157       O  
ATOM   1017  CB  LEU A 129     -10.567  42.813  28.757  1.00 46.31           C  
ANISOU 1017  CB  LEU A 129     5987   4744   6863    190    586   -173       C  
ATOM   1018  CG  LEU A 129     -11.958  42.260  29.132  1.00 46.64           C  
ANISOU 1018  CG  LEU A 129     5991   4794   6934    227    616   -181       C  
ATOM   1019  CD1 LEU A 129     -12.838  42.152  27.905  1.00 45.82           C  
ANISOU 1019  CD1 LEU A 129     5859   4669   6881    238    577   -148       C  
ATOM   1020  CD2 LEU A 129     -11.871  40.914  29.695  1.00 47.70           C  
ANISOU 1020  CD2 LEU A 129     6118   4983   7023    223    654   -180       C  
ATOM   1021  N   GLN A 130      -7.513  44.158  28.858  1.00 46.26           N  
ANISOU 1021  N   GLN A 130     6027   4704   6844    106    554   -203       N  
ATOM   1022  CA  GLN A 130      -6.295  44.513  28.089  1.00 45.22           C  
ANISOU 1022  CA  GLN A 130     5899   4549   6733     56    550   -188       C  
ATOM   1023  C   GLN A 130      -5.017  44.509  28.906  1.00 44.56           C  
ANISOU 1023  C   GLN A 130     5797   4480   6655     31    538   -237       C  
ATOM   1024  O   GLN A 130      -3.979  44.816  28.353  1.00 44.11           O  
ANISOU 1024  O   GLN A 130     5727   4398   6635    -14    543   -233       O  
ATOM   1025  CB  GLN A 130      -6.451  45.896  27.439  1.00 45.26           C  
ANISOU 1025  CB  GLN A 130     5935   4473   6786     46    547   -176       C  
ATOM   1026  CG  GLN A 130      -7.668  46.043  26.535  1.00 45.58           C  
ANISOU 1026  CG  GLN A 130     6001   4487   6830     78    538   -131       C  
ATOM   1027  CD  GLN A 130      -7.698  47.435  25.959  1.00 47.72           C  
ANISOU 1027  CD  GLN A 130     6319   4670   7143     72    531   -118       C  
ATOM   1028  OE1 GLN A 130      -8.229  48.362  26.563  1.00 47.68           O  
ANISOU 1028  OE1 GLN A 130     6319   4625   7172     98    519   -150       O  
ATOM   1029  NE2 GLN A 130      -7.090  47.632  24.790  1.00 48.73           N  
ANISOU 1029  NE2 GLN A 130     6489   4759   7266     37    546    -70       N  
ATOM   1030  N   LYS A 131      -5.082  44.188  30.211  1.00 44.68           N  
ANISOU 1030  N   LYS A 131     5814   4527   6635     61    520   -285       N  
ATOM   1031  CA  LYS A 131      -3.908  44.159  31.072  1.00 45.38           C  
ANISOU 1031  CA  LYS A 131     5892   4626   6725     49    483   -340       C  
ATOM   1032  C   LYS A 131      -3.109  42.865  30.939  1.00 47.10           C  
ANISOU 1032  C   LYS A 131     6079   4898   6917     40    476   -327       C  
ATOM   1033  O   LYS A 131      -3.688  41.798  30.708  1.00 47.13           O  
ANISOU 1033  O   LYS A 131     6088   4945   6873     60    500   -288       O  
ATOM   1034  CB  LYS A 131      -4.298  44.390  32.531  1.00 46.13           C  
ANISOU 1034  CB  LYS A 131     6028   4723   6778     93    461   -398       C  
ATOM   1035  CG  LYS A 131      -5.047  45.679  32.773  1.00 49.04           C  
ANISOU 1035  CG  LYS A 131     6425   5033   7175    107    470   -420       C  
ATOM   1036  CD  LYS A 131      -4.296  46.950  32.341  1.00 52.35           C  
ANISOU 1036  CD  LYS A 131     6830   5385   7674     62    448   -441       C  
ATOM   1037  CE  LYS A 131      -5.117  48.170  32.709  1.00 56.68           C  
ANISOU 1037  CE  LYS A 131     7417   5874   8245     87    454   -468       C  
ATOM   1038  NZ  LYS A 131      -4.524  49.451  32.220  1.00 59.26           N  
ANISOU 1038  NZ  LYS A 131     7740   6123   8654     42    443   -481       N  
ATOM   1039  N   LYS A 132      -1.767  42.968  31.088  1.00 48.22           N  
ANISOU 1039  N   LYS A 132     6184   5033   7103     10    442   -365       N  
ATOM   1040  CA  LYS A 132      -0.826  41.848  31.005  1.00 49.09           C  
ANISOU 1040  CA  LYS A 132     6255   5188   7210      4    427   -364       C  
ATOM   1041  C   LYS A 132      -1.177  40.783  32.030  1.00 49.83           C  
ANISOU 1041  C   LYS A 132     6386   5333   7214     59    399   -375       C  
ATOM   1042  O   LYS A 132      -1.212  39.609  31.680  1.00 50.84           O  
ANISOU 1042  O   LYS A 132     6507   5502   7308     69    419   -338       O  
ATOM   1043  CB  LYS A 132       0.608  42.327  31.241  1.00 51.33           C  
ANISOU 1043  CB  LYS A 132     6482   5444   7577    -30    381   -423       C  
ATOM   1044  CG  LYS A 132       1.634  41.212  31.076  1.00 56.62           C  
ANISOU 1044  CG  LYS A 132     7097   6152   8265    -34    365   -426       C  
ATOM   1045  CD  LYS A 132       2.465  41.015  32.326  1.00 62.34           C  
ANISOU 1045  CD  LYS A 132     7807   6887   8993     -3    266   -503       C  
ATOM   1046  CE  LYS A 132       3.667  41.907  32.371  1.00 67.15           C  
ANISOU 1046  CE  LYS A 132     8340   7445   9729    -47    224   -569       C  
ATOM   1047  NZ  LYS A 132       4.499  41.619  33.568  1.00 70.77           N  
ANISOU 1047  NZ  LYS A 132     8782   7913  10193     -9    104   -650       N  
ATOM   1048  N   GLU A 133      -1.496  41.193  33.275  1.00 49.26           N  
ANISOU 1048  N   GLU A 133     6365   5252   7099     97    362   -424       N  
ATOM   1049  CA  GLU A 133      -1.865  40.313  34.386  1.00 49.00           C  
ANISOU 1049  CA  GLU A 133     6396   5253   6968    154    346   -436       C  
ATOM   1050  C   GLU A 133      -3.152  39.525  34.091  1.00 48.14           C  
ANISOU 1050  C   GLU A 133     6314   5170   6807    173    423   -375       C  
ATOM   1051  O   GLU A 133      -3.275  38.367  34.487  1.00 48.29           O  
ANISOU 1051  O   GLU A 133     6365   5223   6761    202    431   -359       O  
ATOM   1052  CB  GLU A 133      -1.981  41.108  35.707  1.00 52.12           C  
ANISOU 1052  CB  GLU A 133     6861   5620   7324    189    302   -503       C  
ATOM   1053  CG  GLU A 133      -0.863  42.123  35.943  1.00 60.44           C  
ANISOU 1053  CG  GLU A 133     7881   6633   8451    164    223   -572       C  
ATOM   1054  CD  GLU A 133      -1.109  43.523  35.390  1.00 72.24           C  
ANISOU 1054  CD  GLU A 133     9349   8072  10027    123    249   -578       C  
ATOM   1055  OE1 GLU A 133      -0.246  44.027  34.635  1.00 74.90           O  
ANISOU 1055  OE1 GLU A 133     9613   8381  10463     68    239   -584       O  
ATOM   1056  OE2 GLU A 133      -2.165  44.119  35.715  1.00 76.25           O  
ANISOU 1056  OE2 GLU A 133     9910   8557  10503    146    287   -579       O  
ATOM   1057  N   PHE A 134      -4.091  40.138  33.371  1.00 47.24           N  
ANISOU 1057  N   PHE A 134     6186   5034   6730    157    473   -345       N  
ATOM   1058  CA  PHE A 134      -5.323  39.463  32.989  1.00 46.81           C  
ANISOU 1058  CA  PHE A 134     6136   4995   6653    171    536   -295       C  
ATOM   1059  C   PHE A 134      -5.016  38.412  31.908  1.00 47.27           C  
ANISOU 1059  C   PHE A 134     6155   5085   6720    146    546   -245       C  
ATOM   1060  O   PHE A 134      -5.629  37.348  31.916  1.00 47.71           O  
ANISOU 1060  O   PHE A 134     6220   5167   6740    163    579   -216       O  
ATOM   1061  CB  PHE A 134      -6.342  40.487  32.475  1.00 46.33           C  
ANISOU 1061  CB  PHE A 134     6064   4895   6643    166    565   -285       C  
ATOM   1062  CG  PHE A 134      -7.735  39.928  32.358  1.00 46.67           C  
ANISOU 1062  CG  PHE A 134     6105   4945   6681    189    620   -255       C  
ATOM   1063  CD1 PHE A 134      -8.580  39.891  33.460  1.00 47.58           C  
ANISOU 1063  CD1 PHE A 134     6258   5055   6765    228    665   -281       C  
ATOM   1064  CD2 PHE A 134      -8.203  39.432  31.151  1.00 46.98           C  
ANISOU 1064  CD2 PHE A 134     6106   4993   6752    172    631   -206       C  
ATOM   1065  CE1 PHE A 134      -9.858  39.361  33.357  1.00 47.97           C  
ANISOU 1065  CE1 PHE A 134     6288   5105   6832    244    726   -259       C  
ATOM   1066  CE2 PHE A 134      -9.478  38.887  31.056  1.00 47.59           C  
ANISOU 1066  CE2 PHE A 134     6166   5072   6844    191    672   -188       C  
ATOM   1067  CZ  PHE A 134     -10.289  38.839  32.160  1.00 47.69           C  
ANISOU 1067  CZ  PHE A 134     6199   5078   6843    224    723   -215       C  
ATOM   1068  N   ALA A 135      -4.065  38.705  30.970  1.00 47.24           N  
ANISOU 1068  N   ALA A 135     6110   5072   6767    106    526   -236       N  
ATOM   1069  CA  ALA A 135      -3.641  37.782  29.905  1.00 46.82           C  
ANISOU 1069  CA  ALA A 135     6027   5041   6719     84    541   -194       C  
ATOM   1070  C   ALA A 135      -2.964  36.578  30.504  1.00 47.47           C  
ANISOU 1070  C   ALA A 135     6112   5165   6761    104    522   -205       C  
ATOM   1071  O   ALA A 135      -3.131  35.483  29.977  1.00 47.97           O  
ANISOU 1071  O   ALA A 135     6172   5254   6802    105    545   -168       O  
ATOM   1072  CB  ALA A 135      -2.706  38.467  28.937  1.00 46.50           C  
ANISOU 1072  CB  ALA A 135     5954   4972   6743     38    542   -190       C  
ATOM   1073  N   ILE A 136      -2.210  36.755  31.611  1.00 47.42           N  
ANISOU 1073  N   ILE A 136     6117   5159   6743    124    471   -256       N  
ATOM   1074  CA  ILE A 136      -1.589  35.636  32.318  1.00 47.93           C  
ANISOU 1074  CA  ILE A 136     6197   5253   6759    156    436   -269       C  
ATOM   1075  C   ILE A 136      -2.670  34.740  32.926  1.00 48.09           C  
ANISOU 1075  C   ILE A 136     6284   5292   6698    195    474   -243       C  
ATOM   1076  O   ILE A 136      -2.560  33.512  32.860  1.00 48.90           O  
ANISOU 1076  O   ILE A 136     6396   5419   6765    209    483   -217       O  
ATOM   1077  CB  ILE A 136      -0.570  36.123  33.367  1.00 48.78           C  
ANISOU 1077  CB  ILE A 136     6310   5349   6873    176    352   -338       C  
ATOM   1078  CG1 ILE A 136       0.618  36.821  32.686  1.00 49.67           C  
ANISOU 1078  CG1 ILE A 136     6337   5440   7094    129    325   -366       C  
ATOM   1079  CG2 ILE A 136      -0.077  34.959  34.230  1.00 49.50           C  
ANISOU 1079  CG2 ILE A 136     6443   5466   6899    226    303   -350       C  
ATOM   1080  CD1 ILE A 136       1.407  37.701  33.621  1.00 50.86           C  
ANISOU 1080  CD1 ILE A 136     6484   5563   7280    137    240   -443       C  
ATOM   1081  N   LEU A 137      -3.736  35.346  33.469  1.00 47.61           N  
ANISOU 1081  N   LEU A 137     6264   5212   6613    210    507   -249       N  
ATOM   1082  CA  LEU A 137      -4.870  34.623  34.026  1.00 47.75           C  
ANISOU 1082  CA  LEU A 137     6336   5235   6572    239    568   -227       C  
ATOM   1083  C   LEU A 137      -5.592  33.845  32.920  1.00 48.78           C  
ANISOU 1083  C   LEU A 137     6424   5378   6732    215    620   -173       C  
ATOM   1084  O   LEU A 137      -5.877  32.671  33.092  1.00 49.36           O  
ANISOU 1084  O   LEU A 137     6522   5465   6766    228    651   -148       O  
ATOM   1085  CB  LEU A 137      -5.823  35.605  34.716  1.00 47.69           C  
ANISOU 1085  CB  LEU A 137     6364   5198   6559    255    602   -251       C  
ATOM   1086  CG  LEU A 137      -7.105  35.010  35.246  1.00 49.02           C  
ANISOU 1086  CG  LEU A 137     6576   5360   6691    279    689   -232       C  
ATOM   1087  CD1 LEU A 137      -6.816  34.013  36.357  1.00 49.83           C  
ANISOU 1087  CD1 LEU A 137     6771   5471   6693    319    697   -235       C  
ATOM   1088  CD2 LEU A 137      -8.063  36.087  35.699  1.00 48.88           C  
ANISOU 1088  CD2 LEU A 137     6571   5308   6694    291    733   -258       C  
ATOM   1089  N   ILE A 138      -5.856  34.481  31.773  1.00 49.24           N  
ANISOU 1089  N   ILE A 138     6428   5425   6857    181    623   -156       N  
ATOM   1090  CA  ILE A 138      -6.490  33.836  30.612  1.00 49.79           C  
ANISOU 1090  CA  ILE A 138     6465   5500   6954    160    651   -112       C  
ATOM   1091  C   ILE A 138      -5.626  32.684  30.070  1.00 51.00           C  
ANISOU 1091  C   ILE A 138     6609   5680   7090    151    638    -90       C  
ATOM   1092  O   ILE A 138      -6.181  31.656  29.677  1.00 52.44           O  
ANISOU 1092  O   ILE A 138     6791   5871   7263    150    666    -62       O  
ATOM   1093  CB  ILE A 138      -6.810  34.888  29.516  1.00 49.78           C  
ANISOU 1093  CB  ILE A 138     6430   5472   7013    135    640   -101       C  
ATOM   1094  CG1 ILE A 138      -7.935  35.844  29.976  1.00 50.15           C  
ANISOU 1094  CG1 ILE A 138     6480   5488   7087    152    658   -119       C  
ATOM   1095  CG2 ILE A 138      -7.112  34.256  28.157  1.00 49.70           C  
ANISOU 1095  CG2 ILE A 138     6401   5465   7020    115    643    -60       C  
ATOM   1096  CD1 ILE A 138      -9.227  35.189  30.220  1.00 51.14           C  
ANISOU 1096  CD1 ILE A 138     6598   5612   7221    169    705   -109       C  
ATOM   1097  N   SER A 139      -4.278  32.823  30.078  1.00 49.99           N  
ANISOU 1097  N   SER A 139     6468   5560   6966    144    598   -109       N  
ATOM   1098  CA  SER A 139      -3.376  31.768  29.624  1.00 49.29           C  
ANISOU 1098  CA  SER A 139     6364   5493   6871    141    589    -97       C  
ATOM   1099  C   SER A 139      -3.479  30.561  30.546  1.00 49.16           C  
ANISOU 1099  C   SER A 139     6392   5493   6793    179    592    -93       C  
ATOM   1100  O   SER A 139      -3.590  29.432  30.073  1.00 48.89           O  
ANISOU 1100  O   SER A 139     6359   5469   6745    178    614    -65       O  
ATOM   1101  CB  SER A 139      -1.945  32.282  29.559  1.00 50.13           C  
ANISOU 1101  CB  SER A 139     6433   5597   7019    128    548   -129       C  
ATOM   1102  OG  SER A 139      -1.867  33.337  28.613  1.00 52.51           O  
ANISOU 1102  OG  SER A 139     6704   5872   7375     89    564   -123       O  
ATOM   1103  N   LEU A 140      -3.517  30.801  31.860  1.00 49.14           N  
ANISOU 1103  N   LEU A 140     6439   5486   6747    213    574   -122       N  
ATOM   1104  CA  LEU A 140      -3.682  29.729  32.833  1.00 49.83           C  
ANISOU 1104  CA  LEU A 140     6596   5578   6761    254    584   -115       C  
ATOM   1105  C   LEU A 140      -5.077  29.072  32.641  1.00 49.44           C  
ANISOU 1105  C   LEU A 140     6563   5520   6703    246    666    -77       C  
ATOM   1106  O   LEU A 140      -5.163  27.844  32.652  1.00 50.18           O  
ANISOU 1106  O   LEU A 140     6683   5617   6768    256    690    -51       O  
ATOM   1107  CB  LEU A 140      -3.508  30.281  34.260  1.00 51.06           C  
ANISOU 1107  CB  LEU A 140     6822   5719   6858    295    550   -156       C  
ATOM   1108  CG  LEU A 140      -3.881  29.317  35.404  1.00 53.46           C  
ANISOU 1108  CG  LEU A 140     7234   6014   7064    344    578   -144       C  
ATOM   1109  CD1 LEU A 140      -3.009  28.035  35.368  1.00 54.00           C  
ANISOU 1109  CD1 LEU A 140     7319   6094   7105    369    538   -129       C  
ATOM   1110  CD2 LEU A 140      -3.859  30.027  36.778  1.00 53.78           C  
ANISOU 1110  CD2 LEU A 140     7366   6033   7034    386    551   -187       C  
ATOM   1111  N   ALA A 141      -6.138  29.877  32.387  1.00 47.90           N  
ANISOU 1111  N   ALA A 141     6343   5309   6547    226    705    -76       N  
ATOM   1112  CA  ALA A 141      -7.474  29.377  32.081  1.00 47.50           C  
ANISOU 1112  CA  ALA A 141     6280   5245   6522    214    774    -50       C  
ATOM   1113  C   ALA A 141      -7.478  28.480  30.823  1.00 47.96           C  
ANISOU 1113  C   ALA A 141     6295   5313   6614    186    770    -19       C  
ATOM   1114  O   ALA A 141      -8.060  27.394  30.857  1.00 48.42           O  
ANISOU 1114  O   ALA A 141     6366   5364   6667    186    813      1       O  
ATOM   1115  CB  ALA A 141      -8.440  30.531  31.906  1.00 47.31           C  
ANISOU 1115  CB  ALA A 141     6220   5200   6555    203    793    -64       C  
ATOM   1116  N   VAL A 142      -6.807  28.909  29.729  1.00 47.68           N  
ANISOU 1116  N   VAL A 142     6219   5288   6610    164    724    -17       N  
ATOM   1117  CA  VAL A 142      -6.657  28.110  28.505  1.00 47.57           C  
ANISOU 1117  CA  VAL A 142     6181   5280   6612    142    717      8       C  
ATOM   1118  C   VAL A 142      -6.023  26.722  28.819  1.00 47.26           C  
ANISOU 1118  C   VAL A 142     6172   5254   6530    159    724     19       C  
ATOM   1119  O   VAL A 142      -6.565  25.692  28.408  1.00 48.02           O  
ANISOU 1119  O   VAL A 142     6271   5343   6630    151    749     39       O  
ATOM   1120  CB  VAL A 142      -5.849  28.872  27.416  1.00 48.01           C  
ANISOU 1120  CB  VAL A 142     6210   5337   6693    120    682      7       C  
ATOM   1121  CG1 VAL A 142      -5.440  27.948  26.270  1.00 48.04           C  
ANISOU 1121  CG1 VAL A 142     6212   5347   6695    105    683     28       C  
ATOM   1122  CG2 VAL A 142      -6.638  30.057  26.881  1.00 48.32           C  
ANISOU 1122  CG2 VAL A 142     6233   5353   6772    106    675      7       C  
ATOM   1123  N   TRP A 143      -4.912  26.695  29.570  1.00 45.94           N  
ANISOU 1123  N   TRP A 143     6027   5100   6329    185    694      2       N  
ATOM   1124  CA  TRP A 143      -4.277  25.431  29.929  1.00 45.77           C  
ANISOU 1124  CA  TRP A 143     6039   5084   6268    211    689     11       C  
ATOM   1125  C   TRP A 143      -5.192  24.523  30.772  1.00 46.02           C  
ANISOU 1125  C   TRP A 143     6132   5097   6258    229    740     30       C  
ATOM   1126  O   TRP A 143      -5.242  23.329  30.533  1.00 45.41           O  
ANISOU 1126  O   TRP A 143     6071   5012   6169    232    761     51       O  
ATOM   1127  CB  TRP A 143      -2.933  25.671  30.624  1.00 45.24           C  
ANISOU 1127  CB  TRP A 143     5978   5027   6182    243    628    -19       C  
ATOM   1128  CG  TRP A 143      -1.848  26.083  29.679  1.00 44.97           C  
ANISOU 1128  CG  TRP A 143     5877   5004   6205    221    597    -34       C  
ATOM   1129  CD1 TRP A 143      -1.314  27.325  29.533  1.00 45.62           C  
ANISOU 1129  CD1 TRP A 143     5917   5085   6331    203    570    -62       C  
ATOM   1130  CD2 TRP A 143      -1.144  25.234  28.764  1.00 44.99           C  
ANISOU 1130  CD2 TRP A 143     5851   5013   6230    215    602    -24       C  
ATOM   1131  NE1 TRP A 143      -0.323  27.307  28.584  1.00 45.77           N  
ANISOU 1131  NE1 TRP A 143     5880   5107   6403    182    568    -68       N  
ATOM   1132  CE2 TRP A 143      -0.187  26.032  28.104  1.00 45.34           C  
ANISOU 1132  CE2 TRP A 143     5834   5059   6334    192    588    -46       C  
ATOM   1133  CE3 TRP A 143      -1.194  23.860  28.472  1.00 45.38           C  
ANISOU 1133  CE3 TRP A 143     5923   5061   6258    228    622      0       C  
ATOM   1134  CZ2 TRP A 143       0.691  25.513  27.152  1.00 45.33           C  
ANISOU 1134  CZ2 TRP A 143     5793   5058   6370    182    604    -45       C  
ATOM   1135  CZ3 TRP A 143      -0.343  23.358  27.501  1.00 45.61           C  
ANISOU 1135  CZ3 TRP A 143     5915   5094   6321    221    628     -1       C  
ATOM   1136  CH2 TRP A 143       0.589  24.183  26.861  1.00 45.31           C  
ANISOU 1136  CH2 TRP A 143     5816   5058   6340    199    623    -24       C  
ATOM   1137  N   VAL A 144      -5.922  25.093  31.741  1.00 46.76           N  
ANISOU 1137  N   VAL A 144     6261   5175   6329    241    771     20       N  
ATOM   1138  CA  VAL A 144      -6.849  24.334  32.584  1.00 47.56           C  
ANISOU 1138  CA  VAL A 144     6426   5250   6396    255    845     38       C  
ATOM   1139  C   VAL A 144      -8.056  23.789  31.754  1.00 48.12           C  
ANISOU 1139  C   VAL A 144     6447   5302   6534    214    905     59       C  
ATOM   1140  O   VAL A 144      -8.368  22.612  31.819  1.00 48.31           O  
ANISOU 1140  O   VAL A 144     6500   5307   6550    212    949     81       O  
ATOM   1141  CB  VAL A 144      -7.320  25.165  33.815  1.00 48.00           C  
ANISOU 1141  CB  VAL A 144     6538   5289   6412    278    878     18       C  
ATOM   1142  CG1 VAL A 144      -8.449  24.443  34.555  1.00 48.50           C  
ANISOU 1142  CG1 VAL A 144     6660   5312   6454    282    986     39       C  
ATOM   1143  CG2 VAL A 144      -6.159  25.455  34.762  1.00 48.06           C  
ANISOU 1143  CG2 VAL A 144     6614   5304   6342    326    808     -6       C  
ATOM   1144  N   LEU A 145      -8.699  24.642  30.951  1.00 48.11           N  
ANISOU 1144  N   LEU A 145     6374   5303   6603    184    897     48       N  
ATOM   1145  CA  LEU A 145      -9.812  24.260  30.099  1.00 48.38           C  
ANISOU 1145  CA  LEU A 145     6352   5318   6713    150    925     56       C  
ATOM   1146  C   LEU A 145      -9.427  23.112  29.163  1.00 48.10           C  
ANISOU 1146  C   LEU A 145     6310   5285   6679    136    902     73       C  
ATOM   1147  O   LEU A 145     -10.145  22.123  29.101  1.00 48.47           O  
ANISOU 1147  O   LEU A 145     6356   5306   6755    121    946     84       O  
ATOM   1148  CB  LEU A 145     -10.280  25.501  29.288  1.00 49.21           C  
ANISOU 1148  CB  LEU A 145     6391   5425   6881    133    886     39       C  
ATOM   1149  CG  LEU A 145     -11.192  25.261  28.053  1.00 51.41           C  
ANISOU 1149  CG  LEU A 145     6608   5687   7239    104    865     40       C  
ATOM   1150  CD1 LEU A 145     -12.561  24.766  28.465  1.00 52.04           C  
ANISOU 1150  CD1 LEU A 145     6654   5730   7389     92    932     33       C  
ATOM   1151  CD2 LEU A 145     -11.357  26.524  27.234  1.00 51.94           C  
ANISOU 1151  CD2 LEU A 145     6638   5755   7344    100    806     28       C  
ATOM   1152  N   VAL A 146      -8.289  23.237  28.456  1.00 47.78           N  
ANISOU 1152  N   VAL A 146     6267   5272   6615    139    841     73       N  
ATOM   1153  CA  VAL A 146      -7.835  22.238  27.492  1.00 47.67           C  
ANISOU 1153  CA  VAL A 146     6252   5261   6600    129    821     85       C  
ATOM   1154  C   VAL A 146      -7.423  20.953  28.169  1.00 47.86           C  
ANISOU 1154  C   VAL A 146     6330   5275   6581    151    849    100       C  
ATOM   1155  O   VAL A 146      -7.748  19.879  27.660  1.00 48.30           O  
ANISOU 1155  O   VAL A 146     6389   5311   6653    137    866    111       O  
ATOM   1156  CB  VAL A 146      -6.755  22.770  26.533  1.00 47.57           C  
ANISOU 1156  CB  VAL A 146     6222   5271   6580    126    770     80       C  
ATOM   1157  CG1 VAL A 146      -6.234  21.660  25.626  1.00 47.20           C  
ANISOU 1157  CG1 VAL A 146     6186   5223   6525    122    764     89       C  
ATOM   1158  CG2 VAL A 146      -7.293  23.941  25.714  1.00 47.61           C  
ANISOU 1158  CG2 VAL A 146     6193   5273   6625    104    745     73       C  
ATOM   1159  N   THR A 147      -6.821  21.035  29.377  1.00 47.22           N  
ANISOU 1159  N   THR A 147     6299   5198   6443    188    852    100       N  
ATOM   1160  CA  THR A 147      -6.485  19.842  30.167  1.00 46.81           C  
ANISOU 1160  CA  THR A 147     6320   5128   6338    219    875    118       C  
ATOM   1161  C   THR A 147      -7.770  19.090  30.488  1.00 47.61           C  
ANISOU 1161  C   THR A 147     6444   5186   6460    199    959    136       C  
ATOM   1162  O   THR A 147      -7.819  17.877  30.313  1.00 49.02           O  
ANISOU 1162  O   THR A 147     6649   5339   6637    196    983    154       O  
ATOM   1163  CB  THR A 147      -5.687  20.234  31.415  1.00 47.36           C  
ANISOU 1163  CB  THR A 147     6451   5205   6338    269    846    108       C  
ATOM   1164  OG1 THR A 147      -4.419  20.724  30.974  1.00 48.68           O  
ANISOU 1164  OG1 THR A 147     6577   5405   6513    282    768     86       O  
ATOM   1165  CG2 THR A 147      -5.453  19.073  32.361  1.00 47.60           C  
ANISOU 1165  CG2 THR A 147     6582   5205   6299    311    868    130       C  
ATOM   1166  N   LEU A 148      -8.841  19.818  30.842  1.00 46.78           N  
ANISOU 1166  N   LEU A 148     6316   5068   6390    180   1007    127       N  
ATOM   1167  CA  LEU A 148     -10.139  19.236  31.121  1.00 47.14           C  
ANISOU 1167  CA  LEU A 148     6360   5066   6484    153   1099    136       C  
ATOM   1168  C   LEU A 148     -10.813  18.654  29.872  1.00 47.74           C  
ANISOU 1168  C   LEU A 148     6362   5127   6651    108   1089    132       C  
ATOM   1169  O   LEU A 148     -11.448  17.604  29.970  1.00 48.13           O  
ANISOU 1169  O   LEU A 148     6422   5132   6733     88   1151    143       O  
ATOM   1170  CB  LEU A 148     -11.061  20.256  31.801  1.00 47.40           C  
ANISOU 1170  CB  LEU A 148     6376   5088   6547    149   1154    120       C  
ATOM   1171  CG  LEU A 148     -10.663  20.709  33.199  1.00 47.96           C  
ANISOU 1171  CG  LEU A 148     6543   5157   6523    193   1183    122       C  
ATOM   1172  CD1 LEU A 148     -11.581  21.816  33.694  1.00 48.13           C  
ANISOU 1172  CD1 LEU A 148     6538   5167   6583    188   1237     99       C  
ATOM   1173  CD2 LEU A 148     -10.637  19.555  34.162  1.00 47.92           C  
ANISOU 1173  CD2 LEU A 148     6651   5108   6447    216   1258    152       C  
ATOM   1174  N   GLU A 149     -10.677  19.301  28.709  1.00 47.75           N  
ANISOU 1174  N   GLU A 149     6297   5157   6688     93   1012    114       N  
ATOM   1175  CA  GLU A 149     -11.268  18.788  27.459  1.00 48.28           C  
ANISOU 1175  CA  GLU A 149     6310   5208   6827     58    982    104       C  
ATOM   1176  C   GLU A 149     -10.672  17.434  27.041  1.00 49.51           C  
ANISOU 1176  C   GLU A 149     6507   5352   6953     59    976    118       C  
ATOM   1177  O   GLU A 149     -11.348  16.609  26.450  1.00 49.71           O  
ANISOU 1177  O   GLU A 149     6510   5342   7036     30    983    112       O  
ATOM   1178  CB  GLU A 149     -11.018  19.782  26.315  1.00 48.90           C  
ANISOU 1178  CB  GLU A 149     6345   5316   6917     54    897     88       C  
ATOM   1179  CG  GLU A 149     -11.892  21.019  26.325  1.00 49.81           C  
ANISOU 1179  CG  GLU A 149     6406   5430   7092     47    887     69       C  
ATOM   1180  CD  GLU A 149     -11.510  22.078  25.307  1.00 52.96           C  
ANISOU 1180  CD  GLU A 149     6788   5852   7483     50    806     61       C  
ATOM   1181  OE1 GLU A 149     -10.454  21.936  24.654  1.00 53.52           O  
ANISOU 1181  OE1 GLU A 149     6893   5944   7499     56    770     71       O  
ATOM   1182  OE2 GLU A 149     -12.258  23.070  25.174  1.00 55.21           O  
ANISOU 1182  OE2 GLU A 149     7029   6127   7820     48    786     46       O  
ATOM   1183  N   VAL A 150      -9.385  17.247  27.323  1.00 50.09           N  
ANISOU 1183  N   VAL A 150     6635   5451   6945     95    956    132       N  
ATOM   1184  CA  VAL A 150      -8.532  16.109  26.997  1.00 50.45           C  
ANISOU 1184  CA  VAL A 150     6723   5492   6955    110    943    144       C  
ATOM   1185  C   VAL A 150      -8.627  14.970  28.040  1.00 52.05           C  
ANISOU 1185  C   VAL A 150     6996   5651   7128    126   1009    169       C  
ATOM   1186  O   VAL A 150      -8.374  13.809  27.704  1.00 52.62           O  
ANISOU 1186  O   VAL A 150     7099   5698   7197    128   1013    178       O  
ATOM   1187  CB  VAL A 150      -7.107  16.703  26.878  1.00 50.27           C  
ANISOU 1187  CB  VAL A 150     6707   5515   6878    145    887    139       C  
ATOM   1188  CG1 VAL A 150      -6.018  15.671  27.078  1.00 51.07           C  
ANISOU 1188  CG1 VAL A 150     6859   5612   6934    182    879    150       C  
ATOM   1189  CG2 VAL A 150      -6.935  17.438  25.556  1.00 50.05           C  
ANISOU 1189  CG2 VAL A 150     6630   5511   6875    124    838    122       C  
ATOM   1190  N   LEU A 151      -9.005  15.302  29.295  1.00 52.23           N  
ANISOU 1190  N   LEU A 151     7058   5661   7126    140   1064    180       N  
ATOM   1191  CA  LEU A 151      -9.110  14.354  30.404  1.00 53.10           C  
ANISOU 1191  CA  LEU A 151     7262   5723   7191    160   1138    209       C  
ATOM   1192  C   LEU A 151     -10.025  13.134  30.142  1.00 52.61           C  
ANISOU 1192  C   LEU A 151     7200   5596   7192    119   1208    220       C  
ATOM   1193  O   LEU A 151      -9.598  12.034  30.518  1.00 53.18           O  
ANISOU 1193  O   LEU A 151     7355   5633   7220    142   1232    246       O  
ATOM   1194  CB  LEU A 151      -9.533  15.086  31.681  1.00 54.67           C  
ANISOU 1194  CB  LEU A 151     7506   5913   7353    177   1197    215       C  
ATOM   1195  CG  LEU A 151      -8.666  14.880  32.916  1.00 57.25           C  
ANISOU 1195  CG  LEU A 151     7958   6232   7562    241   1195    236       C  
ATOM   1196  CD1 LEU A 151      -7.231  15.340  32.652  1.00 58.18           C  
ANISOU 1196  CD1 LEU A 151     8066   6407   7635    285   1075    219       C  
ATOM   1197  CD2 LEU A 151      -9.275  15.621  34.128  1.00 57.90           C  
ANISOU 1197  CD2 LEU A 151     8098   6297   7606    253   1268    238       C  
ATOM   1198  N   PRO A 152     -11.224  13.226  29.486  1.00 50.97           N  
ANISOU 1198  N   PRO A 152     6905   5367   7094     62   1233    198       N  
ATOM   1199  CA  PRO A 152     -11.989  12.002  29.221  1.00 50.30           C  
ANISOU 1199  CA  PRO A 152     6816   5215   7081     21   1291    201       C  
ATOM   1200  C   PRO A 152     -11.224  11.017  28.335  1.00 49.52           C  
ANISOU 1200  C   PRO A 152     6739   5114   6961     30   1230    201       C  
ATOM   1201  O   PRO A 152     -11.380   9.808  28.515  1.00 49.00           O  
ANISOU 1201  O   PRO A 152     6723   4988   6906     20   1282    218       O  
ATOM   1202  CB  PRO A 152     -13.272  12.512  28.559  1.00 50.88           C  
ANISOU 1202  CB  PRO A 152     6771   5277   7285    -33   1290    163       C  
ATOM   1203  CG  PRO A 152     -13.340  13.925  28.917  1.00 51.32           C  
ANISOU 1203  CG  PRO A 152     6794   5377   7327    -17   1276    153       C  
ATOM   1204  CD  PRO A 152     -11.943  14.398  28.965  1.00 49.94           C  
ANISOU 1204  CD  PRO A 152     6675   5263   7035     35   1204    166       C  
ATOM   1205  N   MET A 153     -10.388  11.521  27.389  1.00 49.15           N  
ANISOU 1205  N   MET A 153     6662   5125   6886     48   1129    183       N  
ATOM   1206  CA  MET A 153      -9.576  10.635  26.556  1.00 49.15           C  
ANISOU 1206  CA  MET A 153     6689   5123   6861     62   1081    180       C  
ATOM   1207  C   MET A 153      -8.566   9.878  27.446  1.00 48.75           C  
ANISOU 1207  C   MET A 153     6736   5060   6728    117   1102    214       C  
ATOM   1208  O   MET A 153      -8.408   8.679  27.291  1.00 49.46           O  
ANISOU 1208  O   MET A 153     6871   5104   6818    120   1119    224       O  
ATOM   1209  CB  MET A 153      -8.846  11.418  25.460  1.00 50.29           C  
ANISOU 1209  CB  MET A 153     6793   5328   6987     73    993    157       C  
ATOM   1210  CG  MET A 153      -7.688  10.647  24.856  1.00 53.29           C  
ANISOU 1210  CG  MET A 153     7212   5713   7322    104    959    157       C  
ATOM   1211  SD  MET A 153      -6.540  11.592  23.874  1.00 60.60           S  
ANISOU 1211  SD  MET A 153     8108   6703   8212    127    891    137       S  
ATOM   1212  CE  MET A 153      -5.862  12.649  25.065  1.00 59.78           C  
ANISOU 1212  CE  MET A 153     8002   6644   8069    163    889    151       C  
ATOM   1213  N   LEU A 154      -7.901  10.574  28.371  1.00 48.04           N  
ANISOU 1213  N   LEU A 154     6680   5004   6568    162   1093    228       N  
ATOM   1214  CA  LEU A 154      -6.934   9.994  29.292  1.00 47.53           C  
ANISOU 1214  CA  LEU A 154     6712   4926   6420    226   1090    255       C  
ATOM   1215  C   LEU A 154      -7.585   9.005  30.239  1.00 48.64           C  
ANISOU 1215  C   LEU A 154     6947   4989   6546    224   1183    291       C  
ATOM   1216  O   LEU A 154      -7.003   7.941  30.503  1.00 48.96           O  
ANISOU 1216  O   LEU A 154     7069   4990   6545    262   1184    314       O  
ATOM   1217  CB  LEU A 154      -6.166  11.089  30.053  1.00 46.72           C  
ANISOU 1217  CB  LEU A 154     6622   4875   6255    273   1043    252       C  
ATOM   1218  CG  LEU A 154      -5.357  12.078  29.187  1.00 46.98           C  
ANISOU 1218  CG  LEU A 154     6569   4977   6306    276    961    219       C  
ATOM   1219  CD1 LEU A 154      -4.610  13.076  30.047  1.00 47.57           C  
ANISOU 1219  CD1 LEU A 154     6656   5089   6330    319    914    210       C  
ATOM   1220  CD2 LEU A 154      -4.394  11.368  28.271  1.00 47.04           C  
ANISOU 1220  CD2 LEU A 154     6561   4990   6322    294    916    208       C  
ATOM   1221  N   THR A 155      -8.831   9.296  30.682  1.00 49.13           N  
ANISOU 1221  N   THR A 155     6994   5020   6651    178   1270    295       N  
ATOM   1222  CA  THR A 155      -9.610   8.392  31.555  1.00 49.60           C  
ANISOU 1222  CA  THR A 155     7140   4993   6713    163   1389    329       C  
ATOM   1223  C   THR A 155      -9.894   7.086  30.797  1.00 50.83           C  
ANISOU 1223  C   THR A 155     7287   5090   6934    127   1409    329       C  
ATOM   1224  O   THR A 155      -9.818   6.015  31.382  1.00 51.38           O  
ANISOU 1224  O   THR A 155     7461   5089   6970    144   1468    365       O  
ATOM   1225  CB  THR A 155     -10.905   9.084  32.062  1.00 49.48           C  
ANISOU 1225  CB  THR A 155     7084   4958   6757    115   1486    323       C  
ATOM   1226  OG1 THR A 155     -10.543  10.297  32.707  1.00 51.00           O  
ANISOU 1226  OG1 THR A 155     7290   5205   6882    153   1457    319       O  
ATOM   1227  CG2 THR A 155     -11.732   8.215  33.026  1.00 48.18           C  
ANISOU 1227  CG2 THR A 155     7012   4696   6599     94   1638    360       C  
ATOM   1228  N   PHE A 156     -10.207   7.178  29.494  1.00 51.46           N  
ANISOU 1228  N   PHE A 156     7257   5193   7103     81   1354    289       N  
ATOM   1229  CA  PHE A 156     -10.436   6.010  28.667  1.00 53.04           C  
ANISOU 1229  CA  PHE A 156     7448   5340   7365     48   1355    277       C  
ATOM   1230  C   PHE A 156      -9.124   5.220  28.548  1.00 54.68           C  
ANISOU 1230  C   PHE A 156     7735   5550   7492    111   1301    293       C  
ATOM   1231  O   PHE A 156      -9.141   3.990  28.681  1.00 54.82           O  
ANISOU 1231  O   PHE A 156     7821   5495   7514    112   1344    313       O  
ATOM   1232  CB  PHE A 156     -10.983   6.407  27.276  1.00 53.41           C  
ANISOU 1232  CB  PHE A 156     7374   5415   7505     -2   1287    224       C  
ATOM   1233  CG  PHE A 156     -10.730   5.366  26.200  1.00 55.56           C  
ANISOU 1233  CG  PHE A 156     7651   5657   7803    -13   1241    202       C  
ATOM   1234  CD1 PHE A 156     -11.335   4.115  26.259  1.00 57.16           C  
ANISOU 1234  CD1 PHE A 156     7883   5768   8067    -49   1304    206       C  
ATOM   1235  CD2 PHE A 156      -9.831   5.609  25.177  1.00 56.80           C  
ANISOU 1235  CD2 PHE A 156     7792   5869   7919     16   1146    179       C  
ATOM   1236  CE1 PHE A 156     -11.067   3.149  25.293  1.00 57.86           C  
ANISOU 1236  CE1 PHE A 156     7985   5824   8175    -55   1260    182       C  
ATOM   1237  CE2 PHE A 156      -9.574   4.649  24.209  1.00 57.40           C  
ANISOU 1237  CE2 PHE A 156     7887   5914   8010     11   1111    156       C  
ATOM   1238  CZ  PHE A 156     -10.190   3.427  24.272  1.00 57.60           C  
ANISOU 1238  CZ  PHE A 156     7941   5851   8094    -23   1162    156       C  
ATOM   1239  N   ILE A 157      -7.997   5.921  28.278  1.00 55.35           N  
ANISOU 1239  N   ILE A 157     7803   5712   7515    162   1211    282       N  
ATOM   1240  CA  ILE A 157      -6.700   5.258  28.133  1.00 56.45           C  
ANISOU 1240  CA  ILE A 157     7996   5856   7597    226   1157    289       C  
ATOM   1241  C   ILE A 157      -6.318   4.482  29.429  1.00 57.28           C  
ANISOU 1241  C   ILE A 157     8233   5904   7628    284   1197    337       C  
ATOM   1242  O   ILE A 157      -5.894   3.331  29.335  1.00 57.52           O  
ANISOU 1242  O   ILE A 157     8325   5882   7648    312   1197    349       O  
ATOM   1243  CB  ILE A 157      -5.608   6.256  27.641  1.00 56.59           C  
ANISOU 1243  CB  ILE A 157     7955   5961   7585    264   1066    263       C  
ATOM   1244  CG1 ILE A 157      -5.883   6.730  26.205  1.00 56.94           C  
ANISOU 1244  CG1 ILE A 157     7905   6042   7688    215   1030    221       C  
ATOM   1245  CG2 ILE A 157      -4.184   5.698  27.772  1.00 56.74           C  
ANISOU 1245  CG2 ILE A 157     8020   5985   7555    341   1014    267       C  
ATOM   1246  CD1 ILE A 157      -5.197   8.040  25.872  1.00 57.33           C  
ANISOU 1246  CD1 ILE A 157     7893   6169   7719    231    972    201       C  
ATOM   1247  N   THR A 158      -6.548   5.065  30.623  1.00 57.38           N  
ANISOU 1247  N   THR A 158     8300   5917   7586    302   1234    363       N  
ATOM   1248  CA  THR A 158      -6.238   4.373  31.875  1.00 58.24           C  
ANISOU 1248  CA  THR A 158     8558   5963   7606    362   1270    411       C  
ATOM   1249  C   THR A 158      -7.092   3.118  32.079  1.00 59.19           C  
ANISOU 1249  C   THR A 158     8755   5977   7758    324   1381    443       C  
ATOM   1250  O   THR A 158      -6.649   2.201  32.772  1.00 59.58           O  
ANISOU 1250  O   THR A 158     8938   5962   7740    379   1397    483       O  
ATOM   1251  CB  THR A 158      -6.287   5.310  33.073  1.00 60.02           C  
ANISOU 1251  CB  THR A 158     8843   6209   7754    393   1284    427       C  
ATOM   1252  OG1 THR A 158      -7.639   5.720  33.320  1.00 62.06           O  
ANISOU 1252  OG1 THR A 158     9075   6444   8062    322   1395    431       O  
ATOM   1253  CG2 THR A 158      -5.365   6.500  32.918  1.00 59.86           C  
ANISOU 1253  CG2 THR A 158     8752   6283   7709    431   1170    392       C  
ATOM   1254  N   SER A 159      -8.271   3.032  31.423  1.00 59.48           N  
ANISOU 1254  N   SER A 159     8705   5989   7904    233   1448    423       N  
ATOM   1255  CA  SER A 159      -9.126   1.839  31.465  1.00 60.00           C  
ANISOU 1255  CA  SER A 159     8818   5948   8033    183   1554    443       C  
ATOM   1256  C   SER A 159      -8.582   0.702  30.576  1.00 60.42           C  
ANISOU 1256  C   SER A 159     8877   5967   8111    192   1504    431       C  
ATOM   1257  O   SER A 159      -8.943  -0.448  30.778  1.00 60.86           O  
ANISOU 1257  O   SER A 159     9009   5925   8190    175   1579    456       O  
ATOM   1258  CB  SER A 159     -10.570   2.174  31.091  1.00 61.28           C  
ANISOU 1258  CB  SER A 159     8869   6090   8323     84   1632    414       C  
ATOM   1259  OG  SER A 159     -10.798   2.240  29.693  1.00 63.27           O  
ANISOU 1259  OG  SER A 159     8991   6376   8674     36   1558    358       O  
ATOM   1260  N   THR A 160      -7.747   1.018  29.584  1.00 60.29           N  
ANISOU 1260  N   THR A 160     8784   6026   8096    217   1390    391       N  
ATOM   1261  CA  THR A 160      -7.123   0.019  28.716  1.00 60.54           C  
ANISOU 1261  CA  THR A 160     8825   6031   8144    236   1342    374       C  
ATOM   1262  C   THR A 160      -5.854  -0.575  29.425  1.00 61.26           C  
ANISOU 1262  C   THR A 160     9034   6104   8136    339   1304    409       C  
ATOM   1263  O   THR A 160      -5.397  -0.011  30.436  1.00 61.26           O  
ANISOU 1263  O   THR A 160     9091   6130   8055    396   1288    437       O  
ATOM   1264  CB  THR A 160      -6.872   0.627  27.313  1.00 60.89           C  
ANISOU 1264  CB  THR A 160     8747   6155   8233    214   1255    314       C  
ATOM   1265  OG1 THR A 160      -5.785   1.559  27.376  1.00 62.03           O  
ANISOU 1265  OG1 THR A 160     8866   6389   8315    275   1178    308       O  
ATOM   1266  CG2 THR A 160      -8.121   1.292  26.727  1.00 60.53           C  
ANISOU 1266  CG2 THR A 160     8598   6124   8277    126   1273    280       C  
ATOM   1267  N   PRO A 161      -5.281  -1.717  28.958  1.00 61.54           N  
ANISOU 1267  N   PRO A 161     9113   6089   8180    371   1282    406       N  
ATOM   1268  CA  PRO A 161      -4.119  -2.292  29.669  1.00 61.51           C  
ANISOU 1268  CA  PRO A 161     9219   6060   8094    477   1237    438       C  
ATOM   1269  C   PRO A 161      -2.759  -1.644  29.345  1.00 60.88           C  
ANISOU 1269  C   PRO A 161     9075   6070   7985    552   1120    406       C  
ATOM   1270  O   PRO A 161      -1.825  -2.336  28.896  1.00 60.69           O  
ANISOU 1270  O   PRO A 161     9059   6032   7968    609   1070    390       O  
ATOM   1271  CB  PRO A 161      -4.166  -3.775  29.283  1.00 62.27           C  
ANISOU 1271  CB  PRO A 161     9381   6055   8225    475   1271    445       C  
ATOM   1272  CG  PRO A 161      -4.734  -3.766  27.914  1.00 63.00           C  
ANISOU 1272  CG  PRO A 161     9358   6166   8412    393   1272    389       C  
ATOM   1273  CD  PRO A 161      -5.691  -2.580  27.829  1.00 61.39           C  
ANISOU 1273  CD  PRO A 161     9057   6024   8245    317   1294    372       C  
ATOM   1274  N   ILE A 162      -2.628  -0.325  29.646  1.00 59.74           N  
ANISOU 1274  N   ILE A 162     8870   6013   7817    553   1083    395       N  
ATOM   1275  CA  ILE A 162      -1.394   0.428  29.408  1.00 59.31           C  
ANISOU 1275  CA  ILE A 162     8742   6040   7752    614    982    360       C  
ATOM   1276  C   ILE A 162      -0.216  -0.087  30.242  1.00 60.06           C  
ANISOU 1276  C   ILE A 162     8923   6107   7790    728    910    378       C  
ATOM   1277  O   ILE A 162       0.923   0.072  29.818  1.00 60.14           O  
ANISOU 1277  O   ILE A 162     8866   6159   7825    783    831    341       O  
ATOM   1278  CB  ILE A 162      -1.575   1.964  29.545  1.00 58.24           C  
ANISOU 1278  CB  ILE A 162     8525   5993   7611    584    961    343       C  
ATOM   1279  CG1 ILE A 162      -2.153   2.368  30.907  1.00 57.19           C  
ANISOU 1279  CG1 ILE A 162     8482   5840   7409    591    996    384       C  
ATOM   1280  CG2 ILE A 162      -2.401   2.502  28.389  1.00 58.71           C  
ANISOU 1280  CG2 ILE A 162     8477   6090   7741    490    995    311       C  
ATOM   1281  CD1 ILE A 162      -2.081   3.815  31.143  1.00 57.35           C  
ANISOU 1281  CD1 ILE A 162     8434   5940   7417    584    959    363       C  
ATOM   1282  N   GLU A 163      -0.495  -0.733  31.395  1.00 60.61           N  
ANISOU 1282  N   GLU A 163     9144   6099   7788    766    941    432       N  
ATOM   1283  CA  GLU A 163       0.476  -1.365  32.308  1.00 61.34           C  
ANISOU 1283  CA  GLU A 163     9354   6142   7811    883    867    457       C  
ATOM   1284  C   GLU A 163       1.311  -2.439  31.592  1.00 61.39           C  
ANISOU 1284  C   GLU A 163     9348   6111   7867    935    828    437       C  
ATOM   1285  O   GLU A 163       2.403  -2.763  32.045  1.00 61.37           O  
ANISOU 1285  O   GLU A 163     9385   6092   7840   1041    733    434       O  
ATOM   1286  CB  GLU A 163      -0.238  -1.985  33.539  1.00 64.23           C  
ANISOU 1286  CB  GLU A 163     9911   6409   8085    898    940    527       C  
ATOM   1287  CG  GLU A 163      -1.284  -1.094  34.207  1.00 70.14           C  
ANISOU 1287  CG  GLU A 163    10682   7174   8792    836   1019    549       C  
ATOM   1288  CD  GLU A 163      -2.688  -1.147  33.618  1.00 77.04           C  
ANISOU 1288  CD  GLU A 163    11501   8028   9741    710   1155    552       C  
ATOM   1289  OE1 GLU A 163      -3.015  -2.169  32.972  1.00 77.83           O  
ANISOU 1289  OE1 GLU A 163    11604   8066   9901    674   1206    555       O  
ATOM   1290  OE2 GLU A 163      -3.459  -0.174  33.802  1.00 80.15           O  
ANISOU 1290  OE2 GLU A 163    11847   8464  10141    650   1205    546       O  
ATOM   1291  N   LYS A 164       0.804  -2.983  30.474  1.00 61.59           N  
ANISOU 1291  N   LYS A 164     9317   6118   7965    863    893    419       N  
ATOM   1292  CA  LYS A 164       1.518  -3.955  29.660  1.00 62.55           C  
ANISOU 1292  CA  LYS A 164     9421   6206   8139    902    869    392       C  
ATOM   1293  C   LYS A 164       2.776  -3.380  28.977  1.00 64.02           C  
ANISOU 1293  C   LYS A 164     9475   6474   8376    952    783    331       C  
ATOM   1294  O   LYS A 164       3.574  -4.150  28.448  1.00 64.46           O  
ANISOU 1294  O   LYS A 164     9518   6501   8474   1006    756    306       O  
ATOM   1295  CB  LYS A 164       0.584  -4.608  28.633  1.00 64.05           C  
ANISOU 1295  CB  LYS A 164     9592   6355   8388    808    959    380       C  
ATOM   1296  CG  LYS A 164      -0.440  -5.534  29.271  1.00 67.65           C  
ANISOU 1296  CG  LYS A 164    10182   6701   8821    773   1048    436       C  
ATOM   1297  CD  LYS A 164      -1.321  -6.229  28.249  1.00 72.29           C  
ANISOU 1297  CD  LYS A 164    10745   7238   9485    683   1121    414       C  
ATOM   1298  CE  LYS A 164      -2.331  -7.142  28.901  1.00 75.88           C  
ANISOU 1298  CE  LYS A 164    11322   7574   9936    641   1221    466       C  
ATOM   1299  NZ  LYS A 164      -3.032  -7.981  27.898  1.00 78.31           N  
ANISOU 1299  NZ  LYS A 164    11605   7818  10330    563   1274    435       N  
ATOM   1300  N   GLY A 165       2.942  -2.055  28.985  1.00 64.54           N  
ANISOU 1300  N   GLY A 165     9444   6633   8447    931    749    307       N  
ATOM   1301  CA  GLY A 165       4.114  -1.386  28.442  1.00 65.66           C  
ANISOU 1301  CA  GLY A 165     9456   6847   8645    970    680    251       C  
ATOM   1302  C   GLY A 165       4.118  -1.160  26.945  1.00 67.04           C  
ANISOU 1302  C   GLY A 165     9517   7064   8890    906    728    203       C  
ATOM   1303  O   GLY A 165       4.786  -0.239  26.456  1.00 67.68           O  
ANISOU 1303  O   GLY A 165     9483   7216   9014    905    702    161       O  
ATOM   1304  N   ASP A 166       3.373  -1.985  26.198  1.00 67.25           N  
ANISOU 1304  N   ASP A 166     9582   7041   8927    853    799    207       N  
ATOM   1305  CA  ASP A 166       3.330  -1.858  24.737  1.00 67.64           C  
ANISOU 1305  CA  ASP A 166     9554   7120   9027    797    840    160       C  
ATOM   1306  C   ASP A 166       1.934  -1.484  24.188  1.00 66.88           C  
ANISOU 1306  C   ASP A 166     9455   7033   8922    687    897    165       C  
ATOM   1307  O   ASP A 166       1.615  -1.768  23.027  1.00 67.16           O  
ANISOU 1307  O   ASP A 166     9476   7059   8983    641    930    134       O  
ATOM   1308  CB  ASP A 166       3.863  -3.141  24.079  1.00 69.70           C  
ANISOU 1308  CB  ASP A 166     9847   7316   9321    842    855    138       C  
ATOM   1309  CG  ASP A 166       2.998  -4.367  24.316  1.00 75.71           C  
ANISOU 1309  CG  ASP A 166    10726   7979  10061    823    895    172       C  
ATOM   1310  OD1 ASP A 166       3.159  -5.358  23.567  1.00 78.10           O  
ANISOU 1310  OD1 ASP A 166    11056   8226  10393    836    919    149       O  
ATOM   1311  OD2 ASP A 166       2.151  -4.336  25.249  1.00 76.93           O  
ANISOU 1311  OD2 ASP A 166    10947   8107  10175    794    910    221       O  
ATOM   1312  N   SER A 167       1.112  -0.861  25.030  1.00 65.50           N  
ANISOU 1312  N   SER A 167     9299   6873   8715    649    903    200       N  
ATOM   1313  CA  SER A 167      -0.240  -0.513  24.654  1.00 64.98           C  
ANISOU 1313  CA  SER A 167     9222   6808   8658    552    950    203       C  
ATOM   1314  C   SER A 167      -0.450   0.977  24.781  1.00 63.74           C  
ANISOU 1314  C   SER A 167     8990   6734   8492    519    933    198       C  
ATOM   1315  O   SER A 167      -0.118   1.559  25.811  1.00 63.66           O  
ANISOU 1315  O   SER A 167     8988   6750   8449    556    905    220       O  
ATOM   1316  CB  SER A 167      -1.235  -1.284  25.520  1.00 66.47           C  
ANISOU 1316  CB  SER A 167     9507   6917   8833    528   1000    249       C  
ATOM   1317  OG  SER A 167      -2.577  -0.888  25.290  1.00 68.99           O  
ANISOU 1317  OG  SER A 167     9798   7235   9180    435   1045    249       O  
ATOM   1318  N   CYS A 168      -0.964   1.599  23.721  1.00 62.65           N  
ANISOU 1318  N   CYS A 168     8789   6634   8381    454    942    168       N  
ATOM   1319  CA  CYS A 168      -1.256   3.025  23.717  1.00 62.20           C  
ANISOU 1319  CA  CYS A 168     8664   6648   8321    418    928    162       C  
ATOM   1320  C   CYS A 168      -2.313   3.304  22.667  1.00 61.60           C  
ANISOU 1320  C   CYS A 168     8559   6574   8274    339    943    139       C  
ATOM   1321  O   CYS A 168      -1.972   3.711  21.559  1.00 62.99           O  
ANISOU 1321  O   CYS A 168     8698   6781   8453    329    929    106       O  
ATOM   1322  CB  CYS A 168      -0.002   3.862  23.479  1.00 62.13           C  
ANISOU 1322  CB  CYS A 168     8591   6704   8313    461    890    138       C  
ATOM   1323  SG  CYS A 168      -0.190   5.570  24.012  1.00 63.00           S  
ANISOU 1323  SG  CYS A 168     8637   6887   8412    437    867    143       S  
ATOM   1324  N   VAL A 169      -3.586   3.093  22.998  1.00 59.43           N  
ANISOU 1324  N   VAL A 169     8302   6260   8021    286    972    154       N  
ATOM   1325  CA  VAL A 169      -4.669   3.239  22.024  1.00 57.57           C  
ANISOU 1325  CA  VAL A 169     8034   6013   7826    215    969    125       C  
ATOM   1326  C   VAL A 169      -5.112   4.684  21.694  1.00 55.35           C  
ANISOU 1326  C   VAL A 169     7684   5796   7551    181    941    112       C  
ATOM   1327  O   VAL A 169      -4.950   5.624  22.490  1.00 54.47           O  
ANISOU 1327  O   VAL A 169     7545   5729   7421    194    941    132       O  
ATOM   1328  CB  VAL A 169      -5.904   2.399  22.425  1.00 57.74           C  
ANISOU 1328  CB  VAL A 169     8082   5957   7899    166   1012    135       C  
ATOM   1329  CG1 VAL A 169      -5.552   0.930  22.509  1.00 58.58           C  
ANISOU 1329  CG1 VAL A 169     8265   5988   8006    192   1038    143       C  
ATOM   1330  CG2 VAL A 169      -6.493   2.884  23.732  1.00 57.67           C  
ANISOU 1330  CG2 VAL A 169     8072   5947   7891    155   1056    174       C  
ATOM   1331  N   ASP A 170      -5.675   4.814  20.466  1.00 53.80           N  
ANISOU 1331  N   ASP A 170     7469   5595   7377    140    911     75       N  
ATOM   1332  CA  ASP A 170      -6.304   6.003  19.924  1.00 52.89           C  
ANISOU 1332  CA  ASP A 170     7303   5520   7274    105    874     58       C  
ATOM   1333  C   ASP A 170      -7.839   5.791  20.087  1.00 52.89           C  
ANISOU 1333  C   ASP A 170     7275   5472   7350     46    875     48       C  
ATOM   1334  O   ASP A 170      -8.363   4.813  19.569  1.00 53.25           O  
ANISOU 1334  O   ASP A 170     7341   5457   7434     20    869     24       O  
ATOM   1335  CB  ASP A 170      -5.925   6.174  18.446  1.00 52.68           C  
ANISOU 1335  CB  ASP A 170     7295   5504   7216    107    833     22       C  
ATOM   1336  CG  ASP A 170      -6.546   7.361  17.735  1.00 56.03           C  
ANISOU 1336  CG  ASP A 170     7689   5959   7640     78    784      4       C  
ATOM   1337  OD1 ASP A 170      -7.284   8.132  18.387  1.00 56.78           O  
ANISOU 1337  OD1 ASP A 170     7732   6071   7772     55    779     17       O  
ATOM   1338  OD2 ASP A 170      -6.294   7.526  16.533  1.00 58.38           O  
ANISOU 1338  OD2 ASP A 170     8024   6259   7899     82    754    -21       O  
ATOM   1339  N   TYR A 171      -8.550   6.696  20.786  1.00 52.11           N  
ANISOU 1339  N   TYR A 171     7123   5394   7282     24    886     61       N  
ATOM   1340  CA  TYR A 171     -10.006   6.591  20.960  1.00 51.93           C  
ANISOU 1340  CA  TYR A 171     7053   5324   7353    -32    896     46       C  
ATOM   1341  C   TYR A 171     -10.768   6.598  19.626  1.00 53.20           C  
ANISOU 1341  C   TYR A 171     7187   5463   7563    -67    817     -7       C  
ATOM   1342  O   TYR A 171     -11.867   6.039  19.552  1.00 53.58           O  
ANISOU 1342  O   TYR A 171     7200   5451   7708   -114    815    -33       O  
ATOM   1343  CB  TYR A 171     -10.551   7.666  21.918  1.00 50.80           C  
ANISOU 1343  CB  TYR A 171     6857   5211   7235    -42    927     66       C  
ATOM   1344  CG  TYR A 171     -10.474   9.087  21.399  1.00 50.08           C  
ANISOU 1344  CG  TYR A 171     6723   5182   7122    -34    867     53       C  
ATOM   1345  CD1 TYR A 171     -11.513   9.638  20.664  1.00 50.32           C  
ANISOU 1345  CD1 TYR A 171     6695   5204   7221    -69    809     17       C  
ATOM   1346  CD2 TYR A 171      -9.411   9.911  21.730  1.00 50.55           C  
ANISOU 1346  CD2 TYR A 171     6798   5304   7104      8    866     76       C  
ATOM   1347  CE1 TYR A 171     -11.438  10.932  20.167  1.00 50.73           C  
ANISOU 1347  CE1 TYR A 171     6722   5304   7247    -57    752     10       C  
ATOM   1348  CE2 TYR A 171      -9.345  11.226  21.276  1.00 51.05           C  
ANISOU 1348  CE2 TYR A 171     6828   5416   7152     11    819     67       C  
ATOM   1349  CZ  TYR A 171     -10.358  11.732  20.489  1.00 51.59           C  
ANISOU 1349  CZ  TYR A 171     6855   5473   7276    -20    765     38       C  
ATOM   1350  OH  TYR A 171     -10.300  13.038  20.059  1.00 52.56           O  
ANISOU 1350  OH  TYR A 171     6957   5635   7379    -13    719     33       O  
ATOM   1351  N   ALA A 172     -10.172   7.189  18.562  1.00 53.51           N  
ANISOU 1351  N   ALA A 172     7249   5544   7538    -44    752    -24       N  
ATOM   1352  CA  ALA A 172     -10.769   7.185  17.222  1.00 54.21           C  
ANISOU 1352  CA  ALA A 172     7344   5608   7645    -64    663    -74       C  
ATOM   1353  C   ALA A 172     -10.830   5.773  16.644  1.00 55.49           C  
ANISOU 1353  C   ALA A 172     7556   5703   7823    -75    653   -105       C  
ATOM   1354  O   ALA A 172     -11.785   5.448  15.937  1.00 55.76           O  
ANISOU 1354  O   ALA A 172     7576   5687   7922   -109    586   -154       O  
ATOM   1355  CB  ALA A 172      -9.978   8.075  16.286  1.00 53.97           C  
ANISOU 1355  CB  ALA A 172     7357   5628   7521    -31    618    -77       C  
ATOM   1356  N   SER A 173      -9.826   4.925  16.982  1.00 56.12           N  
ANISOU 1356  N   SER A 173     7693   5776   7853    -44    715    -81       N  
ATOM   1357  CA  SER A 173      -9.684   3.558  16.502  1.00 57.06           C  
ANISOU 1357  CA  SER A 173     7871   5831   7977    -45    717   -106       C  
ATOM   1358  C   SER A 173     -10.078   2.471  17.487  1.00 57.97           C  
ANISOU 1358  C   SER A 173     7981   5882   8163    -68    785    -88       C  
ATOM   1359  O   SER A 173     -10.334   1.351  17.059  1.00 58.06           O  
ANISOU 1359  O   SER A 173     8028   5823   8210    -86    778   -118       O  
ATOM   1360  CB  SER A 173      -8.246   3.324  16.058  1.00 58.68           C  
ANISOU 1360  CB  SER A 173     8149   6064   8084     11    738    -98       C  
ATOM   1361  OG  SER A 173      -7.886   4.192  14.993  1.00 61.66           O  
ANISOU 1361  OG  SER A 173     8552   6482   8394     28    689   -118       O  
ATOM   1362  N   SER A 174     -10.105   2.772  18.799  1.00 58.53           N  
ANISOU 1362  N   SER A 174     8023   5970   8247    -65    856    -39       N  
ATOM   1363  CA  SER A 174     -10.411   1.794  19.852  1.00 59.03           C  
ANISOU 1363  CA  SER A 174     8104   5966   8358    -81    940     -9       C  
ATOM   1364  C   SER A 174     -11.448   2.299  20.839  1.00 59.87           C  
ANISOU 1364  C   SER A 174     8145   6061   8541   -123    993     10       C  
ATOM   1365  O   SER A 174     -11.643   3.495  20.991  1.00 59.73           O  
ANISOU 1365  O   SER A 174     8073   6103   8517   -122    975     13       O  
ATOM   1366  CB  SER A 174      -9.144   1.428  20.617  1.00 60.16           C  
ANISOU 1366  CB  SER A 174     8317   6126   8415    -16    990     40       C  
ATOM   1367  OG  SER A 174      -8.069   1.113  19.750  1.00 62.52           O  
ANISOU 1367  OG  SER A 174     8663   6444   8649     30    951     22       O  
ATOM   1368  N   GLY A 175     -12.102   1.376  21.515  1.00 61.08           N  
ANISOU 1368  N   GLY A 175     8309   6132   8768   -159   1071     21       N  
ATOM   1369  CA  GLY A 175     -13.129   1.713  22.489  1.00 62.59           C  
ANISOU 1369  CA  GLY A 175     8444   6295   9041   -203   1151     38       C  
ATOM   1370  C   GLY A 175     -14.495   1.905  21.865  1.00 63.57           C  
ANISOU 1370  C   GLY A 175     8461   6383   9311   -273   1112    -22       C  
ATOM   1371  O   GLY A 175     -14.632   1.958  20.642  1.00 64.52           O  
ANISOU 1371  O   GLY A 175     8554   6512   9450   -281   1001    -77       O  
ATOM   1372  N   ASN A 176     -15.506   2.034  22.705  1.00 63.07           N  
ANISOU 1372  N   ASN A 176     8337   6275   9351   -319   1202    -15       N  
ATOM   1373  CA  ASN A 176     -16.896   2.209  22.298  1.00 62.98           C  
ANISOU 1373  CA  ASN A 176     8200   6218   9510   -388   1178    -76       C  
ATOM   1374  C   ASN A 176     -17.091   3.342  21.270  1.00 62.31           C  
ANISOU 1374  C   ASN A 176     8042   6203   9429   -375   1034   -125       C  
ATOM   1375  O   ASN A 176     -16.928   4.506  21.624  1.00 62.90           O  
ANISOU 1375  O   ASN A 176     8096   6350   9454   -345   1032   -102       O  
ATOM   1376  CB  ASN A 176     -17.739   2.448  23.549  1.00 64.01           C  
ANISOU 1376  CB  ASN A 176     8281   6310   9729   -424   1321    -49       C  
ATOM   1377  CG  ASN A 176     -19.173   2.090  23.380  1.00 67.71           C  
ANISOU 1377  CG  ASN A 176     8628   6690  10411   -505   1347   -108       C  
ATOM   1378  OD1 ASN A 176     -19.814   2.431  22.381  1.00 69.50           O  
ANISOU 1378  OD1 ASN A 176     8753   6920  10734   -528   1223   -178       O  
ATOM   1379  ND2 ASN A 176     -19.714   1.401  24.365  1.00 68.84           N  
ANISOU 1379  ND2 ASN A 176     8778   6745  10635   -550   1509    -81       N  
ATOM   1380  N   PRO A 177     -17.454   3.022  20.000  1.00 60.88           N  
ANISOU 1380  N   PRO A 177     7834   5996   9302   -394    910   -192       N  
ATOM   1381  CA  PRO A 177     -17.632   4.080  18.985  1.00 60.11           C  
ANISOU 1381  CA  PRO A 177     7693   5955   9192   -374    765   -235       C  
ATOM   1382  C   PRO A 177     -18.720   5.088  19.312  1.00 60.10           C  
ANISOU 1382  C   PRO A 177     7563   5958   9313   -399    761   -258       C  
ATOM   1383  O   PRO A 177     -18.602   6.228  18.935  1.00 60.44           O  
ANISOU 1383  O   PRO A 177     7592   6067   9305   -365    683   -260       O  
ATOM   1384  CB  PRO A 177     -17.974   3.307  17.704  1.00 60.39           C  
ANISOU 1384  CB  PRO A 177     7737   5933   9276   -395    643   -308       C  
ATOM   1385  CG  PRO A 177     -17.558   1.920  17.959  1.00 60.74           C  
ANISOU 1385  CG  PRO A 177     7854   5915   9308   -409    721   -292       C  
ATOM   1386  CD  PRO A 177     -17.706   1.689  19.429  1.00 59.65           C  
ANISOU 1386  CD  PRO A 177     7700   5751   9214   -431    889   -234       C  
ATOM   1387  N   LYS A 178     -19.774   4.674  20.005  1.00 60.20           N  
ANISOU 1387  N   LYS A 178     7484   5897   9493   -458    850   -275       N  
ATOM   1388  CA  LYS A 178     -20.877   5.549  20.395  1.00 60.50           C  
ANISOU 1388  CA  LYS A 178     7386   5928   9673   -483    865   -301       C  
ATOM   1389  C   LYS A 178     -20.362   6.648  21.336  1.00 59.07           C  
ANISOU 1389  C   LYS A 178     7231   5826   9386   -440    945   -237       C  
ATOM   1390  O   LYS A 178     -20.678   7.810  21.113  1.00 59.49           O  
ANISOU 1390  O   LYS A 178     7222   5924   9456   -420    877   -255       O  
ATOM   1391  CB  LYS A 178     -21.988   4.710  21.061  1.00 64.28           C  
ANISOU 1391  CB  LYS A 178     7769   6299  10354   -560    986   -327       C  
ATOM   1392  CG  LYS A 178     -23.075   5.499  21.794  1.00 71.88           C  
ANISOU 1392  CG  LYS A 178     8593   7245  11473   -588   1065   -343       C  
ATOM   1393  CD  LYS A 178     -23.837   4.563  22.781  1.00 79.74           C  
ANISOU 1393  CD  LYS A 178     9540   8132  12624   -661   1257   -338       C  
ATOM   1394  CE  LYS A 178     -25.040   5.194  23.455  1.00 85.21           C  
ANISOU 1394  CE  LYS A 178    10080   8788  13508   -699   1355   -367       C  
ATOM   1395  NZ  LYS A 178     -24.647   6.290  24.375  1.00 88.71           N  
ANISOU 1395  NZ  LYS A 178    10569   9307  13829   -649   1442   -305       N  
ATOM   1396  N   TYR A 179     -19.548   6.291  22.354  1.00 57.28           N  
ANISOU 1396  N   TYR A 179     7105   5612   9046   -421   1077   -165       N  
ATOM   1397  CA  TYR A 179     -19.004   7.265  23.295  1.00 56.35           C  
ANISOU 1397  CA  TYR A 179     7026   5563   8822   -377   1146   -109       C  
ATOM   1398  C   TYR A 179     -17.875   8.090  22.674  1.00 55.25           C  
ANISOU 1398  C   TYR A 179     6952   5520   8520   -314   1035    -91       C  
ATOM   1399  O   TYR A 179     -17.825   9.295  22.891  1.00 54.91           O  
ANISOU 1399  O   TYR A 179     6883   5534   8445   -287   1018    -82       O  
ATOM   1400  CB  TYR A 179     -18.542   6.607  24.599  1.00 56.47           C  
ANISOU 1400  CB  TYR A 179     7137   5550   8769   -372   1308    -43       C  
ATOM   1401  CG  TYR A 179     -19.663   6.021  25.424  1.00 57.30           C  
ANISOU 1401  CG  TYR A 179     7187   5558   9026   -434   1457    -48       C  
ATOM   1402  CD1 TYR A 179     -19.650   4.688  25.798  1.00 58.36           C  
ANISOU 1402  CD1 TYR A 179     7386   5607   9179   -464   1554    -26       C  
ATOM   1403  CD2 TYR A 179     -20.729   6.805  25.844  1.00 58.12           C  
ANISOU 1403  CD2 TYR A 179     7175   5647   9260   -462   1513    -74       C  
ATOM   1404  CE1 TYR A 179     -20.671   4.141  26.563  1.00 59.33           C  
ANISOU 1404  CE1 TYR A 179     7466   5631   9447   -527   1711    -28       C  
ATOM   1405  CE2 TYR A 179     -21.752   6.273  26.617  1.00 59.11           C  
ANISOU 1405  CE2 TYR A 179     7247   5677   9536   -523   1673    -81       C  
ATOM   1406  CZ  TYR A 179     -21.718   4.937  26.983  1.00 60.46           C  
ANISOU 1406  CZ  TYR A 179     7488   5761   9722   -557   1777    -56       C  
ATOM   1407  OH  TYR A 179     -22.720   4.368  27.745  1.00 62.39           O  
ANISOU 1407  OH  TYR A 179     7687   5898  10121   -623   1955    -59       O  
ATOM   1408  N   SER A 180     -17.007   7.460  21.867  1.00 54.65           N  
ANISOU 1408  N   SER A 180     6956   5455   8353   -292    964    -91       N  
ATOM   1409  CA  SER A 180     -15.923   8.143  21.160  1.00 54.40           C  
ANISOU 1409  CA  SER A 180     6985   5502   8180   -238    872    -80       C  
ATOM   1410  C   SER A 180     -16.465   9.197  20.203  1.00 54.14           C  
ANISOU 1410  C   SER A 180     6890   5497   8185   -236    750   -124       C  
ATOM   1411  O   SER A 180     -15.853  10.254  20.079  1.00 54.31           O  
ANISOU 1411  O   SER A 180     6934   5584   8117   -197    715   -104       O  
ATOM   1412  CB  SER A 180     -15.066   7.152  20.380  1.00 55.24           C  
ANISOU 1412  CB  SER A 180     7182   5599   8210   -222    831    -83       C  
ATOM   1413  OG  SER A 180     -14.352   6.317  21.273  1.00 57.94           O  
ANISOU 1413  OG  SER A 180     7596   5924   8494   -206    932    -35       O  
ATOM   1414  N   LEU A 181     -17.605   8.925  19.532  1.00 53.71           N  
ANISOU 1414  N   LEU A 181     6758   5385   8267   -275    679   -185       N  
ATOM   1415  CA  LEU A 181     -18.234   9.866  18.586  1.00 54.07           C  
ANISOU 1415  CA  LEU A 181     6747   5441   8356   -266    543   -233       C  
ATOM   1416  C   LEU A 181     -18.838  11.059  19.324  1.00 53.81           C  
ANISOU 1416  C   LEU A 181     6626   5433   8387   -263    577   -225       C  
ATOM   1417  O   LEU A 181     -18.633  12.188  18.900  1.00 54.08           O  
ANISOU 1417  O   LEU A 181     6669   5515   8363   -227    502   -222       O  
ATOM   1418  CB  LEU A 181     -19.314   9.164  17.731  1.00 54.20           C  
ANISOU 1418  CB  LEU A 181     6698   5378   8515   -305    444   -310       C  
ATOM   1419  CG  LEU A 181     -19.917   9.957  16.570  1.00 54.80           C  
ANISOU 1419  CG  LEU A 181     6742   5454   8624   -286    268   -366       C  
ATOM   1420  CD1 LEU A 181     -18.831  10.442  15.598  1.00 54.92           C  
ANISOU 1420  CD1 LEU A 181     6894   5525   8448   -230    183   -345       C  
ATOM   1421  CD2 LEU A 181     -20.959   9.119  15.840  1.00 54.74           C  
ANISOU 1421  CD2 LEU A 181     6671   5361   8769   -325    166   -449       C  
ATOM   1422  N   ILE A 182     -19.531  10.820  20.466  1.00 52.87           N  
ANISOU 1422  N   ILE A 182     6433   5276   8380   -298    704   -218       N  
ATOM   1423  CA  ILE A 182     -20.103  11.902  21.261  1.00 52.53           C  
ANISOU 1423  CA  ILE A 182     6311   5250   8397   -294    758   -213       C  
ATOM   1424  C   ILE A 182     -18.976  12.819  21.749  1.00 52.26           C  
ANISOU 1424  C   ILE A 182     6363   5298   8194   -243    789   -153       C  
ATOM   1425  O   ILE A 182     -19.067  14.044  21.618  1.00 53.34           O  
ANISOU 1425  O   ILE A 182     6472   5475   8322   -216    737   -157       O  
ATOM   1426  CB  ILE A 182     -20.927  11.347  22.450  1.00 53.01           C  
ANISOU 1426  CB  ILE A 182     6303   5248   8590   -341    920   -211       C  
ATOM   1427  CG1 ILE A 182     -22.151  10.535  21.980  1.00 53.81           C  
ANISOU 1427  CG1 ILE A 182     6290   5259   8898   -399    892   -280       C  
ATOM   1428  CG2 ILE A 182     -21.354  12.476  23.399  1.00 53.50           C  
ANISOU 1428  CG2 ILE A 182     6308   5332   8688   -328   1002   -199       C  
ATOM   1429  CD1 ILE A 182     -22.881   9.743  23.141  1.00 54.61           C  
ANISOU 1429  CD1 ILE A 182     6338   5279   9131   -458   1084   -274       C  
ATOM   1430  N   TYR A 183     -17.898  12.217  22.260  1.00 50.76           N  
ANISOU 1430  N   TYR A 183     6277   5130   7880   -228    862   -103       N  
ATOM   1431  CA  TYR A 183     -16.740  12.949  22.763  1.00 50.04           C  
ANISOU 1431  CA  TYR A 183     6264   5110   7640   -181    886    -53       C  
ATOM   1432  C   TYR A 183     -16.024  13.743  21.646  1.00 49.10           C  
ANISOU 1432  C   TYR A 183     6181   5045   7431   -147    762    -59       C  
ATOM   1433  O   TYR A 183     -15.774  14.932  21.819  1.00 47.91           O  
ANISOU 1433  O   TYR A 183     6026   4940   7240   -121    747    -46       O  
ATOM   1434  CB  TYR A 183     -15.771  11.989  23.487  1.00 49.80           C  
ANISOU 1434  CB  TYR A 183     6333   5079   7512   -168    972     -7       C  
ATOM   1435  CG  TYR A 183     -14.469  12.638  23.903  1.00 50.37           C  
ANISOU 1435  CG  TYR A 183     6480   5219   7440   -117    974     34       C  
ATOM   1436  CD1 TYR A 183     -14.455  13.718  24.772  1.00 51.49           C  
ANISOU 1436  CD1 TYR A 183     6610   5394   7559    -98   1012     49       C  
ATOM   1437  CD2 TYR A 183     -13.256  12.171  23.427  1.00 50.82           C  
ANISOU 1437  CD2 TYR A 183     6613   5303   7395    -88    936     50       C  
ATOM   1438  CE1 TYR A 183     -13.264  14.322  25.152  1.00 52.39           C  
ANISOU 1438  CE1 TYR A 183     6785   5565   7555    -54   1002     78       C  
ATOM   1439  CE2 TYR A 183     -12.060  12.752  23.816  1.00 52.05           C  
ANISOU 1439  CE2 TYR A 183     6819   5515   7443    -44    935     79       C  
ATOM   1440  CZ  TYR A 183     -12.068  13.847  24.660  1.00 53.35           C  
ANISOU 1440  CZ  TYR A 183     6969   5712   7591    -28    961     91       C  
ATOM   1441  OH  TYR A 183     -10.893  14.468  25.023  1.00 55.20           O  
ANISOU 1441  OH  TYR A 183     7243   5997   7731     13    947    110       O  
ATOM   1442  N   SER A 184     -15.712  13.075  20.513  1.00 49.05           N  
ANISOU 1442  N   SER A 184     6218   5026   7393   -147    682    -78       N  
ATOM   1443  CA  SER A 184     -15.028  13.658  19.353  1.00 48.82           C  
ANISOU 1443  CA  SER A 184     6245   5033   7271   -116    580    -82       C  
ATOM   1444  C   SER A 184     -15.831  14.806  18.712  1.00 49.56           C  
ANISOU 1444  C   SER A 184     6286   5127   7417   -110    482   -112       C  
ATOM   1445  O   SER A 184     -15.245  15.816  18.317  1.00 49.86           O  
ANISOU 1445  O   SER A 184     6365   5207   7373    -79    443    -96       O  
ATOM   1446  CB  SER A 184     -14.699  12.573  18.337  1.00 48.53           C  
ANISOU 1446  CB  SER A 184     6272   4968   7200   -120    530   -102       C  
ATOM   1447  OG  SER A 184     -14.144  13.082  17.144  1.00 49.53           O  
ANISOU 1447  OG  SER A 184     6466   5117   7236    -92    441   -110       O  
ATOM   1448  N   LEU A 185     -17.164  14.674  18.641  1.00 49.61           N  
ANISOU 1448  N   LEU A 185     6198   5082   7568   -137    444   -158       N  
ATOM   1449  CA  LEU A 185     -18.032  15.727  18.099  1.00 49.93           C  
ANISOU 1449  CA  LEU A 185     6178   5114   7678   -125    341   -192       C  
ATOM   1450  C   LEU A 185     -18.105  16.918  19.053  1.00 50.30           C  
ANISOU 1450  C   LEU A 185     6179   5195   7737   -110    404   -167       C  
ATOM   1451  O   LEU A 185     -18.078  18.054  18.592  1.00 50.19           O  
ANISOU 1451  O   LEU A 185     6176   5203   7692    -79    331   -167       O  
ATOM   1452  CB  LEU A 185     -19.438  15.201  17.761  1.00 49.69           C  
ANISOU 1452  CB  LEU A 185     6044   5013   7824   -156    274   -259       C  
ATOM   1453  CG  LEU A 185     -19.499  14.296  16.527  1.00 51.20           C  
ANISOU 1453  CG  LEU A 185     6287   5164   8003   -162    160   -300       C  
ATOM   1454  CD1 LEU A 185     -20.834  13.574  16.454  1.00 51.61           C  
ANISOU 1454  CD1 LEU A 185     6220   5139   8252   -204    118   -369       C  
ATOM   1455  CD2 LEU A 185     -19.217  15.091  15.236  1.00 51.63           C  
ANISOU 1455  CD2 LEU A 185     6429   5234   7954   -114     10   -310       C  
ATOM   1456  N   CYS A 186     -18.137  16.668  20.376  1.00 50.66           N  
ANISOU 1456  N   CYS A 186     6191   5243   7814   -128    542   -144       N  
ATOM   1457  CA  CYS A 186     -18.144  17.761  21.365  1.00 51.63           C  
ANISOU 1457  CA  CYS A 186     6287   5397   7934   -111    611   -122       C  
ATOM   1458  C   CYS A 186     -16.831  18.507  21.393  1.00 50.93           C  
ANISOU 1458  C   CYS A 186     6290   5370   7689    -76    609    -79       C  
ATOM   1459  O   CYS A 186     -16.815  19.716  21.594  1.00 50.80           O  
ANISOU 1459  O   CYS A 186     6262   5378   7662    -54    596    -73       O  
ATOM   1460  CB  CYS A 186     -18.517  17.261  22.754  1.00 53.58           C  
ANISOU 1460  CB  CYS A 186     6500   5621   8237   -136    763   -109       C  
ATOM   1461  SG  CYS A 186     -20.210  16.654  22.877  1.00 60.31           S  
ANISOU 1461  SG  CYS A 186     7212   6390   9315   -184    796   -166       S  
ATOM   1462  N   LEU A 187     -15.736  17.779  21.209  1.00 50.57           N  
ANISOU 1462  N   LEU A 187     6331   5346   7537    -71    625    -52       N  
ATOM   1463  CA  LEU A 187     -14.384  18.300  21.138  1.00 50.45           C  
ANISOU 1463  CA  LEU A 187     6395   5384   7391    -42    625    -17       C  
ATOM   1464  C   LEU A 187     -14.159  19.045  19.817  1.00 50.50           C  
ANISOU 1464  C   LEU A 187     6437   5399   7353    -25    518    -26       C  
ATOM   1465  O   LEU A 187     -13.452  20.030  19.810  1.00 51.09           O  
ANISOU 1465  O   LEU A 187     6542   5507   7362     -5    516     -6       O  
ATOM   1466  CB  LEU A 187     -13.410  17.146  21.312  1.00 50.70           C  
ANISOU 1466  CB  LEU A 187     6492   5422   7349    -41    674      5       C  
ATOM   1467  CG  LEU A 187     -11.961  17.474  21.579  1.00 52.70           C  
ANISOU 1467  CG  LEU A 187     6807   5724   7491    -12    698     37       C  
ATOM   1468  CD1 LEU A 187     -11.805  18.460  22.728  1.00 53.13           C  
ANISOU 1468  CD1 LEU A 187     6844   5806   7535      2    745     52       C  
ATOM   1469  CD2 LEU A 187     -11.206  16.201  21.875  1.00 53.47           C  
ANISOU 1469  CD2 LEU A 187     6955   5816   7546     -7    745     53       C  
ATOM   1470  N   THR A 188     -14.791  18.627  18.719  1.00 50.41           N  
ANISOU 1470  N   THR A 188     6427   5350   7378    -32    430    -58       N  
ATOM   1471  CA  THR A 188     -14.724  19.349  17.441  1.00 50.79           C  
ANISOU 1471  CA  THR A 188     6528   5393   7376     -9    322    -67       C  
ATOM   1472  C   THR A 188     -15.458  20.679  17.595  1.00 51.62           C  
ANISOU 1472  C   THR A 188     6579   5495   7539      6    280    -75       C  
ATOM   1473  O   THR A 188     -14.977  21.701  17.119  1.00 52.16           O  
ANISOU 1473  O   THR A 188     6703   5578   7538     30    247    -56       O  
ATOM   1474  CB  THR A 188     -15.394  18.543  16.310  1.00 51.58           C  
ANISOU 1474  CB  THR A 188     6646   5444   7507    -16    221   -108       C  
ATOM   1475  OG1 THR A 188     -14.729  17.301  16.194  1.00 52.90           O  
ANISOU 1475  OG1 THR A 188     6865   5610   7624    -28    266   -103       O  
ATOM   1476  CG2 THR A 188     -15.360  19.270  14.957  1.00 51.28           C  
ANISOU 1476  CG2 THR A 188     6693   5391   7399     16    103   -116       C  
ATOM   1477  N   LEU A 189     -16.625  20.665  18.265  1.00 51.55           N  
ANISOU 1477  N   LEU A 189     6462   5460   7664     -9    291   -103       N  
ATOM   1478  CA  LEU A 189     -17.420  21.852  18.501  1.00 52.02           C  
ANISOU 1478  CA  LEU A 189     6454   5510   7801      9    258   -118       C  
ATOM   1479  C   LEU A 189     -16.719  22.824  19.462  1.00 52.14           C  
ANISOU 1479  C   LEU A 189     6482   5568   7760     21    344    -81       C  
ATOM   1480  O   LEU A 189     -16.422  23.946  19.071  1.00 52.74           O  
ANISOU 1480  O   LEU A 189     6596   5654   7788     46    298    -68       O  
ATOM   1481  CB  LEU A 189     -18.813  21.459  19.022  1.00 52.73           C  
ANISOU 1481  CB  LEU A 189     6413   5555   8065    -13    269   -163       C  
ATOM   1482  CG  LEU A 189     -19.746  22.614  19.347  1.00 55.30           C  
ANISOU 1482  CG  LEU A 189     6650   5864   8499      7    243   -187       C  
ATOM   1483  CD1 LEU A 189     -20.027  23.457  18.113  1.00 55.98           C  
ANISOU 1483  CD1 LEU A 189     6769   5930   8571     47     82   -204       C  
ATOM   1484  CD2 LEU A 189     -21.045  22.108  19.968  1.00 56.42           C  
ANISOU 1484  CD2 LEU A 189     6650   5957   8828    -20    285   -235       C  
ATOM   1485  N   LEU A 190     -16.411  22.391  20.690  1.00 51.46           N  
ANISOU 1485  N   LEU A 190     6378   5502   7671      4    464    -64       N  
ATOM   1486  CA  LEU A 190     -15.807  23.226  21.717  1.00 51.34           C  
ANISOU 1486  CA  LEU A 190     6376   5522   7608     17    540    -39       C  
ATOM   1487  C   LEU A 190     -14.328  23.563  21.466  1.00 50.24           C  
ANISOU 1487  C   LEU A 190     6328   5425   7336     30    539     -4       C  
ATOM   1488  O   LEU A 190     -13.899  24.684  21.740  1.00 50.38           O  
ANISOU 1488  O   LEU A 190     6359   5461   7321     46    544      7       O  
ATOM   1489  CB  LEU A 190     -16.009  22.520  23.079  1.00 52.52           C  
ANISOU 1489  CB  LEU A 190     6496   5669   7789      0    661    -35       C  
ATOM   1490  CG  LEU A 190     -15.633  23.279  24.358  1.00 54.74           C  
ANISOU 1490  CG  LEU A 190     6791   5974   8033     16    744    -19       C  
ATOM   1491  CD1 LEU A 190     -16.385  24.571  24.481  1.00 55.45           C  
ANISOU 1491  CD1 LEU A 190     6823   6052   8194     31    724    -41       C  
ATOM   1492  CD2 LEU A 190     -15.870  22.426  25.564  1.00 55.31           C  
ANISOU 1492  CD2 LEU A 190     6865   6032   8118      3    861    -13       C  
ATOM   1493  N   GLY A 191     -13.566  22.603  20.953  1.00 48.64           N  
ANISOU 1493  N   GLY A 191     6181   5231   7069     23    539      8       N  
ATOM   1494  CA  GLY A 191     -12.147  22.793  20.716  1.00 47.91           C  
ANISOU 1494  CA  GLY A 191     6160   5173   6873     32    551     35       C  
ATOM   1495  C   GLY A 191     -11.771  23.429  19.398  1.00 47.99           C  
ANISOU 1495  C   GLY A 191     6227   5175   6831     42    483     40       C  
ATOM   1496  O   GLY A 191     -10.783  24.166  19.328  1.00 47.40           O  
ANISOU 1496  O   GLY A 191     6190   5121   6698     49    502     59       O  
ATOM   1497  N   PHE A 192     -12.544  23.160  18.336  1.00 48.16           N  
ANISOU 1497  N   PHE A 192     6262   5161   6874     43    403     21       N  
ATOM   1498  CA  PHE A 192     -12.234  23.716  17.020  1.00 48.18           C  
ANISOU 1498  CA  PHE A 192     6349   5146   6810     58    338     29       C  
ATOM   1499  C   PHE A 192     -13.262  24.753  16.482  1.00 48.32           C  
ANISOU 1499  C   PHE A 192     6359   5128   6871     79    242     15       C  
ATOM   1500  O   PHE A 192     -12.887  25.897  16.244  1.00 48.35           O  
ANISOU 1500  O   PHE A 192     6405   5130   6835     93    235     35       O  
ATOM   1501  CB  PHE A 192     -12.017  22.566  16.007  1.00 47.48           C  
ANISOU 1501  CB  PHE A 192     6328   5040   6671     55    309     20       C  
ATOM   1502  CG  PHE A 192     -11.867  22.956  14.551  1.00 47.39           C  
ANISOU 1502  CG  PHE A 192     6429   4998   6580     75    237     23       C  
ATOM   1503  CD1 PHE A 192     -11.077  24.038  14.180  1.00 48.12           C  
ANISOU 1503  CD1 PHE A 192     6589   5094   6602     86    261     54       C  
ATOM   1504  CD2 PHE A 192     -12.441  22.190  13.550  1.00 47.59           C  
ANISOU 1504  CD2 PHE A 192     6504   4984   6594     82    153     -5       C  
ATOM   1505  CE1 PHE A 192     -10.941  24.399  12.843  1.00 48.26           C  
ANISOU 1505  CE1 PHE A 192     6731   5072   6532    106    209     62       C  
ATOM   1506  CE2 PHE A 192     -12.264  22.521  12.215  1.00 48.15           C  
ANISOU 1506  CE2 PHE A 192     6705   5021   6570    106     89     -1       C  
ATOM   1507  CZ  PHE A 192     -11.522  23.634  11.869  1.00 48.00           C  
ANISOU 1507  CZ  PHE A 192     6762   5002   6473    119    123     36       C  
ATOM   1508  N   LEU A 193     -14.510  24.340  16.226  1.00 47.90           N  
ANISOU 1508  N   LEU A 193     6255   5041   6904     81    164    -22       N  
ATOM   1509  CA  LEU A 193     -15.512  25.177  15.584  1.00 48.10           C  
ANISOU 1509  CA  LEU A 193     6274   5024   6979    109     49    -43       C  
ATOM   1510  C   LEU A 193     -15.894  26.443  16.355  1.00 49.40           C  
ANISOU 1510  C   LEU A 193     6374   5191   7203    123     66    -39       C  
ATOM   1511  O   LEU A 193     -16.112  27.484  15.720  1.00 49.96           O  
ANISOU 1511  O   LEU A 193     6491   5235   7257    155    -11    -33       O  
ATOM   1512  CB  LEU A 193     -16.767  24.361  15.228  1.00 47.31           C  
ANISOU 1512  CB  LEU A 193     6109   4883   6985    107    -42    -95       C  
ATOM   1513  CG  LEU A 193     -16.592  23.265  14.162  1.00 47.40           C  
ANISOU 1513  CG  LEU A 193     6201   4873   6937    104   -101   -110       C  
ATOM   1514  CD1 LEU A 193     -17.879  22.562  13.911  1.00 47.20           C  
ANISOU 1514  CD1 LEU A 193     6094   4800   7039     99   -199   -170       C  
ATOM   1515  CD2 LEU A 193     -16.081  23.841  12.839  1.00 48.00           C  
ANISOU 1515  CD2 LEU A 193     6431   4927   6879    138   -179    -91       C  
ATOM   1516  N   ILE A 194     -15.994  26.367  17.699  1.00 49.25           N  
ANISOU 1516  N   ILE A 194     6264   5200   7248    104    164    -42       N  
ATOM   1517  CA  ILE A 194     -16.353  27.533  18.525  1.00 48.88           C  
ANISOU 1517  CA  ILE A 194     6160   5154   7258    118    191    -44       C  
ATOM   1518  C   ILE A 194     -15.199  28.551  18.515  1.00 49.21           C  
ANISOU 1518  C   ILE A 194     6282   5217   7197    126    224     -5       C  
ATOM   1519  O   ILE A 194     -15.459  29.662  18.064  1.00 49.77           O  
ANISOU 1519  O   ILE A 194     6378   5260   7272    152    164     -2       O  
ATOM   1520  CB  ILE A 194     -16.897  27.194  19.952  1.00 48.10           C  
ANISOU 1520  CB  ILE A 194     5957   5067   7253    100    291    -62       C  
ATOM   1521  CG1 ILE A 194     -18.306  26.572  19.853  1.00 48.06           C  
ANISOU 1521  CG1 ILE A 194     5850   5019   7391     95    249   -109       C  
ATOM   1522  CG2 ILE A 194     -16.936  28.453  20.837  1.00 48.26           C  
ANISOU 1522  CG2 ILE A 194     5950   5094   7294    117    336    -59       C  
ATOM   1523  CD1 ILE A 194     -18.913  26.067  21.166  1.00 48.37           C  
ANISOU 1523  CD1 ILE A 194     5793   5056   7528     71    367   -127       C  
ATOM   1524  N   PRO A 195     -13.917  28.212  18.852  1.00 48.97           N  
ANISOU 1524  N   PRO A 195     6298   5226   7080    106    306     22       N  
ATOM   1525  CA  PRO A 195     -12.840  29.221  18.716  1.00 49.07           C  
ANISOU 1525  CA  PRO A 195     6378   5249   7019    108    331     52       C  
ATOM   1526  C   PRO A 195     -12.693  29.788  17.296  1.00 49.50           C  
ANISOU 1526  C   PRO A 195     6532   5266   7012    125    259     70       C  
ATOM   1527  O   PRO A 195     -12.457  30.978  17.170  1.00 50.69           O  
ANISOU 1527  O   PRO A 195     6717   5396   7145    135    254     86       O  
ATOM   1528  CB  PRO A 195     -11.577  28.461  19.176  1.00 48.78           C  
ANISOU 1528  CB  PRO A 195     6358   5254   6920     85    415     67       C  
ATOM   1529  CG  PRO A 195     -12.086  27.423  20.075  1.00 48.81           C  
ANISOU 1529  CG  PRO A 195     6297   5274   6974     76    451     49       C  
ATOM   1530  CD  PRO A 195     -13.372  26.960  19.418  1.00 47.65           C  
ANISOU 1530  CD  PRO A 195     6122   5091   6891     82    379     25       C  
ATOM   1531  N   LEU A 196     -12.880  28.970  16.237  1.00 48.78           N  
ANISOU 1531  N   LEU A 196     6495   5155   6884    129    201     66       N  
ATOM   1532  CA  LEU A 196     -12.805  29.438  14.851  1.00 48.76           C  
ANISOU 1532  CA  LEU A 196     6613   5107   6806    152    130     84       C  
ATOM   1533  C   LEU A 196     -13.907  30.464  14.539  1.00 48.91           C  
ANISOU 1533  C   LEU A 196     6629   5078   6878    190     24     73       C  
ATOM   1534  O   LEU A 196     -13.643  31.467  13.862  1.00 49.81           O  
ANISOU 1534  O   LEU A 196     6839   5154   6932    210     -2    100       O  
ATOM   1535  CB  LEU A 196     -12.855  28.268  13.856  1.00 48.91           C  
ANISOU 1535  CB  LEU A 196     6698   5112   6773    154     84     73       C  
ATOM   1536  CG  LEU A 196     -12.617  28.631  12.374  1.00 50.40           C  
ANISOU 1536  CG  LEU A 196     7049   5252   6851    180     23     94       C  
ATOM   1537  CD1 LEU A 196     -11.203  29.131  12.136  1.00 50.92           C  
ANISOU 1537  CD1 LEU A 196     7203   5323   6822    163    133    137       C  
ATOM   1538  CD2 LEU A 196     -12.901  27.455  11.464  1.00 50.68           C  
ANISOU 1538  CD2 LEU A 196     7146   5267   6844    188    -43     71       C  
ATOM   1539  N   SER A 197     -15.125  30.237  15.063  1.00 47.79           N  
ANISOU 1539  N   SER A 197     6373   4930   6854    200    -28     32       N  
ATOM   1540  CA  SER A 197     -16.268  31.136  14.900  1.00 46.65           C  
ANISOU 1540  CA  SER A 197     6194   4740   6791    241   -132     11       C  
ATOM   1541  C   SER A 197     -16.064  32.423  15.653  1.00 46.71           C  
ANISOU 1541  C   SER A 197     6178   4749   6820    247    -78     27       C  
ATOM   1542  O   SER A 197     -16.508  33.459  15.186  1.00 47.08           O  
ANISOU 1542  O   SER A 197     6263   4748   6876    286   -155     31       O  
ATOM   1543  CB  SER A 197     -17.535  30.482  15.412  1.00 47.17           C  
ANISOU 1543  CB  SER A 197     6119   4800   7003    242   -172    -42       C  
ATOM   1544  OG  SER A 197     -17.767  29.320  14.647  1.00 51.00           O  
ANISOU 1544  OG  SER A 197     6628   5274   7476    236   -235    -63       O  
ATOM   1545  N   VAL A 198     -15.431  32.369  16.840  1.00 46.33           N  
ANISOU 1545  N   VAL A 198     6072   4750   6782    214     45     32       N  
ATOM   1546  CA  VAL A 198     -15.151  33.549  17.644  1.00 45.82           C  
ANISOU 1546  CA  VAL A 198     5988   4688   6734    216    100     41       C  
ATOM   1547  C   VAL A 198     -14.132  34.418  16.896  1.00 47.15           C  
ANISOU 1547  C   VAL A 198     6282   4834   6800    216    106     84       C  
ATOM   1548  O   VAL A 198     -14.350  35.612  16.797  1.00 48.40           O  
ANISOU 1548  O   VAL A 198     6466   4952   6973    241     74     92       O  
ATOM   1549  CB  VAL A 198     -14.739  33.205  19.102  1.00 44.87           C  
ANISOU 1549  CB  VAL A 198     5789   4620   6638    186    216     30       C  
ATOM   1550  CG1 VAL A 198     -14.138  34.418  19.819  1.00 45.30           C  
ANISOU 1550  CG1 VAL A 198     5853   4676   6682    185    269     39       C  
ATOM   1551  CG2 VAL A 198     -15.914  32.638  19.886  1.00 43.77           C  
ANISOU 1551  CG2 VAL A 198     5534   4483   6612    190    225    -10       C  
ATOM   1552  N   MET A 199     -13.111  33.828  16.260  1.00 47.51           N  
ANISOU 1552  N   MET A 199     6410   4894   6749    192    144    111       N  
ATOM   1553  CA  MET A 199     -12.167  34.599  15.444  1.00 48.67           C  
ANISOU 1553  CA  MET A 199     6680   5008   6805    188    167    151       C  
ATOM   1554  C   MET A 199     -12.859  35.238  14.227  1.00 49.98           C  
ANISOU 1554  C   MET A 199     6952   5102   6937    233     55    166       C  
ATOM   1555  O   MET A 199     -12.565  36.376  13.896  1.00 51.06           O  
ANISOU 1555  O   MET A 199     7165   5192   7042    244     60    195       O  
ATOM   1556  CB  MET A 199     -10.971  33.746  15.013  1.00 49.17           C  
ANISOU 1556  CB  MET A 199     6801   5097   6785    155    243    171       C  
ATOM   1557  CG  MET A 199      -9.982  33.519  16.127  1.00 51.50           C  
ANISOU 1557  CG  MET A 199     7020   5447   7101    116    349    164       C  
ATOM   1558  SD  MET A 199      -8.481  32.677  15.566  1.00 59.07           S  
ANISOU 1558  SD  MET A 199     8037   6426   7980     83    441    184       S  
ATOM   1559  CE  MET A 199      -9.119  31.024  15.278  1.00 53.13           C  
ANISOU 1559  CE  MET A 199     7271   5697   7217     94    394    164       C  
ATOM   1560  N   CYS A 200     -13.798  34.532  13.599  1.00 50.05           N  
ANISOU 1560  N   CYS A 200     6966   5095   6957    263    -50    144       N  
ATOM   1561  CA  CYS A 200     -14.588  35.016  12.468  1.00 50.62           C  
ANISOU 1561  CA  CYS A 200     7138   5095   7001    318   -187    149       C  
ATOM   1562  C   CYS A 200     -15.462  36.193  12.885  1.00 51.39           C  
ANISOU 1562  C   CYS A 200     7180   5155   7190    357   -250    136       C  
ATOM   1563  O   CYS A 200     -15.660  37.113  12.094  1.00 51.84           O  
ANISOU 1563  O   CYS A 200     7350   5144   7202    399   -325    160       O  
ATOM   1564  CB  CYS A 200     -15.453  33.889  11.911  1.00 51.49           C  
ANISOU 1564  CB  CYS A 200     7231   5201   7131    338   -297    111       C  
ATOM   1565  SG  CYS A 200     -14.547  32.681  10.924  1.00 56.79           S  
ANISOU 1565  SG  CYS A 200     8032   5882   7663    315   -263    128       S  
ATOM   1566  N   PHE A 201     -16.051  36.119  14.098  1.00 51.30           N  
ANISOU 1566  N   PHE A 201     7003   5181   7306    347   -223     97       N  
ATOM   1567  CA  PHE A 201     -16.910  37.145  14.661  1.00 51.50           C  
ANISOU 1567  CA  PHE A 201     6954   5176   7437    383   -264     76       C  
ATOM   1568  C   PHE A 201     -16.081  38.397  14.930  1.00 52.25           C  
ANISOU 1568  C   PHE A 201     7113   5253   7487    374   -190    113       C  
ATOM   1569  O   PHE A 201     -16.521  39.502  14.607  1.00 52.66           O  
ANISOU 1569  O   PHE A 201     7210   5242   7556    418   -257    121       O  
ATOM   1570  CB  PHE A 201     -17.596  36.640  15.945  1.00 51.62           C  
ANISOU 1570  CB  PHE A 201     6790   5237   7588    367   -216     26       C  
ATOM   1571  CG  PHE A 201     -18.394  37.701  16.671  1.00 52.61           C  
ANISOU 1571  CG  PHE A 201     6830   5333   7827    401   -228     -1       C  
ATOM   1572  CD1 PHE A 201     -19.593  38.161  16.159  1.00 53.69           C  
ANISOU 1572  CD1 PHE A 201     6938   5409   8052    462   -363    -29       C  
ATOM   1573  CD2 PHE A 201     -17.924  38.265  17.843  1.00 53.52           C  
ANISOU 1573  CD2 PHE A 201     6898   5476   7959    377   -111     -1       C  
ATOM   1574  CE1 PHE A 201     -20.308  39.163  16.804  1.00 54.27           C  
ANISOU 1574  CE1 PHE A 201     6933   5451   8236    498   -370    -55       C  
ATOM   1575  CE2 PHE A 201     -18.633  39.279  18.476  1.00 54.59           C  
ANISOU 1575  CE2 PHE A 201     6969   5580   8193    411   -117    -27       C  
ATOM   1576  CZ  PHE A 201     -19.820  39.720  17.953  1.00 54.34           C  
ANISOU 1576  CZ  PHE A 201     6904   5489   8255    472   -241    -54       C  
ATOM   1577  N   PHE A 202     -14.871  38.236  15.491  1.00 52.31           N  
ANISOU 1577  N   PHE A 202     7124   5308   7444    318    -58    132       N  
ATOM   1578  CA  PHE A 202     -14.020  39.385  15.780  1.00 53.05           C  
ANISOU 1578  CA  PHE A 202     7267   5381   7510    300     15    160       C  
ATOM   1579  C   PHE A 202     -13.388  39.963  14.523  1.00 55.74           C  
ANISOU 1579  C   PHE A 202     7779   5658   7742    307      3    212       C  
ATOM   1580  O   PHE A 202     -13.144  41.161  14.491  1.00 55.78           O  
ANISOU 1580  O   PHE A 202     7839   5612   7743    313     19    234       O  
ATOM   1581  CB  PHE A 202     -13.002  39.089  16.879  1.00 51.97           C  
ANISOU 1581  CB  PHE A 202     7062   5309   7376    244    143    151       C  
ATOM   1582  CG  PHE A 202     -13.655  39.248  18.225  1.00 51.62           C  
ANISOU 1582  CG  PHE A 202     6888   5292   7433    252    161    107       C  
ATOM   1583  CD1 PHE A 202     -13.866  40.503  18.766  1.00 51.86           C  
ANISOU 1583  CD1 PHE A 202     6905   5286   7512    269    165     98       C  
ATOM   1584  CD2 PHE A 202     -14.164  38.154  18.897  1.00 52.18           C  
ANISOU 1584  CD2 PHE A 202     6860   5415   7551    245    176     75       C  
ATOM   1585  CE1 PHE A 202     -14.528  40.655  19.975  1.00 52.29           C  
ANISOU 1585  CE1 PHE A 202     6852   5360   7654    281    189     54       C  
ATOM   1586  CE2 PHE A 202     -14.827  38.310  20.107  1.00 52.68           C  
ANISOU 1586  CE2 PHE A 202     6820   5494   7703    255    208     36       C  
ATOM   1587  CZ  PHE A 202     -15.003  39.560  20.638  1.00 52.09           C  
ANISOU 1587  CZ  PHE A 202     6736   5386   7670    274    215     24       C  
ATOM   1588  N   TYR A 203     -13.223  39.166  13.441  1.00 57.83           N  
ANISOU 1588  N   TYR A 203     8140   5915   7917    310    -28    232       N  
ATOM   1589  CA  TYR A 203     -12.754  39.722  12.168  1.00 60.22           C  
ANISOU 1589  CA  TYR A 203     8632   6144   8104    326    -40    283       C  
ATOM   1590  C   TYR A 203     -13.850  40.673  11.649  1.00 61.01           C  
ANISOU 1590  C   TYR A 203     8792   6164   8224    398   -178    287       C  
ATOM   1591  O   TYR A 203     -13.560  41.789  11.247  1.00 61.30           O  
ANISOU 1591  O   TYR A 203     8942   6131   8219    411   -167    326       O  
ATOM   1592  CB  TYR A 203     -12.462  38.617  11.146  1.00 61.87           C  
ANISOU 1592  CB  TYR A 203     8939   6358   8210    323    -51    296       C  
ATOM   1593  CG  TYR A 203     -12.359  39.152   9.734  1.00 65.48           C  
ANISOU 1593  CG  TYR A 203     9614   6725   8540    360    -95    344       C  
ATOM   1594  CD1 TYR A 203     -11.230  39.842   9.311  1.00 67.55           C  
ANISOU 1594  CD1 TYR A 203    10001   6942   8721    328     27    396       C  
ATOM   1595  CD2 TYR A 203     -13.424  39.043   8.847  1.00 67.74           C  
ANISOU 1595  CD2 TYR A 203     9985   6960   8793    430   -262    335       C  
ATOM   1596  CE1 TYR A 203     -11.144  40.367   8.027  1.00 69.41           C  
ANISOU 1596  CE1 TYR A 203    10458   7084   8830    364      0    446       C  
ATOM   1597  CE2 TYR A 203     -13.354  39.572   7.562  1.00 69.32           C  
ANISOU 1597  CE2 TYR A 203    10410   7068   8861    473   -312    381       C  
ATOM   1598  CZ  TYR A 203     -12.202  40.213   7.148  1.00 71.02           C  
ANISOU 1598  CZ  TYR A 203    10765   7239   8980    440   -172    440       C  
ATOM   1599  OH  TYR A 203     -12.138  40.777   5.890  1.00 73.80           O  
ANISOU 1599  OH  TYR A 203    11362   7490   9191    484   -206    492       O  
ATOM   1600  N   TYR A 204     -15.108  40.227  11.706  1.00 61.47           N  
ANISOU 1600  N   TYR A 204     8767   6228   8359    444   -308    242       N  
ATOM   1601  CA  TYR A 204     -16.278  40.984  11.303  1.00 62.26           C  
ANISOU 1601  CA  TYR A 204     8891   6258   8509    521   -460    230       C  
ATOM   1602  C   TYR A 204     -16.416  42.284  12.127  1.00 62.05           C  
ANISOU 1602  C   TYR A 204     8806   6205   8565    531   -428    229       C  
ATOM   1603  O   TYR A 204     -16.745  43.315  11.556  1.00 61.92           O  
ANISOU 1603  O   TYR A 204     8893   6104   8529    584   -504    254       O  
ATOM   1604  CB  TYR A 204     -17.534  40.088  11.414  1.00 63.29           C  
ANISOU 1604  CB  TYR A 204     8891   6411   8744    555   -584    167       C  
ATOM   1605  CG  TYR A 204     -18.830  40.865  11.440  1.00 65.59           C  
ANISOU 1605  CG  TYR A 204     9126   6644   9151    630   -727    134       C  
ATOM   1606  CD1 TYR A 204     -19.338  41.446  10.286  1.00 66.95           C  
ANISOU 1606  CD1 TYR A 204     9445   6725   9268    707   -885    151       C  
ATOM   1607  CD2 TYR A 204     -19.499  41.096  12.634  1.00 67.36           C  
ANISOU 1607  CD2 TYR A 204     9160   6897   9537    629   -699     86       C  
ATOM   1608  CE1 TYR A 204     -20.508  42.193  10.310  1.00 68.38           C  
ANISOU 1608  CE1 TYR A 204     9569   6847   9565    783  -1025    118       C  
ATOM   1609  CE2 TYR A 204     -20.660  41.857  12.674  1.00 68.84           C  
ANISOU 1609  CE2 TYR A 204     9286   7025   9843    701   -819     51       C  
ATOM   1610  CZ  TYR A 204     -21.162  42.405  11.509  1.00 70.16           C  
ANISOU 1610  CZ  TYR A 204     9587   7104   9967    779   -988     66       C  
ATOM   1611  OH  TYR A 204     -22.315  43.163  11.547  1.00 73.16           O  
ANISOU 1611  OH  TYR A 204     9899   7422  10478    858  -1119     28       O  
ATOM   1612  N   LYS A 205     -16.197  42.226  13.465  1.00 61.62           N  
ANISOU 1612  N   LYS A 205     8596   6216   8600    485   -321    199       N  
ATOM   1613  CA  LYS A 205     -16.275  43.394  14.353  1.00 61.00           C  
ANISOU 1613  CA  LYS A 205     8461   6117   8599    490   -279    190       C  
ATOM   1614  C   LYS A 205     -15.182  44.408  13.994  1.00 61.47           C  
ANISOU 1614  C   LYS A 205     8662   6124   8571    464   -202    245       C  
ATOM   1615  O   LYS A 205     -15.411  45.620  14.043  1.00 61.62           O  
ANISOU 1615  O   LYS A 205     8719   6075   8619    496   -226    256       O  
ATOM   1616  CB  LYS A 205     -16.142  42.981  15.828  1.00 62.06           C  
ANISOU 1616  CB  LYS A 205     8428   6333   8819    444   -174    146       C  
ATOM   1617  CG  LYS A 205     -17.319  42.183  16.394  1.00 65.37           C  
ANISOU 1617  CG  LYS A 205     8694   6790   9354    467   -222     88       C  
ATOM   1618  CD  LYS A 205     -18.625  42.970  16.404  1.00 69.39           C  
ANISOU 1618  CD  LYS A 205     9150   7238   9978    540   -331     55       C  
ATOM   1619  CE  LYS A 205     -18.702  43.985  17.525  1.00 72.76           C  
ANISOU 1619  CE  LYS A 205     9510   7654  10482    544   -263     33       C  
ATOM   1620  NZ  LYS A 205     -19.513  45.174  17.142  1.00 74.42           N  
ANISOU 1620  NZ  LYS A 205     9750   7775  10750    619   -369     30       N  
ATOM   1621  N   MET A 206     -13.988  43.911  13.633  1.00 61.85           N  
ANISOU 1621  N   MET A 206     8783   6197   8520    406   -104    280       N  
ATOM   1622  CA  MET A 206     -12.866  44.733  13.198  1.00 62.30           C  
ANISOU 1622  CA  MET A 206     8971   6199   8501    371    -11    332       C  
ATOM   1623  C   MET A 206     -13.216  45.443  11.889  1.00 63.51           C  
ANISOU 1623  C   MET A 206     9316   6245   8571    429    -98    381       C  
ATOM   1624  O   MET A 206     -12.995  46.639  11.786  1.00 63.91           O  
ANISOU 1624  O   MET A 206     9447   6219   8618    435    -75    411       O  
ATOM   1625  CB  MET A 206     -11.618  43.883  12.993  1.00 62.28           C  
ANISOU 1625  CB  MET A 206     8994   6245   8426    303    107    350       C  
ATOM   1626  CG  MET A 206     -10.907  43.499  14.253  1.00 64.74           C  
ANISOU 1626  CG  MET A 206     9155   6638   8803    243    211    313       C  
ATOM   1627  SD  MET A 206      -9.553  42.338  13.838  1.00 68.09           S  
ANISOU 1627  SD  MET A 206     9607   7114   9150    179    326    330       S  
ATOM   1628  CE  MET A 206      -8.448  42.737  15.063  1.00 65.20           C  
ANISOU 1628  CE  MET A 206     9134   6783   8856    115    443    305       C  
ATOM   1629  N   VAL A 207     -13.773  44.723  10.901  1.00 64.19           N  
ANISOU 1629  N   VAL A 207     9484   6318   8587    474   -204    388       N  
ATOM   1630  CA  VAL A 207     -14.167  45.301   9.617  1.00 65.49           C  
ANISOU 1630  CA  VAL A 207     9853   6377   8655    541   -309    433       C  
ATOM   1631  C   VAL A 207     -15.235  46.404   9.801  1.00 67.00           C  
ANISOU 1631  C   VAL A 207    10027   6499   8930    616   -432    420       C  
ATOM   1632  O   VAL A 207     -15.144  47.463   9.180  1.00 67.77           O  
ANISOU 1632  O   VAL A 207    10285   6495   8969    649   -450    469       O  
ATOM   1633  CB  VAL A 207     -14.603  44.192   8.627  1.00 66.16           C  
ANISOU 1633  CB  VAL A 207    10014   6468   8656    578   -416    428       C  
ATOM   1634  CG1 VAL A 207     -15.412  44.758   7.465  1.00 66.71           C  
ANISOU 1634  CG1 VAL A 207    10267   6429   8651    674   -586    453       C  
ATOM   1635  CG2 VAL A 207     -13.391  43.425   8.113  1.00 66.70           C  
ANISOU 1635  CG2 VAL A 207    10176   6562   8603    516   -281    461       C  
ATOM   1636  N   VAL A 208     -16.217  46.169  10.671  1.00 67.29           N  
ANISOU 1636  N   VAL A 208     9872   6587   9110    641   -505    355       N  
ATOM   1637  CA  VAL A 208     -17.276  47.130  10.954  1.00 67.92           C  
ANISOU 1637  CA  VAL A 208     9902   6608   9296    714   -615    330       C  
ATOM   1638  C   VAL A 208     -16.684  48.390  11.604  1.00 69.93           C  
ANISOU 1638  C   VAL A 208    10167   6825   9578    685   -506    352       C  
ATOM   1639  O   VAL A 208     -17.033  49.500  11.205  1.00 70.75           O  
ANISOU 1639  O   VAL A 208    10374   6829   9679    743   -573    378       O  
ATOM   1640  CB  VAL A 208     -18.405  46.477  11.794  1.00 67.77           C  
ANISOU 1640  CB  VAL A 208     9658   6656   9437    736   -684    250       C  
ATOM   1641  CG1 VAL A 208     -19.291  47.515  12.469  1.00 68.33           C  
ANISOU 1641  CG1 VAL A 208     9634   6683   9646    791   -736    215       C  
ATOM   1642  CG2 VAL A 208     -19.240  45.551  10.936  1.00 67.89           C  
ANISOU 1642  CG2 VAL A 208     9684   6667   9442    787   -841    226       C  
ATOM   1643  N   PHE A 209     -15.760  48.223  12.564  1.00 70.55           N  
ANISOU 1643  N   PHE A 209    10151   6974   9681    599   -347    340       N  
ATOM   1644  CA  PHE A 209     -15.113  49.348  13.239  1.00 71.18           C  
ANISOU 1644  CA  PHE A 209    10232   7020   9794    563   -243    350       C  
ATOM   1645  C   PHE A 209     -14.339  50.227  12.246  1.00 73.47           C  
ANISOU 1645  C   PHE A 209    10737   7204   9973    556   -202    426       C  
ATOM   1646  O   PHE A 209     -14.437  51.452  12.312  1.00 73.70           O  
ANISOU 1646  O   PHE A 209    10824   7147  10031    580   -208    442       O  
ATOM   1647  CB  PHE A 209     -14.181  48.841  14.348  1.00 69.97           C  
ANISOU 1647  CB  PHE A 209     9949   6962   9674    474    -97    320       C  
ATOM   1648  CG  PHE A 209     -13.497  49.934  15.122  1.00 69.33           C  
ANISOU 1648  CG  PHE A 209     9854   6849   9638    433      0    317       C  
ATOM   1649  CD1 PHE A 209     -14.129  50.549  16.182  1.00 69.36           C  
ANISOU 1649  CD1 PHE A 209     9745   6855   9753    459    -18    265       C  
ATOM   1650  CD2 PHE A 209     -12.214  50.346  14.789  1.00 69.54           C  
ANISOU 1650  CD2 PHE A 209     9981   6839   9604    368    113    359       C  
ATOM   1651  CE1 PHE A 209     -13.506  51.571  16.880  1.00 69.86           C  
ANISOU 1651  CE1 PHE A 209     9806   6883   9856    424     61    256       C  
ATOM   1652  CE2 PHE A 209     -11.587  51.360  15.498  1.00 69.72           C  
ANISOU 1652  CE2 PHE A 209     9984   6825   9682    327    193    348       C  
ATOM   1653  CZ  PHE A 209     -12.232  51.960  16.545  1.00 69.52           C  
ANISOU 1653  CZ  PHE A 209     9854   6802   9756    356    161    296       C  
ATOM   1654  N   LEU A 210     -13.588  49.601  11.326  1.00 75.12           N  
ANISOU 1654  N   LEU A 210    11072   7413  10059    523   -153    471       N  
ATOM   1655  CA  LEU A 210     -12.797  50.305  10.321  1.00 77.50           C  
ANISOU 1655  CA  LEU A 210    11593   7611  10244    509    -87    547       C  
ATOM   1656  C   LEU A 210     -13.657  50.983   9.241  1.00 80.59           C  
ANISOU 1656  C   LEU A 210    12171   7883  10566    609   -234    589       C  
ATOM   1657  O   LEU A 210     -13.257  52.012   8.696  1.00 80.87           O  
ANISOU 1657  O   LEU A 210    12378   7807  10543    614   -191    647       O  
ATOM   1658  CB  LEU A 210     -11.750  49.374   9.709  1.00 77.40           C  
ANISOU 1658  CB  LEU A 210    11651   7633  10124    447     25    576       C  
ATOM   1659  CG  LEU A 210     -10.675  48.912  10.683  1.00 78.70           C  
ANISOU 1659  CG  LEU A 210    11661   7890  10353    348    180    544       C  
ATOM   1660  CD1 LEU A 210      -9.820  47.808  10.086  1.00 79.25           C  
ANISOU 1660  CD1 LEU A 210    11777   8003  10332    301    268    562       C  
ATOM   1661  CD2 LEU A 210      -9.822  50.067  11.132  1.00 79.14           C  
ANISOU 1661  CD2 LEU A 210    11724   7888  10460    292    301    559       C  
ATOM   1662  N   LYS A 211     -14.846  50.433   8.958  1.00 82.63           N  
ANISOU 1662  N   LYS A 211    12397   8160  10840    691   -411    556       N  
ATOM   1663  CA  LYS A 211     -15.779  51.033   8.004  1.00 85.05           C  
ANISOU 1663  CA  LYS A 211    12864   8356  11097    800   -586    583       C  
ATOM   1664  C   LYS A 211     -16.345  52.342   8.581  1.00 87.53           C  
ANISOU 1664  C   LYS A 211    13135   8601  11522    847   -632    572       C  
ATOM   1665  O   LYS A 211     -16.505  53.319   7.852  1.00 88.12           O  
ANISOU 1665  O   LYS A 211    13397   8551  11535    907   -692    623       O  
ATOM   1666  CB  LYS A 211     -16.921  50.054   7.677  1.00 87.13           C  
ANISOU 1666  CB  LYS A 211    13061   8661  11383    871   -773    533       C  
ATOM   1667  CG  LYS A 211     -16.580  49.057   6.572  1.00 91.79           C  
ANISOU 1667  CG  LYS A 211    13805   9255  11815    870   -792    562       C  
ATOM   1668  CD  LYS A 211     -17.736  48.091   6.317  1.00 96.74           C  
ANISOU 1668  CD  LYS A 211    14351   9920  12487    937   -989    500       C  
ATOM   1669  CE  LYS A 211     -17.418  47.033   5.286  1.00100.97           C  
ANISOU 1669  CE  LYS A 211    15026  10466  12870    933  -1011    517       C  
ATOM   1670  NZ  LYS A 211     -18.238  45.797   5.482  1.00103.36           N  
ANISOU 1670  NZ  LYS A 211    15159  10852  13262    946  -1126    439       N  
ATOM   1671  N   LYS A 212     -16.624  52.360   9.892  1.00 88.94           N  
ANISOU 1671  N   LYS A 212    13080   8855  11857    820   -597    505       N  
ATOM   1672  CA  LYS A 212     -17.135  53.508  10.632  1.00 90.96           C  
ANISOU 1672  CA  LYS A 212    13266   9062  12234    857   -621    480       C  
ATOM   1673  C   LYS A 212     -16.051  54.614  10.687  1.00 92.70           C  
ANISOU 1673  C   LYS A 212    13605   9204  12412    799   -474    534       C  
ATOM   1674  O   LYS A 212     -16.343  55.794  10.457  1.00 92.74           O  
ANISOU 1674  O   LYS A 212    13715   9094  12427    852   -520    561       O  
ATOM   1675  CB  LYS A 212     -17.522  53.038  12.047  1.00 93.41           C  
ANISOU 1675  CB  LYS A 212    13308   9484  12700    828   -585    394       C  
ATOM   1676  CG  LYS A 212     -18.113  54.099  12.968  1.00 98.66           C  
ANISOU 1676  CG  LYS A 212    13874  10110  13502    866   -598    353       C  
ATOM   1677  CD  LYS A 212     -18.375  53.530  14.367  1.00104.06           C  
ANISOU 1677  CD  LYS A 212    14317  10906  14313    829   -533    272       C  
ATOM   1678  CE  LYS A 212     -17.097  53.149  15.083  1.00108.71           C  
ANISOU 1678  CE  LYS A 212    14867  11574  14866    716   -356    273       C  
ATOM   1679  NZ  LYS A 212     -17.370  52.420  16.352  1.00111.75           N  
ANISOU 1679  NZ  LYS A 212    15046  12064  15350    688   -302    200       N  
ATOM   1680  N   ARG A 213     -14.792  54.219  10.952  1.00 93.78           N  
ANISOU 1680  N   ARG A 213    13728   9397  12508    690   -300    548       N  
ATOM   1681  CA  ARG A 213     -13.665  55.151  11.026  1.00 95.18           C  
ANISOU 1681  CA  ARG A 213    13994   9505  12665    618   -147    590       C  
ATOM   1682  C   ARG A 213     -13.266  55.725   9.646  1.00 96.21           C  
ANISOU 1682  C   ARG A 213    14404   9501  12651    637   -132    683       C  
ATOM   1683  O   ARG A 213     -12.622  56.779   9.587  1.00 96.54           O  
ANISOU 1683  O   ARG A 213    14546   9445  12689    602    -33    723       O  
ATOM   1684  CB  ARG A 213     -12.454  54.509  11.746  1.00 96.76           C  
ANISOU 1684  CB  ARG A 213    14075   9804  12886    500     23    565       C  
ATOM   1685  CG  ARG A 213     -12.708  54.134  13.211  1.00100.32           C  
ANISOU 1685  CG  ARG A 213    14282  10368  13468    477     30    479       C  
ATOM   1686  CD  ARG A 213     -12.966  55.328  14.106  1.00104.35           C  
ANISOU 1686  CD  ARG A 213    14734  10827  14086    490     32    446       C  
ATOM   1687  NE  ARG A 213     -13.958  55.022  15.141  1.00107.93           N  
ANISOU 1687  NE  ARG A 213    15004  11357  14647    534    -40    369       N  
ATOM   1688  CZ  ARG A 213     -13.766  55.207  16.445  1.00110.40           C  
ANISOU 1688  CZ  ARG A 213    15175  11720  15051    497     24    308       C  
ATOM   1689  NH1 ARG A 213     -12.615  55.697  16.893  1.00109.83           N  
ANISOU 1689  NH1 ARG A 213    15111  11634  14985    416    143    307       N  
ATOM   1690  NH2 ARG A 213     -14.726  54.907  17.311  1.00110.43           N  
ANISOU 1690  NH2 ARG A 213    15031  11784  15144    542    -30    242       N  
ATOM   1691  N   SER A 214     -13.662  55.048   8.542  1.00 96.42           N  
ANISOU 1691  N   SER A 214    14564   9513  12556    694   -230    716       N  
ATOM   1692  CA  SER A 214     -13.366  55.480   7.175  1.00 96.94           C  
ANISOU 1692  CA  SER A 214    14924   9450  12460    725   -224    806       C  
ATOM   1693  C   SER A 214     -14.439  56.432   6.640  1.00 97.52           C  
ANISOU 1693  C   SER A 214    15136   9396  12519    847   -399    832       C  
ATOM   1694  O   SER A 214     -14.863  57.361   7.331  1.00 97.76           O  
ANISOU 1694  O   SER A 214    15086   9391  12668    873   -432    806       O  
ATOM   1695  CB  SER A 214     -13.245  54.272   6.251  1.00 98.00           C  
ANISOU 1695  CB  SER A 214    15152   9625  12457    732   -248    825       C  
ATOM   1696  N   ASN A 224      -5.029  46.225   6.510  1.00 81.13           N  
ANISOU 1696  N   ASN A 224    12533   8113  10179     87    912    736       N  
ATOM   1697  CA  ASN A 224      -4.575  46.662   7.832  1.00 81.49           C  
ANISOU 1697  CA  ASN A 224    12362   8209  10392     28    960    690       C  
ATOM   1698  C   ASN A 224      -3.948  45.507   8.626  1.00 80.53           C  
ANISOU 1698  C   ASN A 224    12038   8211  10348    -21   1009    630       C  
ATOM   1699  O   ASN A 224      -4.305  44.348   8.411  1.00 80.47           O  
ANISOU 1699  O   ASN A 224    12017   8271  10287      9    947    613       O  
ATOM   1700  CB  ASN A 224      -5.728  47.299   8.617  1.00 83.87           C  
ANISOU 1700  CB  ASN A 224    12580   8523  10766     81    797    662       C  
ATOM   1701  CG  ASN A 224      -6.416  48.408   7.868  1.00 89.06           C  
ANISOU 1701  CG  ASN A 224    13430   9056  11352    142    726    716       C  
ATOM   1702  OD1 ASN A 224      -6.010  49.584   7.928  1.00 90.84           O  
ANISOU 1702  OD1 ASN A 224    13712   9191  11611    114    802    745       O  
ATOM   1703  ND2 ASN A 224      -7.471  48.055   7.137  1.00 90.28           N  
ANISOU 1703  ND2 ASN A 224    13694   9199  11411    229    571    729       N  
ATOM   1704  N   LYS A 225      -3.018  45.831   9.548  1.00 79.60           N  
ANISOU 1704  N   LYS A 225    11768   8117  10360    -93   1110    596       N  
ATOM   1705  CA  LYS A 225      -2.325  44.847  10.394  1.00 79.17           C  
ANISOU 1705  CA  LYS A 225    11521   8171  10390   -137   1153    538       C  
ATOM   1706  C   LYS A 225      -3.248  44.014  11.294  1.00 78.53           C  
ANISOU 1706  C   LYS A 225    11299   8201  10337    -92   1005    487       C  
ATOM   1707  O   LYS A 225      -3.046  42.793  11.372  1.00 78.53           O  
ANISOU 1707  O   LYS A 225    11236   8278  10323    -94   1008    463       O  
ATOM   1708  CB  LYS A 225      -1.204  45.496  11.243  1.00 80.93           C  
ANISOU 1708  CB  LYS A 225    11612   8384  10755   -214   1263    504       C  
ATOM   1709  CG  LYS A 225      -0.189  46.332  10.443  1.00 85.13           C  
ANISOU 1709  CG  LYS A 225    12258   8798  11291   -273   1436    548       C  
ATOM   1710  CD  LYS A 225       0.856  47.002  11.350  1.00 89.32           C  
ANISOU 1710  CD  LYS A 225    12637   9313  11986   -352   1524    503       C  
ATOM   1711  CE  LYS A 225       1.801  47.908  10.594  1.00 93.76           C  
ANISOU 1711  CE  LYS A 225    13302   9748  12575   -418   1706    543       C  
ATOM   1712  NZ  LYS A 225       2.370  48.994  11.451  1.00 96.63           N  
ANISOU 1712  NZ  LYS A 225    13560  10063  13093   -478   1742    506       N  
ATOM   1713  N   PRO A 226      -4.254  44.613  11.988  1.00 77.62           N  
ANISOU 1713  N   PRO A 226    11133   8093  10266    -52    884    468       N  
ATOM   1714  CA  PRO A 226      -5.118  43.790  12.851  1.00 76.75           C  
ANISOU 1714  CA  PRO A 226    10889   8081  10190    -15    769    419       C  
ATOM   1715  C   PRO A 226      -5.879  42.750  12.051  1.00 75.82           C  
ANISOU 1715  C   PRO A 226    10842   7988   9979     35    688    432       C  
ATOM   1716  O   PRO A 226      -6.029  41.621  12.498  1.00 76.43           O  
ANISOU 1716  O   PRO A 226    10819   8149  10070     38    659    398       O  
ATOM   1717  CB  PRO A 226      -6.070  44.803  13.495  1.00 77.77           C  
ANISOU 1717  CB  PRO A 226    10987   8185  10378     21    675    404       C  
ATOM   1718  CG  PRO A 226      -5.480  46.135  13.254  1.00 78.62           C  
ANISOU 1718  CG  PRO A 226    11173   8194  10504    -10    751    434       C  
ATOM   1719  CD  PRO A 226      -4.663  46.035  12.018  1.00 77.08           C  
ANISOU 1719  CD  PRO A 226    11127   7937  10223    -38    857    488       C  
ATOM   1720  N   LEU A 227      -6.310  43.109  10.846  1.00 74.29           N  
ANISOU 1720  N   LEU A 227    10829   7712   9686     75    651    481       N  
ATOM   1721  CA  LEU A 227      -7.021  42.193   9.972  1.00 73.06           C  
ANISOU 1721  CA  LEU A 227    10762   7565   9434    126    560    490       C  
ATOM   1722  C   LEU A 227      -6.108  41.089   9.460  1.00 72.14           C  
ANISOU 1722  C   LEU A 227    10673   7480   9256     92    660    494       C  
ATOM   1723  O   LEU A 227      -6.557  39.965   9.305  1.00 72.33           O  
ANISOU 1723  O   LEU A 227    10676   7557   9249    116    594    472       O  
ATOM   1724  CB  LEU A 227      -7.643  42.973   8.805  1.00 73.12           C  
ANISOU 1724  CB  LEU A 227    10978   7462   9340    184    488    541       C  
ATOM   1725  CG  LEU A 227      -9.124  43.354   8.949  1.00 74.63           C  
ANISOU 1725  CG  LEU A 227    11153   7640   9565    261    303    524       C  
ATOM   1726  CD1 LEU A 227      -9.392  44.091  10.226  1.00 75.14           C  
ANISOU 1726  CD1 LEU A 227    11053   7730   9765    249    293    489       C  
ATOM   1727  CD2 LEU A 227      -9.562  44.239   7.825  1.00 75.52           C  
ANISOU 1727  CD2 LEU A 227    11483   7633   9578    320    235    577       C  
ATOM   1728  N   ARG A 228      -4.823  41.391   9.237  1.00 71.22           N  
ANISOU 1728  N   ARG A 228    10594   7330   9135     33    823    517       N  
ATOM   1729  CA  ARG A 228      -3.837  40.444   8.721  1.00 70.64           C  
ANISOU 1729  CA  ARG A 228    10548   7276   9016     -1    942    520       C  
ATOM   1730  C   ARG A 228      -3.674  39.212   9.610  1.00 68.42           C  
ANISOU 1730  C   ARG A 228    10084   7108   8803    -16    928    464       C  
ATOM   1731  O   ARG A 228      -3.781  38.098   9.105  1.00 68.53           O  
ANISOU 1731  O   ARG A 228    10135   7152   8753      3    911    458       O  
ATOM   1732  CB  ARG A 228      -2.483  41.151   8.467  1.00 73.48           C  
ANISOU 1732  CB  ARG A 228    10947   7570   9400    -67   1132    546       C  
ATOM   1733  CG  ARG A 228      -1.677  40.590   7.294  1.00 78.97           C  
ANISOU 1733  CG  ARG A 228    11788   8223   9995    -83   1266    578       C  
ATOM   1734  CD  ARG A 228      -0.548  41.521   6.865  1.00 84.54           C  
ANISOU 1734  CD  ARG A 228    12566   8833  10721   -143   1457    613       C  
ATOM   1735  NE  ARG A 228      -1.044  42.708   6.153  1.00 89.41           N  
ANISOU 1735  NE  ARG A 228    13377   9336  11258   -117   1441    673       N  
ATOM   1736  CZ  ARG A 228      -0.733  43.965   6.472  1.00 91.80           C  
ANISOU 1736  CZ  ARG A 228    13670   9572  11639   -155   1499    689       C  
ATOM   1737  NH1 ARG A 228      -1.235  44.977   5.777  1.00 91.57           N  
ANISOU 1737  NH1 ARG A 228    13834   9433  11525   -123   1478    747       N  
ATOM   1738  NH2 ARG A 228       0.080  44.216   7.491  1.00 91.61           N  
ANISOU 1738  NH2 ARG A 228    13447   9585  11777   -221   1572    644       N  
ATOM   1739  N   LEU A 229      -3.442  39.411  10.922  1.00 66.36           N  
ANISOU 1739  N   LEU A 229     9643   6904   8668    -45    931    424       N  
ATOM   1740  CA  LEU A 229      -3.257  38.338  11.903  1.00 65.10           C  
ANISOU 1740  CA  LEU A 229     9316   6843   8573    -57    918    374       C  
ATOM   1741  C   LEU A 229      -4.501  37.423  12.007  1.00 63.84           C  
ANISOU 1741  C   LEU A 229     9136   6736   8386     -5    781    355       C  
ATOM   1742  O   LEU A 229      -4.360  36.202  11.993  1.00 63.58           O  
ANISOU 1742  O   LEU A 229     9067   6754   8336     -4    785    337       O  
ATOM   1743  CB  LEU A 229      -2.903  38.929  13.294  1.00 65.08           C  
ANISOU 1743  CB  LEU A 229     9157   6875   8694    -87    927    336       C  
ATOM   1744  CG  LEU A 229      -2.526  37.927  14.394  1.00 66.69           C  
ANISOU 1744  CG  LEU A 229     9204   7171   8964    -98    923    286       C  
ATOM   1745  CD1 LEU A 229      -1.503  38.516  15.324  1.00 67.11           C  
ANISOU 1745  CD1 LEU A 229     9150   7230   9120   -143    985    254       C  
ATOM   1746  CD2 LEU A 229      -3.760  37.464  15.201  1.00 67.57           C  
ANISOU 1746  CD2 LEU A 229     9247   7341   9087    -56    801    260       C  
ATOM   1747  N   VAL A 230      -5.699  38.022  12.143  1.00 62.64           N  
ANISOU 1747  N   VAL A 230     8995   6565   8242     36    665    356       N  
ATOM   1748  CA  VAL A 230      -6.950  37.295  12.297  1.00 62.03           C  
ANISOU 1748  CA  VAL A 230     8877   6524   8168     82    537    331       C  
ATOM   1749  C   VAL A 230      -7.271  36.492  11.057  1.00 61.62           C  
ANISOU 1749  C   VAL A 230     8954   6449   8012    111    493    347       C  
ATOM   1750  O   VAL A 230      -7.637  35.328  11.177  1.00 61.80           O  
ANISOU 1750  O   VAL A 230     8923   6520   8037    120    450    320       O  
ATOM   1751  CB  VAL A 230      -8.129  38.198  12.725  1.00 62.29           C  
ANISOU 1751  CB  VAL A 230     8879   6533   8254    120    431    322       C  
ATOM   1752  CG1 VAL A 230      -9.317  37.350  13.161  1.00 62.46           C  
ANISOU 1752  CG1 VAL A 230     8808   6603   8322    154    324    283       C  
ATOM   1753  CG2 VAL A 230      -7.711  39.126  13.854  1.00 62.97           C  
ANISOU 1753  CG2 VAL A 230     8868   6628   8428     91    484    307       C  
ATOM   1754  N   VAL A 231      -7.087  37.084   9.863  1.00 60.81           N  
ANISOU 1754  N   VAL A 231     9030   6264   7811    126    509    392       N  
ATOM   1755  CA  VAL A 231      -7.339  36.393   8.593  1.00 60.12           C  
ANISOU 1755  CA  VAL A 231     9100   6142   7603    160    466    407       C  
ATOM   1756  C   VAL A 231      -6.372  35.215   8.428  1.00 58.98           C  
ANISOU 1756  C   VAL A 231     8943   6041   7428    125    573    396       C  
ATOM   1757  O   VAL A 231      -6.805  34.127   8.075  1.00 59.36           O  
ANISOU 1757  O   VAL A 231     9005   6113   7438    147    509    375       O  
ATOM   1758  CB  VAL A 231      -7.305  37.361   7.383  1.00 60.80           C  
ANISOU 1758  CB  VAL A 231     9406   6120   7575    186    471    461       C  
ATOM   1759  CG1 VAL A 231      -7.376  36.602   6.069  1.00 61.16           C  
ANISOU 1759  CG1 VAL A 231     9637   6125   7474    219    449    477       C  
ATOM   1760  CG2 VAL A 231      -8.441  38.364   7.465  1.00 61.38           C  
ANISOU 1760  CG2 VAL A 231     9498   6148   7676    238    329    466       C  
ATOM   1761  N   LEU A 232      -5.090  35.403   8.761  1.00 57.72           N  
ANISOU 1761  N   LEU A 232     8739   5891   7303     71    728    405       N  
ATOM   1762  CA  LEU A 232      -4.108  34.331   8.678  1.00 57.30           C  
ANISOU 1762  CA  LEU A 232     8656   5876   7241     41    835    390       C  
ATOM   1763  C   LEU A 232      -4.471  33.207   9.665  1.00 57.05           C  
ANISOU 1763  C   LEU A 232     8458   5934   7283     43    772    342       C  
ATOM   1764  O   LEU A 232      -4.381  32.033   9.315  1.00 57.38           O  
ANISOU 1764  O   LEU A 232     8516   6000   7286     51    775    326       O  
ATOM   1765  CB  LEU A 232      -2.678  34.851   8.924  1.00 57.68           C  
ANISOU 1765  CB  LEU A 232     8661   5911   7344    -16   1005    399       C  
ATOM   1766  CG  LEU A 232      -1.583  33.796   8.719  1.00 60.18           C  
ANISOU 1766  CG  LEU A 232     8948   6256   7661    -42   1124    382       C  
ATOM   1767  CD1 LEU A 232      -1.512  33.349   7.273  1.00 60.79           C  
ANISOU 1767  CD1 LEU A 232     9223   6277   7597    -19   1167    409       C  
ATOM   1768  CD2 LEU A 232      -0.234  34.264   9.217  1.00 60.95           C  
ANISOU 1768  CD2 LEU A 232     8948   6351   7860    -99   1271    374       C  
ATOM   1769  N   ALA A 233      -4.939  33.558  10.872  1.00 56.07           N  
ANISOU 1769  N   ALA A 233     8190   5854   7261     40    716    319       N  
ATOM   1770  CA  ALA A 233      -5.333  32.562  11.852  1.00 55.23           C  
ANISOU 1770  CA  ALA A 233     7944   5823   7220     42    667    279       C  
ATOM   1771  C   ALA A 233      -6.537  31.767  11.339  1.00 54.94           C  
ANISOU 1771  C   ALA A 233     7948   5784   7143     82    547    266       C  
ATOM   1772  O   ALA A 233      -6.475  30.549  11.321  1.00 55.40           O  
ANISOU 1772  O   ALA A 233     7981   5875   7192     81    548    246       O  
ATOM   1773  CB  ALA A 233      -5.632  33.221  13.188  1.00 55.06           C  
ANISOU 1773  CB  ALA A 233     7789   5834   7299     34    642    259       C  
ATOM   1774  N   VAL A 234      -7.585  32.438  10.841  1.00 54.36           N  
ANISOU 1774  N   VAL A 234     7944   5663   7048    118    440    275       N  
ATOM   1775  CA  VAL A 234      -8.772  31.769  10.314  1.00 54.30           C  
ANISOU 1775  CA  VAL A 234     7967   5643   7020    158    307    254       C  
ATOM   1776  C   VAL A 234      -8.414  30.844   9.144  1.00 54.43           C  
ANISOU 1776  C   VAL A 234     8117   5636   6925    167    318    259       C  
ATOM   1777  O   VAL A 234      -8.868  29.704   9.132  1.00 54.82           O  
ANISOU 1777  O   VAL A 234     8130   5711   6986    173    265    226       O  
ATOM   1778  CB  VAL A 234      -9.915  32.763   9.977  1.00 54.95           C  
ANISOU 1778  CB  VAL A 234     8097   5671   7111    203    179    259       C  
ATOM   1779  CG1 VAL A 234     -11.032  32.087   9.197  1.00 55.28           C  
ANISOU 1779  CG1 VAL A 234     8192   5686   7128    248     30    233       C  
ATOM   1780  CG2 VAL A 234     -10.470  33.409  11.243  1.00 55.49           C  
ANISOU 1780  CG2 VAL A 234     8010   5769   7305    199    160    239       C  
ATOM   1781  N   VAL A 235      -7.547  31.295   8.217  1.00 53.80           N  
ANISOU 1781  N   VAL A 235     8191   5508   6745    163    403    297       N  
ATOM   1782  CA  VAL A 235      -7.090  30.493   7.072  1.00 53.63           C  
ANISOU 1782  CA  VAL A 235     8317   5456   6604    172    439    302       C  
ATOM   1783  C   VAL A 235      -6.243  29.268   7.512  1.00 54.05           C  
ANISOU 1783  C   VAL A 235     8278   5569   6689    139    538    278       C  
ATOM   1784  O   VAL A 235      -6.498  28.137   7.077  1.00 54.36           O  
ANISOU 1784  O   VAL A 235     8350   5615   6689    154    495    252       O  
ATOM   1785  CB  VAL A 235      -6.341  31.368   6.012  1.00 53.81           C  
ANISOU 1785  CB  VAL A 235     8534   5400   6510    174    535    353       C  
ATOM   1786  CG1 VAL A 235      -5.677  30.506   4.946  1.00 53.96           C  
ANISOU 1786  CG1 VAL A 235     8701   5392   6409    179    612    357       C  
ATOM   1787  CG2 VAL A 235      -7.280  32.380   5.364  1.00 53.78           C  
ANISOU 1787  CG2 VAL A 235     8663   5324   6447    223    412    378       C  
ATOM   1788  N   ILE A 236      -5.243  29.482   8.375  1.00 53.85           N  
ANISOU 1788  N   ILE A 236     8139   5584   6739     97    661    282       N  
ATOM   1789  CA  ILE A 236      -4.378  28.389   8.834  1.00 54.01           C  
ANISOU 1789  CA  ILE A 236     8070   5656   6797     73    748    259       C  
ATOM   1790  C   ILE A 236      -5.190  27.287   9.527  1.00 53.96           C  
ANISOU 1790  C   ILE A 236     7956   5701   6847     84    653    221       C  
ATOM   1791  O   ILE A 236      -5.076  26.128   9.146  1.00 54.14           O  
ANISOU 1791  O   ILE A 236     8006   5730   6835     90    658    202       O  
ATOM   1792  CB  ILE A 236      -3.178  28.905   9.694  1.00 54.63           C  
ANISOU 1792  CB  ILE A 236     8034   5762   6961     32    873    263       C  
ATOM   1793  CG1 ILE A 236      -2.143  29.645   8.813  1.00 54.88           C  
ANISOU 1793  CG1 ILE A 236     8178   5733   6942     13   1007    295       C  
ATOM   1794  CG2 ILE A 236      -2.503  27.749  10.469  1.00 55.54           C  
ANISOU 1794  CG2 ILE A 236     8024   5938   7140     20    920    231       C  
ATOM   1795  CD1 ILE A 236      -0.972  30.181   9.539  1.00 55.85           C  
ANISOU 1795  CD1 ILE A 236     8186   5870   7162    -29   1121    291       C  
ATOM   1796  N   PHE A 237      -6.060  27.657  10.485  1.00 53.45           N  
ANISOU 1796  N   PHE A 237     7779   5664   6867     86    572    209       N  
ATOM   1797  CA  PHE A 237      -6.866  26.682  11.210  1.00 53.04           C  
ANISOU 1797  CA  PHE A 237     7623   5651   6879     90    502    176       C  
ATOM   1798  C   PHE A 237      -7.967  26.075  10.355  1.00 52.55           C  
ANISOU 1798  C   PHE A 237     7634   5555   6778    118    382    156       C  
ATOM   1799  O   PHE A 237      -8.192  24.883  10.470  1.00 53.36           O  
ANISOU 1799  O   PHE A 237     7702   5675   6899    116    364    129       O  
ATOM   1800  CB  PHE A 237      -7.403  27.266  12.530  1.00 53.00           C  
ANISOU 1800  CB  PHE A 237     7481   5680   6977     82    475    167       C  
ATOM   1801  CG  PHE A 237      -6.299  27.487  13.546  1.00 53.56           C  
ANISOU 1801  CG  PHE A 237     7466   5792   7093     56    577    171       C  
ATOM   1802  CD1 PHE A 237      -5.654  26.415  14.141  1.00 54.35           C  
ANISOU 1802  CD1 PHE A 237     7503   5932   7214     46    630    156       C  
ATOM   1803  CD2 PHE A 237      -5.875  28.760  13.868  1.00 54.06           C  
ANISOU 1803  CD2 PHE A 237     7516   5845   7177     45    613    187       C  
ATOM   1804  CE1 PHE A 237      -4.622  26.623  15.043  1.00 54.81           C  
ANISOU 1804  CE1 PHE A 237     7487   6023   7316     30    702    154       C  
ATOM   1805  CE2 PHE A 237      -4.835  28.962  14.766  1.00 54.63           C  
ANISOU 1805  CE2 PHE A 237     7508   5950   7297     22    690    182       C  
ATOM   1806  CZ  PHE A 237      -4.224  27.898  15.352  1.00 54.42           C  
ANISOU 1806  CZ  PHE A 237     7420   5965   7293     18    728    164       C  
ATOM   1807  N   SER A 238      -8.615  26.845   9.466  1.00 51.79           N  
ANISOU 1807  N   SER A 238     7646   5404   6628    147    296    166       N  
ATOM   1808  CA  SER A 238      -9.643  26.280   8.576  1.00 51.90           C  
ANISOU 1808  CA  SER A 238     7738   5378   6605    181    161    139       C  
ATOM   1809  C   SER A 238      -9.028  25.230   7.653  1.00 52.12           C  
ANISOU 1809  C   SER A 238     7882   5389   6531    184    200    132       C  
ATOM   1810  O   SER A 238      -9.609  24.181   7.465  1.00 52.66           O  
ANISOU 1810  O   SER A 238     7942   5454   6611    191    126     94       O  
ATOM   1811  CB  SER A 238     -10.277  27.354   7.698  1.00 52.81           C  
ANISOU 1811  CB  SER A 238     7977   5429   6661    222     59    155       C  
ATOM   1812  OG  SER A 238     -10.995  28.303   8.455  1.00 55.78           O  
ANISOU 1812  OG  SER A 238     8249   5809   7134    228      6    155       O  
ATOM   1813  N   VAL A 239      -7.872  25.520   7.066  1.00 51.83           N  
ANISOU 1813  N   VAL A 239     7956   5335   6402    177    320    165       N  
ATOM   1814  CA  VAL A 239      -7.221  24.601   6.148  1.00 51.94           C  
ANISOU 1814  CA  VAL A 239     8092   5326   6314    183    376    158       C  
ATOM   1815  C   VAL A 239      -6.587  23.393   6.854  1.00 52.13           C  
ANISOU 1815  C   VAL A 239     8002   5405   6401    156    459    135       C  
ATOM   1816  O   VAL A 239      -6.824  22.261   6.440  1.00 52.41           O  
ANISOU 1816  O   VAL A 239     8073   5431   6408    167    420    103       O  
ATOM   1817  CB  VAL A 239      -6.218  25.347   5.234  1.00 51.93           C  
ANISOU 1817  CB  VAL A 239     8255   5277   6198    186    495    201       C  
ATOM   1818  CG1 VAL A 239      -5.418  24.370   4.384  1.00 52.12           C  
ANISOU 1818  CG1 VAL A 239     8394   5281   6128    190    589    191       C  
ATOM   1819  CG2 VAL A 239      -6.949  26.354   4.352  1.00 51.63           C  
ANISOU 1819  CG2 VAL A 239     8378   5170   6071    226    393    223       C  
ATOM   1820  N   LEU A 240      -5.822  23.616   7.932  1.00 51.67           N  
ANISOU 1820  N   LEU A 240     7807   5397   6428    126    560    147       N  
ATOM   1821  CA  LEU A 240      -5.097  22.531   8.595  1.00 51.09           C  
ANISOU 1821  CA  LEU A 240     7637   5368   6406    109    637    129       C  
ATOM   1822  C   LEU A 240      -5.934  21.675   9.561  1.00 51.37           C  
ANISOU 1822  C   LEU A 240     7545   5440   6534    104    560    100       C  
ATOM   1823  O   LEU A 240      -5.703  20.457   9.623  1.00 52.22           O  
ANISOU 1823  O   LEU A 240     7637   5556   6646    103    581     78       O  
ATOM   1824  CB  LEU A 240      -3.815  23.060   9.293  1.00 50.41           C  
ANISOU 1824  CB  LEU A 240     7470   5314   6371     84    771    149       C  
ATOM   1825  CG  LEU A 240      -2.830  23.838   8.386  1.00 50.67           C  
ANISOU 1825  CG  LEU A 240     7615   5304   6335     79    884    176       C  
ATOM   1826  CD1 LEU A 240      -1.606  24.324   9.156  1.00 50.79           C  
ANISOU 1826  CD1 LEU A 240     7519   5346   6432     50   1004    183       C  
ATOM   1827  CD2 LEU A 240      -2.435  23.037   7.157  1.00 50.80           C  
ANISOU 1827  CD2 LEU A 240     7779   5278   6246     96    936    169       C  
ATOM   1828  N   PHE A 241      -6.899  22.260  10.286  1.00 50.65           N  
ANISOU 1828  N   PHE A 241     7368   5362   6516    100    481     98       N  
ATOM   1829  CA  PHE A 241      -7.706  21.468  11.232  1.00 50.41           C  
ANISOU 1829  CA  PHE A 241     7219   5357   6578     91    431     72       C  
ATOM   1830  C   PHE A 241      -8.944  20.784  10.633  1.00 51.31           C  
ANISOU 1830  C   PHE A 241     7363   5433   6699    103    309     37       C  
ATOM   1831  O   PHE A 241      -9.450  19.840  11.236  1.00 51.91           O  
ANISOU 1831  O   PHE A 241     7357   5518   6846     90    291     12       O  
ATOM   1832  CB  PHE A 241      -8.137  22.296  12.451  1.00 49.28           C  
ANISOU 1832  CB  PHE A 241     6955   5244   6524     81    424     81       C  
ATOM   1833  CG  PHE A 241      -7.120  22.529  13.545  1.00 49.35           C  
ANISOU 1833  CG  PHE A 241     6885   5299   6567     66    524     97       C  
ATOM   1834  CD1 PHE A 241      -5.758  22.457  13.280  1.00 49.81           C  
ANISOU 1834  CD1 PHE A 241     6978   5365   6582     63    617    110       C  
ATOM   1835  CD2 PHE A 241      -7.524  22.906  14.820  1.00 49.54           C  
ANISOU 1835  CD2 PHE A 241     6803   5352   6669     59    522     95       C  
ATOM   1836  CE1 PHE A 241      -4.823  22.713  14.279  1.00 50.29           C  
ANISOU 1836  CE1 PHE A 241     6959   5463   6687     54    689    116       C  
ATOM   1837  CE2 PHE A 241      -6.588  23.176  15.813  1.00 50.15           C  
ANISOU 1837  CE2 PHE A 241     6820   5465   6768     52    595    105       C  
ATOM   1838  CZ  PHE A 241      -5.245  23.075  15.538  1.00 50.18           C  
ANISOU 1838  CZ  PHE A 241     6850   5477   6738     50    669    113       C  
ATOM   1839  N   THR A 242      -9.485  21.285   9.511  1.00 51.25           N  
ANISOU 1839  N   THR A 242     7468   5378   6627    127    218     32       N  
ATOM   1840  CA  THR A 242     -10.722  20.730   8.947  1.00 51.23           C  
ANISOU 1840  CA  THR A 242     7486   5335   6646    142     76    -11       C  
ATOM   1841  C   THR A 242     -10.570  19.287   8.440  1.00 52.09           C  
ANISOU 1841  C   THR A 242     7644   5425   6722    139     74    -44       C  
ATOM   1842  O   THR A 242     -11.399  18.469   8.839  1.00 52.50           O  
ANISOU 1842  O   THR A 242     7609   5470   6866    124     15    -81       O  
ATOM   1843  CB  THR A 242     -11.326  21.670   7.890  1.00 51.31           C  
ANISOU 1843  CB  THR A 242     7615   5291   6589    179    -40    -10       C  
ATOM   1844  OG1 THR A 242     -11.553  22.936   8.490  1.00 50.95           O  
ANISOU 1844  OG1 THR A 242     7504   5259   6596    181    -41     15       O  
ATOM   1845  CG2 THR A 242     -12.625  21.150   7.303  1.00 51.89           C  
ANISOU 1845  CG2 THR A 242     7701   5317   6698    200   -211    -65       C  
ATOM   1846  N   PRO A 243      -9.566  18.914   7.596  1.00 52.57           N  
ANISOU 1846  N   PRO A 243     7838   5471   6663    150    143    -34       N  
ATOM   1847  CA  PRO A 243      -9.490  17.511   7.140  1.00 52.38           C  
ANISOU 1847  CA  PRO A 243     7861   5426   6614    150    137    -71       C  
ATOM   1848  C   PRO A 243      -9.351  16.521   8.290  1.00 52.09           C  
ANISOU 1848  C   PRO A 243     7682   5426   6683    120    200    -80       C  
ATOM   1849  O   PRO A 243      -9.990  15.472   8.260  1.00 52.48           O  
ANISOU 1849  O   PRO A 243     7709   5451   6780    111    141   -120       O  
ATOM   1850  CB  PRO A 243      -8.261  17.490   6.228  1.00 53.32           C  
ANISOU 1850  CB  PRO A 243     8130   5530   6597    168    242    -51       C  
ATOM   1851  CG  PRO A 243      -8.023  18.923   5.850  1.00 54.03           C  
ANISOU 1851  CG  PRO A 243     8293   5612   6625    181    259    -10       C  
ATOM   1852  CD  PRO A 243      -8.475  19.726   7.013  1.00 52.44           C  
ANISOU 1852  CD  PRO A 243     7935   5451   6539    162    240      7       C  
ATOM   1853  N   TYR A 244      -8.549  16.875   9.319  1.00 51.19           N  
ANISOU 1853  N   TYR A 244     7478   5365   6608    105    314    -43       N  
ATOM   1854  CA  TYR A 244      -8.337  16.056  10.508  1.00 50.30           C  
ANISOU 1854  CA  TYR A 244     7246   5284   6580     85    376    -43       C  
ATOM   1855  C   TYR A 244      -9.632  15.860  11.303  1.00 49.63           C  
ANISOU 1855  C   TYR A 244     7049   5194   6612     64    304    -63       C  
ATOM   1856  O   TYR A 244      -9.915  14.746  11.730  1.00 49.21           O  
ANISOU 1856  O   TYR A 244     6952   5130   6616     49    311    -83       O  
ATOM   1857  CB  TYR A 244      -7.218  16.650  11.390  1.00 50.06           C  
ANISOU 1857  CB  TYR A 244     7156   5305   6559     82    489     -4       C  
ATOM   1858  CG  TYR A 244      -7.168  16.064  12.780  1.00 51.16           C  
ANISOU 1858  CG  TYR A 244     7178   5475   6783     69    532      1       C  
ATOM   1859  CD1 TYR A 244      -6.745  14.756  12.991  1.00 52.18           C  
ANISOU 1859  CD1 TYR A 244     7307   5598   6921     71    573    -10       C  
ATOM   1860  CD2 TYR A 244      -7.619  16.787  13.878  1.00 52.06           C  
ANISOU 1860  CD2 TYR A 244     7197   5617   6966     58    528     16       C  
ATOM   1861  CE1 TYR A 244      -6.743  14.195  14.264  1.00 53.03           C  
ANISOU 1861  CE1 TYR A 244     7330   5724   7094     65    609     -1       C  
ATOM   1862  CE2 TYR A 244      -7.662  16.221  15.147  1.00 52.75           C  
ANISOU 1862  CE2 TYR A 244     7203   5724   7116     50    567     21       C  
ATOM   1863  CZ  TYR A 244      -7.189  14.938  15.343  1.00 53.71           C  
ANISOU 1863  CZ  TYR A 244     7334   5837   7236     54    608     15       C  
ATOM   1864  OH  TYR A 244      -7.173  14.402  16.607  1.00 55.17           O  
ANISOU 1864  OH  TYR A 244     7460   6033   7468     53    648     27       O  
ATOM   1865  N   HIS A 245     -10.381  16.946  11.551  1.00 49.30           N  
ANISOU 1865  N   HIS A 245     6959   5158   6615     63    249    -57       N  
ATOM   1866  CA  HIS A 245     -11.611  16.850  12.323  1.00 48.99           C  
ANISOU 1866  CA  HIS A 245     6803   5111   6701     44    199    -79       C  
ATOM   1867  C   HIS A 245     -12.674  16.079  11.574  1.00 49.92           C  
ANISOU 1867  C   HIS A 245     6935   5172   6861     40     84   -132       C  
ATOM   1868  O   HIS A 245     -13.389  15.306  12.197  1.00 50.03           O  
ANISOU 1868  O   HIS A 245     6859   5170   6983     13     83   -157       O  
ATOM   1869  CB  HIS A 245     -12.091  18.220  12.811  1.00 48.33           C  
ANISOU 1869  CB  HIS A 245     6657   5044   6661     48    178    -63       C  
ATOM   1870  CG  HIS A 245     -11.325  18.684  14.014  1.00 48.10           C  
ANISOU 1870  CG  HIS A 245     6568   5066   6642     41    289    -25       C  
ATOM   1871  ND1 HIS A 245     -10.144  19.397  13.887  1.00 49.48           N  
ANISOU 1871  ND1 HIS A 245     6796   5269   6735     53    351      9       N  
ATOM   1872  CD2 HIS A 245     -11.565  18.471  15.328  1.00 48.11           C  
ANISOU 1872  CD2 HIS A 245     6470   5088   6722     24    347    -20       C  
ATOM   1873  CE1 HIS A 245      -9.721  19.616  15.122  1.00 49.53           C  
ANISOU 1873  CE1 HIS A 245     6727   5314   6778     44    425     28       C  
ATOM   1874  NE2 HIS A 245     -10.542  19.079  16.022  1.00 49.02           N  
ANISOU 1874  NE2 HIS A 245     6581   5247   6799     30    427     14       N  
ATOM   1875  N   ILE A 246     -12.738  16.209  10.235  1.00 50.19           N  
ANISOU 1875  N   ILE A 246     7092   5170   6809     66     -7   -152       N  
ATOM   1876  CA  ILE A 246     -13.690  15.421   9.451  1.00 50.51           C  
ANISOU 1876  CA  ILE A 246     7158   5151   6884     66   -134   -212       C  
ATOM   1877  C   ILE A 246     -13.330  13.941   9.556  1.00 51.11           C  
ANISOU 1877  C   ILE A 246     7239   5213   6966     45    -78   -231       C  
ATOM   1878  O   ILE A 246     -14.185  13.134   9.903  1.00 52.03           O  
ANISOU 1878  O   ILE A 246     7270   5298   7200     16   -115   -270       O  
ATOM   1879  CB  ILE A 246     -13.747  15.888   7.972  1.00 50.91           C  
ANISOU 1879  CB  ILE A 246     7371   5160   6813    109   -249   -228       C  
ATOM   1880  CG1 ILE A 246     -14.334  17.308   7.856  1.00 51.43           C  
ANISOU 1880  CG1 ILE A 246     7430   5222   6889    134   -331   -216       C  
ATOM   1881  CG2 ILE A 246     -14.516  14.886   7.102  1.00 51.55           C  
ANISOU 1881  CG2 ILE A 246     7501   5176   6910    113   -383   -298       C  
ATOM   1882  CD1 ILE A 246     -14.260  17.917   6.465  1.00 52.29           C  
ANISOU 1882  CD1 ILE A 246     7726   5288   6853    184   -428   -216       C  
ATOM   1883  N   MET A 247     -12.047  13.594   9.338  1.00 50.62           N  
ANISOU 1883  N   MET A 247     7266   5172   6794     57     23   -202       N  
ATOM   1884  CA  MET A 247     -11.585  12.202   9.342  1.00 50.24           C  
ANISOU 1884  CA  MET A 247     7242   5107   6739     46     77   -219       C  
ATOM   1885  C   MET A 247     -11.580  11.532  10.695  1.00 50.08           C  
ANISOU 1885  C   MET A 247     7098   5106   6823     15    166   -203       C  
ATOM   1886  O   MET A 247     -11.867  10.349  10.753  1.00 50.07           O  
ANISOU 1886  O   MET A 247     7087   5067   6871     -3    163   -233       O  
ATOM   1887  CB  MET A 247     -10.220  12.060   8.662  1.00 51.02           C  
ANISOU 1887  CB  MET A 247     7470   5217   6699     75    161   -198       C  
ATOM   1888  CG  MET A 247     -10.287  12.230   7.133  1.00 53.92           C  
ANISOU 1888  CG  MET A 247     8004   5538   6945    106     76   -226       C  
ATOM   1889  SD  MET A 247     -11.493  11.089   6.378  1.00 61.41           S  
ANISOU 1889  SD  MET A 247     8990   6408   7936    100    -82   -309       S  
ATOM   1890  CE  MET A 247     -12.557  12.211   5.787  1.00 58.71           C  
ANISOU 1890  CE  MET A 247     8667   6042   7597    118   -242   -327       C  
ATOM   1891  N   ARG A 248     -11.320  12.256  11.797  1.00 50.00           N  
ANISOU 1891  N   ARG A 248     7003   5147   6848      9    241   -159       N  
ATOM   1892  CA  ARG A 248     -11.375  11.649  13.132  1.00 49.86           C  
ANISOU 1892  CA  ARG A 248     6888   5140   6916    -15    324   -141       C  
ATOM   1893  C   ARG A 248     -12.815  11.198  13.407  1.00 50.76           C  
ANISOU 1893  C   ARG A 248     6916   5206   7164    -51    264   -181       C  
ATOM   1894  O   ARG A 248     -13.020  10.082  13.843  1.00 51.37           O  
ANISOU 1894  O   ARG A 248     6969   5250   7300    -74    302   -192       O  
ATOM   1895  CB  ARG A 248     -10.909  12.626  14.218  1.00 49.54           C  
ANISOU 1895  CB  ARG A 248     6786   5157   6879     -9    398    -94       C  
ATOM   1896  CG  ARG A 248     -10.829  11.955  15.573  1.00 50.32           C  
ANISOU 1896  CG  ARG A 248     6822   5263   7036    -23    486    -72       C  
ATOM   1897  CD  ARG A 248     -10.358  12.908  16.630  1.00 51.47           C  
ANISOU 1897  CD  ARG A 248     6923   5460   7173    -12    547    -32       C  
ATOM   1898  NE  ARG A 248     -11.382  13.892  16.979  1.00 52.61           N  
ANISOU 1898  NE  ARG A 248     6997   5608   7386    -26    513    -38       N  
ATOM   1899  CZ  ARG A 248     -11.134  15.065  17.552  1.00 52.08           C  
ANISOU 1899  CZ  ARG A 248     6901   5581   7305    -15    534    -14       C  
ATOM   1900  NH1 ARG A 248      -9.888  15.428  17.825  1.00 52.21           N  
ANISOU 1900  NH1 ARG A 248     6949   5639   7249      8    583     15       N  
ATOM   1901  NH2 ARG A 248     -12.128  15.878  17.861  1.00 50.43           N  
ANISOU 1901  NH2 ARG A 248     6627   5367   7167    -25    506    -24       N  
ATOM   1902  N   ASN A 249     -13.804  12.040  13.063  1.00 50.57           N  
ANISOU 1902  N   ASN A 249     6852   5170   7193    -53    168   -206       N  
ATOM   1903  CA  ASN A 249     -15.217  11.748  13.225  1.00 50.82           C  
ANISOU 1903  CA  ASN A 249     6784   5151   7374    -86    102   -253       C  
ATOM   1904  C   ASN A 249     -15.705  10.661  12.244  1.00 52.20           C  
ANISOU 1904  C   ASN A 249     7001   5258   7573    -98      7   -316       C  
ATOM   1905  O   ASN A 249     -16.500   9.821  12.634  1.00 52.53           O  
ANISOU 1905  O   ASN A 249     6963   5251   7745   -138     10   -350       O  
ATOM   1906  CB  ASN A 249     -16.034  13.034  13.117  1.00 50.53           C  
ANISOU 1906  CB  ASN A 249     6689   5121   7390    -75     20   -265       C  
ATOM   1907  CG  ASN A 249     -15.878  13.909  14.337  1.00 52.43           C  
ANISOU 1907  CG  ASN A 249     6855   5410   7654    -76    120   -217       C  
ATOM   1908  OD1 ASN A 249     -16.159  13.495  15.463  1.00 53.48           O  
ANISOU 1908  OD1 ASN A 249     6906   5541   7872   -105    214   -207       O  
ATOM   1909  ND2 ASN A 249     -15.417  15.138  14.154  1.00 52.33           N  
ANISOU 1909  ND2 ASN A 249     6881   5439   7564    -44    106   -188       N  
ATOM   1910  N   VAL A 250     -15.220  10.659  10.988  1.00 52.81           N  
ANISOU 1910  N   VAL A 250     7211   5326   7527    -64    -70   -332       N  
ATOM   1911  CA  VAL A 250     -15.586   9.640   9.996  1.00 53.59           C  
ANISOU 1911  CA  VAL A 250     7377   5359   7628    -68   -168   -396       C  
ATOM   1912  C   VAL A 250     -14.962   8.269  10.382  1.00 55.03           C  
ANISOU 1912  C   VAL A 250     7579   5525   7806    -89    -63   -389       C  
ATOM   1913  O   VAL A 250     -15.587   7.212  10.208  1.00 55.78           O  
ANISOU 1913  O   VAL A 250     7653   5554   7986   -119   -105   -441       O  
ATOM   1914  CB  VAL A 250     -15.223  10.087   8.546  1.00 53.73           C  
ANISOU 1914  CB  VAL A 250     7557   5366   7492    -19   -272   -413       C  
ATOM   1915  CG1 VAL A 250     -15.363   8.941   7.547  1.00 53.93           C  
ANISOU 1915  CG1 VAL A 250     7680   5324   7488    -17   -356   -477       C  
ATOM   1916  CG2 VAL A 250     -16.059  11.285   8.106  1.00 53.59           C  
ANISOU 1916  CG2 VAL A 250     7524   5342   7494      4   -404   -429       C  
ATOM   1917  N   ARG A 251     -13.754   8.287  10.956  1.00 55.19           N  
ANISOU 1917  N   ARG A 251     7632   5598   7742    -73     71   -327       N  
ATOM   1918  CA  ARG A 251     -13.065   7.074  11.412  1.00 55.39           C  
ANISOU 1918  CA  ARG A 251     7678   5609   7759    -81    172   -314       C  
ATOM   1919  C   ARG A 251     -13.904   6.412  12.525  1.00 56.34           C  
ANISOU 1919  C   ARG A 251     7680   5694   8034   -130    219   -317       C  
ATOM   1920  O   ARG A 251     -14.108   5.196  12.504  1.00 56.81           O  
ANISOU 1920  O   ARG A 251     7747   5693   8144   -154    229   -345       O  
ATOM   1921  CB  ARG A 251     -11.642   7.423  11.906  1.00 55.36           C  
ANISOU 1921  CB  ARG A 251     7711   5671   7653    -47    291   -249       C  
ATOM   1922  CG  ARG A 251     -10.940   6.334  12.693  1.00 56.93           C  
ANISOU 1922  CG  ARG A 251     7908   5862   7860    -47    398   -225       C  
ATOM   1923  CD  ARG A 251     -10.644   5.171  11.806  1.00 58.96           C  
ANISOU 1923  CD  ARG A 251     8260   6066   8078    -38    379   -265       C  
ATOM   1924  NE  ARG A 251      -9.662   4.271  12.393  1.00 61.97           N  
ANISOU 1924  NE  ARG A 251     8663   6446   8439    -19    482   -236       N  
ATOM   1925  CZ  ARG A 251      -9.742   2.945  12.352  1.00 64.19           C  
ANISOU 1925  CZ  ARG A 251     8974   6663   8753    -30    494   -261       C  
ATOM   1926  NH1 ARG A 251     -10.782   2.350  11.775  1.00 63.64           N  
ANISOU 1926  NH1 ARG A 251     8908   6525   8748    -66    412   -319       N  
ATOM   1927  NH2 ARG A 251      -8.785   2.201  12.891  1.00 64.48           N  
ANISOU 1927  NH2 ARG A 251     9035   6698   8767     -2    583   -231       N  
ATOM   1928  N   ILE A 252     -14.418   7.220  13.470  1.00 56.27           N  
ANISOU 1928  N   ILE A 252     7566   5714   8099   -146    254   -290       N  
ATOM   1929  CA  ILE A 252     -15.239   6.709  14.563  1.00 56.58           C  
ANISOU 1929  CA  ILE A 252     7500   5716   8283   -193    320   -289       C  
ATOM   1930  C   ILE A 252     -16.604   6.216  14.056  1.00 57.60           C  
ANISOU 1930  C   ILE A 252     7559   5765   8559   -238    223   -364       C  
ATOM   1931  O   ILE A 252     -17.018   5.109  14.397  1.00 57.60           O  
ANISOU 1931  O   ILE A 252     7530   5700   8654   -279    266   -384       O  
ATOM   1932  CB  ILE A 252     -15.368   7.741  15.702  1.00 56.11           C  
ANISOU 1932  CB  ILE A 252     7361   5706   8252   -193    394   -242       C  
ATOM   1933  CG1 ILE A 252     -13.990   8.098  16.282  1.00 56.47           C  
ANISOU 1933  CG1 ILE A 252     7469   5820   8165   -151    484   -176       C  
ATOM   1934  CG2 ILE A 252     -16.278   7.214  16.776  1.00 56.34           C  
ANISOU 1934  CG2 ILE A 252     7293   5686   8426   -242    477   -243       C  
ATOM   1935  CD1 ILE A 252     -13.949   9.389  17.079  1.00 57.55           C  
ANISOU 1935  CD1 ILE A 252     7556   6017   8295   -138    521   -139       C  
ATOM   1936  N   ALA A 253     -17.262   7.003  13.204  1.00 58.34           N  
ANISOU 1936  N   ALA A 253     7634   5857   8674   -227     86   -409       N  
ATOM   1937  CA  ALA A 253     -18.555   6.657  12.616  1.00 60.18           C  
ANISOU 1937  CA  ALA A 253     7795   6015   9056   -260    -39   -492       C  
ATOM   1938  C   ALA A 253     -18.501   5.349  11.801  1.00 62.77           C  
ANISOU 1938  C   ALA A 253     8198   6274   9376   -274    -95   -545       C  
ATOM   1939  O   ALA A 253     -19.410   4.524  11.894  1.00 63.84           O  
ANISOU 1939  O   ALA A 253     8254   6332   9670   -325   -117   -600       O  
ATOM   1940  CB  ALA A 253     -19.049   7.801  11.741  1.00 60.13           C  
ANISOU 1940  CB  ALA A 253     7790   6023   9036   -226   -196   -526       C  
ATOM   1941  N   SER A 254     -17.411   5.126  11.047  1.00 63.41           N  
ANISOU 1941  N   SER A 254     8433   6380   9282   -230   -105   -530       N  
ATOM   1942  CA  SER A 254     -17.243   3.896  10.275  1.00 63.96           C  
ANISOU 1942  CA  SER A 254     8592   6385   9325   -235   -148   -579       C  
ATOM   1943  C   SER A 254     -17.150   2.641  11.162  1.00 65.01           C  
ANISOU 1943  C   SER A 254     8689   6473   9539   -279    -19   -564       C  
ATOM   1944  O   SER A 254     -17.346   1.524  10.667  1.00 66.40           O  
ANISOU 1944  O   SER A 254     8902   6574   9753   -301    -58   -617       O  
ATOM   1945  CB  SER A 254     -16.029   3.994   9.351  1.00 65.30           C  
ANISOU 1945  CB  SER A 254     8935   6591   9286   -175   -157   -561       C  
ATOM   1946  OG  SER A 254     -14.794   3.824  10.032  1.00 67.72           O  
ANISOU 1946  OG  SER A 254     9280   6949   9503   -155      0   -488       O  
ATOM   1947  N   ARG A 255     -16.832   2.803  12.454  1.00 64.24           N  
ANISOU 1947  N   ARG A 255     8534   6414   9462   -289    131   -492       N  
ATOM   1948  CA  ARG A 255     -16.750   1.669  13.371  1.00 63.82           C  
ANISOU 1948  CA  ARG A 255     8463   6311   9474   -325    259   -468       C  
ATOM   1949  C   ARG A 255     -18.103   1.341  14.028  1.00 64.90           C  
ANISOU 1949  C   ARG A 255     8459   6374   9824   -397    283   -500       C  
ATOM   1950  O   ARG A 255     -18.185   0.355  14.756  1.00 65.23           O  
ANISOU 1950  O   ARG A 255     8491   6356   9936   -435    391   -484       O  
ATOM   1951  CB  ARG A 255     -15.688   1.915  14.450  1.00 63.30           C  
ANISOU 1951  CB  ARG A 255     8428   6311   9312   -292    406   -375       C  
ATOM   1952  CG  ARG A 255     -14.274   1.992  13.901  1.00 64.08           C  
ANISOU 1952  CG  ARG A 255     8652   6465   9231   -228    409   -347       C  
ATOM   1953  CD  ARG A 255     -13.231   1.846  14.981  1.00 64.49           C  
ANISOU 1953  CD  ARG A 255     8731   6556   9216   -198    542   -271       C  
ATOM   1954  NE  ARG A 255     -13.298   2.950  15.932  1.00 66.23           N  
ANISOU 1954  NE  ARG A 255     8883   6838   9442   -194    592   -222       N  
ATOM   1955  CZ  ARG A 255     -13.578   2.818  17.224  1.00 66.73           C  
ANISOU 1955  CZ  ARG A 255     8898   6888   9566   -214    693   -181       C  
ATOM   1956  NH1 ARG A 255     -13.791   1.616  17.744  1.00 64.00           N  
ANISOU 1956  NH1 ARG A 255     8569   6468   9282   -242    763   -176       N  
ATOM   1957  NH2 ARG A 255     -13.604   3.885  18.015  1.00 67.00           N  
ANISOU 1957  NH2 ARG A 255     8884   6980   9592   -205    731   -143       N  
ATOM   1958  N   LEU A 256     -19.157   2.149  13.791  1.00 65.32           N  
ANISOU 1958  N   LEU A 256     8404   6424   9989   -416    190   -546       N  
ATOM   1959  CA  LEU A 256     -20.459   1.903  14.407  1.00 66.32           C  
ANISOU 1959  CA  LEU A 256     8379   6479  10342   -486    222   -584       C  
ATOM   1960  C   LEU A 256     -21.119   0.596  13.941  1.00 67.70           C  
ANISOU 1960  C   LEU A 256     8532   6539  10651   -542    175   -661       C  
ATOM   1961  O   LEU A 256     -21.121   0.264  12.755  1.00 68.44           O  
ANISOU 1961  O   LEU A 256     8685   6605  10714   -528     22   -728       O  
ATOM   1962  CB  LEU A 256     -21.405   3.100  14.228  1.00 66.13           C  
ANISOU 1962  CB  LEU A 256     8235   6475  10417   -485    123   -622       C  
ATOM   1963  CG  LEU A 256     -21.136   4.303  15.125  1.00 67.25           C  
ANISOU 1963  CG  LEU A 256     8344   6701  10506   -457    215   -551       C  
ATOM   1964  CD1 LEU A 256     -21.871   5.513  14.633  1.00 67.91           C  
ANISOU 1964  CD1 LEU A 256     8347   6809  10647   -437     81   -592       C  
ATOM   1965  CD2 LEU A 256     -21.511   4.022  16.553  1.00 67.67           C  
ANISOU 1965  CD2 LEU A 256     8315   6726  10672   -505    402   -510       C  
ATOM   1966  N   GLY A 262     -13.771  -4.636   7.177  1.00 89.41           N  
ANISOU 1966  N   GLY A 262    12505   9213  12253   -197    -23   -778       N  
ATOM   1967  CA  GLY A 262     -14.057  -4.243   5.803  1.00 89.62           C  
ANISOU 1967  CA  GLY A 262    12633   9225  12192   -170   -179   -852       C  
ATOM   1968  C   GLY A 262     -12.965  -3.382   5.201  1.00 89.43           C  
ANISOU 1968  C   GLY A 262    12730   9282  11969    -96   -147   -813       C  
ATOM   1969  O   GLY A 262     -12.170  -2.778   5.937  1.00 89.80           O  
ANISOU 1969  O   GLY A 262    12738   9410  11972    -73    -24   -729       O  
ATOM   1970  N   CYS A 263     -12.908  -3.319   3.853  1.00 88.41           N  
ANISOU 1970  N   CYS A 263    12753   9125  11715    -57   -255   -876       N  
ATOM   1971  CA  CYS A 263     -11.898  -2.503   3.165  1.00 87.87           C  
ANISOU 1971  CA  CYS A 263    12816   9118  11452     11   -214   -843       C  
ATOM   1972  C   CYS A 263     -12.176  -1.002   3.268  1.00 86.39           C  
ANISOU 1972  C   CYS A 263    12576   9004  11242     18   -254   -800       C  
ATOM   1973  O   CYS A 263     -11.242  -0.206   3.275  1.00 86.43           O  
ANISOU 1973  O   CYS A 263    12623   9080  11136     57   -158   -737       O  
ATOM   1974  CB  CYS A 263     -11.709  -2.952   1.716  1.00 88.80           C  
ANISOU 1974  CB  CYS A 263    13138   9174  11429     53   -298   -920       C  
ATOM   1975  SG  CYS A 263     -10.837  -4.537   1.516  1.00 92.64           S  
ANISOU 1975  SG  CYS A 263    13727   9593  11879     73   -194   -950       S  
ATOM   1976  N   SER A 264     -13.454  -0.628   3.377  1.00 85.00           N  
ANISOU 1976  N   SER A 264    12301   8808  11186    -21   -390   -835       N  
ATOM   1977  CA  SER A 264     -13.881   0.751   3.519  1.00 84.26           C  
ANISOU 1977  CA  SER A 264    12146   8772  11098    -16   -443   -802       C  
ATOM   1978  C   SER A 264     -13.317   1.331   4.824  1.00 82.96           C  
ANISOU 1978  C   SER A 264    11854   8692  10974    -27   -280   -705       C  
ATOM   1979  O   SER A 264     -12.801   2.451   4.814  1.00 83.17           O  
ANISOU 1979  O   SER A 264    11902   8788  10911      4   -242   -651       O  
ATOM   1980  CB  SER A 264     -15.404   0.818   3.516  1.00 85.92           C  
ANISOU 1980  CB  SER A 264    12244   8931  11473    -59   -612   -869       C  
ATOM   1981  OG  SER A 264     -15.878   2.140   3.705  1.00 88.82           O  
ANISOU 1981  OG  SER A 264    12543   9348  11858    -50   -669   -841       O  
ATOM   1982  N   GLN A 265     -13.357   0.535   5.925  1.00 81.31           N  
ANISOU 1982  N   GLN A 265    11531   8472  10891    -70   -182   -683       N  
ATOM   1983  CA  GLN A 265     -12.838   0.903   7.245  1.00 80.13           C  
ANISOU 1983  CA  GLN A 265    11275   8391  10781    -78    -34   -596       C  
ATOM   1984  C   GLN A 265     -11.329   1.150   7.227  1.00 77.84           C  
ANISOU 1984  C   GLN A 265    11069   8162  10345    -25     90   -538       C  
ATOM   1985  O   GLN A 265     -10.876   2.126   7.808  1.00 78.09           O  
ANISOU 1985  O   GLN A 265    11051   8267  10351    -11    154   -476       O  
ATOM   1986  CB  GLN A 265     -13.192  -0.165   8.292  1.00 83.03           C  
ANISOU 1986  CB  GLN A 265    11544   8712  11294   -128     39   -591       C  
ATOM   1987  CG  GLN A 265     -14.088   0.359   9.417  1.00 89.37           C  
ANISOU 1987  CG  GLN A 265    12183   9531  12243   -176     60   -562       C  
ATOM   1988  CD  GLN A 265     -13.917  -0.376  10.742  1.00 96.47           C  
ANISOU 1988  CD  GLN A 265    13015  10416  13225   -205    202   -512       C  
ATOM   1989  OE1 GLN A 265     -14.880  -0.940  11.293  1.00 99.05           O  
ANISOU 1989  OE1 GLN A 265    13251  10677  13705   -263    209   -534       O  
ATOM   1990  NE2 GLN A 265     -12.694  -0.382  11.291  1.00 97.04           N  
ANISOU 1990  NE2 GLN A 265    13131  10540  13201   -163    319   -445       N  
ATOM   1991  N   LYS A 266     -10.555   0.287   6.548  1.00 75.75           N  
ANISOU 1991  N   LYS A 266    10926   7862   9993      6    123   -563       N  
ATOM   1992  CA  LYS A 266      -9.111   0.451   6.424  1.00 74.07           C  
ANISOU 1992  CA  LYS A 266    10787   7696   9659     59    244   -520       C  
ATOM   1993  C   LYS A 266      -8.756   1.623   5.505  1.00 72.01           C  
ANISOU 1993  C   LYS A 266    10620   7476   9266     95    219   -513       C  
ATOM   1994  O   LYS A 266      -7.784   2.334   5.766  1.00 72.50           O  
ANISOU 1994  O   LYS A 266    10675   7601   9272    122    322   -458       O  
ATOM   1995  CB  LYS A 266      -8.446  -0.844   5.940  1.00 75.97           C  
ANISOU 1995  CB  LYS A 266    11129   7879   9857     84    291   -555       C  
ATOM   1996  CG  LYS A 266      -8.249  -1.835   7.059  1.00 80.76           C  
ANISOU 1996  CG  LYS A 266    11653   8465  10565     68    375   -529       C  
ATOM   1997  CD  LYS A 266      -7.172  -2.837   6.735  1.00 87.20           C  
ANISOU 1997  CD  LYS A 266    12561   9247  11323    112    459   -542       C  
ATOM   1998  CE  LYS A 266      -6.876  -3.715   7.922  1.00 91.88           C  
ANISOU 1998  CE  LYS A 266    13081   9820  12008    107    542   -505       C  
ATOM   1999  NZ  LYS A 266      -6.416  -2.908   9.086  1.00 94.77           N  
ANISOU 1999  NZ  LYS A 266    13344  10267  12398    116    616   -426       N  
ATOM   2000  N   ALA A 267      -9.561   1.859   4.461  1.00 69.68           N  
ANISOU 2000  N   ALA A 267    10410   7139   8926     96     80   -569       N  
ATOM   2001  CA  ALA A 267      -9.330   2.983   3.563  1.00 68.07           C  
ANISOU 2001  CA  ALA A 267    10316   6959   8588    133     49   -559       C  
ATOM   2002  C   ALA A 267      -9.545   4.295   4.317  1.00 66.35           C  
ANISOU 2002  C   ALA A 267     9982   6812   8418    119     56   -500       C  
ATOM   2003  O   ALA A 267      -8.736   5.207   4.179  1.00 66.54           O  
ANISOU 2003  O   ALA A 267    10047   6883   8352    146    134   -453       O  
ATOM   2004  CB  ALA A 267     -10.261   2.903   2.366  1.00 67.94           C  
ANISOU 2004  CB  ALA A 267    10421   6874   8519    142   -127   -635       C  
ATOM   2005  N   ILE A 268     -10.601   4.370   5.151  1.00 64.50           N  
ANISOU 2005  N   ILE A 268     9598   6578   8331     75    -10   -503       N  
ATOM   2006  CA  ILE A 268     -10.914   5.558   5.942  1.00 63.33           C  
ANISOU 2006  CA  ILE A 268     9332   6490   8241     61     -4   -454       C  
ATOM   2007  C   ILE A 268      -9.794   5.840   6.963  1.00 62.66           C  
ANISOU 2007  C   ILE A 268     9181   6475   8153     66    161   -380       C  
ATOM   2008  O   ILE A 268      -9.401   6.997   7.148  1.00 62.46           O  
ANISOU 2008  O   ILE A 268     9140   6504   8089     79    198   -334       O  
ATOM   2009  CB  ILE A 268     -12.340   5.445   6.561  1.00 63.09           C  
ANISOU 2009  CB  ILE A 268     9159   6432   8381     12   -101   -485       C  
ATOM   2010  CG1 ILE A 268     -13.404   5.724   5.499  1.00 64.08           C  
ANISOU 2010  CG1 ILE A 268     9341   6505   8504     20   -290   -553       C  
ATOM   2011  CG2 ILE A 268     -12.536   6.365   7.759  1.00 63.16           C  
ANISOU 2011  CG2 ILE A 268     9022   6502   8475     -8    -45   -428       C  
ATOM   2012  CD1 ILE A 268     -14.764   5.102   5.793  1.00 65.73           C  
ANISOU 2012  CD1 ILE A 268     9428   6652   8893    -29   -397   -616       C  
ATOM   2013  N   ASN A 269      -9.219   4.773   7.553  1.00 61.80           N  
ANISOU 2013  N   ASN A 269     9046   6357   8080     62    253   -372       N  
ATOM   2014  CA  ASN A 269      -8.117   4.902   8.503  1.00 61.35           C  
ANISOU 2014  CA  ASN A 269     8932   6356   8022     76    391   -312       C  
ATOM   2015  C   ASN A 269      -6.861   5.491   7.824  1.00 61.49           C  
ANISOU 2015  C   ASN A 269     9042   6407   7916    120    467   -292       C  
ATOM   2016  O   ASN A 269      -6.136   6.277   8.434  1.00 61.38           O  
ANISOU 2016  O   ASN A 269     8971   6450   7899    130    544   -244       O  
ATOM   2017  CB  ASN A 269      -7.802   3.559   9.135  1.00 61.76           C  
ANISOU 2017  CB  ASN A 269     8959   6377   8131     72    454   -315       C  
ATOM   2018  CG  ASN A 269      -6.846   3.673  10.287  1.00 64.32           C  
ANISOU 2018  CG  ASN A 269     9211   6752   8474     89    567   -256       C  
ATOM   2019  OD1 ASN A 269      -6.917   4.606  11.107  1.00 65.97           O  
ANISOU 2019  OD1 ASN A 269     9337   7014   8714     80    583   -215       O  
ATOM   2020  ND2 ASN A 269      -5.928   2.727  10.372  1.00 63.72           N  
ANISOU 2020  ND2 ASN A 269     9170   6658   8383    119    640   -256       N  
ATOM   2021  N   CYS A 270      -6.618   5.117   6.554  1.00 61.48           N  
ANISOU 2021  N   CYS A 270     9185   6361   7814    145    448   -333       N  
ATOM   2022  CA  CYS A 270      -5.501   5.631   5.761  1.00 61.11           C  
ANISOU 2022  CA  CYS A 270     9243   6328   7646    184    533   -319       C  
ATOM   2023  C   CYS A 270      -5.700   7.119   5.505  1.00 60.56           C  
ANISOU 2023  C   CYS A 270     9187   6293   7531    182    504   -289       C  
ATOM   2024  O   CYS A 270      -4.760   7.889   5.690  1.00 60.96           O  
ANISOU 2024  O   CYS A 270     9222   6386   7555    195    606   -248       O  
ATOM   2025  CB  CYS A 270      -5.357   4.848   4.459  1.00 61.55           C  
ANISOU 2025  CB  CYS A 270     9470   6319   7600    211    518   -374       C  
ATOM   2026  SG  CYS A 270      -4.739   3.155   4.676  1.00 63.26           S  
ANISOU 2026  SG  CYS A 270     9688   6493   7854    225    591   -405       S  
ATOM   2027  N   LEU A 271      -6.937   7.540   5.151  1.00 59.49           N  
ANISOU 2027  N   LEU A 271     9069   6135   7402    168    361   -312       N  
ATOM   2028  CA  LEU A 271      -7.265   8.958   4.941  1.00 58.82           C  
ANISOU 2028  CA  LEU A 271     8995   6072   7280    170    315   -284       C  
ATOM   2029  C   LEU A 271      -7.047   9.740   6.243  1.00 56.46           C  
ANISOU 2029  C   LEU A 271     8537   5842   7074    149    380   -230       C  
ATOM   2030  O   LEU A 271      -6.508  10.843   6.208  1.00 56.96           O  
ANISOU 2030  O   LEU A 271     8610   5937   7093    158    433   -190       O  
ATOM   2031  CB  LEU A 271      -8.741   9.131   4.519  1.00 59.93           C  
ANISOU 2031  CB  LEU A 271     9149   6173   7449    161    132   -326       C  
ATOM   2032  CG  LEU A 271      -9.123   8.928   3.061  1.00 62.12           C  
ANISOU 2032  CG  LEU A 271     9613   6380   7608    192     20   -380       C  
ATOM   2033  CD1 LEU A 271     -10.591   9.296   2.867  1.00 62.85           C  
ANISOU 2033  CD1 LEU A 271     9678   6442   7762    185   -174   -418       C  
ATOM   2034  CD2 LEU A 271      -8.264   9.790   2.140  1.00 62.63           C  
ANISOU 2034  CD2 LEU A 271     9849   6442   7505    232     90   -350       C  
ATOM   2035  N   TYR A 272      -7.498   9.170   7.377  1.00 53.54           N  
ANISOU 2035  N   TYR A 272     8028   5487   6828    121    375   -229       N  
ATOM   2036  CA  TYR A 272      -7.360   9.721   8.711  1.00 51.11           C  
ANISOU 2036  CA  TYR A 272     7578   5235   6606    103    430   -184       C  
ATOM   2037  C   TYR A 272      -5.861   9.916   9.062  1.00 50.64           C  
ANISOU 2037  C   TYR A 272     7512   5219   6512    124    568   -146       C  
ATOM   2038  O   TYR A 272      -5.497  11.006   9.504  1.00 50.22           O  
ANISOU 2038  O   TYR A 272     7409   5208   6463    123    605   -110       O  
ATOM   2039  CB  TYR A 272      -8.133   8.833   9.723  1.00 49.72           C  
ANISOU 2039  CB  TYR A 272     7293   5046   6551     73    409   -195       C  
ATOM   2040  CG  TYR A 272      -7.863   9.096  11.191  1.00 48.97           C  
ANISOU 2040  CG  TYR A 272     7077   5000   6530     62    483   -150       C  
ATOM   2041  CD1 TYR A 272      -8.026  10.365  11.735  1.00 49.34           C  
ANISOU 2041  CD1 TYR A 272     7060   5091   6595     56    482   -119       C  
ATOM   2042  CD2 TYR A 272      -7.509   8.062  12.049  1.00 49.18           C  
ANISOU 2042  CD2 TYR A 272     7062   5019   6604     60    547   -141       C  
ATOM   2043  CE1 TYR A 272      -7.800  10.606  13.087  1.00 50.17           C  
ANISOU 2043  CE1 TYR A 272     7069   5236   6757     50    543    -84       C  
ATOM   2044  CE2 TYR A 272      -7.259   8.294  13.396  1.00 49.83           C  
ANISOU 2044  CE2 TYR A 272     7057   5140   6737     58    607   -101       C  
ATOM   2045  CZ  TYR A 272      -7.405   9.569  13.916  1.00 50.99           C  
ANISOU 2045  CZ  TYR A 272     7146   5333   6895     53    604    -74       C  
ATOM   2046  OH  TYR A 272      -7.144   9.808  15.251  1.00 51.83           O  
ANISOU 2046  OH  TYR A 272     7181   5474   7039     55    657    -39       O  
ATOM   2047  N   ILE A 273      -4.991   8.899   8.798  1.00 50.35           N  
ANISOU 2047  N   ILE A 273     7522   5163   6447    145    639   -160       N  
ATOM   2048  CA  ILE A 273      -3.536   8.960   9.033  1.00 50.62           C  
ANISOU 2048  CA  ILE A 273     7541   5226   6467    170    765   -137       C  
ATOM   2049  C   ILE A 273      -2.933  10.158   8.303  1.00 51.56           C  
ANISOU 2049  C   ILE A 273     7720   5359   6511    179    813   -120       C  
ATOM   2050  O   ILE A 273      -2.150  10.904   8.893  1.00 51.92           O  
ANISOU 2050  O   ILE A 273     7693   5447   6588    180    884    -89       O  
ATOM   2051  CB  ILE A 273      -2.832   7.634   8.614  1.00 50.95           C  
ANISOU 2051  CB  ILE A 273     7641   5230   6487    197    822   -167       C  
ATOM   2052  CG1 ILE A 273      -3.116   6.491   9.621  1.00 51.85           C  
ANISOU 2052  CG1 ILE A 273     7679   5333   6689    191    807   -170       C  
ATOM   2053  CG2 ILE A 273      -1.313   7.810   8.388  1.00 51.18           C  
ANISOU 2053  CG2 ILE A 273     7681   5276   6491    228    953   -158       C  
ATOM   2054  CD1 ILE A 273      -2.852   5.091   9.064  1.00 52.58           C  
ANISOU 2054  CD1 ILE A 273     7847   5368   6762    212    826   -209       C  
ATOM   2055  N   LEU A 274      -3.313  10.350   7.027  1.00 51.63           N  
ANISOU 2055  N   LEU A 274     7870   5326   6422    187    772   -140       N  
ATOM   2056  CA  LEU A 274      -2.830  11.452   6.199  1.00 51.69           C  
ANISOU 2056  CA  LEU A 274     7970   5330   6341    196    822   -121       C  
ATOM   2057  C   LEU A 274      -3.102  12.852   6.799  1.00 52.48           C  
ANISOU 2057  C   LEU A 274     7992   5470   6479    176    800    -81       C  
ATOM   2058  O   LEU A 274      -2.239  13.735   6.726  1.00 53.85           O  
ANISOU 2058  O   LEU A 274     8168   5659   6635    177    895    -53       O  
ATOM   2059  CB  LEU A 274      -3.436  11.360   4.789  1.00 51.76           C  
ANISOU 2059  CB  LEU A 274     8163   5277   6226    213    750   -151       C  
ATOM   2060  CG  LEU A 274      -3.017  10.182   3.882  1.00 52.51           C  
ANISOU 2060  CG  LEU A 274     8385   5320   6247    239    790   -193       C  
ATOM   2061  CD1 LEU A 274      -3.715  10.273   2.558  1.00 52.65           C  
ANISOU 2061  CD1 LEU A 274     8595   5275   6133    259    695   -223       C  
ATOM   2062  CD2 LEU A 274      -1.533  10.181   3.620  1.00 52.59           C  
ANISOU 2062  CD2 LEU A 274     8424   5333   6227    258    970   -181       C  
ATOM   2063  N   THR A 275      -4.283  13.048   7.406  1.00 51.18           N  
ANISOU 2063  N   THR A 275     7753   5317   6375    157    684    -81       N  
ATOM   2064  CA  THR A 275      -4.704  14.322   7.966  1.00 50.02           C  
ANISOU 2064  CA  THR A 275     7536   5201   6267    142    650    -50       C  
ATOM   2065  C   THR A 275      -4.025  14.732   9.271  1.00 49.70           C  
ANISOU 2065  C   THR A 275     7353   5217   6313    129    725    -21       C  
ATOM   2066  O   THR A 275      -4.014  15.927   9.586  1.00 50.18           O  
ANISOU 2066  O   THR A 275     7378   5300   6388    120    729      6       O  
ATOM   2067  CB  THR A 275      -6.230  14.332   8.149  1.00 50.02           C  
ANISOU 2067  CB  THR A 275     7501   5187   6317    129    505    -70       C  
ATOM   2068  OG1 THR A 275      -6.589  13.437   9.199  1.00 50.26           O  
ANISOU 2068  OG1 THR A 275     7415   5234   6449    111    498    -81       O  
ATOM   2069  CG2 THR A 275      -6.979  14.009   6.866  1.00 49.71           C  
ANISOU 2069  CG2 THR A 275     7602   5088   6199    146    399   -108       C  
ATOM   2070  N   ARG A 276      -3.517  13.767  10.053  1.00 48.78           N  
ANISOU 2070  N   ARG A 276     7161   5118   6254    132    772    -28       N  
ATOM   2071  CA  ARG A 276      -2.918  14.056  11.361  1.00 47.84           C  
ANISOU 2071  CA  ARG A 276     6916   5047   6212    128    821     -5       C  
ATOM   2072  C   ARG A 276      -1.686  14.961  11.293  1.00 47.96           C  
ANISOU 2072  C   ARG A 276     6919   5083   6222    133    915     12       C  
ATOM   2073  O   ARG A 276      -1.765  16.003  11.926  1.00 48.47           O  
ANISOU 2073  O   ARG A 276     6920   5175   6321    119    905     32       O  
ATOM   2074  CB  ARG A 276      -2.635  12.780  12.161  1.00 47.35           C  
ANISOU 2074  CB  ARG A 276     6798   4989   6203    139    841    -15       C  
ATOM   2075  CG  ARG A 276      -3.893  11.958  12.370  1.00 47.11           C  
ANISOU 2075  CG  ARG A 276     6766   4933   6200    125    760    -31       C  
ATOM   2076  CD  ARG A 276      -3.799  11.092  13.588  1.00 47.50           C  
ANISOU 2076  CD  ARG A 276     6742   4990   6314    129    778    -24       C  
ATOM   2077  NE  ARG A 276      -2.749  10.073  13.475  1.00 49.31           N  
ANISOU 2077  NE  ARG A 276     6995   5207   6534    160    840    -35       N  
ATOM   2078  CZ  ARG A 276      -2.949   8.840  13.025  1.00 49.93           C  
ANISOU 2078  CZ  ARG A 276     7127   5239   6604    165    832    -59       C  
ATOM   2079  NH1 ARG A 276      -4.143   8.471  12.589  1.00 47.17           N  
ANISOU 2079  NH1 ARG A 276     6814   4853   6257    139    761    -80       N  
ATOM   2080  NH2 ARG A 276      -1.954   7.969  13.000  1.00 52.23           N  
ANISOU 2080  NH2 ARG A 276     7433   5517   6893    199    891    -68       N  
ATOM   2081  N   PRO A 277      -0.570  14.673  10.554  1.00 47.54           N  
ANISOU 2081  N   PRO A 277     6918   5011   6134    149   1012      3       N  
ATOM   2082  CA  PRO A 277       0.546  15.640  10.522  1.00 47.04           C  
ANISOU 2082  CA  PRO A 277     6824   4959   6088    144   1108     17       C  
ATOM   2083  C   PRO A 277       0.185  16.952   9.812  1.00 47.54           C  
ANISOU 2083  C   PRO A 277     6963   5005   6094    126   1104     39       C  
ATOM   2084  O   PRO A 277       0.815  17.977  10.092  1.00 47.48           O  
ANISOU 2084  O   PRO A 277     6906   5010   6124    111   1160     55       O  
ATOM   2085  CB  PRO A 277       1.684  14.867   9.842  1.00 46.81           C  
ANISOU 2085  CB  PRO A 277     6835   4906   6047    166   1218     -5       C  
ATOM   2086  CG  PRO A 277       1.011  13.876   9.012  1.00 47.45           C  
ANISOU 2086  CG  PRO A 277     7031   4948   6050    180   1176    -25       C  
ATOM   2087  CD  PRO A 277      -0.260  13.490   9.722  1.00 46.64           C  
ANISOU 2087  CD  PRO A 277     6890   4860   5973    170   1047    -25       C  
ATOM   2088  N   LEU A 278      -0.845  16.944   8.934  1.00 47.90           N  
ANISOU 2088  N   LEU A 278     7127   5016   6055    128   1028     38       N  
ATOM   2089  CA  LEU A 278      -1.322  18.161   8.284  1.00 49.03           C  
ANISOU 2089  CA  LEU A 278     7355   5135   6137    120   1000     61       C  
ATOM   2090  C   LEU A 278      -1.885  19.132   9.359  1.00 49.91           C  
ANISOU 2090  C   LEU A 278     7354   5285   6325    101    936     80       C  
ATOM   2091  O   LEU A 278      -1.518  20.310   9.338  1.00 50.63           O  
ANISOU 2091  O   LEU A 278     7445   5373   6419     89    979    103       O  
ATOM   2092  CB  LEU A 278      -2.357  17.868   7.179  1.00 49.21           C  
ANISOU 2092  CB  LEU A 278     7529   5110   6059    137    904     48       C  
ATOM   2093  CG  LEU A 278      -2.914  19.102   6.445  1.00 50.11           C  
ANISOU 2093  CG  LEU A 278     7754   5189   6098    140    856     72       C  
ATOM   2094  CD1 LEU A 278      -1.842  19.785   5.653  1.00 50.02           C  
ANISOU 2094  CD1 LEU A 278     7845   5143   6017    139    995     98       C  
ATOM   2095  CD2 LEU A 278      -4.089  18.723   5.555  1.00 50.79           C  
ANISOU 2095  CD2 LEU A 278     7966   5230   6103    164    718     49       C  
ATOM   2096  N   ALA A 279      -2.687  18.632  10.337  1.00 49.46           N  
ANISOU 2096  N   ALA A 279     7200   5258   6334     99    852     68       N  
ATOM   2097  CA  ALA A 279      -3.173  19.474  11.453  1.00 49.63           C  
ANISOU 2097  CA  ALA A 279     7114   5313   6429     84    808     82       C  
ATOM   2098  C   ALA A 279      -1.996  20.021  12.309  1.00 50.00           C  
ANISOU 2098  C   ALA A 279     7067   5394   6536     76    894     92       C  
ATOM   2099  O   ALA A 279      -2.022  21.168  12.704  1.00 50.64           O  
ANISOU 2099  O   ALA A 279     7113   5485   6644     63    890    107       O  
ATOM   2100  CB  ALA A 279      -4.143  18.694  12.343  1.00 49.10           C  
ANISOU 2100  CB  ALA A 279     6970   5264   6421     83    731     67       C  
ATOM   2101  N   PHE A 280      -0.963  19.219  12.559  1.00 49.81           N  
ANISOU 2101  N   PHE A 280     7004   5383   6539     85    964     79       N  
ATOM   2102  CA  PHE A 280       0.182  19.612  13.377  1.00 50.47           C  
ANISOU 2102  CA  PHE A 280     6988   5494   6694     82   1027     77       C  
ATOM   2103  C   PHE A 280       1.229  20.444  12.653  1.00 52.99           C  
ANISOU 2103  C   PHE A 280     7333   5789   7010     69   1128     83       C  
ATOM   2104  O   PHE A 280       2.192  20.902  13.293  1.00 53.35           O  
ANISOU 2104  O   PHE A 280     7285   5852   7133     62   1177     74       O  
ATOM   2105  CB  PHE A 280       0.821  18.400  14.052  1.00 49.58           C  
ANISOU 2105  CB  PHE A 280     6812   5400   6627    106   1043     57       C  
ATOM   2106  CG  PHE A 280      -0.031  17.939  15.200  1.00 48.62           C  
ANISOU 2106  CG  PHE A 280     6639   5303   6533    113    962     59       C  
ATOM   2107  CD1 PHE A 280      -1.066  17.049  14.996  1.00 48.71           C  
ANISOU 2107  CD1 PHE A 280     6695   5298   6513    115    909     56       C  
ATOM   2108  CD2 PHE A 280       0.115  18.498  16.456  1.00 48.87           C  
ANISOU 2108  CD2 PHE A 280     6583   5366   6618    113    938     61       C  
ATOM   2109  CE1 PHE A 280      -1.901  16.686  16.032  1.00 49.31           C  
ANISOU 2109  CE1 PHE A 280     6728   5388   6621    115    854     60       C  
ATOM   2110  CE2 PHE A 280      -0.703  18.108  17.502  1.00 49.59           C  
ANISOU 2110  CE2 PHE A 280     6646   5472   6724    120    881     66       C  
ATOM   2111  CZ  PHE A 280      -1.704  17.197  17.285  1.00 49.28           C  
ANISOU 2111  CZ  PHE A 280     6649   5414   6661    119    848     67       C  
ATOM   2112  N   LEU A 281       1.036  20.687  11.320  1.00 54.25           N  
ANISOU 2112  N   LEU A 281     7626   5904   7082     65   1161     95       N  
ATOM   2113  CA  LEU A 281       1.878  21.617  10.557  1.00 54.87           C  
ANISOU 2113  CA  LEU A 281     7755   5947   7148     47   1271    108       C  
ATOM   2114  C   LEU A 281       1.721  23.023  11.190  1.00 55.99           C  
ANISOU 2114  C   LEU A 281     7840   6098   7337     22   1247    126       C  
ATOM   2115  O   LEU A 281       2.660  23.812  11.183  1.00 56.85           O  
ANISOU 2115  O   LEU A 281     7914   6191   7497     -1   1338    129       O  
ATOM   2116  CB  LEU A 281       1.497  21.611   9.068  1.00 55.05           C  
ANISOU 2116  CB  LEU A 281     7961   5912   7043     55   1294    123       C  
ATOM   2117  CG  LEU A 281       2.282  22.552   8.102  1.00 56.92           C  
ANISOU 2117  CG  LEU A 281     8294   6094   7240     37   1426    145       C  
ATOM   2118  CD1 LEU A 281       3.809  22.425   8.275  1.00 57.73           C  
ANISOU 2118  CD1 LEU A 281     8302   6195   7436     22   1579    126       C  
ATOM   2119  CD2 LEU A 281       1.893  22.301   6.642  1.00 56.96           C  
ANISOU 2119  CD2 LEU A 281     8508   6038   7096     57   1442    155       C  
ATOM   2120  N   ASN A 282       0.568  23.282  11.830  1.00 56.23           N  
ANISOU 2120  N   ASN A 282     7845   6151   7368     26   1128    133       N  
ATOM   2121  CA  ASN A 282       0.230  24.453  12.611  1.00 56.82           C  
ANISOU 2121  CA  ASN A 282     7859   6240   7492     10   1085    144       C  
ATOM   2122  C   ASN A 282       1.370  24.797  13.610  1.00 56.55           C  
ANISOU 2122  C   ASN A 282     7693   6232   7562     -5   1138    126       C  
ATOM   2123  O   ASN A 282       1.835  25.923  13.641  1.00 56.57           O  
ANISOU 2123  O   ASN A 282     7678   6214   7600    -30   1182    132       O  
ATOM   2124  CB  ASN A 282      -1.105  24.164  13.327  1.00 58.25           C  
ANISOU 2124  CB  ASN A 282     8008   6449   7676     24    961    140       C  
ATOM   2125  CG  ASN A 282      -1.366  24.986  14.543  1.00 62.78           C  
ANISOU 2125  CG  ASN A 282     8485   7050   8317     15    920    139       C  
ATOM   2126  OD1 ASN A 282      -1.471  24.454  15.655  1.00 64.13           O  
ANISOU 2126  OD1 ASN A 282     8572   7260   8536     24    888    122       O  
ATOM   2127  ND2 ASN A 282      -1.445  26.296  14.343  1.00 63.82           N  
ANISOU 2127  ND2 ASN A 282     8644   7157   8449      1    925    155       N  
ATOM   2128  N   SER A 283       1.838  23.822  14.376  1.00 56.36           N  
ANISOU 2128  N   SER A 283     7584   6244   7588     12   1130    100       N  
ATOM   2129  CA  SER A 283       2.892  24.019  15.373  1.00 56.20           C  
ANISOU 2129  CA  SER A 283     7439   6247   7669      9   1153     74       C  
ATOM   2130  C   SER A 283       4.260  24.388  14.780  1.00 55.01           C  
ANISOU 2130  C   SER A 283     7263   6065   7575    -11   1274     61       C  
ATOM   2131  O   SER A 283       5.104  24.948  15.470  1.00 54.46           O  
ANISOU 2131  O   SER A 283     7088   6000   7603    -24   1290     36       O  
ATOM   2132  CB  SER A 283       2.985  22.794  16.277  1.00 58.25           C  
ANISOU 2132  CB  SER A 283     7636   6543   7953     43   1104     52       C  
ATOM   2133  OG  SER A 283       1.708  22.532  16.850  1.00 61.23           O  
ANISOU 2133  OG  SER A 283     8035   6941   8290     54   1013     65       O  
ATOM   2134  N   ALA A 284       4.467  24.107  13.497  1.00 54.64           N  
ANISOU 2134  N   ALA A 284     7314   5978   7470    -15   1361     73       N  
ATOM   2135  CA  ALA A 284       5.707  24.463  12.804  1.00 54.69           C  
ANISOU 2135  CA  ALA A 284     7309   5942   7528    -38   1504     63       C  
ATOM   2136  C   ALA A 284       5.603  25.856  12.148  1.00 54.88           C  
ANISOU 2136  C   ALA A 284     7408   5916   7527    -78   1563     94       C  
ATOM   2137  O   ALA A 284       6.615  26.539  12.009  1.00 55.24           O  
ANISOU 2137  O   ALA A 284     7403   5929   7658   -110   1670     83       O  
ATOM   2138  CB  ALA A 284       6.048  23.410  11.752  1.00 54.27           C  
ANISOU 2138  CB  ALA A 284     7338   5864   7419    -19   1589     59       C  
ATOM   2139  N   VAL A 285       4.385  26.295  11.780  1.00 54.63           N  
ANISOU 2139  N   VAL A 285     7491   5874   7390    -74   1490    130       N  
ATOM   2140  CA  VAL A 285       4.202  27.592  11.131  1.00 54.76           C  
ANISOU 2140  CA  VAL A 285     7601   5836   7371   -102   1534    165       C  
ATOM   2141  C   VAL A 285       3.715  28.711  12.069  1.00 54.58           C  
ANISOU 2141  C   VAL A 285     7511   5827   7399   -117   1450    169       C  
ATOM   2142  O   VAL A 285       3.903  29.857  11.724  1.00 54.61           O  
ANISOU 2142  O   VAL A 285     7556   5782   7413   -147   1506    189       O  
ATOM   2143  CB  VAL A 285       3.311  27.502   9.871  1.00 55.37           C  
ANISOU 2143  CB  VAL A 285     7875   5870   7294    -82   1519    202       C  
ATOM   2144  CG1 VAL A 285       3.896  26.519   8.847  1.00 55.72           C  
ANISOU 2144  CG1 VAL A 285     8006   5887   7278    -69   1622    196       C  
ATOM   2145  CG2 VAL A 285       1.878  27.139  10.233  1.00 55.44           C  
ANISOU 2145  CG2 VAL A 285     7901   5916   7249    -51   1352    205       C  
ATOM   2146  N   ASN A 286       3.143  28.394  13.241  1.00 54.60           N  
ANISOU 2146  N   ASN A 286     7419   5890   7436    -98   1330    149       N  
ATOM   2147  CA  ASN A 286       2.679  29.319  14.301  1.00 54.67           C  
ANISOU 2147  CA  ASN A 286     7357   5919   7497   -105   1248    143       C  
ATOM   2148  C   ASN A 286       3.623  30.439  14.633  1.00 53.59           C  
ANISOU 2148  C   ASN A 286     7150   5753   7458   -144   1312    129       C  
ATOM   2149  O   ASN A 286       3.144  31.522  14.941  1.00 54.05           O  
ANISOU 2149  O   ASN A 286     7217   5796   7525   -157   1273    140       O  
ATOM   2150  CB  ASN A 286       2.484  28.565  15.624  1.00 57.02           C  
ANISOU 2150  CB  ASN A 286     7545   6281   7837    -79   1157    111       C  
ATOM   2151  CG  ASN A 286       1.150  28.043  15.829  1.00 63.49           C  
ANISOU 2151  CG  ASN A 286     8405   7127   8592    -51   1059    123       C  
ATOM   2152  OD1 ASN A 286       0.180  28.497  15.211  1.00 67.77           O  
ANISOU 2152  OD1 ASN A 286     9034   7643   9072    -48   1024    150       O  
ATOM   2153  ND2 ASN A 286       1.066  27.060  16.683  1.00 63.66           N  
ANISOU 2153  ND2 ASN A 286     8365   7193   8631    -27   1012    103       N  
ATOM   2154  N   PRO A 287       4.952  30.214  14.698  1.00 52.34           N  
ANISOU 2154  N   PRO A 287     6904   5588   7393   -163   1402     98       N  
ATOM   2155  CA  PRO A 287       5.856  31.325  15.038  1.00 51.81           C  
ANISOU 2155  CA  PRO A 287     6755   5487   7442   -207   1459     76       C  
ATOM   2156  C   PRO A 287       5.717  32.554  14.139  1.00 51.03           C  
ANISOU 2156  C   PRO A 287     6764   5314   7313   -244   1538    116       C  
ATOM   2157  O   PRO A 287       6.169  33.612  14.523  1.00 51.60           O  
ANISOU 2157  O   PRO A 287     6778   5354   7473   -281   1561    102       O  
ATOM   2158  CB  PRO A 287       7.243  30.679  14.969  1.00 52.39           C  
ANISOU 2158  CB  PRO A 287     6729   5557   7619   -216   1553     35       C  
ATOM   2159  CG  PRO A 287       6.968  29.206  15.215  1.00 52.72           C  
ANISOU 2159  CG  PRO A 287     6763   5657   7612   -165   1487     25       C  
ATOM   2160  CD  PRO A 287       5.703  28.959  14.490  1.00 51.26           C  
ANISOU 2160  CD  PRO A 287     6730   5471   7276   -145   1452     74       C  
ATOM   2161  N   ILE A 288       5.050  32.439  12.983  1.00 50.73           N  
ANISOU 2161  N   ILE A 288     6888   5241   7144   -232   1568    166       N  
ATOM   2162  CA  ILE A 288       4.821  33.568  12.064  1.00 51.36           C  
ANISOU 2162  CA  ILE A 288     7105   5242   7169   -256   1634    213       C  
ATOM   2163  C   ILE A 288       3.979  34.673  12.734  1.00 51.20           C  
ANISOU 2163  C   ILE A 288     7078   5217   7156   -256   1529    222       C  
ATOM   2164  O   ILE A 288       4.147  35.837  12.411  1.00 51.02           O  
ANISOU 2164  O   ILE A 288     7107   5127   7151   -288   1587    245       O  
ATOM   2165  CB  ILE A 288       4.179  33.113  10.708  1.00 51.97           C  
ANISOU 2165  CB  ILE A 288     7379   5283   7085   -227   1656    261       C  
ATOM   2166  CG1 ILE A 288       4.352  34.168   9.616  1.00 52.98           C  
ANISOU 2166  CG1 ILE A 288     7663   5310   7158   -254   1771    310       C  
ATOM   2167  CG2 ILE A 288       2.686  32.743  10.859  1.00 52.22           C  
ANISOU 2167  CG2 ILE A 288     7466   5355   7018   -176   1487    274       C  
ATOM   2168  CD1 ILE A 288       5.720  34.242   9.066  1.00 55.13           C  
ANISOU 2168  CD1 ILE A 288     7927   5527   7494   -299   1970    304       C  
ATOM   2169  N   PHE A 289       3.085  34.305  13.665  1.00 50.78           N  
ANISOU 2169  N   PHE A 289     6968   5232   7093   -220   1384    205       N  
ATOM   2170  CA  PHE A 289       2.240  35.261  14.358  1.00 50.82           C  
ANISOU 2170  CA  PHE A 289     6962   5237   7109   -213   1288    207       C  
ATOM   2171  C   PHE A 289       3.026  36.269  15.199  1.00 50.82           C  
ANISOU 2171  C   PHE A 289     6855   5219   7235   -254   1315    174       C  
ATOM   2172  O   PHE A 289       2.546  37.397  15.397  1.00 51.30           O  
ANISOU 2172  O   PHE A 289     6944   5243   7303   -262   1283    186       O  
ATOM   2173  CB  PHE A 289       1.176  34.545  15.173  1.00 51.00           C  
ANISOU 2173  CB  PHE A 289     6944   5332   7103   -168   1153    192       C  
ATOM   2174  CG  PHE A 289       0.162  33.899  14.260  1.00 52.24           C  
ANISOU 2174  CG  PHE A 289     7219   5484   7144   -131   1108    225       C  
ATOM   2175  CD1 PHE A 289      -0.759  34.674  13.559  1.00 53.32           C  
ANISOU 2175  CD1 PHE A 289     7474   5570   7214   -115   1066    262       C  
ATOM   2176  CD2 PHE A 289       0.143  32.527  14.078  1.00 52.67           C  
ANISOU 2176  CD2 PHE A 289     7272   5580   7162   -110   1099    215       C  
ATOM   2177  CE1 PHE A 289      -1.682  34.085  12.704  1.00 54.11           C  
ANISOU 2177  CE1 PHE A 289     7683   5661   7214    -78   1006    284       C  
ATOM   2178  CE2 PHE A 289      -0.772  31.938  13.216  1.00 53.68           C  
ANISOU 2178  CE2 PHE A 289     7508   5697   7190    -79   1049    238       C  
ATOM   2179  CZ  PHE A 289      -1.678  32.719  12.533  1.00 53.93           C  
ANISOU 2179  CZ  PHE A 289     7653   5680   7159    -62    998    269       C  
ATOM   2180  N   TYR A 290       4.254  35.902  15.630  1.00 49.88           N  
ANISOU 2180  N   TYR A 290     6616   5116   7220   -280   1373    130       N  
ATOM   2181  CA  TYR A 290       5.137  36.810  16.372  1.00 50.14           C  
ANISOU 2181  CA  TYR A 290     6538   5125   7390   -322   1396     87       C  
ATOM   2182  C   TYR A 290       5.429  38.094  15.581  1.00 51.70           C  
ANISOU 2182  C   TYR A 290     6810   5224   7609   -372   1501    118       C  
ATOM   2183  O   TYR A 290       5.744  39.131  16.167  1.00 51.89           O  
ANISOU 2183  O   TYR A 290     6775   5215   7727   -406   1496     92       O  
ATOM   2184  CB  TYR A 290       6.482  36.119  16.659  1.00 49.10           C  
ANISOU 2184  CB  TYR A 290     6274   5011   7372   -339   1452     35       C  
ATOM   2185  CG  TYR A 290       6.500  35.313  17.934  1.00 49.02           C  
ANISOU 2185  CG  TYR A 290     6151   5080   7393   -299   1331    -16       C  
ATOM   2186  CD1 TYR A 290       5.846  34.085  18.019  1.00 48.94           C  
ANISOU 2186  CD1 TYR A 290     6173   5132   7289   -248   1268     -2       C  
ATOM   2187  CD2 TYR A 290       7.157  35.779  19.063  1.00 49.50           C  
ANISOU 2187  CD2 TYR A 290     6085   5149   7574   -311   1275    -78       C  
ATOM   2188  CE1 TYR A 290       5.858  33.343  19.193  1.00 49.19           C  
ANISOU 2188  CE1 TYR A 290     6122   5227   7340   -209   1166    -43       C  
ATOM   2189  CE2 TYR A 290       7.165  35.050  20.249  1.00 49.84           C  
ANISOU 2189  CE2 TYR A 290     6051   5257   7628   -266   1158   -122       C  
ATOM   2190  CZ  TYR A 290       6.518  33.832  20.308  1.00 50.34           C  
ANISOU 2190  CZ  TYR A 290     6158   5378   7591   -215   1110   -101       C  
ATOM   2191  OH  TYR A 290       6.633  33.092  21.457  1.00 51.89           O  
ANISOU 2191  OH  TYR A 290     6290   5629   7798   -171   1009   -141       O  
ATOM   2192  N   PHE A 291       5.385  37.991  14.249  1.00 52.64           N  
ANISOU 2192  N   PHE A 291     7066   5292   7642   -377   1602    172       N  
ATOM   2193  CA  PHE A 291       5.686  39.051  13.307  1.00 54.30           C  
ANISOU 2193  CA  PHE A 291     7385   5398   7850   -421   1728    214       C  
ATOM   2194  C   PHE A 291       4.449  39.818  12.818  1.00 55.66           C  
ANISOU 2194  C   PHE A 291     7720   5528   7900   -392   1664    272       C  
ATOM   2195  O   PHE A 291       4.578  40.681  11.957  1.00 56.87           O  
ANISOU 2195  O   PHE A 291     7998   5587   8024   -418   1761    317       O  
ATOM   2196  CB  PHE A 291       6.482  38.469  12.128  1.00 54.25           C  
ANISOU 2196  CB  PHE A 291     7448   5349   7816   -440   1892    236       C  
ATOM   2197  CG  PHE A 291       7.695  37.716  12.602  1.00 55.01           C  
ANISOU 2197  CG  PHE A 291     7371   5482   8049   -462   1951    173       C  
ATOM   2198  CD1 PHE A 291       8.773  38.383  13.139  1.00 56.06           C  
ANISOU 2198  CD1 PHE A 291     7360   5579   8361   -520   2016    124       C  
ATOM   2199  CD2 PHE A 291       7.708  36.337  12.617  1.00 56.39           C  
ANISOU 2199  CD2 PHE A 291     7515   5726   8184   -420   1918    156       C  
ATOM   2200  CE1 PHE A 291       9.868  37.689  13.622  1.00 57.02           C  
ANISOU 2200  CE1 PHE A 291     7310   5733   8622   -532   2047     58       C  
ATOM   2201  CE2 PHE A 291       8.801  35.644  13.112  1.00 57.34           C  
ANISOU 2201  CE2 PHE A 291     7471   5878   8436   -431   1954     96       C  
ATOM   2202  CZ  PHE A 291       9.884  36.327  13.595  1.00 56.98           C  
ANISOU 2202  CZ  PHE A 291     7283   5796   8571   -484   2017     46       C  
ATOM   2203  N   LEU A 292       3.275  39.555  13.387  1.00 55.43           N  
ANISOU 2203  N   LEU A 292     7689   5561   7810   -338   1506    270       N  
ATOM   2204  CA  LEU A 292       2.053  40.220  12.963  1.00 55.22           C  
ANISOU 2204  CA  LEU A 292     7799   5497   7685   -302   1429    316       C  
ATOM   2205  C   LEU A 292       1.403  41.070  14.044  1.00 55.17           C  
ANISOU 2205  C   LEU A 292     7722   5504   7735   -291   1320    292       C  
ATOM   2206  O   LEU A 292       0.239  41.440  13.871  1.00 55.92           O  
ANISOU 2206  O   LEU A 292     7901   5584   7760   -248   1229    319       O  
ATOM   2207  CB  LEU A 292       1.060  39.181  12.408  1.00 54.99           C  
ANISOU 2207  CB  LEU A 292     7858   5511   7527   -241   1345    339       C  
ATOM   2208  CG  LEU A 292       1.562  38.392  11.202  1.00 55.75           C  
ANISOU 2208  CG  LEU A 292     8061   5581   7539   -243   1447    366       C  
ATOM   2209  CD1 LEU A 292       0.581  37.337  10.805  1.00 56.23           C  
ANISOU 2209  CD1 LEU A 292     8189   5687   7490   -185   1344    374       C  
ATOM   2210  CD2 LEU A 292       1.844  39.291  10.040  1.00 55.92           C  
ANISOU 2210  CD2 LEU A 292     8256   5490   7500   -263   1559    422       C  
ATOM   2211  N   VAL A 293       2.140  41.420  15.132  1.00 54.25           N  
ANISOU 2211  N   VAL A 293     7457   5407   7747   -327   1326    236       N  
ATOM   2212  CA  VAL A 293       1.579  42.214  16.233  1.00 53.72           C  
ANISOU 2212  CA  VAL A 293     7329   5351   7732   -316   1228    205       C  
ATOM   2213  C   VAL A 293       2.150  43.664  16.306  1.00 53.92           C  
ANISOU 2213  C   VAL A 293     7355   5285   7846   -368   1290    200       C  
ATOM   2214  O   VAL A 293       2.129  44.286  17.361  1.00 54.20           O  
ANISOU 2214  O   VAL A 293     7307   5328   7958   -374   1232    154       O  
ATOM   2215  CB  VAL A 293       1.644  41.481  17.599  1.00 53.58           C  
ANISOU 2215  CB  VAL A 293     7162   5428   7766   -298   1143    141       C  
ATOM   2216  CG1 VAL A 293       0.661  40.326  17.635  1.00 53.63           C  
ANISOU 2216  CG1 VAL A 293     7188   5508   7681   -240   1062    152       C  
ATOM   2217  CG2 VAL A 293       3.053  40.989  17.912  1.00 54.07           C  
ANISOU 2217  CG2 VAL A 293     7110   5510   7925   -338   1209     95       C  
ATOM   2218  N   GLY A 294       2.591  44.193  15.173  1.00 53.89           N  
ANISOU 2218  N   GLY A 294     7461   5190   7825   -403   1410    249       N  
ATOM   2219  CA  GLY A 294       3.007  45.586  15.009  1.00 54.69           C  
ANISOU 2219  CA  GLY A 294     7601   5185   7995   -453   1484    260       C  
ATOM   2220  C   GLY A 294       4.175  46.194  15.766  1.00 55.62           C  
ANISOU 2220  C   GLY A 294     7577   5274   8282   -523   1542    198       C  
ATOM   2221  O   GLY A 294       4.393  47.405  15.686  1.00 56.00           O  
ANISOU 2221  O   GLY A 294     7659   5228   8392   -564   1593    205       O  
ATOM   2222  N   ASP A 295       4.962  45.383  16.461  1.00 55.72           N  
ANISOU 2222  N   ASP A 295     7435   5357   8378   -537   1534    135       N  
ATOM   2223  CA  ASP A 295       6.083  45.848  17.279  1.00 55.78           C  
ANISOU 2223  CA  ASP A 295     7288   5344   8560   -596   1558     60       C  
ATOM   2224  C   ASP A 295       7.434  45.896  16.586  1.00 57.34           C  
ANISOU 2224  C   ASP A 295     7444   5474   8870   -670   1731     54       C  
ATOM   2225  O   ASP A 295       8.422  46.286  17.219  1.00 57.94           O  
ANISOU 2225  O   ASP A 295     7376   5524   9113   -723   1752    -16       O  
ATOM   2226  CB  ASP A 295       6.194  44.940  18.505  1.00 55.89           C  
ANISOU 2226  CB  ASP A 295     7158   5470   8609   -561   1435    -12       C  
ATOM   2227  CG  ASP A 295       6.255  43.450  18.198  1.00 56.76           C  
ANISOU 2227  CG  ASP A 295     7255   5660   8650   -524   1437     -1       C  
ATOM   2228  OD1 ASP A 295       6.384  43.089  17.016  1.00 56.42           O  
ANISOU 2228  OD1 ASP A 295     7301   5588   8550   -533   1546     53       O  
ATOM   2229  OD2 ASP A 295       6.185  42.657  19.135  1.00 58.26           O  
ANISOU 2229  OD2 ASP A 295     7358   5936   8842   -485   1333    -46       O  
ATOM   2230  N   HIS A 296       7.505  45.444  15.317  1.00 57.74           N  
ANISOU 2230  N   HIS A 296     7613   5493   8834   -672   1855    119       N  
ATOM   2231  CA  HIS A 296       8.753  45.367  14.558  1.00 58.16           C  
ANISOU 2231  CA  HIS A 296     7637   5478   8982   -738   2046    118       C  
ATOM   2232  C   HIS A 296       9.716  44.371  15.193  1.00 58.78           C  
ANISOU 2232  C   HIS A 296     7520   5630   9182   -745   2034     40       C  
ATOM   2233  O   HIS A 296      10.914  44.628  15.242  1.00 58.76           O  
ANISOU 2233  O   HIS A 296     7394   5575   9355   -811   2140    -10       O  
ATOM   2234  CB  HIS A 296       9.399  46.749  14.355  1.00 58.39           C  
ANISOU 2234  CB  HIS A 296     7672   5377   9139   -821   2169    117       C  
ATOM   2235  CG  HIS A 296       8.650  47.626  13.399  1.00 60.95           C  
ANISOU 2235  CG  HIS A 296     8220   5605   9335   -816   2227    209       C  
ATOM   2236  ND1 HIS A 296       9.021  47.733  12.070  1.00 62.93           N  
ANISOU 2236  ND1 HIS A 296     8620   5759   9530   -847   2420    278       N  
ATOM   2237  CD2 HIS A 296       7.572  48.414  13.613  1.00 62.64           C  
ANISOU 2237  CD2 HIS A 296     8535   5802   9465   -778   2115    241       C  
ATOM   2238  CE1 HIS A 296       8.171  48.587  11.524  1.00 63.67           C  
ANISOU 2238  CE1 HIS A 296     8908   5779   9505   -825   2409    350       C  
ATOM   2239  NE2 HIS A 296       7.288  49.034  12.416  1.00 63.95           N  
ANISOU 2239  NE2 HIS A 296     8913   5858   9528   -783   2226    329       N  
ATOM   2240  N   PHE A 297       9.183  43.235  15.689  1.00 59.37           N  
ANISOU 2240  N   PHE A 297     7566   5821   9173   -675   1903     26       N  
ATOM   2241  CA  PHE A 297       9.977  42.175  16.310  1.00 60.64           C  
ANISOU 2241  CA  PHE A 297     7560   6055   9426   -663   1869    -43       C  
ATOM   2242  C   PHE A 297      10.967  41.568  15.324  1.00 64.65           C  
ANISOU 2242  C   PHE A 297     8055   6526   9984   -696   2048    -35       C  
ATOM   2243  O   PHE A 297      12.080  41.254  15.729  1.00 64.89           O  
ANISOU 2243  O   PHE A 297     7914   6560  10180   -722   2079   -106       O  
ATOM   2244  CB  PHE A 297       9.083  41.077  16.901  1.00 58.80           C  
ANISOU 2244  CB  PHE A 297     7335   5938   9068   -580   1710    -42       C  
ATOM   2245  CG  PHE A 297       9.785  39.888  17.527  1.00 57.08           C  
ANISOU 2245  CG  PHE A 297     6974   5795   8919   -554   1662   -103       C  
ATOM   2246  CD1 PHE A 297      10.641  40.055  18.600  1.00 56.48           C  
ANISOU 2246  CD1 PHE A 297     6726   5729   9004   -570   1595   -190       C  
ATOM   2247  CD2 PHE A 297       9.531  38.601  17.086  1.00 56.64           C  
ANISOU 2247  CD2 PHE A 297     6962   5797   8762   -507   1665    -77       C  
ATOM   2248  CE1 PHE A 297      11.233  38.962  19.210  1.00 56.48           C  
ANISOU 2248  CE1 PHE A 297     6606   5794   9059   -533   1530   -246       C  
ATOM   2249  CE2 PHE A 297      10.115  37.508  17.708  1.00 56.54           C  
ANISOU 2249  CE2 PHE A 297     6827   5849   8806   -475   1609   -131       C  
ATOM   2250  CZ  PHE A 297      10.963  37.695  18.762  1.00 56.24           C  
ANISOU 2250  CZ  PHE A 297     6624   5819   8925   -486   1541   -213       C  
ATOM   2251  N   ARG A 298      10.604  41.444  14.024  1.00 67.40           N  
ANISOU 2251  N   ARG A 298     8582   6829  10196   -692   2169     45       N  
ATOM   2252  CA  ARG A 298      11.526  40.916  13.006  1.00 70.34           C  
ANISOU 2252  CA  ARG A 298     8966   7155  10603   -722   2364     56       C  
ATOM   2253  C   ARG A 298      12.774  41.787  12.920  1.00 72.48           C  
ANISOU 2253  C   ARG A 298     9128   7325  11085   -813   2525     16       C  
ATOM   2254  O   ARG A 298      13.889  41.279  12.858  1.00 72.75           O  
ANISOU 2254  O   ARG A 298     9025   7352  11267   -842   2627    -36       O  
ATOM   2255  CB  ARG A 298      10.856  40.866  11.627  1.00 73.00           C  
ANISOU 2255  CB  ARG A 298     9552   7443  10742   -703   2462    151       C  
ATOM   2256  CG  ARG A 298      11.766  40.295  10.528  1.00 78.46           C  
ANISOU 2256  CG  ARG A 298    10284   8081  11448   -730   2679    164       C  
ATOM   2257  CD  ARG A 298      11.572  40.979   9.184  1.00 84.26           C  
ANISOU 2257  CD  ARG A 298    11256   8698  12060   -754   2847    250       C  
ATOM   2258  NE  ARG A 298      10.160  40.981   8.783  1.00 90.33           N  
ANISOU 2258  NE  ARG A 298    12235   9488  12599   -686   2718    319       N  
ATOM   2259  CZ  ARG A 298       9.615  41.863   7.949  1.00 94.41           C  
ANISOU 2259  CZ  ARG A 298    12969   9910  12992   -688   2771    395       C  
ATOM   2260  NH1 ARG A 298      10.359  42.819   7.403  1.00 94.71           N  
ANISOU 2260  NH1 ARG A 298    13059   9823  13104   -759   2968    419       N  
ATOM   2261  NH2 ARG A 298       8.322  41.797   7.655  1.00 94.86           N  
ANISOU 2261  NH2 ARG A 298    13193   9990  12858   -619   2628    446       N  
ATOM   2262  N   ASP A 299      12.575  43.102  12.958  1.00 73.86           N  
ANISOU 2262  N   ASP A 299     9356   7420  11288   -858   2543     36       N  
ATOM   2263  CA  ASP A 299      13.643  44.082  12.923  1.00 75.67           C  
ANISOU 2263  CA  ASP A 299     9487   7540  11724   -951   2689     -1       C  
ATOM   2264  C   ASP A 299      14.436  43.999  14.242  1.00 77.18           C  
ANISOU 2264  C   ASP A 299     9413   7780  12134   -968   2573   -117       C  
ATOM   2265  O   ASP A 299      15.658  44.036  14.210  1.00 77.33           O  
ANISOU 2265  O   ASP A 299     9275   7746  12361  -1029   2694   -178       O  
ATOM   2266  CB  ASP A 299      13.060  45.498  12.682  1.00 77.28           C  
ANISOU 2266  CB  ASP A 299     9834   7648  11881   -984   2710     54       C  
ATOM   2267  CG  ASP A 299      12.134  45.621  11.466  1.00 80.80           C  
ANISOU 2267  CG  ASP A 299    10562   8047  12091   -950   2778    168       C  
ATOM   2268  OD1 ASP A 299      12.383  46.497  10.625  1.00 81.95           O  
ANISOU 2268  OD1 ASP A 299    10832   8064  12240  -1005   2953    220       O  
ATOM   2269  OD2 ASP A 299      11.136  44.853  11.381  1.00 81.47           O  
ANISOU 2269  OD2 ASP A 299    10745   8219  11990   -867   2649    204       O  
ATOM   2270  N   MET A 300      13.749  43.828  15.382  1.00 78.42           N  
ANISOU 2270  N   MET A 300     9520   8032  12242   -909   2341   -151       N  
ATOM   2271  CA  MET A 300      14.364  43.685  16.701  1.00 80.33           C  
ANISOU 2271  CA  MET A 300     9543   8325  12652   -905   2196   -260       C  
ATOM   2272  C   MET A 300      15.259  42.456  16.773  1.00 82.34           C  
ANISOU 2272  C   MET A 300     9652   8633  13000   -885   2214   -314       C  
ATOM   2273  O   MET A 300      16.308  42.504  17.410  1.00 82.60           O  
ANISOU 2273  O   MET A 300     9484   8651  13249   -915   2194   -409       O  
ATOM   2274  CB  MET A 300      13.288  43.595  17.798  1.00 81.26           C  
ANISOU 2274  CB  MET A 300     9689   8538  12648   -832   1959   -269       C  
ATOM   2275  CG  MET A 300      12.747  44.949  18.248  1.00 83.97           C  
ANISOU 2275  CG  MET A 300    10084   8827  12993   -857   1900   -266       C  
ATOM   2276  SD  MET A 300      11.271  44.873  19.304  1.00 87.97           S  
ANISOU 2276  SD  MET A 300    10668   9432  13324   -767   1664   -258       S  
ATOM   2277  CE  MET A 300      11.799  43.723  20.497  1.00 85.92           C  
ANISOU 2277  CE  MET A 300    10240   9278  13127   -715   1513   -349       C  
ATOM   2278  N   LEU A 301      14.843  41.358  16.119  1.00 83.66           N  
ANISOU 2278  N   LEU A 301     9920   8856  13011   -830   2245   -259       N  
ATOM   2279  CA  LEU A 301      15.551  40.079  16.067  1.00 85.36           C  
ANISOU 2279  CA  LEU A 301    10027   9122  13284   -799   2267   -299       C  
ATOM   2280  C   LEU A 301      16.884  40.221  15.331  1.00 87.78           C  
ANISOU 2280  C   LEU A 301    10229   9334  13789   -873   2491   -332       C  
ATOM   2281  O   LEU A 301      17.897  39.696  15.790  1.00 87.94           O  
ANISOU 2281  O   LEU A 301    10050   9368  13995   -873   2478   -417       O  
ATOM   2282  CB  LEU A 301      14.682  39.019  15.357  1.00 84.95           C  
ANISOU 2282  CB  LEU A 301    10143   9131  13002   -732   2271   -222       C  
ATOM   2283  CG  LEU A 301      14.088  37.911  16.215  1.00 85.44           C  
ANISOU 2283  CG  LEU A 301    10181   9313  12968   -644   2070   -239       C  
ATOM   2284  CD1 LEU A 301      13.257  36.991  15.378  1.00 85.41           C  
ANISOU 2284  CD1 LEU A 301    10346   9349  12759   -593   2095   -165       C  
ATOM   2285  CD2 LEU A 301      15.160  37.115  16.905  1.00 86.28           C  
ANISOU 2285  CD2 LEU A 301    10083   9456  13245   -626   2018   -330       C  
ATOM   2286  N   PHE A 302      16.883  40.944  14.203  1.00 89.47           N  
ANISOU 2286  N   PHE A 302    10579   9447  13970   -933   2696   -265       N  
ATOM   2287  CA  PHE A 302      18.066  41.167  13.368  1.00 91.57           C  
ANISOU 2287  CA  PHE A 302    10778   9605  14410  -1011   2952   -283       C  
ATOM   2288  C   PHE A 302      19.089  42.076  14.040  1.00 93.04           C  
ANISOU 2288  C   PHE A 302    10746   9719  14884  -1091   2968   -376       C  
ATOM   2289  O   PHE A 302      20.283  41.904  13.830  1.00 93.48           O  
ANISOU 2289  O   PHE A 302    10639   9720  15160  -1140   3113   -438       O  
ATOM   2290  CB  PHE A 302      17.666  41.725  11.992  1.00 92.13           C  
ANISOU 2290  CB  PHE A 302    11095   9579  14330  -1046   3164   -175       C  
ATOM   2291  CG  PHE A 302      16.834  40.819  11.104  1.00 93.68           C  
ANISOU 2291  CG  PHE A 302    11511   9822  14262   -976   3184    -90       C  
ATOM   2292  CD1 PHE A 302      16.389  39.586  11.557  1.00 94.80           C  
ANISOU 2292  CD1 PHE A 302    11624  10088  14306   -890   3017   -106       C  
ATOM   2293  CD2 PHE A 302      16.495  41.205   9.817  1.00 95.00           C  
ANISOU 2293  CD2 PHE A 302    11920   9900  14274   -994   3364      4       C  
ATOM   2294  CE1 PHE A 302      15.608  38.766  10.746  1.00 95.82           C  
ANISOU 2294  CE1 PHE A 302    11950  10253  14202   -829   3026    -35       C  
ATOM   2295  CE2 PHE A 302      15.726  40.374   9.001  1.00 95.94           C  
ANISOU 2295  CE2 PHE A 302    12245  10058  14149   -926   3364     74       C  
ATOM   2296  CZ  PHE A 302      15.288  39.162   9.472  1.00 95.73           C  
ANISOU 2296  CZ  PHE A 302    12173  10156  14043   -846   3194     51       C  
ATOM   2297  N   SER A 303      18.631  43.026  14.861  1.00 93.92           N  
ANISOU 2297  N   SER A 303    10850   9829  15007  -1103   2817   -393       N  
ATOM   2298  CA  SER A 303      19.501  43.934  15.612  1.00 95.20           C  
ANISOU 2298  CA  SER A 303    10809   9924  15437  -1175   2794   -491       C  
ATOM   2299  C   SER A 303      20.384  43.142  16.609  1.00 96.61           C  
ANISOU 2299  C   SER A 303    10729  10169  15810  -1142   2652   -614       C  
ATOM   2300  O   SER A 303      21.554  43.485  16.789  1.00 97.20           O  
ANISOU 2300  O   SER A 303    10596  10172  16165  -1208   2720   -705       O  
ATOM   2301  CB  SER A 303      18.665  44.982  16.347  1.00 95.94           C  
ANISOU 2301  CB  SER A 303    10974  10016  15463  -1175   2634   -483       C  
ATOM   2302  OG  SER A 303      19.473  45.871  17.100  1.00 97.72           O  
ANISOU 2302  OG  SER A 303    11015  10171  15943  -1246   2603   -581       O  
ATOM   2303  N   LYS A 304      19.827  42.065  17.218  1.00 96.94           N  
ANISOU 2303  N   LYS A 304    10786  10340  15708  -1040   2458   -616       N  
ATOM   2304  CA  LYS A 304      20.528  41.180  18.157  1.00 97.55           C  
ANISOU 2304  CA  LYS A 304    10655  10484  15924   -987   2300   -720       C  
ATOM   2305  C   LYS A 304      21.294  40.082  17.387  1.00 97.86           C  
ANISOU 2305  C   LYS A 304    10623  10523  16036   -976   2456   -727       C  
ATOM   2306  O   LYS A 304      22.518  39.956  17.485  1.00 97.88           O  
ANISOU 2306  O   LYS A 304    10401  10489  16298  -1000   2488   -825       O  
ATOM   2307  CB  LYS A 304      19.519  40.530  19.126  1.00 99.43           C  
ANISOU 2307  CB  LYS A 304    10971  10850  15958   -882   2042   -707       C  
ATOM   2308  CG  LYS A 304      19.050  41.439  20.259  1.00103.81           C  
ANISOU 2308  CG  LYS A 304    11524  11415  16505   -878   1844   -745       C  
ATOM   2309  CD  LYS A 304      19.743  41.129  21.583  1.00108.61           C  
ANISOU 2309  CD  LYS A 304    11936  12061  17270   -838   1630   -870       C  
ATOM   2310  CE  LYS A 304      19.443  42.182  22.630  1.00112.43           C  
ANISOU 2310  CE  LYS A 304    12416  12529  17771   -848   1464   -919       C  
ATOM   2311  NZ  LYS A 304      20.248  41.987  23.868  1.00114.55           N  
ANISOU 2311  NZ  LYS A 304    12501  12818  18205   -812   1254  -1049       N  
TER    2312      LYS A 304                                                      
ATOM   2313  N   GLU B   9      18.703  59.920  14.838  1.00 85.59           N  
ANISOU 2313  N   GLU B   9     9765   8398  14355  -2024   4599  -1565       N  
ATOM   2314  CA  GLU B   9      19.459  60.785  15.743  1.00 85.68           C  
ANISOU 2314  CA  GLU B   9     9403   8381  14770  -2044   4524  -1703       C  
ATOM   2315  C   GLU B   9      18.710  62.071  16.152  1.00 84.93           C  
ANISOU 2315  C   GLU B   9     9585   8328  14356  -2065   4346  -1467       C  
ATOM   2316  O   GLU B   9      19.024  63.146  15.627  1.00 86.16           O  
ANISOU 2316  O   GLU B   9     9921   8333  14482  -2288   4721  -1501       O  
ATOM   2317  CB  GLU B   9      20.832  61.141  15.126  1.00 88.30           C  
ANISOU 2317  CB  GLU B   9     9487   8497  15564  -2300   5106  -2060       C  
ATOM   2318  N   VAL B  10      17.768  61.989  17.107  1.00 82.88           N  
ANISOU 2318  N   VAL B  10     9357   8243  13892  -1846   3816  -1247       N  
ATOM   2319  CA  VAL B  10      17.063  63.188  17.577  1.00 81.62           C  
ANISOU 2319  CA  VAL B  10     9411   8114  13488  -1854   3642  -1056       C  
ATOM   2320  C   VAL B  10      17.090  63.336  19.109  1.00 79.40           C  
ANISOU 2320  C   VAL B  10     8795   7960  13412  -1677   3171  -1074       C  
ATOM   2321  O   VAL B  10      17.125  62.344  19.839  1.00 79.34           O  
ANISOU 2321  O   VAL B  10     8557   8060  13528  -1479   2848  -1097       O  
ATOM   2322  CB  VAL B  10      15.616  63.351  17.030  1.00 82.87           C  
ANISOU 2322  CB  VAL B  10    10108   8319  13060  -1814   3536   -738       C  
ATOM   2323  CG1 VAL B  10      15.595  63.432  15.503  1.00 83.69           C  
ANISOU 2323  CG1 VAL B  10    10636   8280  12883  -1995   3979   -712       C  
ATOM   2324  CG2 VAL B  10      14.692  62.250  17.540  1.00 83.26           C  
ANISOU 2324  CG2 VAL B  10    10149   8540  12946  -1584   3125   -602       C  
ATOM   2325  N   GLN B  11      17.083  64.598  19.583  1.00 77.24           N  
ANISOU 2325  N   GLN B  11     8537   7655  13157  -1753   3145  -1065       N  
ATOM   2326  CA  GLN B  11      17.025  64.959  21.002  1.00 75.53           C  
ANISOU 2326  CA  GLN B  11     8090   7551  13056  -1617   2722  -1083       C  
ATOM   2327  C   GLN B  11      15.693  65.670  21.229  1.00 72.15           C  
ANISOU 2327  C   GLN B  11     8039   7177  12198  -1576   2548   -801       C  
ATOM   2328  O   GLN B  11      15.313  66.492  20.400  1.00 72.46           O  
ANISOU 2328  O   GLN B  11     8402   7099  12029  -1716   2812   -690       O  
ATOM   2329  CB  GLN B  11      18.157  65.912  21.390  1.00 78.75           C  
ANISOU 2329  CB  GLN B  11     8157   7861  13904  -1758   2854  -1369       C  
ATOM   2330  CG  GLN B  11      19.526  65.514  20.866  1.00 87.08           C  
ANISOU 2330  CG  GLN B  11     8839   8794  15452  -1872   3174  -1701       C  
ATOM   2331  CD  GLN B  11      20.329  64.773  21.902  1.00 94.99           C  
ANISOU 2331  CD  GLN B  11     9320   9885  16887  -1686   2785  -1947       C  
ATOM   2332  OE1 GLN B  11      20.251  63.543  22.016  1.00 97.57           O  
ANISOU 2332  OE1 GLN B  11     9527  10271  17275  -1511   2610  -1951       O  
ATOM   2333  NE2 GLN B  11      21.125  65.508  22.677  1.00 96.14           N  
ANISOU 2333  NE2 GLN B  11     9156  10028  17346  -1710   2624  -2166       N  
ATOM   2334  N   LEU B  12      14.990  65.380  22.343  1.00 68.72           N  
ANISOU 2334  N   LEU B  12     7581   6895  11636  -1385   2119   -693       N  
ATOM   2335  CA  LEU B  12      13.705  66.026  22.625  1.00 65.95           C  
ANISOU 2335  CA  LEU B  12     7532   6584  10941  -1342   1964   -469       C  
ATOM   2336  C   LEU B  12      13.744  66.930  23.843  1.00 63.25           C  
ANISOU 2336  C   LEU B  12     7059   6282  10693  -1322   1746   -534       C  
ATOM   2337  O   LEU B  12      14.404  66.617  24.827  1.00 63.52           O  
ANISOU 2337  O   LEU B  12     6805   6392  10938  -1238   1518   -690       O  
ATOM   2338  CB  LEU B  12      12.589  64.990  22.814  1.00 65.56           C  
ANISOU 2338  CB  LEU B  12     7640   6654  10616  -1170   1723   -283       C  
ATOM   2339  CG  LEU B  12      12.391  63.997  21.673  1.00 66.33           C  
ANISOU 2339  CG  LEU B  12     7877   6731  10596  -1173   1887   -229       C  
ATOM   2340  CD1 LEU B  12      11.404  62.923  22.047  1.00 66.48           C  
ANISOU 2340  CD1 LEU B  12     7970   6854  10434  -1008   1644   -102       C  
ATOM   2341  CD2 LEU B  12      11.987  64.694  20.398  1.00 66.86           C  
ANISOU 2341  CD2 LEU B  12     8280   6686  10439  -1307   2155   -135       C  
ATOM   2342  N   VAL B  13      13.024  68.048  23.785  1.00 60.59           N  
ANISOU 2342  N   VAL B  13     6948   5882  10191  -1387   1795   -424       N  
ATOM   2343  CA  VAL B  13      12.898  68.946  24.923  1.00 59.27           C  
ANISOU 2343  CA  VAL B  13     6697   5744  10077  -1375   1606   -485       C  
ATOM   2344  C   VAL B  13      11.420  69.326  25.049  1.00 57.97           C  
ANISOU 2344  C   VAL B  13     6833   5596   9599  -1303   1490   -265       C  
ATOM   2345  O   VAL B  13      10.868  69.876  24.101  1.00 58.64           O  
ANISOU 2345  O   VAL B  13     7178   5559   9542  -1363   1667   -130       O  
ATOM   2346  CB  VAL B  13      13.770  70.235  24.812  1.00 59.58           C  
ANISOU 2346  CB  VAL B  13     6620   5630  10388  -1568   1845   -666       C  
ATOM   2347  CG1 VAL B  13      13.448  71.201  25.945  1.00 59.89           C  
ANISOU 2347  CG1 VAL B  13     6621   5695  10439  -1556   1647   -722       C  
ATOM   2348  CG2 VAL B  13      15.263  69.919  24.791  1.00 59.97           C  
ANISOU 2348  CG2 VAL B  13     6290   5653  10844  -1647   1957   -955       C  
ATOM   2349  N   GLU B  14      10.785  69.068  26.200  1.00 56.31           N  
ANISOU 2349  N   GLU B  14     6600   5510   9284  -1176   1202   -241       N  
ATOM   2350  CA  GLU B  14       9.398  69.495  26.424  1.00 55.48           C  
ANISOU 2350  CA  GLU B  14     6717   5402   8960  -1120   1118    -91       C  
ATOM   2351  C   GLU B  14       9.404  70.887  27.047  1.00 54.92           C  
ANISOU 2351  C   GLU B  14     6630   5257   8981  -1197   1128   -178       C  
ATOM   2352  O   GLU B  14      10.269  71.207  27.866  1.00 54.66           O  
ANISOU 2352  O   GLU B  14     6393   5257   9119  -1238   1061   -366       O  
ATOM   2353  CB  GLU B  14       8.623  68.564  27.376  1.00 56.78           C  
ANISOU 2353  CB  GLU B  14     6899   5705   8971   -975    882    -38       C  
ATOM   2354  CG  GLU B  14       8.552  67.116  26.952  1.00 60.09           C  
ANISOU 2354  CG  GLU B  14     7328   6186   9318   -889    856     37       C  
ATOM   2355  CD  GLU B  14       9.740  66.279  27.373  1.00 63.56           C  
ANISOU 2355  CD  GLU B  14     7560   6686   9904   -843    768    -77       C  
ATOM   2356  OE1 GLU B  14       9.655  65.043  27.245  1.00 66.59           O  
ANISOU 2356  OE1 GLU B  14     7953   7109  10240   -753    722    -19       O  
ATOM   2357  OE2 GLU B  14      10.745  66.838  27.860  1.00 63.48           O  
ANISOU 2357  OE2 GLU B  14     7364   6673  10083   -887    725   -242       O  
ATOM   2358  N   SER B  15       8.411  71.694  26.688  1.00 54.35           N  
ANISOU 2358  N   SER B  15     6763   5079   8808  -1201   1184    -59       N  
ATOM   2359  CA  SER B  15       8.257  73.027  27.231  1.00 54.49           C  
ANISOU 2359  CA  SER B  15     6791   4996   8916  -1265   1209   -129       C  
ATOM   2360  C   SER B  15       6.760  73.417  27.338  1.00 54.43           C  
ANISOU 2360  C   SER B  15     6962   4943   8775  -1173   1126     -6       C  
ATOM   2361  O   SER B  15       5.895  72.732  26.794  1.00 54.80           O  
ANISOU 2361  O   SER B  15     7127   5018   8678  -1075   1067    131       O  
ATOM   2362  CB  SER B  15       9.078  74.038  26.430  1.00 55.86           C  
ANISOU 2362  CB  SER B  15     6993   4972   9259  -1423   1477   -173       C  
ATOM   2363  OG  SER B  15       8.385  74.564  25.312  1.00 58.27           O  
ANISOU 2363  OG  SER B  15     7597   5100   9443  -1420   1610     21       O  
ATOM   2364  N   GLY B  16       6.466  74.465  28.099  1.00 53.85           N  
ANISOU 2364  N   GLY B  16     6874   4803   8786  -1202   1114    -93       N  
ATOM   2365  CA  GLY B  16       5.103  74.933  28.282  1.00 53.56           C  
ANISOU 2365  CA  GLY B  16     6952   4697   8703  -1119   1052    -28       C  
ATOM   2366  C   GLY B  16       4.487  74.654  29.634  1.00 53.65           C  
ANISOU 2366  C   GLY B  16     6886   4832   8666  -1072    929   -136       C  
ATOM   2367  O   GLY B  16       3.376  75.111  29.901  1.00 53.70           O  
ANISOU 2367  O   GLY B  16     6943   4767   8693  -1020    915   -135       O  
ATOM   2368  N   GLY B  17       5.172  73.889  30.474  1.00 53.93           N  
ANISOU 2368  N   GLY B  17     6820   5035   8637  -1082    843   -232       N  
ATOM   2369  CA  GLY B  17       4.653  73.549  31.794  1.00 55.01           C  
ANISOU 2369  CA  GLY B  17     6966   5278   8658  -1046    748   -321       C  
ATOM   2370  C   GLY B  17       4.430  74.757  32.683  1.00 55.57           C  
ANISOU 2370  C   GLY B  17     7034   5275   8804  -1112    784   -482       C  
ATOM   2371  O   GLY B  17       5.239  75.686  32.675  1.00 56.15           O  
ANISOU 2371  O   GLY B  17     7032   5277   9026  -1204    826   -592       O  
ATOM   2372  N   GLY B  18       3.339  74.754  33.441  1.00 55.17           N  
ANISOU 2372  N   GLY B  18     7058   5225   8680  -1080    801   -521       N  
ATOM   2373  CA  GLY B  18       3.023  75.870  34.316  1.00 55.11           C  
ANISOU 2373  CA  GLY B  18     7056   5138   8744  -1146    863   -697       C  
ATOM   2374  C   GLY B  18       1.923  75.567  35.299  1.00 55.75           C  
ANISOU 2374  C   GLY B  18     7231   5245   8706  -1126    918   -767       C  
ATOM   2375  O   GLY B  18       1.646  74.407  35.571  1.00 56.50           O  
ANISOU 2375  O   GLY B  18     7403   5443   8620  -1077    892   -698       O  
ATOM   2376  N   LEU B  19       1.332  76.607  35.888  1.00 55.92           N  
ANISOU 2376  N   LEU B  19     7255   5154   8837  -1178   1027   -923       N  
ATOM   2377  CA  LEU B  19       0.255  76.505  36.860  1.00 56.42           C  
ANISOU 2377  CA  LEU B  19     7403   5202   8831  -1192   1155  -1041       C  
ATOM   2378  C   LEU B  19      -1.030  76.910  36.184  1.00 58.01           C  
ANISOU 2378  C   LEU B  19     7515   5227   9298  -1130   1264  -1015       C  
ATOM   2379  O   LEU B  19      -1.114  77.956  35.565  1.00 57.88           O  
ANISOU 2379  O   LEU B  19     7418   5050   9522  -1114   1269  -1018       O  
ATOM   2380  CB  LEU B  19       0.519  77.428  38.057  1.00 56.42           C  
ANISOU 2380  CB  LEU B  19     7459   5188   8788  -1299   1210  -1288       C  
ATOM   2381  CG  LEU B  19      -0.564  77.450  39.143  1.00 56.98           C  
ANISOU 2381  CG  LEU B  19     7651   5219   8781  -1347   1410  -1453       C  
ATOM   2382  CD1 LEU B  19      -0.758  76.087  39.753  1.00 57.05           C  
ANISOU 2382  CD1 LEU B  19     7855   5358   8462  -1331   1426  -1386       C  
ATOM   2383  CD2 LEU B  19      -0.224  78.440  40.215  1.00 57.40           C  
ANISOU 2383  CD2 LEU B  19     7770   5252   8787  -1459   1459  -1712       C  
ATOM   2384  N   VAL B  20      -2.033  76.059  36.282  1.00 59.82           N  
ANISOU 2384  N   VAL B  20     7757   5467   9505  -1088   1344   -997       N  
ATOM   2385  CA  VAL B  20      -3.344  76.235  35.663  1.00 60.95           C  
ANISOU 2385  CA  VAL B  20     7770   5455   9935  -1008   1406  -1009       C  
ATOM   2386  C   VAL B  20      -4.411  76.154  36.756  1.00 61.86           C  
ANISOU 2386  C   VAL B  20     7891   5514  10097  -1073   1649  -1225       C  
ATOM   2387  O   VAL B  20      -4.276  75.359  37.683  1.00 62.22           O  
ANISOU 2387  O   VAL B  20     8100   5671   9869  -1152   1758  -1263       O  
ATOM   2388  CB  VAL B  20      -3.544  75.106  34.616  1.00 61.79           C  
ANISOU 2388  CB  VAL B  20     7842   5622  10015   -911   1291   -821       C  
ATOM   2389  CG1 VAL B  20      -4.869  75.238  33.897  1.00 62.32           C  
ANISOU 2389  CG1 VAL B  20     7751   5537  10393   -805   1280   -857       C  
ATOM   2390  CG2 VAL B  20      -2.396  75.055  33.604  1.00 62.61           C  
ANISOU 2390  CG2 VAL B  20     7980   5787  10024   -877   1110   -624       C  
ATOM   2391  N   GLN B  21      -5.436  76.994  36.687  1.00 62.40           N  
ANISOU 2391  N   GLN B  21     7807   5391  10511  -1042   1748  -1376       N  
ATOM   2392  CA  GLN B  21      -6.555  76.900  37.627  1.00 63.74           C  
ANISOU 2392  CA  GLN B  21     7943   5477  10800  -1114   2035  -1617       C  
ATOM   2393  C   GLN B  21      -7.469  75.750  37.081  1.00 64.02           C  
ANISOU 2393  C   GLN B  21     7864   5512  10950  -1052   2060  -1577       C  
ATOM   2394  O   GLN B  21      -7.489  75.518  35.862  1.00 64.32           O  
ANISOU 2394  O   GLN B  21     7789   5549  11099   -919   1821  -1415       O  
ATOM   2395  CB  GLN B  21      -7.299  78.256  37.693  1.00 67.07           C  
ANISOU 2395  CB  GLN B  21     8188   5667  11629  -1088   2123  -1823       C  
ATOM   2396  CG  GLN B  21      -6.908  79.166  38.882  1.00 73.92           C  
ANISOU 2396  CG  GLN B  21     9179   6507  12400  -1231   2305  -2030       C  
ATOM   2397  CD  GLN B  21      -5.421  79.506  38.973  1.00 83.47           C  
ANISOU 2397  CD  GLN B  21    10553   7850  13312  -1281   2131  -1918       C  
ATOM   2398  OE1 GLN B  21      -4.643  78.853  39.695  1.00 86.79           O  
ANISOU 2398  OE1 GLN B  21    11184   8460  13333  -1369   2122  -1897       O  
ATOM   2399  NE2 GLN B  21      -4.981  80.553  38.265  1.00 84.56           N  
ANISOU 2399  NE2 GLN B  21    10602   7870  13655  -1224   1988  -1861       N  
ATOM   2400  N   PRO B  22      -8.195  74.977  37.928  1.00 63.58           N  
ANISOU 2400  N   PRO B  22     7857   5447  10853  -1155   2356  -1726       N  
ATOM   2401  CA  PRO B  22      -9.061  73.910  37.391  1.00 63.29           C  
ANISOU 2401  CA  PRO B  22     7678   5387  10983  -1115   2402  -1726       C  
ATOM   2402  C   PRO B  22     -10.025  74.419  36.327  1.00 63.42           C  
ANISOU 2402  C   PRO B  22     7346   5246  11504   -960   2238  -1808       C  
ATOM   2403  O   PRO B  22     -10.707  75.414  36.540  1.00 64.10           O  
ANISOU 2403  O   PRO B  22     7262   5161  11934   -940   2320  -2016       O  
ATOM   2404  CB  PRO B  22      -9.815  73.407  38.628  1.00 63.86           C  
ANISOU 2404  CB  PRO B  22     7849   5389  11025  -1286   2848  -1952       C  
ATOM   2405  CG  PRO B  22      -8.950  73.757  39.767  1.00 64.42           C  
ANISOU 2405  CG  PRO B  22     8254   5542  10681  -1403   2949  -1952       C  
ATOM   2406  CD  PRO B  22      -8.322  75.072  39.393  1.00 63.13           C  
ANISOU 2406  CD  PRO B  22     8002   5373  10610  -1326   2694  -1926       C  
ATOM   2407  N   GLY B  23     -10.031  73.762  35.181  1.00 62.66           N  
ANISOU 2407  N   GLY B  23     7164   5203  11440   -839   1980  -1648       N  
ATOM   2408  CA  GLY B  23     -10.840  74.158  34.038  1.00 62.70           C  
ANISOU 2408  CA  GLY B  23     6892   5077  11852   -654   1720  -1692       C  
ATOM   2409  C   GLY B  23     -10.067  74.944  32.995  1.00 62.47           C  
ANISOU 2409  C   GLY B  23     6949   5051  11735   -507   1359  -1454       C  
ATOM   2410  O   GLY B  23     -10.557  75.151  31.886  1.00 62.46           O  
ANISOU 2410  O   GLY B  23     6820   4960  11953   -328   1070  -1417       O  
ATOM   2411  N   GLY B  24      -8.860  75.375  33.346  1.00 62.22           N  
ANISOU 2411  N   GLY B  24     7151   5108  11384   -585   1375  -1306       N  
ATOM   2412  CA  GLY B  24      -8.000  76.130  32.460  1.00 62.73           C  
ANISOU 2412  CA  GLY B  24     7331   5152  11351   -495   1125  -1091       C  
ATOM   2413  C   GLY B  24      -7.325  75.300  31.388  1.00 63.65           C  
ANISOU 2413  C   GLY B  24     7564   5403  11217   -441    918   -843       C  
ATOM   2414  O   GLY B  24      -7.353  74.068  31.428  1.00 64.80           O  
ANISOU 2414  O   GLY B  24     7713   5686  11222   -483    964   -823       O  
ATOM   2415  N   SER B  25      -6.691  75.982  30.426  1.00 63.18           N  
ANISOU 2415  N   SER B  25     7626   5281  11097   -358    723   -657       N  
ATOM   2416  CA  SER B  25      -5.999  75.383  29.289  1.00 62.83           C  
ANISOU 2416  CA  SER B  25     7727   5329  10816   -312    553   -429       C  
ATOM   2417  C   SER B  25      -4.517  75.661  29.346  1.00 62.11           C  
ANISOU 2417  C   SER B  25     7815   5314  10471   -424    622   -290       C  
ATOM   2418  O   SER B  25      -4.082  76.615  29.992  1.00 62.51           O  
ANISOU 2418  O   SER B  25     7886   5297  10569   -499    730   -352       O  
ATOM   2419  CB  SER B  25      -6.547  75.947  27.982  1.00 64.73           C  
ANISOU 2419  CB  SER B  25     8011   5398  11187   -119    279   -332       C  
ATOM   2420  OG  SER B  25      -7.850  75.452  27.725  1.00 68.30           O  
ANISOU 2420  OG  SER B  25     8262   5808  11881      5    143   -475       O  
ATOM   2421  N   LEU B  26      -3.735  74.845  28.631  1.00 60.92           N  
ANISOU 2421  N   LEU B  26     7773   5289  10086   -438    566   -131       N  
ATOM   2422  CA  LEU B  26      -2.282  74.968  28.548  1.00 60.15           C  
ANISOU 2422  CA  LEU B  26     7798   5258   9797   -544    635    -27       C  
ATOM   2423  C   LEU B  26      -1.812  74.229  27.290  1.00 58.73           C  
ANISOU 2423  C   LEU B  26     7738   5131   9444   -507    547    145       C  
ATOM   2424  O   LEU B  26      -2.376  73.196  26.949  1.00 58.81           O  
ANISOU 2424  O   LEU B  26     7708   5225   9413   -448    470    151       O  
ATOM   2425  CB  LEU B  26      -1.641  74.341  29.804  1.00 60.42           C  
ANISOU 2425  CB  LEU B  26     7777   5470   9711   -668    760   -125       C  
ATOM   2426  CG  LEU B  26      -0.205  74.691  30.109  1.00 61.71           C  
ANISOU 2426  CG  LEU B  26     7981   5687   9778   -779    816   -119       C  
ATOM   2427  CD1 LEU B  26      -0.093  76.101  30.544  1.00 61.91           C  
ANISOU 2427  CD1 LEU B  26     8002   5569   9953   -831    883   -216       C  
ATOM   2428  CD2 LEU B  26       0.304  73.847  31.228  1.00 62.86           C  
ANISOU 2428  CD2 LEU B  26     8099   6013   9772   -843    845   -201       C  
ATOM   2429  N   ARG B  27      -0.806  74.756  26.597  1.00 57.55           N  
ANISOU 2429  N   ARG B  27     7740   4918   9210   -555    591    262       N  
ATOM   2430  CA  ARG B  27      -0.256  74.088  25.426  1.00 57.27           C  
ANISOU 2430  CA  ARG B  27     7848   4922   8991   -549    568    404       C  
ATOM   2431  C   ARG B  27       1.187  73.713  25.672  1.00 56.42           C  
ANISOU 2431  C   ARG B  27     7711   4927   8800   -693    725    394       C  
ATOM   2432  O   ARG B  27       1.989  74.568  26.021  1.00 56.56           O  
ANISOU 2432  O   ARG B  27     7721   4876   8891   -793    844    352       O  
ATOM   2433  CB  ARG B  27      -0.372  74.926  24.144  1.00 58.95           C  
ANISOU 2433  CB  ARG B  27     8322   4922   9153   -476    508    557       C  
ATOM   2434  CG  ARG B  27      -0.006  74.121  22.910  1.00 62.63           C  
ANISOU 2434  CG  ARG B  27     8977   5432   9389   -465    486    682       C  
ATOM   2435  CD  ARG B  27      -0.058  74.923  21.648  1.00 67.13           C  
ANISOU 2435  CD  ARG B  27     9898   5779   9829   -399    440    851       C  
ATOM   2436  NE  ARG B  27       1.017  75.902  21.627  1.00 72.98           N  
ANISOU 2436  NE  ARG B  27    10773   6371  10587   -541    693    900       N  
ATOM   2437  CZ  ARG B  27       1.241  76.752  20.629  1.00 78.11           C  
ANISOU 2437  CZ  ARG B  27    11789   6776  11115   -535    760   1062       C  
ATOM   2438  NH1 ARG B  27       0.469  76.736  19.544  1.00 78.63           N  
ANISOU 2438  NH1 ARG B  27    12156   6732  10987   -367    540   1205       N  
ATOM   2439  NH2 ARG B  27       2.232  77.633  20.710  1.00 79.07           N  
ANISOU 2439  NH2 ARG B  27    11996   6743  11304   -696   1047   1073       N  
ATOM   2440  N   LEU B  28       1.516  72.435  25.516  1.00 55.95           N  
ANISOU 2440  N   LEU B  28     7606   5025   8626   -700    719    407       N  
ATOM   2441  CA  LEU B  28       2.893  71.977  25.659  1.00 55.84           C  
ANISOU 2441  CA  LEU B  28     7532   5107   8579   -807    836    380       C  
ATOM   2442  C   LEU B  28       3.518  71.796  24.278  1.00 56.08           C  
ANISOU 2442  C   LEU B  28     7724   5077   8507   -840    929    485       C  
ATOM   2443  O   LEU B  28       2.813  71.556  23.297  1.00 55.87           O  
ANISOU 2443  O   LEU B  28     7863   5002   8362   -759    853    584       O  
ATOM   2444  CB  LEU B  28       2.987  70.661  26.429  1.00 55.33           C  
ANISOU 2444  CB  LEU B  28     7327   5226   8468   -789    787    321       C  
ATOM   2445  CG  LEU B  28       2.302  70.583  27.778  1.00 56.02           C  
ANISOU 2445  CG  LEU B  28     7327   5373   8586   -765    734    226       C  
ATOM   2446  CD1 LEU B  28       2.436  69.192  28.354  1.00 56.20           C  
ANISOU 2446  CD1 LEU B  28     7300   5535   8519   -740    707    214       C  
ATOM   2447  CD2 LEU B  28       2.827  71.634  28.745  1.00 56.10           C  
ANISOU 2447  CD2 LEU B  28     7286   5355   8674   -839    769    116       C  
ATOM   2448  N   SER B  29       4.841  71.920  24.206  1.00 56.34           N  
ANISOU 2448  N   SER B  29     7710   5102   8593   -964   1098    438       N  
ATOM   2449  CA  SER B  29       5.596  71.691  22.989  1.00 56.93           C  
ANISOU 2449  CA  SER B  29     7929   5113   8589  -1034   1269    499       C  
ATOM   2450  C   SER B  29       6.654  70.643  23.223  1.00 57.73           C  
ANISOU 2450  C   SER B  29     7822   5352   8760  -1089   1339    394       C  
ATOM   2451  O   SER B  29       7.231  70.555  24.296  1.00 57.42           O  
ANISOU 2451  O   SER B  29     7547   5401   8867  -1110   1292    265       O  
ATOM   2452  CB  SER B  29       6.265  72.965  22.517  1.00 58.22           C  
ANISOU 2452  CB  SER B  29     8235   5066   8821  -1158   1489    514       C  
ATOM   2453  OG  SER B  29       5.250  73.894  22.198  1.00 61.81           O  
ANISOU 2453  OG  SER B  29     8917   5362   9207  -1074   1397    634       O  
ATOM   2454  N   CYS B  30       6.903  69.843  22.206  1.00 58.81           N  
ANISOU 2454  N   CYS B  30     8059   5496   8791  -1100   1432    439       N  
ATOM   2455  CA  CYS B  30       7.938  68.835  22.197  1.00 60.15           C  
ANISOU 2455  CA  CYS B  30     8043   5755   9057  -1145   1526    335       C  
ATOM   2456  C   CYS B  30       8.773  69.244  21.014  1.00 62.24           C  
ANISOU 2456  C   CYS B  30     8467   5867   9316  -1289   1838    333       C  
ATOM   2457  O   CYS B  30       8.297  69.158  19.887  1.00 62.21           O  
ANISOU 2457  O   CYS B  30     8766   5789   9083  -1282   1902    452       O  
ATOM   2458  CB  CYS B  30       7.343  67.441  22.012  1.00 60.19           C  
ANISOU 2458  CB  CYS B  30     8045   5882   8942  -1036   1396    376       C  
ATOM   2459  SG  CYS B  30       8.581  66.130  21.848  1.00 62.18           S  
ANISOU 2459  SG  CYS B  30     8089   6203   9332  -1067   1518    254       S  
ATOM   2460  N   GLU B  31       9.952  69.813  21.261  1.00 64.37           N  
ANISOU 2460  N   GLU B  31     8568   6063   9827  -1428   2040    189       N  
ATOM   2461  CA  GLU B  31      10.807  70.276  20.178  1.00 67.30           C  
ANISOU 2461  CA  GLU B  31     9094   6248  10229  -1605   2425    159       C  
ATOM   2462  C   GLU B  31      11.957  69.331  19.987  1.00 69.86           C  
ANISOU 2462  C   GLU B  31     9165   6620  10758  -1677   2600    -22       C  
ATOM   2463  O   GLU B  31      12.561  68.874  20.954  1.00 69.63           O  
ANISOU 2463  O   GLU B  31     8755   6709  10993  -1635   2458   -188       O  
ATOM   2464  CB  GLU B  31      11.326  71.684  20.445  1.00 71.49           C  
ANISOU 2464  CB  GLU B  31     9613   6604  10946  -1745   2609     90       C  
ATOM   2465  CG  GLU B  31      10.238  72.693  20.784  1.00 78.48           C  
ANISOU 2465  CG  GLU B  31    10699   7421  11698  -1663   2428    241       C  
ATOM   2466  CD  GLU B  31      10.543  73.510  22.026  1.00 84.45           C  
ANISOU 2466  CD  GLU B  31    11177   8189  12720  -1696   2343     87       C  
ATOM   2467  OE1 GLU B  31      11.342  74.469  21.909  1.00 84.57           O  
ANISOU 2467  OE1 GLU B  31    11164   8025  12944  -1869   2616    -24       O  
ATOM   2468  OE2 GLU B  31      10.018  73.168  23.117  1.00 85.15           O  
ANISOU 2468  OE2 GLU B  31    11087   8457  12812  -1565   2029     58       O  
ATOM   2469  N   ALA B  32      12.248  69.022  18.733  1.00 72.34           N  
ANISOU 2469  N   ALA B  32     9709   6831  10946  -1773   2897      2       N  
ATOM   2470  CA  ALA B  32      13.312  68.105  18.397  1.00 75.41           C  
ANISOU 2470  CA  ALA B  32     9871   7234  11548  -1850   3117   -187       C  
ATOM   2471  C   ALA B  32      14.510  68.789  17.750  1.00 78.70           C  
ANISOU 2471  C   ALA B  32    10282   7433  12189  -2100   3618   -353       C  
ATOM   2472  O   ALA B  32      14.372  69.791  17.043  1.00 78.56           O  
ANISOU 2472  O   ALA B  32    10636   7216  11998  -2228   3880   -245       O  
ATOM   2473  CB  ALA B  32      12.782  67.014  17.488  1.00 75.76           C  
ANISOU 2473  CB  ALA B  32    10144   7334  11308  -1785   3116    -91       C  
ATOM   2474  N   SER B  33      15.692  68.212  17.994  1.00 81.16           N  
ANISOU 2474  N   SER B  33    10168   7760  12908  -2164   3759   -628       N  
ATOM   2475  CA  SER B  33      16.971  68.624  17.433  1.00 83.70           C  
ANISOU 2475  CA  SER B  33    10361   7876  13563  -2414   4274   -874       C  
ATOM   2476  C   SER B  33      17.521  67.401  16.703  1.00 86.38           C  
ANISOU 2476  C   SER B  33    10610   8227  13985  -2439   4489  -1008       C  
ATOM   2477  O   SER B  33      17.644  66.339  17.313  1.00 86.91           O  
ANISOU 2477  O   SER B  33    10334   8463  14224  -2268   4187  -1095       O  
ATOM   2478  CB  SER B  33      17.930  69.018  18.550  1.00 85.33           C  
ANISOU 2478  CB  SER B  33    10015   8100  14307  -2443   4181  -1165       C  
ATOM   2479  OG  SER B  33      18.032  70.427  18.664  1.00 88.60           O  
ANISOU 2479  OG  SER B  33    10531   8343  14790  -2602   4370  -1177       O  
ATOM   2480  N   GLY B  34      17.822  67.532  15.413  1.00 87.70           N  
ANISOU 2480  N   GLY B  34    11117   8196  14009  -2646   5012  -1018       N  
ATOM   2481  CA  GLY B  34      18.345  66.408  14.642  1.00 89.26           C  
ANISOU 2481  CA  GLY B  34    11258   8381  14276  -2696   5279  -1169       C  
ATOM   2482  C   GLY B  34      18.226  66.562  13.140  1.00 90.55           C  
ANISOU 2482  C   GLY B  34    12023   8354  14030  -2887   5776  -1071       C  
ATOM   2483  O   GLY B  34      17.443  67.380  12.652  1.00 91.22           O  
ANISOU 2483  O   GLY B  34    12652   8348  13659  -2912   5790   -804       O  
ATOM   2484  N   THR B  36      15.874  65.054  10.773  1.00 92.43           N  
ANISOU 2484  N   THR B  36    13558   8716  12846  -2704   5587   -570       N  
ATOM   2485  CA  THR B  36      14.448  65.148  10.472  1.00 92.52           C  
ANISOU 2485  CA  THR B  36    14042   8816  12296  -2529   5173   -267       C  
ATOM   2486  C   THR B  36      13.568  64.383  11.464  1.00 91.21           C  
ANISOU 2486  C   THR B  36    13531   8919  12207  -2252   4554   -203       C  
ATOM   2487  O   THR B  36      13.968  63.345  11.988  1.00 91.32           O  
ANISOU 2487  O   THR B  36    13093   9055  12551  -2187   4474   -371       O  
ATOM   2488  CB  THR B  36      14.159  64.733   9.016  1.00 94.24           C  
ANISOU 2488  CB  THR B  36    14865   8950  11992  -2608   5409   -219       C  
ATOM   2489  OG1 THR B  36      12.802  65.061   8.690  1.00 95.29           O  
ANISOU 2489  OG1 THR B  36    15481   9130  11596  -2437   4987     61       O  
ATOM   2490  CG2 THR B  36      14.426  63.255   8.760  1.00 94.82           C  
ANISOU 2490  CG2 THR B  36    14700   9144  12184  -2590   5461   -426       C  
ATOM   2491  N   LEU B  37      12.365  64.929  11.712  1.00 89.69           N  
ANISOU 2491  N   LEU B  37    13571   8786  11719  -2092   4136     38       N  
ATOM   2492  CA  LEU B  37      11.304  64.392  12.576  1.00 88.23           C  
ANISOU 2492  CA  LEU B  37    13164   8818  11542  -1849   3584    123       C  
ATOM   2493  C   LEU B  37      10.195  63.698  11.735  1.00 86.79           C  
ANISOU 2493  C   LEU B  37    13338   8707  10930  -1738   3355    216       C  
ATOM   2494  O   LEU B  37       9.400  62.949  12.288  1.00 87.00           O  
ANISOU 2494  O   LEU B  37    13156   8898  11000  -1570   2985    224       O  
ATOM   2495  CB  LEU B  37      10.688  65.538  13.422  1.00 87.84           C  
ANISOU 2495  CB  LEU B  37    13096   8765  11516  -1758   3301    278       C  
ATOM   2496  CG  LEU B  37       9.849  65.139  14.647  1.00 88.76           C  
ANISOU 2496  CG  LEU B  37    12876   9078  11773  -1551   2825    314       C  
ATOM   2497  CD1 LEU B  37      10.699  64.454  15.703  1.00 89.32           C  
ANISOU 2497  CD1 LEU B  37    12415   9252  12272  -1540   2821    139       C  
ATOM   2498  CD2 LEU B  37       9.159  66.333  15.262  1.00 88.93           C  
ANISOU 2498  CD2 LEU B  37    12965   9062  11761  -1479   2600    455       C  
ATOM   2499  N   ALA B  38      10.159  63.938  10.410  1.00 85.00           N  
ANISOU 2499  N   ALA B  38    13661   8344  10291  -1838   3583    267       N  
ATOM   2500  CA  ALA B  38       9.180  63.418   9.465  1.00 83.81           C  
ANISOU 2500  CA  ALA B  38    13919   8237   9686  -1745   3365    329       C  
ATOM   2501  C   ALA B  38       8.804  61.957   9.671  1.00 81.89           C  
ANISOU 2501  C   ALA B  38    13368   8183   9564  -1646   3160    188       C  
ATOM   2502  O   ALA B  38       7.616  61.656   9.748  1.00 82.08           O  
ANISOU 2502  O   ALA B  38    13429   8317   9441  -1475   2731    246       O  
ATOM   2503  CB  ALA B  38       9.655  63.650   8.032  1.00 83.83           C  
ANISOU 2503  CB  ALA B  38    14523   8053   9276  -1922   3780    331       C  
ATOM   2504  N   ASN B  39       9.801  61.062   9.803  1.00 79.76           N  
ANISOU 2504  N   ASN B  39    12767   7929   9607  -1746   3464    -12       N  
ATOM   2505  CA  ASN B  39       9.568  59.629   9.945  1.00 78.00           C  
ANISOU 2505  CA  ASN B  39    12274   7838   9524  -1667   3337   -153       C  
ATOM   2506  C   ASN B  39       9.373  59.148  11.381  1.00 73.81           C  
ANISOU 2506  C   ASN B  39    11202   7438   9405  -1516   3041   -157       C  
ATOM   2507  O   ASN B  39       9.321  57.944  11.594  1.00 73.88           O  
ANISOU 2507  O   ASN B  39    10971   7517   9583  -1457   2983   -269       O  
ATOM   2508  CB  ASN B  39      10.694  58.821   9.251  1.00 80.89           C  
ANISOU 2508  CB  ASN B  39    12600   8125  10010  -1836   3818   -379       C  
ATOM   2509  CG  ASN B  39      12.020  58.821   9.987  1.00 85.93           C  
ANISOU 2509  CG  ASN B  39    12762   8706  11183  -1916   4104   -520       C  
ATOM   2510  OD1 ASN B  39      12.313  57.922  10.804  1.00 87.23           O  
ANISOU 2510  OD1 ASN B  39    12451   8944  11746  -1819   3991   -627       O  
ATOM   2511  ND2 ASN B  39      12.848  59.833   9.705  1.00 87.45           N  
ANISOU 2511  ND2 ASN B  39    13080   8742  11403  -2090   4473   -533       N  
ATOM   2512  N   TYR B  40       9.264  60.055  12.350  1.00 70.53           N  
ANISOU 2512  N   TYR B  40    10629   7035   9133  -1458   2870    -39       N  
ATOM   2513  CA  TYR B  40       9.065  59.671  13.744  1.00 68.09           C  
ANISOU 2513  CA  TYR B  40     9888   6836   9148  -1322   2600    -32       C  
ATOM   2514  C   TYR B  40       7.621  59.755  14.208  1.00 65.08           C  
ANISOU 2514  C   TYR B  40     9554   6547   8628  -1168   2189     92       C  
ATOM   2515  O   TYR B  40       6.864  60.606  13.779  1.00 64.82           O  
ANISOU 2515  O   TYR B  40     9814   6485   8331  -1144   2052    204       O  
ATOM   2516  CB  TYR B  40       9.922  60.525  14.689  1.00 68.20           C  
ANISOU 2516  CB  TYR B  40     9644   6815   9455  -1357   2668    -31       C  
ATOM   2517  CG  TYR B  40      11.388  60.159  14.735  1.00 69.65           C  
ANISOU 2517  CG  TYR B  40     9543   6932   9987  -1460   2989   -223       C  
ATOM   2518  CD1 TYR B  40      12.280  60.660  13.797  1.00 71.54           C  
ANISOU 2518  CD1 TYR B  40     9947   7026  10208  -1655   3419   -316       C  
ATOM   2519  CD2 TYR B  40      11.905  59.414  15.784  1.00 70.64           C  
ANISOU 2519  CD2 TYR B  40     9237   7117  10485  -1358   2861   -317       C  
ATOM   2520  CE1 TYR B  40      13.639  60.372  13.862  1.00 72.96           C  
ANISOU 2520  CE1 TYR B  40     9804   7128  10791  -1758   3733   -541       C  
ATOM   2521  CE2 TYR B  40      13.260  59.100  15.850  1.00 72.19           C  
ANISOU 2521  CE2 TYR B  40     9122   7241  11064  -1423   3105   -523       C  
ATOM   2522  CZ  TYR B  40      14.128  59.578  14.883  1.00 74.04           C  
ANISOU 2522  CZ  TYR B  40     9459   7336  11336  -1629   3550   -656       C  
ATOM   2523  OH  TYR B  40      15.483  59.308  14.934  1.00 76.09           O  
ANISOU 2523  OH  TYR B  40     9357   7504  12048  -1707   3821   -910       O  
ATOM   2524  N   ALA B  41       7.247  58.865  15.101  1.00 63.00           N  
ANISOU 2524  N   ALA B  41     9002   6371   8566  -1060   2003     62       N  
ATOM   2525  CA  ALA B  41       5.961  58.925  15.786  1.00 60.99           C  
ANISOU 2525  CA  ALA B  41     8706   6186   8282   -934   1672    141       C  
ATOM   2526  C   ALA B  41       6.308  59.582  17.117  1.00 59.02           C  
ANISOU 2526  C   ALA B  41     8227   5951   8247   -901   1609    202       C  
ATOM   2527  O   ALA B  41       7.385  59.352  17.682  1.00 58.46           O  
ANISOU 2527  O   ALA B  41     7936   5872   8404   -925   1732    146       O  
ATOM   2528  CB  ALA B  41       5.392  57.533  16.029  1.00 60.47           C  
ANISOU 2528  CB  ALA B  41     8487   6172   8317   -864   1577     60       C  
ATOM   2529  N   ILE B  42       5.428  60.462  17.588  1.00 57.60           N  
ANISOU 2529  N   ILE B  42     8101   5782   8002   -845   1408    294       N  
ATOM   2530  CA  ILE B  42       5.637  61.178  18.838  1.00 55.70           C  
ANISOU 2530  CA  ILE B  42     7686   5555   7924   -822   1341    336       C  
ATOM   2531  C   ILE B  42       4.464  60.922  19.753  1.00 53.06           C  
ANISOU 2531  C   ILE B  42     7258   5273   7628   -720   1119    359       C  
ATOM   2532  O   ILE B  42       3.333  61.142  19.384  1.00 52.67           O  
ANISOU 2532  O   ILE B  42     7321   5217   7474   -675    979    375       O  
ATOM   2533  CB  ILE B  42       5.855  62.691  18.595  1.00 55.95           C  
ANISOU 2533  CB  ILE B  42     7874   5506   7878   -883   1393    404       C  
ATOM   2534  CG1 ILE B  42       6.999  62.954  17.578  1.00 57.14           C  
ANISOU 2534  CG1 ILE B  42     8164   5564   7983  -1020   1696    368       C  
ATOM   2535  CG2 ILE B  42       6.049  63.452  19.920  1.00 56.24           C  
ANISOU 2535  CG2 ILE B  42     7723   5558   8088   -867   1317    414       C  
ATOM   2536  CD1 ILE B  42       8.433  62.780  18.098  1.00 58.75           C  
ANISOU 2536  CD1 ILE B  42     8089   5760   8474  -1098   1895    249       C  
ATOM   2537  N   GLY B  43       4.750  60.432  20.931  1.00 51.56           N  
ANISOU 2537  N   GLY B  43     6873   5120   7596   -682   1094    346       N  
ATOM   2538  CA  GLY B  43       3.745  60.169  21.937  1.00 50.71           C  
ANISOU 2538  CA  GLY B  43     6702   5037   7528   -613    962    360       C  
ATOM   2539  C   GLY B  43       4.008  61.029  23.153  1.00 50.30           C  
ANISOU 2539  C   GLY B  43     6581   4996   7533   -606    910    389       C  
ATOM   2540  O   GLY B  43       5.157  61.337  23.472  1.00 50.16           O  
ANISOU 2540  O   GLY B  43     6487   4985   7586   -631    952    375       O  
ATOM   2541  N   TRP B  44       2.936  61.458  23.814  1.00 49.81           N  
ANISOU 2541  N   TRP B  44     6531   4930   7463   -579    823    398       N  
ATOM   2542  CA  TRP B  44       2.984  62.216  25.045  1.00 49.58           C  
ANISOU 2542  CA  TRP B  44     6465   4909   7465   -577    782    403       C  
ATOM   2543  C   TRP B  44       2.566  61.262  26.146  1.00 49.08           C  
ANISOU 2543  C   TRP B  44     6385   4853   7411   -536    781    399       C  
ATOM   2544  O   TRP B  44       1.604  60.521  26.008  1.00 48.80           O  
ANISOU 2544  O   TRP B  44     6362   4789   7391   -524    812    378       O  
ATOM   2545  CB  TRP B  44       2.038  63.435  24.992  1.00 49.78           C  
ANISOU 2545  CB  TRP B  44     6537   4890   7486   -583    727    398       C  
ATOM   2546  CG  TRP B  44       2.613  64.639  24.290  1.00 50.10           C  
ANISOU 2546  CG  TRP B  44     6646   4885   7506   -625    743    429       C  
ATOM   2547  CD1 TRP B  44       2.420  64.998  22.990  1.00 51.04           C  
ANISOU 2547  CD1 TRP B  44     6904   4945   7545   -627    739    469       C  
ATOM   2548  CD2 TRP B  44       3.462  65.645  24.862  1.00 49.79           C  
ANISOU 2548  CD2 TRP B  44     6571   4828   7517   -678    778    416       C  
ATOM   2549  NE1 TRP B  44       3.084  66.170  22.719  1.00 51.33           N  
ANISOU 2549  NE1 TRP B  44     7021   4907   7574   -685    806    504       N  
ATOM   2550  CE2 TRP B  44       3.731  66.590  23.853  1.00 50.88           C  
ANISOU 2550  CE2 TRP B  44     6829   4875   7626   -724    838    457       C  
ATOM   2551  CE3 TRP B  44       3.996  65.857  26.138  1.00 49.84           C  
ANISOU 2551  CE3 TRP B  44     6479   4877   7579   -692    757    362       C  
ATOM   2552  CZ2 TRP B  44       4.519  67.720  24.079  1.00 51.31           C  
ANISOU 2552  CZ2 TRP B  44     6874   4867   7754   -801    918    436       C  
ATOM   2553  CZ3 TRP B  44       4.783  66.968  26.355  1.00 50.60           C  
ANISOU 2553  CZ3 TRP B  44     6542   4937   7747   -758    791    318       C  
ATOM   2554  CH2 TRP B  44       5.048  67.878  25.333  1.00 51.01           C  
ANISOU 2554  CH2 TRP B  44     6679   4887   7816   -821    890    349       C  
ATOM   2555  N   PHE B  45       3.342  61.239  27.206  1.00 49.19           N  
ANISOU 2555  N   PHE B  45     6387   4890   7414   -515    748    411       N  
ATOM   2556  CA  PHE B  45       3.159  60.420  28.398  1.00 49.56           C  
ANISOU 2556  CA  PHE B  45     6504   4920   7406   -468    743    436       C  
ATOM   2557  C   PHE B  45       3.207  61.348  29.622  1.00 49.45           C  
ANISOU 2557  C   PHE B  45     6545   4924   7319   -478    684    416       C  
ATOM   2558  O   PHE B  45       3.678  62.468  29.520  1.00 49.08           O  
ANISOU 2558  O   PHE B  45     6435   4908   7307   -513    635    374       O  
ATOM   2559  CB  PHE B  45       4.288  59.371  28.480  1.00 49.83           C  
ANISOU 2559  CB  PHE B  45     6514   4952   7465   -394    697    469       C  
ATOM   2560  CG  PHE B  45       4.277  58.435  27.299  1.00 50.80           C  
ANISOU 2560  CG  PHE B  45     6587   5048   7666   -395    782    464       C  
ATOM   2561  CD1 PHE B  45       4.911  58.782  26.107  1.00 52.17           C  
ANISOU 2561  CD1 PHE B  45     6670   5246   7905   -438    817    421       C  
ATOM   2562  CD2 PHE B  45       3.621  57.219  27.368  1.00 51.32           C  
ANISOU 2562  CD2 PHE B  45     6720   5045   7734   -369    861    488       C  
ATOM   2563  CE1 PHE B  45       4.836  57.950  24.991  1.00 53.00           C  
ANISOU 2563  CE1 PHE B  45     6765   5327   8046   -452    910    395       C  
ATOM   2564  CE2 PHE B  45       3.556  56.381  26.265  1.00 52.24           C  
ANISOU 2564  CE2 PHE B  45     6789   5135   7926   -381    942    453       C  
ATOM   2565  CZ  PHE B  45       4.150  56.753  25.079  1.00 52.76           C  
ANISOU 2565  CZ  PHE B  45     6777   5245   8027   -420    956    403       C  
ATOM   2566  N   ARG B  46       2.699  60.898  30.760  1.00 49.75           N  
ANISOU 2566  N   ARG B  46     6728   4927   7248   -461    718    434       N  
ATOM   2567  CA  ARG B  46       2.715  61.691  31.986  1.00 50.62           C  
ANISOU 2567  CA  ARG B  46     6940   5051   7241   -477    675    398       C  
ATOM   2568  C   ARG B  46       2.912  60.801  33.194  1.00 53.44           C  
ANISOU 2568  C   ARG B  46     7524   5371   7409   -412    648    460       C  
ATOM   2569  O   ARG B  46       2.536  59.627  33.182  1.00 53.73           O  
ANISOU 2569  O   ARG B  46     7662   5331   7421   -383    746    532       O  
ATOM   2570  CB  ARG B  46       1.447  62.567  32.134  1.00 49.47           C  
ANISOU 2570  CB  ARG B  46     6797   4865   7134   -560    807    322       C  
ATOM   2571  CG  ARG B  46       0.189  61.791  32.442  1.00 49.87           C  
ANISOU 2571  CG  ARG B  46     6938   4823   7185   -593   1002    309       C  
ATOM   2572  CD  ARG B  46      -0.999  62.693  32.478  1.00 52.36           C  
ANISOU 2572  CD  ARG B  46     7182   5089   7624   -663   1117    189       C  
ATOM   2573  NE  ARG B  46      -2.258  61.969  32.647  1.00 54.48           N  
ANISOU 2573  NE  ARG B  46     7464   5251   7984   -713   1334    122       N  
ATOM   2574  CZ  ARG B  46      -3.458  62.546  32.655  1.00 56.39           C  
ANISOU 2574  CZ  ARG B  46     7592   5420   8413   -769   1458    -25       C  
ATOM   2575  NH1 ARG B  46      -3.573  63.857  32.487  1.00 56.72           N  
ANISOU 2575  NH1 ARG B  46     7525   5477   8549   -765   1368    -92       N  
ATOM   2576  NH2 ARG B  46      -4.552  61.814  32.827  1.00 55.70           N  
ANISOU 2576  NH2 ARG B  46     7483   5222   8460   -829   1682   -124       N  
ATOM   2577  N   GLN B  47       3.529  61.346  34.235  1.00 55.60           N  
ANISOU 2577  N   GLN B  47     7902   5686   7538   -385    506    431       N  
ATOM   2578  CA  GLN B  47       3.711  60.606  35.475  1.00 57.96           C  
ANISOU 2578  CA  GLN B  47     8503   5937   7583   -307    441    501       C  
ATOM   2579  C   GLN B  47       3.390  61.491  36.666  1.00 59.94           C  
ANISOU 2579  C   GLN B  47     8950   6199   7627   -364    453    424       C  
ATOM   2580  O   GLN B  47       4.005  62.541  36.852  1.00 59.73           O  
ANISOU 2580  O   GLN B  47     8814   6257   7622   -378    295    316       O  
ATOM   2581  CB  GLN B  47       5.099  59.973  35.571  1.00 60.16           C  
ANISOU 2581  CB  GLN B  47     8758   6244   7857   -152    156    547       C  
ATOM   2582  CG  GLN B  47       5.284  59.130  36.826  1.00 65.30           C  
ANISOU 2582  CG  GLN B  47     9785   6815   8210    -30     38    651       C  
ATOM   2583  CD  GLN B  47       6.400  58.131  36.646  1.00 73.18           C  
ANISOU 2583  CD  GLN B  47    10734   7784   9288    153   -206    723       C  
ATOM   2584  OE1 GLN B  47       7.470  58.426  36.086  1.00 75.92           O  
ANISOU 2584  OE1 GLN B  47    10767   8213   9868    207   -407    628       O  
ATOM   2585  NE2 GLN B  47       6.169  56.912  37.097  1.00 74.94           N  
ANISOU 2585  NE2 GLN B  47    11260   7863   9353    247   -165    879       N  
ATOM   2586  N   ALA B  48       2.354  61.102  37.412  1.00 61.79           N  
ANISOU 2586  N   ALA B  48     9463   6328   7687   -424    690    452       N  
ATOM   2587  CA  ALA B  48       1.899  61.785  38.624  1.00 64.20           C  
ANISOU 2587  CA  ALA B  48    10026   6612   7756   -498    782    370       C  
ATOM   2588  C   ALA B  48       2.689  61.220  39.819  1.00 67.03           C  
ANISOU 2588  C   ALA B  48    10775   6955   7738   -378    568    455       C  
ATOM   2589  O   ALA B  48       3.189  60.093  39.741  1.00 66.98           O  
ANISOU 2589  O   ALA B  48    10878   6896   7674   -249    450    602       O  
ATOM   2590  CB  ALA B  48       0.406  61.543  38.819  1.00 64.26           C  
ANISOU 2590  CB  ALA B  48    10152   6482   7782   -632   1192    338       C  
ATOM   2591  N   PRO B  49       2.874  61.992  40.913  1.00 69.39           N  
ANISOU 2591  N   PRO B  49    11296   7293   7775   -400    477    359       N  
ATOM   2592  CA  PRO B  49       3.660  61.463  42.048  1.00 70.59           C  
ANISOU 2592  CA  PRO B  49    11866   7431   7524   -257    201    438       C  
ATOM   2593  C   PRO B  49       3.069  60.184  42.654  1.00 71.37           C  
ANISOU 2593  C   PRO B  49    12447   7341   7331   -230    419    627       C  
ATOM   2594  O   PRO B  49       1.884  60.140  43.012  1.00 71.46           O  
ANISOU 2594  O   PRO B  49    12668   7230   7256   -391    850    610       O  
ATOM   2595  CB  PRO B  49       3.691  62.631  43.048  1.00 71.35           C  
ANISOU 2595  CB  PRO B  49    12125   7594   7391   -333    144    259       C  
ATOM   2596  CG  PRO B  49       2.543  63.518  42.665  1.00 71.46           C  
ANISOU 2596  CG  PRO B  49    11927   7585   7639   -539    539    124       C  
ATOM   2597  CD  PRO B  49       2.399  63.369  41.174  1.00 69.52           C  
ANISOU 2597  CD  PRO B  49    11215   7357   7843   -543    597    165       C  
ATOM   2598  N   GLY B  50       3.899  59.141  42.693  1.00 71.38           N  
ANISOU 2598  N   GLY B  50    12588   7295   7236    -31    142    793       N  
ATOM   2599  CA  GLY B  50       3.536  57.833  43.230  1.00 71.58           C  
ANISOU 2599  CA  GLY B  50    13103   7107   6987     30    303   1006       C  
ATOM   2600  C   GLY B  50       2.808  56.902  42.281  1.00 71.40           C  
ANISOU 2600  C   GLY B  50    12910   6956   7262    -36    646   1096       C  
ATOM   2601  O   GLY B  50       2.516  55.757  42.640  1.00 72.12           O  
ANISOU 2601  O   GLY B  50    13384   6839   7179      5    813   1272       O  
ATOM   2602  N   LYS B  51       2.506  57.382  41.072  1.00 70.51           N  
ANISOU 2602  N   LYS B  51    12254   6949   7588   -138    753    973       N  
ATOM   2603  CA  LYS B  51       1.797  56.626  40.049  1.00 70.23           C  
ANISOU 2603  CA  LYS B  51    11998   6822   7865   -209   1040   1003       C  
ATOM   2604  C   LYS B  51       2.723  56.175  38.909  1.00 69.64           C  
ANISOU 2604  C   LYS B  51    11550   6825   8085    -74    772   1040       C  
ATOM   2605  O   LYS B  51       3.811  56.714  38.725  1.00 69.30           O  
ANISOU 2605  O   LYS B  51    11297   6929   8105     33    414    991       O  
ATOM   2606  CB  LYS B  51       0.668  57.480  39.458  1.00 72.25           C  
ANISOU 2606  CB  LYS B  51    11939   7121   8391   -416   1349    820       C  
ATOM   2607  CG  LYS B  51      -0.470  57.751  40.405  1.00 76.95           C  
ANISOU 2607  CG  LYS B  51    12831   7594   8811   -584   1734    742       C  
ATOM   2608  CD  LYS B  51      -1.625  58.374  39.645  1.00 82.59           C  
ANISOU 2608  CD  LYS B  51    13160   8315   9904   -753   2018    550       C  
ATOM   2609  CE  LYS B  51      -2.824  58.593  40.543  1.00 88.33           C  
ANISOU 2609  CE  LYS B  51    14123   8890  10548   -937   2466    426       C  
ATOM   2610  NZ  LYS B  51      -3.934  57.630  40.267  1.00 91.61           N  
ANISOU 2610  NZ  LYS B  51    14521   9104  11183  -1058   2890    387       N  
ATOM   2611  N   GLU B  52       2.273  55.183  38.138  1.00 69.27           N  
ANISOU 2611  N   GLU B  52    11411   6665   8243    -96    979   1095       N  
ATOM   2612  CA  GLU B  52       3.007  54.705  36.981  1.00 68.86           C  
ANISOU 2612  CA  GLU B  52    11015   6667   8482     -1    810   1103       C  
ATOM   2613  C   GLU B  52       2.830  55.692  35.801  1.00 66.56           C  
ANISOU 2613  C   GLU B  52    10258   6546   8485   -112    826    937       C  
ATOM   2614  O   GLU B  52       1.887  56.489  35.765  1.00 66.46           O  
ANISOU 2614  O   GLU B  52    10179   6564   8508   -259   1015    832       O  
ATOM   2615  CB  GLU B  52       2.518  53.305  36.561  1.00 73.51           C  
ANISOU 2615  CB  GLU B  52    11685   7063   9183     -2   1049   1194       C  
ATOM   2616  CG  GLU B  52       2.308  52.314  37.695  1.00 84.90           C  
ANISOU 2616  CG  GLU B  52    13662   8265  10331     55   1177   1371       C  
ATOM   2617  CD  GLU B  52       3.491  52.042  38.608  1.00 97.64           C  
ANISOU 2617  CD  GLU B  52    15596   9845  11658    292    790   1521       C  
ATOM   2618  OE1 GLU B  52       4.650  52.095  38.128  1.00100.80           O  
ANISOU 2618  OE1 GLU B  52    15725  10360  12214    456    414   1499       O  
ATOM   2619  OE2 GLU B  52       3.252  51.754  39.805  1.00100.42           O  
ANISOU 2619  OE2 GLU B  52    16484  10040  11634    316    866   1650       O  
ATOM   2620  N   ARG B  53       3.746  55.626  34.843  1.00 64.39           N  
ANISOU 2620  N   ARG B  53     9684   6357   8422    -35    635    913       N  
ATOM   2621  CA  ARG B  53       3.688  56.451  33.657  1.00 62.93           C  
ANISOU 2621  CA  ARG B  53     9139   6300   8472   -127    654    789       C  
ATOM   2622  C   ARG B  53       2.525  55.991  32.792  1.00 61.38           C  
ANISOU 2622  C   ARG B  53     8857   6040   8425   -236    925    753       C  
ATOM   2623  O   ARG B  53       2.296  54.788  32.643  1.00 61.54           O  
ANISOU 2623  O   ARG B  53     8962   5936   8485   -212   1045    811       O  
ATOM   2624  CB  ARG B  53       4.990  56.300  32.871  1.00 64.06           C  
ANISOU 2624  CB  ARG B  53     9036   6509   8794    -30    448    766       C  
ATOM   2625  CG  ARG B  53       5.173  57.313  31.751  1.00 67.09           C  
ANISOU 2625  CG  ARG B  53     9121   7009   9360   -124    461    650       C  
ATOM   2626  CD  ARG B  53       6.357  56.933  30.893  1.00 70.24           C  
ANISOU 2626  CD  ARG B  53     9301   7429   9959    -58    367    612       C  
ATOM   2627  NE  ARG B  53       6.150  55.636  30.248  1.00 72.78           N  
ANISOU 2627  NE  ARG B  53     9630   7656  10368    -27    489    657       N  
ATOM   2628  CZ  ARG B  53       7.119  54.767  29.979  1.00 73.79           C  
ANISOU 2628  CZ  ARG B  53     9666   7732  10640     84    410    656       C  
ATOM   2629  NH1 ARG B  53       6.837  53.616  29.380  1.00 72.25           N  
ANISOU 2629  NH1 ARG B  53     9483   7437  10530     97    551    682       N  
ATOM   2630  NH2 ARG B  53       8.377  55.040  30.313  1.00 73.68           N  
ANISOU 2630  NH2 ARG B  53     9520   7753  10723    185    188    600       N  
ATOM   2631  N   GLU B  54       1.794  56.945  32.214  1.00 59.68           N  
ANISOU 2631  N   GLU B  54     8471   5893   8310   -347   1002    644       N  
ATOM   2632  CA  GLU B  54       0.683  56.626  31.346  1.00 58.41           C  
ANISOU 2632  CA  GLU B  54     8192   5685   8315   -434   1186    567       C  
ATOM   2633  C   GLU B  54       0.681  57.489  30.078  1.00 57.31           C  
ANISOU 2633  C   GLU B  54     7808   5654   8315   -464   1096    483       C  
ATOM   2634  O   GLU B  54       0.861  58.711  30.150  1.00 57.37           O  
ANISOU 2634  O   GLU B  54     7762   5736   8301   -482   1004    452       O  
ATOM   2635  CB  GLU B  54      -0.648  56.767  32.104  1.00 60.22           C  
ANISOU 2635  CB  GLU B  54     8531   5818   8530   -536   1417    500       C  
ATOM   2636  CG  GLU B  54      -0.951  58.180  32.555  1.00 64.72           C  
ANISOU 2636  CG  GLU B  54     9070   6456   9067   -586   1386    422       C  
ATOM   2637  CD  GLU B  54      -2.350  58.475  33.073  1.00 72.09           C  
ANISOU 2637  CD  GLU B  54    10019   7291  10081   -700   1638    292       C  
ATOM   2638  OE1 GLU B  54      -3.324  57.853  32.586  1.00 72.97           O  
ANISOU 2638  OE1 GLU B  54    10021   7314  10391   -759   1808    198       O  
ATOM   2639  OE2 GLU B  54      -2.471  59.362  33.953  1.00 74.34           O  
ANISOU 2639  OE2 GLU B  54    10401   7584  10261   -738   1671    251       O  
ATOM   2640  N   GLY B  55       0.448  56.847  28.931  1.00 55.64           N  
ANISOU 2640  N   GLY B  55     7484   5430   8229   -474   1132    443       N  
ATOM   2641  CA  GLY B  55       0.307  57.543  27.661  1.00 54.65           C  
ANISOU 2641  CA  GLY B  55     7208   5376   8181   -499   1054    373       C  
ATOM   2642  C   GLY B  55      -0.963  58.371  27.657  1.00 54.02           C  
ANISOU 2642  C   GLY B  55     7073   5280   8173   -549   1075    274       C  
ATOM   2643  O   GLY B  55      -1.958  57.993  28.291  1.00 54.23           O  
ANISOU 2643  O   GLY B  55     7116   5223   8268   -592   1216    208       O  
ATOM   2644  N   VAL B  56      -0.935  59.539  26.999  1.00 53.09           N  
ANISOU 2644  N   VAL B  56     6895   5217   8060   -545    952    255       N  
ATOM   2645  CA  VAL B  56      -2.107  60.397  26.934  1.00 52.56           C  
ANISOU 2645  CA  VAL B  56     6756   5115   8099   -560    925    154       C  
ATOM   2646  C   VAL B  56      -2.538  60.635  25.495  1.00 52.36           C  
ANISOU 2646  C   VAL B  56     6672   5099   8124   -526    783    102       C  
ATOM   2647  O   VAL B  56      -3.723  60.612  25.188  1.00 52.13           O  
ANISOU 2647  O   VAL B  56     6542   5020   8244   -515    742    -29       O  
ATOM   2648  CB  VAL B  56      -1.978  61.721  27.741  1.00 53.30           C  
ANISOU 2648  CB  VAL B  56     6874   5215   8162   -570    901    166       C  
ATOM   2649  CG1 VAL B  56      -1.973  61.457  29.230  1.00 54.27           C  
ANISOU 2649  CG1 VAL B  56     7091   5311   8219   -607   1041    170       C  
ATOM   2650  CG2 VAL B  56      -0.765  62.532  27.345  1.00 53.31           C  
ANISOU 2650  CG2 VAL B  56     6913   5277   8066   -556    797    256       C  
ATOM   2651  N   SER B  57      -1.579  60.814  24.603  1.00 52.48           N  
ANISOU 2651  N   SER B  57     6760   5165   8017   -509    709    186       N  
ATOM   2652  CA  SER B  57      -1.866  61.118  23.214  1.00 52.60           C  
ANISOU 2652  CA  SER B  57     6818   5178   7991   -474    570    162       C  
ATOM   2653  C   SER B  57      -0.675  60.756  22.335  1.00 52.11           C  
ANISOU 2653  C   SER B  57     6862   5156   7781   -495    609    236       C  
ATOM   2654  O   SER B  57       0.454  60.785  22.805  1.00 52.25           O  
ANISOU 2654  O   SER B  57     6887   5199   7769   -526    705    307       O  
ATOM   2655  CB  SER B  57      -2.196  62.597  23.105  1.00 54.92           C  
ANISOU 2655  CB  SER B  57     7149   5430   8288   -436    447    184       C  
ATOM   2656  OG  SER B  57      -2.544  62.870  21.767  1.00 59.64           O  
ANISOU 2656  OG  SER B  57     7852   6004   8806   -378    277    178       O  
ATOM   2657  N   CYS B  58      -0.909  60.397  21.072  1.00 51.87           N  
ANISOU 2657  N   CYS B  58     6911   5126   7671   -480    538    193       N  
ATOM   2658  CA  CYS B  58       0.175  59.945  20.179  1.00 52.15           C  
ANISOU 2658  CA  CYS B  58     7059   5184   7571   -522    635    228       C  
ATOM   2659  C   CYS B  58      -0.129  60.358  18.739  1.00 51.41           C  
ANISOU 2659  C   CYS B  58     7174   5069   7291   -501    513    217       C  
ATOM   2660  O   CYS B  58      -1.283  60.323  18.317  1.00 51.19           O  
ANISOU 2660  O   CYS B  58     7148   5029   7273   -436    318    131       O  
ATOM   2661  CB  CYS B  58       0.364  58.423  20.311  1.00 53.49           C  
ANISOU 2661  CB  CYS B  58     7134   5367   7822   -542    750    162       C  
ATOM   2662  SG  CYS B  58       1.737  57.716  19.344  1.00 60.34           S  
ANISOU 2662  SG  CYS B  58     8083   6243   8601   -596    919    159       S  
ATOM   2663  N   ILE B  59       0.907  60.744  17.995  1.00 51.24           N  
ANISOU 2663  N   ILE B  59     7337   5029   7102   -555    629    289       N  
ATOM   2664  CA  ILE B  59       0.810  61.126  16.592  1.00 52.22           C  
ANISOU 2664  CA  ILE B  59     7764   5111   6967   -549    561    306       C  
ATOM   2665  C   ILE B  59       1.795  60.301  15.758  1.00 54.03           C  
ANISOU 2665  C   ILE B  59     8101   5350   7078   -643    786    263       C  
ATOM   2666  O   ILE B  59       2.978  60.253  16.061  1.00 54.05           O  
ANISOU 2666  O   ILE B  59     8031   5344   7162   -726   1028    285       O  
ATOM   2667  CB  ILE B  59       0.903  62.675  16.324  1.00 52.36           C  
ANISOU 2667  CB  ILE B  59     8010   5034   6851   -533    511    439       C  
ATOM   2668  CG1 ILE B  59       0.573  63.006  14.846  1.00 53.03           C  
ANISOU 2668  CG1 ILE B  59     8493   5049   6607   -493    384    472       C  
ATOM   2669  CG2 ILE B  59       2.235  63.320  16.784  1.00 51.75           C  
ANISOU 2669  CG2 ILE B  59     7915   4919   6830   -642    781    518       C  
ATOM   2670  CD1 ILE B  59       0.042  64.390  14.627  1.00 53.57           C  
ANISOU 2670  CD1 ILE B  59     8785   4996   6571   -399    191    592       C  
ATOM   2671  N   SER B  60       1.294  59.588  14.745  1.00 55.42           N  
ANISOU 2671  N   SER B  60     8419   5541   7099   -627    701    166       N  
ATOM   2672  CA  SER B  60       2.132  58.777  13.870  1.00 56.69           C  
ANISOU 2672  CA  SER B  60     8704   5700   7137   -723    931     94       C  
ATOM   2673  C   SER B  60       2.858  59.668  12.843  1.00 58.34           C  
ANISOU 2673  C   SER B  60     9300   5823   7042   -799   1086    180       C  
ATOM   2674  O   SER B  60       2.497  60.839  12.664  1.00 58.10           O  
ANISOU 2674  O   SER B  60     9487   5728   6858   -751    948    302       O  
ATOM   2675  CB  SER B  60       1.269  57.755  13.144  1.00 57.49           C  
ANISOU 2675  CB  SER B  60     8844   5841   7160   -687    776    -67       C  
ATOM   2676  OG  SER B  60       0.437  58.404  12.200  1.00 59.49           O  
ANISOU 2676  OG  SER B  60     9406   6072   7125   -613    501    -60       O  
ATOM   2677  N   SER B  61       3.862  59.106  12.137  1.00 59.46           N  
ANISOU 2677  N   SER B  61     9552   5937   7102   -922   1399    109       N  
ATOM   2678  CA  SER B  61       4.565  59.853  11.089  1.00 60.27           C  
ANISOU 2678  CA  SER B  61    10072   5929   6898  -1029   1632    170       C  
ATOM   2679  C   SER B  61       3.627  60.195   9.916  1.00 61.72           C  
ANISOU 2679  C   SER B  61    10733   6079   6639   -958   1377    204       C  
ATOM   2680  O   SER B  61       3.810  61.236   9.279  1.00 62.58           O  
ANISOU 2680  O   SER B  61    11256   6066   6456   -984   1433    338       O  
ATOM   2681  CB  SER B  61       5.784  59.089  10.599  1.00 60.38           C  
ANISOU 2681  CB  SER B  61    10072   5908   6960  -1186   2055     40       C  
ATOM   2682  OG  SER B  61       5.377  57.837  10.085  1.00 62.45           O  
ANISOU 2682  OG  SER B  61    10324   6235   7168  -1169   1998   -117       O  
ATOM   2683  N   GLY B  62       2.609  59.364   9.689  1.00 61.76           N  
ANISOU 2683  N   GLY B  62    10678   6174   6612   -859   1077     80       N  
ATOM   2684  CA  GLY B  62       1.593  59.598   8.674  1.00 62.47           C  
ANISOU 2684  CA  GLY B  62    11156   6251   6327   -749    722     68       C  
ATOM   2685  C   GLY B  62       0.574  60.666   9.041  1.00 63.26           C  
ANISOU 2685  C   GLY B  62    11279   6319   6439   -574    315    193       C  
ATOM   2686  O   GLY B  62      -0.205  61.085   8.180  1.00 63.74           O  
ANISOU 2686  O   GLY B  62    11709   6334   6176   -452    -22    213       O  
ATOM   2687  N   GLY B  63       0.559  61.096  10.312  1.00 63.10           N  
ANISOU 2687  N   GLY B  63    10875   6310   6788   -550    326    262       N  
ATOM   2688  CA  GLY B  63      -0.326  62.149  10.802  1.00 63.19           C  
ANISOU 2688  CA  GLY B  63    10851   6273   6886   -398      2    362       C  
ATOM   2689  C   GLY B  63      -1.542  61.709  11.596  1.00 63.32           C  
ANISOU 2689  C   GLY B  63    10444   6374   7241   -274   -311    221       C  
ATOM   2690  O   GLY B  63      -2.327  62.564  12.019  1.00 63.83           O  
ANISOU 2690  O   GLY B  63    10438   6387   7428   -146   -569    268       O  
ATOM   2691  N   SER B  64      -1.733  60.381  11.780  1.00 62.46           N  
ANISOU 2691  N   SER B  64    10056   6369   7307   -318   -266     32       N  
ATOM   2692  CA  SER B  64      -2.857  59.811  12.523  1.00 62.20           C  
ANISOU 2692  CA  SER B  64     9618   6391   7625   -242   -474   -138       C  
ATOM   2693  C   SER B  64      -2.706  60.078  14.005  1.00 62.15           C  
ANISOU 2693  C   SER B  64     9271   6385   7956   -273   -307    -69       C  
ATOM   2694  O   SER B  64      -1.610  59.929  14.537  1.00 62.92           O  
ANISOU 2694  O   SER B  64     9317   6496   8094   -382     11     22       O  
ATOM   2695  CB  SER B  64      -2.922  58.307  12.311  1.00 63.70           C  
ANISOU 2695  CB  SER B  64     9649   6653   7903   -314   -381   -343       C  
ATOM   2696  OG  SER B  64      -3.268  58.004  10.973  1.00 66.95           O  
ANISOU 2696  OG  SER B  64    10352   7073   8011   -276   -593   -463       O  
ATOM   2697  N   THR B  65      -3.800  60.434  14.694  1.00 61.08           N  
ANISOU 2697  N   THR B  65     8896   6232   8080   -177   -522   -140       N  
ATOM   2698  CA  THR B  65      -3.729  60.747  16.123  1.00 60.25           C  
ANISOU 2698  CA  THR B  65     8519   6119   8254   -211   -360    -87       C  
ATOM   2699  C   THR B  65      -4.556  59.795  16.982  1.00 59.20           C  
ANISOU 2699  C   THR B  65     8027   6007   8457   -230   -322   -272       C  
ATOM   2700  O   THR B  65      -5.632  59.364  16.567  1.00 59.81           O  
ANISOU 2700  O   THR B  65     7990   6077   8656   -171   -536   -472       O  
ATOM   2701  CB  THR B  65      -4.162  62.209  16.364  1.00 61.53           C  
ANISOU 2701  CB  THR B  65     8737   6198   8444   -110   -539      7       C  
ATOM   2702  OG1 THR B  65      -5.532  62.353  16.012  1.00 63.10           O  
ANISOU 2702  OG1 THR B  65     8845   6357   8772     33   -897   -152       O  
ATOM   2703  CG2 THR B  65      -3.346  63.211  15.564  1.00 61.29           C  
ANISOU 2703  CG2 THR B  65     9100   6099   8090   -105   -526    206       C  
ATOM   2704  N   VAL B  66      -4.060  59.465  18.181  1.00 57.55           N  
ANISOU 2704  N   VAL B  66     7658   5810   8400   -315    -51   -219       N  
ATOM   2705  CA  VAL B  66      -4.786  58.621  19.141  1.00 56.41           C  
ANISOU 2705  CA  VAL B  66     7238   5644   8551   -354     62   -360       C  
ATOM   2706  C   VAL B  66      -4.784  59.293  20.503  1.00 55.76           C  
ANISOU 2706  C   VAL B  66     7058   5531   8598   -372    188   -283       C  
ATOM   2707  O   VAL B  66      -3.826  59.987  20.840  1.00 56.19           O  
ANISOU 2707  O   VAL B  66     7230   5605   8516   -387    262   -111       O  
ATOM   2708  CB  VAL B  66      -4.336  57.134  19.223  1.00 56.56           C  
ANISOU 2708  CB  VAL B  66     7209   5675   8606   -441    284   -408       C  
ATOM   2709  CG1 VAL B  66      -4.669  56.398  17.948  1.00 57.51           C  
ANISOU 2709  CG1 VAL B  66     7377   5814   8659   -432    153   -566       C  
ATOM   2710  CG2 VAL B  66      -2.857  56.995  19.550  1.00 56.40           C  
ANISOU 2710  CG2 VAL B  66     7304   5683   8442   -489    494   -222       C  
ATOM   2711  N   TYR B  67      -5.851  59.102  21.284  1.00 54.90           N  
ANISOU 2711  N   TYR B  67     6734   5363   8762   -385    231   -435       N  
ATOM   2712  CA  TYR B  67      -5.985  59.712  22.604  1.00 54.70           C  
ANISOU 2712  CA  TYR B  67     6639   5295   8851   -415    375   -399       C  
ATOM   2713  C   TYR B  67      -6.398  58.687  23.638  1.00 55.02           C  
ANISOU 2713  C   TYR B  67     6563   5274   9066   -510    649   -491       C  
ATOM   2714  O   TYR B  67      -7.182  57.793  23.310  1.00 55.19           O  
ANISOU 2714  O   TYR B  67     6448   5248   9271   -538    674   -675       O  
ATOM   2715  CB  TYR B  67      -7.056  60.832  22.553  1.00 54.37           C  
ANISOU 2715  CB  TYR B  67     6474   5190   8993   -332    178   -516       C  
ATOM   2716  CG  TYR B  67      -6.682  61.948  21.605  1.00 54.26           C  
ANISOU 2716  CG  TYR B  67     6640   5190   8785   -226    -85   -391       C  
ATOM   2717  CD1 TYR B  67      -7.092  61.927  20.277  1.00 54.64           C  
ANISOU 2717  CD1 TYR B  67     6759   5238   8762   -126   -377   -454       C  
ATOM   2718  CD2 TYR B  67      -5.823  62.960  21.999  1.00 54.46           C  
ANISOU 2718  CD2 TYR B  67     6811   5217   8663   -234    -26   -206       C  
ATOM   2719  CE1 TYR B  67      -6.676  62.901  19.377  1.00 54.95           C  
ANISOU 2719  CE1 TYR B  67     7061   5261   8557    -34   -583   -304       C  
ATOM   2720  CE2 TYR B  67      -5.409  63.946  21.108  1.00 54.83           C  
ANISOU 2720  CE2 TYR B  67     7071   5239   8522   -159   -204    -76       C  
ATOM   2721  CZ  TYR B  67      -5.834  63.910  19.796  1.00 55.08           C  
ANISOU 2721  CZ  TYR B  67     7224   5254   8452    -59   -471   -109       C  
ATOM   2722  OH  TYR B  67      -5.454  64.889  18.917  1.00 55.28           O  
ANISOU 2722  OH  TYR B  67     7536   5219   8250     16   -626     40       O  
ATOM   2723  N   SER B  68      -5.905  58.810  24.891  1.00 54.89           N  
ANISOU 2723  N   SER B  68     6622   5242   8992   -564    857   -378       N  
ATOM   2724  CA  SER B  68      -6.375  57.923  25.949  1.00 55.60           C  
ANISOU 2724  CA  SER B  68     6681   5235   9209   -657   1145   -448       C  
ATOM   2725  C   SER B  68      -7.801  58.343  26.316  1.00 57.72           C  
ANISOU 2725  C   SER B  68     6740   5403   9787   -689   1204   -683       C  
ATOM   2726  O   SER B  68      -8.215  59.474  26.022  1.00 58.49           O  
ANISOU 2726  O   SER B  68     6743   5514   9967   -619   1009   -741       O  
ATOM   2727  CB  SER B  68      -5.455  57.943  27.159  1.00 55.80           C  
ANISOU 2727  CB  SER B  68     6904   5263   9034   -686   1307   -264       C  
ATOM   2728  OG  SER B  68      -5.556  59.145  27.897  1.00 58.21           O  
ANISOU 2728  OG  SER B  68     7225   5574   9318   -686   1298   -254       O  
ATOM   2729  N   GLU B  69      -8.579  57.426  26.893  1.00 58.38           N  
ANISOU 2729  N   GLU B  69     6740   5361  10079   -794   1481   -838       N  
ATOM   2730  CA  GLU B  69      -9.963  57.702  27.235  1.00 59.62           C  
ANISOU 2730  CA  GLU B  69     6649   5397  10607   -849   1596  -1118       C  
ATOM   2731  C   GLU B  69     -10.100  58.833  28.233  1.00 60.25           C  
ANISOU 2731  C   GLU B  69     6763   5448  10682   -863   1693  -1102       C  
ATOM   2732  O   GLU B  69     -11.091  59.556  28.184  1.00 60.92           O  
ANISOU 2732  O   GLU B  69     6605   5469  11074   -844   1639  -1322       O  
ATOM   2733  CB  GLU B  69     -10.679  56.438  27.729  1.00 62.75           C  
ANISOU 2733  CB  GLU B  69     6978   5631  11232   -997   1967  -1290       C  
ATOM   2734  CG  GLU B  69     -10.696  55.311  26.714  1.00 69.57           C  
ANISOU 2734  CG  GLU B  69     7764   6501  12167   -995   1884  -1367       C  
ATOM   2735  CD  GLU B  69     -11.562  55.554  25.494  1.00 79.68           C  
ANISOU 2735  CD  GLU B  69     8731   7818  13725   -915   1548  -1637       C  
ATOM   2736  OE1 GLU B  69     -11.025  55.493  24.364  1.00 80.75           O  
ANISOU 2736  OE1 GLU B  69     8927   8081  13675   -812   1230  -1559       O  
ATOM   2737  OE2 GLU B  69     -12.777  55.812  25.665  1.00 84.38           O  
ANISOU 2737  OE2 GLU B  69     9027   8307  14727   -952   1597  -1942       O  
ATOM   2738  N   SER B  70      -9.115  59.018  29.127  1.00 60.02           N  
ANISOU 2738  N   SER B  70     7019   5459  10326   -887   1811   -868       N  
ATOM   2739  CA  SER B  70      -9.180  60.093  30.123  1.00 60.33           C  
ANISOU 2739  CA  SER B  70     7121   5475  10326   -912   1909   -867       C  
ATOM   2740  C   SER B  70      -8.950  61.511  29.562  1.00 59.80           C  
ANISOU 2740  C   SER B  70     6978   5493  10249   -792   1583   -829       C  
ATOM   2741  O   SER B  70      -9.273  62.492  30.233  1.00 60.12           O  
ANISOU 2741  O   SER B  70     6994   5488  10362   -809   1652   -899       O  
ATOM   2742  CB  SER B  70      -8.220  59.820  31.277  1.00 62.49           C  
ANISOU 2742  CB  SER B  70     7741   5761  10240   -967   2097   -658       C  
ATOM   2743  OG  SER B  70      -6.917  59.534  30.799  1.00 66.60           O  
ANISOU 2743  OG  SER B  70     8411   6412  10482   -880   1875   -422       O  
ATOM   2744  N   VAL B  71      -8.386  61.631  28.353  1.00 58.90           N  
ANISOU 2744  N   VAL B  71     6862   5482  10036   -680   1263   -720       N  
ATOM   2745  CA  VAL B  71      -8.110  62.945  27.757  1.00 58.65           C  
ANISOU 2745  CA  VAL B  71     6827   5495   9964   -570    982   -652       C  
ATOM   2746  C   VAL B  71      -8.807  63.174  26.404  1.00 60.75           C  
ANISOU 2746  C   VAL B  71     6932   5743  10406   -445    664   -759       C  
ATOM   2747  O   VAL B  71      -8.652  64.253  25.828  1.00 61.55           O  
ANISOU 2747  O   VAL B  71     7076   5843  10467   -339    424   -689       O  
ATOM   2748  CB  VAL B  71      -6.580  63.232  27.639  1.00 56.78           C  
ANISOU 2748  CB  VAL B  71     6827   5373   9374   -550    897   -390       C  
ATOM   2749  CG1 VAL B  71      -5.822  62.861  28.906  1.00 56.48           C  
ANISOU 2749  CG1 VAL B  71     6958   5360   9142   -639   1123   -294       C  
ATOM   2750  CG2 VAL B  71      -5.975  62.554  26.425  1.00 56.03           C  
ANISOU 2750  CG2 VAL B  71     6793   5353   9141   -503    740   -291       C  
ATOM   2751  N   LYS B  72      -9.532  62.169  25.891  1.00 61.59           N  
ANISOU 2751  N   LYS B  72     6885   5824  10693   -454    652   -925       N  
ATOM   2752  CA  LYS B  72     -10.161  62.173  24.576  1.00 63.53           C  
ANISOU 2752  CA  LYS B  72     7004   6067  11068   -330    309  -1049       C  
ATOM   2753  C   LYS B  72     -11.018  63.413  24.253  1.00 64.93           C  
ANISOU 2753  C   LYS B  72     7026   6157  11487   -185     29  -1176       C  
ATOM   2754  O   LYS B  72     -10.905  63.962  23.150  1.00 65.63           O  
ANISOU 2754  O   LYS B  72     7219   6264  11453    -35   -334  -1100       O  
ATOM   2755  CB  LYS B  72     -10.973  60.898  24.389  1.00 66.60           C  
ANISOU 2755  CB  LYS B  72     7187   6415  11705   -395    401  -1290       C  
ATOM   2756  CG  LYS B  72     -11.134  60.451  22.949  1.00 73.03           C  
ANISOU 2756  CG  LYS B  72     7980   7281  12487   -294     59  -1363       C  
ATOM   2757  CD  LYS B  72     -11.855  59.090  22.914  1.00 79.26           C  
ANISOU 2757  CD  LYS B  72     8549   8018  13549   -396    214  -1627       C  
ATOM   2758  CE  LYS B  72     -11.929  58.439  21.553  1.00 83.76           C  
ANISOU 2758  CE  LYS B  72     9120   8650  14053   -327    -85  -1723       C  
ATOM   2759  NZ  LYS B  72     -10.588  58.287  20.954  1.00 86.41           N  
ANISOU 2759  NZ  LYS B  72     9808   9107  13915   -316   -121  -1425       N  
ATOM   2760  N   ASP B  73     -11.847  63.871  25.192  1.00 64.91           N  
ANISOU 2760  N   ASP B  73     6808   6042  11815   -223    200  -1364       N  
ATOM   2761  CA  ASP B  73     -12.709  65.029  24.926  1.00 65.25           C  
ANISOU 2761  CA  ASP B  73     6664   5971  12157    -68    -69  -1512       C  
ATOM   2762  C   ASP B  73     -12.043  66.380  25.198  1.00 64.02           C  
ANISOU 2762  C   ASP B  73     6707   5796  11820    -12   -113  -1300       C  
ATOM   2763  O   ASP B  73     -12.735  67.408  25.170  1.00 64.97           O  
ANISOU 2763  O   ASP B  73     6679   5789  12217    110   -279  -1418       O  
ATOM   2764  CB  ASP B  73     -13.987  64.938  25.776  1.00 68.92           C  
ANISOU 2764  CB  ASP B  73     6749   6290  13147   -138    163  -1874       C  
ATOM   2765  CG  ASP B  73     -14.873  63.728  25.523  1.00 78.64           C  
ANISOU 2765  CG  ASP B  73     7701   7486  14694   -203    228  -2169       C  
ATOM   2766  OD1 ASP B  73     -15.904  63.596  26.228  1.00 81.57           O  
ANISOU 2766  OD1 ASP B  73     7748   7716  15529   -292    485  -2494       O  
ATOM   2767  OD2 ASP B  73     -14.549  62.918  24.603  1.00 81.52           O  
ANISOU 2767  OD2 ASP B  73     8161   7949  14864   -175     44  -2102       O  
ATOM   2768  N   ARG B  74     -10.735  66.395  25.527  1.00 61.37           N  
ANISOU 2768  N   ARG B  74     6673   5566  11077   -103     47  -1021       N  
ATOM   2769  CA  ARG B  74     -10.079  67.617  25.964  1.00 58.82           C  
ANISOU 2769  CA  ARG B  74     6509   5216  10624    -94     74   -865       C  
ATOM   2770  C   ARG B  74      -8.742  67.944  25.324  1.00 57.76           C  
ANISOU 2770  C   ARG B  74     6691   5165  10089    -76    -32   -568       C  
ATOM   2771  O   ARG B  74      -8.370  69.112  25.323  1.00 57.87           O  
ANISOU 2771  O   ARG B  74     6818   5112  10057    -30    -94   -466       O  
ATOM   2772  CB  ARG B  74      -9.833  67.533  27.469  1.00 58.47           C  
ANISOU 2772  CB  ARG B  74     6472   5182  10562   -267    472   -899       C  
ATOM   2773  CG  ARG B  74     -11.035  67.172  28.315  1.00 59.96           C  
ANISOU 2773  CG  ARG B  74     6397   5267  11119   -346    720  -1196       C  
ATOM   2774  CD  ARG B  74     -10.625  66.282  29.474  1.00 62.10           C  
ANISOU 2774  CD  ARG B  74     6802   5587  11207   -537   1120  -1170       C  
ATOM   2775  NE  ARG B  74      -9.748  67.023  30.364  1.00 62.85           N  
ANISOU 2775  NE  ARG B  74     7113   5717  11048   -597   1242  -1034       N  
ATOM   2776  CZ  ARG B  74      -8.826  66.486  31.147  1.00 62.41           C  
ANISOU 2776  CZ  ARG B  74     7303   5751  10660   -702   1425   -889       C  
ATOM   2777  NH1 ARG B  74      -8.657  65.170  31.182  1.00 58.75           N  
ANISOU 2777  NH1 ARG B  74     6919   5330  10074   -759   1540   -837       N  
ATOM   2778  NH2 ARG B  74      -8.064  67.259  31.903  1.00 63.13           N  
ANISOU 2778  NH2 ARG B  74     7562   5875  10549   -740   1473   -807       N  
ATOM   2779  N   PHE B  75      -7.950  66.941  24.908  1.00 56.88           N  
ANISOU 2779  N   PHE B  75     6719   5180   9712   -136     12   -445       N  
ATOM   2780  CA  PHE B  75      -6.611  67.221  24.361  1.00 55.90           C  
ANISOU 2780  CA  PHE B  75     6868   5121   9250   -150    -17   -200       C  
ATOM   2781  C   PHE B  75      -6.576  67.131  22.837  1.00 56.18           C  
ANISOU 2781  C   PHE B  75     7058   5153   9133    -41   -285   -124       C  
ATOM   2782  O   PHE B  75      -7.394  66.432  22.241  1.00 56.30           O  
ANISOU 2782  O   PHE B  75     6970   5174   9248     23   -443   -257       O  
ATOM   2783  CB  PHE B  75      -5.522  66.293  24.974  1.00 54.42           C  
ANISOU 2783  CB  PHE B  75     6755   5060   8861   -287    227   -109       C  
ATOM   2784  CG  PHE B  75      -5.198  66.407  26.453  1.00 53.55           C  
ANISOU 2784  CG  PHE B  75     6618   4967   8760   -392    466   -128       C  
ATOM   2785  CD1 PHE B  75      -6.016  67.122  27.311  1.00 53.72           C  
ANISOU 2785  CD1 PHE B  75     6523   4899   8988   -400    541   -265       C  
ATOM   2786  CD2 PHE B  75      -4.095  65.773  26.986  1.00 54.08           C  
ANISOU 2786  CD2 PHE B  75     6788   5131   8630   -472    603    -27       C  
ATOM   2787  CE1 PHE B  75      -5.731  67.205  28.674  1.00 54.05           C  
ANISOU 2787  CE1 PHE B  75     6598   4956   8982   -503    764   -294       C  
ATOM   2788  CE2 PHE B  75      -3.812  65.858  28.348  1.00 54.54           C  
ANISOU 2788  CE2 PHE B  75     6872   5202   8647   -548    771    -47       C  
ATOM   2789  CZ  PHE B  75      -4.637  66.564  29.182  1.00 53.97           C  
ANISOU 2789  CZ  PHE B  75     6731   5050   8727   -571    859   -178       C  
ATOM   2790  N   THR B  76      -5.624  67.837  22.215  1.00 56.33           N  
ANISOU 2790  N   THR B  76     7342   5152   8907    -32   -320     73       N  
ATOM   2791  CA  THR B  76      -5.387  67.783  20.777  1.00 57.23           C  
ANISOU 2791  CA  THR B  76     7711   5252   8781     43   -511    178       C  
ATOM   2792  C   THR B  76      -3.881  67.692  20.539  1.00 58.28           C  
ANISOU 2792  C   THR B  76     8064   5444   8637    -82   -293    352       C  
ATOM   2793  O   THR B  76      -3.148  68.545  21.011  1.00 58.73           O  
ANISOU 2793  O   THR B  76     8180   5455   8680   -145   -149    442       O  
ATOM   2794  CB  THR B  76      -5.933  69.012  20.040  1.00 58.42           C  
ANISOU 2794  CB  THR B  76     8031   5234   8932    210   -795    236       C  
ATOM   2795  OG1 THR B  76      -7.234  69.346  20.517  1.00 60.26           O  
ANISOU 2795  OG1 THR B  76     7992   5386   9518    328   -972     47       O  
ATOM   2796  CG2 THR B  76      -5.972  68.818  18.538  1.00 58.29           C  
ANISOU 2796  CG2 THR B  76     8322   5192   8633    311  -1040    318       C  
ATOM   2797  N   ILE B  77      -3.418  66.662  19.833  1.00 58.62           N  
ANISOU 2797  N   ILE B  77     8195   5576   8502   -127   -252    365       N  
ATOM   2798  CA  ILE B  77      -2.012  66.529  19.479  1.00 59.76           C  
ANISOU 2798  CA  ILE B  77     8519   5754   8432   -243    -33    489       C  
ATOM   2799  C   ILE B  77      -1.869  66.952  18.006  1.00 61.75           C  
ANISOU 2799  C   ILE B  77     9141   5917   8406   -193   -143    595       C  
ATOM   2800  O   ILE B  77      -2.742  66.667  17.175  1.00 62.27           O  
ANISOU 2800  O   ILE B  77     9300   5967   8391    -77   -402    543       O  
ATOM   2801  CB  ILE B  77      -1.455  65.098  19.756  1.00 59.88           C  
ANISOU 2801  CB  ILE B  77     8395   5904   8452   -335    139    427       C  
ATOM   2802  CG1 ILE B  77       0.090  65.052  19.711  1.00 59.93           C  
ANISOU 2802  CG1 ILE B  77     8482   5934   8353   -456    389    510       C  
ATOM   2803  CG2 ILE B  77      -2.081  64.043  18.846  1.00 60.21           C  
ANISOU 2803  CG2 ILE B  77     8463   5987   8427   -289     10    334       C  
ATOM   2804  CD1 ILE B  77       0.710  63.779  20.191  1.00 60.13           C  
ANISOU 2804  CD1 ILE B  77     8344   6063   8441   -518    537    454       C  
ATOM   2805  N   SER B  78      -0.822  67.707  17.700  1.00 62.68           N  
ANISOU 2805  N   SER B  78     9486   5952   8378   -277     46    730       N  
ATOM   2806  CA  SER B  78      -0.559  68.151  16.336  1.00 64.31           C  
ANISOU 2806  CA  SER B  78    10128   6038   8270   -259     23    854       C  
ATOM   2807  C   SER B  78       0.940  68.241  16.080  1.00 66.77           C  
ANISOU 2807  C   SER B  78    10586   6319   8464   -444    404    924       C  
ATOM   2808  O   SER B  78       1.720  68.237  17.030  1.00 66.61           O  
ANISOU 2808  O   SER B  78    10309   6352   8648   -555    617    880       O  
ATOM   2809  CB  SER B  78      -1.268  69.464  16.030  1.00 64.63           C  
ANISOU 2809  CB  SER B  78    10392   5887   8276   -116   -206    958       C  
ATOM   2810  OG  SER B  78      -1.013  70.417  17.042  1.00 66.66           O  
ANISOU 2810  OG  SER B  78    10494   6074   8759   -161    -78    982       O  
ATOM   2811  N   ARG B  79       1.355  68.245  14.800  1.00 68.81           N  
ANISOU 2811  N   ARG B  79    11252   6491   8401   -483    496   1003       N  
ATOM   2812  CA  ARG B  79       2.778  68.304  14.483  1.00 71.16           C  
ANISOU 2812  CA  ARG B  79    11675   6735   8628   -682    917   1028       C  
ATOM   2813  C   ARG B  79       3.079  69.236  13.357  1.00 74.59           C  
ANISOU 2813  C   ARG B  79    12654   6942   8743   -719   1046   1186       C  
ATOM   2814  O   ARG B  79       2.270  69.393  12.444  1.00 75.51           O  
ANISOU 2814  O   ARG B  79    13146   6982   8561   -582    785   1273       O  
ATOM   2815  CB  ARG B  79       3.377  66.912  14.209  1.00 71.24           C  
ANISOU 2815  CB  ARG B  79    11561   6888   8620   -775   1087    902       C  
ATOM   2816  CG  ARG B  79       2.960  66.280  12.881  1.00 72.55           C  
ANISOU 2816  CG  ARG B  79    12085   7050   8430   -733    990    899       C  
ATOM   2817  CD  ARG B  79       3.387  64.818  12.774  1.00 73.48           C  
ANISOU 2817  CD  ARG B  79    12003   7314   8601   -807   1130    741       C  
ATOM   2818  NE  ARG B  79       4.843  64.683  12.821  1.00 73.75           N  
ANISOU 2818  NE  ARG B  79    11959   7317   8748   -998   1574    693       N  
ATOM   2819  CZ  ARG B  79       5.486  63.580  13.180  1.00 73.69           C  
ANISOU 2819  CZ  ARG B  79    11632   7415   8954  -1062   1735    551       C  
ATOM   2820  NH1 ARG B  79       4.810  62.493  13.523  1.00 72.79           N  
ANISOU 2820  NH1 ARG B  79    11286   7436   8935   -967   1522    463       N  
ATOM   2821  NH2 ARG B  79       6.811  63.556  13.204  1.00 72.65           N  
ANISOU 2821  NH2 ARG B  79    11398   7230   8975  -1219   2115    480       N  
ATOM   2822  N   ASP B  80       4.260  69.856  13.418  1.00 76.41           N  
ANISOU 2822  N   ASP B  80    12943   7050   9040   -905   1451   1211       N  
ATOM   2823  CA  ASP B  80       4.781  70.749  12.392  1.00 78.47           C  
ANISOU 2823  CA  ASP B  80    13749   7050   9016  -1003   1718   1357       C  
ATOM   2824  C   ASP B  80       6.173  70.223  12.055  1.00 79.75           C  
ANISOU 2824  C   ASP B  80    13882   7209   9212  -1251   2227   1243       C  
ATOM   2825  O   ASP B  80       7.134  70.551  12.741  1.00 80.15           O  
ANISOU 2825  O   ASP B  80    13639   7231   9584  -1406   2524   1150       O  
ATOM   2826  CB  ASP B  80       4.855  72.191  12.910  1.00 81.11           C  
ANISOU 2826  CB  ASP B  80    14129   7181   9508  -1013   1778   1460       C  
ATOM   2827  CG  ASP B  80       5.021  73.225  11.816  1.00 89.42           C  
ANISOU 2827  CG  ASP B  80    15847   7910  10220  -1053   1963   1665       C  
ATOM   2828  OD1 ASP B  80       4.688  74.412  12.066  1.00 91.22           O  
ANISOU 2828  OD1 ASP B  80    16211   7937  10512   -983   1883   1791       O  
ATOM   2829  OD2 ASP B  80       5.481  72.851  10.697  1.00 92.60           O  
ANISOU 2829  OD2 ASP B  80    16669   8236  10278  -1155   2206   1702       O  
ATOM   2830  N   ASN B  81       6.275  69.376  11.030  1.00 80.19           N  
ANISOU 2830  N   ASN B  81    14205   7295   8971  -1287   2317   1213       N  
ATOM   2831  CA  ASN B  81       7.551  68.789  10.644  1.00 81.33           C  
ANISOU 2831  CA  ASN B  81    14305   7424   9173  -1520   2817   1069       C  
ATOM   2832  C   ASN B  81       8.569  69.817  10.192  1.00 82.42           C  
ANISOU 2832  C   ASN B  81    14753   7281   9282  -1742   3333   1117       C  
ATOM   2833  O   ASN B  81       9.763  69.561  10.336  1.00 82.90           O  
ANISOU 2833  O   ASN B  81    14557   7322   9619  -1952   3772    939       O  
ATOM   2834  CB  ASN B  81       7.356  67.747   9.553  1.00 82.46           C  
ANISOU 2834  CB  ASN B  81    14741   7630   8961  -1515   2818   1022       C  
ATOM   2835  CG  ASN B  81       6.856  66.423  10.046  1.00 84.70           C  
ANISOU 2835  CG  ASN B  81    14586   8182   9415  -1397   2522    875       C  
ATOM   2836  OD1 ASN B  81       6.882  66.132  11.240  1.00 86.10           O  
ANISOU 2836  OD1 ASN B  81    14219   8501   9994  -1351   2400    792       O  
ATOM   2837  ND2 ASN B  81       6.390  65.590   9.133  1.00 84.99           N  
ANISOU 2837  ND2 ASN B  81    14882   8278   9132  -1352   2410    834       N  
ATOM   2838  N   ALA B  82       8.117  70.981   9.666  1.00 82.59           N  
ANISOU 2838  N   ALA B  82    15311   7062   9007  -1697   3293   1342       N  
ATOM   2839  CA  ALA B  82       9.019  72.038   9.192  1.00 83.17           C  
ANISOU 2839  CA  ALA B  82    15755   6812   9033  -1921   3826   1409       C  
ATOM   2840  C   ALA B  82       9.757  72.686  10.358  1.00 83.05           C  
ANISOU 2840  C   ALA B  82    15212   6771   9573  -2041   4017   1283       C  
ATOM   2841  O   ALA B  82      10.946  72.969  10.253  1.00 83.53           O  
ANISOU 2841  O   ALA B  82    15217   6675   9845  -2303   4566   1151       O  
ATOM   2842  CB  ALA B  82       8.247  73.087   8.403  1.00 83.51           C  
ANISOU 2842  CB  ALA B  82    16529   6587   8616  -1799   3669   1706       C  
ATOM   2843  N   LYS B  83       9.049  72.914  11.462  1.00 82.27           N  
ANISOU 2843  N   LYS B  83    14720   6817   9720  -1858   3575   1294       N  
ATOM   2844  CA  LYS B  83       9.613  73.465  12.696  1.00 81.87           C  
ANISOU 2844  CA  LYS B  83    14148   6785  10173  -1939   3656   1153       C  
ATOM   2845  C   LYS B  83      10.096  72.340  13.649  1.00 80.72           C  
ANISOU 2845  C   LYS B  83    13323   6943  10402  -1945   3571    899       C  
ATOM   2846  O   LYS B  83      10.648  72.649  14.705  1.00 81.22           O  
ANISOU 2846  O   LYS B  83    12933   7054  10874  -2003   3601    746       O  
ATOM   2847  CB  LYS B  83       8.553  74.324  13.420  1.00 84.08           C  
ANISOU 2847  CB  LYS B  83    14396   7048  10501  -1736   3231   1288       C  
ATOM   2848  CG  LYS B  83       8.036  75.488  12.583  1.00 89.25           C  
ANISOU 2848  CG  LYS B  83    15704   7377  10832  -1683   3246   1550       C  
ATOM   2849  CD  LYS B  83       6.984  76.320  13.328  1.00 95.42           C  
ANISOU 2849  CD  LYS B  83    16395   8129  11731  -1468   2821   1649       C  
ATOM   2850  CE  LYS B  83       6.493  77.494  12.494  1.00 99.43           C  
ANISOU 2850  CE  LYS B  83    17564   8273  11943  -1386   2812   1919       C  
ATOM   2851  NZ  LYS B  83       5.637  78.428  13.280  1.00101.13           N  
ANISOU 2851  NZ  LYS B  83    17644   8413  12368  -1199   2470   1979       N  
ATOM   2852  N   LYS B  84       9.852  71.052  13.291  1.00 78.86           N  
ANISOU 2852  N   LYS B  84    13041   6901  10019  -1868   3437    855       N  
ATOM   2853  CA  LYS B  84      10.152  69.846  14.052  1.00 77.47           C  
ANISOU 2853  CA  LYS B  84    12323   6988  10125  -1829   3312    661       C  
ATOM   2854  C   LYS B  84       9.573  69.935  15.471  1.00 74.67           C  
ANISOU 2854  C   LYS B  84    11553   6802  10017  -1672   2908    643       C  
ATOM   2855  O   LYS B  84      10.261  69.653  16.452  1.00 74.80           O  
ANISOU 2855  O   LYS B  84    11107   6925  10390  -1707   2917    470       O  
ATOM   2856  CB  LYS B  84      11.664  69.541  14.058  1.00 80.53           C  
ANISOU 2856  CB  LYS B  84    12420   7330  10850  -2050   3768    420       C  
ATOM   2857  CG  LYS B  84      12.220  69.071  12.704  1.00 85.57           C  
ANISOU 2857  CG  LYS B  84    13405   7843  11266  -2209   4195    380       C  
ATOM   2858  CD  LYS B  84      13.334  68.025  12.812  1.00 90.07           C  
ANISOU 2858  CD  LYS B  84    13536   8494  12193  -2316   4450     98       C  
ATOM   2859  CE  LYS B  84      14.455  68.406  13.741  1.00 94.09           C  
ANISOU 2859  CE  LYS B  84    13514   8973  13263  -2429   4618   -135       C  
ATOM   2860  NZ  LYS B  84      15.117  69.667  13.319  1.00 96.58           N  
ANISOU 2860  NZ  LYS B  84    14048   8998  13648  -2669   5092   -161       N  
ATOM   2861  N   ILE B  85       8.312  70.360  15.576  1.00 72.00           N  
ANISOU 2861  N   ILE B  85    11397   6471   9490  -1497   2553    808       N  
ATOM   2862  CA  ILE B  85       7.638  70.518  16.858  1.00 69.79           C  
ANISOU 2862  CA  ILE B  85    10789   6321   9407  -1361   2215    790       C  
ATOM   2863  C   ILE B  85       6.346  69.713  16.895  1.00 66.66           C  
ANISOU 2863  C   ILE B  85    10388   6080   8859  -1160   1827    843       C  
ATOM   2864  O   ILE B  85       5.608  69.664  15.917  1.00 66.46           O  
ANISOU 2864  O   ILE B  85    10714   5997   8540  -1078   1707    955       O  
ATOM   2865  CB  ILE B  85       7.368  72.032  17.159  1.00 70.80           C  
ANISOU 2865  CB  ILE B  85    11057   6259   9585  -1364   2208    881       C  
ATOM   2866  CG1 ILE B  85       8.671  72.792  17.455  1.00 72.62           C  
ANISOU 2866  CG1 ILE B  85    11152   6356  10085  -1578   2582    758       C  
ATOM   2867  CG2 ILE B  85       6.399  72.224  18.320  1.00 71.14           C  
ANISOU 2867  CG2 ILE B  85    10851   6414   9764  -1206   1849    872       C  
ATOM   2868  CD1 ILE B  85       8.510  74.348  17.606  1.00 74.21           C  
ANISOU 2868  CD1 ILE B  85    11546   6313  10339  -1616   2658    843       C  
ATOM   2869  N   VAL B  86       6.055  69.116  18.038  1.00 64.16           N  
ANISOU 2869  N   VAL B  86     9691   5944   8743  -1082   1627    752       N  
ATOM   2870  CA  VAL B  86       4.793  68.439  18.261  1.00 62.39           C  
ANISOU 2870  CA  VAL B  86     9409   5842   8456   -916   1303    768       C  
ATOM   2871  C   VAL B  86       4.114  69.185  19.405  1.00 61.23           C  
ANISOU 2871  C   VAL B  86     9091   5698   8476   -841   1122    763       C  
ATOM   2872  O   VAL B  86       4.735  69.387  20.440  1.00 61.87           O  
ANISOU 2872  O   VAL B  86     8927   5823   8756   -903   1195    680       O  
ATOM   2873  CB  VAL B  86       4.967  66.931  18.554  1.00 62.01           C  
ANISOU 2873  CB  VAL B  86     9114   5970   8475   -902   1284    663       C  
ATOM   2874  CG1 VAL B  86       3.690  66.326  19.128  1.00 62.05           C  
ANISOU 2874  CG1 VAL B  86     8986   6081   8509   -761   1000    644       C  
ATOM   2875  CG2 VAL B  86       5.400  66.192  17.299  1.00 61.96           C  
ANISOU 2875  CG2 VAL B  86     9309   5948   8287   -961   1446    653       C  
ATOM   2876  N   TYR B  87       2.861  69.619  19.224  1.00 59.42           N  
ANISOU 2876  N   TYR B  87     8985   5412   8179   -705    880    827       N  
ATOM   2877  CA  TYR B  87       2.134  70.319  20.282  1.00 58.15           C  
ANISOU 2877  CA  TYR B  87     8656   5236   8203   -636    737    793       C  
ATOM   2878  C   TYR B  87       1.111  69.431  20.962  1.00 55.79           C  
ANISOU 2878  C   TYR B  87     8125   5075   7998   -538    546    700       C  
ATOM   2879  O   TYR B  87       0.525  68.569  20.323  1.00 55.80           O  
ANISOU 2879  O   TYR B  87     8167   5129   7907   -471    427    688       O  
ATOM   2880  CB  TYR B  87       1.371  71.517  19.708  1.00 58.69           C  
ANISOU 2880  CB  TYR B  87     8982   5102   8215   -536    600    900       C  
ATOM   2881  CG  TYR B  87       2.238  72.514  18.986  1.00 60.37           C  
ANISOU 2881  CG  TYR B  87     9503   5115   8318   -634    817   1016       C  
ATOM   2882  CD1 TYR B  87       2.318  72.519  17.601  1.00 61.73           C  
ANISOU 2882  CD1 TYR B  87    10084   5171   8201   -621    844   1145       C  
ATOM   2883  CD2 TYR B  87       2.951  73.479  19.684  1.00 61.64           C  
ANISOU 2883  CD2 TYR B  87     9578   5184   8660   -749   1012    985       C  
ATOM   2884  CE1 TYR B  87       3.109  73.441  16.928  1.00 63.10           C  
ANISOU 2884  CE1 TYR B  87    10597   5121   8258   -732   1108   1259       C  
ATOM   2885  CE2 TYR B  87       3.717  74.427  19.023  1.00 63.14           C  
ANISOU 2885  CE2 TYR B  87    10055   5150   8786   -859   1260   1077       C  
ATOM   2886  CZ  TYR B  87       3.794  74.408  17.640  1.00 64.80           C  
ANISOU 2886  CZ  TYR B  87    10697   5226   8699   -855   1329   1225       C  
ATOM   2887  OH  TYR B  87       4.574  75.333  16.968  1.00 67.69           O  
ANISOU 2887  OH  TYR B  87    11401   5334   8983   -990   1643   1323       O  
ATOM   2888  N   LEU B  88       0.847  69.693  22.243  1.00 53.91           N  
ANISOU 2888  N   LEU B  88     7665   4874   7943   -540    534    618       N  
ATOM   2889  CA  LEU B  88      -0.222  69.039  22.982  1.00 52.33           C  
ANISOU 2889  CA  LEU B  88     7274   4754   7855   -469    417    518       C  
ATOM   2890  C   LEU B  88      -1.065  70.160  23.554  1.00 52.14           C  
ANISOU 2890  C   LEU B  88     7203   4619   7991   -411    337    475       C  
ATOM   2891  O   LEU B  88      -0.624  70.847  24.465  1.00 52.25           O  
ANISOU 2891  O   LEU B  88     7150   4615   8087   -479    441    439       O  
ATOM   2892  CB  LEU B  88       0.265  68.113  24.111  1.00 51.01           C  
ANISOU 2892  CB  LEU B  88     6922   4727   7732   -536    526    444       C  
ATOM   2893  CG  LEU B  88      -0.859  67.268  24.773  1.00 50.65           C  
ANISOU 2893  CG  LEU B  88     6735   4732   7778   -489    477    347       C  
ATOM   2894  CD1 LEU B  88      -1.507  66.314  23.764  1.00 50.58           C  
ANISOU 2894  CD1 LEU B  88     6747   4740   7733   -429    382    334       C  
ATOM   2895  CD2 LEU B  88      -0.350  66.512  25.994  1.00 50.09           C  
ANISOU 2895  CD2 LEU B  88     6575   4756   7702   -547    591    309       C  
ATOM   2896  N   GLN B  89      -2.235  70.404  22.977  1.00 51.85           N  
ANISOU 2896  N   GLN B  89     7196   4491   8014   -280    138    460       N  
ATOM   2897  CA  GLN B  89      -3.150  71.417  23.481  1.00 52.28           C  
ANISOU 2897  CA  GLN B  89     7166   4416   8282   -202     50    389       C  
ATOM   2898  C   GLN B  89      -3.992  70.701  24.539  1.00 52.29           C  
ANISOU 2898  C   GLN B  89     6895   4502   8471   -214     91    209       C  
ATOM   2899  O   GLN B  89      -4.632  69.704  24.229  1.00 51.72           O  
ANISOU 2899  O   GLN B  89     6737   4490   8424   -173     15    139       O  
ATOM   2900  CB  GLN B  89      -4.041  71.955  22.345  1.00 54.16           C  
ANISOU 2900  CB  GLN B  89     7549   4500   8532    -24   -228    436       C  
ATOM   2901  CG  GLN B  89      -5.069  72.984  22.792  1.00 57.29           C  
ANISOU 2901  CG  GLN B  89     7824   4732   9213     91   -353    342       C  
ATOM   2902  CD  GLN B  89      -4.413  74.212  23.356  1.00 62.44           C  
ANISOU 2902  CD  GLN B  89     8549   5266   9910     18   -187    397       C  
ATOM   2903  OE1 GLN B  89      -3.523  74.814  22.741  1.00 63.42           O  
ANISOU 2903  OE1 GLN B  89     8939   5300   9858    -23   -121    563       O  
ATOM   2904  NE2 GLN B  89      -4.839  74.606  24.548  1.00 63.95           N  
ANISOU 2904  NE2 GLN B  89     8512   5439  10345    -17    -86    238       N  
ATOM   2905  N   MET B  90      -3.934  71.156  25.792  1.00 52.44           N  
ANISOU 2905  N   MET B  90     6803   4518   8604   -289    243    122       N  
ATOM   2906  CA  MET B  90      -4.669  70.529  26.879  1.00 52.89           C  
ANISOU 2906  CA  MET B  90     6670   4627   8801   -330    357    -46       C  
ATOM   2907  C   MET B  90      -5.745  71.459  27.373  1.00 54.77           C  
ANISOU 2907  C   MET B  90     6770   4717   9322   -275    343   -199       C  
ATOM   2908  O   MET B  90      -5.438  72.480  27.987  1.00 55.19           O  
ANISOU 2908  O   MET B  90     6850   4703   9418   -315    424   -214       O  
ATOM   2909  CB  MET B  90      -3.733  70.171  28.027  1.00 52.76           C  
ANISOU 2909  CB  MET B  90     6680   4725   8641   -465    559    -43       C  
ATOM   2910  CG  MET B  90      -2.596  69.264  27.592  1.00 55.30           C  
ANISOU 2910  CG  MET B  90     7098   5173   8740   -505    566     85       C  
ATOM   2911  SD  MET B  90      -1.536  68.741  28.948  1.00 60.11           S  
ANISOU 2911  SD  MET B  90     7734   5905   9200   -610    709     75       S  
ATOM   2912  CE  MET B  90      -0.953  70.308  29.515  1.00 57.74           C  
ANISOU 2912  CE  MET B  90     7453   5543   8942   -663    729     34       C  
ATOM   2913  N   ASN B  91      -7.006  71.123  27.094  1.00 55.51           N  
ANISOU 2913  N   ASN B  91     6692   4750   9650   -183    240   -342       N  
ATOM   2914  CA  ASN B  91      -8.105  71.953  27.533  1.00 57.25           C  
ANISOU 2914  CA  ASN B  91     6725   4811  10217   -118    228   -531       C  
ATOM   2915  C   ASN B  91      -8.765  71.335  28.742  1.00 57.67           C  
ANISOU 2915  C   ASN B  91     6595   4885  10433   -236    507   -751       C  
ATOM   2916  O   ASN B  91      -8.617  70.128  28.975  1.00 57.75           O  
ANISOU 2916  O   ASN B  91     6619   5011  10312   -326    639   -748       O  
ATOM   2917  CB  ASN B  91      -9.111  72.179  26.396  1.00 59.74           C  
ANISOU 2917  CB  ASN B  91     6946   5001  10752     87   -107   -585       C  
ATOM   2918  CG  ASN B  91      -8.553  72.970  25.235  1.00 64.18           C  
ANISOU 2918  CG  ASN B  91     7777   5487  11122    211   -364   -354       C  
ATOM   2919  OD1 ASN B  91      -7.705  73.855  25.388  1.00 65.09           O  
ANISOU 2919  OD1 ASN B  91     8072   5549  11110    165   -277   -216       O  
ATOM   2920  ND2 ASN B  91      -9.017  72.657  24.042  1.00 65.82           N  
ANISOU 2920  ND2 ASN B  91     8041   5673  11293    363   -673   -320       N  
ATOM   2921  N   SER B  92      -9.473  72.179  29.531  1.00 57.32           N  
ANISOU 2921  N   SER B  92     6404   4703  10670   -245    631   -942       N  
ATOM   2922  CA  SER B  92     -10.230  71.766  30.716  1.00 57.21           C  
ANISOU 2922  CA  SER B  92     6238   4659  10841   -373    959  -1189       C  
ATOM   2923  C   SER B  92      -9.438  70.894  31.682  1.00 56.55           C  
ANISOU 2923  C   SER B  92     6358   4722  10408   -555   1239  -1113       C  
ATOM   2924  O   SER B  92      -9.837  69.769  31.983  1.00 56.92           O  
ANISOU 2924  O   SER B  92     6371   4797  10458   -634   1418  -1189       O  
ATOM   2925  CB  SER B  92     -11.530  71.090  30.294  1.00 58.74           C  
ANISOU 2925  CB  SER B  92     6141   4775  11403   -312    915  -1411       C  
ATOM   2926  OG  SER B  92     -12.337  72.036  29.615  1.00 61.61           O  
ANISOU 2926  OG  SER B  92     6303   4973  12132   -122    636  -1524       O  
ATOM   2927  N   LEU B  93      -8.293  71.402  32.133  1.00 55.69           N  
ANISOU 2927  N   LEU B  93     6466   4690  10004   -611   1259   -967       N  
ATOM   2928  CA  LEU B  93      -7.421  70.654  33.023  1.00 55.80           C  
ANISOU 2928  CA  LEU B  93     6699   4840   9663   -740   1433   -882       C  
ATOM   2929  C   LEU B  93      -7.961  70.600  34.436  1.00 56.98           C  
ANISOU 2929  C   LEU B  93     6897   4932   9822   -878   1776  -1076       C  
ATOM   2930  O   LEU B  93      -8.569  71.543  34.887  1.00 56.94           O  
ANISOU 2930  O   LEU B  93     6789   4804  10039   -896   1885  -1258       O  
ATOM   2931  CB  LEU B  93      -6.006  71.234  32.990  1.00 55.24           C  
ANISOU 2931  CB  LEU B  93     6802   4864   9323   -744   1298   -708       C  
ATOM   2932  CG  LEU B  93      -5.228  70.954  31.721  1.00 55.32           C  
ANISOU 2932  CG  LEU B  93     6847   4948   9224   -660   1058   -499       C  
ATOM   2933  CD1 LEU B  93      -4.109  71.960  31.537  1.00 55.69           C  
ANISOU 2933  CD1 LEU B  93     6984   5002   9172   -667    961   -401       C  
ATOM   2934  CD2 LEU B  93      -4.720  69.528  31.702  1.00 55.37           C  
ANISOU 2934  CD2 LEU B  93     6942   5086   9010   -689   1082   -395       C  
ATOM   2935  N   GLN B  94      -7.806  69.469  35.118  1.00 58.21           N  
ANISOU 2935  N   GLN B  94     7227   5149   9743   -973   1969  -1045       N  
ATOM   2936  CA  GLN B  94      -8.303  69.308  36.487  1.00 59.25           C  
ANISOU 2936  CA  GLN B  94     7500   5207   9806  -1122   2344  -1211       C  
ATOM   2937  C   GLN B  94      -7.156  68.919  37.415  1.00 59.65           C  
ANISOU 2937  C   GLN B  94     7922   5378   9363  -1183   2364  -1062       C  
ATOM   2938  O   GLN B  94      -6.146  68.445  36.919  1.00 59.62           O  
ANISOU 2938  O   GLN B  94     7998   5503   9153  -1110   2120   -850       O  
ATOM   2939  CB  GLN B  94      -9.412  68.239  36.522  1.00 60.80           C  
ANISOU 2939  CB  GLN B  94     7599   5299  10206  -1187   2612  -1343       C  
ATOM   2940  CG  GLN B  94     -10.648  68.562  35.685  1.00 64.48           C  
ANISOU 2940  CG  GLN B  94     7653   5635  11213  -1117   2567  -1556       C  
ATOM   2941  CD  GLN B  94     -11.337  69.871  36.012  1.00 69.33           C  
ANISOU 2941  CD  GLN B  94     8077   6112  12153  -1113   2640  -1789       C  
ATOM   2942  OE1 GLN B  94     -11.220  70.435  37.110  1.00 72.42           O  
ANISOU 2942  OE1 GLN B  94     8635   6467  12416  -1224   2884  -1880       O  
ATOM   2943  NE2 GLN B  94     -12.087  70.378  35.055  1.00 68.36           N  
ANISOU 2943  NE2 GLN B  94     7610   5898  12464   -971   2414  -1904       N  
ATOM   2944  N   PRO B  95      -7.261  69.098  38.752  1.00 59.75           N  
ANISOU 2944  N   PRO B  95     8179   5346   9175  -1308   2635  -1179       N  
ATOM   2945  CA  PRO B  95      -6.156  68.698  39.642  1.00 59.64           C  
ANISOU 2945  CA  PRO B  95     8554   5445   8661  -1333   2579  -1039       C  
ATOM   2946  C   PRO B  95      -5.555  67.313  39.402  1.00 60.07           C  
ANISOU 2946  C   PRO B  95     8775   5572   8478  -1276   2475   -812       C  
ATOM   2947  O   PRO B  95      -4.353  67.142  39.565  1.00 60.56           O  
ANISOU 2947  O   PRO B  95     9010   5759   8240  -1209   2222   -657       O  
ATOM   2948  CB  PRO B  95      -6.779  68.803  41.028  1.00 60.22           C  
ANISOU 2948  CB  PRO B  95     8900   5408   8575  -1489   2974  -1225       C  
ATOM   2949  CG  PRO B  95      -7.785  69.870  40.890  1.00 60.73           C  
ANISOU 2949  CG  PRO B  95     8657   5343   9074  -1532   3139  -1482       C  
ATOM   2950  CD  PRO B  95      -8.373  69.689  39.523  1.00 59.44           C  
ANISOU 2950  CD  PRO B  95     8089   5144   9352  -1426   2997  -1462       C  
ATOM   2951  N   GLU B  96      -6.375  66.346  38.972  1.00 59.65           N  
ANISOU 2951  N   GLU B  96     8631   5428   8606  -1295   2656   -816       N  
ATOM   2952  CA  GLU B  96      -5.968  64.985  38.641  1.00 59.63           C  
ANISOU 2952  CA  GLU B  96     8748   5453   8456  -1246   2599   -623       C  
ATOM   2953  C   GLU B  96      -5.033  64.897  37.412  1.00 58.88           C  
ANISOU 2953  C   GLU B  96     8463   5501   8409  -1100   2198   -451       C  
ATOM   2954  O   GLU B  96      -4.448  63.841  37.172  1.00 60.04           O  
ANISOU 2954  O   GLU B  96     8718   5686   8410  -1043   2109   -287       O  
ATOM   2955  CB  GLU B  96      -7.204  64.087  38.449  1.00 62.62           C  
ANISOU 2955  CB  GLU B  96     9026   5671   9096  -1330   2933   -733       C  
ATOM   2956  CG  GLU B  96      -8.021  63.868  39.713  1.00 68.88           C  
ANISOU 2956  CG  GLU B  96    10083   6290   9799  -1504   3419   -885       C  
ATOM   2957  CD  GLU B  96      -9.011  64.967  40.060  1.00 77.80           C  
ANISOU 2957  CD  GLU B  96    11009   7319  11233  -1603   3656  -1181       C  
ATOM   2958  OE1 GLU B  96      -9.120  65.939  39.276  1.00 76.52           O  
ANISOU 2958  OE1 GLU B  96    10487   7213  11376  -1514   3404  -1258       O  
ATOM   2959  OE2 GLU B  96      -9.685  64.852  41.115  1.00 82.64           O  
ANISOU 2959  OE2 GLU B  96    11841   7775  11785  -1769   4112  -1338       O  
ATOM   2960  N   ASP B  97      -4.907  65.975  36.632  1.00 57.00           N  
ANISOU 2960  N   ASP B  97     7965   5316   8377  -1045   1990   -492       N  
ATOM   2961  CA  ASP B  97      -3.991  66.058  35.488  1.00 56.18           C  
ANISOU 2961  CA  ASP B  97     7724   5324   8299   -935   1668   -347       C  
ATOM   2962  C   ASP B  97      -2.610  66.602  35.874  1.00 54.52           C  
ANISOU 2962  C   ASP B  97     7632   5227   7855   -905   1460   -269       C  
ATOM   2963  O   ASP B  97      -1.774  66.755  34.989  1.00 54.22           O  
ANISOU 2963  O   ASP B  97     7481   5264   7858   -839   1244   -176       O  
ATOM   2964  CB  ASP B  97      -4.558  66.925  34.355  1.00 58.28           C  
ANISOU 2964  CB  ASP B  97     7701   5553   8892   -886   1555   -415       C  
ATOM   2965  CG  ASP B  97      -5.873  66.419  33.835  1.00 63.86           C  
ANISOU 2965  CG  ASP B  97     8225   6156   9883   -887   1673   -529       C  
ATOM   2966  OD1 ASP B  97      -5.878  65.380  33.135  1.00 63.91           O  
ANISOU 2966  OD1 ASP B  97     8200   6186   9896   -853   1627   -456       O  
ATOM   2967  OD2 ASP B  97      -6.908  67.053  34.135  1.00 67.34           O  
ANISOU 2967  OD2 ASP B  97     8531   6482  10571   -922   1812   -722       O  
ATOM   2968  N   THR B  98      -2.377  66.903  37.171  1.00 53.41           N  
ANISOU 2968  N   THR B  98     7719   5090   7484   -962   1532   -333       N  
ATOM   2969  CA  THR B  98      -1.100  67.365  37.697  1.00 52.95           C  
ANISOU 2969  CA  THR B  98     7768   5137   7212   -935   1311   -311       C  
ATOM   2970  C   THR B  98      -0.127  66.219  37.567  1.00 52.70           C  
ANISOU 2970  C   THR B  98     7837   5182   7005   -841   1129   -144       C  
ATOM   2971  O   THR B  98      -0.365  65.137  38.124  1.00 53.62           O  
ANISOU 2971  O   THR B  98     8189   5252   6932   -830   1233    -69       O  
ATOM   2972  CB  THR B  98      -1.230  67.753  39.166  1.00 53.76           C  
ANISOU 2972  CB  THR B  98     8146   5218   7063  -1012   1430   -434       C  
ATOM   2973  OG1 THR B  98      -2.158  68.833  39.284  1.00 55.09           O  
ANISOU 2973  OG1 THR B  98     8191   5296   7445  -1101   1625   -617       O  
ATOM   2974  CG2 THR B  98       0.105  68.130  39.782  1.00 53.88           C  
ANISOU 2974  CG2 THR B  98     8276   5348   6845   -971   1148   -444       C  
ATOM   2975  N   ALA B  99       0.940  66.427  36.781  1.00 51.28           N  
ANISOU 2975  N   ALA B  99     7476   5088   6919   -776    888    -92       N  
ATOM   2976  CA  ALA B  99       1.942  65.407  36.468  1.00 49.85           C  
ANISOU 2976  CA  ALA B  99     7306   4967   6667   -675    705     37       C  
ATOM   2977  C   ALA B  99       3.108  66.041  35.686  1.00 48.81           C  
ANISOU 2977  C   ALA B  99     6932   4911   6704   -649    505     13       C  
ATOM   2978  O   ALA B  99       3.000  67.164  35.213  1.00 48.52           O  
ANISOU 2978  O   ALA B  99     6742   4857   6836   -712    541    -64       O  
ATOM   2979  CB  ALA B  99       1.293  64.301  35.610  1.00 49.15           C  
ANISOU 2979  CB  ALA B  99     7173   4822   6681   -652    833    144       C  
ATOM   2980  N   VAL B 100       4.229  65.313  35.555  1.00 48.14           N  
ANISOU 2980  N   VAL B 100     6814   4881   6596   -558    315     69       N  
ATOM   2981  CA  VAL B 100       5.310  65.697  34.683  1.00 47.24           C  
ANISOU 2981  CA  VAL B 100     6448   4809   6691   -552    199     31       C  
ATOM   2982  C   VAL B 100       4.923  65.048  33.349  1.00 47.05           C  
ANISOU 2982  C   VAL B 100     6327   4747   6803   -548    329    139       C  
ATOM   2983  O   VAL B 100       4.652  63.846  33.299  1.00 47.25           O  
ANISOU 2983  O   VAL B 100     6441   4752   6759   -486    358    237       O  
ATOM   2984  CB  VAL B 100       6.648  65.143  35.180  1.00 47.50           C  
ANISOU 2984  CB  VAL B 100     6455   4902   6690   -445    -66      0       C  
ATOM   2985  CG1 VAL B 100       7.775  65.507  34.218  1.00 47.87           C  
ANISOU 2985  CG1 VAL B 100     6196   4970   7024   -465   -119    -81       C  
ATOM   2986  CG2 VAL B 100       6.942  65.638  36.587  1.00 47.61           C  
ANISOU 2986  CG2 VAL B 100     6628   4959   6504   -428   -246   -112       C  
ATOM   2987  N   TYR B 101       4.837  65.845  32.294  1.00 46.61           N  
ANISOU 2987  N   TYR B 101     6128   4664   6918   -615    415    120       N  
ATOM   2988  CA  TYR B 101       4.508  65.405  30.944  1.00 46.46           C  
ANISOU 2988  CA  TYR B 101     6051   4611   6992   -615    513    201       C  
ATOM   2989  C   TYR B 101       5.793  65.244  30.130  1.00 47.37           C  
ANISOU 2989  C   TYR B 101     6024   4745   7230   -616    482    188       C  
ATOM   2990  O   TYR B 101       6.640  66.142  30.118  1.00 47.61           O  
ANISOU 2990  O   TYR B 101     5949   4773   7368   -671    462     97       O  
ATOM   2991  CB  TYR B 101       3.587  66.429  30.273  1.00 46.11           C  
ANISOU 2991  CB  TYR B 101     6001   4496   7023   -672    609    195       C  
ATOM   2992  CG  TYR B 101       2.177  66.376  30.807  1.00 46.52           C  
ANISOU 2992  CG  TYR B 101     6131   4506   7037   -668    678    180       C  
ATOM   2993  CD1 TYR B 101       1.130  65.904  30.023  1.00 47.10           C  
ANISOU 2993  CD1 TYR B 101     6195   4534   7168   -646    733    212       C  
ATOM   2994  CD2 TYR B 101       1.897  66.732  32.118  1.00 47.10           C  
ANISOU 2994  CD2 TYR B 101     6286   4581   7030   -693    697    104       C  
ATOM   2995  CE1 TYR B 101      -0.159  65.784  30.536  1.00 47.45           C  
ANISOU 2995  CE1 TYR B 101     6258   4523   7248   -653    823    150       C  
ATOM   2996  CE2 TYR B 101       0.620  66.596  32.647  1.00 47.67           C  
ANISOU 2996  CE2 TYR B 101     6424   4594   7095   -710    825     61       C  
ATOM   2997  CZ  TYR B 101      -0.408  66.144  31.847  1.00 48.50           C  
ANISOU 2997  CZ  TYR B 101     6466   4643   7320   -694    896     74       C  
ATOM   2998  OH  TYR B 101      -1.656  66.044  32.406  1.00 50.58           O  
ANISOU 2998  OH  TYR B 101     6744   4830   7646   -726   1050    -18       O  
ATOM   2999  N   TYR B 102       5.958  64.089  29.485  1.00 48.14           N  
ANISOU 2999  N   TYR B 102     6107   4845   7340   -566    505    250       N  
ATOM   3000  CA  TYR B 102       7.122  63.775  28.654  1.00 49.45           C  
ANISOU 3000  CA  TYR B 102     6131   5011   7648   -573    528    215       C  
ATOM   3001  C   TYR B 102       6.661  63.442  27.231  1.00 51.24           C  
ANISOU 3001  C   TYR B 102     6398   5196   7876   -609    680    276       C  
ATOM   3002  O   TYR B 102       5.551  62.946  27.023  1.00 51.60           O  
ANISOU 3002  O   TYR B 102     6547   5230   7828   -584    703    342       O  
ATOM   3003  CB  TYR B 102       7.868  62.520  29.165  1.00 49.09           C  
ANISOU 3003  CB  TYR B 102     6035   4989   7628   -459    406    213       C  
ATOM   3004  CG  TYR B 102       8.272  62.522  30.619  1.00 49.37           C  
ANISOU 3004  CG  TYR B 102     6106   5063   7591   -376    188    173       C  
ATOM   3005  CD1 TYR B 102       9.572  62.841  31.000  1.00 50.53           C  
ANISOU 3005  CD1 TYR B 102     6071   5237   7891   -345     24     34       C  
ATOM   3006  CD2 TYR B 102       7.397  62.080  31.605  1.00 49.51           C  
ANISOU 3006  CD2 TYR B 102     6350   5073   7387   -321    145    259       C  
ATOM   3007  CE1 TYR B 102       9.957  62.823  32.336  1.00 51.38           C  
ANISOU 3007  CE1 TYR B 102     6241   5384   7898   -246   -239    -15       C  
ATOM   3008  CE2 TYR B 102       7.768  62.051  32.942  1.00 50.46           C  
ANISOU 3008  CE2 TYR B 102     6585   5218   7369   -238    -62    233       C  
ATOM   3009  CZ  TYR B 102       9.049  62.422  33.307  1.00 52.05           C  
ANISOU 3009  CZ  TYR B 102     6623   5465   7690   -188   -287    100       C  
ATOM   3010  OH  TYR B 102       9.386  62.399  34.638  1.00 53.61           O  
ANISOU 3010  OH  TYR B 102     6968   5690   7712    -88   -547     63       O  
ATOM   3011  N   CYS B 103       7.541  63.649  26.266  1.00 51.75           N  
ANISOU 3011  N   CYS B 103     6383   5229   8050   -672    791    230       N  
ATOM   3012  CA  CYS B 103       7.322  63.222  24.903  1.00 52.97           C  
ANISOU 3012  CA  CYS B 103     6615   5345   8167   -706    933    271       C  
ATOM   3013  C   CYS B 103       8.393  62.181  24.548  1.00 53.71           C  
ANISOU 3013  C   CYS B 103     6574   5439   8396   -689    996    203       C  
ATOM   3014  O   CYS B 103       9.522  62.220  25.060  1.00 54.04           O  
ANISOU 3014  O   CYS B 103     6429   5486   8618   -679    957    100       O  
ATOM   3015  CB  CYS B 103       7.264  64.379  23.902  1.00 54.67           C  
ANISOU 3015  CB  CYS B 103     6946   5481   8344   -809   1069    288       C  
ATOM   3016  SG  CYS B 103       8.803  65.348  23.722  1.00 61.73           S  
ANISOU 3016  SG  CYS B 103     7709   6304   9440   -940   1240    165       S  
ATOM   3017  N   ALA B 104       8.013  61.200  23.736  1.00 53.67           N  
ANISOU 3017  N   ALA B 104     6639   5423   8332   -672   1069    235       N  
ATOM   3018  CA  ALA B 104       8.929  60.161  23.299  1.00 54.14           C  
ANISOU 3018  CA  ALA B 104     6575   5460   8535   -654   1158    159       C  
ATOM   3019  C   ALA B 104       8.852  60.033  21.782  1.00 54.83           C  
ANISOU 3019  C   ALA B 104     6788   5501   8544   -749   1374    142       C  
ATOM   3020  O   ALA B 104       7.783  60.201  21.197  1.00 54.74           O  
ANISOU 3020  O   ALA B 104     6977   5492   8329   -764   1364    215       O  
ATOM   3021  CB  ALA B 104       8.570  58.838  23.955  1.00 54.28           C  
ANISOU 3021  CB  ALA B 104     6579   5490   8557   -527   1037    202       C  
ATOM   3022  N   ALA B 105       9.972  59.695  21.146  1.00 55.39           N  
ANISOU 3022  N   ALA B 105     6745   5522   8779   -807   1564     24       N  
ATOM   3023  CA  ALA B 105      10.021  59.556  19.698  1.00 56.50           C  
ANISOU 3023  CA  ALA B 105     7049   5606   8813   -916   1814    -12       C  
ATOM   3024  C   ALA B 105      10.345  58.132  19.269  1.00 57.36           C  
ANISOU 3024  C   ALA B 105     7073   5696   9026   -879   1903   -100       C  
ATOM   3025  O   ALA B 105      11.342  57.543  19.727  1.00 58.26           O  
ANISOU 3025  O   ALA B 105     6924   5782   9430   -828   1915   -208       O  
ATOM   3026  CB  ALA B 105      11.051  60.521  19.115  1.00 56.99           C  
ANISOU 3026  CB  ALA B 105     7100   5581   8972  -1070   2079   -106       C  
ATOM   3027  N   ASP B 106       9.526  57.589  18.344  1.00 56.78           N  
ANISOU 3027  N   ASP B 106     7215   5623   8734   -899   1952    -75       N  
ATOM   3028  CA  ASP B 106       9.718  56.253  17.784  1.00 56.67           C  
ANISOU 3028  CA  ASP B 106     7159   5577   8795   -886   2068   -174       C  
ATOM   3029  C   ASP B 106      10.185  56.398  16.337  1.00 56.98           C  
ANISOU 3029  C   ASP B 106     7379   5553   8717  -1041   2384   -278       C  
ATOM   3030  O   ASP B 106       9.441  56.922  15.508  1.00 56.48           O  
ANISOU 3030  O   ASP B 106     7632   5497   8330  -1102   2392   -216       O  
ATOM   3031  CB  ASP B 106       8.399  55.452  17.842  1.00 57.82           C  
ANISOU 3031  CB  ASP B 106     7413   5764   8791   -807   1895   -112       C  
ATOM   3032  CG  ASP B 106       8.502  53.959  17.556  1.00 61.93           C  
ANISOU 3032  CG  ASP B 106     7855   6236   9438   -771   1979   -212       C  
ATOM   3033  OD1 ASP B 106       9.576  53.512  17.120  1.00 61.83           O  
ANISOU 3033  OD1 ASP B 106     7728   6159   9607   -808   2187   -339       O  
ATOM   3034  OD2 ASP B 106       7.496  53.235  17.774  1.00 64.29           O  
ANISOU 3034  OD2 ASP B 106     8194   6545   9688   -712   1858   -183       O  
ATOM   3035  N   PRO B 107      11.399  55.911  15.999  1.00 57.51           N  
ANISOU 3035  N   PRO B 107     7268   5541   9042  -1100   2647   -448       N  
ATOM   3036  CA  PRO B 107      11.858  55.982  14.600  1.00 58.25           C  
ANISOU 3036  CA  PRO B 107     7572   5553   9009  -1274   3020   -569       C  
ATOM   3037  C   PRO B 107      11.001  55.157  13.624  1.00 59.48           C  
ANISOU 3037  C   PRO B 107     8002   5726   8872  -1286   3036   -588       C  
ATOM   3038  O   PRO B 107      11.058  55.399  12.411  1.00 61.22           O  
ANISOU 3038  O   PRO B 107     8540   5895   8827  -1426   3285   -643       O  
ATOM   3039  CB  PRO B 107      13.298  55.473  14.688  1.00 58.54           C  
ANISOU 3039  CB  PRO B 107     7259   5495   9490  -1307   3272   -786       C  
ATOM   3040  CG  PRO B 107      13.269  54.526  15.871  1.00 58.53           C  
ANISOU 3040  CG  PRO B 107     6939   5532   9767  -1097   2962   -765       C  
ATOM   3041  CD  PRO B 107      12.394  55.235  16.856  1.00 56.88           C  
ANISOU 3041  CD  PRO B 107     6799   5426   9388  -1002   2612   -554       C  
ATOM   3042  N   PHE B 108      10.226  54.185  14.133  1.00 58.25           N  
ANISOU 3042  N   PHE B 108     7748   5628   8758  -1150   2788   -556       N  
ATOM   3043  CA  PHE B 108       9.286  53.412  13.332  1.00 58.15           C  
ANISOU 3043  CA  PHE B 108     7950   5638   8505  -1154   2747   -599       C  
ATOM   3044  C   PHE B 108       7.984  54.199  13.444  1.00 57.67           C  
ANISOU 3044  C   PHE B 108     8104   5662   8145  -1104   2441   -441       C  
ATOM   3045  O   PHE B 108       7.193  53.976  14.351  1.00 57.80           O  
ANISOU 3045  O   PHE B 108     7985   5729   8247   -990   2181   -362       O  
ATOM   3046  CB  PHE B 108       9.135  51.979  13.874  1.00 58.42           C  
ANISOU 3046  CB  PHE B 108     7743   5652   8801  -1045   2672   -667       C  
ATOM   3047  CG  PHE B 108      10.354  51.098  13.665  1.00 60.01           C  
ANISOU 3047  CG  PHE B 108     7728   5744   9328  -1069   2953   -847       C  
ATOM   3048  CD1 PHE B 108      10.768  50.745  12.387  1.00 61.23           C  
ANISOU 3048  CD1 PHE B 108     8037   5839   9388  -1210   3278  -1034       C  
ATOM   3049  CD2 PHE B 108      11.070  50.606  14.742  1.00 60.94           C  
ANISOU 3049  CD2 PHE B 108     7504   5806   9845   -939   2882   -844       C  
ATOM   3050  CE1 PHE B 108      11.881  49.938  12.196  1.00 62.06           C  
ANISOU 3050  CE1 PHE B 108     7909   5825   9844  -1232   3561  -1232       C  
ATOM   3051  CE2 PHE B 108      12.178  49.786  14.543  1.00 61.83           C  
ANISOU 3051  CE2 PHE B 108     7383   5797  10311   -933   3109  -1030       C  
ATOM   3052  CZ  PHE B 108      12.574  49.460  13.273  1.00 61.85           C  
ANISOU 3052  CZ  PHE B 108     7496   5736  10266  -1085   3464  -1233       C  
ATOM   3053  N   GLY B 109       7.834  55.174  12.560  1.00 57.13           N  
ANISOU 3053  N   GLY B 109     8375   5583   7750  -1190   2495   -397       N  
ATOM   3054  CA  GLY B 109       6.737  56.125  12.524  1.00 57.43           C  
ANISOU 3054  CA  GLY B 109     8641   5666   7515  -1135   2212   -254       C  
ATOM   3055  C   GLY B 109       5.322  55.606  12.611  1.00 57.94           C  
ANISOU 3055  C   GLY B 109     8707   5803   7503  -1025   1881   -263       C  
ATOM   3056  O   GLY B 109       4.428  56.341  13.053  1.00 58.29           O  
ANISOU 3056  O   GLY B 109     8773   5883   7493   -942   1611   -157       O  
ATOM   3057  N   GLU B 110       5.087  54.377  12.146  1.00 57.81           N  
ANISOU 3057  N   GLU B 110     8662   5795   7508  -1033   1915   -419       N  
ATOM   3058  CA  GLU B 110       3.753  53.791  12.205  1.00 58.36           C  
ANISOU 3058  CA  GLU B 110     8689   5916   7569   -950   1631   -483       C  
ATOM   3059  C   GLU B 110       3.583  52.780  13.342  1.00 58.27           C  
ANISOU 3059  C   GLU B 110     8318   5897   7926   -890   1619   -512       C  
ATOM   3060  O   GLU B 110       2.535  52.143  13.413  1.00 59.48           O  
ANISOU 3060  O   GLU B 110     8401   6063   8137   -851   1459   -602       O  
ATOM   3061  CB  GLU B 110       3.362  53.176  10.851  1.00 61.21           C  
ANISOU 3061  CB  GLU B 110     9310   6282   7665   -999   1624   -660       C  
ATOM   3062  CG  GLU B 110       3.221  54.215   9.744  1.00 67.50           C  
ANISOU 3062  CG  GLU B 110    10561   7073   8011  -1023   1542   -605       C  
ATOM   3063  CD  GLU B 110       2.208  55.327   9.972  1.00 75.80           C  
ANISOU 3063  CD  GLU B 110    11706   8151   8943   -904   1169   -470       C  
ATOM   3064  OE1 GLU B 110       2.588  56.514   9.845  1.00 77.16           O  
ANISOU 3064  OE1 GLU B 110    12107   8273   8936   -914   1205   -304       O  
ATOM   3065  OE2 GLU B 110       1.032  55.016  10.271  1.00 79.00           O  
ANISOU 3065  OE2 GLU B 110    11945   8605   9466   -805    859   -547       O  
ATOM   3066  N   ARG B 111       4.577  52.652  14.252  1.00 56.76           N  
ANISOU 3066  N   ARG B 111     7912   5667   7988   -879   1775   -441       N  
ATOM   3067  CA  ARG B 111       4.529  51.679  15.346  1.00 55.71           C  
ANISOU 3067  CA  ARG B 111     7517   5491   8159   -807   1770   -435       C  
ATOM   3068  C   ARG B 111       3.904  52.190  16.647  1.00 55.40           C  
ANISOU 3068  C   ARG B 111     7371   5475   8204   -726   1583   -294       C  
ATOM   3069  O   ARG B 111       2.928  51.610  17.084  1.00 55.23           O  
ANISOU 3069  O   ARG B 111     7286   5433   8266   -695   1498   -325       O  
ATOM   3070  CB  ARG B 111       5.936  51.075  15.631  1.00 55.68           C  
ANISOU 3070  CB  ARG B 111     7347   5410   8398   -801   1991   -459       C  
ATOM   3071  CG  ARG B 111       5.986  50.164  16.865  1.00 55.70           C  
ANISOU 3071  CG  ARG B 111     7142   5338   8684   -691   1949   -405       C  
ATOM   3072  CD  ARG B 111       7.312  49.493  17.137  1.00 56.79           C  
ANISOU 3072  CD  ARG B 111     7103   5379   9096   -641   2095   -444       C  
ATOM   3073  NE  ARG B 111       8.390  50.434  17.456  1.00 59.04           N  
ANISOU 3073  NE  ARG B 111     7295   5691   9447   -635   2105   -400       N  
ATOM   3074  CZ  ARG B 111       9.599  50.071  17.878  1.00 60.14           C  
ANISOU 3074  CZ  ARG B 111     7221   5751   9879   -564   2163   -445       C  
ATOM   3075  NH1 ARG B 111       9.889  48.788  18.058  1.00 61.72           N  
ANISOU 3075  NH1 ARG B 111     7306   5829  10317   -474   2206   -503       N  
ATOM   3076  NH2 ARG B 111      10.535  50.985  18.102  1.00 57.68           N  
ANISOU 3076  NH2 ARG B 111     6795   5463   9657   -579   2173   -454       N  
ATOM   3077  N   LEU B 112       4.500  53.218  17.294  1.00 55.25           N  
ANISOU 3077  N   LEU B 112     7324   5482   8188   -708   1557   -165       N  
ATOM   3078  CA  LEU B 112       4.138  53.703  18.626  1.00 54.91           C  
ANISOU 3078  CA  LEU B 112     7188   5452   8222   -640   1419    -43       C  
ATOM   3079  C   LEU B 112       2.640  53.787  18.945  1.00 54.95           C  
ANISOU 3079  C   LEU B 112     7212   5472   8197   -619   1265    -50       C  
ATOM   3080  O   LEU B 112       2.205  53.256  19.964  1.00 54.25           O  
ANISOU 3080  O   LEU B 112     7034   5338   8239   -580   1260    -23       O  
ATOM   3081  CB  LEU B 112       4.801  55.062  18.904  1.00 54.33           C  
ANISOU 3081  CB  LEU B 112     7133   5415   8093   -655   1396     48       C  
ATOM   3082  CG  LEU B 112       4.670  55.633  20.321  1.00 54.37           C  
ANISOU 3082  CG  LEU B 112     7052   5437   8169   -594   1272    153       C  
ATOM   3083  CD1 LEU B 112       5.140  54.624  21.405  1.00 54.31           C  
ANISOU 3083  CD1 LEU B 112     6918   5381   8337   -512   1277    179       C  
ATOM   3084  CD2 LEU B 112       5.450  56.930  20.424  1.00 54.35           C  
ANISOU 3084  CD2 LEU B 112     7053   5458   8141   -630   1278    197       C  
ATOM   3085  N   CYS B 113       1.867  54.471  18.092  1.00 55.16           N  
ANISOU 3085  N   CYS B 113     7361   5540   8059   -639   1144    -94       N  
ATOM   3086  CA  CYS B 113       0.457  54.757  18.331  1.00 54.98           C  
ANISOU 3086  CA  CYS B 113     7308   5524   8059   -608    968   -138       C  
ATOM   3087  C   CYS B 113      -0.459  53.545  18.268  1.00 54.28           C  
ANISOU 3087  C   CYS B 113     7118   5391   8116   -618    980   -295       C  
ATOM   3088  O   CYS B 113      -1.636  53.660  18.637  1.00 54.55           O  
ANISOU 3088  O   CYS B 113     7060   5407   8259   -604    876   -371       O  
ATOM   3089  CB  CYS B 113      -0.016  55.874  17.409  1.00 56.18           C  
ANISOU 3089  CB  CYS B 113     7627   5711   8007   -592    784   -139       C  
ATOM   3090  SG  CYS B 113       1.044  57.352  17.433  1.00 61.01           S  
ANISOU 3090  SG  CYS B 113     8383   6328   8469   -608    829     37       S  
ATOM   3091  N   ILE B 114       0.070  52.369  17.857  1.00 53.19           N  
ANISOU 3091  N   ILE B 114     6970   5212   8027   -651   1133   -367       N  
ATOM   3092  CA  ILE B 114      -0.693  51.121  17.862  1.00 52.00           C  
ANISOU 3092  CA  ILE B 114     6717   4986   8054   -677   1195   -526       C  
ATOM   3093  C   ILE B 114      -0.931  50.705  19.334  1.00 51.66           C  
ANISOU 3093  C   ILE B 114     6567   4848   8214   -662   1308   -442       C  
ATOM   3094  O   ILE B 114      -2.043  50.317  19.707  1.00 52.25           O  
ANISOU 3094  O   ILE B 114     6550   4857   8448   -691   1325   -553       O  
ATOM   3095  CB  ILE B 114       0.071  50.010  17.094  1.00 51.64           C  
ANISOU 3095  CB  ILE B 114     6701   4898   8023   -715   1360   -616       C  
ATOM   3096  CG1 ILE B 114       0.136  50.299  15.589  1.00 52.10           C  
ANISOU 3096  CG1 ILE B 114     6925   5032   7837   -753   1280   -734       C  
ATOM   3097  CG2 ILE B 114      -0.506  48.613  17.373  1.00 51.77           C  
ANISOU 3097  CG2 ILE B 114     6600   4789   8280   -744   1488   -751       C  
ATOM   3098  CD1 ILE B 114       1.094  49.346  14.812  1.00 52.69           C  
ANISOU 3098  CD1 ILE B 114     7050   5063   7907   -806   1496   -831       C  
ATOM   3099  N   ASP B 115       0.105  50.820  20.168  1.00 50.36           N  
ANISOU 3099  N   ASP B 115     6429   4666   8041   -617   1384   -262       N  
ATOM   3100  CA  ASP B 115       0.052  50.389  21.559  1.00 50.17           C  
ANISOU 3100  CA  ASP B 115     6396   4538   8130   -587   1483   -155       C  
ATOM   3101  C   ASP B 115       1.034  51.285  22.347  1.00 50.94           C  
ANISOU 3101  C   ASP B 115     6538   4692   8125   -522   1412     27       C  
ATOM   3102  O   ASP B 115       2.121  50.835  22.713  1.00 51.15           O  
ANISOU 3102  O   ASP B 115     6574   4675   8186   -459   1448    112       O  
ATOM   3103  CB  ASP B 115       0.512  48.920  21.564  1.00 50.07           C  
ANISOU 3103  CB  ASP B 115     6382   4384   8256   -574   1650   -175       C  
ATOM   3104  CG  ASP B 115       0.203  48.120  22.789  1.00 51.84           C  
ANISOU 3104  CG  ASP B 115     6666   4438   8595   -553   1791    -91       C  
ATOM   3105  OD1 ASP B 115       0.176  48.699  23.871  1.00 52.66           O  
ANISOU 3105  OD1 ASP B 115     6846   4541   8623   -519   1759     45       O  
ATOM   3106  OD2 ASP B 115       0.019  46.901  22.665  1.00 53.74           O  
ANISOU 3106  OD2 ASP B 115     6906   4526   8985   -575   1949   -162       O  
ATOM   3107  N   PRO B 116       0.679  52.570  22.587  1.00 51.18           N  
ANISOU 3107  N   PRO B 116     6578   4811   8059   -530   1294     63       N  
ATOM   3108  CA  PRO B 116       1.642  53.500  23.199  1.00 51.57           C  
ANISOU 3108  CA  PRO B 116     6652   4920   8025   -487   1221    191       C  
ATOM   3109  C   PRO B 116       2.250  53.085  24.534  1.00 52.55           C  
ANISOU 3109  C   PRO B 116     6819   4977   8172   -416   1241    310       C  
ATOM   3110  O   PRO B 116       3.451  53.261  24.708  1.00 52.93           O  
ANISOU 3110  O   PRO B 116     6840   5050   8220   -358   1181    365       O  
ATOM   3111  CB  PRO B 116       0.849  54.797  23.325  1.00 51.84           C  
ANISOU 3111  CB  PRO B 116     6693   5016   7990   -513   1118    185       C  
ATOM   3112  CG  PRO B 116      -0.174  54.708  22.256  1.00 52.15           C  
ANISOU 3112  CG  PRO B 116     6707   5062   8046   -550   1075     49       C  
ATOM   3113  CD  PRO B 116      -0.559  53.270  22.186  1.00 50.48           C  
ANISOU 3113  CD  PRO B 116     6457   4762   7961   -570   1199    -41       C  
ATOM   3114  N   ASN B 117       1.451  52.525  25.452  1.00 52.38           N  
ANISOU 3114  N   ASN B 117     6876   4854   8172   -418   1325    336       N  
ATOM   3115  CA  ASN B 117       1.932  52.116  26.761  1.00 52.70           C  
ANISOU 3115  CA  ASN B 117     7052   4807   8164   -339   1330    470       C  
ATOM   3116  C   ASN B 117       2.885  50.927  26.735  1.00 53.38           C  
ANISOU 3116  C   ASN B 117     7159   4790   8332   -241   1342    523       C  
ATOM   3117  O   ASN B 117       3.719  50.800  27.633  1.00 53.92           O  
ANISOU 3117  O   ASN B 117     7319   4817   8351   -125   1234    638       O  
ATOM   3118  CB  ASN B 117       0.770  51.868  27.688  1.00 53.39           C  
ANISOU 3118  CB  ASN B 117     7273   4784   8229   -393   1479    479       C  
ATOM   3119  CG  ASN B 117       0.176  53.170  28.115  1.00 56.73           C  
ANISOU 3119  CG  ASN B 117     7685   5295   8574   -448   1434    449       C  
ATOM   3120  OD1 ASN B 117       0.897  54.119  28.427  1.00 58.57           O  
ANISOU 3120  OD1 ASN B 117     7921   5630   8703   -406   1281    505       O  
ATOM   3121  ND2 ASN B 117      -1.132  53.273  28.121  1.00 57.39           N  
ANISOU 3121  ND2 ASN B 117     7727   5332   8746   -543   1567    334       N  
ATOM   3122  N   THR B 118       2.783  50.065  25.714  1.00 52.98           N  
ANISOU 3122  N   THR B 118     7025   4691   8415   -273   1447    426       N  
ATOM   3123  CA  THR B 118       3.687  48.937  25.605  1.00 52.78           C  
ANISOU 3123  CA  THR B 118     6992   4547   8514   -177   1473    453       C  
ATOM   3124  C   THR B 118       4.903  49.346  24.801  1.00 52.95           C  
ANISOU 3124  C   THR B 118     6847   4672   8599   -145   1383    391       C  
ATOM   3125  O   THR B 118       6.026  49.069  25.215  1.00 53.39           O  
ANISOU 3125  O   THR B 118     6863   4679   8743    -18   1286    441       O  
ATOM   3126  CB  THR B 118       3.006  47.723  24.970  1.00 53.41           C  
ANISOU 3126  CB  THR B 118     7067   4493   8734   -238   1671    352       C  
ATOM   3127  OG1 THR B 118       1.875  47.369  25.746  1.00 54.93           O  
ANISOU 3127  OG1 THR B 118     7399   4562   8909   -294   1808    382       O  
ATOM   3128  CG2 THR B 118       3.927  46.538  24.858  1.00 53.35           C  
ANISOU 3128  CG2 THR B 118     7052   4333   8887   -130   1713    373       C  
ATOM   3129  N   PHE B 119       4.684  50.016  23.661  1.00 52.17           N  
ANISOU 3129  N   PHE B 119     6661   4699   8463   -256   1415    273       N  
ATOM   3130  CA  PHE B 119       5.736  50.321  22.718  1.00 52.44           C  
ANISOU 3130  CA  PHE B 119     6574   4797   8554   -272   1429    187       C  
ATOM   3131  C   PHE B 119       6.680  51.432  23.183  1.00 53.79           C  
ANISOU 3131  C   PHE B 119     6676   5053   8709   -238   1302    231       C  
ATOM   3132  O   PHE B 119       7.811  51.489  22.688  1.00 54.00           O  
ANISOU 3132  O   PHE B 119     6568   5082   8868   -231   1340    151       O  
ATOM   3133  CB  PHE B 119       5.154  50.576  21.318  1.00 51.83           C  
ANISOU 3133  CB  PHE B 119     6515   4792   8386   -402   1520     56       C  
ATOM   3134  CG  PHE B 119       4.469  49.384  20.667  1.00 51.82           C  
ANISOU 3134  CG  PHE B 119     6534   4707   8448   -442   1641    -57       C  
ATOM   3135  CD1 PHE B 119       4.507  48.127  21.251  1.00 52.67           C  
ANISOU 3135  CD1 PHE B 119     6633   4657   8723   -373   1716    -34       C  
ATOM   3136  CD2 PHE B 119       3.799  49.520  19.472  1.00 52.18           C  
ANISOU 3136  CD2 PHE B 119     6627   4815   8383   -541   1667   -193       C  
ATOM   3137  CE1 PHE B 119       3.908  47.036  20.638  1.00 53.16           C  
ANISOU 3137  CE1 PHE B 119     6698   4623   8876   -425   1852   -163       C  
ATOM   3138  CE2 PHE B 119       3.203  48.425  18.860  1.00 52.86           C  
ANISOU 3138  CE2 PHE B 119     6714   4828   8543   -585   1763   -338       C  
ATOM   3139  CZ  PHE B 119       3.252  47.194  19.451  1.00 52.77           C  
ANISOU 3139  CZ  PHE B 119     6660   4658   8734   -537   1872   -331       C  
ATOM   3140  N   ALA B 120       6.259  52.254  24.179  1.00 54.28           N  
ANISOU 3140  N   ALA B 120     6812   5166   8646   -222   1174    329       N  
ATOM   3141  CA  ALA B 120       7.109  53.278  24.800  1.00 54.53           C  
ANISOU 3141  CA  ALA B 120     6777   5268   8675   -188   1034    352       C  
ATOM   3142  C   ALA B 120       8.351  52.634  25.424  1.00 55.46           C  
ANISOU 3142  C   ALA B 120     6791   5313   8970    -39    920    353       C  
ATOM   3143  O   ALA B 120       9.413  53.262  25.465  1.00 55.73           O  
ANISOU 3143  O   ALA B 120     6663   5389   9123    -21    839    280       O  
ATOM   3144  CB  ALA B 120       6.346  54.008  25.887  1.00 53.92           C  
ANISOU 3144  CB  ALA B 120     6827   5229   8432   -187    930    443       C  
ATOM   3145  N   GLY B 121       8.192  51.406  25.922  1.00 55.73           N  
ANISOU 3145  N   GLY B 121     6916   5217   9041     70    907    425       N  
ATOM   3146  CA  GLY B 121       9.246  50.633  26.552  1.00 56.99           C  
ANISOU 3146  CA  GLY B 121     7017   5267   9370    257    753    446       C  
ATOM   3147  C   GLY B 121      10.390  50.266  25.635  1.00 58.05           C  
ANISOU 3147  C   GLY B 121     6886   5368   9804    278    818    285       C  
ATOM   3148  O   GLY B 121      11.465  49.892  26.115  1.00 58.51           O  
ANISOU 3148  O   GLY B 121     6806   5351  10074    445    641    251       O  
ATOM   3149  N   TYR B 122      10.167  50.333  24.309  1.00 58.14           N  
ANISOU 3149  N   TYR B 122     6831   5418   9841    117   1067    169       N  
ATOM   3150  CA  TYR B 122      11.207  49.999  23.325  1.00 58.45           C  
ANISOU 3150  CA  TYR B 122     6643   5413  10154     96   1216    -14       C  
ATOM   3151  C   TYR B 122      12.055  51.214  22.934  1.00 58.79           C  
ANISOU 3151  C   TYR B 122     6507   5553  10277     -2   1253   -142       C  
ATOM   3152  O   TYR B 122      13.049  51.034  22.231  1.00 59.35           O  
ANISOU 3152  O   TYR B 122     6366   5572  10615    -31   1405   -322       O  
ATOM   3153  CB  TYR B 122      10.597  49.441  22.017  1.00 58.38           C  
ANISOU 3153  CB  TYR B 122     6702   5384  10096    -45   1497   -101       C  
ATOM   3154  CG  TYR B 122       9.534  48.368  22.145  1.00 59.39           C  
ANISOU 3154  CG  TYR B 122     7001   5421  10144    -20   1535    -22       C  
ATOM   3155  CD1 TYR B 122       9.532  47.481  23.214  1.00 60.48           C  
ANISOU 3155  CD1 TYR B 122     7203   5415  10361    152   1404    103       C  
ATOM   3156  CD2 TYR B 122       8.593  48.173  21.142  1.00 59.98           C  
ANISOU 3156  CD2 TYR B 122     7181   5525  10084   -165   1710    -94       C  
ATOM   3157  CE1 TYR B 122       8.571  46.485  23.322  1.00 61.19           C  
ANISOU 3157  CE1 TYR B 122     7457   5383  10409    150   1501    162       C  
ATOM   3158  CE2 TYR B 122       7.666  47.142  21.212  1.00 60.54           C  
ANISOU 3158  CE2 TYR B 122     7360   5492  10149   -161   1772    -75       C  
ATOM   3159  CZ  TYR B 122       7.648  46.309  22.312  1.00 61.70           C  
ANISOU 3159  CZ  TYR B 122     7565   5483  10395    -16   1696     54       C  
ATOM   3160  OH  TYR B 122       6.724  45.295  22.407  1.00 62.90           O  
ANISOU 3160  OH  TYR B 122     7835   5497  10566    -33   1810     67       O  
ATOM   3161  N   LEU B 123      11.626  52.444  23.319  1.00 58.47           N  
ANISOU 3161  N   LEU B 123     6558   5632  10026    -75   1166    -70       N  
ATOM   3162  CA  LEU B 123      12.199  53.733  22.934  1.00 58.06           C  
ANISOU 3162  CA  LEU B 123     6399   5653  10006   -204   1243   -171       C  
ATOM   3163  C   LEU B 123      13.330  54.248  23.793  1.00 59.35           C  
ANISOU 3163  C   LEU B 123     6324   5820  10407   -116   1047   -261       C  
ATOM   3164  O   LEU B 123      13.246  54.246  25.020  1.00 59.64           O  
ANISOU 3164  O   LEU B 123     6399   5875  10386     28    753   -168       O  
ATOM   3165  CB  LEU B 123      11.101  54.811  22.863  1.00 56.79           C  
ANISOU 3165  CB  LEU B 123     6463   5593   9523   -322   1252    -58       C  
ATOM   3166  CG  LEU B 123       9.819  54.447  22.117  1.00 55.92           C  
ANISOU 3166  CG  LEU B 123     6578   5492   9176   -393   1363     11       C  
ATOM   3167  CD1 LEU B 123       8.884  55.625  22.053  1.00 55.87           C  
ANISOU 3167  CD1 LEU B 123     6739   5565   8925   -480   1331     90       C  
ATOM   3168  CD2 LEU B 123      10.109  53.940  20.731  1.00 55.58           C  
ANISOU 3168  CD2 LEU B 123     6536   5404   9179   -488   1618   -113       C  
ATOM   3169  N   GLU B 124      14.375  54.754  23.114  1.00 59.99           N  
ANISOU 3169  N   GLU B 124     6171   5876  10745   -221   1230   -464       N  
ATOM   3170  CA  GLU B 124      15.561  55.381  23.705  1.00 60.52           C  
ANISOU 3170  CA  GLU B 124     5933   5938  11124   -183   1095   -636       C  
ATOM   3171  C   GLU B 124      15.462  56.932  23.674  1.00 59.93           C  
ANISOU 3171  C   GLU B 124     5904   5937  10931   -357   1173   -652       C  
ATOM   3172  O   GLU B 124      16.200  57.602  24.392  1.00 60.48           O  
ANISOU 3172  O   GLU B 124     5761   6023  11197   -329   1004   -777       O  
ATOM   3173  CB  GLU B 124      16.835  54.932  22.966  1.00 63.54           C  
ANISOU 3173  CB  GLU B 124     5976   6207  11958   -211   1311   -906       C  
ATOM   3174  CG  GLU B 124      17.116  53.448  23.094  1.00 72.43           C  
ANISOU 3174  CG  GLU B 124     7001   7229  13291    -13   1208   -923       C  
ATOM   3175  CD  GLU B 124      18.286  52.940  22.267  1.00 83.87           C  
ANISOU 3175  CD  GLU B 124     8101   8547  15221    -46   1464  -1217       C  
ATOM   3176  OE1 GLU B 124      18.369  51.709  22.034  1.00 85.25           O  
ANISOU 3176  OE1 GLU B 124     8234   8614  15544     73   1488  -1236       O  
ATOM   3177  OE2 GLU B 124      19.122  53.778  21.853  1.00 88.21           O  
ANISOU 3177  OE2 GLU B 124     8412   9079  16023   -201   1673  -1445       O  
ATOM   3178  N   THR B 125      14.570  57.499  22.851  1.00 58.72           N  
ANISOU 3178  N   THR B 125     6025   5812  10474   -524   1406   -542       N  
ATOM   3179  CA  THR B 125      14.451  58.948  22.728  1.00 58.11           C  
ANISOU 3179  CA  THR B 125     6026   5761  10294   -681   1503   -542       C  
ATOM   3180  C   THR B 125      13.278  59.501  23.544  1.00 57.37           C  
ANISOU 3180  C   THR B 125     6165   5756   9876   -634   1275   -342       C  
ATOM   3181  O   THR B 125      12.118  59.334  23.188  1.00 57.04           O  
ANISOU 3181  O   THR B 125     6386   5740   9548   -645   1303   -184       O  
ATOM   3182  CB  THR B 125      14.422  59.358  21.242  1.00 58.69           C  
ANISOU 3182  CB  THR B 125     6258   5764  10278   -892   1917   -575       C  
ATOM   3183  OG1 THR B 125      15.577  58.818  20.590  1.00 59.98           O  
ANISOU 3183  OG1 THR B 125     6179   5829  10783   -950   2170   -801       O  
ATOM   3184  CG2 THR B 125      14.367  60.852  21.048  1.00 58.18           C  
ANISOU 3184  CG2 THR B 125     6312   5676  10119  -1052   2049   -561       C  
ATOM   3185  N   TRP B 126      13.619  60.194  24.626  1.00 56.88           N  
ANISOU 3185  N   TRP B 126     5986   5735   9890   -588   1055   -388       N  
ATOM   3186  CA  TRP B 126      12.695  60.810  25.556  1.00 56.79           C  
ANISOU 3186  CA  TRP B 126     6157   5796   9625   -552    856   -253       C  
ATOM   3187  C   TRP B 126      13.177  62.199  25.929  1.00 57.46           C  
ANISOU 3187  C   TRP B 126     6138   5884   9811   -652    849   -368       C  
ATOM   3188  O   TRP B 126      14.388  62.455  25.962  1.00 57.87           O  
ANISOU 3188  O   TRP B 126     5905   5899  10183   -686    866   -578       O  
ATOM   3189  CB  TRP B 126      12.648  59.997  26.860  1.00 56.08           C  
ANISOU 3189  CB  TRP B 126     6068   5746   9493   -349    522   -200       C  
ATOM   3190  CG  TRP B 126      11.925  58.698  26.762  1.00 55.74           C  
ANISOU 3190  CG  TRP B 126     6187   5680   9312   -249    518    -55       C  
ATOM   3191  CD1 TRP B 126      12.456  57.491  26.421  1.00 56.55           C  
ANISOU 3191  CD1 TRP B 126     6185   5716   9585   -157    535    -91       C  
ATOM   3192  CD2 TRP B 126      10.543  58.460  27.067  1.00 55.35           C  
ANISOU 3192  CD2 TRP B 126     6412   5649   8970   -235    508    121       C  
ATOM   3193  NE1 TRP B 126      11.483  56.519  26.462  1.00 56.84           N  
ANISOU 3193  NE1 TRP B 126     6435   5725   9437    -95    548     64       N  
ATOM   3194  CE2 TRP B 126      10.305  57.082  26.878  1.00 56.27           C  
ANISOU 3194  CE2 TRP B 126     6587   5705   9089   -146    534    186       C  
ATOM   3195  CE3 TRP B 126       9.489  59.274  27.496  1.00 55.15           C  
ANISOU 3195  CE3 TRP B 126     6566   5667   8722   -293    498    204       C  
ATOM   3196  CZ2 TRP B 126       9.056  56.507  27.093  1.00 56.44           C  
ANISOU 3196  CZ2 TRP B 126     6833   5705   8906   -132    568    321       C  
ATOM   3197  CZ3 TRP B 126       8.249  58.706  27.689  1.00 55.88           C  
ANISOU 3197  CZ3 TRP B 126     6859   5743   8627   -273    530    326       C  
ATOM   3198  CH2 TRP B 126       8.040  57.339  27.492  1.00 56.12           C  
ANISOU 3198  CH2 TRP B 126     6939   5711   8671   -201    571    379       C  
ATOM   3199  N   GLY B 127      12.234  63.062  26.292  1.00 56.96           N  
ANISOU 3199  N   GLY B 127     6274   5852   9517   -693    812   -258       N  
ATOM   3200  CA  GLY B 127      12.589  64.372  26.804  1.00 56.79           C  
ANISOU 3200  CA  GLY B 127     6172   5824   9582   -779    785   -366       C  
ATOM   3201  C   GLY B 127      12.783  64.330  28.315  1.00 56.42           C  
ANISOU 3201  C   GLY B 127     6055   5860   9524   -649    438   -426       C  
ATOM   3202  O   GLY B 127      12.599  63.285  28.958  1.00 56.45           O  
ANISOU 3202  O   GLY B 127     6119   5908   9420   -487    229   -350       O  
ATOM   3203  N   GLN B 128      13.140  65.481  28.893  1.00 56.07           N  
ANISOU 3203  N   GLN B 128     5919   5817   9568   -723    380   -563       N  
ATOM   3204  CA  GLN B 128      13.385  65.662  30.328  1.00 56.41           C  
ANISOU 3204  CA  GLN B 128     5921   5938   9573   -621     42   -660       C  
ATOM   3205  C   GLN B 128      12.085  65.782  31.183  1.00 55.60           C  
ANISOU 3205  C   GLN B 128     6139   5889   9098   -572    -58   -491       C  
ATOM   3206  O   GLN B 128      12.118  65.618  32.402  1.00 55.81           O  
ANISOU 3206  O   GLN B 128     6242   5979   8986   -464   -334   -523       O  
ATOM   3207  CB  GLN B 128      14.323  66.886  30.535  1.00 59.56           C  
ANISOU 3207  CB  GLN B 128     6067   6306  10255   -746     48   -926       C  
ATOM   3208  CG  GLN B 128      13.649  68.285  30.715  1.00 65.57           C  
ANISOU 3208  CG  GLN B 128     6969   7034  10909   -889    174   -918       C  
ATOM   3209  CD  GLN B 128      12.925  68.894  29.515  1.00 69.95           C  
ANISOU 3209  CD  GLN B 128     7694   7476  11406  -1033    543   -765       C  
ATOM   3210  OE1 GLN B 128      13.150  68.496  28.359  1.00 73.75           O  
ANISOU 3210  OE1 GLN B 128     8163   7889  11968  -1083    772   -714       O  
ATOM   3211  NE2 GLN B 128      12.014  69.850  29.777  1.00 66.51           N  
ANISOU 3211  NE2 GLN B 128     7447   7008  10815  -1088    591   -693       N  
ATOM   3212  N   GLY B 129      10.978  66.085  30.524  1.00 54.37           N  
ANISOU 3212  N   GLY B 129     6171   5693   8794   -653    170   -335       N  
ATOM   3213  CA  GLY B 129       9.677  66.289  31.128  1.00 54.27           C  
ANISOU 3213  CA  GLY B 129     6409   5697   8512   -639    159   -214       C  
ATOM   3214  C   GLY B 129       9.402  67.729  31.499  1.00 53.64           C  
ANISOU 3214  C   GLY B 129     6349   5591   8441   -746    205   -300       C  
ATOM   3215  O   GLY B 129      10.331  68.475  31.770  1.00 53.27           O  
ANISOU 3215  O   GLY B 129     6132   5540   8569   -805    149   -481       O  
ATOM   3216  N   THR B 130       8.117  68.129  31.527  1.00 53.45           N  
ANISOU 3216  N   THR B 130     6507   5533   8270   -773    308   -200       N  
ATOM   3217  CA  THR B 130       7.695  69.477  31.942  1.00 53.18           C  
ANISOU 3217  CA  THR B 130     6506   5448   8251   -860    360   -280       C  
ATOM   3218  C   THR B 130       6.515  69.346  32.928  1.00 52.97           C  
ANISOU 3218  C   THR B 130     6674   5445   8009   -818    332   -243       C  
ATOM   3219  O   THR B 130       5.570  68.615  32.666  1.00 53.05           O  
ANISOU 3219  O   THR B 130     6792   5444   7921   -771    400   -116       O  
ATOM   3220  CB  THR B 130       7.457  70.424  30.735  1.00 53.62           C  
ANISOU 3220  CB  THR B 130     6554   5373   8446   -957    571   -236       C  
ATOM   3221  OG1 THR B 130       7.539  71.789  31.166  1.00 53.56           O  
ANISOU 3221  OG1 THR B 130     6519   5292   8539  -1049    611   -361       O  
ATOM   3222  CG2 THR B 130       6.129  70.159  30.009  1.00 53.90           C  
ANISOU 3222  CG2 THR B 130     6745   5358   8377   -913    657    -66       C  
ATOM   3223  N   GLN B 131       6.608  70.011  34.082  1.00 52.42           N  
ANISOU 3223  N   GLN B 131     6645   5399   7874   -846    249   -382       N  
ATOM   3224  CA  GLN B 131       5.610  69.935  35.139  1.00 52.52           C  
ANISOU 3224  CA  GLN B 131     6865   5421   7671   -832    267   -386       C  
ATOM   3225  C   GLN B 131       4.371  70.764  34.860  1.00 52.67           C  
ANISOU 3225  C   GLN B 131     6915   5333   7765   -895    468   -381       C  
ATOM   3226  O   GLN B 131       4.461  71.985  34.690  1.00 52.85           O  
ANISOU 3226  O   GLN B 131     6855   5282   7945   -969    523   -475       O  
ATOM   3227  CB  GLN B 131       6.239  70.336  36.489  1.00 54.00           C  
ANISOU 3227  CB  GLN B 131     7119   5675   7724   -839     89   -562       C  
ATOM   3228  CG  GLN B 131       5.279  70.410  37.666  1.00 57.59           C  
ANISOU 3228  CG  GLN B 131     7838   6121   7922   -856    156   -601       C  
ATOM   3229  CD  GLN B 131       4.848  69.049  38.127  1.00 63.93           C  
ANISOU 3229  CD  GLN B 131     8884   6946   8461   -766    149   -457       C  
ATOM   3230  OE1 GLN B 131       5.664  68.187  38.434  1.00 66.41           O  
ANISOU 3230  OE1 GLN B 131     9262   7322   8648   -661    -69   -412       O  
ATOM   3231  NE2 GLN B 131       3.549  68.821  38.204  1.00 65.57           N  
ANISOU 3231  NE2 GLN B 131     9228   7078   8609   -804    395   -397       N  
ATOM   3232  N   VAL B 132       3.211  70.107  34.865  1.00 52.20           N  
ANISOU 3232  N   VAL B 132     6966   5245   7624   -862    578   -293       N  
ATOM   3233  CA  VAL B 132       1.927  70.766  34.702  1.00 52.91           C  
ANISOU 3233  CA  VAL B 132     7054   5224   7824   -895    742   -322       C  
ATOM   3234  C   VAL B 132       1.222  70.652  36.056  1.00 55.02           C  
ANISOU 3234  C   VAL B 132     7493   5490   7922   -929    841   -423       C  
ATOM   3235  O   VAL B 132       1.088  69.540  36.573  1.00 55.70           O  
ANISOU 3235  O   VAL B 132     7735   5618   7812   -898    857   -363       O  
ATOM   3236  CB  VAL B 132       1.106  70.133  33.554  1.00 52.45           C  
ANISOU 3236  CB  VAL B 132     6944   5117   7866   -841    801   -196       C  
ATOM   3237  CG1 VAL B 132      -0.347  70.609  33.574  1.00 52.37           C  
ANISOU 3237  CG1 VAL B 132     6910   4992   7998   -847    933   -265       C  
ATOM   3238  CG2 VAL B 132       1.761  70.419  32.203  1.00 52.35           C  
ANISOU 3238  CG2 VAL B 132     6832   5084   7976   -825    738   -106       C  
ATOM   3239  N   THR B 133       0.861  71.789  36.675  1.00 55.59           N  
ANISOU 3239  N   THR B 133     7572   5498   8053  -1001    925   -581       N  
ATOM   3240  CA  THR B 133       0.208  71.787  37.979  1.00 56.84           C  
ANISOU 3240  CA  THR B 133     7923   5638   8036  -1059   1069   -709       C  
ATOM   3241  C   THR B 133      -1.152  72.422  37.864  1.00 59.25           C  
ANISOU 3241  C   THR B 133     8142   5796   8574  -1099   1297   -809       C  
ATOM   3242  O   THR B 133      -1.269  73.563  37.432  1.00 59.22           O  
ANISOU 3242  O   THR B 133     7987   5704   8812  -1110   1298   -880       O  
ATOM   3243  CB  THR B 133       1.029  72.561  39.007  1.00 57.36           C  
ANISOU 3243  CB  THR B 133     8084   5757   7953  -1116    970   -871       C  
ATOM   3244  OG1 THR B 133       2.362  72.069  39.015  1.00 58.69           O  
ANISOU 3244  OG1 THR B 133     8257   6052   7991  -1058    704   -815       O  
ATOM   3245  CG2 THR B 133       0.450  72.469  40.396  1.00 57.19           C  
ANISOU 3245  CG2 THR B 133     8345   5723   7662  -1182   1122   -999       C  
ATOM   3246  N   VAL B 134      -2.187  71.669  38.205  1.00 61.19           N  
ANISOU 3246  N   VAL B 134     8472   5992   8788  -1116   1498   -824       N  
ATOM   3247  CA  VAL B 134      -3.547  72.172  38.170  1.00 63.59           C  
ANISOU 3247  CA  VAL B 134     8648   6141   9370  -1151   1727   -969       C  
ATOM   3248  C   VAL B 134      -4.046  72.248  39.614  1.00 67.38           C  
ANISOU 3248  C   VAL B 134     9351   6575   9675  -1271   1998  -1154       C  
ATOM   3249  O   VAL B 134      -4.232  71.231  40.270  1.00 67.04           O  
ANISOU 3249  O   VAL B 134     9543   6548   9383  -1311   2144  -1122       O  
ATOM   3250  CB  VAL B 134      -4.488  71.358  37.268  1.00 62.84           C  
ANISOU 3250  CB  VAL B 134     8399   5986   9490  -1092   1782   -905       C  
ATOM   3251  CG1 VAL B 134      -5.783  72.131  37.051  1.00 63.12           C  
ANISOU 3251  CG1 VAL B 134     8211   5850   9920  -1092   1926  -1090       C  
ATOM   3252  CG2 VAL B 134      -3.833  71.031  35.938  1.00 62.30           C  
ANISOU 3252  CG2 VAL B 134     8219   5990   9463   -985   1519   -706       C  
ATOM   3253  N   SER B 135      -4.172  73.459  40.132  1.00 70.75           N  
ANISOU 3253  N   SER B 135     9749   6934  10200  -1333   2076  -1343       N  
ATOM   3254  CA  SER B 135      -4.547  73.688  41.516  1.00 74.20           C  
ANISOU 3254  CA  SER B 135    10426   7325  10443  -1463   2344  -1549       C  
ATOM   3255  C   SER B 135      -5.347  74.982  41.608  1.00 77.86           C  
ANISOU 3255  C   SER B 135    10689   7624  11271  -1513   2524  -1792       C  
ATOM   3256  O   SER B 135      -5.076  75.936  40.869  1.00 78.15           O  
ANISOU 3256  O   SER B 135    10498   7619  11575  -1448   2346  -1783       O  
ATOM   3257  CB  SER B 135      -3.281  73.791  42.362  1.00 75.60           C  
ANISOU 3257  CB  SER B 135    10879   7647  10199  -1487   2149  -1543       C  
ATOM   3258  OG  SER B 135      -3.562  74.095  43.715  1.00 79.11           O  
ANISOU 3258  OG  SER B 135    11614   8053  10391  -1614   2381  -1752       O  
ATOM   3259  N   SER B 136      -6.354  75.009  42.486  1.00 80.48           N  
ANISOU 3259  N   SER B 136    11111   7832  11635  -1630   2904  -2013       N  
ATOM   3260  CA  SER B 136      -7.171  76.210  42.661  1.00 83.42           C  
ANISOU 3260  CA  SER B 136    11279   8023  12394  -1677   3108  -2282       C  
ATOM   3261  C   SER B 136      -6.465  77.247  43.534  1.00 85.36           C  
ANISOU 3261  C   SER B 136    11691   8296  12447  -1763   3091  -2439       C  
ATOM   3262  O   SER B 136      -5.509  76.907  44.240  1.00 85.81           O  
ANISOU 3262  O   SER B 136    12066   8512  12027  -1806   2968  -2382       O  
ATOM   3263  CB  SER B 136      -8.556  75.863  43.212  1.00 85.89           C  
ANISOU 3263  CB  SER B 136    11570   8168  12895  -1784   3567  -2508       C  
ATOM   3264  OG  SER B 136      -8.508  75.134  44.428  1.00 89.22           O  
ANISOU 3264  OG  SER B 136    12424   8628  12848  -1936   3852  -2559       O  
ATOM   3265  N   LEU B 137      -6.909  78.521  43.430  1.00 86.29           N  
ANISOU 3265  N   LEU B 137    11578   8248  12961  -1770   3174  -2643       N  
ATOM   3266  CA  LEU B 137      -6.412  79.705  44.159  1.00 87.77           C  
ANISOU 3266  CA  LEU B 137    11847   8408  13094  -1860   3196  -2852       C  
ATOM   3267  C   LEU B 137      -5.165  80.335  43.522  1.00 88.66           C  
ANISOU 3267  C   LEU B 137    11877   8605  13205  -1787   2812  -2710       C  
ATOM   3268  O   LEU B 137      -4.633  79.816  42.541  1.00 89.18           O  
ANISOU 3268  O   LEU B 137    11853   8759  13271  -1672   2542  -2440       O  
ATOM   3269  CB  LEU B 137      -6.193  79.451  45.672  1.00 88.07           C  
ANISOU 3269  CB  LEU B 137    12313   8529  12620  -2030   3409  -3030       C  
TER    3270      LEU B 137                                                      
HETATM 3271  C1  Q4T A 401       2.657   6.403  18.247  1.00 53.99           C  
ANISOU 3271  C1  Q4T A 401     7376   5807   7332    415    978    -12       C  
HETATM 3272  C2  Q4T A 401       3.092   5.376  17.416  1.00 54.68           C  
ANISOU 3272  C2  Q4T A 401     7505   5852   7419    439   1016    -37       C  
HETATM 3273  C3  Q4T A 401       2.655   4.078  17.622  1.00 55.29           C  
ANISOU 3273  C3  Q4T A 401     7641   5877   7490    454   1004    -32       C  
HETATM 3274  C11 Q4T A 401       0.161   9.357  20.491  1.00 50.32           C  
ANISOU 3274  C11 Q4T A 401     6845   5435   6842    312    878     60       C  
HETATM 3275  C12 Q4T A 401       0.538   9.296  21.836  1.00 50.18           C  
ANISOU 3275  C12 Q4T A 401     6815   5423   6829    352    855     76       C  
HETATM 3276  C13 Q4T A 401      -0.679  10.526  19.975  1.00 49.65           C  
ANISOU 3276  C13 Q4T A 401     6745   5373   6747    259    871     61       C  
HETATM 3277  C16 Q4T A 401      -1.666  11.660  17.974  1.00 50.26           C  
ANISOU 3277  C16 Q4T A 401     6854   5452   6793    192    865     44       C  
HETATM 3278  C17 Q4T A 401      -1.124  12.316  16.839  1.00 50.53           C  
ANISOU 3278  C17 Q4T A 401     6907   5492   6802    186    889     32       C  
HETATM 3279  C18 Q4T A 401      -1.917  13.206  16.109  1.00 50.38           C  
ANISOU 3279  C18 Q4T A 401     6914   5471   6756    154    862     33       C  
HETATM 3280  C19 Q4T A 401      -3.221  13.472  16.514  1.00 50.57           C  
ANISOU 3280  C19 Q4T A 401     6925   5493   6798    128    808     40       C  
HETATM 3281  C20 Q4T A 401      -3.764  12.851  17.640  1.00 50.71           C  
ANISOU 3281  C20 Q4T A 401     6909   5506   6853    129    798     49       C  
HETATM 3282  C21 Q4T A 401      -2.987  11.931  18.360  1.00 50.74           C  
ANISOU 3282  C21 Q4T A 401     6908   5507   6866    160    829     54       C  
HETATM 3283  C22 Q4T A 401       0.297  12.024  16.320  1.00 50.65           C  
ANISOU 3283  C22 Q4T A 401     6923   5505   6818    217    950     15       C  
HETATM 3284  C23 Q4T A 401       0.171  10.859  15.376  1.00 50.74           C  
ANISOU 3284  C23 Q4T A 401     7010   5473   6797    224    965     -4       C  
HETATM 3285  C27 Q4T A 401       0.289   2.058  19.642  1.00 56.34           C  
ANISOU 3285  C27 Q4T A 401     7893   5898   7615    424    949     39       C  
HETATM 3286  C28 Q4T A 401      -1.057   2.350  18.908  1.00 56.51           C  
ANISOU 3286  C28 Q4T A 401     7927   5913   7633    345    945     28       C  
HETATM 3287  C30 Q4T A 401      -0.981   0.179  17.804  1.00 56.09           C  
ANISOU 3287  C30 Q4T A 401     7977   5747   7588    364    969    -13       C  
HETATM 3288  C4  Q4T A 401       1.777   3.783  18.643  1.00 54.98           C  
ANISOU 3288  C4  Q4T A 401     7622   5822   7445    441    965      1       C  
HETATM 3289  C5  Q4T A 401       1.356   4.815  19.495  1.00 54.11           C  
ANISOU 3289  C5  Q4T A 401     7471   5755   7332    419    936     27       C  
HETATM 3290  C6  Q4T A 401       1.753   6.125  19.274  1.00 53.03           C  
ANISOU 3290  C6  Q4T A 401     7275   5674   7200    405    937     19       C  
HETATM 3291  C7  Q4T A 401       1.276   8.235  22.363  1.00 50.25           C  
ANISOU 3291  C7  Q4T A 401     6847   5404   6843    410    848     77       C  
HETATM 3292  C8  Q4T A 401       1.688   7.205  21.522  1.00 51.02           C  
ANISOU 3292  C8  Q4T A 401     6968   5467   6950    427    874     60       C  
HETATM 3293  C9  Q4T A 401       1.303   7.208  20.178  1.00 51.81           C  
ANISOU 3293  C9  Q4T A 401     7082   5559   7042    384    906     42       C  
HETATM 3294  C10 Q4T A 401       0.536   8.267  19.665  1.00 51.38           C  
ANISOU 3294  C10 Q4T A 401     7016   5532   6974    329    904     43       C  
HETATM 3295  N14 Q4T A 401      -0.906  10.667  18.645  1.00 49.78           N  
ANISOU 3295  N14 Q4T A 401     6788   5380   6747    232    882     45       N  
HETATM 3296  O15 Q4T A 401      -1.143  11.293  20.804  1.00 49.10           O  
ANISOU 3296  O15 Q4T A 401     6649   5324   6681    248    851     76       O  
HETATM 3297  O24 Q4T A 401       0.097  10.949  14.159  1.00 50.47           O  
ANISOU 3297  O24 Q4T A 401     7044   5418   6716    213    984    -17       O  
HETATM 3298  O25 Q4T A 401       0.037   9.707  16.004  1.00 51.21           O  
ANISOU 3298  O25 Q4T A 401     7070   5511   6875    243    950     -4       O  
HETATM 3299  O26 Q4T A 401       1.411   2.445  18.814  1.00 55.68           O  
ANISOU 3299  O26 Q4T A 401     7775   5847   7535    454    965      7       O  
HETATM 3300  N29 Q4T A 401      -1.087   1.641  17.610  1.00 56.36           N  
ANISOU 3300  N29 Q4T A 401     7953   5854   7606    336    954    -12       N  
HETATM 3301  C31 Q4T A 401       0.343  -0.189  18.530  1.00 56.04           C  
ANISOU 3301  C31 Q4T A 401     7961   5743   7587    445    982      3       C  
HETATM 3302  C32 Q4T A 401       0.407   0.532  19.897  1.00 56.16           C  
ANISOU 3302  C32 Q4T A 401     7938   5798   7601    460    961     45       C  
HETATM 3303  F33 Q4T A 401      -3.933  14.356  15.840  1.00 50.98           F  
ANISOU 3303  F33 Q4T A 401     6997   5540   6832    107    771     39       F  
HETATM 3304  F34 Q4T A 401       0.209   8.184  18.372  1.00 51.53           F  
ANISOU 3304  F34 Q4T A 401     7070   5536   6975    299    922     24       F  
HETATM 3305 CL1  Q4T A 401       3.228   2.790  16.603  1.00 56.71          CL  
ANISOU 3305 CL1  Q4T A 401     7878   5998   7670    489   1051    -69      CL  
HETATM 3306  F36 Q4T A 401       3.073   7.647  17.992  1.00 54.05           F  
ANISOU 3306  F36 Q4T A 401     7330   5857   7349    398    992    -19       F  
HETATM 3307  C10 OLC A 402     -12.532  30.551  29.212  1.00 69.41           C  
ANISOU 3307  C10 OLC A 402     8817   7930   9627    149    840    -39       C  
HETATM 3308  C9  OLC A 402     -13.768  31.030  28.997  1.00 69.71           C  
ANISOU 3308  C9  OLC A 402     8795   7935   9754    152    848    -55       C  
HETATM 3309  C11 OLC A 402     -11.214  31.239  28.958  1.00 69.19           C  
ANISOU 3309  C11 OLC A 402     8824   7922   9541    148    784    -36       C  
HETATM 3310  C8  OLC A 402     -14.167  32.387  28.465  1.00 69.94           C  
ANISOU 3310  C8  OLC A 402     8793   7942   9838    164    797    -71       C  
HETATM 3311  C24 OLC A 402      -8.093  41.088  25.299  1.00 71.88           C  
ANISOU 3311  C24 OLC A 402     9270   8020  10019     84    556    -44       C  
HETATM 3312  C12 OLC A 402     -10.205  30.143  28.533  1.00 68.98           C  
ANISOU 3312  C12 OLC A 402     8823   7924   9462    137    767    -14       C  
HETATM 3313  C7  OLC A 402     -15.216  33.019  29.412  1.00 69.96           C  
ANISOU 3313  C7  OLC A 402     8764   7914   9904    186    864   -103       C  
HETATM 3314  C6  OLC A 402     -14.949  34.535  29.601  1.00 70.41           C  
ANISOU 3314  C6  OLC A 402     8840   7957   9955    206    835   -121       C  
HETATM 3315  C5  OLC A 402     -13.449  34.893  29.410  1.00 70.97           C  
ANISOU 3315  C5  OLC A 402     8974   8055   9935    195    782   -105       C  
HETATM 3316  C4  OLC A 402     -13.251  36.316  28.811  1.00 71.56           C  
ANISOU 3316  C4  OLC A 402     9051   8103  10035    200    722   -111       C  
HETATM 3317  C3  OLC A 402     -13.009  36.243  27.278  1.00 72.37           C  
ANISOU 3317  C3  OLC A 402     9150   8200  10146    184    647    -78       C  
HETATM 3318  C2  OLC A 402     -12.443  37.553  26.659  1.00 73.28           C  
ANISOU 3318  C2  OLC A 402     9298   8287  10258    182    598    -72       C  
HETATM 3319  C21 OLC A 402      -9.212  39.294  26.752  1.00 73.04           C  
ANISOU 3319  C21 OLC A 402     9360   8247  10144    126    582    -74       C  
HETATM 3320  C1  OLC A 402     -11.034  37.831  27.126  1.00 74.19           C  
ANISOU 3320  C1  OLC A 402     9455   8421  10312    161    609    -75       C  
HETATM 3321  C22 OLC A 402      -8.117  39.591  25.689  1.00 72.57           C  
ANISOU 3321  C22 OLC A 402     9328   8171  10072     90    571    -46       C  
HETATM 3322  O19 OLC A 402     -10.747  37.590  28.290  1.00 75.16           O  
ANISOU 3322  O19 OLC A 402     9586   8567  10406    167    646    -99       O  
HETATM 3323  O25 OLC A 402      -6.812  41.614  25.668  1.00 71.10           O  
ANISOU 3323  O25 OLC A 402     9173   7915   9928     52    572    -66       O  
HETATM 3324  O23 OLC A 402      -6.813  39.293  26.203  1.00 72.64           O  
ANISOU 3324  O23 OLC A 402     9330   8208  10061     66    586    -64       O  
HETATM 3325  O20 OLC A 402     -10.158  38.337  26.218  1.00 73.69           O  
ANISOU 3325  O20 OLC A 402     9423   8343  10234    139    577    -53       O  
HETATM 3326  C10 OLC A 403     -13.472  31.462  23.589  1.00 60.18           C  
ANISOU 3326  C10 OLC A 403     7594   6696   8575    124    539      0       C  
HETATM 3327  C9  OLC A 403     -13.692  32.788  23.743  1.00 61.32           C  
ANISOU 3327  C9  OLC A 403     7735   6818   8746    142    522     -9       C  
HETATM 3328  C11 OLC A 403     -14.441  30.326  23.815  1.00 59.33           C  
ANISOU 3328  C11 OLC A 403     7431   6584   8528    119    562    -15       C  
HETATM 3329  C8  OLC A 403     -14.954  33.520  24.161  1.00 62.41           C  
ANISOU 3329  C8  OLC A 403     7810   6922   8981    168    517    -38       C  
HETATM 3330  C24 OLC A 403     -18.747  44.300  21.426  1.00 80.46           C  
ANISOU 3330  C24 OLC A 403    10209   8735  11628    486     38    -75       C  
HETATM 3331  C12 OLC A 403     -13.721  28.953  23.889  1.00 58.87           C  
ANISOU 3331  C12 OLC A 403     7404   6554   8411     97    596      1       C  
HETATM 3332  C7  OLC A 403     -14.574  34.956  24.581  1.00 63.81           C  
ANISOU 3332  C7  OLC A 403     8012   7085   9147    182    522    -43       C  
HETATM 3333  C6  OLC A 403     -15.459  36.072  23.955  1.00 65.58           C  
ANISOU 3333  C6  OLC A 403     8220   7257   9441    214    452    -52       C  
HETATM 3334  C5  OLC A 403     -15.583  37.306  24.918  1.00 67.55           C  
ANISOU 3334  C5  OLC A 403     8460   7487   9719    233    489    -76       C  
HETATM 3335  C4  OLC A 403     -14.517  38.440  24.739  1.00 69.17           C  
ANISOU 3335  C4  OLC A 403     8738   7679   9864    227    473    -58       C  
HETATM 3336  C3  OLC A 403     -15.029  39.839  25.207  1.00 70.83           C  
ANISOU 3336  C3  OLC A 403     8938   7843  10130    258    470    -84       C  
HETATM 3337  C2  OLC A 403     -14.329  40.993  24.429  1.00 73.11           C  
ANISOU 3337  C2  OLC A 403     9300   8091  10387    255    422    -58       C  
HETATM 3338  C21 OLC A 403     -16.623  43.313  22.555  1.00 78.43           C  
ANISOU 3338  C21 OLC A 403     9989   8592  11217    374    219    -55       C  
HETATM 3339  C1  OLC A 403     -15.165  42.227  24.107  1.00 75.24           C  
ANISOU 3339  C1  OLC A 403     9569   8294  10725    298    370    -67       C  
HETATM 3340  C22 OLC A 403     -18.068  43.031  22.018  1.00 79.50           C  
ANISOU 3340  C22 OLC A 403    10058   8697  11450    426    131    -75       C  
HETATM 3341  O19 OLC A 403     -15.016  43.287  24.702  1.00 75.29           O  
ANISOU 3341  O19 OLC A 403     9586   8271  10748    307    391    -86       O  
HETATM 3342  O25 OLC A 403     -17.739  45.219  20.929  1.00 81.08           O  
ANISOU 3342  O25 OLC A 403    10413   8778  11617    471     38    -31       O  
HETATM 3343  O23 OLC A 403     -18.136  41.941  21.073  1.00 79.50           O  
ANISOU 3343  O23 OLC A 403    10073   8717  11416    415     75    -54       O  
HETATM 3344  O20 OLC A 403     -16.053  42.091  23.098  1.00 77.15           O  
ANISOU 3344  O20 OLC A 403     9803   8503  11007    329    288    -56       O  
HETATM 3345  C8  OLC A 404     -20.880  10.675  28.973  1.00 71.48           C  
ANISOU 3345  C8  OLC A 404     8877   7480  10801   -357   1755      3       C  
HETATM 3346  C24 OLC A 404     -16.037   5.014  26.852  1.00 79.64           C  
ANISOU 3346  C24 OLC A 404    10435   8473  11353   -269   1518    128       C  
HETATM 3347  C7  OLC A 404     -19.468  10.064  28.790  1.00 71.88           C  
ANISOU 3347  C7  OLC A 404     9075   7570  10667   -315   1692     50       C  
HETATM 3348  C6  OLC A 404     -18.649  10.810  27.694  1.00 72.39           C  
ANISOU 3348  C6  OLC A 404     9132   7727  10645   -273   1504     36       C  
HETATM 3349  C5  OLC A 404     -17.753   9.842  26.867  1.00 72.74           C  
ANISOU 3349  C5  OLC A 404     9245   7777  10613   -262   1417     45       C  
HETATM 3350  C4  OLC A 404     -16.347  10.454  26.664  1.00 73.16           C  
ANISOU 3350  C4  OLC A 404     9379   7921  10497   -198   1324     72       C  
HETATM 3351  C3  OLC A 404     -15.241   9.375  26.617  1.00 74.02           C  
ANISOU 3351  C3  OLC A 404     9599   8026  10498   -171   1315    105       C  
HETATM 3352  C2  OLC A 404     -15.231   8.626  25.263  1.00 75.33           C  
ANISOU 3352  C2  OLC A 404     9740   8173  10708   -193   1221     68       C  
HETATM 3353  C21 OLC A 404     -14.984   5.953  24.675  1.00 78.66           C  
ANISOU 3353  C21 OLC A 404    10254   8476  11158   -225   1247     67       C  
HETATM 3354  C1  OLC A 404     -13.858   8.082  24.935  1.00 76.77           C  
ANISOU 3354  C1  OLC A 404    10019   8386  10765   -147   1173     92       C  
HETATM 3355  C22 OLC A 404     -14.850   4.936  25.848  1.00 79.43           C  
ANISOU 3355  C22 OLC A 404    10446   8507  11227   -222   1380    119       C  
HETATM 3356  O19 OLC A 404     -12.881   8.823  24.999  1.00 76.55           O  
ANISOU 3356  O19 OLC A 404    10023   8427  10635    -99   1131    109       O  
HETATM 3357  O25 OLC A 404     -15.747   4.200  28.004  1.00 79.68           O  
ANISOU 3357  O25 OLC A 404    10563   8418  11295   -253   1643    186       O  
HETATM 3358  O23 OLC A 404     -14.725   3.592  25.340  1.00 79.88           O  
ANISOU 3358  O23 OLC A 404    10544   8497  11310   -241   1376    109       O  
HETATM 3359  O20 OLC A 404     -13.787   6.765  24.577  1.00 78.03           O  
ANISOU 3359  O20 OLC A 404    10217   8486  10943   -163   1181     87       O  
HETATM 3360  C10 OLC A 405       1.419  27.580  31.403  1.00 87.14           C  
ANISOU 3360  C10 OLC A 405    11148  10346  11615    279    400   -164       C  
HETATM 3361  C9  OLC A 405       1.464  28.853  31.860  1.00 87.29           C  
ANISOU 3361  C9  OLC A 405    11157  10354  11657    268    370   -200       C  
HETATM 3362  C11 OLC A 405       2.565  26.597  31.252  1.00 86.62           C  
ANISOU 3362  C11 OLC A 405    11047  10286  11580    307    363   -177       C  
HETATM 3363  C8  OLC A 405       0.275  29.791  31.972  1.00 87.16           C  
ANISOU 3363  C8  OLC A 405    11174  10327  11615    246    412   -188       C  
HETATM 3364  C24 OLC A 405       7.098  40.950  31.791  1.00 88.28           C  
ANISOU 3364  C24 OLC A 405    10746  10108  12688   -106    157   -671       C  
HETATM 3365  C12 OLC A 405       2.027  25.195  30.852  1.00 86.31           C  
ANISOU 3365  C12 OLC A 405    11051  10252  11491    319    414   -127       C  
HETATM 3366  C7  OLC A 405       0.669  31.143  32.616  1.00 86.94           C  
ANISOU 3366  C7  OLC A 405    11136  10281  11617    243    358   -242       C  
HETATM 3367  C13 OLC A 405       0.977  24.657  31.870  1.00 86.24           C  
ANISOU 3367  C13 OLC A 405    11152  10235  11379    354    426   -100       C  
HETATM 3368  C6  OLC A 405       1.187  32.148  31.557  1.00 87.07           C  
ANISOU 3368  C6  OLC A 405    11065  10282  11736    185    375   -252       C  
HETATM 3369  C14 OLC A 405       0.712  23.126  31.726  1.00 86.05           C  
ANISOU 3369  C14 OLC A 405    11176  10205  11313    376    460    -61       C  
HETATM 3370  C5  OLC A 405       2.743  32.235  31.589  1.00 87.45           C  
ANISOU 3370  C5  OLC A 405    11036  10324  11868    183    313   -303       C  
HETATM 3371  C4  OLC A 405       3.325  33.454  30.811  1.00 87.54           C  
ANISOU 3371  C4  OLC A 405    10968  10305  11990    122    335   -325       C  
HETATM 3372  C3  OLC A 405       4.243  34.360  31.680  1.00 87.60           C  
ANISOU 3372  C3  OLC A 405    10938  10286  12061    126    246   -403       C  
HETATM 3373  C2  OLC A 405       4.673  35.607  30.861  1.00 88.07           C  
ANISOU 3373  C2  OLC A 405    10926  10304  12233     57    291   -416       C  
HETATM 3374  C21 OLC A 405       5.654  38.876  32.317  1.00 88.59           C  
ANISOU 3374  C21 OLC A 405    10931  10258  12472      6    150   -583       C  
HETATM 3375  C1  OLC A 405       5.462  36.652  31.626  1.00 88.62           C  
ANISOU 3375  C1  OLC A 405    10950  10337  12385     48    209   -497       C  
HETATM 3376  C22 OLC A 405       6.976  39.408  31.706  1.00 88.50           C  
ANISOU 3376  C22 OLC A 405    10791  10201  12633    -57    162   -627       C  
HETATM 3377  O19 OLC A 405       6.387  36.365  32.375  1.00 89.10           O  
ANISOU 3377  O19 OLC A 405    10969  10398  12486     78    113   -559       O  
HETATM 3378  O25 OLC A 405       8.499  41.277  31.797  1.00 88.32           O  
ANISOU 3378  O25 OLC A 405    10623  10071  12862   -145    119   -746       O  
HETATM 3379  O23 OLC A 405       8.082  38.793  32.378  1.00 88.61           O  
ANISOU 3379  O23 OLC A 405    10733  10224  12710    -25     60   -694       O  
HETATM 3380  O20 OLC A 405       5.077  37.918  31.407  1.00 88.50           O  
ANISOU 3380  O20 OLC A 405    10943  10283  12402      6    241   -501       O  
HETATM 3381  C24 OLC A 406       5.578  14.088  26.712  1.00 97.35           C  
ANISOU 3381  C24 OLC A 406    12477  11552  12960    541    555    -33       C  
HETATM 3382  C7  OLC A 406      10.047  25.181  27.046  1.00 96.10           C  
ANISOU 3382  C7  OLC A 406    11625  11430  13457    260    445   -359       C  
HETATM 3383  C6  OLC A 406      10.045  23.682  26.631  1.00 96.15           C  
ANISOU 3383  C6  OLC A 406    11666  11446  13421    303    473   -330       C  
HETATM 3384  C5  OLC A 406       8.764  22.936  27.098  1.00 96.15           C  
ANISOU 3384  C5  OLC A 406    11806  11468  13260    335    447   -273       C  
HETATM 3385  C4  OLC A 406       9.034  21.429  27.344  1.00 96.35           C  
ANISOU 3385  C4  OLC A 406    11859  11492  13258    403    412   -267       C  
HETATM 3386  C3  OLC A 406       7.701  20.648  27.447  1.00 96.77           C  
ANISOU 3386  C3  OLC A 406    12045  11555  13169    411    439   -201       C  
HETATM 3387  C2  OLC A 406       7.841  19.374  28.329  1.00 97.35           C  
ANISOU 3387  C2  OLC A 406    12179  11620  13191    491    365   -196       C  
HETATM 3388  C21 OLC A 406       6.460  16.465  26.556  1.00 97.59           C  
ANISOU 3388  C21 OLC A 406    12356  11625  13100    487    537    -92       C  
HETATM 3389  C1  OLC A 406       7.785  18.085  27.534  1.00 97.84           C  
ANISOU 3389  C1  OLC A 406    12264  11671  13240    502    429   -168       C  
HETATM 3390  C22 OLC A 406       6.764  15.025  27.047  1.00 97.69           C  
ANISOU 3390  C22 OLC A 406    12417  11611  13088    559    497    -86       C  
HETATM 3391  O19 OLC A 406       8.715  17.735  26.815  1.00 98.24           O  
ANISOU 3391  O19 OLC A 406    12235  11712  13380    509    459   -195       O  
HETATM 3392  O25 OLC A 406       6.030  12.729  26.810  1.00 97.02           O  
ANISOU 3392  O25 OLC A 406    12471  11478  12916    601    537    -30       O  
HETATM 3393  O23 OLC A 406       8.000  14.509  26.505  1.00 97.85           O  
ANISOU 3393  O23 OLC A 406    12356  11619  13203    591    503   -123       O  
HETATM 3394  O20 OLC A 406       6.658  17.361  27.666  1.00 97.62           O  
ANISOU 3394  O20 OLC A 406    12346  11639  13105    503    456   -116       O  
HETATM 3395  C18 OLC A 407     -15.094  27.245  29.119  1.00 67.86           C  
ANISOU 3395  C18 OLC A 407     8525   7675   9584    105    986    -30       C  
HETATM 3396  C10 OLC A 407     -19.627  31.982  21.714  1.00 75.00           C  
ANISOU 3396  C10 OLC A 407     9145   8381  10970    213    265   -136       C  
HETATM 3397  C9  OLC A 407     -19.563  31.019  20.764  1.00 76.37           C  
ANISOU 3397  C9  OLC A 407     9347   8553  11115    199    197   -132       C  
HETATM 3398  C17 OLC A 407     -15.516  28.524  28.356  1.00 68.13           C  
ANISOU 3398  C17 OLC A 407     8504   7701   9680    114    909    -49       C  
HETATM 3399  C11 OLC A 407     -18.932  31.942  23.054  1.00 73.44           C  
ANISOU 3399  C11 OLC A 407     8962   8224  10718    191    406   -122       C  
HETATM 3400  C8  OLC A 407     -20.262  31.006  19.409  1.00 77.23           C  
ANISOU 3400  C8  OLC A 407     9461   8617  11267    227     38   -152       C  
HETATM 3401  C24 OLC A 407     -20.655  37.907  12.180  1.00 85.75           C  
ANISOU 3401  C24 OLC A 407    11309   9307  11966    601   -821    -16       C  
HETATM 3402  C16 OLC A 407     -16.530  28.204  27.222  1.00 68.54           C  
ANISOU 3402  C16 OLC A 407     8475   7723   9842    100    852    -63       C  
HETATM 3403  C12 OLC A 407     -19.055  30.495  23.605  1.00 72.09           C  
ANISOU 3403  C12 OLC A 407     8757   8069  10564    156    489   -128       C  
HETATM 3404  C7  OLC A 407     -19.299  31.389  18.254  1.00 77.91           C  
ANISOU 3404  C7  OLC A 407     9697   8703  11200    241    -37   -108       C  
HETATM 3405  C15 OLC A 407     -17.578  29.338  27.049  1.00 69.08           C  
ANISOU 3405  C15 OLC A 407     8469   7759  10018    119    824    -95       C  
HETATM 3406  C13 OLC A 407     -17.951  30.216  24.660  1.00 71.11           C  
ANISOU 3406  C13 OLC A 407     8698   7989  10330    138    601   -100       C  
HETATM 3407  C6  OLC A 407     -19.065  32.922  18.080  1.00 78.74           C  
ANISOU 3407  C6  OLC A 407     9862   8786  11270    278    -71    -87       C  
HETATM 3408  C14 OLC A 407     -18.386  29.175  25.730  1.00 70.02           C  
ANISOU 3408  C14 OLC A 407     8522   7850  10233    116    720   -111       C  
HETATM 3409  C5  OLC A 407     -20.371  33.759  18.102  1.00 79.89           C  
ANISOU 3409  C5  OLC A 407     9918   8879  11558    325   -153   -128       C  
HETATM 3410  C4  OLC A 407     -20.829  34.153  16.667  1.00 81.42           C  
ANISOU 3410  C4  OLC A 407    10183   9013  11739    376   -332   -131       C  
HETATM 3411  C3  OLC A 407     -20.091  33.328  15.567  1.00 82.76           C  
ANISOU 3411  C3  OLC A 407    10484   9191  11770    361   -378   -103       C  
HETATM 3412  C2  OLC A 407     -20.895  33.135  14.237  1.00 83.61           C  
ANISOU 3412  C2  OLC A 407    10637   9238  11893    409   -569   -129       C  
HETATM 3413  C21 OLC A 407     -20.423  35.487  12.965  1.00 85.33           C  
ANISOU 3413  C21 OLC A 407    11098   9366  11956    499   -694    -60       C  
HETATM 3414  C1  OLC A 407     -20.012  33.161  12.997  1.00 84.27           C  
ANISOU 3414  C1  OLC A 407    10922   9305  11792    421   -619    -82       C  
HETATM 3415  C22 OLC A 407     -20.417  36.440  11.746  1.00 85.71           C  
ANISOU 3415  C22 OLC A 407    11321   9338  11905    564   -823    -27       C  
HETATM 3416  O19 OLC A 407     -19.750  32.146  12.352  1.00 84.08           O  
ANISOU 3416  O19 OLC A 407    10958   9288  11701    404   -642    -85       O  
HETATM 3417  O25 OLC A 407     -22.028  38.261  11.930  1.00 85.94           O  
ANISOU 3417  O25 OLC A 407    11258   9271  12124    673   -989    -67       O  
HETATM 3418  O23 OLC A 407     -19.170  36.298  11.036  1.00 86.04           O  
ANISOU 3418  O23 OLC A 407    11546   9387  11759    538   -759     33       O  
HETATM 3419  O20 OLC A 407     -19.539  34.382  12.667  1.00 84.92           O  
ANISOU 3419  O20 OLC A 407    11117   9358  11792    450   -626    -39       O  
HETATM 3420  C24 OLC A 408      12.491  38.387  29.382  1.00 91.81           C  
ANISOU 3420  C24 OLC A 408    10625  10519  13739   -203    272   -789       C  
HETATM 3421  C3  OLC A 408       9.036  32.630  32.037  1.00 91.98           C  
ANISOU 3421  C3  OLC A 408    11161  10825  12963    181     22   -588       C  
HETATM 3422  C2  OLC A 408       9.168  34.142  32.392  1.00 92.28           C  
ANISOU 3422  C2  OLC A 408    11170  10823  13068    140    -13   -643       C  
HETATM 3423  C21 OLC A 408      10.650  36.780  30.208  1.00 91.89           C  
ANISOU 3423  C21 OLC A 408    10869  10646  13397    -74    194   -690       C  
HETATM 3424  C1  OLC A 408       9.624  34.932  31.190  1.00 92.42           C  
ANISOU 3424  C1  OLC A 408    11087  10805  13224     53     99   -639       C  
HETATM 3425  C22 OLC A 408      11.453  38.086  30.498  1.00 91.91           C  
ANISOU 3425  C22 OLC A 408    10776  10584  13561   -126    153   -774       C  
HETATM 3426  O19 OLC A 408       9.561  34.408  30.086  1.00 92.84           O  
ANISOU 3426  O19 OLC A 408    11122  10867  13286     26    212   -585       O  
HETATM 3427  O25 OLC A 408      12.774  39.800  29.348  1.00 91.73           O  
ANISOU 3427  O25 OLC A 408    10571  10438  13845   -274    296   -829       O  
HETATM 3428  O23 OLC A 408      10.581  39.223  30.642  1.00 92.04           O  
ANISOU 3428  O23 OLC A 408    10875  10574  13521   -154    172   -756       O  
HETATM 3429  O20 OLC A 408      10.098  36.180  31.407  1.00 91.95           O  
ANISOU 3429  O20 OLC A 408    10971  10697  13268      9     70   -698       O  
HETATM 3430  C24 OLC A 409     -20.884  12.574  11.414  1.00 82.49           C  
ANISOU 3430  C24 OLC A 409    10446   8939  11956   -120   -470   -530       C  
HETATM 3431  C5  OLC A 409     -15.185  19.598  11.354  1.00 79.16           C  
ANISOU 3431  C5  OLC A 409    10530   8842  10704     88   -169   -148       C  
HETATM 3432  C4  OLC A 409     -16.528  19.051  10.804  1.00 79.37           C  
ANISOU 3432  C4  OLC A 409    10510   8811  10837     90   -317   -216       C  
HETATM 3433  C3  OLC A 409     -16.932  17.689  11.434  1.00 79.90           C  
ANISOU 3433  C3  OLC A 409    10479   8867  11012     45   -272   -249       C  
HETATM 3434  C2  OLC A 409     -17.311  16.676  10.317  1.00 80.77           C  
ANISOU 3434  C2  OLC A 409    10664   8921  11103     49   -386   -303       C  
HETATM 3435  C21 OLC A 409     -19.072  13.524   9.844  1.00 82.15           C  
ANISOU 3435  C21 OLC A 409    10720   8957  11536    -28   -531   -464       C  
HETATM 3436  C1  OLC A 409     -18.154  15.513  10.784  1.00 81.73           C  
ANISOU 3436  C1  OLC A 409    10668   9006  11380      5   -392   -355       C  
HETATM 3437  C22 OLC A 409     -19.386  12.536  11.002  1.00 82.32           C  
ANISOU 3437  C22 OLC A 409    10605   8968  11704    -89   -408   -469       C  
HETATM 3438  O19 OLC A 409     -18.984  15.662  11.664  1.00 82.21           O  
ANISOU 3438  O19 OLC A 409    10580   9062  11595    -20   -366   -369       O  
HETATM 3439  O25 OLC A 409     -21.400  11.232  11.562  1.00 82.56           O  
ANISOU 3439  O25 OLC A 409    10389   8888  12092   -174   -453   -579       O  
HETATM 3440  O23 OLC A 409     -19.001  11.200  10.642  1.00 82.40           O  
ANISOU 3440  O23 OLC A 409    10683   8947  11680   -109   -390   -489       O  
HETATM 3441  O20 OLC A 409     -17.915  14.326  10.179  1.00 82.06           O  
ANISOU 3441  O20 OLC A 409    10782   9015  11382     -5   -415   -385       O  
HETATM 3442  C24 OLC A 410     -24.185   6.926  18.615  1.00101.42           C  
ANISOU 3442  C24 OLC A 410    12172  11018  15345   -546    540   -529       C  
HETATM 3443  C4  OLC A 410     -23.291  15.636  19.373  1.00100.28           C  
ANISOU 3443  C4  OLC A 410    12007  11277  14818   -237    356   -388       C  
HETATM 3444  C3  OLC A 410     -24.146  14.336  19.460  1.00100.55           C  
ANISOU 3444  C3  OLC A 410    11954  11231  15020   -300    401   -435       C  
HETATM 3445  C2  OLC A 410     -23.508  13.105  18.744  1.00100.83           C  
ANISOU 3445  C2  OLC A 410    12090  11251  14970   -315    348   -436       C  
HETATM 3446  C21 OLC A 410     -23.888   9.492  18.983  1.00101.49           C  
ANISOU 3446  C21 OLC A 410    12170  11169  15222   -452    505   -475       C  
HETATM 3447  C1  OLC A 410     -24.287  11.814  18.923  1.00101.14           C  
ANISOU 3447  C1  OLC A 410    12049  11204  15176   -381    404   -480       C  
HETATM 3448  C22 OLC A 410     -23.739   8.284  18.010  1.00101.74           C  
ANISOU 3448  C22 OLC A 410    12256  11150  15251   -473    409   -517       C  
HETATM 3449  O19 OLC A 410     -25.268  11.758  19.651  1.00101.19           O  
ANISOU 3449  O19 OLC A 410    11921  11159  15368   -421    498   -508       O  
HETATM 3450  O25 OLC A 410     -24.982   6.246  17.627  1.00101.15           O  
ANISOU 3450  O25 OLC A 410    12066  10905  15463   -581    400   -623       O  
HETATM 3451  O23 OLC A 410     -24.454   8.505  16.781  1.00102.17           O  
ANISOU 3451  O23 OLC A 410    12252  11174  15393   -464    201   -602       O  
HETATM 3452  O20 OLC A 410     -23.833  10.738  18.244  1.00101.32           O  
ANISOU 3452  O20 OLC A 410    12157  11205  15136   -394    355   -488       O  
HETATM 3453  C18 OLC A 411       1.903  21.444   2.482  1.00 83.10           C  
ANISOU 3453  C18 OLC A 411    12462   9149   9965    127   1600    168       C  
HETATM 3454  C10 OLC A 411      -4.244  15.161   3.499  1.00 84.21           C  
ANISOU 3454  C10 OLC A 411    12465   9364  10166    218    664    -67       C  
HETATM 3455  C9  OLC A 411      -5.527  14.784   3.613  1.00 84.51           C  
ANISOU 3455  C9  OLC A 411    12475   9392  10243    217    499    -99       C  
HETATM 3456  C17 OLC A 411       0.991  20.242   2.847  1.00 83.16           C  
ANISOU 3456  C17 OLC A 411    12426   9195   9977    152   1435    129       C  
HETATM 3457  C11 OLC A 411      -3.387  15.222   2.258  1.00 83.94           C  
ANISOU 3457  C11 OLC A 411    12625   9279   9988    244    774    -63       C  
HETATM 3458  C8  OLC A 411      -6.480  14.333   2.534  1.00 84.91           C  
ANISOU 3458  C8  OLC A 411    12676   9378  10208    244    353   -145       C  
HETATM 3459  C24 OLC A 411     -14.143   8.468   2.825  1.00 90.22           C  
ANISOU 3459  C24 OLC A 411    12945   9790  11545    133   -616   -583       C  
HETATM 3460  C16 OLC A 411       1.249  18.993   1.962  1.00 83.24           C  
ANISOU 3460  C16 OLC A 411    12553   9172   9902    182   1485     93       C  
HETATM 3461  C12 OLC A 411      -1.904  14.988   2.656  1.00 83.81           C  
ANISOU 3461  C12 OLC A 411    12534   9289  10019    233    972    -49       C  
HETATM 3462  C7  OLC A 411      -7.901  14.852   2.885  1.00 85.53           C  
ANISOU 3462  C7  OLC A 411    12680   9454  10362    238    173   -158       C  
HETATM 3463  C15 OLC A 411       0.897  17.685   2.721  1.00 83.53           C  
ANISOU 3463  C15 OLC A 411    12457   9259  10021    190   1388     51       C  
HETATM 3464  C13 OLC A 411      -1.219  16.274   3.199  1.00 83.75           C  
ANISOU 3464  C13 OLC A 411    12444   9313  10064    210   1072      0       C  
HETATM 3465  C6  OLC A 411      -8.779  13.759   3.562  1.00 86.15           C  
ANISOU 3465  C6  OLC A 411    12620   9538  10575    214     81   -206       C  
HETATM 3466  C14 OLC A 411      -0.331  16.950   2.112  1.00 83.74           C  
ANISOU 3466  C14 OLC A 411    12609   9259   9951    219   1221     23       C  
HETATM 3467  C5  OLC A 411     -10.271  13.858   3.133  1.00 86.64           C  
ANISOU 3467  C5  OLC A 411    12696   9555  10669    224   -130   -253       C  
HETATM 3468  C4  OLC A 411     -11.063  14.957   3.904  1.00 87.09           C  
ANISOU 3468  C4  OLC A 411    12612   9641  10836    211   -194   -231       C  
HETATM 3469  C3  OLC A 411     -12.556  14.995   3.464  1.00 87.59           C  
ANISOU 3469  C3  OLC A 411    12671   9653  10957    226   -410   -288       C  
HETATM 3470  C2  OLC A 411     -12.928  13.810   2.523  1.00 88.25           C  
ANISOU 3470  C2  OLC A 411    12864   9672  10995    240   -516   -359       C  
HETATM 3471  C21 OLC A 411     -14.733  10.850   3.677  1.00 89.67           C  
ANISOU 3471  C21 OLC A 411    12731   9797  11543    143   -640   -505       C  
HETATM 3472  C1  OLC A 411     -14.154  13.034   2.958  1.00 88.93           C  
ANISOU 3472  C1  OLC A 411    12801   9734  11255    211   -642   -426       C  
HETATM 3473  C22 OLC A 411     -15.248   9.533   3.041  1.00 89.96           C  
ANISOU 3473  C22 OLC A 411    12811   9761  11609    134   -745   -589       C  
HETATM 3474  O19 OLC A 411     -15.087  13.591   3.521  1.00 89.06           O  
ANISOU 3474  O19 OLC A 411    12679   9757  11404    199   -721   -434       O  
HETATM 3475  O25 OLC A 411     -14.777   7.211   2.496  1.00 90.39           O  
ANISOU 3475  O25 OLC A 411    12964   9742  11639    112   -712   -665       O  
HETATM 3476  O23 OLC A 411     -16.287   8.982   3.867  1.00 90.04           O  
ANISOU 3476  O23 OLC A 411    12624   9752  11835     82   -789   -629       O  
HETATM 3477  O20 OLC A 411     -14.126  11.707   2.683  1.00 89.40           O  
ANISOU 3477  O20 OLC A 411    12889   9758  11320    197   -652   -476       O  
HETATM 3478  C10 OLC A 412      -1.837   8.894  -0.634  1.00 91.36           C  
ANISOU 3478  C10 OLC A 412    14006  10026  10682    354    941   -296       C  
HETATM 3479  C9  OLC A 412      -2.788   7.962  -0.822  1.00 91.65           C  
ANISOU 3479  C9  OLC A 412    14076  10029  10719    357    788   -349       C  
HETATM 3480  C8  OLC A 412      -4.264   8.214  -1.064  1.00 92.04           C  
ANISOU 3480  C8  OLC A 412    14149  10058  10762    349    566   -370       C  
HETATM 3481  C24 OLC A 412     -12.931  -0.130  -0.367  1.00 98.94           C  
ANISOU 3481  C24 OLC A 412    14622  10490  12482    127   -636   -961       C  
HETATM 3482  C7  OLC A 412      -5.093   6.934  -0.767  1.00 92.52           C  
ANISOU 3482  C7  OLC A 412    14150  10095  10909    335    441   -431       C  
HETATM 3483  C6  OLC A 412      -6.434   7.269  -0.057  1.00 93.12           C  
ANISOU 3483  C6  OLC A 412    14091  10188  11103    302    260   -437       C  
HETATM 3484  C5  OLC A 412      -7.374   6.039   0.068  1.00 93.88           C  
ANISOU 3484  C5  OLC A 412    14150  10240  11282    284    130   -506       C  
HETATM 3485  C4  OLC A 412      -8.722   6.232  -0.687  1.00 94.94           C  
ANISOU 3485  C4  OLC A 412    14368  10317  11387    292    -94   -562       C  
HETATM 3486  C3  OLC A 412      -9.970   5.851   0.170  1.00 96.06           C  
ANISOU 3486  C3  OLC A 412    14319  10457  11721    244   -229   -594       C  
HETATM 3487  C2  OLC A 412     -11.249   5.623  -0.694  1.00 97.21           C  
ANISOU 3487  C2  OLC A 412    14548  10526  11860    254   -461   -678       C  
HETATM 3488  C21 OLC A 412     -12.951   2.451   0.028  1.00 98.67           C  
ANISOU 3488  C21 OLC A 412    14517  10581  12391    154   -632   -846       C  
HETATM 3489  C1  OLC A 412     -12.303   4.742  -0.042  1.00 98.36           C  
ANISOU 3489  C1  OLC A 412    14528  10644  12202    203   -563   -733       C  
HETATM 3490  C22 OLC A 412     -12.338   1.256  -0.751  1.00 98.90           C  
ANISOU 3490  C22 OLC A 412    14711  10548  12319    177   -599   -898       C  
HETATM 3491  O19 OLC A 412     -12.823   5.041   1.031  1.00 98.98           O  
ANISOU 3491  O19 OLC A 412    14408  10762  12440    160   -557   -706       O  
HETATM 3492  O25 OLC A 412     -12.289  -1.162  -1.148  1.00 98.96           O  
ANISOU 3492  O25 OLC A 412    14793  10434  12374    157   -601  -1008       O  
HETATM 3493  O23 OLC A 412     -12.461   1.505  -2.162  1.00 99.01           O  
ANISOU 3493  O23 OLC A 412    14949  10508  12161    232   -730   -953       O  
HETATM 3494  O20 OLC A 412     -12.637   3.634  -0.742  1.00 98.51           O  
ANISOU 3494  O20 OLC A 412    14639  10584  12206    206   -656   -816       O  
HETATM 3495  C18 OLC A 413      -3.068  15.377  33.464  1.00 81.54           C  
ANISOU 3495  C18 OLC A 413    11103   9434  10446    464    786    182       C  
HETATM 3496  C10 OLC A 413       4.534  16.253  30.453  1.00 85.68           C  
ANISOU 3496  C10 OLC A 413    11133  10094  11329    588    377    -33       C  
HETATM 3497  C9  OLC A 413       4.638  15.474  31.542  1.00 86.42           C  
ANISOU 3497  C9  OLC A 413    11323  10159  11355    659    319    -22       C  
HETATM 3498  C17 OLC A 413      -1.728  15.665  32.739  1.00 81.79           C  
ANISOU 3498  C17 OLC A 413    11047   9506  10522    483    688    147       C  
HETATM 3499  C11 OLC A 413       3.227  16.744  29.871  1.00 84.95           C  
ANISOU 3499  C11 OLC A 413    11055  10012  11210    512    467      0       C  
HETATM 3500  C8  OLC A 413       5.898  14.931  32.175  1.00 87.00           C  
ANISOU 3500  C8  OLC A 413    11393  10213  11451    747    207    -56       C  
HETATM 3501  C24 OLC A 413       6.784   3.326  31.923  1.00 87.97           C  
ANISOU 3501  C24 OLC A 413    12117   9895  11411   1153    274    166       C  
HETATM 3502  C16 OLC A 413      -1.229  14.435  31.921  1.00 82.28           C  
ANISOU 3502  C16 OLC A 413    11094   9554  10616    491    686    158       C  
HETATM 3503  C12 OLC A 413       2.410  17.487  30.961  1.00 84.44           C  
ANISOU 3503  C12 OLC A 413    11058   9947  11078    511    456      8       C  
HETATM 3504  C7  OLC A 413       5.828  13.381  32.178  1.00 87.64           C  
ANISOU 3504  C7  OLC A 413    11550  10254  11495    791    227    -19       C  
HETATM 3505  C15 OLC A 413       0.311  14.224  32.020  1.00 82.87           C  
ANISOU 3505  C15 OLC A 413    11148   9639  10700    556    587    130       C  
HETATM 3506  C13 OLC A 413       1.361  16.596  31.704  1.00 84.04           C  
ANISOU 3506  C13 OLC A 413    11133   9863  10935    530    497     54       C  
HETATM 3507  C6  OLC A 413       7.068  12.736  31.498  1.00 88.04           C  
ANISOU 3507  C6  OLC A 413    11503  10298  11649    831    191    -56       C  
HETATM 3508  C14 OLC A 413       1.118  15.181  31.084  1.00 83.55           C  
ANISOU 3508  C14 OLC A 413    11100   9773  10871    529    549     87       C  
HETATM 3509  C5  OLC A 413       7.372  11.341  32.111  1.00 88.33           C  
ANISOU 3509  C5  OLC A 413    11641  10284  11637    918    144    -34       C  
HETATM 3510  C4  OLC A 413       8.783  11.305  32.759  1.00 88.52           C  
ANISOU 3510  C4  OLC A 413    11630  10292  11711   1017     -8    -88       C  
HETATM 3511  C3  OLC A 413       9.601  10.087  32.257  1.00 88.67           C  
ANISOU 3511  C3  OLC A 413    11615  10278  11798   1078    -26   -100       C  
HETATM 3512  C2  OLC A 413       8.665   8.898  31.914  1.00 89.02           C  
ANISOU 3512  C2  OLC A 413    11769  10288  11768   1059     79    -34       C  
HETATM 3513  C21 OLC A 413       8.059   5.552  32.275  1.00 88.54           C  
ANISOU 3513  C21 OLC A 413    11992  10077  11573   1170    125     72       C  
HETATM 3514  C1  OLC A 413       9.292   7.564  32.247  1.00 89.39           C  
ANISOU 3514  C1  OLC A 413    11880  10275  11808   1158     17    -27       C  
HETATM 3515  C22 OLC A 413       7.430   4.566  31.250  1.00 88.00           C  
ANISOU 3515  C22 OLC A 413    11940   9981  11513   1116    251    103       C  
HETATM 3516  O19 OLC A 413      10.162   7.463  33.100  1.00 89.91           O  
ANISOU 3516  O19 OLC A 413    11964  10318  11879   1254   -119    -55       O  
HETATM 3517  O25 OLC A 413       7.254   3.187  33.275  1.00 88.01           O  
ANISOU 3517  O25 OLC A 413    12236   9863  11342   1254    160    178       O  
HETATM 3518  O23 OLC A 413       6.517   5.209  30.335  1.00 87.35           O  
ANISOU 3518  O23 OLC A 413    11802   9944  11444   1001    361    109       O  
HETATM 3519  O20 OLC A 413       8.829   6.521  31.532  1.00 89.08           O  
ANISOU 3519  O20 OLC A 413    11880  10206  11760   1137    113      8       O  
HETATM 3520  S   SO4 A 414     -12.878  46.135  31.673  0.50 51.10           S  
HETATM 3521  O1  SO4 A 414     -11.976  45.255  30.950  0.50 51.45           O  
HETATM 3522  O2  SO4 A 414     -13.673  46.873  30.699  0.50 50.98           O  
HETATM 3523  O3  SO4 A 414     -13.743  45.322  32.518  0.50 51.42           O  
HETATM 3524  O4  SO4 A 414     -12.117  47.052  32.512  0.50 51.04           O  
HETATM 3525 CL    CL A 415      -5.075   2.007  17.947  1.00 66.82          CL  
HETATM 3526  O   HOH A 501       6.287  39.702  18.463  1.00 48.78           O  
HETATM 3527  O   HOH A 502      -6.945  10.503  19.171  1.00 51.02           O  
HETATM 3528  O   HOH A 503       5.301  41.742  15.178  1.00 44.67           O  
HETATM 3529  O   HOH A 504      -7.345  53.885  24.763  1.00 41.92           O  
HETATM 3530  O   HOH A 505      -1.148  50.824  25.114  1.00 50.43           O  
HETATM 3531  O   HOH A 506     -11.617  24.944  23.591  1.00 45.29           O  
HETATM 3532  O   HOH A 507      -4.202  50.186  18.273  1.00 47.19           O  
HETATM 3533  O   HOH A 508      -5.324  40.757  28.735  1.00 42.59           O  
HETATM 3534  O   HOH A 509       1.846   0.982  27.406  1.00 54.08           O  
HETATM 3535  O   HOH A 510      -5.746  17.979   8.803  1.00 45.25           O  
HETATM 3536  O   HOH A 511      -2.191  42.266  14.389  1.00 63.43           O  
HETATM 3537  O   HOH A 512      -6.947  11.788  16.974  1.00 55.59           O  
HETATM 3538  O   HOH A 513      -3.843   1.433  25.582  1.00 72.25           O  
HETATM 3539  O   HOH A 514      -0.424  -4.982  25.311  1.00 77.34           O  
HETATM 3540  O   HOH A 515      -2.205   5.146  12.871  1.00 59.06           O  
HETATM 3541  O   HOH A 516      -4.772  -2.286  24.571  1.00 80.02           O  
HETATM 3542  O   HOH A 517     -21.552   0.344  10.090  1.00 75.05           O  
HETATM 3543  O   HOH A 518      -4.829  45.906  16.681  1.00 53.43           O  
HETATM 3544  O   HOH A 519      -5.815  45.097  23.706  1.00 44.44           O  
HETATM 3545  O   HOH A 520      -0.434  45.730  32.461  1.00 53.73           O  
HETATM 3546  O   HOH A 521      -1.311  44.303  27.804  1.00 47.46           O  
HETATM 3547  O   HOH A 522      -9.690  24.871  21.781  1.00 36.46           O  
HETATM 3548  O   HOH A 523      -3.494  12.652  21.507  1.00 41.03           O  
HETATM 3549  O   HOH A 524      -5.029   5.696  12.879  1.00 62.47           O  
HETATM 3550  O   HOH A 525      -8.572  49.396  34.479  1.00 71.70           O  
HETATM 3551  O   HOH A 526       8.489  44.167  10.612  1.00 71.97           O  
HETATM 3552  O   HOH A 527     -19.416  47.116  19.620  1.00 85.44           O  
HETATM 3553  O   HOH A 528      -6.508   8.011  22.348  1.00 34.94           O  
HETATM 3554  O   HOH A 529       6.153  41.313   9.476  1.00 80.38           O  
HETATM 3555  O   HOH A 530       3.853   1.536  11.972  1.00 58.80           O  
HETATM 3556  O   HOH A 531       2.546  43.805  20.572  1.00 48.71           O  
HETATM 3557  O   HOH A 532      -2.115  45.078  15.213  1.00 68.23           O  
HETATM 3558  O   HOH A 533     -15.663   4.487   0.988  1.00 80.70           O  
HETATM 3559  O   HOH A 534       0.047  50.812  11.715  1.00 66.76           O  
HETATM 3560  O   HOH A 535      -6.098  51.428  33.772  1.00 56.14           O  
HETATM 3561  O   HOH A 536     -10.020  -9.812   2.369  1.00 74.93           O  
HETATM 3562  O   HOH A 537      -3.241   8.260  17.050  1.00 43.00           O  
HETATM 3563  O   HOH A 538      -8.954  -5.917  -1.068  1.00 72.70           O  
HETATM 3564  O   HOH A 539      23.334  42.279  13.580  1.00 88.21           O  
HETATM 3565  O   HOH A 540      -3.209  51.857  30.803  1.00 67.81           O  
HETATM 3566  O   HOH A 541       3.040  -7.118  27.653  1.00 59.94           O  
HETATM 3567  O   HOH A 542       5.344  50.117  10.229  1.00 51.87           O  
HETATM 3568  O   HOH A 543     -18.103   2.883   5.773  1.00 67.18           O  
HETATM 3569  O   HOH A 544      -5.229  10.337  20.994  1.00 46.45           O  
HETATM 3570  O   HOH A 545     -18.413  42.717   6.031  1.00 80.23           O  
HETATM 3571  O   HOH A 546     -18.811   1.872   7.868  1.00 60.93           O  
HETATM 3572  O   HOH A 547     -10.088  -1.974  -3.331  1.00 74.67           O  
HETATM 3573  O   HOH A 548       5.755  44.869  12.656  1.00 63.00           O  
HETATM 3574  O   HOH A 549       7.709  42.249  12.759  1.00 71.33           O  
HETATM 3575  O   HOH A 550     -14.189  -1.281  20.510  1.00 78.24           O  
HETATM 3576  O   HOH A 551      11.349   4.519   8.787  1.00 69.00           O  
HETATM 3577  O   HOH A 552       0.716  47.481   6.736  1.00 58.01           O  
HETATM 3578  O   HOH A 553      -8.265  -0.356  10.744  1.00 64.25           O  
HETATM 3579  O   HOH A 554      -7.927  -3.611  30.742  1.00 63.63           O  
HETATM 3580  O   HOH A 555     -11.729  58.998   7.278  1.00100.54           O  
HETATM 3581  O   HOH A 556     -13.221   4.425  30.372  1.00 49.66           O  
HETATM 3582  O   HOH A 557     -23.371  -1.834  14.080  1.00 69.97           O  
HETATM 3583  O   HOH A 558      -9.867  -0.999  13.028  1.00 87.61           O  
HETATM 3584  O   HOH A 559     -16.006  57.726  13.215  1.00 84.71           O  
HETATM 3585  O   HOH A 560     -20.835   3.009   9.174  1.00 76.07           O  
HETATM 3586  O   HOH A 561      -1.732   5.526  16.887  1.00 52.83           O  
HETATM 3587  O   HOH A 562      12.616  10.458   9.808  1.00 76.35           O  
HETATM 3588  O   HOH A 563       5.626  44.413  31.776  1.00 69.44           O  
HETATM 3589  O   HOH A 564       7.069  -7.159  18.843  1.00 64.45           O  
HETATM 3590  O   HOH A 565     -14.895  -3.155   0.953  1.00 75.35           O  
HETATM 3591  O   HOH A 566      14.363  14.932  12.015  1.00 68.60           O  
HETATM 3592  O   HOH A 567      24.876  42.688  15.774  1.00 76.27           O  
HETATM 3593  O   HOH A 568       2.698  40.671  36.514  1.00 78.68           O  
HETATM 3594  O   HOH A 569     -16.728  36.501   8.419  1.00 71.11           O  
HETATM 3595  O   HOH A 570      -8.701  41.500   5.087  1.00 74.49           O  
HETATM 3596  O   HOH A 571      -4.543  -6.110  25.146  1.00 74.13           O  
HETATM 3597  O   HOH A 572     -14.522  25.077   8.622  1.00 55.39           O  
HETATM 3598  O   HOH A 573       6.653  38.550   8.300  1.00 67.75           O  
HETATM 3599  O   HOH A 574     -20.355  26.858  15.719  1.00 58.34           O  
HETATM 3600  O   HOH A 575      25.799  41.665  18.202  1.00 78.65           O  
HETATM 3601  O   HOH A 576     -17.408  56.692  15.301  1.00 75.45           O  
HETATM 3602  O   HOH A 577      15.630  36.459  31.150  1.00 69.69           O  
HETATM 3603  O   HOH A 578     -11.112  -0.946  27.507  1.00 70.12           O  
HETATM 3604  O   HOH A 579     -17.282  -1.403  22.993  1.00 57.09           O  
HETATM 3605  O   HOH A 580     -14.617  29.679   7.306  1.00 67.81           O  
HETATM 3606  O   HOH A 581      10.713   8.541   3.458  1.00 75.85           O  
HETATM 3607  O   HOH A 582       7.612  30.444  10.126  1.00 67.99           O  
HETATM 3608  O   HOH A 583      -4.605  48.800  15.944  1.00 44.34           O  
HETATM 3609  O   HOH A 584       8.943  10.002   2.165  1.00 65.55           O  
HETATM 3610  O   HOH A 585      22.396  38.473  23.425  1.00 71.10           O  
HETATM 3611  O   HOH A 586      12.087   6.457   6.973  1.00 70.91           O  
HETATM 3612  O   HOH A 587      -6.312  41.118  36.782  1.00 45.40           O  
HETATM 3613  O   HOH A 588     -20.290  19.152  15.181  1.00 50.89           O  
HETATM 3614  O   HOH A 589     -19.141   5.105   7.112  1.00 68.99           O  
HETATM 3615  O   HOH A 590      16.417  20.773  15.127  1.00 67.90           O  
HETATM 3616  O   HOH A 591       5.801  15.168   3.588  1.00 58.23           O  
HETATM 3617  O   HOH A 592     -16.032  17.105  25.640  1.00 59.87           O  
HETATM 3618  O   HOH A 593      10.824  32.145  12.358  1.00 54.17           O  
HETATM 3619  O   HOH A 594      -6.968  -6.418  26.325  1.00 85.07           O  
HETATM 3620  O   HOH A 595     -24.931  13.161  14.448  1.00 74.20           O  
HETATM 3621  O   HOH A 596       6.553  11.220   1.900  1.00 62.86           O  
HETATM 3622  O   HOH A 597      21.915  38.424  26.410  1.00 84.88           O  
HETATM 3623  O   HOH A 598     -11.662  46.707   5.491  1.00 68.11           O  
HETATM 3624  O   HOH A 599      -5.779  50.264  13.988  1.00 55.35           O  
HETATM 3625  O   HOH A 600      -1.751  24.132  34.699  1.00 69.73           O  
HETATM 3626  O   HOH A 601       9.634  39.674   3.048  1.00 76.39           O  
HETATM 3627  O   HOH A 602      -1.606  26.629   5.124  1.00 68.20           O  
HETATM 3628  O   HOH A 603     -23.879  15.861  13.844  1.00 66.29           O  
HETATM 3629  O   HOH A 604     -25.206  13.989  24.815  1.00 68.37           O  
HETATM 3630  O   HOH A 605      -2.094  30.335   3.645  1.00 67.26           O  
HETATM 3631  O   HOH A 606     -18.696  18.976   6.857  1.00 75.04           O  
HETATM 3632  O   HOH A 607      -9.225  58.943   5.439  1.00 70.86           O  
HETATM 3633  O   HOH A 609      -2.857  33.381   3.512  1.00 63.09           O  
HETATM 3634  O   HOH B 201       7.502  76.080  31.914  1.00 47.59           O  
HETATM 3635  O   HOH B 202       6.410  43.952  24.538  1.00 45.95           O  
HETATM 3636  O   HOH B 203     -16.789  65.176  28.067  1.00 53.32           O  
HETATM 3637  O   HOH B 204     -11.973  68.419  32.516  1.00 58.24           O  
HETATM 3638  O   HOH B 205      -2.914  55.684  28.981  1.00 48.32           O  
HETATM 3639  O   HOH B 206       5.095  43.444  21.507  1.00 51.07           O  
HETATM 3640  O   HOH B 207      13.873  50.643  19.761  1.00 83.69           O  
HETATM 3641  O   HOH B 208      -6.740  65.155  16.622  1.00 56.20           O  
HETATM 3642  O   HOH B 209      -8.858  55.601  22.845  1.00 50.89           O  
HETATM 3643  O   HOH B 210      -2.426  70.665  19.291  1.00 53.92           O  
HETATM 3644  O   HOH B 211       0.802  58.892  36.320  1.00 54.20           O  
HETATM 3645  O   HOH B 212     -14.462  60.177  24.755  1.00 78.68           O  
HETATM 3646  O   HOH B 213       3.993  75.461  24.146  1.00 55.36           O  
HETATM 3647  O   HOH B 214       4.015  73.421  37.197  1.00 46.62           O  
HETATM 3648  O   HOH B 215      -8.015  57.436  20.159  1.00 57.16           O  
HETATM 3649  O   HOH B 216      12.732  48.760  18.330  1.00 67.89           O  
HETATM 3650  O   HOH B 217       3.904  68.628   9.340  1.00 64.52           O  
HETATM 3651  O   HOH B 218      -0.852  74.695  17.773  1.00 60.52           O  
HETATM 3652  O   HOH B 219      -6.220  60.628  12.883  1.00 61.67           O  
HETATM 3653  O   HOH B 220       4.035  65.801  39.350  1.00 65.27           O  
HETATM 3654  O   HOH B 221       6.707  51.968  11.157  1.00 55.07           O  
HETATM 3655  O   HOH B 222       6.240  53.944  35.516  1.00 74.95           O  
HETATM 3656  O   HOH B 223       8.345  55.676   9.543  1.00 69.20           O  
HETATM 3657  O   HOH B 224      12.848  53.937  10.342  1.00 72.75           O  
HETATM 3658  O   HOH B 225     -10.805  74.982  28.683  1.00 58.72           O  
HETATM 3659  O   HOH B 226      -9.266  59.315  18.250  1.00 65.92           O  
HETATM 3660  O   HOH B 227      -2.838  74.772  19.617  1.00 53.91           O  
HETATM 3661  O   HOH B 228       8.518  56.084  34.167  1.00 67.24           O  
HETATM 3662  O   HOH B 229      -6.922  79.271  30.286  1.00 64.25           O  
HETATM 3663  O   HOH B 230       1.043  55.995  45.605  1.00 66.19           O  
HETATM 3664  O   HOH B 231     -13.364  73.407  36.616  1.00 62.28           O  
HETATM 3665  O   HOH B 232      -7.700  62.670  34.019  1.00 75.20           O  
HETATM 3666  O   HOH B 233      11.702  53.607  28.271  1.00 70.96           O  
HETATM 3667  O   HOH B 234      16.993  69.382  21.920  1.00 56.40           O  
HETATM 3668  O   HOH B 235       6.385  63.640  39.376  1.00 64.08           O  
HETATM 3669  O   HOH B 236       8.674  50.508  30.028  1.00 65.50           O  
HETATM 3670  O   HOH B 237      14.596  53.435  19.652  1.00 60.09           O  
HETATM 3671  O   HOH B 238       9.106  58.276  32.734  1.00 53.10           O  
HETATM 3672  O   HOH B 239      -6.610  63.367  12.573  1.00 68.85           O  
HETATM 3673  O   HOH B 240       4.705  70.457  41.471  1.00 76.73           O  
HETATM 3674  O   HOH B 241      15.658  50.444  24.933  1.00 59.99           O  
HETATM 3675  O   HOH B 242       4.757  59.929   5.605  1.00 67.66           O  
HETATM 3676  O   HOH B 243     -11.602  66.064  33.863  1.00 65.88           O  
HETATM 3677  O   HOH B 244     -15.132  58.863  20.108  1.00 73.09           O  
HETATM 3678  O   HOH B 245      -0.205  70.130  43.351  1.00 54.93           O  
HETATM 3679  O   HOH B 246      14.654  52.398  11.886  1.00 85.60           O  
CONECT    6 1975                                                                
CONECT  690 1323                                                                
CONECT 1323  690                                                                
CONECT 1975    6                                                                
CONECT 2459 3016                                                                
CONECT 2662 3090                                                                
CONECT 3016 2459                                                                
CONECT 3090 2662                                                                
CONECT 3271 3272 3290 3306                                                      
CONECT 3272 3271 3273                                                           
CONECT 3273 3272 3288 3305                                                      
CONECT 3274 3275 3276 3294                                                      
CONECT 3275 3274 3291                                                           
CONECT 3276 3274 3295 3296                                                      
CONECT 3277 3278 3282 3295                                                      
CONECT 3278 3277 3279 3283                                                      
CONECT 3279 3278 3280                                                           
CONECT 3280 3279 3281 3303                                                      
CONECT 3281 3280 3282                                                           
CONECT 3282 3277 3281                                                           
CONECT 3283 3278 3284                                                           
CONECT 3284 3283 3297 3298                                                      
CONECT 3285 3286 3299 3302                                                      
CONECT 3286 3285 3300                                                           
CONECT 3287 3300 3301                                                           
CONECT 3288 3273 3289 3299                                                      
CONECT 3289 3288 3290                                                           
CONECT 3290 3271 3289 3293                                                      
CONECT 3291 3275 3292                                                           
CONECT 3292 3291 3293                                                           
CONECT 3293 3290 3292 3294                                                      
CONECT 3294 3274 3293 3304                                                      
CONECT 3295 3276 3277                                                           
CONECT 3296 3276                                                                
CONECT 3297 3284                                                                
CONECT 3298 3284                                                                
CONECT 3299 3285 3288                                                           
CONECT 3300 3286 3287                                                           
CONECT 3301 3287 3302                                                           
CONECT 3302 3285 3301                                                           
CONECT 3303 3280                                                                
CONECT 3304 3294                                                                
CONECT 3305 3273                                                                
CONECT 3306 3271                                                                
CONECT 3307 3308 3309                                                           
CONECT 3308 3307 3310                                                           
CONECT 3309 3307 3312                                                           
CONECT 3310 3308 3313                                                           
CONECT 3311 3321 3323                                                           
CONECT 3312 3309                                                                
CONECT 3313 3310 3314                                                           
CONECT 3314 3313 3315                                                           
CONECT 3315 3314 3316                                                           
CONECT 3316 3315 3317                                                           
CONECT 3317 3316 3318                                                           
CONECT 3318 3317 3320                                                           
CONECT 3319 3321 3325                                                           
CONECT 3320 3318 3322 3325                                                      
CONECT 3321 3311 3319 3324                                                      
CONECT 3322 3320                                                                
CONECT 3323 3311                                                                
CONECT 3324 3321                                                                
CONECT 3325 3319 3320                                                           
CONECT 3326 3327 3328                                                           
CONECT 3327 3326 3329                                                           
CONECT 3328 3326 3331                                                           
CONECT 3329 3327 3332                                                           
CONECT 3330 3340 3342                                                           
CONECT 3331 3328                                                                
CONECT 3332 3329 3333                                                           
CONECT 3333 3332 3334                                                           
CONECT 3334 3333 3335                                                           
CONECT 3335 3334 3336                                                           
CONECT 3336 3335 3337                                                           
CONECT 3337 3336 3339                                                           
CONECT 3338 3340 3344                                                           
CONECT 3339 3337 3341 3344                                                      
CONECT 3340 3330 3338 3343                                                      
CONECT 3341 3339                                                                
CONECT 3342 3330                                                                
CONECT 3343 3340                                                                
CONECT 3344 3338 3339                                                           
CONECT 3345 3347                                                                
CONECT 3346 3355 3357                                                           
CONECT 3347 3345 3348                                                           
CONECT 3348 3347 3349                                                           
CONECT 3349 3348 3350                                                           
CONECT 3350 3349 3351                                                           
CONECT 3351 3350 3352                                                           
CONECT 3352 3351 3354                                                           
CONECT 3353 3355 3359                                                           
CONECT 3354 3352 3356 3359                                                      
CONECT 3355 3346 3353 3358                                                      
CONECT 3356 3354                                                                
CONECT 3357 3346                                                                
CONECT 3358 3355                                                                
CONECT 3359 3353 3354                                                           
CONECT 3360 3361 3362                                                           
CONECT 3361 3360 3363                                                           
CONECT 3362 3360 3365                                                           
CONECT 3363 3361 3366                                                           
CONECT 3364 3376 3378                                                           
CONECT 3365 3362 3367                                                           
CONECT 3366 3363 3368                                                           
CONECT 3367 3365 3369                                                           
CONECT 3368 3366 3370                                                           
CONECT 3369 3367                                                                
CONECT 3370 3368 3371                                                           
CONECT 3371 3370 3372                                                           
CONECT 3372 3371 3373                                                           
CONECT 3373 3372 3375                                                           
CONECT 3374 3376 3380                                                           
CONECT 3375 3373 3377 3380                                                      
CONECT 3376 3364 3374 3379                                                      
CONECT 3377 3375                                                                
CONECT 3378 3364                                                                
CONECT 3379 3376                                                                
CONECT 3380 3374 3375                                                           
CONECT 3381 3390 3392                                                           
CONECT 3382 3383                                                                
CONECT 3383 3382 3384                                                           
CONECT 3384 3383 3385                                                           
CONECT 3385 3384 3386                                                           
CONECT 3386 3385 3387                                                           
CONECT 3387 3386 3389                                                           
CONECT 3388 3390 3394                                                           
CONECT 3389 3387 3391 3394                                                      
CONECT 3390 3381 3388 3393                                                      
CONECT 3391 3389                                                                
CONECT 3392 3381                                                                
CONECT 3393 3390                                                                
CONECT 3394 3388 3389                                                           
CONECT 3395 3398                                                                
CONECT 3396 3397 3399                                                           
CONECT 3397 3396 3400                                                           
CONECT 3398 3395 3402                                                           
CONECT 3399 3396 3403                                                           
CONECT 3400 3397 3404                                                           
CONECT 3401 3415 3417                                                           
CONECT 3402 3398 3405                                                           
CONECT 3403 3399 3406                                                           
CONECT 3404 3400 3407                                                           
CONECT 3405 3402 3408                                                           
CONECT 3406 3403 3408                                                           
CONECT 3407 3404 3409                                                           
CONECT 3408 3405 3406                                                           
CONECT 3409 3407 3410                                                           
CONECT 3410 3409 3411                                                           
CONECT 3411 3410 3412                                                           
CONECT 3412 3411 3414                                                           
CONECT 3413 3415 3419                                                           
CONECT 3414 3412 3416 3419                                                      
CONECT 3415 3401 3413 3418                                                      
CONECT 3416 3414                                                                
CONECT 3417 3401                                                                
CONECT 3418 3415                                                                
CONECT 3419 3413 3414                                                           
CONECT 3420 3425 3427                                                           
CONECT 3421 3422                                                                
CONECT 3422 3421 3424                                                           
CONECT 3423 3425 3429                                                           
CONECT 3424 3422 3426 3429                                                      
CONECT 3425 3420 3423 3428                                                      
CONECT 3426 3424                                                                
CONECT 3427 3420                                                                
CONECT 3428 3425                                                                
CONECT 3429 3423 3424                                                           
CONECT 3430 3437 3439                                                           
CONECT 3431 3432                                                                
CONECT 3432 3431 3433                                                           
CONECT 3433 3432 3434                                                           
CONECT 3434 3433 3436                                                           
CONECT 3435 3437 3441                                                           
CONECT 3436 3434 3438 3441                                                      
CONECT 3437 3430 3435 3440                                                      
CONECT 3438 3436                                                                
CONECT 3439 3430                                                                
CONECT 3440 3437                                                                
CONECT 3441 3435 3436                                                           
CONECT 3442 3448 3450                                                           
CONECT 3443 3444                                                                
CONECT 3444 3443 3445                                                           
CONECT 3445 3444 3447                                                           
CONECT 3446 3448 3452                                                           
CONECT 3447 3445 3449 3452                                                      
CONECT 3448 3442 3446 3451                                                      
CONECT 3449 3447                                                                
CONECT 3450 3442                                                                
CONECT 3451 3448                                                                
CONECT 3452 3446 3447                                                           
CONECT 3453 3456                                                                
CONECT 3454 3455 3457                                                           
CONECT 3455 3454 3458                                                           
CONECT 3456 3453 3460                                                           
CONECT 3457 3454 3461                                                           
CONECT 3458 3455 3462                                                           
CONECT 3459 3473 3475                                                           
CONECT 3460 3456 3463                                                           
CONECT 3461 3457 3464                                                           
CONECT 3462 3458 3465                                                           
CONECT 3463 3460 3466                                                           
CONECT 3464 3461 3466                                                           
CONECT 3465 3462 3467                                                           
CONECT 3466 3463 3464                                                           
CONECT 3467 3465 3468                                                           
CONECT 3468 3467 3469                                                           
CONECT 3469 3468 3470                                                           
CONECT 3470 3469 3472                                                           
CONECT 3471 3473 3477                                                           
CONECT 3472 3470 3474 3477                                                      
CONECT 3473 3459 3471 3476                                                      
CONECT 3474 3472                                                                
CONECT 3475 3459                                                                
CONECT 3476 3473                                                                
CONECT 3477 3471 3472                                                           
CONECT 3478 3479                                                                
CONECT 3479 3478 3480                                                           
CONECT 3480 3479 3482                                                           
CONECT 3481 3490 3492                                                           
CONECT 3482 3480 3483                                                           
CONECT 3483 3482 3484                                                           
CONECT 3484 3483 3485                                                           
CONECT 3485 3484 3486                                                           
CONECT 3486 3485 3487                                                           
CONECT 3487 3486 3489                                                           
CONECT 3488 3490 3494                                                           
CONECT 3489 3487 3491 3494                                                      
CONECT 3490 3481 3488 3493                                                      
CONECT 3491 3489                                                                
CONECT 3492 3481                                                                
CONECT 3493 3490                                                                
CONECT 3494 3488 3489                                                           
CONECT 3495 3498                                                                
CONECT 3496 3497 3499                                                           
CONECT 3497 3496 3500                                                           
CONECT 3498 3495 3502                                                           
CONECT 3499 3496 3503                                                           
CONECT 3500 3497 3504                                                           
CONECT 3501 3515 3517                                                           
CONECT 3502 3498 3505                                                           
CONECT 3503 3499 3506                                                           
CONECT 3504 3500 3507                                                           
CONECT 3505 3502 3508                                                           
CONECT 3506 3503 3508                                                           
CONECT 3507 3504 3509                                                           
CONECT 3508 3505 3506                                                           
CONECT 3509 3507 3510                                                           
CONECT 3510 3509 3511                                                           
CONECT 3511 3510 3512                                                           
CONECT 3512 3511 3514                                                           
CONECT 3513 3515 3519                                                           
CONECT 3514 3512 3516 3519                                                      
CONECT 3515 3501 3513 3518                                                      
CONECT 3516 3514                                                                
CONECT 3517 3501                                                                
CONECT 3518 3515                                                                
CONECT 3519 3513 3514                                                           
CONECT 3520 3521 3522 3523 3524                                                 
CONECT 3521 3520                                                                
CONECT 3522 3520                                                                
CONECT 3523 3520                                                                
CONECT 3524 3520                                                                
MASTER      453    0   15   18   14    0   30    6 3677    2  262   38          
END