HEADER    MEMBRANE PROTEIN                        11-MAR-13   4JKV              
TITLE     STRUCTURE OF THE HUMAN SMOOTHENED 7TM RECEPTOR IN COMPLEX WITH AN     
TITLE    2 ANTITUMOR AGENT                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUBLE CYTOCHROME B562, SMOOTHENED HOMOLOG;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: BRIL;                                                      
COMPND   5 SYNONYM: CYTOCHROME B-562, SMO, PROTEIN GX;                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 562, 9606;                                           
SOURCE   5 GENE: CYBC, SMO_HUMAN, SMO, SMOH;                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    HUMAN SMOOTHENED RECEPTOR, ANTITUMOR AGENT, NOVEL PROTEIN             
KEYWDS   2 ENGINEERING, GPCR NETWORK, MEMBRANE PROTEIN, PSI-BIOLOGY, STRUCTURAL 
KEYWDS   3 GENOMICS, GPCR, MEMBRANE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.WANG,H.WU,V.KATRITCH,G.W.HAN,X.HUANG,W.LIU,F.Y.SIU,B.L.ROTH,        
AUTHOR   2 V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR)                           
REVDAT   6   15-NOV-17 4JKV    1       REMARK                                   
REVDAT   5   02-AUG-17 4JKV    1       SOURCE REMARK                            
REVDAT   4   27-NOV-13 4JKV    1       REMARK                                   
REVDAT   3   29-MAY-13 4JKV    1       JRNL                                     
REVDAT   2   15-MAY-13 4JKV    1       JRNL                                     
REVDAT   1   24-APR-13 4JKV    0                                                
JRNL        AUTH   C.WANG,H.WU,V.KATRITCH,G.W.HAN,X.P.HUANG,W.LIU,F.Y.SIU,      
JRNL        AUTH 2 B.L.ROTH,V.CHEREZOV,R.C.STEVENS                              
JRNL        TITL   STRUCTURE OF THE HUMAN SMOOTHENED RECEPTOR BOUND TO AN       
JRNL        TITL 2 ANTITUMOUR AGENT.                                            
JRNL        REF    NATURE                        V. 497   338 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   23636324                                                     
JRNL        DOI    10.1038/NATURE12167                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 43776                          
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)  : 0.201                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.231                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2202                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.45                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.51                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.35                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3066                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2383                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2914                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2352                   
REMARK   3   BIN FREE R VALUE                        : 0.2966                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.96                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 152                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7032                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 237                                     
REMARK   3   SOLVENT ATOMS            : 110                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.52                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.77080                                              
REMARK   3    B22 (A**2) : -11.05980                                            
REMARK   3    B33 (A**2) : 1.28900                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.39650                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.402               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.349               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7461   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10113  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3371   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 148    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1084   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7461   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 950    ; 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   : 9119   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.87                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.24                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|-1 - A|106 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.2326    4.7180   43.8814           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0051 T22:    0.2708                                    
REMARK   3     T33:   -0.3585 T12:    0.0209                                    
REMARK   3     T13:   -0.0791 T23:    0.0868                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2165 L22:    2.6123                                    
REMARK   3     L33:    2.7053 L12:   -0.1630                                    
REMARK   3     L13:   -1.0503 L23:    1.7990                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1593 S12:   -0.2825 S13:   -0.0609                     
REMARK   3     S21:    0.1340 S22:    0.0646 S23:    0.0396                     
REMARK   3     S31:    0.4776 S32:    0.2647 S33:    0.0947                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|190 - A|550 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.3911   19.8145   16.6583           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1778 T22:    0.0165                                    
REMARK   3     T33:   -0.1145 T12:    0.0004                                    
REMARK   3     T13:    0.0236 T23:   -0.0964                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1075 L22:    0.6355                                    
REMARK   3     L33:    1.0152 L12:   -0.3825                                    
REMARK   3     L13:    0.9988 L23:   -0.2383                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1032 S12:   -0.4985 S13:    0.2460                     
REMARK   3     S21:    0.1504 S22:    0.0332 S23:    0.1134                     
REMARK   3     S31:    0.0315 S32:   -0.2574 S33:    0.0700                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|0 - B|106 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    6.3134   32.6956  -17.7637           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2185 T22:    0.0822                                    
REMARK   3     T33:   -0.1022 T12:   -0.0264                                    
REMARK   3     T13:    0.0330 T23:    0.1289                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2378 L22:    5.5830                                    
REMARK   3     L33:    2.5364 L12:    0.1832                                    
REMARK   3     L13:    0.0453 L23:    0.7922                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0276 S12:    0.2131 S13:    0.1647                     
REMARK   3     S21:   -0.0621 S22:   -0.0032 S23:   -0.1619                     
REMARK   3     S31:   -0.0226 S32:    0.0523 S33:    0.0308                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B|190 - B|552 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.2107    8.0613  -10.8824           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2549 T22:    0.0543                                    
REMARK   3     T33:   -0.1619 T12:   -0.0399                                    
REMARK   3     T13:    0.0043 T23:   -0.0581                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6964 L22:    1.4472                                    
REMARK   3     L33:    0.8969 L12:    0.8357                                    
REMARK   3     L13:   -0.3105 L23:   -0.0212                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1777 S12:    0.6152 S13:   -0.1398                     
REMARK   3     S21:   -0.1490 S22:    0.1285 S23:    0.1806                     
REMARK   3     S31:    0.0527 S32:   -0.2377 S33:    0.0493                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4JKV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078173.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-12                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43797                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: EXPERIMENTAL PHASING BY USING TA6BR12 SOAK           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.8, 70 MM AMMONIUM     
REMARK 280  FLUORIDE, 32% (V/V) PEG400, 4% 8% (V/V) P400, LIPIDIC CUBIC         
REMARK 280  PHASE (LCP), TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       49.08850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     SER A   354                                                      
REMARK 465     VAL A   494                                                      
REMARK 465     THR A   495                                                      
REMARK 465     ILE A   496                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     THR A   500                                                      
REMARK 465     LYS A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     PRO A   503                                                      
REMARK 465     ILE A   504                                                      
REMARK 465     PRO A   505                                                      
REMARK 465     ASP A   506                                                      
REMARK 465     ARG A   551                                                      
REMARK 465     LEU A   552                                                      
REMARK 465     THR A   553                                                      
REMARK 465     GLY A   554                                                      
REMARK 465     GLN A   555                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B   347                                                      
REMARK 465     THR B   348                                                      
REMARK 465     THR B   349                                                      
REMARK 465     TYR B   350                                                      
REMARK 465     GLN B   351                                                      
REMARK 465     PRO B   352                                                      
REMARK 465     LEU B   353                                                      
REMARK 465     SER B   354                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     THR B   495                                                      
REMARK 465     ILE B   496                                                      
REMARK 465     GLY B   497                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     THR B   500                                                      
REMARK 465     LYS B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     PRO B   503                                                      
REMARK 465     ILE B   504                                                      
REMARK 465     PRO B   505                                                      
REMARK 465     THR B   553                                                      
REMARK 465     GLY B   554                                                      
REMARK 465     GLN B   555                                                      
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     ASP A   5    CG   OD1  OD2                                       
REMARK 470     LYS A  15    CG   CD   CE   NZ                                   
REMARK 470     GLU A 194    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 356    CG   CD   CE   NZ                                   
REMARK 470     GLU A 439    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 493    CG   OD1  ND2                                       
REMARK 470     GLU A 508    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 539    CG   CD   CE   NZ                                   
REMARK 470     ARG A 546    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 547    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 548    OG1  CG2                                            
REMARK 470     GLU B 194    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 258    CG   OD1  ND2                                       
REMARK 470     ARG B 261    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 344    CG   CD   CE   NZ                                   
REMARK 470     LEU B 346    CG   CD1  CD2                                       
REMARK 470     LYS B 356    CG   CD   CE   NZ                                   
REMARK 470     LYS B 444    CG   CD   CE   NZ                                   
REMARK 470     ILE B 445    CG1  CG2  CD1                                       
REMARK 470     MET B 449    CG   SD   CE                                        
REMARK 470     ASN B 493    CG   OD1  ND2                                       
REMARK 470     LYS B 539    CG   CD   CE   NZ                                   
REMARK 470     ARG B 547    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 548    OG1  CG2                                            
REMARK 470     CYS B 550    SG                                                  
REMARK 470     ARG B 551    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 552    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    VAL A  16       59.50   -100.80                                   
REMARK 500    ILE A  17      -54.46   -138.67                                   
REMARK 500    GLU A 208     -128.67     48.34                                   
REMARK 500    THR A 349       98.40    -66.63                                   
REMARK 500    TYR A 350      118.23   -166.74                                   
REMARK 500    LYS A 356     -151.03     52.68                                   
REMARK 500    TYR A 359       74.00   -106.22                                   
REMARK 500    VAL A 404      -59.28   -123.67                                   
REMARK 500    ALA A 441     -110.33   -114.78                                   
REMARK 500    GLN B 103      -39.91    -38.63                                   
REMARK 500    SER B 190      -73.20   -120.90                                   
REMARK 500    GLU B 208     -117.66     51.52                                   
REMARK 500    LYS B 356        9.32     59.05                                   
REMARK 500    SER B 358     -146.78   -123.69                                   
REMARK 500    TYR B 359       43.41    -83.85                                   
REMARK 500    VAL B 404      -57.15   -123.93                                   
REMARK 500    ALA B 442       56.58   -118.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  602                                                       
REMARK 610     OLC A  603                                                       
REMARK 610     OLC A  604                                                       
REMARK 610     OLA A  606                                                       
REMARK 610     OLC B  602                                                       
REMARK 610     OLC B  603                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KS A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KS B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: GPCR-131   RELATED DB: TARGETTRACK                       
DBREF  4JKV A    1   105  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  4JKV A  190   555  UNP    Q99835   SMO_HUMAN      190    555             
DBREF  4JKV B    1   105  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  4JKV B  190   555  UNP    Q99835   SMO_HUMAN      190    555             
SEQADV 4JKV GLY A   -2  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV GLY A   -1  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV THR A    0  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV TRP A    7  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 4JKV ILE A  102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 4JKV LEU A  106  UNP  P0ABE7              LINKER                         
SEQADV 4JKV GLY B   -2  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV GLY B   -1  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV THR B    0  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 4JKV TRP B    7  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 4JKV ILE B  102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 4JKV LEU B  106  UNP  P0ABE7              LINKER                         
SEQRES   1 A  475  GLY GLY THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU          
SEQRES   2 A  475  ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA          
SEQRES   3 A  475  ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA          
SEQRES   4 A  475  ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU          
SEQRES   5 A  475  ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG          
SEQRES   6 A  475  HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA          
SEQRES   7 A  475  LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN          
SEQRES   8 A  475  ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR          
SEQRES   9 A  475  ILE GLN LYS TYR LEU SER GLY GLN CYS GLU VAL PRO LEU          
SEQRES  10 A  475  VAL ARG THR ASP ASN PRO LYS SER TRP TYR GLU ASP VAL          
SEQRES  11 A  475  GLU GLY CYS GLY ILE GLN CYS GLN ASN PRO LEU PHE THR          
SEQRES  12 A  475  GLU ALA GLU HIS GLN ASP MET HIS SER TYR ILE ALA ALA          
SEQRES  13 A  475  PHE GLY ALA VAL THR GLY LEU CYS THR LEU PHE THR LEU          
SEQRES  14 A  475  ALA THR PHE VAL ALA ASP TRP ARG ASN SER ASN ARG TYR          
SEQRES  15 A  475  PRO ALA VAL ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE          
SEQRES  16 A  475  VAL GLY SER ILE GLY TRP LEU ALA GLN PHE MET ASP GLY          
SEQRES  17 A  475  ALA ARG ARG GLU ILE VAL CYS ARG ALA ASP GLY THR MET          
SEQRES  18 A  475  ARG LEU GLY GLU PRO THR SER ASN GLU THR LEU SER CYS          
SEQRES  19 A  475  VAL ILE ILE PHE VAL ILE VAL TYR TYR ALA LEU MET ALA          
SEQRES  20 A  475  GLY VAL VAL TRP PHE VAL VAL LEU THR TYR ALA TRP HIS          
SEQRES  21 A  475  THR SER PHE LYS ALA LEU GLY THR THR TYR GLN PRO LEU          
SEQRES  22 A  475  SER GLY LYS THR SER TYR PHE HIS LEU LEU THR TRP SER          
SEQRES  23 A  475  LEU PRO PHE VAL LEU THR VAL ALA ILE LEU ALA VAL ALA          
SEQRES  24 A  475  GLN VAL ASP GLY ASP SER VAL SER GLY ILE CYS PHE VAL          
SEQRES  25 A  475  GLY TYR LYS ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU          
SEQRES  26 A  475  ALA PRO ILE GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE          
SEQRES  27 A  475  LEU ILE ARG GLY VAL MET THR LEU PHE SER ILE LYS SER          
SEQRES  28 A  475  ASN HIS PRO GLY LEU LEU SER GLU LYS ALA ALA SER LYS          
SEQRES  29 A  475  ILE ASN GLU THR MET LEU ARG LEU GLY ILE PHE GLY PHE          
SEQRES  30 A  475  LEU ALA PHE GLY PHE VAL LEU ILE THR PHE SER CYS HIS          
SEQRES  31 A  475  PHE TYR ASP PHE PHE ASN GLN ALA GLU TRP GLU ARG SER          
SEQRES  32 A  475  PHE ARG ASP TYR VAL LEU CYS GLN ALA ASN VAL THR ILE          
SEQRES  33 A  475  GLY LEU PRO THR LYS GLN PRO ILE PRO ASP CYS GLU ILE          
SEQRES  34 A  475  LYS ASN ARG PRO SER LEU LEU VAL GLU LYS ILE ASN LEU          
SEQRES  35 A  475  PHE ALA MET PHE GLY THR GLY ILE ALA MET SER THR TRP          
SEQRES  36 A  475  VAL TRP THR LYS ALA THR LEU LEU ILE TRP ARG ARG THR          
SEQRES  37 A  475  TRP CYS ARG LEU THR GLY GLN                                  
SEQRES   1 B  475  GLY GLY THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU          
SEQRES   2 B  475  ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA          
SEQRES   3 B  475  ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA          
SEQRES   4 B  475  ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU          
SEQRES   5 B  475  ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG          
SEQRES   6 B  475  HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA          
SEQRES   7 B  475  LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN          
SEQRES   8 B  475  ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR          
SEQRES   9 B  475  ILE GLN LYS TYR LEU SER GLY GLN CYS GLU VAL PRO LEU          
SEQRES  10 B  475  VAL ARG THR ASP ASN PRO LYS SER TRP TYR GLU ASP VAL          
SEQRES  11 B  475  GLU GLY CYS GLY ILE GLN CYS GLN ASN PRO LEU PHE THR          
SEQRES  12 B  475  GLU ALA GLU HIS GLN ASP MET HIS SER TYR ILE ALA ALA          
SEQRES  13 B  475  PHE GLY ALA VAL THR GLY LEU CYS THR LEU PHE THR LEU          
SEQRES  14 B  475  ALA THR PHE VAL ALA ASP TRP ARG ASN SER ASN ARG TYR          
SEQRES  15 B  475  PRO ALA VAL ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE          
SEQRES  16 B  475  VAL GLY SER ILE GLY TRP LEU ALA GLN PHE MET ASP GLY          
SEQRES  17 B  475  ALA ARG ARG GLU ILE VAL CYS ARG ALA ASP GLY THR MET          
SEQRES  18 B  475  ARG LEU GLY GLU PRO THR SER ASN GLU THR LEU SER CYS          
SEQRES  19 B  475  VAL ILE ILE PHE VAL ILE VAL TYR TYR ALA LEU MET ALA          
SEQRES  20 B  475  GLY VAL VAL TRP PHE VAL VAL LEU THR TYR ALA TRP HIS          
SEQRES  21 B  475  THR SER PHE LYS ALA LEU GLY THR THR TYR GLN PRO LEU          
SEQRES  22 B  475  SER GLY LYS THR SER TYR PHE HIS LEU LEU THR TRP SER          
SEQRES  23 B  475  LEU PRO PHE VAL LEU THR VAL ALA ILE LEU ALA VAL ALA          
SEQRES  24 B  475  GLN VAL ASP GLY ASP SER VAL SER GLY ILE CYS PHE VAL          
SEQRES  25 B  475  GLY TYR LYS ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU          
SEQRES  26 B  475  ALA PRO ILE GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE          
SEQRES  27 B  475  LEU ILE ARG GLY VAL MET THR LEU PHE SER ILE LYS SER          
SEQRES  28 B  475  ASN HIS PRO GLY LEU LEU SER GLU LYS ALA ALA SER LYS          
SEQRES  29 B  475  ILE ASN GLU THR MET LEU ARG LEU GLY ILE PHE GLY PHE          
SEQRES  30 B  475  LEU ALA PHE GLY PHE VAL LEU ILE THR PHE SER CYS HIS          
SEQRES  31 B  475  PHE TYR ASP PHE PHE ASN GLN ALA GLU TRP GLU ARG SER          
SEQRES  32 B  475  PHE ARG ASP TYR VAL LEU CYS GLN ALA ASN VAL THR ILE          
SEQRES  33 B  475  GLY LEU PRO THR LYS GLN PRO ILE PRO ASP CYS GLU ILE          
SEQRES  34 B  475  LYS ASN ARG PRO SER LEU LEU VAL GLU LYS ILE ASN LEU          
SEQRES  35 B  475  PHE ALA MET PHE GLY THR GLY ILE ALA MET SER THR TRP          
SEQRES  36 B  475  VAL TRP THR LYS ALA THR LEU LEU ILE TRP ARG ARG THR          
SEQRES  37 B  475  TRP CYS ARG LEU THR GLY GLN                                  
HET    1KS  A 601      37                                                       
HET    OLC  A 602      15                                                       
HET    OLC  A 603      15                                                       
HET    OLC  A 604      14                                                       
HET    OLA  A 605      20                                                       
HET    OLA  A 606      15                                                       
HET    PEG  A 607       7                                                       
HET    PGE  A 608      10                                                       
HET    PG4  A 609      13                                                       
HET    1KS  B 601      37                                                       
HET    OLC  B 602      13                                                       
HET    OLC  B 603      14                                                       
HET    OLA  B 604      20                                                       
HET    PEG  B 605       7                                                       
HETNAM     1KS 4-FLUORO-N-METHYL-N-{1-[4-(1-METHYL-1H-PYRAZOL-5-YL)             
HETNAM   2 1KS  PHTHALAZIN-1-YL]PIPERIDIN-4-YL}-2-(TRIFLUOROMETHYL)             
HETNAM   3 1KS  BENZAMIDE                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  1KS    2(C26 H24 F4 N6 O)                                           
FORMUL   4  OLC    5(C21 H40 O4)                                                
FORMUL   7  OLA    3(C18 H34 O2)                                                
FORMUL   9  PEG    2(C4 H10 O3)                                                 
FORMUL  10  PGE    C6 H14 O4                                                    
FORMUL  11  PG4    C8 H18 O5                                                    
FORMUL  17  HOH   *110(H2 O)                                                    
HELIX    1   1 ASP A    2  LYS A   19  1                                  18    
HELIX    2   2 ASN A   22  ALA A   43  1                                  22    
HELIX    3   3 PRO A   45  GLU A   49  5                                   5    
HELIX    4   4 SER A   55  GLU A   81  1                                  27    
HELIX    5   5 LYS A   83  ILE A  102  1                                  20    
HELIX    6   6 ASN A  202  LYS A  204  5                                   3    
HELIX    7   7 THR A  223  ASP A  255  1                                  33    
HELIX    8   8 ASP A  255  ASN A  260  1                                   6    
HELIX    9   9 VAL A  265  ALA A  283  1                                  19    
HELIX   10  10 GLN A  284  MET A  286  5                                   3    
HELIX   11  11 GLY A  288  CYS A  295  1                                   8    
HELIX   12  12 LEU A  312  THR A  348  1                                  37    
HELIX   13  13 PHE A  360  ALA A  379  1                                  20    
HELIX   14  14 ASN A  396  VAL A  404  1                                   9    
HELIX   15  15 VAL A  404  HIS A  433  1                                  30    
HELIX   16  16 ALA A  442  ASN A  493  1                                  52    
HELIX   17  17 SER A  514  SER A  533  1                                  20    
HELIX   18  18 THR A  534  TRP A  537  5                                   4    
HELIX   19  19 THR A  538  TRP A  549  1                                  12    
HELIX   20  20 ASP B    2  LYS B   19  1                                  18    
HELIX   21  21 ASN B   22  ALA B   43  1                                  22    
HELIX   22  22 PRO B   45  GLU B   49  5                                   5    
HELIX   23  23 SER B   55  ASN B   80  1                                  26    
HELIX   24  24 LYS B   83  ILE B  102  1                                  20    
HELIX   25  25 GLN B  103  LEU B  106  5                                   4    
HELIX   26  26 ASN B  202  TRP B  206  5                                   5    
HELIX   27  27 THR B  223  ASP B  255  1                                  33    
HELIX   28  28 ASP B  255  ASN B  260  1                                   6    
HELIX   29  29 PRO B  263  ALA B  283  1                                  21    
HELIX   30  30 GLN B  284  MET B  286  5                                   3    
HELIX   31  31 GLY B  288  CYS B  295  1                                   8    
HELIX   32  32 LEU B  312  LEU B  346  1                                  35    
HELIX   33  33 TYR B  359  ALA B  379  1                                  21    
HELIX   34  34 ASN B  396  VAL B  404  1                                   9    
HELIX   35  35 VAL B  404  HIS B  433  1                                  30    
HELIX   36  36 GLU B  439  ALA B  441  5                                   3    
HELIX   37  37 ALA B  442  GLN B  491  1                                  50    
HELIX   38  38 SER B  514  THR B  534  1                                  21    
HELIX   39  39 TRP B  535  TRP B  537  5                                   3    
HELIX   40  40 THR B  538  CYS B  550  1                                  13    
SHEET    1   A 3 LEU A 197  ARG A 199  0                                        
SHEET    2   A 3 VAL A 210  ILE A 215 -1  O  GLY A 214   N  VAL A 198           
SHEET    3   A 3 TRP A 206  TYR A 207 -1  N  TYR A 207   O  CYS A 213           
SHEET    1   B 2 VAL A 381  ASP A 384  0                                        
SHEET    2   B 2 ILE A 389  VAL A 392 -1  O  PHE A 391   N  ASP A 382           
SHEET    1   C 2 LEU B 197  ARG B 199  0                                        
SHEET    2   C 2 CYS B 213  ILE B 215 -1  O  GLY B 214   N  VAL B 198           
SHEET    1   D 2 VAL B 381  ASP B 384  0                                        
SHEET    2   D 2 ILE B 389  VAL B 392 -1  O  PHE B 391   N  ASP B 382           
SSBOND   1 CYS A  193    CYS A  213                          1555   1555  2.04  
SSBOND   2 CYS A  217    CYS A  295                          1555   1555  2.03  
SSBOND   3 CYS A  314    CYS A  390                          1555   1555  2.06  
SSBOND   4 CYS A  490    CYS A  507                          1555   1555  2.03  
SSBOND   5 CYS B  193    CYS B  213                          1555   1555  2.04  
SSBOND   6 CYS B  217    CYS B  295                          1555   1555  2.02  
SSBOND   7 CYS B  314    CYS B  390                          1555   1555  2.06  
SSBOND   8 CYS B  490    CYS B  507                          1555   1555  2.04  
CISPEP   1 VAL A  195    PRO A  196          0         8.49                     
CISPEP   2 TYR A  262    PRO A  263          0         4.23                     
CISPEP   3 GLU A  305    PRO A  306          0         3.20                     
CISPEP   4 VAL B  195    PRO B  196          0         6.39                     
CISPEP   5 TYR B  262    PRO B  263          0         9.02                     
CISPEP   6 GLU B  305    PRO B  306          0        -2.31                     
SITE     1 AC1 17 ASN A 219  LEU A 221  TRP A 281  ASP A 384                    
SITE     2 AC1 17 VAL A 386  SER A 387  PHE A 391  TYR A 394                    
SITE     3 AC1 17 LYS A 395  ARG A 400  GLN A 477  TRP A 480                    
SITE     4 AC1 17 GLU A 481  PRO A 513  GLU A 518  ASN A 521                    
SITE     5 AC1 17 LEU A 522                                                     
SITE     1 AC2  3 GLU A 447  ARG A 451  THR A 534                               
SITE     1 AC3  6 TYR A 397  ARG A 398  ALA A 401  ALA A 406                    
SITE     2 AC3  6 PHE A 474  ALA B 377                                          
SITE     1 AC4  4 SER A 468  TYR A 472  PHE A 475  ASN A 476                    
SITE     1 AC5  2 GLY A 288  ILE A 316                                          
SITE     1 AC6  3 TYR A 323  HIS A 361  TRP A 365                               
SITE     1 AC7  2 PRO A 220  LEU A 221                                          
SITE     1 AC8  6 GLN A 380  ASN A 396  TYR A 399  HOH A 714                    
SITE     2 AC8  6 ASN B 396  TYR B 399                                          
SITE     1 AC9  3 ASP A 229  TYR A 233  LYS A 519                               
SITE     1 BC1 19 ASN B 219  LEU B 221  MET B 230  TRP B 281                    
SITE     2 BC1 19 MET B 301  ASP B 384  VAL B 386  SER B 387                    
SITE     3 BC1 19 PHE B 391  TYR B 394  LYS B 395  ARG B 400                    
SITE     4 BC1 19 GLN B 477  TRP B 480  GLU B 481  PRO B 513                    
SITE     5 BC1 19 GLU B 518  ASN B 521  LEU B 522                               
SITE     1 BC2  3 ASP B 287  GLU B 292  ILE B 293                               
SITE     1 BC3  2 TYR B 233  LYS B 519                                          
SITE     1 BC4  2 ILE B 413  TYR B 417                                          
SITE     1 BC5  4 THR B 311  LEU B 312  SER B 313  HOH B 759                    
CRYST1   75.444   98.177   84.293  90.00 103.27  90.00 P 1 21 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      0.013255  0.000000  0.003126        0.00000                         
SCALE2      0.000000  0.010186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012189        0.00000                         
ATOM      1  N   GLY A  -1      -6.361  13.515  55.827  1.00108.49           N  
ANISOU    1  N   GLY A  -1    12879  18546   9795    375  -1244    -98       N  
ATOM      2  CA  GLY A  -1      -5.999  12.132  55.546  1.00109.09           C  
ANISOU    2  CA  GLY A  -1    13081  18593   9775    564  -1301     30       C  
ATOM      3  C   GLY A  -1      -4.724  11.687  56.235  1.00116.05           C  
ANISOU    3  C   GLY A  -1    13892  19710  10492    779  -1445    -46       C  
ATOM      4  O   GLY A  -1      -3.774  12.470  56.345  1.00116.70           O  
ANISOU    4  O   GLY A  -1    13748  19989  10604    759  -1501   -237       O  
ATOM      5  N   THR A   0      -4.697  10.415  56.706  1.00113.64           N  
ANISOU    5  N   THR A   0    13785  19384  10009    992  -1503     92       N  
ATOM      6  CA  THR A   0      -3.556   9.798  57.403  1.00115.47           C  
ANISOU    6  CA  THR A   0    13997  19826  10051   1261  -1666     47       C  
ATOM      7  C   THR A   0      -2.380   9.649  56.416  1.00118.81           C  
ANISOU    7  C   THR A   0    14224  20338  10582   1337  -1727    -50       C  
ATOM      8  O   THR A   0      -1.260  10.064  56.724  1.00119.98           O  
ANISOU    8  O   THR A   0    14146  20739  10704   1420  -1843   -241       O  
ATOM      9  CB  THR A   0      -3.980   8.459  58.054  1.00123.98           C  
ANISOU    9  CB  THR A   0    15402  20792  10913   1465  -1680    249       C  
ATOM     10  OG1 THR A   0      -5.049   8.702  58.973  1.00122.22           O  
ANISOU   10  OG1 THR A   0    15348  20484  10606   1355  -1590    311       O  
ATOM     11  CG2 THR A   0      -2.830   7.763  58.788  1.00125.01           C  
ANISOU   11  CG2 THR A   0    15551  21129  10817   1790  -1870    219       C  
ATOM     12  N   ALA A   1      -2.650   9.077  55.233  1.00113.28           N  
ANISOU   12  N   ALA A   1    13601  19437  10005   1298  -1641     63       N  
ATOM     13  CA  ALA A   1      -1.664   8.915  54.169  1.00112.57           C  
ANISOU   13  CA  ALA A   1    13352  19389  10032   1338  -1658    -18       C  
ATOM     14  C   ALA A   1      -1.823  10.046  53.151  1.00114.03           C  
ANISOU   14  C   ALA A   1    13381  19506  10440   1060  -1536   -118       C  
ATOM     15  O   ALA A   1      -2.883  10.681  53.105  1.00111.94           O  
ANISOU   15  O   ALA A   1    13187  19103  10241    869  -1440    -67       O  
ATOM     16  CB  ALA A   1      -1.835   7.556  53.502  1.00112.95           C  
ANISOU   16  CB  ALA A   1    13608  19250  10058   1472  -1632    165       C  
ATOM     17  N   ASP A   2      -0.769  10.313  52.353  1.00110.75           N  
ANISOU   17  N   ASP A   2    12762  19183  10134   1044  -1534   -269       N  
ATOM     18  CA  ASP A   2      -0.773  11.350  51.311  1.00109.11           C  
ANISOU   18  CA  ASP A   2    12441  18898  10118    792  -1401   -367       C  
ATOM     19  C   ASP A   2      -1.750  10.986  50.176  1.00109.74           C  
ANISOU   19  C   ASP A   2    12722  18690  10285    689  -1291   -182       C  
ATOM     20  O   ASP A   2      -2.001   9.801  49.928  1.00109.01           O  
ANISOU   20  O   ASP A   2    12792  18490  10137    821  -1310    -28       O  
ATOM     21  CB  ASP A   2       0.647  11.552  50.746  1.00112.29           C  
ANISOU   21  CB  ASP A   2    12600  19463  10602    807  -1403   -580       C  
ATOM     22  CG  ASP A   2       0.877  12.874  50.034  1.00121.45           C  
ANISOU   22  CG  ASP A   2    13618  20601  11925    538  -1259   -747       C  
ATOM     23  OD1 ASP A   2       1.755  13.644  50.482  1.00123.55           O  
ANISOU   23  OD1 ASP A   2    13650  21079  12213    487  -1269   -987       O  
ATOM     24  OD2 ASP A   2       0.221  13.114  48.995  1.00125.32           O  
ANISOU   24  OD2 ASP A   2    14241  20862  12514    384  -1131   -648       O  
ATOM     25  N   LEU A   3      -2.302  12.016  49.502  1.00103.95           N  
ANISOU   25  N   LEU A   3    11986  17832   9681    460  -1177   -207       N  
ATOM     26  CA  LEU A   3      -3.235  11.875  48.382  1.00101.45           C  
ANISOU   26  CA  LEU A   3    11838  17263   9447    354  -1089    -65       C  
ATOM     27  C   LEU A   3      -2.556  11.147  47.212  1.00105.46           C  
ANISOU   27  C   LEU A   3    12361  17712   9996    400  -1058    -51       C  
ATOM     28  O   LEU A   3      -3.139  10.204  46.677  1.00103.96           O  
ANISOU   28  O   LEU A   3    12340  17367   9794    446  -1049    103       O  
ATOM     29  CB  LEU A   3      -3.765  13.261  47.949  1.00100.20           C  
ANISOU   29  CB  LEU A   3    11663  17008   9400    135   -993   -123       C  
ATOM     30  CG  LEU A   3      -4.849  13.322  46.857  1.00102.82           C  
ANISOU   30  CG  LEU A   3    12166  17093   9807     35   -927      6       C  
ATOM     31  CD1 LEU A   3      -6.101  12.537  47.235  1.00101.66           C  
ANISOU   31  CD1 LEU A   3    12170  16842   9616     89   -968    166       C  
ATOM     32  CD2 LEU A   3      -5.224  14.753  46.561  1.00104.98           C  
ANISOU   32  CD2 LEU A   3    12427  17288  10173   -141   -845    -67       C  
ATOM     33  N   GLU A   4      -1.302  11.540  46.870  1.00103.34           N  
ANISOU   33  N   GLU A   4    11910  17577   9779    384  -1032   -229       N  
ATOM     34  CA  GLU A   4      -0.515  10.922  45.796  1.00103.43           C  
ANISOU   34  CA  GLU A   4    11906  17555   9836    420   -985   -254       C  
ATOM     35  C   GLU A   4      -0.099   9.484  46.172  1.00107.11           C  
ANISOU   35  C   GLU A   4    12403  18087  10207    677  -1091   -181       C  
ATOM     36  O   GLU A   4       0.076   8.653  45.280  1.00106.70           O  
ANISOU   36  O   GLU A   4    12434  17930  10177    728  -1055   -116       O  
ATOM     37  CB  GLU A   4       0.712  11.785  45.443  1.00106.13           C  
ANISOU   37  CB  GLU A   4    12024  18032  10267    314   -905   -499       C  
ATOM     38  CG  GLU A   4       1.258  11.580  44.031  1.00119.31           C  
ANISOU   38  CG  GLU A   4    13716  19599  12019    245   -784   -534       C  
ATOM     39  CD  GLU A   4       0.338  11.841  42.845  1.00144.52           C  
ANISOU   39  CD  GLU A   4    17136  22522  15254     86   -672   -398       C  
ATOM     40  OE1 GLU A   4      -0.492  12.778  42.910  1.00141.68           O  
ANISOU   40  OE1 GLU A   4    16857  22065  14911    -51   -636   -362       O  
ATOM     41  OE2 GLU A   4       0.478  11.123  41.828  1.00138.37           O  
ANISOU   41  OE2 GLU A   4    16454  21634  14487    106   -623   -339       O  
ATOM     42  N   ASP A   5       0.013   9.188  47.479  1.00104.06           N  
ANISOU   42  N   ASP A   5    11976  17858   9704    844  -1217   -186       N  
ATOM     43  CA  ASP A   5       0.347   7.855  47.980  1.00105.12           C  
ANISOU   43  CA  ASP A   5    12184  18042   9717   1119  -1326   -103       C  
ATOM     44  C   ASP A   5      -0.862   6.931  47.831  1.00107.43           C  
ANISOU   44  C   ASP A   5    12770  18096   9952   1144  -1295    142       C  
ATOM     45  O   ASP A   5      -0.719   5.830  47.300  1.00107.39           O  
ANISOU   45  O   ASP A   5    12882  17997   9925   1273  -1288    233       O  
ATOM     46  CB  ASP A   5       0.819   7.916  49.445  1.00108.83           C  
ANISOU   46  CB  ASP A   5    12549  18750  10052   1291  -1474   -187       C  
ATOM     47  N   ASN A   6      -2.058   7.398  48.268  1.00102.44           N  
ANISOU   47  N   ASN A   6    12249  17366   9309   1010  -1261    228       N  
ATOM     48  CA  ASN A   6      -3.331   6.670  48.182  1.00100.70           C  
ANISOU   48  CA  ASN A   6    12280  16927   9056    987  -1210    420       C  
ATOM     49  C   ASN A   6      -3.775   6.479  46.731  1.00102.39           C  
ANISOU   49  C   ASN A   6    12570  16946   9386    857  -1113    475       C  
ATOM     50  O   ASN A   6      -4.459   5.498  46.430  1.00101.52           O  
ANISOU   50  O   ASN A   6    12649  16672   9252    886  -1074    608       O  
ATOM     51  CB  ASN A   6      -4.416   7.398  48.958  1.00 99.11           C  
ANISOU   51  CB  ASN A   6    12121  16698   8839    861  -1193    447       C  
ATOM     52  CG  ASN A   6      -4.228   7.336  50.447  1.00114.03           C  
ANISOU   52  CG  ASN A   6    14015  18737  10574    997  -1277    434       C  
ATOM     53  OD1 ASN A   6      -4.225   6.258  51.052  1.00108.84           O  
ANISOU   53  OD1 ASN A   6    13522  18058   9775   1180  -1312    538       O  
ATOM     54  ND2 ASN A   6      -4.120   8.496  51.075  1.00102.45           N  
ANISOU   54  ND2 ASN A   6    12397  17410   9120    907  -1302    310       N  
ATOM     55  N   TRP A   7      -3.393   7.422  45.843  1.00 97.72           N  
ANISOU   55  N   TRP A   7    11849  16369   8911    709  -1066    365       N  
ATOM     56  CA  TRP A   7      -3.686   7.374  44.415  1.00 96.71           C  
ANISOU   56  CA  TRP A   7    11798  16074   8874    589   -982    399       C  
ATOM     57  C   TRP A   7      -2.903   6.238  43.768  1.00101.81           C  
ANISOU   57  C   TRP A   7    12478  16698   9507    720   -969    416       C  
ATOM     58  O   TRP A   7      -3.460   5.517  42.949  1.00100.76           O  
ANISOU   58  O   TRP A   7    12500  16397   9388    695   -920    514       O  
ATOM     59  CB  TRP A   7      -3.351   8.716  43.751  1.00 95.23           C  
ANISOU   59  CB  TRP A   7    11494  15906   8784    412   -921    273       C  
ATOM     60  CG  TRP A   7      -3.951   8.901  42.389  1.00 95.28           C  
ANISOU   60  CG  TRP A   7    11626  15720   8854    275   -844    325       C  
ATOM     61  CD1 TRP A   7      -3.281   8.997  41.206  1.00 98.52           C  
ANISOU   61  CD1 TRP A   7    12039  16082   9312    213   -765    269       C  
ATOM     62  CD2 TRP A   7      -5.343   9.049  42.075  1.00 93.93           C  
ANISOU   62  CD2 TRP A   7    11598  15390   8700    187   -844    429       C  
ATOM     63  NE1 TRP A   7      -4.168   9.191  40.172  1.00 97.13           N  
ANISOU   63  NE1 TRP A   7    12022  15723   9159    102   -726    345       N  
ATOM     64  CE2 TRP A   7      -5.441   9.232  40.678  1.00 97.54           C  
ANISOU   64  CE2 TRP A   7    12148  15714   9199     92   -785    437       C  
ATOM     65  CE3 TRP A   7      -6.522   9.045  42.840  1.00 94.55           C  
ANISOU   65  CE3 TRP A   7    11730  15433   8762    180   -887    500       C  
ATOM     66  CZ2 TRP A   7      -6.669   9.415  40.030  1.00 95.86           C  
ANISOU   66  CZ2 TRP A   7    12070  15347   9005     14   -795    513       C  
ATOM     67  CZ3 TRP A   7      -7.737   9.204  42.195  1.00 95.10           C  
ANISOU   67  CZ3 TRP A   7    11908  15351   8873     90   -882    561       C  
ATOM     68  CH2 TRP A   7      -7.801   9.406  40.809  1.00 95.45           C  
ANISOU   68  CH2 TRP A   7    12033  15280   8953     18   -850    565       C  
ATOM     69  N   GLU A   8      -1.625   6.057  44.174  1.00100.46           N  
ANISOU   69  N   GLU A   8    12155  16706   9309    870  -1020    307       N  
ATOM     70  CA  GLU A   8      -0.727   4.996  43.706  1.00101.33           C  
ANISOU   70  CA  GLU A   8    12263  16826   9410   1033  -1020    295       C  
ATOM     71  C   GLU A   8      -1.218   3.619  44.172  1.00105.90           C  
ANISOU   71  C   GLU A   8    13055  17298   9883   1214  -1054    464       C  
ATOM     72  O   GLU A   8      -1.077   2.649  43.433  1.00106.36           O  
ANISOU   72  O   GLU A   8    13221  17237   9952   1276  -1004    522       O  
ATOM     73  CB  GLU A   8       0.705   5.246  44.204  1.00104.48           C  
ANISOU   73  CB  GLU A   8    12412  17475   9810   1164  -1088    106       C  
ATOM     74  CG  GLU A   8       1.757   5.254  43.106  1.00115.50           C  
ANISOU   74  CG  GLU A   8    13674  18900  11311   1129  -1006    -38       C  
ATOM     75  CD  GLU A   8       1.788   6.472  42.199  1.00132.79           C  
ANISOU   75  CD  GLU A   8    15796  21045  13613    853   -875   -145       C  
ATOM     76  OE1 GLU A   8       1.871   6.280  40.963  1.00127.56           O  
ANISOU   76  OE1 GLU A   8    15208  20248  13010    760   -762   -139       O  
ATOM     77  OE2 GLU A   8       1.747   7.613  42.716  1.00120.92           O  
ANISOU   77  OE2 GLU A   8    14184  19631  12129    730   -876   -236       O  
ATOM     78  N   THR A   9      -1.804   3.543  45.384  1.00102.33           N  
ANISOU   78  N   THR A   9    12681  16875   9325   1287  -1118    540       N  
ATOM     79  CA  THR A   9      -2.366   2.321  45.976  1.00102.84           C  
ANISOU   79  CA  THR A   9    12987  16818   9269   1438  -1121    702       C  
ATOM     80  C   THR A   9      -3.612   1.910  45.195  1.00106.37           C  
ANISOU   80  C   THR A   9    13628  17019   9767   1270  -1006    820       C  
ATOM     81  O   THR A   9      -3.820   0.723  44.935  1.00106.36           O  
ANISOU   81  O   THR A   9    13818  16867   9728   1354   -951    922       O  
ATOM     82  CB  THR A   9      -2.677   2.560  47.466  1.00108.33           C  
ANISOU   82  CB  THR A   9    13715  17611   9834   1517  -1198    729       C  
ATOM     83  OG1 THR A   9      -1.478   2.964  48.124  1.00110.31           O  
ANISOU   83  OG1 THR A   9    13758  18115  10040   1668  -1322    589       O  
ATOM     84  CG2 THR A   9      -3.263   1.333  48.160  1.00106.15           C  
ANISOU   84  CG2 THR A   9    13728  17195   9409   1673  -1177    897       C  
ATOM     85  N   LEU A  10      -4.430   2.910  44.827  1.00102.70           N  
ANISOU   85  N   LEU A  10    13111  16519   9391   1040   -971    791       N  
ATOM     86  CA  LEU A  10      -5.669   2.771  44.067  1.00101.89           C  
ANISOU   86  CA  LEU A  10    13139  16224   9351    866   -889    860       C  
ATOM     87  C   LEU A  10      -5.398   2.184  42.670  1.00105.83           C  
ANISOU   87  C   LEU A  10    13687  16611   9912    837   -829    863       C  
ATOM     88  O   LEU A  10      -6.165   1.339  42.212  1.00104.70           O  
ANISOU   88  O   LEU A  10    13708  16302   9772    792   -764    938       O  
ATOM     89  CB  LEU A  10      -6.341   4.156  43.959  1.00100.79           C  
ANISOU   89  CB  LEU A  10    12894  16110   9291    671   -897    800       C  
ATOM     90  CG  LEU A  10      -7.860   4.244  44.143  1.00104.85           C  
ANISOU   90  CG  LEU A  10    13506  16504   9827    542   -862    856       C  
ATOM     91  CD1 LEU A  10      -8.286   3.859  45.550  1.00105.44           C  
ANISOU   91  CD1 LEU A  10    13657  16602   9803    615   -861    907       C  
ATOM     92  CD2 LEU A  10      -8.341   5.651  43.870  1.00107.05           C  
ANISOU   92  CD2 LEU A  10    13673  16807  10196    384   -881    785       C  
ATOM     93  N   ASN A  11      -4.289   2.607  42.027  1.00103.58           N  
ANISOU   93  N   ASN A  11    13260  16420   9674    855   -838    763       N  
ATOM     94  CA  ASN A  11      -3.871   2.162  40.698  1.00104.16           C  
ANISOU   94  CA  ASN A  11    13370  16406   9802    823   -771    743       C  
ATOM     95  C   ASN A  11      -3.267   0.758  40.734  1.00110.83           C  
ANISOU   95  C   ASN A  11    14309  17207  10595   1021   -752    791       C  
ATOM     96  O   ASN A  11      -3.587  -0.052  39.863  1.00110.27           O  
ANISOU   96  O   ASN A  11    14379  16978  10540    989   -678    841       O  
ATOM     97  CB  ASN A  11      -2.853   3.142  40.083  1.00106.56           C  
ANISOU   97  CB  ASN A  11    13491  16822  10174    755   -757    600       C  
ATOM     98  CG  ASN A  11      -3.283   4.593  39.994  1.00135.42           C  
ANISOU   98  CG  ASN A  11    17072  20507  13877    572   -758    545       C  
ATOM     99  OD1 ASN A  11      -4.457   4.957  40.164  1.00128.84           O  
ANISOU   99  OD1 ASN A  11    16317  19594  13043    476   -775    612       O  
ATOM    100  ND2 ASN A  11      -2.318   5.466  39.742  1.00129.52           N  
ANISOU  100  ND2 ASN A  11    16165  19871  13177    520   -730    406       N  
ATOM    101  N   ASP A  12      -2.373   0.483  41.717  1.00109.90           N  
ANISOU  101  N   ASP A  12    14115  17229  10412   1237   -825    766       N  
ATOM    102  CA  ASP A  12      -1.669  -0.797  41.879  1.00111.71           C  
ANISOU  102  CA  ASP A  12    14431  17433  10582   1480   -828    805       C  
ATOM    103  C   ASP A  12      -2.637  -1.961  42.097  1.00116.98           C  
ANISOU  103  C   ASP A  12    15384  17889  11176   1518   -764    966       C  
ATOM    104  O   ASP A  12      -2.457  -3.012  41.483  1.00116.94           O  
ANISOU  104  O   ASP A  12    15509  17750  11172   1591   -692   1007       O  
ATOM    105  CB  ASP A  12      -0.647  -0.727  43.030  1.00115.03           C  
ANISOU  105  CB  ASP A  12    14714  18066  10926   1721   -954    741       C  
ATOM    106  CG  ASP A  12       0.590   0.112  42.740  1.00123.80           C  
ANISOU  106  CG  ASP A  12    15526  19392  12120   1722   -997    540       C  
ATOM    107  OD1 ASP A  12       1.268   0.524  43.707  1.00124.52           O  
ANISOU  107  OD1 ASP A  12    15455  19695  12163   1859  -1113    449       O  
ATOM    108  OD2 ASP A  12       0.871   0.372  41.544  1.00129.02           O  
ANISOU  108  OD2 ASP A  12    16120  20011  12891   1576   -905    462       O  
ATOM    109  N   ASN A  13      -3.668  -1.766  42.936  1.00114.60           N  
ANISOU  109  N   ASN A  13    15179  17549  10816   1451   -768   1042       N  
ATOM    110  CA  ASN A  13      -4.682  -2.788  43.202  1.00115.66           C  
ANISOU  110  CA  ASN A  13    15584  17475  10886   1443   -673   1171       C  
ATOM    111  C   ASN A  13      -5.558  -3.015  41.969  1.00120.45           C  
ANISOU  111  C   ASN A  13    16266  17909  11590   1223   -565   1174       C  
ATOM    112  O   ASN A  13      -5.912  -4.157  41.681  1.00120.69           O  
ANISOU  112  O   ASN A  13    16500  17757  11598   1243   -461   1240       O  
ATOM    113  CB  ASN A  13      -5.533  -2.409  44.405  1.00116.03           C  
ANISOU  113  CB  ASN A  13    15688  17539  10857   1399   -688   1219       C  
ATOM    114  CG  ASN A  13      -4.859  -2.715  45.710  1.00137.57           C  
ANISOU  114  CG  ASN A  13    18472  20367  13432   1656   -768   1261       C  
ATOM    115  OD1 ASN A  13      -4.949  -3.831  46.228  1.00133.02           O  
ANISOU  115  OD1 ASN A  13    18148  19657  12736   1809   -711   1371       O  
ATOM    116  ND2 ASN A  13      -4.147  -1.739  46.256  1.00129.02           N  
ANISOU  116  ND2 ASN A  13    17168  19516  12337   1713   -899   1168       N  
ATOM    117  N   LEU A  14      -5.862  -1.931  41.223  1.00117.18           N  
ANISOU  117  N   LEU A  14    15697  17551  11275   1025   -590   1094       N  
ATOM    118  CA  LEU A  14      -6.657  -1.945  39.987  1.00116.53           C  
ANISOU  118  CA  LEU A  14    15661  17342  11273    826   -526   1075       C  
ATOM    119  C   LEU A  14      -5.906  -2.684  38.859  1.00122.46           C  
ANISOU  119  C   LEU A  14    16455  18024  12050    872   -469   1054       C  
ATOM    120  O   LEU A  14      -6.547  -3.285  37.993  1.00121.74           O  
ANISOU  120  O   LEU A  14    16483  17786  11986    763   -393   1062       O  
ATOM    121  CB  LEU A  14      -6.999  -0.501  39.573  1.00115.04           C  
ANISOU  121  CB  LEU A  14    15312  17242  11155    656   -589   1001       C  
ATOM    122  CG  LEU A  14      -8.231  -0.252  38.689  1.00118.82           C  
ANISOU  122  CG  LEU A  14    15839  17615  11694    456   -568    985       C  
ATOM    123  CD1 LEU A  14      -9.475  -0.982  39.198  1.00119.40           C  
ANISOU  123  CD1 LEU A  14    16043  17569  11756    400   -509   1029       C  
ATOM    124  CD2 LEU A  14      -8.529   1.223  38.611  1.00120.16           C  
ANISOU  124  CD2 LEU A  14    15872  17874  11910    345   -644    928       C  
ATOM    125  N   LYS A  15      -4.554  -2.664  38.899  1.00121.11           N  
ANISOU  125  N   LYS A  15    16177  17967  11872   1033   -504   1009       N  
ATOM    126  CA  LYS A  15      -3.682  -3.362  37.951  1.00122.34           C  
ANISOU  126  CA  LYS A  15    16351  18075  12056   1103   -444    971       C  
ATOM    127  C   LYS A  15      -3.664  -4.866  38.257  1.00129.25           C  
ANISOU  127  C   LYS A  15    17436  18803  12870   1272   -374   1061       C  
ATOM    128  O   LYS A  15      -3.537  -5.678  37.336  1.00129.22           O  
ANISOU  128  O   LYS A  15    17533  18672  12893   1264   -282   1056       O  
ATOM    129  CB  LYS A  15      -2.259  -2.785  37.994  1.00125.46           C  
ANISOU  129  CB  LYS A  15    16529  18660  12480   1217   -501    860       C  
ATOM    130  N   VAL A  16      -3.802  -5.230  39.549  1.00127.99           N  
ANISOU  130  N   VAL A  16    17363  18648  12618   1423   -407   1143       N  
ATOM    131  CA  VAL A  16      -3.832  -6.621  40.004  1.00130.06           C  
ANISOU  131  CA  VAL A  16    17874  18747  12797   1600   -330   1246       C  
ATOM    132  C   VAL A  16      -5.313  -7.008  40.253  1.00134.79           C  
ANISOU  132  C   VAL A  16    18680  19164  13371   1427   -224   1323       C  
ATOM    133  O   VAL A  16      -5.712  -7.342  41.374  1.00135.42           O  
ANISOU  133  O   VAL A  16    18909  19194  13352   1508   -204   1408       O  
ATOM    134  CB  VAL A  16      -2.902  -6.893  41.229  1.00135.91           C  
ANISOU  134  CB  VAL A  16    18618  19595  13425   1918   -427   1284       C  
ATOM    135  CG1 VAL A  16      -2.702  -8.394  41.449  1.00137.86           C  
ANISOU  135  CG1 VAL A  16    19146  19649  13585   2140   -339   1387       C  
ATOM    136  CG2 VAL A  16      -1.546  -6.211  41.060  1.00136.12           C  
ANISOU  136  CG2 VAL A  16    18359  19857  13502   2040   -548   1153       C  
ATOM    137  N   ILE A  17      -6.124  -6.909  39.184  1.00131.01           N  
ANISOU  137  N   ILE A  17    18200  18598  12980   1182   -156   1275       N  
ATOM    138  CA  ILE A  17      -7.545  -7.273  39.125  1.00131.12           C  
ANISOU  138  CA  ILE A  17    18358  18453  13007    981    -49   1293       C  
ATOM    139  C   ILE A  17      -7.761  -7.981  37.774  1.00137.11           C  
ANISOU  139  C   ILE A  17    19199  19068  13828    863     54   1246       C  
ATOM    140  O   ILE A  17      -8.224  -9.126  37.752  1.00137.96           O  
ANISOU  140  O   ILE A  17    19525  18981  13914    845    200   1279       O  
ATOM    141  CB  ILE A  17      -8.516  -6.071  39.373  1.00132.50           C  
ANISOU  141  CB  ILE A  17    18384  18732  13227    787   -123   1245       C  
ATOM    142  CG1 ILE A  17      -8.643  -5.789  40.884  1.00133.15           C  
ANISOU  142  CG1 ILE A  17    18489  18875  13226    877   -154   1306       C  
ATOM    143  CG2 ILE A  17      -9.916  -6.326  38.760  1.00132.73           C  
ANISOU  143  CG2 ILE A  17    18477  18634  13322    542    -35   1194       C  
ATOM    144  CD1 ILE A  17      -9.232  -4.431  41.282  1.00138.84           C  
ANISOU  144  CD1 ILE A  17    19022  19744  13989    746   -252   1254       C  
ATOM    145  N   GLU A  18      -7.374  -7.319  36.659  1.00133.80           N  
ANISOU  145  N   GLU A  18    18625  18737  13475    784     -9   1164       N  
ATOM    146  CA  GLU A  18      -7.475  -7.889  35.315  1.00134.27           C  
ANISOU  146  CA  GLU A  18    18756  18684  13577    676     73   1109       C  
ATOM    147  C   GLU A  18      -6.358  -8.934  35.095  1.00140.91           C  
ANISOU  147  C   GLU A  18    19698  19445  14398    872    153   1133       C  
ATOM    148  O   GLU A  18      -6.483  -9.793  34.220  1.00141.17           O  
ANISOU  148  O   GLU A  18    19857  19333  14449    813    265   1105       O  
ATOM    149  CB  GLU A  18      -7.452  -6.787  34.228  1.00134.31           C  
ANISOU  149  CB  GLU A  18    18601  18799  13634    527    -14   1020       C  
ATOM    150  CG  GLU A  18      -6.116  -6.080  34.010  1.00144.29           C  
ANISOU  150  CG  GLU A  18    19708  20207  14908    633    -80    986       C  
ATOM    151  CD  GLU A  18      -5.873  -4.768  34.734  1.00161.40           C  
ANISOU  151  CD  GLU A  18    21688  22557  17079    649   -201    975       C  
ATOM    152  OE1 GLU A  18      -6.854  -4.075  35.087  1.00158.90           O  
ANISOU  152  OE1 GLU A  18    21339  22268  16769    531   -259    982       O  
ATOM    153  OE2 GLU A  18      -4.686  -4.399  34.886  1.00151.21           O  
ANISOU  153  OE2 GLU A  18    20271  21388  15796    771   -234    939       O  
ATOM    154  N   LYS A  19      -5.283  -8.859  35.909  1.00139.18           N  
ANISOU  154  N   LYS A  19    19416  19328  14139   1113     88   1172       N  
ATOM    155  CA  LYS A  19      -4.122  -9.750  35.863  1.00141.14           C  
ANISOU  155  CA  LYS A  19    19724  19533  14370   1354    131   1185       C  
ATOM    156  C   LYS A  19      -4.151 -10.782  37.007  1.00147.63           C  
ANISOU  156  C   LYS A  19    20770  20228  15094   1569    185   1303       C  
ATOM    157  O   LYS A  19      -3.310 -11.685  37.029  1.00148.84           O  
ANISOU  157  O   LYS A  19    21026  20305  15221   1797    230   1329       O  
ATOM    158  CB  LYS A  19      -2.820  -8.927  35.919  1.00143.90           C  
ANISOU  158  CB  LYS A  19    19822  20108  14747   1494      9   1111       C  
ATOM    159  CG  LYS A  19      -2.568  -8.087  34.669  1.00159.66           C  
ANISOU  159  CG  LYS A  19    21655  22184  16826   1307      5    994       C  
ATOM    160  CD  LYS A  19      -1.300  -7.248  34.785  1.00170.34           C  
ANISOU  160  CD  LYS A  19    22753  23754  18215   1413    -83    895       C  
ATOM    161  CE  LYS A  19      -1.017  -6.444  33.537  1.00179.73           C  
ANISOU  161  CE  LYS A  19    23824  24994  19472   1217    -49    781       C  
ATOM    162  NZ  LYS A  19      -0.535  -7.295  32.413  1.00189.14           N  
ANISOU  162  NZ  LYS A  19    25099  26069  20697   1217     77    729       N  
ATOM    163  N   ALA A  20      -5.121 -10.655  37.943  1.00144.81           N  
ANISOU  163  N   ALA A  20    20505  19837  14678   1501    190   1371       N  
ATOM    164  CA  ALA A  20      -5.284 -11.540  39.104  1.00146.75           C  
ANISOU  164  CA  ALA A  20    21008  19946  14806   1677    259   1493       C  
ATOM    165  C   ALA A  20      -5.673 -12.966  38.687  1.00152.79           C  
ANISOU  165  C   ALA A  20    22077  20419  15558   1660    471   1534       C  
ATOM    166  O   ALA A  20      -6.592 -13.152  37.882  1.00151.57           O  
ANISOU  166  O   ALA A  20    21962  20153  15475   1395    584   1474       O  
ATOM    167  CB  ALA A  20      -6.323 -10.971  40.060  1.00146.76           C  
ANISOU  167  CB  ALA A  20    21027  19973  14761   1545    246   1529       C  
ATOM    168  N   ASP A  21      -4.951 -13.965  39.236  1.00152.05           N  
ANISOU  168  N   ASP A  21    22199  20203  15369   1956    520   1626       N  
ATOM    169  CA  ASP A  21      -5.147 -15.394  38.963  1.00153.78           C  
ANISOU  169  CA  ASP A  21    22747  20121  15562   1993    736   1677       C  
ATOM    170  C   ASP A  21      -6.014 -16.085  40.048  1.00159.06           C  
ANISOU  170  C   ASP A  21    23756  20572  16105   1992    891   1793       C  
ATOM    171  O   ASP A  21      -6.275 -17.288  39.943  1.00160.51           O  
ANISOU  171  O   ASP A  21    24259  20474  16254   2010   1103   1842       O  
ATOM    172  CB  ASP A  21      -3.782 -16.107  38.817  1.00157.44           C  
ANISOU  172  CB  ASP A  21    23260  20559  16001   2340    709   1701       C  
ATOM    173  CG  ASP A  21      -2.897 -16.085  40.052  1.00167.21           C  
ANISOU  173  CG  ASP A  21    24524  21903  17104   2719    557   1791       C  
ATOM    174  OD1 ASP A  21      -2.499 -14.978  40.481  1.00166.25           O  
ANISOU  174  OD1 ASP A  21    24122  22061  16985   2756    355   1746       O  
ATOM    175  OD2 ASP A  21      -2.561 -17.177  40.560  1.00174.81           O  
ANISOU  175  OD2 ASP A  21    25794  22670  17955   2990    639   1899       O  
ATOM    176  N   ASN A  22      -6.471 -15.323  41.065  1.00154.64           N  
ANISOU  176  N   ASN A  22    23142  20133  15480   1955    807   1829       N  
ATOM    177  CA  ASN A  22      -7.307 -15.830  42.157  1.00155.65           C  
ANISOU  177  CA  ASN A  22    23584  20074  15482   1932    960   1929       C  
ATOM    178  C   ASN A  22      -8.583 -14.997  42.318  1.00157.02           C  
ANISOU  178  C   ASN A  22    23624  20318  15719   1589    984   1854       C  
ATOM    179  O   ASN A  22      -8.531 -13.767  42.212  1.00154.75           O  
ANISOU  179  O   ASN A  22    23006  20290  15501   1509    794   1783       O  
ATOM    180  CB  ASN A  22      -6.525 -15.840  43.476  1.00158.11           C  
ANISOU  180  CB  ASN A  22    24019  20449  15606   2294    838   2059       C  
ATOM    181  CG  ASN A  22      -5.460 -16.906  43.558  1.00183.42           C  
ANISOU  181  CG  ASN A  22    27460  23519  18714   2669    853   2152       C  
ATOM    182  OD1 ASN A  22      -5.664 -17.978  44.137  1.00180.00           O  
ANISOU  182  OD1 ASN A  22    27443  22805  18143   2795   1033   2273       O  
ATOM    183  ND2 ASN A  22      -4.288 -16.627  43.007  1.00174.94           N  
ANISOU  183  ND2 ASN A  22    26131  22634  17706   2866    671   2091       N  
ATOM    184  N   ALA A  23      -9.722 -15.669  42.593  1.00153.55           N  
ANISOU  184  N   ALA A  23    23444  19639  15258   1388   1231   1858       N  
ATOM    185  CA  ALA A  23     -11.022 -15.026  42.822  1.00151.54           C  
ANISOU  185  CA  ALA A  23    23084  19425  15068   1066   1287   1769       C  
ATOM    186  C   ALA A  23     -11.034 -14.306  44.177  1.00153.51           C  
ANISOU  186  C   ALA A  23    23326  19803  15197   1169   1187   1845       C  
ATOM    187  O   ALA A  23     -11.760 -13.325  44.346  1.00151.33           O  
ANISOU  187  O   ALA A  23    22823  19682  14992    969   1119   1761       O  
ATOM    188  CB  ALA A  23     -12.139 -16.055  42.760  1.00153.92           C  
ANISOU  188  CB  ALA A  23    23670  19426  15385    829   1607   1727       C  
ATOM    189  N   ALA A  24     -10.218 -14.797  45.133  1.00150.75           N  
ANISOU  189  N   ALA A  24    23229  19392  14658   1495   1171   1998       N  
ATOM    190  CA  ALA A  24     -10.052 -14.218  46.466  1.00150.42           C  
ANISOU  190  CA  ALA A  24    23220  19472  14460   1648   1063   2081       C  
ATOM    191  C   ALA A  24      -9.241 -12.924  46.384  1.00150.55           C  
ANISOU  191  C   ALA A  24    22829  19845  14528   1753    747   2029       C  
ATOM    192  O   ALA A  24      -9.486 -12.003  47.164  1.00149.34           O  
ANISOU  192  O   ALA A  24    22549  19857  14335   1715    647   2017       O  
ATOM    193  CB  ALA A  24      -9.367 -15.215  47.390  1.00154.24           C  
ANISOU  193  CB  ALA A  24    24116  19779  14709   2000   1122   2256       C  
ATOM    194  N   GLN A  25      -8.286 -12.856  45.423  1.00144.94           N  
ANISOU  194  N   GLN A  25    21917  19243  13909   1869    611   1984       N  
ATOM    195  CA  GLN A  25      -7.424 -11.697  45.168  1.00142.21           C  
ANISOU  195  CA  GLN A  25    21186  19215  13632   1948    347   1909       C  
ATOM    196  C   GLN A  25      -8.233 -10.510  44.645  1.00141.06           C  
ANISOU  196  C   GLN A  25    20734  19216  13646   1620    298   1782       C  
ATOM    197  O   GLN A  25      -7.879  -9.368  44.938  1.00139.27           O  
ANISOU  197  O   GLN A  25    20247  19233  13437   1639    117   1735       O  
ATOM    198  CB  GLN A  25      -6.301 -12.052  44.179  1.00143.72           C  
ANISOU  198  CB  GLN A  25    21274  19441  13893   2114    277   1875       C  
ATOM    199  CG  GLN A  25      -5.026 -12.544  44.864  1.00159.92           C  
ANISOU  199  CG  GLN A  25    23426  21538  15799   2535    162   1955       C  
ATOM    200  CD  GLN A  25      -3.874 -12.760  43.908  1.00178.22           C  
ANISOU  200  CD  GLN A  25    25578  23929  18210   2693     83   1885       C  
ATOM    201  OE1 GLN A  25      -3.540 -11.906  43.077  1.00171.70           O  
ANISOU  201  OE1 GLN A  25    24419  23289  17529   2561    -13   1758       O  
ATOM    202  NE2 GLN A  25      -3.196 -13.887  44.051  1.00172.02           N  
ANISOU  202  NE2 GLN A  25    25031  22996  17335   2994    125   1964       N  
ATOM    203  N   VAL A  26      -9.321 -10.784  43.886  1.00135.25           N  
ANISOU  203  N   VAL A  26    20034  18332  13024   1330    458   1718       N  
ATOM    204  CA  VAL A  26     -10.247  -9.787  43.328  1.00132.16           C  
ANISOU  204  CA  VAL A  26    19388  18048  12780   1031    419   1594       C  
ATOM    205  C   VAL A  26     -10.976  -9.088  44.497  1.00134.05           C  
ANISOU  205  C   VAL A  26    19607  18356  12968    951    412   1599       C  
ATOM    206  O   VAL A  26     -10.985  -7.858  44.563  1.00131.95           O  
ANISOU  206  O   VAL A  26    19076  18299  12761    890    257   1538       O  
ATOM    207  CB  VAL A  26     -11.238 -10.421  42.304  1.00135.90           C  
ANISOU  207  CB  VAL A  26    19925  18343  13366    771    589   1509       C  
ATOM    208  CG1 VAL A  26     -12.209  -9.383  41.742  1.00133.71           C  
ANISOU  208  CG1 VAL A  26    19385  18190  13229    501    519   1374       C  
ATOM    209  CG2 VAL A  26     -10.495 -11.124  41.169  1.00136.04           C  
ANISOU  209  CG2 VAL A  26    19975  18289  13423    848    606   1500       C  
ATOM    210  N   LYS A  27     -11.538  -9.885  45.432  1.00130.98           N  
ANISOU  210  N   LYS A  27    19522  17781  12463    957    594   1674       N  
ATOM    211  CA  LYS A  27     -12.233  -9.426  46.640  1.00130.27           C  
ANISOU  211  CA  LYS A  27    19483  17716  12299    888    635   1686       C  
ATOM    212  C   LYS A  27     -11.250  -8.690  47.575  1.00132.11           C  
ANISOU  212  C   LYS A  27    19629  18163  12405   1137    428   1752       C  
ATOM    213  O   LYS A  27     -11.647  -7.733  48.241  1.00130.39           O  
ANISOU  213  O   LYS A  27    19269  18085  12189   1053    362   1710       O  
ATOM    214  CB  LYS A  27     -12.880 -10.630  47.351  1.00135.25           C  
ANISOU  214  CB  LYS A  27    20522  18059  12809    861    912   1760       C  
ATOM    215  CG  LYS A  27     -13.752 -10.289  48.558  1.00151.16           C  
ANISOU  215  CG  LYS A  27    22629  20056  14751    737   1020   1755       C  
ATOM    216  CD  LYS A  27     -14.131 -11.547  49.329  1.00163.46           C  
ANISOU  216  CD  LYS A  27    24650  21305  16151    748   1312   1848       C  
ATOM    217  CE  LYS A  27     -14.359 -11.286  50.797  1.00172.55           C  
ANISOU  217  CE  LYS A  27    25989  22458  17117    806   1362   1922       C  
ATOM    218  NZ  LYS A  27     -14.714 -12.535  51.523  1.00182.08           N  
ANISOU  218  NZ  LYS A  27    27705  23336  18142    832   1665   2028       N  
ATOM    219  N   ASP A  28      -9.970  -9.130  47.597  1.00128.74           N  
ANISOU  219  N   ASP A  28    19269  17768  11877   1444    323   1834       N  
ATOM    220  CA  ASP A  28      -8.893  -8.552  48.407  1.00128.45           C  
ANISOU  220  CA  ASP A  28    19136  17950  11717   1714    110   1870       C  
ATOM    221  C   ASP A  28      -8.453  -7.187  47.857  1.00128.18           C  
ANISOU  221  C   ASP A  28    18679  18197  11826   1641    -95   1746       C  
ATOM    222  O   ASP A  28      -8.247  -6.259  48.646  1.00127.54           O  
ANISOU  222  O   ASP A  28    18457  18309  11695   1680   -224   1719       O  
ATOM    223  CB  ASP A  28      -7.692  -9.514  48.470  1.00132.49           C  
ANISOU  223  CB  ASP A  28    19824  18411  12103   2069     61   1964       C  
ATOM    224  CG  ASP A  28      -6.569  -9.069  49.386  1.00144.64           C  
ANISOU  224  CG  ASP A  28    21282  20179  13495   2383   -165   1986       C  
ATOM    225  OD1 ASP A  28      -6.776  -9.060  50.621  1.00146.80           O  
ANISOU  225  OD1 ASP A  28    21733  20455  13588   2470   -166   2056       O  
ATOM    226  OD2 ASP A  28      -5.470  -8.777  48.874  1.00149.96           O  
ANISOU  226  OD2 ASP A  28    21724  21028  14228   2544   -333   1921       O  
ATOM    227  N   ALA A  29      -8.298  -7.071  46.514  1.00121.39           N  
ANISOU  227  N   ALA A  29    17640  17349  11134   1533   -112   1668       N  
ATOM    228  CA  ALA A  29      -7.885  -5.835  45.845  1.00118.23           C  
ANISOU  228  CA  ALA A  29    16885  17171  10867   1449   -269   1552       C  
ATOM    229  C   ALA A  29      -8.978  -4.760  45.915  1.00118.15           C  
ANISOU  229  C   ALA A  29    16723  17219  10950   1180   -267   1479       C  
ATOM    230  O   ALA A  29      -8.649  -3.583  46.067  1.00116.59           O  
ANISOU  230  O   ALA A  29    16286  17221  10793   1160   -403   1409       O  
ATOM    231  CB  ALA A  29      -7.517  -6.114  44.401  1.00118.34           C  
ANISOU  231  CB  ALA A  29    16818  17141  11005   1402   -254   1501       C  
ATOM    232  N   LEU A  30     -10.268  -5.165  45.823  1.00113.01           N  
ANISOU  232  N   LEU A  30    16205  16394  10339    976   -108   1478       N  
ATOM    233  CA  LEU A  30     -11.424  -4.266  45.920  1.00110.86           C  
ANISOU  233  CA  LEU A  30    15797  16162  10163    734    -96   1395       C  
ATOM    234  C   LEU A  30     -11.585  -3.691  47.342  1.00114.38           C  
ANISOU  234  C   LEU A  30    16254  16698  10505    773   -120   1417       C  
ATOM    235  O   LEU A  30     -12.007  -2.540  47.484  1.00113.09           O  
ANISOU  235  O   LEU A  30    15889  16663  10419    650   -192   1338       O  
ATOM    236  CB  LEU A  30     -12.721  -4.988  45.516  1.00111.04           C  
ANISOU  236  CB  LEU A  30    15948  15982  10258    518     90   1358       C  
ATOM    237  CG  LEU A  30     -12.985  -5.227  44.029  1.00114.84           C  
ANISOU  237  CG  LEU A  30    16354  16406  10874    392    100   1284       C  
ATOM    238  CD1 LEU A  30     -14.063  -6.275  43.842  1.00115.92           C  
ANISOU  238  CD1 LEU A  30    16679  16325  11041    231    310   1252       C  
ATOM    239  CD2 LEU A  30     -13.381  -3.940  43.311  1.00115.31           C  
ANISOU  239  CD2 LEU A  30    16134  16612  11068    247    -36   1174       C  
ATOM    240  N   THR A  31     -11.263  -4.499  48.384  1.00111.41           N  
ANISOU  240  N   THR A  31    16137  16248   9947    950    -57   1524       N  
ATOM    241  CA  THR A  31     -11.350  -4.116  49.799  1.00111.46           C  
ANISOU  241  CA  THR A  31    16213  16325   9810   1013    -70   1557       C  
ATOM    242  C   THR A  31     -10.288  -3.056  50.121  1.00113.54           C  
ANISOU  242  C   THR A  31    16235  16859  10046   1160   -297   1519       C  
ATOM    243  O   THR A  31     -10.623  -2.032  50.720  1.00112.65           O  
ANISOU  243  O   THR A  31    15983  16874   9945   1070   -347   1458       O  
ATOM    244  CB  THR A  31     -11.226  -5.362  50.706  1.00120.88           C  
ANISOU  244  CB  THR A  31    17798  17342  10789   1189     60   1694       C  
ATOM    245  OG1 THR A  31     -12.254  -6.288  50.357  1.00122.41           O  
ANISOU  245  OG1 THR A  31    18204  17276  11030   1012    300   1702       O  
ATOM    246  CG2 THR A  31     -11.338  -5.031  52.196  1.00118.11           C  
ANISOU  246  CG2 THR A  31    17571  17049  10257   1255     60   1735       C  
ATOM    247  N   LYS A  32      -9.021  -3.299  49.720  1.00109.40           N  
ANISOU  247  N   LYS A  32    15651  16420   9495   1375   -420   1533       N  
ATOM    248  CA  LYS A  32      -7.898  -2.387  49.951  1.00108.75           C  
ANISOU  248  CA  LYS A  32    15322  16600   9400   1514   -622   1464       C  
ATOM    249  C   LYS A  32      -8.109  -1.036  49.260  1.00110.68           C  
ANISOU  249  C   LYS A  32    15251  16973   9830   1296   -683   1335       C  
ATOM    250  O   LYS A  32      -7.684  -0.011  49.796  1.00110.45           O  
ANISOU  250  O   LYS A  32    15035  17141   9791   1310   -797   1259       O  
ATOM    251  CB  LYS A  32      -6.584  -3.015  49.477  1.00112.03           C  
ANISOU  251  CB  LYS A  32    15722  17061   9784   1764   -711   1476       C  
ATOM    252  CG  LYS A  32      -5.889  -3.845  50.539  1.00123.60           C  
ANISOU  252  CG  LYS A  32    17410  18531  11022   2085   -763   1571       C  
ATOM    253  CD  LYS A  32      -4.494  -4.258  50.084  1.00132.66           C  
ANISOU  253  CD  LYS A  32    18466  19775  12162   2352   -886   1542       C  
ATOM    254  CE  LYS A  32      -4.396  -5.721  49.721  1.00142.53           C  
ANISOU  254  CE  LYS A  32    20012  20788  13354   2507   -776   1660       C  
ATOM    255  NZ  LYS A  32      -5.162  -6.048  48.487  1.00148.51           N  
ANISOU  255  NZ  LYS A  32    20794  21349  14284   2255   -609   1657       N  
ATOM    256  N   MET A  33      -8.770  -1.040  48.083  1.00105.29           N  
ANISOU  256  N   MET A  33    14527  16173   9305   1102   -606   1306       N  
ATOM    257  CA  MET A  33      -9.088   0.155  47.295  1.00102.84           C  
ANISOU  257  CA  MET A  33    13976  15938   9159    906   -652   1201       C  
ATOM    258  C   MET A  33     -10.168   0.990  47.967  1.00104.65           C  
ANISOU  258  C   MET A  33    14158  16187   9419    741   -626   1161       C  
ATOM    259  O   MET A  33     -10.107   2.220  47.905  1.00103.28           O  
ANISOU  259  O   MET A  33    13780  16140   9322    659   -704   1077       O  
ATOM    260  CB  MET A  33      -9.543  -0.235  45.887  1.00104.36           C  
ANISOU  260  CB  MET A  33    14187  15989   9475    776   -584   1189       C  
ATOM    261  CG  MET A  33      -8.453  -0.141  44.868  1.00107.79           C  
ANISOU  261  CG  MET A  33    14507  16486   9961    842   -649   1150       C  
ATOM    262  SD  MET A  33      -8.940  -0.884  43.301  1.00111.68           S  
ANISOU  262  SD  MET A  33    15086  16796  10551    720   -559   1151       S  
ATOM    263  CE  MET A  33     -10.009   0.403  42.648  1.00106.69           C  
ANISOU  263  CE  MET A  33    14302  16186  10048    478   -596   1064       C  
ATOM    264  N   ARG A  34     -11.160   0.320  48.602  1.00100.48           N  
ANISOU  264  N   ARG A  34    13823  15520   8834    684   -498   1213       N  
ATOM    265  CA  ARG A  34     -12.265   0.963  49.316  1.00 99.27           C  
ANISOU  265  CA  ARG A  34    13640  15367   8710    526   -442   1165       C  
ATOM    266  C   ARG A  34     -11.728   1.821  50.462  1.00102.46           C  
ANISOU  266  C   ARG A  34    13963  15951   9015    612   -535   1145       C  
ATOM    267  O   ARG A  34     -12.206   2.935  50.669  1.00101.09           O  
ANISOU  267  O   ARG A  34    13628  15859   8922    487   -563   1061       O  
ATOM    268  CB  ARG A  34     -13.253  -0.085  49.845  1.00 99.44           C  
ANISOU  268  CB  ARG A  34    13913  15196   8673    457   -253   1216       C  
ATOM    269  CG  ARG A  34     -14.670   0.444  49.945  1.00104.16           C  
ANISOU  269  CG  ARG A  34    14433  15751   9391    222   -162   1119       C  
ATOM    270  CD  ARG A  34     -15.593  -0.513  50.669  1.00102.97           C  
ANISOU  270  CD  ARG A  34    14530  15424   9170    140     55   1144       C  
ATOM    271  NE  ARG A  34     -16.948   0.028  50.779  1.00 98.31           N  
ANISOU  271  NE  ARG A  34    13827  14810   8715    -90    146   1018       N  
ATOM    272  CZ  ARG A  34     -17.365   0.818  51.764  1.00108.59           C  
ANISOU  272  CZ  ARG A  34    15070  16189   9999   -147    162    968       C  
ATOM    273  NH1 ARG A  34     -16.535   1.170  52.740  1.00 88.38           N  
ANISOU  273  NH1 ARG A  34    12561  13742   7278      4     86   1035       N  
ATOM    274  NH2 ARG A  34     -18.615   1.263  51.782  1.00 97.45           N  
ANISOU  274  NH2 ARG A  34    13541  14754   8734   -350    250    835       N  
ATOM    275  N   ALA A  35     -10.707   1.314  51.172  1.00 99.73           N  
ANISOU  275  N   ALA A  35    13725  15673   8496    838   -593   1211       N  
ATOM    276  CA  ALA A  35     -10.064   2.024  52.273  1.00 99.95           C  
ANISOU  276  CA  ALA A  35    13680  15893   8404    948   -701   1179       C  
ATOM    277  C   ALA A  35      -9.191   3.165  51.736  1.00101.46           C  
ANISOU  277  C   ALA A  35    13570  16283   8697    947   -848   1065       C  
ATOM    278  O   ALA A  35      -9.269   4.285  52.244  1.00100.99           O  
ANISOU  278  O   ALA A  35    13361  16359   8653    879   -898    979       O  
ATOM    279  CB  ALA A  35      -9.232   1.057  53.107  1.00102.81           C  
ANISOU  279  CB  ALA A  35    14260  16265   8536   1217   -735   1278       C  
ATOM    280  N   ALA A  36      -8.396   2.889  50.686  1.00 96.35           N  
ANISOU  280  N   ALA A  36    12845  15640   8123   1006   -893   1055       N  
ATOM    281  CA  ALA A  36      -7.492   3.854  50.049  1.00 94.86           C  
ANISOU  281  CA  ALA A  36    12396  15612   8034    992   -994    938       C  
ATOM    282  C   ALA A  36      -8.242   5.073  49.498  1.00 94.80           C  
ANISOU  282  C   ALA A  36    12239  15592   8190    755   -967    858       C  
ATOM    283  O   ALA A  36      -7.692   6.174  49.521  1.00 93.83           O  
ANISOU  283  O   ALA A  36    11924  15612   8116    714  -1028    749       O  
ATOM    284  CB  ALA A  36      -6.706   3.179  48.935  1.00 95.72           C  
ANISOU  284  CB  ALA A  36    12495  15684   8191   1079  -1005    948       C  
ATOM    285  N   ALA A  37      -9.495   4.878  49.032  1.00 88.89           N  
ANISOU  285  N   ALA A  37    11581  14671   7524    606   -873    900       N  
ATOM    286  CA  ALA A  37     -10.342   5.942  48.490  1.00 86.46           C  
ANISOU  286  CA  ALA A  37    11156  14331   7363    414   -859    831       C  
ATOM    287  C   ALA A  37     -10.887   6.842  49.608  1.00 87.74           C  
ANISOU  287  C   ALA A  37    11258  14568   7513    345   -857    777       C  
ATOM    288  O   ALA A  37     -10.918   8.064  49.445  1.00 85.90           O  
ANISOU  288  O   ALA A  37    10874  14395   7370    254   -889    691       O  
ATOM    289  CB  ALA A  37     -11.489   5.343  47.688  1.00 86.71           C  
ANISOU  289  CB  ALA A  37    11289  14179   7477    305   -780    869       C  
ATOM    290  N   LEU A  38     -11.294   6.238  50.746  1.00 84.54           N  
ANISOU  290  N   LEU A  38    10990  14144   6985    390   -805    827       N  
ATOM    291  CA  LEU A  38     -11.849   6.952  51.906  1.00 83.74           C  
ANISOU  291  CA  LEU A  38    10861  14105   6850    326   -781    778       C  
ATOM    292  C   LEU A  38     -10.805   7.852  52.574  1.00 85.96           C  
ANISOU  292  C   LEU A  38    11000  14593   7068    397   -884    699       C  
ATOM    293  O   LEU A  38     -11.174   8.896  53.114  1.00 84.87           O  
ANISOU  293  O   LEU A  38    10757  14518   6973    297   -880    614       O  
ATOM    294  CB  LEU A  38     -12.457   5.983  52.925  1.00 84.90           C  
ANISOU  294  CB  LEU A  38    11234  14166   6857    357   -677    854       C  
ATOM    295  CG  LEU A  38     -13.736   5.258  52.486  1.00 89.66           C  
ANISOU  295  CG  LEU A  38    11958  14568   7542    226   -534    883       C  
ATOM    296  CD1 LEU A  38     -14.001   4.061  53.365  1.00 91.97           C  
ANISOU  296  CD1 LEU A  38    12527  14752   7666    286   -409    975       C  
ATOM    297  CD2 LEU A  38     -14.947   6.183  52.488  1.00 91.21           C  
ANISOU  297  CD2 LEU A  38    12024  14741   7890     34   -483    779       C  
ATOM    298  N   ASP A  39      -9.511   7.478  52.497  1.00 82.75           N  
ANISOU  298  N   ASP A  39    10572  14297   6573    564   -973    706       N  
ATOM    299  CA  ASP A  39      -8.429   8.295  53.042  1.00 83.18           C  
ANISOU  299  CA  ASP A  39    10457  14570   6577    630  -1076    595       C  
ATOM    300  C   ASP A  39      -8.070   9.392  52.044  1.00 84.54           C  
ANISOU  300  C   ASP A  39    10421  14779   6921    507  -1090    484       C  
ATOM    301  O   ASP A  39      -7.717  10.501  52.448  1.00 84.45           O  
ANISOU  301  O   ASP A  39    10254  14899   6933    448  -1118    360       O  
ATOM    302  CB  ASP A  39      -7.197   7.454  53.409  1.00 87.18           C  
ANISOU  302  CB  ASP A  39    11001  15196   6926    873  -1175    617       C  
ATOM    303  CG  ASP A  39      -6.277   8.165  54.392  1.00103.15           C  
ANISOU  303  CG  ASP A  39    12871  17470   8850    960  -1289    487       C  
ATOM    304  OD1 ASP A  39      -5.196   8.632  53.964  1.00105.23           O  
ANISOU  304  OD1 ASP A  39    12929  17880   9174    991  -1361    364       O  
ATOM    305  OD2 ASP A  39      -6.656   8.288  55.585  1.00108.19           O  
ANISOU  305  OD2 ASP A  39    13590  18163   9352    982  -1296    491       O  
ATOM    306  N   ALA A  40      -8.184   9.091  50.738  1.00 78.84           N  
ANISOU  306  N   ALA A  40     9718  13927   6310    461  -1056    525       N  
ATOM    307  CA  ALA A  40      -7.939  10.059  49.671  1.00 76.46           C  
ANISOU  307  CA  ALA A  40     9283  13613   6154    341  -1045    442       C  
ATOM    308  C   ALA A  40      -9.036  11.136  49.683  1.00 76.85           C  
ANISOU  308  C   ALA A  40     9306  13586   6309    174   -998    409       C  
ATOM    309  O   ALA A  40      -8.734  12.305  49.446  1.00 77.02           O  
ANISOU  309  O   ALA A  40     9211  13644   6410     83   -990    310       O  
ATOM    310  CB  ALA A  40      -7.884   9.356  48.324  1.00 76.47           C  
ANISOU  310  CB  ALA A  40     9354  13486   6215    349  -1021    507       C  
ATOM    311  N   GLN A  41     -10.291  10.743  50.012  1.00 69.85           N  
ANISOU  311  N   GLN A  41     8528  12589   5422    135   -955    478       N  
ATOM    312  CA  GLN A  41     -11.454  11.630  50.119  1.00 68.49           C  
ANISOU  312  CA  GLN A  41     8327  12345   5352      2   -915    438       C  
ATOM    313  C   GLN A  41     -11.259  12.691  51.228  1.00 73.18           C  
ANISOU  313  C   GLN A  41     8816  13069   5920    -34   -918    337       C  
ATOM    314  O   GLN A  41     -11.733  13.824  51.082  1.00 71.46           O  
ANISOU  314  O   GLN A  41     8522  12820   5808   -138   -897    265       O  
ATOM    315  CB  GLN A  41     -12.716  10.801  50.393  1.00 69.44           C  
ANISOU  315  CB  GLN A  41     8569  12347   5470    -24   -855    505       C  
ATOM    316  CG  GLN A  41     -14.020  11.573  50.240  1.00 75.86           C  
ANISOU  316  CG  GLN A  41     9332  13073   6417   -150   -820    450       C  
ATOM    317  CD  GLN A  41     -15.220  10.735  50.587  1.00 90.34           C  
ANISOU  317  CD  GLN A  41    11259  14809   8259   -194   -740    476       C  
ATOM    318  OE1 GLN A  41     -15.264  10.045  51.609  1.00 86.17           O  
ANISOU  318  OE1 GLN A  41    10828  14299   7614   -167   -678    509       O  
ATOM    319  NE2 GLN A  41     -16.240  10.802  49.753  1.00 84.65           N  
ANISOU  319  NE2 GLN A  41    10513  13981   7669   -265   -734    449       N  
ATOM    320  N   LYS A  42     -10.559  12.311  52.327  1.00 71.99           N  
ANISOU  320  N   LYS A  42     8672  13061   5619     64   -950    327       N  
ATOM    321  CA  LYS A  42     -10.244  13.180  53.469  1.00 72.68           C  
ANISOU  321  CA  LYS A  42     8665  13300   5648     44   -964    220       C  
ATOM    322  C   LYS A  42      -9.239  14.266  53.087  1.00 78.97           C  
ANISOU  322  C   LYS A  42     9290  14204   6511     -1   -991     88       C  
ATOM    323  O   LYS A  42      -9.264  15.352  53.675  1.00 78.96           O  
ANISOU  323  O   LYS A  42     9194  14268   6540    -90   -968    -26       O  
ATOM    324  CB  LYS A  42      -9.678  12.363  54.644  1.00 75.80           C  
ANISOU  324  CB  LYS A  42     9138  13827   5835    194  -1014    249       C  
ATOM    325  CG  LYS A  42     -10.685  11.464  55.346  1.00 85.85           C  
ANISOU  325  CG  LYS A  42    10611  14993   7014    213   -946    357       C  
ATOM    326  CD  LYS A  42     -10.045  10.719  56.504  1.00 92.11           C  
ANISOU  326  CD  LYS A  42    11522  15907   7569    383   -999    394       C  
ATOM    327  CE  LYS A  42     -10.160   9.220  56.376  1.00100.59           C  
ANISOU  327  CE  LYS A  42    12824  16859   8538    509   -972    547       C  
ATOM    328  NZ  LYS A  42     -11.513   8.725  56.747  1.00108.13           N  
ANISOU  328  NZ  LYS A  42    13963  17635   9486    409   -824    619       N  
ATOM    329  N   ALA A  43      -8.338  13.957  52.124  1.00 76.77           N  
ANISOU  329  N   ALA A  43     8976  13938   6257     49  -1021     89       N  
ATOM    330  CA  ALA A  43      -7.269  14.848  51.668  1.00 77.57           C  
ANISOU  330  CA  ALA A  43     8921  14131   6420     -6  -1017    -51       C  
ATOM    331  C   ALA A  43      -7.790  16.041  50.873  1.00 81.21           C  
ANISOU  331  C   ALA A  43     9369  14452   7034   -170   -933    -92       C  
ATOM    332  O   ALA A  43      -8.888  16.000  50.318  1.00 79.24           O  
ANISOU  332  O   ALA A  43     9227  14029   6854   -208   -907      4       O  
ATOM    333  CB  ALA A  43      -6.263  14.074  50.826  1.00 78.70           C  
ANISOU  333  CB  ALA A  43     9048  14302   6552     89  -1048    -36       C  
ATOM    334  N   THR A  44      -6.990  17.113  50.842  1.00 79.76           N  
ANISOU  334  N   THR A  44     9058  14347   6899   -260   -890   -248       N  
ATOM    335  CA  THR A  44      -7.295  18.328  50.098  1.00 80.12           C  
ANISOU  335  CA  THR A  44     9118  14251   7072   -407   -794   -297       C  
ATOM    336  C   THR A  44      -6.271  18.456  48.948  1.00 86.25           C  
ANISOU  336  C   THR A  44     9872  15003   7895   -447   -739   -352       C  
ATOM    337  O   THR A  44      -5.063  18.535  49.203  1.00 87.25           O  
ANISOU  337  O   THR A  44     9856  15300   7996   -448   -733   -492       O  
ATOM    338  CB  THR A  44      -7.378  19.578  51.008  1.00 88.78           C  
ANISOU  338  CB  THR A  44    10128  15410   8196   -512   -742   -438       C  
ATOM    339  OG1 THR A  44      -7.417  20.747  50.187  1.00 84.19           O  
ANISOU  339  OG1 THR A  44     9581  14680   7729   -642   -633   -494       O  
ATOM    340  CG2 THR A  44      -6.214  19.687  52.004  1.00 92.95           C  
ANISOU  340  CG2 THR A  44    10484  16193   8642   -499   -771   -606       C  
ATOM    341  N   PRO A  45      -6.733  18.434  47.676  1.00 82.87           N  
ANISOU  341  N   PRO A  45     9583  14374   7528   -476   -699   -255       N  
ATOM    342  CA  PRO A  45      -5.789  18.566  46.557  1.00 83.55           C  
ANISOU  342  CA  PRO A  45     9677  14420   7647   -529   -621   -307       C  
ATOM    343  C   PRO A  45      -5.101  19.936  46.549  1.00 89.98           C  
ANISOU  343  C   PRO A  45    10422  15245   8522   -685   -488   -486       C  
ATOM    344  O   PRO A  45      -5.767  20.939  46.825  1.00 88.97           O  
ANISOU  344  O   PRO A  45    10338  15028   8437   -762   -440   -506       O  
ATOM    345  CB  PRO A  45      -6.674  18.381  45.317  1.00 84.33           C  
ANISOU  345  CB  PRO A  45     9976  14290   7777   -525   -616   -157       C  
ATOM    346  CG  PRO A  45      -7.953  17.798  45.812  1.00 87.83           C  
ANISOU  346  CG  PRO A  45    10473  14693   8205   -446   -713    -33       C  
ATOM    347  CD  PRO A  45      -8.123  18.334  47.189  1.00 83.61           C  
ANISOU  347  CD  PRO A  45     9828  14278   7661   -465   -722   -114       C  
ATOM    348  N   PRO A  46      -3.779  20.008  46.236  1.00 89.52           N  
ANISOU  348  N   PRO A  46    10254  15284   8474   -740   -411   -633       N  
ATOM    349  CA  PRO A  46      -3.089  21.315  46.214  1.00 91.27           C  
ANISOU  349  CA  PRO A  46    10411  15507   8761   -919   -248   -832       C  
ATOM    350  C   PRO A  46      -3.712  22.310  45.223  1.00 96.18           C  
ANISOU  350  C   PRO A  46    11260  15846   9439  -1035   -112   -772       C  
ATOM    351  O   PRO A  46      -3.611  23.518  45.440  1.00 97.12           O  
ANISOU  351  O   PRO A  46    11381  15912   9607  -1176     21   -898       O  
ATOM    352  CB  PRO A  46      -1.651  20.954  45.821  1.00 94.29           C  
ANISOU  352  CB  PRO A  46    10645  16027   9153   -945   -188   -988       C  
ATOM    353  CG  PRO A  46      -1.501  19.513  46.201  1.00 98.15           C  
ANISOU  353  CG  PRO A  46    11057  16670   9565   -742   -365   -901       C  
ATOM    354  CD  PRO A  46      -2.846  18.912  45.904  1.00 91.88           C  
ANISOU  354  CD  PRO A  46    10475  15699   8738   -647   -453   -646       C  
ATOM    355  N   LYS A  47      -4.393  21.804  44.172  1.00 92.10           N  
ANISOU  355  N   LYS A  47    10946  15145   8905   -966   -151   -584       N  
ATOM    356  CA  LYS A  47      -5.112  22.611  43.177  1.00 92.32           C  
ANISOU  356  CA  LYS A  47    11227  14898   8954  -1020    -68   -495       C  
ATOM    357  C   LYS A  47      -6.303  23.365  43.821  1.00 96.26           C  
ANISOU  357  C   LYS A  47    11777  15314   9483   -999   -114   -448       C  
ATOM    358  O   LYS A  47      -6.689  24.437  43.339  1.00 96.40           O  
ANISOU  358  O   LYS A  47    11968  15131   9530  -1059    -17   -441       O  
ATOM    359  CB  LYS A  47      -5.634  21.719  42.033  1.00 94.16           C  
ANISOU  359  CB  LYS A  47    11635  14999   9142   -921   -144   -315       C  
ATOM    360  CG  LYS A  47      -4.563  21.135  41.126  1.00110.89           C  
ANISOU  360  CG  LYS A  47    13767  17129  11238   -958    -59   -354       C  
ATOM    361  CD  LYS A  47      -5.197  20.388  39.954  1.00120.94           C  
ANISOU  361  CD  LYS A  47    15245  18249  12460   -873   -127   -179       C  
ATOM    362  CE  LYS A  47      -4.165  19.866  38.986  1.00130.96           C  
ANISOU  362  CE  LYS A  47    16543  19511  13703   -917    -27   -219       C  
ATOM    363  NZ  LYS A  47      -4.794  19.177  37.830  1.00139.61           N  
ANISOU  363  NZ  LYS A  47    17853  20455  14738   -843    -89    -58       N  
ATOM    364  N   LEU A  48      -6.886  22.791  44.898  1.00 91.80           N  
ANISOU  364  N   LEU A  48    11079  14894   8906   -906   -255   -415       N  
ATOM    365  CA  LEU A  48      -8.031  23.368  45.603  1.00 91.24           C  
ANISOU  365  CA  LEU A  48    11027  14769   8871   -882   -299   -386       C  
ATOM    366  C   LEU A  48      -7.724  23.693  47.083  1.00 94.98           C  
ANISOU  366  C   LEU A  48    11303  15439   9344   -928   -293   -527       C  
ATOM    367  O   LEU A  48      -8.656  23.696  47.890  1.00 94.00           O  
ANISOU  367  O   LEU A  48    11154  15332   9229   -881   -361   -493       O  
ATOM    368  CB  LEU A  48      -9.268  22.434  45.530  1.00 90.14           C  
ANISOU  368  CB  LEU A  48    10941  14591   8718   -743   -455   -220       C  
ATOM    369  CG  LEU A  48      -9.444  21.504  44.329  1.00 93.98           C  
ANISOU  369  CG  LEU A  48    11552  14984   9170   -668   -516    -87       C  
ATOM    370  CD1 LEU A  48     -10.436  20.412  44.653  1.00 93.02           C  
ANISOU  370  CD1 LEU A  48    11409  14900   9036   -558   -653     18       C  
ATOM    371  CD2 LEU A  48      -9.872  22.266  43.088  1.00 96.70           C  
ANISOU  371  CD2 LEU A  48    12115  15094   9532   -679   -471    -34       C  
ATOM    372  N   GLU A  49      -6.449  23.987  47.444  1.00 92.36           N  
ANISOU  372  N   GLU A  49    10827  15261   9003  -1022   -209   -702       N  
ATOM    373  CA  GLU A  49      -6.114  24.324  48.839  1.00 92.93           C  
ANISOU  373  CA  GLU A  49    10710  15539   9059  -1063   -215   -857       C  
ATOM    374  C   GLU A  49      -6.548  25.773  49.179  1.00 96.54           C  
ANISOU  374  C   GLU A  49    11214  15878   9589  -1186    -91   -950       C  
ATOM    375  O   GLU A  49      -6.818  26.075  50.341  1.00 95.76           O  
ANISOU  375  O   GLU A  49    11014  15890   9480  -1198   -116  -1025       O  
ATOM    376  CB  GLU A  49      -4.628  24.078  49.166  1.00 95.60           C  
ANISOU  376  CB  GLU A  49    10847  16112   9363  -1106   -194  -1041       C  
ATOM    377  CG  GLU A  49      -3.628  24.922  48.396  1.00110.61           C  
ANISOU  377  CG  GLU A  49    12747  17950  11331  -1275     -2  -1203       C  
ATOM    378  CD  GLU A  49      -2.188  24.686  48.808  1.00138.48           C  
ANISOU  378  CD  GLU A  49    16025  21746  14846  -1317     12  -1431       C  
ATOM    379  OE1 GLU A  49      -1.639  23.612  48.471  1.00134.51           O  
ANISOU  379  OE1 GLU A  49    15459  21349  14302  -1208    -75  -1395       O  
ATOM    380  OE2 GLU A  49      -1.610  25.575  49.473  1.00137.60           O  
ANISOU  380  OE2 GLU A  49    15772  21743  14767  -1455    109  -1659       O  
ATOM    381  N   ASP A  50      -6.650  26.639  48.151  1.00 93.53           N  
ANISOU  381  N   ASP A  50    11012  15255   9270  -1267     47   -937       N  
ATOM    382  CA  ASP A  50      -7.112  28.032  48.240  1.00 93.94           C  
ANISOU  382  CA  ASP A  50    11169  15130   9392  -1364    182  -1000       C  
ATOM    383  C   ASP A  50      -8.643  28.077  48.372  1.00 94.47           C  
ANISOU  383  C   ASP A  50    11341  15065   9487  -1240     78   -848       C  
ATOM    384  O   ASP A  50      -9.208  29.080  48.821  1.00 94.85           O  
ANISOU  384  O   ASP A  50    11423  15022   9593  -1281    145   -905       O  
ATOM    385  CB  ASP A  50      -6.670  28.814  46.988  1.00 97.46           C  
ANISOU  385  CB  ASP A  50    11823  15338   9870  -1467    368  -1015       C  
ATOM    386  CG  ASP A  50      -7.114  28.176  45.678  1.00111.42           C  
ANISOU  386  CG  ASP A  50    13797  16935  11603  -1352    299   -811       C  
ATOM    387  OD1 ASP A  50      -8.218  28.522  45.189  1.00111.86           O  
ANISOU  387  OD1 ASP A  50    14048  16782  11673  -1259    255   -674       O  
ATOM    388  OD2 ASP A  50      -6.371  27.313  45.158  1.00118.50           O  
ANISOU  388  OD2 ASP A  50    14650  17916  12456  -1346    280   -800       O  
ATOM    389  N   LYS A  51      -9.303  26.984  47.943  1.00 87.20           N  
ANISOU  389  N   LYS A  51    10465  14134   8533  -1093    -78   -673       N  
ATOM    390  CA  LYS A  51     -10.751  26.798  47.958  1.00 84.78           C  
ANISOU  390  CA  LYS A  51    10227  13727   8259   -969   -192   -545       C  
ATOM    391  C   LYS A  51     -11.247  26.344  49.335  1.00 84.98           C  
ANISOU  391  C   LYS A  51    10083  13933   8271   -939   -273   -576       C  
ATOM    392  O   LYS A  51     -10.567  25.582  50.036  1.00 83.14           O  
ANISOU  392  O   LYS A  51     9713  13913   7963   -945   -313   -618       O  
ATOM    393  CB  LYS A  51     -11.173  25.764  46.884  1.00 86.13           C  
ANISOU  393  CB  LYS A  51    10504  13826   8398   -849   -311   -375       C  
ATOM    394  CG  LYS A  51     -10.737  26.091  45.448  1.00 98.93           C  
ANISOU  394  CG  LYS A  51    12324  15261  10002   -866   -239   -326       C  
ATOM    395  CD  LYS A  51     -11.721  27.007  44.710  1.00109.18           C  
ANISOU  395  CD  LYS A  51    13838  16303  11343   -801   -235   -259       C  
ATOM    396  CE  LYS A  51     -11.082  27.773  43.568  1.00120.20           C  
ANISOU  396  CE  LYS A  51    15469  17496  12704   -860    -95   -252       C  
ATOM    397  NZ  LYS A  51     -10.755  26.905  42.404  1.00125.48           N  
ANISOU  397  NZ  LYS A  51    16240  18140  13297   -816   -146   -149       N  
ATOM    398  N   SER A  52     -12.451  26.812  49.704  1.00 80.51           N  
ANISOU  398  N   SER A  52     9542  13276   7773   -897   -295   -559       N  
ATOM    399  CA  SER A  52     -13.165  26.447  50.931  1.00 79.34           C  
ANISOU  399  CA  SER A  52     9271  13253   7621   -874   -347   -584       C  
ATOM    400  C   SER A  52     -13.510  24.941  50.886  1.00 80.92           C  
ANISOU  400  C   SER A  52     9447  13539   7758   -777   -473   -463       C  
ATOM    401  O   SER A  52     -13.726  24.417  49.787  1.00 79.04           O  
ANISOU  401  O   SER A  52     9303  13203   7527   -708   -533   -353       O  
ATOM    402  CB  SER A  52     -14.432  27.294  51.064  1.00 82.80           C  
ANISOU  402  CB  SER A  52     9751  13538   8170   -843   -330   -598       C  
ATOM    403  OG  SER A  52     -15.471  26.661  51.797  1.00 90.16           O  
ANISOU  403  OG  SER A  52    10599  14542   9118   -796   -393   -586       O  
ATOM    404  N   PRO A  53     -13.582  24.214  52.028  1.00 76.89           N  
ANISOU  404  N   PRO A  53     8839  13198   7177   -771   -506   -480       N  
ATOM    405  CA  PRO A  53     -13.924  22.782  51.947  1.00 75.93           C  
ANISOU  405  CA  PRO A  53     8734  13120   6994   -686   -595   -363       C  
ATOM    406  C   PRO A  53     -15.358  22.534  51.461  1.00 79.07           C  
ANISOU  406  C   PRO A  53     9180  13377   7484   -630   -637   -294       C  
ATOM    407  O   PRO A  53     -15.641  21.437  50.984  1.00 77.98           O  
ANISOU  407  O   PRO A  53     9081  13226   7321   -572   -700   -198       O  
ATOM    408  CB  PRO A  53     -13.722  22.270  53.372  1.00 77.97           C  
ANISOU  408  CB  PRO A  53     8918  13564   7143   -695   -594   -408       C  
ATOM    409  CG  PRO A  53     -13.075  23.365  54.116  1.00 83.03           C  
ANISOU  409  CG  PRO A  53     9479  14290   7776   -784   -524   -557       C  
ATOM    410  CD  PRO A  53     -13.372  24.637  53.426  1.00 78.84           C  
ANISOU  410  CD  PRO A  53     8985  13590   7382   -840   -454   -605       C  
ATOM    411  N   ASP A  54     -16.243  23.554  51.534  1.00 76.30           N  
ANISOU  411  N   ASP A  54     8822  12921   7249   -644   -604   -357       N  
ATOM    412  CA  ASP A  54     -17.639  23.451  51.073  1.00 76.01           C  
ANISOU  412  CA  ASP A  54     8795  12765   7320   -579   -655   -332       C  
ATOM    413  C   ASP A  54     -17.835  24.060  49.673  1.00 79.31           C  
ANISOU  413  C   ASP A  54     9320  13010   7805   -507   -707   -286       C  
ATOM    414  O   ASP A  54     -18.973  24.256  49.247  1.00 80.15           O  
ANISOU  414  O   ASP A  54     9429  13017   8009   -431   -768   -292       O  
ATOM    415  CB  ASP A  54     -18.602  24.115  52.070  1.00 78.08           C  
ANISOU  415  CB  ASP A  54     8972  13024   7670   -611   -597   -442       C  
ATOM    416  CG  ASP A  54     -18.503  23.563  53.466  1.00 87.18           C  
ANISOU  416  CG  ASP A  54    10054  14332   8737   -680   -537   -486       C  
ATOM    417  OD1 ASP A  54     -17.956  24.262  54.334  1.00 89.07           O  
ANISOU  417  OD1 ASP A  54    10259  14647   8938   -750   -465   -572       O  
ATOM    418  OD2 ASP A  54     -18.974  22.427  53.690  1.00 93.18           O  
ANISOU  418  OD2 ASP A  54    10811  15132   9461   -666   -555   -440       O  
ATOM    419  N   SER A  55     -16.737  24.344  48.958  1.00 74.80           N  
ANISOU  419  N   SER A  55     8841  12403   7175   -527   -683   -252       N  
ATOM    420  CA  SER A  55     -16.778  24.912  47.610  1.00 74.60           C  
ANISOU  420  CA  SER A  55     8970  12200   7174   -464   -712   -197       C  
ATOM    421  C   SER A  55     -17.281  23.866  46.596  1.00 78.59           C  
ANISOU  421  C   SER A  55     9528  12673   7661   -371   -836    -94       C  
ATOM    422  O   SER A  55     -17.120  22.671  46.856  1.00 77.62           O  
ANISOU  422  O   SER A  55     9340  12668   7486   -386   -863    -59       O  
ATOM    423  CB  SER A  55     -15.395  25.426  47.206  1.00 76.87           C  
ANISOU  423  CB  SER A  55     9342  12467   7397   -544   -613   -207       C  
ATOM    424  OG  SER A  55     -14.452  24.386  47.007  1.00 79.42           O  
ANISOU  424  OG  SER A  55     9642  12906   7628   -570   -626   -162       O  
ATOM    425  N   PRO A  56     -17.857  24.277  45.433  1.00 75.55           N  
ANISOU  425  N   PRO A  56     9276  12127   7302   -270   -912    -47       N  
ATOM    426  CA  PRO A  56     -18.306  23.282  44.432  1.00 74.73           C  
ANISOU  426  CA  PRO A  56     9218  12006   7170   -189  -1035     32       C  
ATOM    427  C   PRO A  56     -17.233  22.259  44.035  1.00 76.22           C  
ANISOU  427  C   PRO A  56     9446  12262   7250   -242  -1012    104       C  
ATOM    428  O   PRO A  56     -17.539  21.079  43.852  1.00 74.69           O  
ANISOU  428  O   PRO A  56     9214  12128   7036   -222  -1077    143       O  
ATOM    429  CB  PRO A  56     -18.666  24.146  43.219  1.00 77.48           C  
ANISOU  429  CB  PRO A  56     9750  12166   7522    -73  -1103     68       C  
ATOM    430  CG  PRO A  56     -18.990  25.470  43.772  1.00 82.92           C  
ANISOU  430  CG  PRO A  56    10443  12775   8289    -60  -1044     -5       C  
ATOM    431  CD  PRO A  56     -18.120  25.657  44.969  1.00 78.24           C  
ANISOU  431  CD  PRO A  56     9753  12289   7687   -214   -890    -65       C  
ATOM    432  N   GLU A  57     -15.981  22.730  43.918  1.00 72.48           N  
ANISOU  432  N   GLU A  57     9043  11780   6718   -316   -906    103       N  
ATOM    433  CA  GLU A  57     -14.795  21.972  43.526  1.00 71.82           C  
ANISOU  433  CA  GLU A  57     8986  11758   6544   -367   -864    144       C  
ATOM    434  C   GLU A  57     -14.450  20.870  44.550  1.00 74.48           C  
ANISOU  434  C   GLU A  57     9164  12283   6850   -397   -864    133       C  
ATOM    435  O   GLU A  57     -14.249  19.719  44.154  1.00 74.52           O  
ANISOU  435  O   GLU A  57     9182  12328   6805   -369   -906    196       O  
ATOM    436  CB  GLU A  57     -13.594  22.922  43.330  1.00 73.86           C  
ANISOU  436  CB  GLU A  57     9318  11972   6773   -459   -724     95       C  
ATOM    437  CG  GLU A  57     -13.760  23.933  42.196  1.00 85.92           C  
ANISOU  437  CG  GLU A  57    11073  13280   8294   -430   -693    126       C  
ATOM    438  CD  GLU A  57     -14.522  25.221  42.480  1.00103.81           C  
ANISOU  438  CD  GLU A  57    13393  15419  10630   -394   -678     86       C  
ATOM    439  OE1 GLU A  57     -14.936  25.445  43.641  1.00 87.48           O  
ANISOU  439  OE1 GLU A  57    11164  13442   8633   -414   -674     13       O  
ATOM    440  OE2 GLU A  57     -14.700  26.015  41.528  1.00 98.95           O  
ANISOU  440  OE2 GLU A  57    13002  14604   9992   -338   -665    128       O  
ATOM    441  N   MET A  58     -14.382  21.216  45.852  1.00 69.47           N  
ANISOU  441  N   MET A  58     8405  11757   6235   -447   -815     54       N  
ATOM    442  CA  MET A  58     -14.060  20.265  46.922  1.00 68.17           C  
ANISOU  442  CA  MET A  58     8125  11764   6014   -458   -815     45       C  
ATOM    443  C   MET A  58     -15.178  19.246  47.105  1.00 71.42           C  
ANISOU  443  C   MET A  58     8519  12175   6441   -407   -881     96       C  
ATOM    444  O   MET A  58     -14.900  18.065  47.322  1.00 70.20           O  
ANISOU  444  O   MET A  58     8360  12096   6216   -386   -893    146       O  
ATOM    445  CB  MET A  58     -13.772  20.993  48.243  1.00 70.42           C  
ANISOU  445  CB  MET A  58     8301  12156   6298   -522   -748    -62       C  
ATOM    446  CG  MET A  58     -12.374  21.574  48.304  1.00 73.85           C  
ANISOU  446  CG  MET A  58     8704  12665   6691   -590   -673   -141       C  
ATOM    447  SD  MET A  58     -11.075  20.312  48.398  1.00 77.37           S  
ANISOU  447  SD  MET A  58     9092  13286   7019   -553   -704   -121       S  
ATOM    448  CE  MET A  58     -11.137  19.919  50.154  1.00 74.84           C  
ANISOU  448  CE  MET A  58     8657  13158   6622   -533   -729   -170       C  
ATOM    449  N   LYS A  59     -16.438  19.714  46.976  1.00 68.35           N  
ANISOU  449  N   LYS A  59     8127  11695   6149   -385   -916     72       N  
ATOM    450  CA  LYS A  59     -17.655  18.919  47.059  1.00 67.68           C  
ANISOU  450  CA  LYS A  59     8004  11599   6111   -358   -962     77       C  
ATOM    451  C   LYS A  59     -17.696  17.906  45.916  1.00 72.39           C  
ANISOU  451  C   LYS A  59     8679  12147   6677   -313  -1029    156       C  
ATOM    452  O   LYS A  59     -18.094  16.765  46.146  1.00 73.00           O  
ANISOU  452  O   LYS A  59     8738  12258   6740   -320  -1027    174       O  
ATOM    453  CB  LYS A  59     -18.899  19.820  47.035  1.00 69.70           C  
ANISOU  453  CB  LYS A  59     8213  11774   6494   -331   -994      0       C  
ATOM    454  CG  LYS A  59     -19.215  20.451  48.381  1.00 75.63           C  
ANISOU  454  CG  LYS A  59     8861  12586   7289   -387   -915    -94       C  
ATOM    455  CD  LYS A  59     -20.570  21.155  48.394  1.00 80.02           C  
ANISOU  455  CD  LYS A  59     9349  13066   7988   -346   -947   -184       C  
ATOM    456  CE  LYS A  59     -20.984  21.538  49.797  1.00 87.03           C  
ANISOU  456  CE  LYS A  59    10128  14020   8920   -416   -851   -286       C  
ATOM    457  NZ  LYS A  59     -22.013  22.612  49.809  1.00 96.86           N  
ANISOU  457  NZ  LYS A  59    11308  15183  10313   -367   -868   -389       N  
ATOM    458  N   ASP A  60     -17.254  18.299  44.706  1.00 68.93           N  
ANISOU  458  N   ASP A  60     8348  11623   6220   -277  -1070    200       N  
ATOM    459  CA  ASP A  60     -17.226  17.397  43.557  1.00 68.87           C  
ANISOU  459  CA  ASP A  60     8429  11568   6172   -239  -1131    269       C  
ATOM    460  C   ASP A  60     -16.086  16.374  43.673  1.00 72.72           C  
ANISOU  460  C   ASP A  60     8937  12132   6562   -262  -1078    327       C  
ATOM    461  O   ASP A  60     -16.264  15.224  43.272  1.00 72.60           O  
ANISOU  461  O   ASP A  60     8953  12112   6520   -246  -1101    370       O  
ATOM    462  CB  ASP A  60     -17.121  18.169  42.249  1.00 71.70           C  
ANISOU  462  CB  ASP A  60     8925  11800   6518   -190  -1182    297       C  
ATOM    463  CG  ASP A  60     -17.365  17.284  41.044  1.00 87.58           C  
ANISOU  463  CG  ASP A  60    11029  13760   8488   -145  -1262    351       C  
ATOM    464  OD1 ASP A  60     -16.370  16.797  40.453  1.00 88.16           O  
ANISOU  464  OD1 ASP A  60    11187  13831   8479   -165  -1222    408       O  
ATOM    465  OD2 ASP A  60     -18.552  17.029  40.724  1.00 95.34           O  
ANISOU  465  OD2 ASP A  60    11983  14717   9525    -93  -1362    318       O  
ATOM    466  N   PHE A  61     -14.932  16.785  44.230  1.00 69.50           N  
ANISOU  466  N   PHE A  61     8503  11797   6106   -295  -1008    311       N  
ATOM    467  CA  PHE A  61     -13.779  15.915  44.468  1.00 69.33           C  
ANISOU  467  CA  PHE A  61     8473  11872   5997   -291   -971    342       C  
ATOM    468  C   PHE A  61     -14.170  14.755  45.419  1.00 72.96           C  
ANISOU  468  C   PHE A  61     8896  12405   6421   -269   -968    367       C  
ATOM    469  O   PHE A  61     -13.905  13.587  45.108  1.00 71.95           O  
ANISOU  469  O   PHE A  61     8822  12278   6239   -232   -970    429       O  
ATOM    470  CB  PHE A  61     -12.607  16.738  45.046  1.00 71.42           C  
ANISOU  470  CB  PHE A  61     8675  12227   6236   -331   -907    274       C  
ATOM    471  CG  PHE A  61     -11.458  15.934  45.614  1.00 72.90           C  
ANISOU  471  CG  PHE A  61     8804  12558   6336   -302   -889    270       C  
ATOM    472  CD1 PHE A  61     -10.580  15.254  44.775  1.00 76.06           C  
ANISOU  472  CD1 PHE A  61     9246  12957   6695   -272   -883    302       C  
ATOM    473  CD2 PHE A  61     -11.239  15.877  46.984  1.00 75.09           C  
ANISOU  473  CD2 PHE A  61     8990  12975   6568   -290   -883    225       C  
ATOM    474  CE1 PHE A  61      -9.517  14.516  45.301  1.00 77.31           C  
ANISOU  474  CE1 PHE A  61     9339  13254   6780   -215   -882    286       C  
ATOM    475  CE2 PHE A  61     -10.178  15.137  47.508  1.00 78.79           C  
ANISOU  475  CE2 PHE A  61     9410  13583   6941   -226   -894    217       C  
ATOM    476  CZ  PHE A  61      -9.315  14.473  46.663  1.00 77.04           C  
ANISOU  476  CZ  PHE A  61     9215  13363   6694   -182   -897    243       C  
ATOM    477  N   ARG A  62     -14.828  15.092  46.554  1.00 69.48           N  
ANISOU  477  N   ARG A  62     8385  12008   6008   -296   -946    318       N  
ATOM    478  CA  ARG A  62     -15.305  14.127  47.548  1.00 69.37           C  
ANISOU  478  CA  ARG A  62     8368  12039   5949   -292   -912    334       C  
ATOM    479  C   ARG A  62     -16.435  13.260  46.983  1.00 73.62           C  
ANISOU  479  C   ARG A  62     8953  12481   6540   -300   -921    357       C  
ATOM    480  O   ARG A  62     -16.501  12.070  47.292  1.00 73.77           O  
ANISOU  480  O   ARG A  62     9033  12497   6498   -290   -878    403       O  
ATOM    481  CB  ARG A  62     -15.789  14.838  48.814  1.00 67.92           C  
ANISOU  481  CB  ARG A  62     8108  11913   5785   -336   -870    258       C  
ATOM    482  CG  ARG A  62     -14.694  15.523  49.611  1.00 70.83           C  
ANISOU  482  CG  ARG A  62     8422  12405   6084   -337   -854    213       C  
ATOM    483  CD  ARG A  62     -15.215  15.990  50.957  1.00 71.36           C  
ANISOU  483  CD  ARG A  62     8435  12535   6145   -382   -804    142       C  
ATOM    484  NE  ARG A  62     -16.277  16.993  50.841  1.00 74.51           N  
ANISOU  484  NE  ARG A  62     8779  12850   6682   -438   -790     70       N  
ATOM    485  CZ  ARG A  62     -16.122  18.290  51.092  1.00 86.57           C  
ANISOU  485  CZ  ARG A  62    10244  14389   8261   -477   -771    -13       C  
ATOM    486  NH1 ARG A  62     -14.949  18.761  51.495  1.00 68.55           N  
ANISOU  486  NH1 ARG A  62     7930  12209   5907   -490   -758    -53       N  
ATOM    487  NH2 ARG A  62     -17.145  19.123  50.957  1.00 79.75           N  
ANISOU  487  NH2 ARG A  62     9343  13434   7524   -501   -764    -73       N  
ATOM    488  N   HIS A  63     -17.319  13.854  46.158  1.00 70.08           N  
ANISOU  488  N   HIS A  63     8479  11949   6198   -313   -975    314       N  
ATOM    489  CA  HIS A  63     -18.425  13.138  45.522  1.00 69.78           C  
ANISOU  489  CA  HIS A  63     8451  11838   6223   -324  -1003    297       C  
ATOM    490  C   HIS A  63     -17.896  12.066  44.561  1.00 73.83           C  
ANISOU  490  C   HIS A  63     9067  12313   6672   -296  -1018    375       C  
ATOM    491  O   HIS A  63     -18.512  11.005  44.448  1.00 73.76           O  
ANISOU  491  O   HIS A  63     9085  12268   6672   -322   -990    371       O  
ATOM    492  CB  HIS A  63     -19.364  14.097  44.792  1.00 70.73           C  
ANISOU  492  CB  HIS A  63     8519  11898   6457   -305  -1092    226       C  
ATOM    493  CG  HIS A  63     -20.546  13.405  44.193  1.00 74.80           C  
ANISOU  493  CG  HIS A  63     9005  12369   7045   -314  -1137    168       C  
ATOM    494  ND1 HIS A  63     -20.579  13.070  42.849  1.00 76.47           N  
ANISOU  494  ND1 HIS A  63     9287  12527   7243   -271  -1228    194       N  
ATOM    495  CD2 HIS A  63     -21.671  12.946  44.788  1.00 77.01           C  
ANISOU  495  CD2 HIS A  63     9191  12661   7409   -372  -1090     70       C  
ATOM    496  CE1 HIS A  63     -21.729  12.446  42.666  1.00 76.66           C  
ANISOU  496  CE1 HIS A  63     9241  12542   7345   -300  -1249    102       C  
ATOM    497  NE2 HIS A  63     -22.421  12.350  43.804  1.00 77.47           N  
ANISOU  497  NE2 HIS A  63     9237  12681   7516   -367  -1160     19       N  
ATOM    498  N   GLY A  64     -16.756  12.341  43.910  1.00 69.62           N  
ANISOU  498  N   GLY A  64     8589  11783   6078   -257  -1043    430       N  
ATOM    499  CA  GLY A  64     -16.089  11.401  43.013  1.00 68.96           C  
ANISOU  499  CA  GLY A  64     8603  11669   5931   -229  -1045    498       C  
ATOM    500  C   GLY A  64     -15.681  10.128  43.734  1.00 72.14           C  
ANISOU  500  C   GLY A  64     9046  12105   6257   -212   -971    548       C  
ATOM    501  O   GLY A  64     -15.833   9.028  43.197  1.00 70.97           O  
ANISOU  501  O   GLY A  64     8976  11900   6090   -208   -953    582       O  
ATOM    502  N   PHE A  65     -15.200  10.280  44.985  1.00 69.02           N  
ANISOU  502  N   PHE A  65     8614  11800   5812   -197   -927    548       N  
ATOM    503  CA  PHE A  65     -14.815   9.170  45.854  1.00 69.43           C  
ANISOU  503  CA  PHE A  65     8734  11881   5764   -151   -863    603       C  
ATOM    504  C   PHE A  65     -16.030   8.434  46.389  1.00 76.37           C  
ANISOU  504  C   PHE A  65     9657  12693   6666   -210   -788    589       C  
ATOM    505  O   PHE A  65     -15.915   7.249  46.679  1.00 75.96           O  
ANISOU  505  O   PHE A  65     9724  12600   6539   -182   -718    647       O  
ATOM    506  CB  PHE A  65     -13.917   9.637  47.003  1.00 70.81           C  
ANISOU  506  CB  PHE A  65     8864  12185   5855   -100   -860    597       C  
ATOM    507  CG  PHE A  65     -12.495   9.824  46.534  1.00 71.49           C  
ANISOU  507  CG  PHE A  65     8921  12344   5899    -32   -901    603       C  
ATOM    508  CD1 PHE A  65     -11.710   8.729  46.186  1.00 73.99           C  
ANISOU  508  CD1 PHE A  65     9315  12655   6144     59   -896    665       C  
ATOM    509  CD2 PHE A  65     -11.964  11.095  46.372  1.00 72.64           C  
ANISOU  509  CD2 PHE A  65     8963  12551   6085    -67   -928    531       C  
ATOM    510  CE1 PHE A  65     -10.415   8.904  45.698  1.00 74.70           C  
ANISOU  510  CE1 PHE A  65     9352  12817   6213    114   -924    642       C  
ATOM    511  CE2 PHE A  65     -10.662  11.268  45.905  1.00 75.15           C  
ANISOU  511  CE2 PHE A  65     9241  12935   6378    -30   -939    507       C  
ATOM    512  CZ  PHE A  65      -9.899  10.173  45.565  1.00 73.45           C  
ANISOU  512  CZ  PHE A  65     9078  12730   6101     61   -940    556       C  
ATOM    513  N   ASP A  66     -17.198   9.115  46.482  1.00 75.86           N  
ANISOU  513  N   ASP A  66     9505  12608   6711   -292   -792    502       N  
ATOM    514  CA  ASP A  66     -18.460   8.505  46.911  1.00 77.30           C  
ANISOU  514  CA  ASP A  66     9695  12730   6945   -377   -704    445       C  
ATOM    515  C   ASP A  66     -18.964   7.569  45.820  1.00 83.65           C  
ANISOU  515  C   ASP A  66    10549  13441   7794   -409   -700    436       C  
ATOM    516  O   ASP A  66     -19.356   6.448  46.138  1.00 85.11           O  
ANISOU  516  O   ASP A  66    10824  13561   7954   -459   -584    438       O  
ATOM    517  CB  ASP A  66     -19.529   9.562  47.261  1.00 79.37           C  
ANISOU  517  CB  ASP A  66     9814  13012   7331   -443   -720    326       C  
ATOM    518  CG  ASP A  66     -19.266  10.352  48.533  1.00 91.64           C  
ANISOU  518  CG  ASP A  66    11326  14649   8845   -442   -686    311       C  
ATOM    519  OD1 ASP A  66     -18.863   9.732  49.551  1.00 92.08           O  
ANISOU  519  OD1 ASP A  66    11475  14731   8781   -433   -598    360       O  
ATOM    520  OD2 ASP A  66     -19.504  11.583  48.528  1.00 98.21           O  
ANISOU  520  OD2 ASP A  66    12047  15512   9758   -447   -745    246       O  
ATOM    521  N   ILE A  67     -18.921   8.004  44.533  1.00 80.04           N  
ANISOU  521  N   ILE A  67    10056  12969   7389   -385   -816    424       N  
ATOM    522  CA  ILE A  67     -19.351   7.163  43.411  1.00 80.38           C  
ANISOU  522  CA  ILE A  67    10144  12936   7461   -412   -831    404       C  
ATOM    523  C   ILE A  67     -18.298   6.046  43.209  1.00 84.16           C  
ANISOU  523  C   ILE A  67    10774  13376   7826   -363   -769    515       C  
ATOM    524  O   ILE A  67     -18.686   4.924  42.890  1.00 85.93           O  
ANISOU  524  O   ILE A  67    11077  13522   8050   -409   -695    504       O  
ATOM    525  CB  ILE A  67     -19.726   7.934  42.090  1.00 83.44           C  
ANISOU  525  CB  ILE A  67    10473  13316   7914   -388   -982    353       C  
ATOM    526  CG1 ILE A  67     -20.003   6.999  40.886  1.00 84.60           C  
ANISOU  526  CG1 ILE A  67    10685  13399   8060   -408  -1007    335       C  
ATOM    527  CG2 ILE A  67     -18.738   9.008  41.705  1.00 83.74           C  
ANISOU  527  CG2 ILE A  67    10526  13384   7907   -312  -1061    418       C  
ATOM    528  CD1 ILE A  67     -21.439   6.370  40.836  1.00 97.53           C  
ANISOU  528  CD1 ILE A  67    12245  15013   9799   -504   -978    190       C  
ATOM    529  N   LEU A  68     -17.004   6.321  43.478  1.00 78.24           N  
ANISOU  529  N   LEU A  68    10057  12682   6987   -272   -789    602       N  
ATOM    530  CA  LEU A  68     -15.937   5.319  43.361  1.00 77.54           C  
ANISOU  530  CA  LEU A  68    10091  12573   6797   -194   -743    696       C  
ATOM    531  C   LEU A  68     -16.130   4.190  44.402  1.00 84.51           C  
ANISOU  531  C   LEU A  68    11093  13408   7610   -190   -612    736       C  
ATOM    532  O   LEU A  68     -16.039   3.022  44.029  1.00 85.09           O  
ANISOU  532  O   LEU A  68    11294  13388   7647   -180   -540    776       O  
ATOM    533  CB  LEU A  68     -14.550   5.972  43.497  1.00 76.33           C  
ANISOU  533  CB  LEU A  68     9901  12519   6581    -99   -798    739       C  
ATOM    534  CG  LEU A  68     -13.333   5.089  43.250  1.00 80.39           C  
ANISOU  534  CG  LEU A  68    10502  13034   7008      6   -777    810       C  
ATOM    535  CD1 LEU A  68     -13.098   4.860  41.760  1.00 80.49           C  
ANISOU  535  CD1 LEU A  68    10548  12983   7051    -10   -803    809       C  
ATOM    536  CD2 LEU A  68     -12.102   5.707  43.856  1.00 81.76           C  
ANISOU  536  CD2 LEU A  68    10601  13340   7123     96   -816    813       C  
ATOM    537  N   VAL A  69     -16.430   4.543  45.681  1.00 82.22           N  
ANISOU  537  N   VAL A  69    10782  13166   7294   -202   -568    724       N  
ATOM    538  CA  VAL A  69     -16.703   3.609  46.791  1.00 83.38           C  
ANISOU  538  CA  VAL A  69    11075  13254   7353   -205   -427    761       C  
ATOM    539  C   VAL A  69     -18.008   2.844  46.497  1.00 88.35           C  
ANISOU  539  C   VAL A  69    11747  13756   8067   -351   -307    686       C  
ATOM    540  O   VAL A  69     -18.062   1.630  46.694  1.00 88.48           O  
ANISOU  540  O   VAL A  69    11944  13657   8018   -358   -171    730       O  
ATOM    541  CB  VAL A  69     -16.747   4.349  48.169  1.00 87.63           C  
ANISOU  541  CB  VAL A  69    11574  13883   7837   -197   -415    749       C  
ATOM    542  CG1 VAL A  69     -17.440   3.522  49.255  1.00 88.73           C  
ANISOU  542  CG1 VAL A  69    11875  13935   7904   -251   -242    758       C  
ATOM    543  CG2 VAL A  69     -15.344   4.749  48.622  1.00 87.19           C  
ANISOU  543  CG2 VAL A  69    11510  13954   7665    -42   -509    815       C  
ATOM    544  N   GLY A  70     -19.014   3.567  45.998  1.00 85.80           N  
ANISOU  544  N   GLY A  70    11258  13454   7890   -458   -360    562       N  
ATOM    545  CA  GLY A  70     -20.333   3.048  45.648  1.00 87.15           C  
ANISOU  545  CA  GLY A  70    11396  13544   8173   -605   -274    436       C  
ATOM    546  C   GLY A  70     -20.328   2.012  44.545  1.00 94.06           C  
ANISOU  546  C   GLY A  70    12360  14324   9054   -627   -248    438       C  
ATOM    547  O   GLY A  70     -21.204   1.142  44.513  1.00 95.38           O  
ANISOU  547  O   GLY A  70    12579  14395   9266   -751   -106    355       O  
ATOM    548  N   GLN A  71     -19.346   2.108  43.624  1.00 91.01           N  
ANISOU  548  N   GLN A  71    11991  13961   8626   -522   -369    518       N  
ATOM    549  CA  GLN A  71     -19.163   1.175  42.506  1.00 91.06           C  
ANISOU  549  CA  GLN A  71    12091  13884   8625   -529   -353    528       C  
ATOM    550  C   GLN A  71     -18.294  -0.008  42.938  1.00 97.70           C  
ANISOU  550  C   GLN A  71    13150  14633   9340   -452   -222    653       C  
ATOM    551  O   GLN A  71     -18.338  -1.063  42.297  1.00 97.97           O  
ANISOU  551  O   GLN A  71    13300  14555   9369   -488   -136    648       O  
ATOM    552  CB  GLN A  71     -18.555   1.877  41.295  1.00 90.66           C  
ANISOU  552  CB  GLN A  71    11973  13892   8582   -459   -525    545       C  
ATOM    553  CG  GLN A  71     -19.523   2.798  40.573  1.00 91.42           C  
ANISOU  553  CG  GLN A  71    11909  14037   8789   -520   -656    419       C  
ATOM    554  CD  GLN A  71     -18.812   3.704  39.604  1.00 98.88           C  
ANISOU  554  CD  GLN A  71    12824  15034   9710   -434   -813    460       C  
ATOM    555  OE1 GLN A  71     -19.248   3.891  38.468  1.00 95.51           O  
ANISOU  555  OE1 GLN A  71    12375  14600   9315   -448   -915    398       O  
ATOM    556  NE2 GLN A  71     -17.707   4.300  40.032  1.00 82.13           N  
ANISOU  556  NE2 GLN A  71    10710  12966   7529   -348   -833    553       N  
ATOM    557  N   ILE A  72     -17.513   0.170  44.031  1.00 95.46           N  
ANISOU  557  N   ILE A  72    12926  14395   8950   -336   -212    757       N  
ATOM    558  CA  ILE A  72     -16.694  -0.885  44.629  1.00 96.89           C  
ANISOU  558  CA  ILE A  72    13326  14496   8991   -218   -107    880       C  
ATOM    559  C   ILE A  72     -17.668  -1.843  45.331  1.00104.13           C  
ANISOU  559  C   ILE A  72    14408  15265   9893   -334    109    852       C  
ATOM    560  O   ILE A  72     -17.527  -3.056  45.185  1.00104.11           O  
ANISOU  560  O   ILE A  72    14611  15114   9831   -318    242    902       O  
ATOM    561  CB  ILE A  72     -15.575  -0.311  45.553  1.00 99.56           C  
ANISOU  561  CB  ILE A  72    13656  14958   9213    -46   -193    973       C  
ATOM    562  CG1 ILE A  72     -14.382   0.187  44.701  1.00 98.80           C  
ANISOU  562  CG1 ILE A  72    13457  14963   9120     70   -345    999       C  
ATOM    563  CG2 ILE A  72     -15.106  -1.329  46.609  1.00101.30           C  
ANISOU  563  CG2 ILE A  72    14122  15097   9269     79    -76   1085       C  
ATOM    564  CD1 ILE A  72     -13.456   1.241  45.372  1.00105.16           C  
ANISOU  564  CD1 ILE A  72    14140  15942   9875    180   -464   1014       C  
ATOM    565  N   ASP A  73     -18.703  -1.290  46.006  1.00103.63           N  
ANISOU  565  N   ASP A  73    14251  15228   9894   -467    159    754       N  
ATOM    566  CA  ASP A  73     -19.760  -2.056  46.678  1.00106.60           C  
ANISOU  566  CA  ASP A  73    14757  15469  10280   -621    391    686       C  
ATOM    567  C   ASP A  73     -20.526  -2.915  45.662  1.00114.46           C  
ANISOU  567  C   ASP A  73    15764  16344  11381   -773    491    573       C  
ATOM    568  O   ASP A  73     -20.895  -4.048  45.973  1.00116.42           O  
ANISOU  568  O   ASP A  73    16222  16421  11590   -859    719    566       O  
ATOM    569  CB  ASP A  73     -20.733  -1.127  47.440  1.00108.49           C  
ANISOU  569  CB  ASP A  73    14832  15786  10601   -743    407    566       C  
ATOM    570  CG  ASP A  73     -20.158  -0.404  48.651  1.00118.78           C  
ANISOU  570  CG  ASP A  73    16155  17188  11789   -632    361    653       C  
ATOM    571  OD1 ASP A  73     -19.170  -0.909  49.238  1.00120.24           O  
ANISOU  571  OD1 ASP A  73    16545  17344  11795   -474    380    805       O  
ATOM    572  OD2 ASP A  73     -20.722   0.643  49.039  1.00123.40           O  
ANISOU  572  OD2 ASP A  73    16551  17876  12457   -697    307    559       O  
ATOM    573  N   ASP A  74     -20.733  -2.383  44.443  1.00111.69           N  
ANISOU  573  N   ASP A  74    15208  16079  11152   -804    326    483       N  
ATOM    574  CA  ASP A  74     -21.397  -3.088  43.347  1.00113.18           C  
ANISOU  574  CA  ASP A  74    15376  16193  11437   -934    373    357       C  
ATOM    575  C   ASP A  74     -20.507  -4.211  42.804  1.00118.79           C  
ANISOU  575  C   ASP A  74    16305  16780  12051   -850    436    472       C  
ATOM    576  O   ASP A  74     -21.029  -5.227  42.349  1.00119.69           O  
ANISOU  576  O   ASP A  74    16511  16763  12203   -974    584    389       O  
ATOM    577  CB  ASP A  74     -21.768  -2.114  42.213  1.00114.38           C  
ANISOU  577  CB  ASP A  74    15269  16484  11709   -949    144    244       C  
ATOM    578  CG  ASP A  74     -22.722  -0.995  42.599  1.00128.26           C  
ANISOU  578  CG  ASP A  74    16795  18357  13581  -1017     67    109       C  
ATOM    579  OD1 ASP A  74     -23.646  -1.250  43.410  1.00130.47           O  
ANISOU  579  OD1 ASP A  74    17062  18594  13917  -1156    235     -2       O  
ATOM    580  OD2 ASP A  74     -22.576   0.121  42.056  1.00134.50           O  
ANISOU  580  OD2 ASP A  74    17425  19270  14408   -937   -148    103       O  
ATOM    581  N   ALA A  75     -19.168  -4.026  42.863  1.00115.20           N  
ANISOU  581  N   ALA A  75    15921  16368  11482   -642    331    644       N  
ATOM    582  CA  ALA A  75     -18.159  -4.977  42.383  1.00115.49           C  
ANISOU  582  CA  ALA A  75    16145  16306  11428   -519    368    758       C  
ATOM    583  C   ALA A  75     -17.752  -6.008  43.453  1.00120.91           C  
ANISOU  583  C   ALA A  75    17125  16838  11975   -433    562    882       C  
ATOM    584  O   ALA A  75     -17.362  -7.121  43.093  1.00121.34           O  
ANISOU  584  O   ALA A  75    17382  16740  11982   -395    680    931       O  
ATOM    585  CB  ALA A  75     -16.930  -4.226  41.899  1.00114.77           C  
ANISOU  585  CB  ALA A  75    15957  16352  11298   -340    161    848       C  
ATOM    586  N   LEU A  76     -17.831  -5.644  44.750  1.00117.93           N  
ANISOU  586  N   LEU A  76    16793  16493  11522   -391    596    934       N  
ATOM    587  CA  LEU A  76     -17.488  -6.542  45.857  1.00119.72           C  
ANISOU  587  CA  LEU A  76    17333  16574  11583   -289    769   1061       C  
ATOM    588  C   LEU A  76     -18.549  -7.636  46.034  1.00126.76           C  
ANISOU  588  C   LEU A  76    18433  17236  12495   -488   1064    986       C  
ATOM    589  O   LEU A  76     -18.190  -8.776  46.333  1.00127.82           O  
ANISOU  589  O   LEU A  76    18883  17174  12507   -409   1236   1089       O  
ATOM    590  CB  LEU A  76     -17.293  -5.775  47.179  1.00119.55           C  
ANISOU  590  CB  LEU A  76    17302  16662  11460   -201    716   1122       C  
ATOM    591  CG  LEU A  76     -15.849  -5.414  47.559  1.00123.50           C  
ANISOU  591  CG  LEU A  76    17807  17293  11824     82    531   1262       C  
ATOM    592  CD1 LEU A  76     -15.820  -4.382  48.664  1.00123.21           C  
ANISOU  592  CD1 LEU A  76    17676  17411  11728    117    447   1266       C  
ATOM    593  CD2 LEU A  76     -15.050  -6.643  47.994  1.00127.49           C  
ANISOU  593  CD2 LEU A  76    18649  17643  12147    290    630   1414       C  
ATOM    594  N   LYS A  77     -19.845  -7.296  45.832  1.00124.41           N  
ANISOU  594  N   LYS A  77    17959  16958  12353   -744   1130    795       N  
ATOM    595  CA  LYS A  77     -20.957  -8.248  45.935  1.00126.68           C  
ANISOU  595  CA  LYS A  77    18390  17048  12694   -982   1426    667       C  
ATOM    596  C   LYS A  77     -20.907  -9.271  44.781  1.00132.80           C  
ANISOU  596  C   LYS A  77    19252  17689  13517  -1036   1505    624       C  
ATOM    597  O   LYS A  77     -21.316 -10.415  44.976  1.00134.66           O  
ANISOU  597  O   LYS A  77    19746  17695  13723  -1150   1788    597       O  
ATOM    598  CB  LYS A  77     -22.329  -7.541  46.011  1.00128.99           C  
ANISOU  598  CB  LYS A  77    18417  17432  13160  -1230   1454    437       C  
ATOM    599  CG  LYS A  77     -22.731  -6.706  44.799  1.00141.51           C  
ANISOU  599  CG  LYS A  77    19639  19204  14924  -1289   1216    282       C  
ATOM    600  CD  LYS A  77     -24.014  -5.933  45.063  1.00152.34           C  
ANISOU  600  CD  LYS A  77    20750  20680  16454  -1480   1223     64       C  
ATOM    601  CE  LYS A  77     -24.486  -5.167  43.852  1.00161.89           C  
ANISOU  601  CE  LYS A  77    21630  22055  17826  -1520    987    -98       C  
ATOM    602  NZ  LYS A  77     -25.615  -4.256  44.180  1.00170.09           N  
ANISOU  602  NZ  LYS A  77    22393  23220  19013  -1642    948   -296       N  
ATOM    603  N   LEU A  78     -20.373  -8.870  43.606  1.00128.81           N  
ANISOU  603  N   LEU A  78    18558  17312  13073   -956   1273    618       N  
ATOM    604  CA  LEU A  78     -20.213  -9.761  42.453  1.00129.57           C  
ANISOU  604  CA  LEU A  78    18726  17301  13203   -989   1321    581       C  
ATOM    605  C   LEU A  78     -18.987 -10.658  42.657  1.00134.88           C  
ANISOU  605  C   LEU A  78    19707  17827  13714   -761   1387    790       C  
ATOM    606  O   LEU A  78     -19.014 -11.821  42.245  1.00136.23           O  
ANISOU  606  O   LEU A  78    20090  17797  13874   -810   1575    778       O  
ATOM    607  CB  LEU A  78     -20.099  -8.980  41.127  1.00127.93           C  
ANISOU  607  CB  LEU A  78    18230  17279  13097   -984   1056    500       C  
ATOM    608  CG  LEU A  78     -21.305  -8.127  40.691  1.00132.45           C  
ANISOU  608  CG  LEU A  78    18494  18000  13830  -1173    950    281       C  
ATOM    609  CD1 LEU A  78     -20.930  -7.212  39.538  1.00131.06           C  
ANISOU  609  CD1 LEU A  78    18101  18002  13695  -1090    661    267       C  
ATOM    610  CD2 LEU A  78     -22.506  -8.983  40.302  1.00136.47           C  
ANISOU  610  CD2 LEU A  78    19009  18395  14448  -1434   1152     59       C  
ATOM    611  N   ALA A  79     -17.920 -10.117  43.303  1.00130.59           N  
ANISOU  611  N   ALA A  79    19180  17386  13050   -507   1232    964       N  
ATOM    612  CA  ALA A  79     -16.682 -10.840  43.624  1.00131.24           C  
ANISOU  612  CA  ALA A  79    19522  17371  12974   -237   1249   1157       C  
ATOM    613  C   ALA A  79     -16.936 -11.909  44.703  1.00137.81           C  
ANISOU  613  C   ALA A  79    20743  17950  13670   -226   1532   1240       C  
ATOM    614  O   ALA A  79     -16.333 -12.985  44.660  1.00138.55           O  
ANISOU  614  O   ALA A  79    21124  17851  13665    -87   1653   1345       O  
ATOM    615  CB  ALA A  79     -15.606  -9.868  44.087  1.00130.57           C  
ANISOU  615  CB  ALA A  79    19302  17500  12810      8    998   1271       C  
ATOM    616  N   ASN A  80     -17.844 -11.610  45.656  1.00135.49           N  
ANISOU  616  N   ASN A  80    20470  17641  13367   -375   1652   1188       N  
ATOM    617  CA  ASN A  80     -18.238 -12.521  46.732  1.00138.05           C  
ANISOU  617  CA  ASN A  80    21181  17716  13556   -407   1953   1251       C  
ATOM    618  C   ASN A  80     -19.176 -13.616  46.203  1.00144.00           C  
ANISOU  618  C   ASN A  80    22095  18219  14400   -673   2264   1113       C  
ATOM    619  O   ASN A  80     -19.242 -14.696  46.794  1.00146.28           O  
ANISOU  619  O   ASN A  80    22787  18230  14563   -665   2547   1191       O  
ATOM    620  CB  ASN A  80     -18.896 -11.755  47.878  1.00138.54           C  
ANISOU  620  CB  ASN A  80    21191  17860  13589   -502   1984   1217       C  
ATOM    621  CG  ASN A  80     -17.909 -11.219  48.882  1.00162.86           C  
ANISOU  621  CG  ASN A  80    24342  21059  16478   -209   1810   1400       C  
ATOM    622  OD1 ASN A  80     -17.540 -11.896  49.847  1.00162.42           O  
ANISOU  622  OD1 ASN A  80    24660  20841  16210    -53   1945   1550       O  
ATOM    623  ND2 ASN A  80     -17.474  -9.985  48.692  1.00151.37           N  
ANISOU  623  ND2 ASN A  80    22542  19888  15084   -125   1510   1383       N  
ATOM    624  N   GLU A  81     -19.886 -13.341  45.085  1.00139.40           N  
ANISOU  624  N   GLU A  81    21208  17731  14025   -903   2214    904       N  
ATOM    625  CA  GLU A  81     -20.804 -14.283  44.436  1.00140.83           C  
ANISOU  625  CA  GLU A  81    21464  17723  14321  -1181   2478    721       C  
ATOM    626  C   GLU A  81     -20.077 -15.155  43.386  1.00144.68           C  
ANISOU  626  C   GLU A  81    22077  18094  14800  -1083   2483    769       C  
ATOM    627  O   GLU A  81     -20.720 -15.930  42.672  1.00145.29           O  
ANISOU  627  O   GLU A  81    22204  18026  14972  -1303   2681    610       O  
ATOM    628  CB  GLU A  81     -21.985 -13.534  43.797  1.00141.28           C  
ANISOU  628  CB  GLU A  81    21118  17964  14598  -1461   2400    446       C  
ATOM    629  CG  GLU A  81     -23.118 -13.260  44.770  1.00152.60           C  
ANISOU  629  CG  GLU A  81    22519  19384  16080  -1680   2584    310       C  
ATOM    630  CD  GLU A  81     -24.240 -12.411  44.207  1.00172.37           C  
ANISOU  630  CD  GLU A  81    24590  22100  18803  -1907   2465     34       C  
ATOM    631  OE1 GLU A  81     -24.989 -12.911  43.337  1.00167.13           O  
ANISOU  631  OE1 GLU A  81    23819  21403  18281  -2125   2555   -189       O  
ATOM    632  OE2 GLU A  81     -24.379 -11.248  44.648  1.00165.66           O  
ANISOU  632  OE2 GLU A  81    23511  21450  17981  -1862   2282     30       O  
ATOM    633  N   GLY A  82     -18.751 -15.024  43.323  1.00140.37           N  
ANISOU  633  N   GLY A  82    21574  17617  14144   -761   2277    969       N  
ATOM    634  CA  GLY A  82     -17.888 -15.778  42.419  1.00140.55           C  
ANISOU  634  CA  GLY A  82    21712  17542  14147   -622   2265   1033       C  
ATOM    635  C   GLY A  82     -17.906 -15.359  40.961  1.00142.66           C  
ANISOU  635  C   GLY A  82    21662  17974  14566   -715   2078    892       C  
ATOM    636  O   GLY A  82     -17.308 -16.044  40.125  1.00142.59           O  
ANISOU  636  O   GLY A  82    21750  17871  14556   -646   2102    912       O  
ATOM    637  N   LYS A  83     -18.581 -14.237  40.637  1.00137.44           N  
ANISOU  637  N   LYS A  83    20640  17553  14027   -862   1892    749       N  
ATOM    638  CA  LYS A  83     -18.668 -13.734  39.265  1.00135.75           C  
ANISOU  638  CA  LYS A  83    20142  17505  13934   -941   1695    617       C  
ATOM    639  C   LYS A  83     -17.432 -12.877  38.956  1.00137.89           C  
ANISOU  639  C   LYS A  83    20269  17969  14154   -682   1403    757       C  
ATOM    640  O   LYS A  83     -17.501 -11.646  38.978  1.00136.18           O  
ANISOU  640  O   LYS A  83    19793  17974  13975   -667   1183    737       O  
ATOM    641  CB  LYS A  83     -19.987 -12.970  39.032  1.00137.50           C  
ANISOU  641  CB  LYS A  83    20067  17876  14301  -1198   1634    389       C  
ATOM    642  CG  LYS A  83     -21.208 -13.890  38.952  1.00150.89           C  
ANISOU  642  CG  LYS A  83    21845  19402  16085  -1495   1922    179       C  
ATOM    643  CD  LYS A  83     -22.464 -13.180  38.448  1.00158.60           C  
ANISOU  643  CD  LYS A  83    22478  20558  17226  -1730   1820    -90       C  
ATOM    644  CE  LYS A  83     -23.308 -12.575  39.546  1.00168.56           C  
ANISOU  644  CE  LYS A  83    23627  21883  18535  -1829   1868   -160       C  
ATOM    645  NZ  LYS A  83     -23.971 -13.608  40.385  1.00180.37           N  
ANISOU  645  NZ  LYS A  83    25369  23137  20027  -2021   2253   -232       N  
ATOM    646  N   VAL A  84     -16.292 -13.557  38.685  1.00134.44           N  
ANISOU  646  N   VAL A  84    20011  17436  13636   -479   1420    887       N  
ATOM    647  CA  VAL A  84     -14.971 -12.975  38.391  1.00132.61           C  
ANISOU  647  CA  VAL A  84    19676  17356  13356   -227   1195   1005       C  
ATOM    648  C   VAL A  84     -15.041 -12.098  37.125  1.00133.74           C  
ANISOU  648  C   VAL A  84    19533  17687  13597   -322    992    888       C  
ATOM    649  O   VAL A  84     -14.527 -10.976  37.140  1.00131.33           O  
ANISOU  649  O   VAL A  84    19030  17581  13288   -221    778    926       O  
ATOM    650  CB  VAL A  84     -13.863 -14.067  38.272  1.00137.93           C  
ANISOU  650  CB  VAL A  84    20606  17859  13942     -7   1295   1128       C  
ATOM    651  CG1 VAL A  84     -12.478 -13.446  38.090  1.00136.52           C  
ANISOU  651  CG1 VAL A  84    20294  17854  13725    254   1074   1223       C  
ATOM    652  CG2 VAL A  84     -13.867 -14.996  39.483  1.00139.98           C  
ANISOU  652  CG2 VAL A  84    21206  17899  14083     97   1508   1249       C  
ATOM    653  N   LYS A  85     -15.691 -12.606  36.052  1.00130.56           N  
ANISOU  653  N   LYS A  85    19124  17214  13269   -517   1066    740       N  
ATOM    654  CA  LYS A  85     -15.864 -11.916  34.766  1.00128.85           C  
ANISOU  654  CA  LYS A  85    18691  17149  13119   -612    889    620       C  
ATOM    655  C   LYS A  85     -16.710 -10.638  34.932  1.00130.58           C  
ANISOU  655  C   LYS A  85    18652  17563  13398   -710    712    536       C  
ATOM    656  O   LYS A  85     -16.431  -9.638  34.265  1.00128.61           O  
ANISOU  656  O   LYS A  85    18230  17478  13157   -669    502    527       O  
ATOM    657  CB  LYS A  85     -16.500 -12.860  33.725  1.00132.49           C  
ANISOU  657  CB  LYS A  85    19227  17483  13630   -807   1024    461       C  
ATOM    658  CG  LYS A  85     -16.390 -12.383  32.275  1.00143.33           C  
ANISOU  658  CG  LYS A  85    20457  18978  15024   -853    853    366       C  
ATOM    659  CD  LYS A  85     -15.181 -12.967  31.550  1.00151.78           C  
ANISOU  659  CD  LYS A  85    21661  19969  16038   -716    890    447       C  
ATOM    660  CE  LYS A  85     -15.163 -12.568  30.094  1.00158.15           C  
ANISOU  660  CE  LYS A  85    22365  20876  16847   -787    751    343       C  
ATOM    661  NZ  LYS A  85     -13.997 -13.144  29.376  1.00163.88           N  
ANISOU  661  NZ  LYS A  85    23218  21521  17526   -671    811    404       N  
ATOM    662  N   GLU A  86     -17.722 -10.670  35.827  1.00127.15           N  
ANISOU  662  N   GLU A  86    18209  17098  13005   -836    813    472       N  
ATOM    663  CA  GLU A  86     -18.582  -9.518  36.108  1.00125.85           C  
ANISOU  663  CA  GLU A  86    17804  17103  12909   -922    670    380       C  
ATOM    664  C   GLU A  86     -17.891  -8.519  37.055  1.00127.07           C  
ANISOU  664  C   GLU A  86    17893  17379  13008   -744    541    531       C  
ATOM    665  O   GLU A  86     -18.132  -7.315  36.934  1.00125.36           O  
ANISOU  665  O   GLU A  86    17463  17334  12834   -746    351    492       O  
ATOM    666  CB  GLU A  86     -19.935  -9.955  36.683  1.00128.82           C  
ANISOU  666  CB  GLU A  86    18180  17401  13364  -1139    851    225       C  
ATOM    667  CG  GLU A  86     -20.944 -10.334  35.613  1.00140.87           C  
ANISOU  667  CG  GLU A  86    19611  18923  14990  -1356    875    -12       C  
ATOM    668  CD  GLU A  86     -22.379  -9.946  35.917  1.00164.24           C  
ANISOU  668  CD  GLU A  86    22369  21963  18073  -1555    887   -231       C  
ATOM    669  OE1 GLU A  86     -22.662  -8.730  36.010  1.00157.17           O  
ANISOU  669  OE1 GLU A  86    21247  21253  17217  -1510    671   -256       O  
ATOM    670  OE2 GLU A  86     -23.229 -10.859  36.022  1.00161.15           O  
ANISOU  670  OE2 GLU A  86    22039  21444  17745  -1761   1119   -394       O  
ATOM    671  N   ALA A  87     -17.032  -9.014  37.981  1.00122.82           N  
ANISOU  671  N   ALA A  87    17545  16753  12370   -581    640    696       N  
ATOM    672  CA  ALA A  87     -16.285  -8.185  38.937  1.00121.20           C  
ANISOU  672  CA  ALA A  87    17289  16665  12095   -402    525    828       C  
ATOM    673  C   ALA A  87     -15.189  -7.369  38.237  1.00122.48           C  
ANISOU  673  C   ALA A  87    17314  16979  12243   -258    316    880       C  
ATOM    674  O   ALA A  87     -14.969  -6.212  38.600  1.00120.82           O  
ANISOU  674  O   ALA A  87    16941  16929  12036   -205    165    900       O  
ATOM    675  CB  ALA A  87     -15.674  -9.051  40.028  1.00123.19           C  
ANISOU  675  CB  ALA A  87    17801  16781  12226   -249    676    974       C  
ATOM    676  N   GLN A  88     -14.512  -7.964  37.240  1.00118.45           N  
ANISOU  676  N   GLN A  88    16875  16409  11720   -209    330    891       N  
ATOM    677  CA  GLN A  88     -13.457  -7.298  36.473  1.00117.02           C  
ANISOU  677  CA  GLN A  88    16586  16348  11529    -98    176    920       C  
ATOM    678  C   GLN A  88     -14.065  -6.285  35.482  1.00119.45           C  
ANISOU  678  C   GLN A  88    16713  16769  11904   -234     29    809       C  
ATOM    679  O   GLN A  88     -13.463  -5.236  35.244  1.00117.47           O  
ANISOU  679  O   GLN A  88    16338  16649  11646   -169   -113    829       O  
ATOM    680  CB  GLN A  88     -12.569  -8.325  35.752  1.00119.10           C  
ANISOU  680  CB  GLN A  88    16998  16497  11758     -8    264    954       C  
ATOM    681  CG  GLN A  88     -11.619  -9.064  36.701  1.00133.64           C  
ANISOU  681  CG  GLN A  88    18996  18265  13515    214    346   1084       C  
ATOM    682  CD  GLN A  88     -11.229 -10.456  36.249  1.00154.19           C  
ANISOU  682  CD  GLN A  88    21817  20675  16093    272    507   1107       C  
ATOM    683  OE1 GLN A  88     -11.961 -11.148  35.528  1.00150.62           O  
ANISOU  683  OE1 GLN A  88    21452  20094  15684    106    623   1024       O  
ATOM    684  NE2 GLN A  88     -10.085 -10.926  36.723  1.00146.55           N  
ANISOU  684  NE2 GLN A  88    20947  19680  15055    519    521   1210       N  
ATOM    685  N   ALA A  89     -15.266  -6.585  34.936  1.00116.82           N  
ANISOU  685  N   ALA A  89    16371  16386  11631   -416     65    682       N  
ATOM    686  CA  ALA A  89     -15.990  -5.705  34.010  1.00116.28           C  
ANISOU  686  CA  ALA A  89    16150  16420  11612   -524    -90    565       C  
ATOM    687  C   ALA A  89     -16.513  -4.457  34.732  1.00119.62           C  
ANISOU  687  C   ALA A  89    16401  16975  12072   -524   -216    554       C  
ATOM    688  O   ALA A  89     -16.544  -3.378  34.138  1.00118.45           O  
ANISOU  688  O   ALA A  89    16140  16934  11930   -512   -381    530       O  
ATOM    689  CB  ALA A  89     -17.140  -6.454  33.356  1.00118.25           C  
ANISOU  689  CB  ALA A  89    16419  16595  11916   -703    -21    407       C  
ATOM    690  N   ALA A  90     -16.914  -4.609  36.015  1.00116.54           N  
ANISOU  690  N   ALA A  90    16017  16563  11698   -537   -124    573       N  
ATOM    691  CA  ALA A  90     -17.387  -3.515  36.868  1.00115.60           C  
ANISOU  691  CA  ALA A  90    15750  16557  11616   -538   -210    562       C  
ATOM    692  C   ALA A  90     -16.208  -2.663  37.352  1.00117.71           C  
ANISOU  692  C   ALA A  90    15983  16920  11822   -376   -299    690       C  
ATOM    693  O   ALA A  90     -16.387  -1.472  37.619  1.00116.45           O  
ANISOU  693  O   ALA A  90    15683  16873  11690   -367   -417    675       O  
ATOM    694  CB  ALA A  90     -18.155  -4.071  38.058  1.00117.39           C  
ANISOU  694  CB  ALA A  90    16026  16713  11866   -617    -48    535       C  
ATOM    695  N   ALA A  91     -15.003  -3.281  37.453  1.00113.63           N  
ANISOU  695  N   ALA A  91    15587  16359  11226   -246   -240    798       N  
ATOM    696  CA  ALA A  91     -13.751  -2.640  37.874  1.00112.19           C  
ANISOU  696  CA  ALA A  91    15361  16277  10988    -88   -313    889       C  
ATOM    697  C   ALA A  91     -13.195  -1.695  36.789  1.00113.47           C  
ANISOU  697  C   ALA A  91    15423  16526  11166    -83   -442    862       C  
ATOM    698  O   ALA A  91     -12.366  -0.834  37.097  1.00112.50           O  
ANISOU  698  O   ALA A  91    15212  16509  11025     -2   -512    893       O  
ATOM    699  CB  ALA A  91     -12.715  -3.696  38.230  1.00113.77           C  
ANISOU  699  CB  ALA A  91    15712  16405  11110     61   -216    983       C  
ATOM    700  N   GLU A  92     -13.646  -1.857  35.528  1.00108.50           N  
ANISOU  700  N   GLU A  92    14818  15845  10560   -176   -462    795       N  
ATOM    701  CA  GLU A  92     -13.238  -1.000  34.413  1.00107.02           C  
ANISOU  701  CA  GLU A  92    14588  15710  10364   -183   -566    770       C  
ATOM    702  C   GLU A  92     -14.025   0.319  34.462  1.00107.33           C  
ANISOU  702  C   GLU A  92    14506  15832  10443   -234   -695    722       C  
ATOM    703  O   GLU A  92     -13.568   1.327  33.920  1.00106.75           O  
ANISOU  703  O   GLU A  92    14402  15808  10350   -214   -776    726       O  
ATOM    704  CB  GLU A  92     -13.428  -1.719  33.067  1.00109.24           C  
ANISOU  704  CB  GLU A  92    14970  15905  10630   -250   -542    718       C  
ATOM    705  CG  GLU A  92     -12.409  -1.332  32.000  1.00121.91           C  
ANISOU  705  CG  GLU A  92    16613  17523  12185   -215   -569    730       C  
ATOM    706  CD  GLU A  92     -10.941  -1.644  32.255  1.00146.61           C  
ANISOU  706  CD  GLU A  92    19760  20659  15287   -100   -486    793       C  
ATOM    707  OE1 GLU A  92     -10.087  -0.876  31.754  1.00146.10           O  
ANISOU  707  OE1 GLU A  92    19666  20646  15200    -78   -510    790       O  
ATOM    708  OE2 GLU A  92     -10.639  -2.653  32.935  1.00138.81           O  
ANISOU  708  OE2 GLU A  92    18821  19621  14298    -28   -391    834       O  
ATOM    709  N   GLN A  93     -15.195   0.311  35.137  1.00101.39           N  
ANISOU  709  N   GLN A  93    13693  15083   9747   -298   -699    671       N  
ATOM    710  CA  GLN A  93     -16.032   1.492  35.359  1.00 99.61           C  
ANISOU  710  CA  GLN A  93    13340  14931   9574   -329   -814    615       C  
ATOM    711  C   GLN A  93     -15.415   2.335  36.496  1.00 99.19           C  
ANISOU  711  C   GLN A  93    13215  14959   9515   -259   -819    678       C  
ATOM    712  O   GLN A  93     -15.735   3.520  36.621  1.00 98.22           O  
ANISOU  712  O   GLN A  93    12999  14897   9422   -259   -913    652       O  
ATOM    713  CB  GLN A  93     -17.483   1.085  35.673  1.00101.94           C  
ANISOU  713  CB  GLN A  93    13578  15208   9948   -431   -795    507       C  
ATOM    714  CG  GLN A  93     -18.521   2.179  35.395  1.00121.16           C  
ANISOU  714  CG  GLN A  93    15879  17709  12445   -458   -945    406       C  
ATOM    715  CD  GLN A  93     -19.900   1.881  35.956  1.00148.10           C  
ANISOU  715  CD  GLN A  93    19186  21128  15958   -559   -914    271       C  
ATOM    716  OE1 GLN A  93     -20.089   1.040  36.849  1.00145.38           O  
ANISOU  716  OE1 GLN A  93    18870  20735  15635   -621   -756    266       O  
ATOM    717  NE2 GLN A  93     -20.902   2.601  35.467  1.00142.10           N  
ANISOU  717  NE2 GLN A  93    18306  20426  15261   -571  -1060    150       N  
ATOM    718  N   LEU A  94     -14.512   1.717  37.308  1.00 92.97           N  
ANISOU  718  N   LEU A  94    12475  14171   8681   -186   -724    756       N  
ATOM    719  CA  LEU A  94     -13.764   2.380  38.380  1.00 90.87           C  
ANISOU  719  CA  LEU A  94    12141  13997   8388   -107   -732    804       C  
ATOM    720  C   LEU A  94     -12.657   3.226  37.767  1.00 90.48           C  
ANISOU  720  C   LEU A  94    12054  14008   8316    -59   -788    814       C  
ATOM    721  O   LEU A  94     -12.396   4.328  38.247  1.00 88.84           O  
ANISOU  721  O   LEU A  94    11752  13885   8119    -47   -834    803       O  
ATOM    722  CB  LEU A  94     -13.169   1.368  39.382  1.00 91.72           C  
ANISOU  722  CB  LEU A  94    12329  14087   8431    -17   -633    874       C  
ATOM    723  CG  LEU A  94     -14.134   0.546  40.244  1.00 97.12           C  
ANISOU  723  CG  LEU A  94    13086  14698   9118    -67   -533    873       C  
ATOM    724  CD1 LEU A  94     -13.381  -0.516  41.020  1.00 98.03           C  
ANISOU  724  CD1 LEU A  94    13348  14762   9137     53   -433    963       C  
ATOM    725  CD2 LEU A  94     -14.906   1.423  41.212  1.00 99.64           C  
ANISOU  725  CD2 LEU A  94    13299  15088   9472   -116   -561    834       C  
ATOM    726  N   LYS A  95     -12.021   2.710  36.685  1.00 85.72           N  
ANISOU  726  N   LYS A  95    11531  13353   7685    -48   -764    822       N  
ATOM    727  CA  LYS A  95     -10.982   3.388  35.895  1.00 84.42           C  
ANISOU  727  CA  LYS A  95    11357  13220   7499    -31   -779    813       C  
ATOM    728  C   LYS A  95     -11.539   4.674  35.289  1.00 84.29           C  
ANISOU  728  C   LYS A  95    11320  13205   7503   -100   -863    774       C  
ATOM    729  O   LYS A  95     -10.823   5.662  35.178  1.00 83.75           O  
ANISOU  729  O   LYS A  95    11215  13179   7426    -99   -866    762       O  
ATOM    730  CB  LYS A  95     -10.451   2.470  34.781  1.00 87.82           C  
ANISOU  730  CB  LYS A  95    11899  13573   7897    -26   -720    817       C  
ATOM    731  CG  LYS A  95      -9.004   2.042  34.989  1.00110.73           C  
ANISOU  731  CG  LYS A  95    14781  16517  10774     76   -650    832       C  
ATOM    732  CD  LYS A  95      -8.489   1.200  33.830  1.00125.16           C  
ANISOU  732  CD  LYS A  95    16716  18261  12579     75   -580    823       C  
ATOM    733  CE  LYS A  95      -7.097   0.668  34.077  1.00138.78           C  
ANISOU  733  CE  LYS A  95    18404  20031  14294    199   -512    822       C  
ATOM    734  NZ  LYS A  95      -6.630  -0.191  32.956  1.00148.07           N  
ANISOU  734  NZ  LYS A  95    19684  21118  15457    196   -430    803       N  
ATOM    735  N   THR A  96     -12.827   4.656  34.917  1.00 77.91           N  
ANISOU  735  N   THR A  96    10536  12347   6719   -156   -927    744       N  
ATOM    736  CA  THR A  96     -13.554   5.797  34.377  1.00 76.35           C  
ANISOU  736  CA  THR A  96    10333  12142   6535   -186  -1032    707       C  
ATOM    737  C   THR A  96     -13.772   6.834  35.488  1.00 78.10           C  
ANISOU  737  C   THR A  96    10435  12434   6805   -175  -1060    699       C  
ATOM    738  O   THR A  96     -13.518   8.013  35.272  1.00 77.29           O  
ANISOU  738  O   THR A  96    10334  12337   6695   -172  -1090    694       O  
ATOM    739  CB  THR A  96     -14.872   5.304  33.762  1.00 77.30           C  
ANISOU  739  CB  THR A  96    10479  12216   6676   -227  -1104    650       C  
ATOM    740  OG1 THR A  96     -14.561   4.568  32.582  1.00 70.49           O  
ANISOU  740  OG1 THR A  96     9742  11289   5752   -243  -1085    650       O  
ATOM    741  CG2 THR A  96     -15.857   6.438  33.461  1.00 74.89           C  
ANISOU  741  CG2 THR A  96    10137  11920   6396   -222  -1241    598       C  
ATOM    742  N   THR A  97     -14.226   6.390  36.668  1.00 74.05           N  
ANISOU  742  N   THR A  97     9840  11962   6336   -176  -1031    693       N  
ATOM    743  CA  THR A  97     -14.514   7.262  37.809  1.00 73.60           C  
ANISOU  743  CA  THR A  97     9671  11972   6321   -174  -1046    676       C  
ATOM    744  C   THR A  97     -13.241   7.962  38.290  1.00 76.95           C  
ANISOU  744  C   THR A  97    10058  12467   6714   -138  -1009    699       C  
ATOM    745  O   THR A  97     -13.278   9.165  38.567  1.00 76.35           O  
ANISOU  745  O   THR A  97     9925  12422   6664   -150  -1038    670       O  
ATOM    746  CB  THR A  97     -15.194   6.462  38.911  1.00 81.93           C  
ANISOU  746  CB  THR A  97    10685  13040   7404   -191   -991    667       C  
ATOM    747  OG1 THR A  97     -16.289   5.760  38.326  1.00 83.32           O  
ANISOU  747  OG1 THR A  97    10887  13152   7620   -247  -1004    615       O  
ATOM    748  CG2 THR A  97     -15.703   7.340  40.045  1.00 80.72           C  
ANISOU  748  CG2 THR A  97    10422  12950   7297   -204  -1001    632       C  
ATOM    749  N   ARG A  98     -12.123   7.211  38.352  1.00 73.12           N  
ANISOU  749  N   ARG A  98     9599  12006   6177    -92   -944    733       N  
ATOM    750  CA  ARG A  98     -10.807   7.697  38.757  1.00 72.60           C  
ANISOU  750  CA  ARG A  98     9469  12029   6085    -54   -908    722       C  
ATOM    751  C   ARG A  98     -10.344   8.780  37.785  1.00 75.49           C  
ANISOU  751  C   ARG A  98     9861  12366   6455   -104   -905    687       C  
ATOM    752  O   ARG A  98     -10.164   9.928  38.185  1.00 75.32           O  
ANISOU  752  O   ARG A  98     9773  12390   6455   -132   -902    645       O  
ATOM    753  CB  ARG A  98      -9.805   6.525  38.773  1.00 73.65           C  
ANISOU  753  CB  ARG A  98     9631  12183   6170     26   -852    751       C  
ATOM    754  CG  ARG A  98      -9.243   6.112  40.137  1.00 86.21           C  
ANISOU  754  CG  ARG A  98    11153  13879   7722    124   -841    764       C  
ATOM    755  CD  ARG A  98      -7.721   5.908  40.134  1.00102.88           C  
ANISOU  755  CD  ARG A  98    13206  16083   9802    214   -817    732       C  
ATOM    756  NE  ARG A  98      -7.237   5.015  39.071  1.00121.76           N  
ANISOU  756  NE  ARG A  98    15681  18397  12184    240   -770    748       N  
ATOM    757  CZ  ARG A  98      -6.669   5.420  37.932  1.00140.35           C  
ANISOU  757  CZ  ARG A  98    18040  20724  14560    181   -732    699       C  
ATOM    758  NH1 ARG A  98      -6.495   6.714  37.689  1.00128.49           N  
ANISOU  758  NH1 ARG A  98    16477  19254  13087     91   -728    635       N  
ATOM    759  NH2 ARG A  98      -6.275   4.531  37.029  1.00128.53           N  
ANISOU  759  NH2 ARG A  98    16627  19155  13051    204   -681    711       N  
ATOM    760  N   ASN A  99     -10.232   8.415  36.494  1.00 72.07           N  
ANISOU  760  N   ASN A  99     9546  11844   5994   -124   -893    700       N  
ATOM    761  CA  ASN A  99      -9.750   9.246  35.396  1.00 72.04           C  
ANISOU  761  CA  ASN A  99     9628  11779   5965   -174   -862    677       C  
ATOM    762  C   ASN A  99     -10.653  10.427  35.046  1.00 77.17           C  
ANISOU  762  C   ASN A  99    10340  12360   6623   -207   -929    673       C  
ATOM    763  O   ASN A  99     -10.146  11.540  34.891  1.00 76.76           O  
ANISOU  763  O   ASN A  99    10315  12287   6563   -246   -881    644       O  
ATOM    764  CB  ASN A  99      -9.541   8.394  34.142  1.00 69.75           C  
ANISOU  764  CB  ASN A  99     9471  11406   5623   -181   -831    696       C  
ATOM    765  CG  ASN A  99      -8.470   7.331  34.249  1.00 84.32           C  
ANISOU  765  CG  ASN A  99    11278  13299   7461   -135   -750    692       C  
ATOM    766  OD1 ASN A  99      -7.634   7.322  35.160  1.00 84.19           O  
ANISOU  766  OD1 ASN A  99    11134  13390   7466    -91   -713    662       O  
ATOM    767  ND2 ASN A  99      -8.501   6.376  33.335  1.00 72.81           N  
ANISOU  767  ND2 ASN A  99     9928  11766   5970   -133   -730    713       N  
ATOM    768  N   ALA A 100     -11.967  10.194  34.890  1.00 75.38           N  
ANISOU  768  N   ALA A 100    10139  12091   6411   -190  -1032    688       N  
ATOM    769  CA  ALA A 100     -12.880  11.243  34.447  1.00 76.49           C  
ANISOU  769  CA  ALA A 100    10345  12164   6554   -184  -1121    678       C  
ATOM    770  C   ALA A 100     -13.370  12.169  35.540  1.00 81.04           C  
ANISOU  770  C   ALA A 100    10804  12787   7203   -177  -1149    649       C  
ATOM    771  O   ALA A 100     -13.645  13.329  35.232  1.00 81.92           O  
ANISOU  771  O   ALA A 100    10982  12834   7311   -166  -1182    640       O  
ATOM    772  CB  ALA A 100     -14.077  10.645  33.718  1.00 77.69           C  
ANISOU  772  CB  ALA A 100    10555  12268   6696   -158  -1236    673       C  
ATOM    773  N   TYR A 101     -13.518  11.695  36.781  1.00 77.16           N  
ANISOU  773  N   TYR A 101    10162  12390   6764   -177  -1132    635       N  
ATOM    774  CA  TYR A 101     -14.074  12.569  37.810  1.00 77.16           C  
ANISOU  774  CA  TYR A 101    10055  12432   6831   -178  -1153    597       C  
ATOM    775  C   TYR A 101     -13.061  13.019  38.862  1.00 79.77           C  
ANISOU  775  C   TYR A 101    10289  12856   7164   -202  -1066    576       C  
ATOM    776  O   TYR A 101     -13.222  14.121  39.386  1.00 80.25           O  
ANISOU  776  O   TYR A 101    10302  12926   7264   -218  -1063    536       O  
ATOM    777  CB  TYR A 101     -15.298  11.916  38.502  1.00 79.30           C  
ANISOU  777  CB  TYR A 101    10232  12735   7163   -173  -1202    570       C  
ATOM    778  CG  TYR A 101     -16.298  11.284  37.550  1.00 83.49           C  
ANISOU  778  CG  TYR A 101    10815  13205   7701   -161  -1286    555       C  
ATOM    779  CD1 TYR A 101     -16.709  11.945  36.393  1.00 86.72           C  
ANISOU  779  CD1 TYR A 101    11322  13539   8090   -121  -1386    545       C  
ATOM    780  CD2 TYR A 101     -16.854  10.036  37.819  1.00 84.82           C  
ANISOU  780  CD2 TYR A 101    10946  13390   7890   -187  -1264    538       C  
ATOM    781  CE1 TYR A 101     -17.584  11.346  35.488  1.00 88.81           C  
ANISOU  781  CE1 TYR A 101    11624  13771   8349   -102  -1483    510       C  
ATOM    782  CE2 TYR A 101     -17.755   9.438  36.934  1.00 86.61           C  
ANISOU  782  CE2 TYR A 101    11203  13575   8130   -193  -1335    493       C  
ATOM    783  CZ  TYR A 101     -18.118  10.099  35.769  1.00 96.29           C  
ANISOU  783  CZ  TYR A 101    12501  14752   9332   -147  -1457    473       C  
ATOM    784  OH  TYR A 101     -19.005   9.525  34.888  1.00 99.77           O  
ANISOU  784  OH  TYR A 101    12958  15174   9777   -144  -1548    408       O  
ATOM    785  N   ILE A 102     -12.030  12.211  39.179  1.00 74.53           N  
ANISOU  785  N   ILE A 102     9593  12266   6460   -194  -1002    589       N  
ATOM    786  CA  ILE A 102     -11.103  12.582  40.252  1.00 73.73           C  
ANISOU  786  CA  ILE A 102     9376  12285   6354   -199   -946    545       C  
ATOM    787  C   ILE A 102      -9.730  13.125  39.749  1.00 77.83           C  
ANISOU  787  C   ILE A 102     9898  12822   6850   -234   -865    497       C  
ATOM    788  O   ILE A 102      -9.256  14.126  40.298  1.00 78.30           O  
ANISOU  788  O   ILE A 102     9883  12935   6931   -280   -820    424       O  
ATOM    789  CB  ILE A 102     -10.913  11.409  41.251  1.00 76.47           C  
ANISOU  789  CB  ILE A 102     9659  12729   6667   -139   -943    570       C  
ATOM    790  CG1 ILE A 102     -12.287  10.837  41.726  1.00 76.21           C  
ANISOU  790  CG1 ILE A 102     9640  12656   6659   -135   -980    601       C  
ATOM    791  CG2 ILE A 102     -10.081  11.872  42.453  1.00 76.90           C  
ANISOU  791  CG2 ILE A 102     9588  12928   6704   -125   -918    511       C  
ATOM    792  CD1 ILE A 102     -12.277   9.371  42.210  1.00 80.07           C  
ANISOU  792  CD1 ILE A 102    10167  13159   7096    -82   -951    654       C  
ATOM    793  N   GLN A 103      -9.109  12.482  38.734  1.00 72.76           N  
ANISOU  793  N   GLN A 103     9336  12137   6171   -228   -830    518       N  
ATOM    794  CA  GLN A 103      -7.787  12.810  38.167  1.00 72.36           C  
ANISOU  794  CA  GLN A 103     9287  12102   6106   -274   -728    454       C  
ATOM    795  C   GLN A 103      -7.587  14.310  37.817  1.00 75.45           C  
ANISOU  795  C   GLN A 103     9729  12424   6515   -371   -653    392       C  
ATOM    796  O   GLN A 103      -6.444  14.761  37.758  1.00 76.08           O  
ANISOU  796  O   GLN A 103     9753  12551   6602   -436   -541    296       O  
ATOM    797  CB  GLN A 103      -7.533  11.948  36.912  1.00 73.78           C  
ANISOU  797  CB  GLN A 103     9593  12195   6244   -265   -702    496       C  
ATOM    798  CG  GLN A 103      -6.098  11.925  36.383  1.00 85.93           C  
ANISOU  798  CG  GLN A 103    11109  13768   7774   -302   -581    417       C  
ATOM    799  CD  GLN A 103      -5.193  11.061  37.214  1.00105.63           C  
ANISOU  799  CD  GLN A 103    13433  16423  10279   -218   -581    371       C  
ATOM    800  OE1 GLN A 103      -4.428  11.551  38.050  1.00 99.09           O  
ANISOU  800  OE1 GLN A 103    12442  15731   9476   -220   -559    273       O  
ATOM    801  NE2 GLN A 103      -5.250   9.754  36.986  1.00103.17           N  
ANISOU  801  NE2 GLN A 103    13161  16097   9941   -133   -608    433       N  
ATOM    802  N   LYS A 104      -8.671  15.071  37.595  1.00 71.49           N  
ANISOU  802  N   LYS A 104     9332  11809   6022   -380   -705    434       N  
ATOM    803  CA  LYS A 104      -8.592  16.499  37.254  1.00 72.04           C  
ANISOU  803  CA  LYS A 104     9499  11776   6099   -454   -629    393       C  
ATOM    804  C   LYS A 104      -8.116  17.359  38.441  1.00 76.69           C  
ANISOU  804  C   LYS A 104     9928  12468   6741   -510   -566    289       C  
ATOM    805  O   LYS A 104      -7.576  18.446  38.232  1.00 77.81           O  
ANISOU  805  O   LYS A 104    10124  12549   6892   -604   -442    216       O  
ATOM    806  CB  LYS A 104      -9.937  17.030  36.709  1.00 74.32           C  
ANISOU  806  CB  LYS A 104     9942  11918   6379   -404   -729    465       C  
ATOM    807  CG  LYS A 104     -11.159  16.843  37.601  1.00 80.85           C  
ANISOU  807  CG  LYS A 104    10654  12801   7263   -336   -858    484       C  
ATOM    808  CD  LYS A 104     -12.292  17.753  37.152  1.00 88.72           C  
ANISOU  808  CD  LYS A 104    11772  13665   8272   -288   -936    507       C  
ATOM    809  CE  LYS A 104     -13.652  17.113  37.280  1.00 99.60           C  
ANISOU  809  CE  LYS A 104    13096  15061   9686   -205  -1089    533       C  
ATOM    810  NZ  LYS A 104     -13.994  16.306  36.079  1.00109.11           N  
ANISOU  810  NZ  LYS A 104    14425  16205  10826   -161  -1164    584       N  
ATOM    811  N   TYR A 105      -8.309  16.870  39.669  1.00 72.65           N  
ANISOU  811  N   TYR A 105     9240  12107   6256   -461   -637    277       N  
ATOM    812  CA  TYR A 105      -7.928  17.576  40.893  1.00 72.83           C  
ANISOU  812  CA  TYR A 105     9105  12252   6316   -504   -598    173       C  
ATOM    813  C   TYR A 105      -6.523  17.184  41.352  1.00 80.02           C  
ANISOU  813  C   TYR A 105     9854  13338   7214   -520   -540     65       C  
ATOM    814  O   TYR A 105      -5.953  17.856  42.211  1.00 81.37           O  
ANISOU  814  O   TYR A 105     9888  13620   7408   -577   -489    -60       O  
ATOM    815  CB  TYR A 105      -8.958  17.310  42.003  1.00 71.96           C  
ANISOU  815  CB  TYR A 105     8911  12208   6224   -440   -704    209       C  
ATOM    816  CG  TYR A 105     -10.378  17.645  41.597  1.00 71.58           C  
ANISOU  816  CG  TYR A 105     8976  12014   6207   -411   -774    283       C  
ATOM    817  CD1 TYR A 105     -10.765  18.961  41.360  1.00 73.74           C  
ANISOU  817  CD1 TYR A 105     9329  12170   6519   -451   -739    254       C  
ATOM    818  CD2 TYR A 105     -11.334  16.647  41.448  1.00 71.13           C  
ANISOU  818  CD2 TYR A 105     8945  11935   6144   -338   -873    366       C  
ATOM    819  CE1 TYR A 105     -12.069  19.275  40.983  1.00 73.81           C  
ANISOU  819  CE1 TYR A 105     9428  12058   6559   -392   -826    307       C  
ATOM    820  CE2 TYR A 105     -12.643  16.950  41.076  1.00 71.59           C  
ANISOU  820  CE2 TYR A 105     9071  11886   6244   -305   -950    399       C  
ATOM    821  CZ  TYR A 105     -13.006  18.266  40.846  1.00 77.52           C  
ANISOU  821  CZ  TYR A 105     9888  12536   7032   -318   -939    369       C  
ATOM    822  OH  TYR A 105     -14.291  18.575  40.477  1.00 77.65           O  
ANISOU  822  OH  TYR A 105     9956  12457   7088   -254  -1037    388       O  
ATOM    823  N   LEU A 106      -5.955  16.127  40.753  1.00 77.22           N  
ANISOU  823  N   LEU A 106     9506  13009   6825   -467   -547     96       N  
ATOM    824  CA  LEU A 106      -4.624  15.627  41.076  1.00 78.13           C  
ANISOU  824  CA  LEU A 106     9461  13294   6933   -447   -511    -11       C  
ATOM    825  C   LEU A 106      -3.606  15.963  39.997  1.00 83.80           C  
ANISOU  825  C   LEU A 106    10216  13957   7668   -547   -364   -103       C  
ATOM    826  O   LEU A 106      -3.976  16.454  38.931  1.00 84.41           O  
ANISOU  826  O   LEU A 106    10488  13846   7739   -622   -294    -53       O  
ATOM    827  CB  LEU A 106      -4.681  14.108  41.276  1.00 77.89           C  
ANISOU  827  CB  LEU A 106     9412  13328   6855   -298   -613     80       C  
ATOM    828  CG  LEU A 106      -5.175  13.653  42.632  1.00 82.47           C  
ANISOU  828  CG  LEU A 106     9910  14024   7399   -197   -721    117       C  
ATOM    829  CD1 LEU A 106      -6.610  13.229  42.560  1.00 81.57           C  
ANISOU  829  CD1 LEU A 106     9931  13782   7280   -174   -784    258       C  
ATOM    830  CD2 LEU A 106      -4.311  12.532  43.168  1.00 86.39           C  
ANISOU  830  CD2 LEU A 106    10318  14666   7841    -54   -773    106       C  
ATOM    831  N   SER A 190      -2.313  15.701  40.279  1.00 93.54           N  
ANISOU  831  N   SER A 190    10659  15317   9566    775  -1599   -968       N  
ATOM    832  CA  SER A 190      -1.226  15.892  39.316  1.00 92.05           C  
ANISOU  832  CA  SER A 190    10469  14879   9627    739  -1640   -938       C  
ATOM    833  C   SER A 190      -1.376  14.833  38.237  1.00 92.61           C  
ANISOU  833  C   SER A 190    10617  14765   9804    704  -1521   -698       C  
ATOM    834  O   SER A 190      -1.413  13.636  38.549  1.00 93.16           O  
ANISOU  834  O   SER A 190    10714  14918   9765    717  -1477   -492       O  
ATOM    835  CB  SER A 190       0.138  15.793  39.999  1.00 97.11           C  
ANISOU  835  CB  SER A 190    11042  15625  10231    767  -1761   -925       C  
ATOM    836  OG  SER A 190       0.674  17.070  40.302  1.00107.13           O  
ANISOU  836  OG  SER A 190    12234  16901  11568    775  -1897  -1178       O  
ATOM    837  N   GLY A 191      -1.545  15.275  37.000  1.00 85.33           N  
ANISOU  837  N   GLY A 191     9725  13604   9093    661  -1475   -726       N  
ATOM    838  CA  GLY A 191      -1.729  14.352  35.893  1.00 82.73           C  
ANISOU  838  CA  GLY A 191     9463  13101   8868    637  -1369   -538       C  
ATOM    839  C   GLY A 191      -1.455  14.915  34.520  1.00 83.75           C  
ANISOU  839  C   GLY A 191     9593  12993   9233    598  -1348   -567       C  
ATOM    840  O   GLY A 191      -1.086  16.083  34.362  1.00 83.28           O  
ANISOU  840  O   GLY A 191     9477  12876   9289    578  -1422   -717       O  
ATOM    841  N   GLN A 192      -1.658  14.057  33.518  1.00 78.18           N  
ANISOU  841  N   GLN A 192     8946  12156   8604    589  -1253   -417       N  
ATOM    842  CA  GLN A 192      -1.470  14.320  32.095  1.00 76.00           C  
ANISOU  842  CA  GLN A 192     8672  11683   8521    561  -1209   -400       C  
ATOM    843  C   GLN A 192      -2.374  15.433  31.568  1.00 75.71           C  
ANISOU  843  C   GLN A 192     8639  11560   8569    518  -1187   -536       C  
ATOM    844  O   GLN A 192      -1.936  16.225  30.734  1.00 75.29           O  
ANISOU  844  O   GLN A 192     8540  11384   8681    487  -1207   -570       O  
ATOM    845  CB  GLN A 192      -1.795  13.035  31.308  1.00 76.56           C  
ANISOU  845  CB  GLN A 192     8813  11670   8607    575  -1111   -235       C  
ATOM    846  CG  GLN A 192      -0.610  12.306  30.704  1.00 91.85           C  
ANISOU  846  CG  GLN A 192    10724  13545  10631    610  -1120   -119       C  
ATOM    847  CD  GLN A 192      -1.088  11.172  29.828  1.00112.07           C  
ANISOU  847  CD  GLN A 192    13351  16002  13228    631  -1033     -3       C  
ATOM    848  OE1 GLN A 192      -1.098  10.002  30.230  1.00110.32           O  
ANISOU  848  OE1 GLN A 192    13165  15805  12948    665  -1030    113       O  
ATOM    849  NE2 GLN A 192      -1.521  11.495  28.615  1.00 98.78           N  
ANISOU  849  NE2 GLN A 192    11682  14202  11650    611   -969    -33       N  
ATOM    850  N   CYS A 193      -3.637  15.470  32.031  1.00 68.79           N  
ANISOU  850  N   CYS A 193     7807  10750   7582    517  -1145   -597       N  
ATOM    851  CA  CYS A 193      -4.667  16.359  31.498  1.00 66.48           C  
ANISOU  851  CA  CYS A 193     7525  10372   7364    485  -1112   -712       C  
ATOM    852  C   CYS A 193      -5.043  17.501  32.422  1.00 71.66           C  
ANISOU  852  C   CYS A 193     8134  11121   7974    494  -1193   -921       C  
ATOM    853  O   CYS A 193      -4.911  17.399  33.640  1.00 74.12           O  
ANISOU  853  O   CYS A 193     8422  11615   8123    533  -1246   -975       O  
ATOM    854  CB  CYS A 193      -5.896  15.539  31.127  1.00 64.80           C  
ANISOU  854  CB  CYS A 193     7392  10142   7086    479   -994   -624       C  
ATOM    855  SG  CYS A 193      -5.495  13.937  30.393  1.00 67.46           S  
ANISOU  855  SG  CYS A 193     7785  10405   7440    492   -923   -397       S  
ATOM    856  N   GLU A 194      -5.540  18.585  31.809  1.00 66.73           N  
ANISOU  856  N   GLU A 194     7490  10371   7493    465  -1207  -1042       N  
ATOM    857  CA  GLU A 194      -6.020  19.799  32.456  1.00 67.37           C  
ANISOU  857  CA  GLU A 194     7523  10490   7585    479  -1291  -1271       C  
ATOM    858  C   GLU A 194      -7.423  20.141  31.934  1.00 69.05           C  
ANISOU  858  C   GLU A 194     7773  10634   7830    466  -1215  -1325       C  
ATOM    859  O   GLU A 194      -7.647  20.106  30.720  1.00 67.51           O  
ANISOU  859  O   GLU A 194     7604  10275   7770    423  -1151  -1228       O  
ATOM    860  CB  GLU A 194      -5.047  20.966  32.209  1.00 69.51           C  
ANISOU  860  CB  GLU A 194     7708  10637   8068    452  -1424  -1372       C  
ATOM    861  N   VAL A 195      -8.358  20.458  32.858  1.00 64.58           N  
ANISOU  861  N   VAL A 195     7199  10212   7126    509  -1223  -1480       N  
ATOM    862  CA  VAL A 195      -9.751  20.856  32.603  1.00 63.88           C  
ANISOU  862  CA  VAL A 195     7131  10097   7044    512  -1163  -1565       C  
ATOM    863  C   VAL A 195      -9.764  21.918  31.475  1.00 66.83           C  
ANISOU  863  C   VAL A 195     7478  10222   7691    465  -1202  -1615       C  
ATOM    864  O   VAL A 195      -8.918  22.809  31.496  1.00 67.04           O  
ANISOU  864  O   VAL A 195     7438  10161   7872    455  -1326  -1708       O  
ATOM    865  CB  VAL A 195     -10.454  21.355  33.912  1.00 69.56           C  
ANISOU  865  CB  VAL A 195     7805  11030   7593    583  -1209  -1783       C  
ATOM    866  CG1 VAL A 195     -11.872  21.881  33.647  1.00 69.35           C  
ANISOU  866  CG1 VAL A 195     7783  10975   7590    595  -1158  -1894       C  
ATOM    867  CG2 VAL A 195     -10.492  20.251  34.966  1.00 69.70           C  
ANISOU  867  CG2 VAL A 195     7837  11318   7326    621  -1159  -1688       C  
ATOM    868  N   PRO A 196     -10.622  21.797  30.433  1.00 62.23           N  
ANISOU  868  N   PRO A 196     6940   9519   7185    430  -1106  -1530       N  
ATOM    869  CA  PRO A 196     -11.728  20.835  30.273  1.00 60.75           C  
ANISOU  869  CA  PRO A 196     6825   9400   6856    431   -969  -1426       C  
ATOM    870  C   PRO A 196     -11.346  19.484  29.652  1.00 62.54           C  
ANISOU  870  C   PRO A 196     7115   9607   7039    404   -878  -1188       C  
ATOM    871  O   PRO A 196     -12.239  18.753  29.202  1.00 62.34           O  
ANISOU  871  O   PRO A 196     7146   9574   6964    390   -775  -1090       O  
ATOM    872  CB  PRO A 196     -12.728  21.607  29.412  1.00 61.97           C  
ANISOU  872  CB  PRO A 196     6977   9409   7158    408   -944  -1484       C  
ATOM    873  CG  PRO A 196     -11.902  22.536  28.587  1.00 66.31           C  
ANISOU  873  CG  PRO A 196     7477   9766   7953    367  -1030  -1487       C  
ATOM    874  CD  PRO A 196     -10.624  22.807  29.356  1.00 63.08           C  
ANISOU  874  CD  PRO A 196     7013   9408   7549    384  -1149  -1553       C  
ATOM    875  N   LEU A 197     -10.052  19.127  29.654  1.00 57.13           N  
ANISOU  875  N   LEU A 197     6416   8913   6378    401   -922  -1105       N  
ATOM    876  CA  LEU A 197      -9.645  17.802  29.195  1.00 56.06           C  
ANISOU  876  CA  LEU A 197     6333   8767   6199    394   -850   -903       C  
ATOM    877  C   LEU A 197      -9.601  16.891  30.409  1.00 59.27           C  
ANISOU  877  C   LEU A 197     6756   9363   6400    429   -845   -852       C  
ATOM    878  O   LEU A 197      -9.471  17.359  31.529  1.00 61.12           O  
ANISOU  878  O   LEU A 197     6946   9743   6533    461   -914   -967       O  
ATOM    879  CB  LEU A 197      -8.327  17.765  28.389  1.00 55.81           C  
ANISOU  879  CB  LEU A 197     6273   8629   6305    378   -885   -816       C  
ATOM    880  CG  LEU A 197      -8.370  18.367  26.969  1.00 60.46           C  
ANISOU  880  CG  LEU A 197     6843   9048   7081    338   -864   -789       C  
ATOM    881  CD1 LEU A 197      -7.129  18.008  26.190  1.00 60.54           C  
ANISOU  881  CD1 LEU A 197     6817   9006   7178    333   -876   -671       C  
ATOM    882  CD2 LEU A 197      -9.591  17.904  26.171  1.00 61.77           C  
ANISOU  882  CD2 LEU A 197     7075   9161   7234    325   -755   -728       C  
ATOM    883  N   VAL A 198      -9.756  15.602  30.191  1.00 53.89           N  
ANISOU  883  N   VAL A 198     6132   8685   5661    426   -770   -681       N  
ATOM    884  CA  VAL A 198      -9.862  14.595  31.235  1.00 53.76           C  
ANISOU  884  CA  VAL A 198     6128   8833   5463    448   -757   -580       C  
ATOM    885  C   VAL A 198      -9.150  13.312  30.741  1.00 56.31           C  
ANISOU  885  C   VAL A 198     6489   9077   5828    449   -737   -388       C  
ATOM    886  O   VAL A 198      -9.183  13.006  29.548  1.00 53.70           O  
ANISOU  886  O   VAL A 198     6193   8584   5626    433   -693   -333       O  
ATOM    887  CB  VAL A 198     -11.396  14.439  31.466  1.00 58.31           C  
ANISOU  887  CB  VAL A 198     6728   9486   5941    435   -680   -583       C  
ATOM    888  CG1 VAL A 198     -11.880  12.995  31.482  1.00 58.70           C  
ANISOU  888  CG1 VAL A 198     6826   9549   5929    418   -613   -376       C  
ATOM    889  CG2 VAL A 198     -11.872  15.225  32.678  1.00 59.30           C  
ANISOU  889  CG2 VAL A 198     6798   9825   5910    469   -716   -735       C  
ATOM    890  N   ARG A 199      -8.479  12.595  31.645  1.00 55.13           N  
ANISOU  890  N   ARG A 199     6327   9049   5573    475   -777   -294       N  
ATOM    891  CA  ARG A 199      -7.767  11.361  31.318  1.00 55.34           C  
ANISOU  891  CA  ARG A 199     6379   9004   5643    489   -776   -119       C  
ATOM    892  C   ARG A 199      -8.752  10.306  30.829  1.00 59.27           C  
ANISOU  892  C   ARG A 199     6937   9423   6159    467   -700     11       C  
ATOM    893  O   ARG A 199      -9.859  10.180  31.358  1.00 59.89           O  
ANISOU  893  O   ARG A 199     7024   9594   6137    444   -660     34       O  
ATOM    894  CB  ARG A 199      -6.956  10.859  32.535  1.00 58.78           C  
ANISOU  894  CB  ARG A 199     6778   9604   5951    521   -844    -42       C  
ATOM    895  CG  ARG A 199      -6.081   9.604  32.319  1.00 73.92           C  
ANISOU  895  CG  ARG A 199     8711  11450   7927    547   -865    134       C  
ATOM    896  CD  ARG A 199      -4.818   9.848  31.497  1.00 87.20           C  
ANISOU  896  CD  ARG A 199    10369  13010   9752    573   -901     96       C  
ATOM    897  NE  ARG A 199      -4.826   9.054  30.265  1.00 99.29           N  
ANISOU  897  NE  ARG A 199    11943  14360  11421    584   -854    173       N  
ATOM    898  CZ  ARG A 199      -3.917   8.139  29.945  1.00118.83           C  
ANISOU  898  CZ  ARG A 199    14414  16769  13967    630   -881    273       C  
ATOM    899  NH1 ARG A 199      -2.889   7.903  30.752  1.00111.90           N  
ANISOU  899  NH1 ARG A 199    13492  15984  13040    663   -955    327       N  
ATOM    900  NH2 ARG A 199      -4.018   7.463  28.808  1.00107.06           N  
ANISOU  900  NH2 ARG A 199    12958  15126  12596    651   -842    308       N  
ATOM    901  N   THR A 200      -8.376   9.623  29.760  1.00 55.35           N  
ANISOU  901  N   THR A 200     6474   8758   5799    477   -684     82       N  
ATOM    902  CA  THR A 200      -9.143   8.526  29.169  1.00 55.22           C  
ANISOU  902  CA  THR A 200     6512   8631   5838    464   -635    196       C  
ATOM    903  C   THR A 200      -8.167   7.592  28.465  1.00 59.78           C  
ANISOU  903  C   THR A 200     7102   9080   6534    509   -664    277       C  
ATOM    904  O   THR A 200      -7.258   8.051  27.771  1.00 57.31           O  
ANISOU  904  O   THR A 200     6764   8714   6298    539   -679    207       O  
ATOM    905  CB  THR A 200     -10.313   8.994  28.258  1.00 60.84           C  
ANISOU  905  CB  THR A 200     7255   9255   6607    427   -565    115       C  
ATOM    906  OG1 THR A 200     -10.909   7.829  27.683  1.00 57.22           O  
ANISOU  906  OG1 THR A 200     6844   8681   6215    417   -535    224       O  
ATOM    907  CG2 THR A 200      -9.882   9.984  27.141  1.00 57.84           C  
ANISOU  907  CG2 THR A 200     6861   8780   6338    433   -557    -11       C  
ATOM    908  N   ASP A 201      -8.353   6.281  28.684  1.00 60.04           N  
ANISOU  908  N   ASP A 201     7160   9068   6585    516   -678    429       N  
ATOM    909  CA  ASP A 201      -7.561   5.192  28.110  1.00 60.94           C  
ANISOU  909  CA  ASP A 201     7284   9048   6821    571   -717    507       C  
ATOM    910  C   ASP A 201      -8.179   4.740  26.787  1.00 64.64           C  
ANISOU  910  C   ASP A 201     7797   9343   7421    576   -677    471       C  
ATOM    911  O   ASP A 201      -7.688   3.787  26.170  1.00 65.68           O  
ANISOU  911  O   ASP A 201     7939   9350   7668    632   -710    505       O  
ATOM    912  CB  ASP A 201      -7.467   4.020  29.106  1.00 65.37           C  
ANISOU  912  CB  ASP A 201     7841   9639   7357    575   -774    695       C  
ATOM    913  CG  ASP A 201      -6.815   4.390  30.435  1.00 87.00           C  
ANISOU  913  CG  ASP A 201    10530  12576   9950    579   -820    737       C  
ATOM    914  OD1 ASP A 201      -7.369   4.016  31.495  1.00 91.04           O  
ANISOU  914  OD1 ASP A 201    11027  13214  10348    543   -828    860       O  
ATOM    915  OD2 ASP A 201      -5.758   5.066  30.416  1.00 94.17           O  
ANISOU  915  OD2 ASP A 201    11401  13526  10851    617   -851    650       O  
ATOM    916  N   ASN A 202      -9.265   5.426  26.357  1.00 58.56           N  
ANISOU  916  N   ASN A 202     7049   8570   6633    525   -612    391       N  
ATOM    917  CA  ASN A 202      -9.949   5.160  25.106  1.00 57.18           C  
ANISOU  917  CA  ASN A 202     6910   8255   6560    525   -573    340       C  
ATOM    918  C   ASN A 202      -9.377   6.107  24.035  1.00 58.49           C  
ANISOU  918  C   ASN A 202     7051   8410   6763    554   -545    206       C  
ATOM    919  O   ASN A 202      -9.656   7.309  24.069  1.00 57.45           O  
ANISOU  919  O   ASN A 202     6899   8347   6581    516   -513    124       O  
ATOM    920  CB  ASN A 202     -11.470   5.303  25.281  1.00 59.49           C  
ANISOU  920  CB  ASN A 202     7230   8562   6813    452   -523    351       C  
ATOM    921  CG  ASN A 202     -12.304   5.160  24.025  1.00 73.27           C  
ANISOU  921  CG  ASN A 202     9009  10179   8651    442   -483    290       C  
ATOM    922  OD1 ASN A 202     -11.894   4.583  23.015  1.00 62.24           O  
ANISOU  922  OD1 ASN A 202     7624   8666   7359    495   -500    260       O  
ATOM    923  ND2 ASN A 202     -13.516   5.669  24.079  1.00 69.97           N  
ANISOU  923  ND2 ASN A 202     8602   9795   8190    381   -431    264       N  
ATOM    924  N   PRO A 203      -8.550   5.582  23.096  1.00 54.64           N  
ANISOU  924  N   PRO A 203     6551   7843   6365    625   -562    185       N  
ATOM    925  CA  PRO A 203      -7.927   6.450  22.073  1.00 53.53           C  
ANISOU  925  CA  PRO A 203     6366   7723   6250    653   -535     88       C  
ATOM    926  C   PRO A 203      -8.917   7.151  21.152  1.00 57.04           C  
ANISOU  926  C   PRO A 203     6823   8144   6705    612   -472     12       C  
ATOM    927  O   PRO A 203      -8.597   8.225  20.642  1.00 56.97           O  
ANISOU  927  O   PRO A 203     6767   8184   6696    601   -450    -44       O  
ATOM    928  CB  PRO A 203      -7.051   5.484  21.274  1.00 55.75           C  
ANISOU  928  CB  PRO A 203     6631   7941   6612    750   -563     88       C  
ATOM    929  CG  PRO A 203      -6.804   4.333  22.204  1.00 61.47           C  
ANISOU  929  CG  PRO A 203     7379   8621   7356    774   -628    190       C  
ATOM    930  CD  PRO A 203      -8.095   4.184  22.946  1.00 57.03           C  
ANISOU  930  CD  PRO A 203     6869   8045   6756    691   -615    252       C  
ATOM    931  N   LYS A 204     -10.119   6.570  20.965  1.00 53.02           N  
ANISOU  931  N   LYS A 204     6369   7561   6214    584   -451     23       N  
ATOM    932  CA  LYS A 204     -11.187   7.149  20.157  1.00 52.61           C  
ANISOU  932  CA  LYS A 204     6332   7487   6170    543   -396    -41       C  
ATOM    933  C   LYS A 204     -11.670   8.481  20.791  1.00 57.25           C  
ANISOU  933  C   LYS A 204     6902   8157   6693    473   -371    -74       C  
ATOM    934  O   LYS A 204     -12.102   9.383  20.068  1.00 57.20           O  
ANISOU  934  O   LYS A 204     6877   8153   6703    449   -335   -136       O  
ATOM    935  CB  LYS A 204     -12.340   6.124  20.009  1.00 55.80           C  
ANISOU  935  CB  LYS A 204     6794   7793   6615    524   -394    -11       C  
ATOM    936  CG  LYS A 204     -13.653   6.610  19.360  1.00 62.65           C  
ANISOU  936  CG  LYS A 204     7681   8638   7486    472   -341    -64       C  
ATOM    937  CD  LYS A 204     -13.477   7.102  17.931  1.00 65.69           C  
ANISOU  937  CD  LYS A 204     8038   9019   7901    509   -313   -151       C  
ATOM    938  CE  LYS A 204     -14.794   7.361  17.249  1.00 72.10           C  
ANISOU  938  CE  LYS A 204     8870   9801   8724    465   -271   -193       C  
ATOM    939  NZ  LYS A 204     -14.612   7.698  15.814  1.00 81.14           N  
ANISOU  939  NZ  LYS A 204     9982  10961   9888    509   -249   -262       N  
ATOM    940  N   SER A 205     -11.552   8.616  22.127  1.00 53.83           N  
ANISOU  940  N   SER A 205     6466   7799   6188    449   -397    -36       N  
ATOM    941  CA  SER A 205     -11.956   9.825  22.848  1.00 52.81           C  
ANISOU  941  CA  SER A 205     6312   7757   5994    401   -389    -93       C  
ATOM    942  C   SER A 205     -10.874  10.896  22.890  1.00 57.39           C  
ANISOU  942  C   SER A 205     6831   8386   6589    413   -424   -151       C  
ATOM    943  O   SER A 205     -11.192  12.022  23.264  1.00 57.61           O  
ANISOU  943  O   SER A 205     6832   8458   6601    379   -430   -226       O  
ATOM    944  CB  SER A 205     -12.346   9.486  24.281  1.00 54.43           C  
ANISOU  944  CB  SER A 205     6529   8055   6097    380   -406    -38       C  
ATOM    945  OG  SER A 205     -13.529   8.714  24.334  1.00 57.23           O  
ANISOU  945  OG  SER A 205     6924   8380   6442    347   -372     23       O  
ATOM    946  N   TRP A 206      -9.613  10.572  22.542  1.00 55.35           N  
ANISOU  946  N   TRP A 206     6542   8118   6369    461   -455   -119       N  
ATOM    947  CA  TRP A 206      -8.510  11.542  22.628  1.00 56.62           C  
ANISOU  947  CA  TRP A 206     6631   8327   6556    465   -497   -154       C  
ATOM    948  C   TRP A 206      -8.780  12.777  21.773  1.00 62.45           C  
ANISOU  948  C   TRP A 206     7326   9038   7365    428   -478   -215       C  
ATOM    949  O   TRP A 206      -9.185  12.656  20.616  1.00 62.90           O  
ANISOU  949  O   TRP A 206     7388   9045   7466    432   -431   -207       O  
ATOM    950  CB  TRP A 206      -7.138  10.917  22.289  1.00 55.65           C  
ANISOU  950  CB  TRP A 206     6472   8207   6467    527   -525    -99       C  
ATOM    951  CG  TRP A 206      -6.704   9.830  23.241  1.00 57.55           C  
ANISOU  951  CG  TRP A 206     6739   8472   6657    564   -564    -29       C  
ATOM    952  CD1 TRP A 206      -7.272   9.511  24.443  1.00 60.88           C  
ANISOU  952  CD1 TRP A 206     7197   8940   6993    540   -581      3       C  
ATOM    953  CD2 TRP A 206      -5.595   8.930  23.072  1.00 58.07           C  
ANISOU  953  CD2 TRP A 206     6783   8529   6753    635   -596     28       C  
ATOM    954  NE1 TRP A 206      -6.605   8.452  25.018  1.00 61.18           N  
ANISOU  954  NE1 TRP A 206     7240   8989   7015    584   -624     95       N  
ATOM    955  CE2 TRP A 206      -5.563   8.085  24.207  1.00 62.62           C  
ANISOU  955  CE2 TRP A 206     7389   9127   7275    646   -638    103       C  
ATOM    956  CE3 TRP A 206      -4.635   8.742  22.061  1.00 59.52           C  
ANISOU  956  CE3 TRP A 206     6914   8700   7001    696   -593     27       C  
ATOM    957  CZ2 TRP A 206      -4.604   7.074  24.364  1.00 62.79           C  
ANISOU  957  CZ2 TRP A 206     7397   9135   7325    714   -684    175       C  
ATOM    958  CZ3 TRP A 206      -3.674   7.750  22.225  1.00 61.87           C  
ANISOU  958  CZ3 TRP A 206     7195   8995   7316    772   -635     79       C  
ATOM    959  CH2 TRP A 206      -3.668   6.927  23.363  1.00 63.26           C  
ANISOU  959  CH2 TRP A 206     7409   9169   7457    780   -684    151       C  
ATOM    960  N   TYR A 207      -8.653  13.957  22.392  1.00 59.55           N  
ANISOU  960  N   TYR A 207     6913   8704   7010    392   -523   -279       N  
ATOM    961  CA  TYR A 207      -8.872  15.240  21.747  1.00 59.49           C  
ANISOU  961  CA  TYR A 207     6852   8655   7096    350   -529   -328       C  
ATOM    962  C   TYR A 207      -7.622  15.627  21.005  1.00 64.94           C  
ANISOU  962  C   TYR A 207     7456   9345   7872    356   -556   -277       C  
ATOM    963  O   TYR A 207      -6.575  15.845  21.620  1.00 64.45           O  
ANISOU  963  O   TYR A 207     7344   9322   7821    363   -620   -275       O  
ATOM    964  CB  TYR A 207      -9.267  16.320  22.777  1.00 61.88           C  
ANISOU  964  CB  TYR A 207     7136   8979   7397    316   -584   -435       C  
ATOM    965  CG  TYR A 207      -9.736  17.618  22.154  1.00 64.54           C  
ANISOU  965  CG  TYR A 207     7423   9245   7854    272   -600   -489       C  
ATOM    966  CD1 TYR A 207     -11.055  17.778  21.735  1.00 65.64           C  
ANISOU  966  CD1 TYR A 207     7601   9344   7997    253   -548   -520       C  
ATOM    967  CD2 TYR A 207      -8.858  18.684  21.967  1.00 66.59           C  
ANISOU  967  CD2 TYR A 207     7590   9472   8239    246   -675   -498       C  
ATOM    968  CE1 TYR A 207     -11.489  18.962  21.141  1.00 65.78           C  
ANISOU  968  CE1 TYR A 207     7567   9287   8138    215   -570   -559       C  
ATOM    969  CE2 TYR A 207      -9.277  19.868  21.359  1.00 68.06           C  
ANISOU  969  CE2 TYR A 207     7722   9575   8563    201   -702   -525       C  
ATOM    970  CZ  TYR A 207     -10.596  20.004  20.954  1.00 74.62           C  
ANISOU  970  CZ  TYR A 207     8595  10364   9392    188   -650   -557       C  
ATOM    971  OH  TYR A 207     -11.029  21.169  20.371  1.00 76.62           O  
ANISOU  971  OH  TYR A 207     8791  10529   9792    146   -685   -576       O  
ATOM    972  N   GLU A 208      -7.727  15.674  19.668  1.00 63.88           N  
ANISOU  972  N   GLU A 208     7296   9184   7791    357   -508   -229       N  
ATOM    973  CA  GLU A 208      -6.665  16.052  18.728  1.00 65.05           C  
ANISOU  973  CA  GLU A 208     7345   9360   8013    362   -515   -157       C  
ATOM    974  C   GLU A 208      -5.343  15.311  19.035  1.00 72.24           C  
ANISOU  974  C   GLU A 208     8225  10333   8891    417   -540   -112       C  
ATOM    975  O   GLU A 208      -5.363  14.086  19.162  1.00 73.13           O  
ANISOU  975  O   GLU A 208     8401  10455   8930    477   -513   -105       O  
ATOM    976  CB  GLU A 208      -6.475  17.582  18.700  1.00 66.88           C  
ANISOU  976  CB  GLU A 208     7484   9559   8367    292   -577   -162       C  
ATOM    977  CG  GLU A 208      -7.759  18.334  18.367  1.00 77.68           C  
ANISOU  977  CG  GLU A 208     8872  10858   9785    244   -560   -203       C  
ATOM    978  CD  GLU A 208      -7.638  19.693  17.705  1.00 94.47           C  
ANISOU  978  CD  GLU A 208    10892  12937  12065    181   -607   -161       C  
ATOM    979  OE1 GLU A 208      -6.533  20.285  17.719  1.00 92.90           O  
ANISOU  979  OE1 GLU A 208    10593  12748  11955    157   -673   -109       O  
ATOM    980  OE2 GLU A 208      -8.663  20.167  17.165  1.00 81.83           O  
ANISOU  980  OE2 GLU A 208     9301  11285  10508    152   -583   -168       O  
ATOM    981  N   ASP A 209      -4.218  16.033  19.158  1.00 70.20           N  
ANISOU  981  N   ASP A 209     7864  10107   8700    398   -600    -78       N  
ATOM    982  CA  ASP A 209      -2.902  15.442  19.412  1.00 71.07           C  
ANISOU  982  CA  ASP A 209     7928  10285   8791    449   -629    -32       C  
ATOM    983  C   ASP A 209      -2.598  15.313  20.923  1.00 72.32           C  
ANISOU  983  C   ASP A 209     8122  10452   8906    450   -701    -83       C  
ATOM    984  O   ASP A 209      -1.479  14.922  21.293  1.00 72.72           O  
ANISOU  984  O   ASP A 209     8128  10556   8944    487   -740    -47       O  
ATOM    985  CB  ASP A 209      -1.811  16.278  18.703  1.00 75.01           C  
ANISOU  985  CB  ASP A 209     8280  10833   9389    423   -657     49       C  
ATOM    986  CG  ASP A 209      -1.801  16.103  17.190  1.00 94.62           C  
ANISOU  986  CG  ASP A 209    10707  13372  11873    450   -581    126       C  
ATOM    987  OD1 ASP A 209      -1.203  15.112  16.709  1.00 97.32           O  
ANISOU  987  OD1 ASP A 209    11031  13792  12153    536   -542    156       O  
ATOM    988  OD2 ASP A 209      -2.395  16.956  16.485  1.00101.45           O  
ANISOU  988  OD2 ASP A 209    11538  14212  12797    394   -564    152       O  
ATOM    989  N   VAL A 210      -3.592  15.625  21.791  1.00 65.63           N  
ANISOU  989  N   VAL A 210     7343   9570   8023    415   -717   -166       N  
ATOM    990  CA  VAL A 210      -3.436  15.539  23.248  1.00 64.17           C  
ANISOU  990  CA  VAL A 210     7184   9428   7767    420   -782   -221       C  
ATOM    991  C   VAL A 210      -3.725  14.106  23.666  1.00 66.81           C  
ANISOU  991  C   VAL A 210     7609   9791   7987    475   -742   -181       C  
ATOM    992  O   VAL A 210      -4.832  13.792  24.097  1.00 66.44           O  
ANISOU  992  O   VAL A 210     7639   9736   7870    466   -709   -209       O  
ATOM    993  CB  VAL A 210      -4.286  16.554  24.057  1.00 66.83           C  
ANISOU  993  CB  VAL A 210     7534   9752   8106    371   -826   -340       C  
ATOM    994  CG1 VAL A 210      -3.698  16.755  25.449  1.00 66.92           C  
ANISOU  994  CG1 VAL A 210     7524   9842   8060    381   -918   -403       C  
ATOM    995  CG2 VAL A 210      -4.430  17.890  23.327  1.00 66.63           C  
ANISOU  995  CG2 VAL A 210     7436   9649   8231    312   -854   -369       C  
ATOM    996  N   GLU A 211      -2.730  13.237  23.490  1.00 62.70           N  
ANISOU  996  N   GLU A 211     7066   9298   7460    532   -748   -107       N  
ATOM    997  CA  GLU A 211      -2.781  11.818  23.810  1.00 62.84           C  
ANISOU  997  CA  GLU A 211     7149   9319   7409    592   -731    -49       C  
ATOM    998  C   GLU A 211      -3.150  11.614  25.282  1.00 66.60           C  
ANISOU  998  C   GLU A 211     7670   9852   7781    579   -772    -58       C  
ATOM    999  O   GLU A 211      -2.645  12.324  26.151  1.00 67.57           O  
ANISOU  999  O   GLU A 211     7748  10047   7878    560   -839   -100       O  
ATOM   1000  CB  GLU A 211      -1.410  11.193  23.478  1.00 65.28           C  
ANISOU 1000  CB  GLU A 211     7397   9657   7751    659   -756     15       C  
ATOM   1001  CG  GLU A 211      -1.132   9.799  24.020  1.00 81.50           C  
ANISOU 1001  CG  GLU A 211     9496  11709   9762    728   -774     80       C  
ATOM   1002  CD  GLU A 211       0.240   9.670  24.657  1.00117.02           C  
ANISOU 1002  CD  GLU A 211    13927  16278  14256    766   -846    122       C  
ATOM   1003  OE1 GLU A 211       0.306   9.426  25.884  1.00120.51           O  
ANISOU 1003  OE1 GLU A 211    14391  16769  14627    761   -899    147       O  
ATOM   1004  OE2 GLU A 211       1.248   9.855  23.937  1.00115.62           O  
ANISOU 1004  OE2 GLU A 211    13665  16125  14141    801   -850    134       O  
ATOM   1005  N   GLY A 212      -4.057  10.673  25.525  1.00 61.51           N  
ANISOU 1005  N   GLY A 212     7106   9186   7080    588   -735    -16       N  
ATOM   1006  CA  GLY A 212      -4.502  10.285  26.857  1.00 60.99           C  
ANISOU 1006  CA  GLY A 212     7076   9198   6899    578   -761     13       C  
ATOM   1007  C   GLY A 212      -5.604  11.133  27.447  1.00 63.14           C  
ANISOU 1007  C   GLY A 212     7363   9526   7101    525   -747    -73       C  
ATOM   1008  O   GLY A 212      -6.161  10.769  28.483  1.00 61.84           O  
ANISOU 1008  O   GLY A 212     7222   9454   6822    519   -753    -44       O  
ATOM   1009  N   CYS A 213      -5.939  12.256  26.788  1.00 59.45           N  
ANISOU 1009  N   CYS A 213     6873   9011   6704    490   -730   -174       N  
ATOM   1010  CA  CYS A 213      -6.941  13.206  27.274  1.00 59.32           C  
ANISOU 1010  CA  CYS A 213     6859   9036   6645    451   -727   -283       C  
ATOM   1011  C   CYS A 213      -8.078  13.388  26.291  1.00 61.43           C  
ANISOU 1011  C   CYS A 213     7163   9208   6970    421   -653   -306       C  
ATOM   1012  O   CYS A 213      -7.836  13.617  25.106  1.00 60.38           O  
ANISOU 1012  O   CYS A 213     7015   8982   6946    416   -630   -297       O  
ATOM   1013  CB  CYS A 213      -6.295  14.550  27.584  1.00 60.28           C  
ANISOU 1013  CB  CYS A 213     6905   9182   6818    436   -806   -400       C  
ATOM   1014  SG  CYS A 213      -4.784  14.435  28.552  1.00 65.79           S  
ANISOU 1014  SG  CYS A 213     7544   9985   7469    470   -905   -382       S  
ATOM   1015  N   GLY A 214      -9.295  13.375  26.826  1.00 56.35           N  
ANISOU 1015  N   GLY A 214     6556   8613   6243    403   -619   -335       N  
ATOM   1016  CA  GLY A 214     -10.528  13.609  26.097  1.00 55.00           C  
ANISOU 1016  CA  GLY A 214     6417   8373   6109    373   -554   -366       C  
ATOM   1017  C   GLY A 214     -11.296  14.767  26.691  1.00 60.41           C  
ANISOU 1017  C   GLY A 214     7075   9117   6763    354   -570   -502       C  
ATOM   1018  O   GLY A 214     -11.004  15.187  27.810  1.00 61.39           O  
ANISOU 1018  O   GLY A 214     7165   9359   6802    370   -625   -571       O  
ATOM   1019  N   ILE A 215     -12.277  15.304  25.951  1.00 58.09           N  
ANISOU 1019  N   ILE A 215     6789   8745   6535    327   -527   -553       N  
ATOM   1020  CA  ILE A 215     -13.088  16.432  26.411  1.00 58.74           C  
ANISOU 1020  CA  ILE A 215     6841   8865   6612    319   -545   -697       C  
ATOM   1021  C   ILE A 215     -14.140  15.907  27.381  1.00 61.04           C  
ANISOU 1021  C   ILE A 215     7155   9294   6742    327   -503   -697       C  
ATOM   1022  O   ILE A 215     -14.859  14.960  27.056  1.00 59.54           O  
ANISOU 1022  O   ILE A 215     7013   9088   6519    311   -433   -589       O  
ATOM   1023  CB  ILE A 215     -13.687  17.302  25.257  1.00 62.12           C  
ANISOU 1023  CB  ILE A 215     7258   9160   7184    289   -525   -743       C  
ATOM   1024  CG1 ILE A 215     -14.669  18.388  25.767  1.00 63.26           C  
ANISOU 1024  CG1 ILE A 215     7370   9332   7333    291   -548   -901       C  
ATOM   1025  CG2 ILE A 215     -14.316  16.477  24.142  1.00 64.15           C  
ANISOU 1025  CG2 ILE A 215     7570   9341   7465    271   -440   -636       C  
ATOM   1026  CD1 ILE A 215     -14.006  19.618  26.379  1.00 74.30           C  
ANISOU 1026  CD1 ILE A 215     8696  10736   8799    307   -660  -1048       C  
ATOM   1027  N   GLN A 216     -14.189  16.521  28.588  1.00 56.90           N  
ANISOU 1027  N   GLN A 216     6587   8917   6117    356   -552   -817       N  
ATOM   1028  CA  GLN A 216     -15.114  16.191  29.670  1.00 57.23           C  
ANISOU 1028  CA  GLN A 216     6622   9148   5977    373   -517   -829       C  
ATOM   1029  C   GLN A 216     -16.561  16.277  29.192  1.00 62.81           C  
ANISOU 1029  C   GLN A 216     7345   9824   6697    351   -441   -842       C  
ATOM   1030  O   GLN A 216     -16.898  17.117  28.347  1.00 61.95           O  
ANISOU 1030  O   GLN A 216     7233   9579   6728    338   -442   -923       O  
ATOM   1031  CB  GLN A 216     -14.898  17.106  30.888  1.00 59.41           C  
ANISOU 1031  CB  GLN A 216     6829   9590   6155    423   -594  -1008       C  
ATOM   1032  CG  GLN A 216     -15.134  18.594  30.615  1.00 62.44           C  
ANISOU 1032  CG  GLN A 216     7167   9888   6668    436   -653  -1221       C  
ATOM   1033  CD  GLN A 216     -15.181  19.441  31.851  1.00 68.46           C  
ANISOU 1033  CD  GLN A 216     7860  10825   7327    499   -731  -1429       C  
ATOM   1034  OE1 GLN A 216     -14.351  19.332  32.771  1.00 61.09           O  
ANISOU 1034  OE1 GLN A 216     6896  10025   6289    531   -794  -1454       O  
ATOM   1035  NE2 GLN A 216     -16.126  20.356  31.860  1.00 63.22           N  
ANISOU 1035  NE2 GLN A 216     7162  10161   6699    525   -739  -1601       N  
ATOM   1036  N   CYS A 217     -17.416  15.407  29.737  1.00 60.62           N  
ANISOU 1036  N   CYS A 217     7076   9678   6279    343   -377   -745       N  
ATOM   1037  CA  CYS A 217     -18.809  15.349  29.331  1.00 59.94           C  
ANISOU 1037  CA  CYS A 217     7000   9579   6197    317   -303   -735       C  
ATOM   1038  C   CYS A 217     -19.564  16.662  29.567  1.00 62.41           C  
ANISOU 1038  C   CYS A 217     7259   9943   6512    350   -316   -944       C  
ATOM   1039  O   CYS A 217     -20.320  17.071  28.690  1.00 61.37           O  
ANISOU 1039  O   CYS A 217     7138   9688   6492    329   -285   -980       O  
ATOM   1040  CB  CYS A 217     -19.532  14.187  29.987  1.00 60.99           C  
ANISOU 1040  CB  CYS A 217     7132   9858   6182    296   -243   -573       C  
ATOM   1041  SG  CYS A 217     -21.166  13.901  29.282  1.00 64.43           S  
ANISOU 1041  SG  CYS A 217     7582  10244   6656    249   -153   -521       S  
ATOM   1042  N   GLN A 218     -19.378  17.304  30.726  1.00 58.76           N  
ANISOU 1042  N   GLN A 218     6735   9663   5931    406   -368  -1087       N  
ATOM   1043  CA  GLN A 218     -20.060  18.563  31.014  1.00 58.55           C  
ANISOU 1043  CA  GLN A 218     6647   9686   5913    455   -398  -1316       C  
ATOM   1044  C   GLN A 218     -19.551  19.659  30.089  1.00 61.48           C  
ANISOU 1044  C   GLN A 218     7019   9822   6520    450   -473  -1434       C  
ATOM   1045  O   GLN A 218     -18.346  19.895  30.021  1.00 60.95           O  
ANISOU 1045  O   GLN A 218     6951   9677   6529    448   -549  -1442       O  
ATOM   1046  CB  GLN A 218     -19.894  18.964  32.481  1.00 61.27           C  
ANISOU 1046  CB  GLN A 218     6917  10295   6066    530   -450  -1460       C  
ATOM   1047  CG  GLN A 218     -21.244  19.205  33.177  1.00 78.18           C  
ANISOU 1047  CG  GLN A 218     8994  12658   8051    578   -397  -1561       C  
ATOM   1048  CD  GLN A 218     -21.437  20.588  33.772  1.00100.70           C  
ANISOU 1048  CD  GLN A 218    11768  15579  10913    668   -481  -1870       C  
ATOM   1049  OE1 GLN A 218     -20.534  21.439  33.816  1.00 99.03           O  
ANISOU 1049  OE1 GLN A 218    11543  15264  10821    696   -595  -2024       O  
ATOM   1050  NE2 GLN A 218     -22.635  20.836  34.267  1.00 93.54           N  
ANISOU 1050  NE2 GLN A 218    10800  14856   9887    720   -433  -1974       N  
ATOM   1051  N   ASN A 219     -20.462  20.278  29.329  1.00 57.99           N  
ANISOU 1051  N   ASN A 219     6572   9263   6200    440   -452  -1500       N  
ATOM   1052  CA  ASN A 219     -20.123  21.356  28.396  1.00 57.40           C  
ANISOU 1052  CA  ASN A 219     6484   8963   6363    427   -524  -1583       C  
ATOM   1053  C   ASN A 219     -19.289  22.417  29.144  1.00 62.07           C  
ANISOU 1053  C   ASN A 219     7012   9569   7004    478   -655  -1779       C  
ATOM   1054  O   ASN A 219     -19.772  22.978  30.133  1.00 62.60           O  
ANISOU 1054  O   ASN A 219     7021   9784   6980    547   -693  -1970       O  
ATOM   1055  CB  ASN A 219     -21.381  21.958  27.761  1.00 56.42           C  
ANISOU 1055  CB  ASN A 219     6345   8759   6333    425   -491  -1648       C  
ATOM   1056  CG  ASN A 219     -21.116  22.799  26.538  1.00 78.67           C  
ANISOU 1056  CG  ASN A 219     9158  11331   9402    388   -542  -1643       C  
ATOM   1057  OD1 ASN A 219     -20.110  23.513  26.434  1.00 69.77           O  
ANISOU 1057  OD1 ASN A 219     8001  10098   8412    385   -641  -1690       O  
ATOM   1058  ND2 ASN A 219     -22.048  22.763  25.594  1.00 74.61           N  
ANISOU 1058  ND2 ASN A 219     8663  10730   8956    357   -479  -1579       N  
ATOM   1059  N   PRO A 220     -18.009  22.623  28.743  1.00 58.31           N  
ANISOU 1059  N   PRO A 220     6536   8963   6657    449   -729  -1734       N  
ATOM   1060  CA  PRO A 220     -17.148  23.559  29.493  1.00 59.60           C  
ANISOU 1060  CA  PRO A 220     6634   9136   6877    490   -867  -1913       C  
ATOM   1061  C   PRO A 220     -17.462  25.034  29.263  1.00 64.22           C  
ANISOU 1061  C   PRO A 220     7152   9573   7675    511   -974  -2111       C  
ATOM   1062  O   PRO A 220     -16.869  25.886  29.927  1.00 65.86           O  
ANISOU 1062  O   PRO A 220     7297   9784   7944    553  -1105  -2296       O  
ATOM   1063  CB  PRO A 220     -15.744  23.228  28.989  1.00 60.71           C  
ANISOU 1063  CB  PRO A 220     6790   9170   7106    439   -901  -1766       C  
ATOM   1064  CG  PRO A 220     -15.944  22.649  27.635  1.00 63.17           C  
ANISOU 1064  CG  PRO A 220     7157   9345   7500    376   -808  -1565       C  
ATOM   1065  CD  PRO A 220     -17.283  21.995  27.614  1.00 58.24           C  
ANISOU 1065  CD  PRO A 220     6577   8808   6741    382   -692  -1524       C  
ATOM   1066  N   LEU A 221     -18.369  25.337  28.326  1.00 59.37           N  
ANISOU 1066  N   LEU A 221     6548   8824   7188    483   -929  -2073       N  
ATOM   1067  CA  LEU A 221     -18.734  26.714  28.006  1.00 59.12           C  
ANISOU 1067  CA  LEU A 221     6450   8626   7388    498  -1033  -2235       C  
ATOM   1068  C   LEU A 221     -19.793  27.257  28.949  1.00 64.11           C  
ANISOU 1068  C   LEU A 221     7035   9391   7932    593  -1054  -2480       C  
ATOM   1069  O   LEU A 221     -19.928  28.479  29.062  1.00 65.33           O  
ANISOU 1069  O   LEU A 221     7119   9432   8272    634  -1178  -2681       O  
ATOM   1070  CB  LEU A 221     -19.224  26.815  26.557  1.00 57.25           C  
ANISOU 1070  CB  LEU A 221     6233   8198   7319    431   -981  -2077       C  
ATOM   1071  CG  LEU A 221     -18.284  26.309  25.460  1.00 59.94           C  
ANISOU 1071  CG  LEU A 221     6608   8427   7741    347   -949  -1834       C  
ATOM   1072  CD1 LEU A 221     -18.883  26.544  24.114  1.00 58.86           C  
ANISOU 1072  CD1 LEU A 221     6477   8144   7744    295   -903  -1708       C  
ATOM   1073  CD2 LEU A 221     -16.902  26.973  25.520  1.00 61.25           C  
ANISOU 1073  CD2 LEU A 221     6714   8487   8072    323  -1083  -1848       C  
ATOM   1074  N   PHE A 222     -20.535  26.365  29.636  1.00 60.03           N  
ANISOU 1074  N   PHE A 222     6546   9119   7143    630   -940  -2465       N  
ATOM   1075  CA  PHE A 222     -21.623  26.775  30.522  1.00 61.03           C  
ANISOU 1075  CA  PHE A 222     6617   9425   7148    726   -937  -2683       C  
ATOM   1076  C   PHE A 222     -21.424  26.248  31.947  1.00 66.94           C  
ANISOU 1076  C   PHE A 222     7341  10488   7605    795   -925  -2764       C  
ATOM   1077  O   PHE A 222     -20.952  25.123  32.149  1.00 66.08           O  
ANISOU 1077  O   PHE A 222     7283  10494   7329    754   -849  -2570       O  
ATOM   1078  CB  PHE A 222     -22.987  26.353  29.938  1.00 61.49           C  
ANISOU 1078  CB  PHE A 222     6701   9503   7161    708   -805  -2586       C  
ATOM   1079  CG  PHE A 222     -23.184  26.874  28.527  1.00 61.33           C  
ANISOU 1079  CG  PHE A 222     6697   9195   7410    643   -819  -2498       C  
ATOM   1080  CD1 PHE A 222     -23.640  28.172  28.304  1.00 64.95           C  
ANISOU 1080  CD1 PHE A 222     7088   9503   8085    685   -921  -2684       C  
ATOM   1081  CD2 PHE A 222     -22.817  26.102  27.423  1.00 60.68           C  
ANISOU 1081  CD2 PHE A 222     6689   8993   7374    544   -744  -2234       C  
ATOM   1082  CE1 PHE A 222     -23.754  28.677  27.002  1.00 64.90           C  
ANISOU 1082  CE1 PHE A 222     7087   9240   8332    620   -943  -2577       C  
ATOM   1083  CE2 PHE A 222     -22.934  26.605  26.122  1.00 62.37           C  
ANISOU 1083  CE2 PHE A 222     6907   8974   7819    488   -760  -2146       C  
ATOM   1084  CZ  PHE A 222     -23.411  27.885  25.920  1.00 61.86           C  
ANISOU 1084  CZ  PHE A 222     6773   8770   7961    521   -857  -2304       C  
ATOM   1085  N   THR A 223     -21.751  27.105  32.937  1.00 65.20           N  
ANISOU 1085  N   THR A 223     7034  10407   7331    908  -1011  -3059       N  
ATOM   1086  CA  THR A 223     -21.622  26.814  34.369  1.00 66.39           C  
ANISOU 1086  CA  THR A 223     7136  10895   7195    996  -1018  -3184       C  
ATOM   1087  C   THR A 223     -22.640  25.742  34.787  1.00 72.12           C  
ANISOU 1087  C   THR A 223     7868  11907   7629   1003   -850  -3044       C  
ATOM   1088  O   THR A 223     -23.539  25.411  34.006  1.00 70.73           O  
ANISOU 1088  O   THR A 223     7725  11650   7498    953   -747  -2910       O  
ATOM   1089  CB  THR A 223     -21.812  28.097  35.201  1.00 67.71           C  
ANISOU 1089  CB  THR A 223     7197  11128   7403   1128  -1165  -3569       C  
ATOM   1090  OG1 THR A 223     -23.192  28.469  35.183  1.00 72.08           O  
ANISOU 1090  OG1 THR A 223     7704  11739   7945   1193  -1117  -3696       O  
ATOM   1091  CG2 THR A 223     -20.947  29.254  34.730  1.00 60.79           C  
ANISOU 1091  CG2 THR A 223     6298   9936   6863   1115  -1350  -3708       C  
ATOM   1092  N   GLU A 224     -22.515  25.226  36.026  1.00 70.96           N  
ANISOU 1092  N   GLU A 224     7678  12100   7185   1062   -829  -3070       N  
ATOM   1093  CA  GLU A 224     -23.435  24.240  36.597  1.00 71.40           C  
ANISOU 1093  CA  GLU A 224     7712  12469   6947   1071   -683  -2929       C  
ATOM   1094  C   GLU A 224     -24.829  24.871  36.778  1.00 74.03           C  
ANISOU 1094  C   GLU A 224     7964  12923   7240   1157   -649  -3122       C  
ATOM   1095  O   GLU A 224     -25.834  24.208  36.501  1.00 73.01           O  
ANISOU 1095  O   GLU A 224     7842  12868   7031   1116   -517  -2954       O  
ATOM   1096  CB  GLU A 224     -22.879  23.710  37.934  1.00 75.01           C  
ANISOU 1096  CB  GLU A 224     8119  13279   7104   1125   -693  -2930       C  
ATOM   1097  CG  GLU A 224     -23.745  22.659  38.619  1.00 92.48           C  
ANISOU 1097  CG  GLU A 224    10290  15845   9003   1126   -551  -2747       C  
ATOM   1098  CD  GLU A 224     -23.622  21.216  38.156  1.00125.40           C  
ANISOU 1098  CD  GLU A 224    14541  19967  13136    998   -441  -2351       C  
ATOM   1099  OE1 GLU A 224     -23.142  20.973  37.024  1.00118.46           O  
ANISOU 1099  OE1 GLU A 224    13765  18750  12496    901   -443  -2205       O  
ATOM   1100  OE2 GLU A 224     -24.033  20.323  38.932  1.00128.15           O  
ANISOU 1100  OE2 GLU A 224    14841  20629  13221    996   -356  -2184       O  
ATOM   1101  N   ALA A 225     -24.876  26.160  37.208  1.00 70.31           N  
ANISOU 1101  N   ALA A 225     7413  12456   6847   1276   -779  -3479       N  
ATOM   1102  CA  ALA A 225     -26.111  26.924  37.420  1.00 70.61           C  
ANISOU 1102  CA  ALA A 225     7359  12597   6872   1383   -774  -3719       C  
ATOM   1103  C   ALA A 225     -26.814  27.147  36.100  1.00 73.00           C  
ANISOU 1103  C   ALA A 225     7714  12585   7437   1310   -732  -3622       C  
ATOM   1104  O   ALA A 225     -28.032  26.974  36.035  1.00 72.85           O  
ANISOU 1104  O   ALA A 225     7657  12690   7334   1331   -630  -3603       O  
ATOM   1105  CB  ALA A 225     -25.815  28.255  38.096  1.00 73.26           C  
ANISOU 1105  CB  ALA A 225     7604  12944   7286   1526   -954  -4131       C  
ATOM   1106  N   GLU A 226     -26.043  27.466  35.030  1.00 67.99           N  
ANISOU 1106  N   GLU A 226     7160  11564   7108   1218   -805  -3538       N  
ATOM   1107  CA  GLU A 226     -26.575  27.635  33.673  1.00 65.87           C  
ANISOU 1107  CA  GLU A 226     6944  10992   7092   1137   -770  -3412       C  
ATOM   1108  C   GLU A 226     -27.169  26.314  33.177  1.00 67.26           C  
ANISOU 1108  C   GLU A 226     7186  11234   7134   1036   -593  -3086       C  
ATOM   1109  O   GLU A 226     -28.248  26.338  32.592  1.00 67.85           O  
ANISOU 1109  O   GLU A 226     7257  11259   7265   1021   -523  -3045       O  
ATOM   1110  CB  GLU A 226     -25.505  28.162  32.708  1.00 66.12           C  
ANISOU 1110  CB  GLU A 226     7031  10650   7441   1058   -883  -3361       C  
ATOM   1111  CG  GLU A 226     -25.315  29.669  32.801  1.00 74.81           C  
ANISOU 1111  CG  GLU A 226     8056  11579   8790   1141  -1068  -3671       C  
ATOM   1112  CD  GLU A 226     -24.065  30.254  32.166  1.00 88.45           C  
ANISOU 1112  CD  GLU A 226     9807  12990  10810   1072  -1207  -3640       C  
ATOM   1113  OE1 GLU A 226     -23.139  29.484  31.824  1.00 66.43           O  
ANISOU 1113  OE1 GLU A 226     7090  10153   7997    974  -1167  -3402       O  
ATOM   1114  OE2 GLU A 226     -23.998  31.498  32.045  1.00 88.24           O  
ANISOU 1114  OE2 GLU A 226     9716  12767  11045   1121  -1366  -3856       O  
ATOM   1115  N   HIS A 227     -26.516  25.167  33.479  1.00 61.98           N  
ANISOU 1115  N   HIS A 227     6570  10688   6291    973   -529  -2867       N  
ATOM   1116  CA  HIS A 227     -27.017  23.822  33.139  1.00 60.40           C  
ANISOU 1116  CA  HIS A 227     6426  10557   5967    880   -379  -2559       C  
ATOM   1117  C   HIS A 227     -28.335  23.551  33.887  1.00 67.65           C  
ANISOU 1117  C   HIS A 227     7260  11793   6653    936   -279  -2585       C  
ATOM   1118  O   HIS A 227     -29.337  23.223  33.254  1.00 67.31           O  
ANISOU 1118  O   HIS A 227     7226  11705   6643    888   -189  -2465       O  
ATOM   1119  CB  HIS A 227     -25.984  22.722  33.490  1.00 60.25           C  
ANISOU 1119  CB  HIS A 227     6462  10612   5818    820   -359  -2348       C  
ATOM   1120  CG  HIS A 227     -24.909  22.473  32.468  1.00 61.34           C  
ANISOU 1120  CG  HIS A 227     6698  10446   6161    728   -395  -2195       C  
ATOM   1121  ND1 HIS A 227     -23.842  23.351  32.302  1.00 62.88           N  
ANISOU 1121  ND1 HIS A 227     6896  10466   6530    745   -524  -2331       N  
ATOM   1122  CD2 HIS A 227     -24.708  21.393  31.675  1.00 61.12           C  
ANISOU 1122  CD2 HIS A 227     6755  10296   6170    627   -323  -1923       C  
ATOM   1123  CE1 HIS A 227     -23.068  22.807  31.376  1.00 60.68           C  
ANISOU 1123  CE1 HIS A 227     6698   9978   6378    654   -514  -2129       C  
ATOM   1124  NE2 HIS A 227     -23.549  21.628  30.966  1.00 60.01           N  
ANISOU 1124  NE2 HIS A 227     6667   9917   6215    588   -396  -1894       N  
ATOM   1125  N   GLN A 228     -28.335  23.732  35.228  1.00 67.40           N  
ANISOU 1125  N   GLN A 228     7133  12095   6383   1043   -300  -2751       N  
ATOM   1126  CA  GLN A 228     -29.484  23.496  36.121  1.00 69.10           C  
ANISOU 1126  CA  GLN A 228     7238  12684   6332   1113   -206  -2784       C  
ATOM   1127  C   GLN A 228     -30.695  24.349  35.746  1.00 72.95           C  
ANISOU 1127  C   GLN A 228     7664  13129   6927   1177   -198  -2970       C  
ATOM   1128  O   GLN A 228     -31.820  23.856  35.823  1.00 73.42           O  
ANISOU 1128  O   GLN A 228     7671  13370   6856   1169    -82  -2868       O  
ATOM   1129  CB  GLN A 228     -29.109  23.703  37.601  1.00 72.61           C  
ANISOU 1129  CB  GLN A 228     7582  13503   6503   1233   -251  -2963       C  
ATOM   1130  CG  GLN A 228     -28.255  22.549  38.142  1.00 96.12           C  
ANISOU 1130  CG  GLN A 228    10596  16628   9297   1165   -219  -2708       C  
ATOM   1131  CD  GLN A 228     -27.822  22.698  39.581  1.00126.66           C  
ANISOU 1131  CD  GLN A 228    14363  20876  12884   1280   -268  -2867       C  
ATOM   1132  OE1 GLN A 228     -28.289  21.975  40.470  1.00124.85           O  
ANISOU 1132  OE1 GLN A 228    14051  21035  12352   1300   -180  -2742       O  
ATOM   1133  NE2 GLN A 228     -26.863  23.581  39.836  1.00122.41           N  
ANISOU 1133  NE2 GLN A 228    13826  20244  12440   1352   -416  -3128       N  
ATOM   1134  N   ASP A 229     -30.462  25.603  35.325  1.00 68.29           N  
ANISOU 1134  N   ASP A 229     7073  12291   6584   1237   -325  -3228       N  
ATOM   1135  CA  ASP A 229     -31.504  26.520  34.874  1.00 67.95           C  
ANISOU 1135  CA  ASP A 229     6973  12151   6695   1302   -344  -3416       C  
ATOM   1136  C   ASP A 229     -32.093  26.015  33.531  1.00 72.07           C  
ANISOU 1136  C   ASP A 229     7575  12422   7386   1173   -257  -3161       C  
ATOM   1137  O   ASP A 229     -33.311  26.084  33.325  1.00 74.01           O  
ANISOU 1137  O   ASP A 229     7766  12734   7620   1196   -188  -3176       O  
ATOM   1138  CB  ASP A 229     -30.939  27.944  34.744  1.00 69.64           C  
ANISOU 1138  CB  ASP A 229     7168  12125   7168   1384   -526  -3726       C  
ATOM   1139  CG  ASP A 229     -31.878  28.907  34.057  1.00 81.34           C  
ANISOU 1139  CG  ASP A 229     8608  13413   8885   1432   -567  -3883       C  
ATOM   1140  OD1 ASP A 229     -32.851  29.352  34.703  1.00 85.05           O  
ANISOU 1140  OD1 ASP A 229     8965  14113   9237   1558   -549  -4093       O  
ATOM   1141  OD2 ASP A 229     -31.678  29.167  32.859  1.00 85.54           O  
ANISOU 1141  OD2 ASP A 229     9213  13582   9708   1344   -610  -3781       O  
ATOM   1142  N   MET A 230     -31.238  25.479  32.643  1.00 65.45           N  
ANISOU 1142  N   MET A 230     6857  11320   6692   1045   -261  -2932       N  
ATOM   1143  CA  MET A 230     -31.696  24.941  31.359  1.00 62.93           C  
ANISOU 1143  CA  MET A 230     6615  10777   6519    927   -188  -2696       C  
ATOM   1144  C   MET A 230     -32.521  23.670  31.563  1.00 66.74           C  
ANISOU 1144  C   MET A 230     7093  11477   6789    865    -38  -2457       C  
ATOM   1145  O   MET A 230     -33.547  23.514  30.907  1.00 66.70           O  
ANISOU 1145  O   MET A 230     7082  11420   6842    827     29  -2376       O  
ATOM   1146  CB  MET A 230     -30.522  24.677  30.402  1.00 62.80           C  
ANISOU 1146  CB  MET A 230     6714  10458   6690    822   -235  -2533       C  
ATOM   1147  CG  MET A 230     -30.953  24.331  28.977  1.00 64.19           C  
ANISOU 1147  CG  MET A 230     6961  10393   7037    718   -183  -2336       C  
ATOM   1148  SD  MET A 230     -32.187  25.434  28.247  1.00 68.02           S  
ANISOU 1148  SD  MET A 230     7387  10740   7717    761   -204  -2479       S  
ATOM   1149  CE  MET A 230     -31.144  26.781  27.733  1.00 64.93           C  
ANISOU 1149  CE  MET A 230     6999  10048   7625    785   -376  -2637       C  
ATOM   1150  N   HIS A 231     -32.102  22.800  32.494  1.00 63.33           N  
ANISOU 1150  N   HIS A 231     6651  11291   6120    855      5  -2343       N  
ATOM   1151  CA  HIS A 231     -32.782  21.541  32.782  1.00 63.57           C  
ANISOU 1151  CA  HIS A 231     6664  11531   5959    788    132  -2088       C  
ATOM   1152  C   HIS A 231     -34.160  21.777  33.390  1.00 69.87           C  
ANISOU 1152  C   HIS A 231     7332  12615   6603    862    204  -2182       C  
ATOM   1153  O   HIS A 231     -35.090  21.056  33.034  1.00 70.14           O  
ANISOU 1153  O   HIS A 231     7354  12680   6617    789    299  -1991       O  
ATOM   1154  CB  HIS A 231     -31.921  20.644  33.681  1.00 65.33           C  
ANISOU 1154  CB  HIS A 231     6895  11951   5978    766    143  -1943       C  
ATOM   1155  CG  HIS A 231     -30.582  20.320  33.079  1.00 67.35           C  
ANISOU 1155  CG  HIS A 231     7270  11941   6377    696     79  -1837       C  
ATOM   1156  ND1 HIS A 231     -29.447  20.203  33.863  1.00 70.09           N  
ANISOU 1156  ND1 HIS A 231     7621  12392   6618    727     20  -1864       N  
ATOM   1157  CD2 HIS A 231     -30.231  20.154  31.782  1.00 66.48           C  
ANISOU 1157  CD2 HIS A 231     7268  11492   6499    607     64  -1724       C  
ATOM   1158  CE1 HIS A 231     -28.458  19.944  33.025  1.00 67.31           C  
ANISOU 1158  CE1 HIS A 231     7376  11757   6441    654    -25  -1757       C  
ATOM   1159  NE2 HIS A 231     -28.881  19.912  31.765  1.00 65.83           N  
ANISOU 1159  NE2 HIS A 231     7252  11307   6455    585      2  -1675       N  
ATOM   1160  N   SER A 232     -34.314  22.821  34.236  1.00 66.62           N  
ANISOU 1160  N   SER A 232     6816  12397   6100   1010    150  -2487       N  
ATOM   1161  CA  SER A 232     -35.603  23.184  34.821  1.00 68.01           C  
ANISOU 1161  CA  SER A 232     6851  12862   6129   1107    211  -2622       C  
ATOM   1162  C   SER A 232     -36.552  23.677  33.731  1.00 71.29           C  
ANISOU 1162  C   SER A 232     7274  13040   6773   1089    221  -2659       C  
ATOM   1163  O   SER A 232     -37.708  23.251  33.682  1.00 70.56           O  
ANISOU 1163  O   SER A 232     7115  13095   6598   1068    323  -2553       O  
ATOM   1164  CB  SER A 232     -35.428  24.247  35.901  1.00 72.98           C  
ANISOU 1164  CB  SER A 232     7371  13720   6637   1285    128  -2982       C  
ATOM   1165  OG  SER A 232     -34.826  23.686  37.054  1.00 80.62           O  
ANISOU 1165  OG  SER A 232     8299  15007   7327   1310    141  -2931       O  
ATOM   1166  N   TYR A 233     -36.034  24.534  32.830  1.00 67.70           N  
ANISOU 1166  N   TYR A 233     6897  12217   6609   1087    113  -2781       N  
ATOM   1167  CA  TYR A 233     -36.752  25.102  31.694  1.00 66.46           C  
ANISOU 1167  CA  TYR A 233     6758  11793   6702   1068     99  -2811       C  
ATOM   1168  C   TYR A 233     -37.285  23.991  30.775  1.00 69.20           C  
ANISOU 1168  C   TYR A 233     7171  12041   7080    919    205  -2487       C  
ATOM   1169  O   TYR A 233     -38.469  24.014  30.439  1.00 69.02           O  
ANISOU 1169  O   TYR A 233     7095  12048   7082    918    263  -2470       O  
ATOM   1170  CB  TYR A 233     -35.820  26.055  30.919  1.00 66.42           C  
ANISOU 1170  CB  TYR A 233     6827  11416   6993   1069    -43  -2935       C  
ATOM   1171  CG  TYR A 233     -36.510  26.870  29.847  1.00 67.34           C  
ANISOU 1171  CG  TYR A 233     6939  11270   7375   1071    -83  -2999       C  
ATOM   1172  CD1 TYR A 233     -37.086  28.102  30.142  1.00 70.73           C  
ANISOU 1172  CD1 TYR A 233     7267  11711   7898   1209   -163  -3299       C  
ATOM   1173  CD2 TYR A 233     -36.567  26.421  28.530  1.00 65.86           C  
ANISOU 1173  CD2 TYR A 233     6846  10826   7353    942    -52  -2765       C  
ATOM   1174  CE1 TYR A 233     -37.715  28.861  29.158  1.00 71.43           C  
ANISOU 1174  CE1 TYR A 233     7345  11550   8244   1211   -209  -3343       C  
ATOM   1175  CE2 TYR A 233     -37.193  27.171  27.536  1.00 66.22           C  
ANISOU 1175  CE2 TYR A 233     6880  10645   7634    944    -93  -2808       C  
ATOM   1176  CZ  TYR A 233     -37.759  28.394  27.853  1.00 77.21           C  
ANISOU 1176  CZ  TYR A 233     8170  12040   9125   1074   -172  -3087       C  
ATOM   1177  OH  TYR A 233     -38.377  29.134  26.877  1.00 79.64           O  
ANISOU 1177  OH  TYR A 233     8461  12121   9677   1076   -220  -3114       O  
ATOM   1178  N   ILE A 234     -36.423  23.016  30.385  1.00 64.64           N  
ANISOU 1178  N   ILE A 234     6705  11349   6507    799    221  -2243       N  
ATOM   1179  CA  ILE A 234     -36.801  21.895  29.491  1.00 62.35           C  
ANISOU 1179  CA  ILE A 234     6485  10942   6263    659    300  -1948       C  
ATOM   1180  C   ILE A 234     -37.865  21.003  30.167  1.00 66.26           C  
ANISOU 1180  C   ILE A 234     6889  11747   6539    635    417  -1800       C  
ATOM   1181  O   ILE A 234     -38.818  20.586  29.504  1.00 64.48           O  
ANISOU 1181  O   ILE A 234     6656  11470   6372    568    477  -1669       O  
ATOM   1182  CB  ILE A 234     -35.559  21.077  29.040  1.00 63.31           C  
ANISOU 1182  CB  ILE A 234     6733  10879   6441    560    276  -1759       C  
ATOM   1183  CG1 ILE A 234     -34.642  21.937  28.146  1.00 61.92           C  
ANISOU 1183  CG1 ILE A 234     6635  10385   6507    565    170  -1864       C  
ATOM   1184  CG2 ILE A 234     -35.959  19.760  28.324  1.00 63.17           C  
ANISOU 1184  CG2 ILE A 234     6774  10788   6440    428    351  -1466       C  
ATOM   1185  CD1 ILE A 234     -33.194  21.381  27.892  1.00 61.80           C  
ANISOU 1185  CD1 ILE A 234     6722  10231   6529    506    126  -1746       C  
ATOM   1186  N   ALA A 235     -37.698  20.738  31.480  1.00 64.17           N  
ANISOU 1186  N   ALA A 235     6546  11813   6023    690    445  -1816       N  
ATOM   1187  CA  ALA A 235     -38.597  19.922  32.300  1.00 65.62           C  
ANISOU 1187  CA  ALA A 235     6617  12345   5970    673    552  -1658       C  
ATOM   1188  C   ALA A 235     -40.001  20.489  32.324  1.00 71.47           C  
ANISOU 1188  C   ALA A 235     7235  13231   6688    739    604  -1779       C  
ATOM   1189  O   ALA A 235     -40.944  19.731  32.124  1.00 71.25           O  
ANISOU 1189  O   ALA A 235     7163  13280   6629    658    689  -1576       O  
ATOM   1190  CB  ALA A 235     -38.065  19.806  33.726  1.00 68.04           C  
ANISOU 1190  CB  ALA A 235     6847  13000   6005    747    555  -1698       C  
ATOM   1191  N   ALA A 236     -40.146  21.813  32.562  1.00 69.65           N  
ANISOU 1191  N   ALA A 236     6944  13027   6491    886    543  -2111       N  
ATOM   1192  CA  ALA A 236     -41.449  22.482  32.628  1.00 70.70           C  
ANISOU 1192  CA  ALA A 236     6950  13299   6613    977    579  -2272       C  
ATOM   1193  C   ALA A 236     -42.124  22.505  31.265  1.00 73.21           C  
ANISOU 1193  C   ALA A 236     7325  13311   7179    893    585  -2183       C  
ATOM   1194  O   ALA A 236     -43.279  22.095  31.165  1.00 74.10           O  
ANISOU 1194  O   ALA A 236     7356  13557   7240    860    672  -2071       O  
ATOM   1195  CB  ALA A 236     -41.296  23.898  33.163  1.00 72.90           C  
ANISOU 1195  CB  ALA A 236     7162  13626   6910   1159    484  -2664       C  
ATOM   1196  N   PHE A 237     -41.400  22.949  30.216  1.00 67.23           N  
ANISOU 1196  N   PHE A 237     6699  12162   6683    854    494  -2217       N  
ATOM   1197  CA  PHE A 237     -41.927  23.022  28.854  1.00 65.39           C  
ANISOU 1197  CA  PHE A 237     6523  11636   6685    778    488  -2136       C  
ATOM   1198  C   PHE A 237     -42.250  21.639  28.285  1.00 67.53           C  
ANISOU 1198  C   PHE A 237     6850  11868   6942    618    569  -1807       C  
ATOM   1199  O   PHE A 237     -43.303  21.469  27.686  1.00 67.01           O  
ANISOU 1199  O   PHE A 237     6749  11771   6942    575    613  -1730       O  
ATOM   1200  CB  PHE A 237     -40.954  23.769  27.934  1.00 65.97           C  
ANISOU 1200  CB  PHE A 237     6710  11339   7016    773    370  -2226       C  
ATOM   1201  CG  PHE A 237     -41.334  25.211  27.719  1.00 68.53           C  
ANISOU 1201  CG  PHE A 237     6974  11556   7510    892    285  -2500       C  
ATOM   1202  CD1 PHE A 237     -42.381  25.552  26.867  1.00 71.47           C  
ANISOU 1202  CD1 PHE A 237     7314  11810   8029    883    295  -2494       C  
ATOM   1203  CD2 PHE A 237     -40.667  26.229  28.388  1.00 72.44           C  
ANISOU 1203  CD2 PHE A 237     7434  12063   8027   1015    184  -2766       C  
ATOM   1204  CE1 PHE A 237     -42.757  26.889  26.692  1.00 73.51           C  
ANISOU 1204  CE1 PHE A 237     7508  11960   8462    997    206  -2740       C  
ATOM   1205  CE2 PHE A 237     -41.054  27.566  28.227  1.00 76.53           C  
ANISOU 1205  CE2 PHE A 237     7886  12465   8729   1130     88  -3027       C  
ATOM   1206  CZ  PHE A 237     -42.090  27.887  27.372  1.00 74.37           C  
ANISOU 1206  CZ  PHE A 237     7582  12066   8609   1120    100  -3006       C  
ATOM   1207  N   GLY A 238     -41.363  20.675  28.505  1.00 63.71           N  
ANISOU 1207  N   GLY A 238     6441  11385   6382    537    578  -1625       N  
ATOM   1208  CA  GLY A 238     -41.511  19.300  28.039  1.00 62.71           C  
ANISOU 1208  CA  GLY A 238     6368  11200   6258    389    632  -1320       C  
ATOM   1209  C   GLY A 238     -42.628  18.521  28.703  1.00 67.98           C  
ANISOU 1209  C   GLY A 238     6912  12160   6756    351    733  -1160       C  
ATOM   1210  O   GLY A 238     -43.311  17.755  28.027  1.00 67.66           O  
ANISOU 1210  O   GLY A 238     6881  12029   6796    244    767   -972       O  
ATOM   1211  N   ALA A 239     -42.820  18.689  30.026  1.00 66.57           N  
ANISOU 1211  N   ALA A 239     6608  12347   6340    436    776  -1226       N  
ATOM   1212  CA  ALA A 239     -43.887  18.001  30.773  1.00 68.46           C  
ANISOU 1212  CA  ALA A 239     6699  12923   6389    407    878  -1061       C  
ATOM   1213  C   ALA A 239     -45.260  18.540  30.358  1.00 73.96           C  
ANISOU 1213  C   ALA A 239     7297  13661   7145    441    918  -1149       C  
ATOM   1214  O   ALA A 239     -46.174  17.747  30.125  1.00 74.92           O  
ANISOU 1214  O   ALA A 239     7360  13841   7266    342    981   -934       O  
ATOM   1215  CB  ALA A 239     -43.686  18.155  32.282  1.00 71.14           C  
ANISOU 1215  CB  ALA A 239     6919  13674   6439    508    911  -1131       C  
ATOM   1216  N   VAL A 240     -45.387  19.886  30.230  1.00 69.94           N  
ANISOU 1216  N   VAL A 240     6766  13099   6708    579    869  -1462       N  
ATOM   1217  CA  VAL A 240     -46.609  20.569  29.800  1.00 69.85           C  
ANISOU 1217  CA  VAL A 240     6663  13099   6778    634    889  -1584       C  
ATOM   1218  C   VAL A 240     -46.929  20.138  28.346  1.00 71.37           C  
ANISOU 1218  C   VAL A 240     6957  12948   7213    501    873  -1423       C  
ATOM   1219  O   VAL A 240     -48.069  19.748  28.090  1.00 71.36           O  
ANISOU 1219  O   VAL A 240     6873  13025   7214    447    934  -1302       O  
ATOM   1220  CB  VAL A 240     -46.508  22.113  29.972  1.00 74.22           C  
ANISOU 1220  CB  VAL A 240     7181  13627   7391    814    814  -1960       C  
ATOM   1221  CG1 VAL A 240     -47.647  22.842  29.261  1.00 73.86           C  
ANISOU 1221  CG1 VAL A 240     7074  13483   7505    859    808  -2076       C  
ATOM   1222  CG2 VAL A 240     -46.477  22.497  31.449  1.00 76.38           C  
ANISOU 1222  CG2 VAL A 240     7316  14309   7397    961    840  -2140       C  
ATOM   1223  N   THR A 241     -45.923  20.142  27.429  1.00 64.60           N  
ANISOU 1223  N   THR A 241     6266  11736   6542    446    792  -1410       N  
ATOM   1224  CA  THR A 241     -46.130  19.719  26.034  1.00 62.93           C  
ANISOU 1224  CA  THR A 241     6152  11217   6541    331    768  -1271       C  
ATOM   1225  C   THR A 241     -46.519  18.227  25.966  1.00 67.45           C  
ANISOU 1225  C   THR A 241     6723  11840   7066    181    828   -965       C  
ATOM   1226  O   THR A 241     -47.383  17.880  25.171  1.00 67.96           O  
ANISOU 1226  O   THR A 241     6771  11817   7233    107    844   -864       O  
ATOM   1227  CB  THR A 241     -44.917  20.024  25.133  1.00 66.60           C  
ANISOU 1227  CB  THR A 241     6777  11346   7183    313    674  -1316       C  
ATOM   1228  OG1 THR A 241     -44.528  21.388  25.311  1.00 68.05           O  
ANISOU 1228  OG1 THR A 241     6947  11489   7422    445    607  -1583       O  
ATOM   1229  CG2 THR A 241     -45.210  19.786  23.657  1.00 58.42           C  
ANISOU 1229  CG2 THR A 241     5820  10027   6351    224    646  -1218       C  
ATOM   1230  N   GLY A 242     -45.923  17.385  26.808  1.00 63.21           N  
ANISOU 1230  N   GLY A 242     6191  11445   6382    139    852   -821       N  
ATOM   1231  CA  GLY A 242     -46.254  15.965  26.864  1.00 63.05           C  
ANISOU 1231  CA  GLY A 242     6153  11472   6329     -2    894   -519       C  
ATOM   1232  C   GLY A 242     -47.698  15.731  27.279  1.00 69.21           C  
ANISOU 1232  C   GLY A 242     6763  12516   7017    -24    977   -421       C  
ATOM   1233  O   GLY A 242     -48.441  15.041  26.578  1.00 68.57           O  
ANISOU 1233  O   GLY A 242     6674  12329   7049   -136    984   -252       O  
ATOM   1234  N   LEU A 243     -48.119  16.367  28.390  1.00 67.61           N  
ANISOU 1234  N   LEU A 243     6414  12663   6611     92   1035   -545       N  
ATOM   1235  CA  LEU A 243     -49.471  16.249  28.958  1.00 69.03           C  
ANISOU 1235  CA  LEU A 243     6401  13165   6662     94   1125   -468       C  
ATOM   1236  C   LEU A 243     -50.561  16.824  28.048  1.00 70.87           C  
ANISOU 1236  C   LEU A 243     6596  13284   7049    108   1126   -567       C  
ATOM   1237  O   LEU A 243     -51.609  16.200  27.916  1.00 71.17           O  
ANISOU 1237  O   LEU A 243     6532  13415   7093     21   1177   -386       O  
ATOM   1238  CB  LEU A 243     -49.546  16.905  30.339  1.00 71.05           C  
ANISOU 1238  CB  LEU A 243     6508  13842   6648    242   1181   -620       C  
ATOM   1239  CG  LEU A 243     -48.886  16.122  31.472  1.00 77.26           C  
ANISOU 1239  CG  LEU A 243     7256  14885   7213    213   1213   -442       C  
ATOM   1240  CD1 LEU A 243     -48.668  17.004  32.680  1.00 79.23           C  
ANISOU 1240  CD1 LEU A 243     7401  15486   7217    393   1234   -686       C  
ATOM   1241  CD2 LEU A 243     -49.709  14.892  31.864  1.00 80.86           C  
ANISOU 1241  CD2 LEU A 243     7578  15569   7577     77   1292    -86       C  
ATOM   1242  N   CYS A 244     -50.313  17.985  27.419  1.00 65.77           N  
ANISOU 1242  N   CYS A 244     6021  12432   6536    212   1062   -836       N  
ATOM   1243  CA  CYS A 244     -51.237  18.644  26.498  1.00 65.25           C  
ANISOU 1243  CA  CYS A 244     5929  12231   6633    237   1047   -944       C  
ATOM   1244  C   CYS A 244     -51.436  17.816  25.223  1.00 69.40           C  
ANISOU 1244  C   CYS A 244     6552  12459   7357     79   1014   -746       C  
ATOM   1245  O   CYS A 244     -52.573  17.646  24.782  1.00 69.71           O  
ANISOU 1245  O   CYS A 244     6508  12523   7456     34   1042   -676       O  
ATOM   1246  CB  CYS A 244     -50.754  20.052  26.171  1.00 64.88           C  
ANISOU 1246  CB  CYS A 244     5937  12019   6695    379    969  -1254       C  
ATOM   1247  SG  CYS A 244     -50.936  21.226  27.535  1.00 71.18           S  
ANISOU 1247  SG  CYS A 244     6578  13169   7299    595    992  -1559       S  
ATOM   1248  N   THR A 245     -50.338  17.298  24.635  1.00 65.25           N  
ANISOU 1248  N   THR A 245     6195  11664   6932      3    951   -666       N  
ATOM   1249  CA  THR A 245     -50.410  16.489  23.417  1.00 63.70           C  
ANISOU 1249  CA  THR A 245     6097  11188   6917   -132    907   -506       C  
ATOM   1250  C   THR A 245     -51.036  15.133  23.721  1.00 69.09           C  
ANISOU 1250  C   THR A 245     6708  11987   7558   -270    951   -226       C  
ATOM   1251  O   THR A 245     -51.829  14.662  22.908  1.00 69.99           O  
ANISOU 1251  O   THR A 245     6808  11987   7799   -359    937   -125       O  
ATOM   1252  CB  THR A 245     -49.037  16.339  22.739  1.00 66.59           C  
ANISOU 1252  CB  THR A 245     6647  11265   7387   -157    828   -517       C  
ATOM   1253  OG1 THR A 245     -48.086  15.834  23.683  1.00 63.70           O  
ANISOU 1253  OG1 THR A 245     6309  11006   6889   -158    839   -452       O  
ATOM   1254  CG2 THR A 245     -48.553  17.644  22.100  1.00 61.01           C  
ANISOU 1254  CG2 THR A 245     6010  10380   6792    -53    766   -750       C  
ATOM   1255  N   LEU A 246     -50.710  14.523  24.887  1.00 65.79           N  
ANISOU 1255  N   LEU A 246     6233  11796   6968   -290    997    -94       N  
ATOM   1256  CA  LEU A 246     -51.266  13.228  25.316  1.00 67.06           C  
ANISOU 1256  CA  LEU A 246     6305  12085   7091   -427   1033    206       C  
ATOM   1257  C   LEU A 246     -52.777  13.338  25.523  1.00 74.05           C  
ANISOU 1257  C   LEU A 246     7002  13201   7933   -437   1103    256       C  
ATOM   1258  O   LEU A 246     -53.496  12.378  25.239  1.00 75.78           O  
ANISOU 1258  O   LEU A 246     7167  13387   8240   -574   1101    482       O  
ATOM   1259  CB  LEU A 246     -50.582  12.701  26.596  1.00 68.06           C  
ANISOU 1259  CB  LEU A 246     6392  12444   7024   -429   1067    335       C  
ATOM   1260  CG  LEU A 246     -51.018  11.327  27.118  1.00 73.77           C  
ANISOU 1260  CG  LEU A 246     7018  13294   7718   -579   1092    685       C  
ATOM   1261  CD1 LEU A 246     -50.756  10.220  26.103  1.00 72.91           C  
ANISOU 1261  CD1 LEU A 246     7035  12821   7845   -725   1001    854       C  
ATOM   1262  CD2 LEU A 246     -50.353  11.009  28.437  1.00 76.46           C  
ANISOU 1262  CD2 LEU A 246     7298  13917   7835   -555   1133    791       C  
ATOM   1263  N   PHE A 247     -53.260  14.508  25.979  1.00 70.33           N  
ANISOU 1263  N   PHE A 247     6427  12951   7344   -291   1155     39       N  
ATOM   1264  CA  PHE A 247     -54.687  14.735  26.160  1.00 71.34           C  
ANISOU 1264  CA  PHE A 247     6367  13312   7425   -276   1224     53       C  
ATOM   1265  C   PHE A 247     -55.378  14.783  24.798  1.00 74.05           C  
ANISOU 1265  C   PHE A 247     6756  13379   8001   -334   1172     35       C  
ATOM   1266  O   PHE A 247     -56.445  14.190  24.637  1.00 75.40           O  
ANISOU 1266  O   PHE A 247     6812  13626   8212   -429   1201    204       O  
ATOM   1267  CB  PHE A 247     -54.969  16.024  26.961  1.00 73.92           C  
ANISOU 1267  CB  PHE A 247     6577  13930   7581    -81   1278   -216       C  
ATOM   1268  CG  PHE A 247     -56.439  16.393  27.013  1.00 76.42           C  
ANISOU 1268  CG  PHE A 247     6703  14466   7867    -41   1343   -247       C  
ATOM   1269  CD1 PHE A 247     -56.945  17.422  26.223  1.00 78.34           C  
ANISOU 1269  CD1 PHE A 247     6954  14564   8246     55   1307   -481       C  
ATOM   1270  CD2 PHE A 247     -57.326  15.674  27.808  1.00 79.90           C  
ANISOU 1270  CD2 PHE A 247     6947  15257   8156   -105   1434    -21       C  
ATOM   1271  CE1 PHE A 247     -58.306  17.748  26.255  1.00 80.37           C  
ANISOU 1271  CE1 PHE A 247     7031  15023   8484     96   1364   -510       C  
ATOM   1272  CE2 PHE A 247     -58.688  15.996  27.831  1.00 83.92           C  
ANISOU 1272  CE2 PHE A 247     7269  15979   8639    -68   1496    -44       C  
ATOM   1273  CZ  PHE A 247     -59.167  17.031  27.059  1.00 81.15           C  
ANISOU 1273  CZ  PHE A 247     6933  15478   8421     37   1460   -297       C  
ATOM   1274  N   THR A 248     -54.771  15.498  23.835  1.00 67.26           N  
ANISOU 1274  N   THR A 248     6051  12215   7289   -279   1095   -159       N  
ATOM   1275  CA  THR A 248     -55.295  15.672  22.485  1.00 65.50           C  
ANISOU 1275  CA  THR A 248     5883  11730   7275   -316   1036   -198       C  
ATOM   1276  C   THR A 248     -55.254  14.330  21.735  1.00 69.63           C  
ANISOU 1276  C   THR A 248     6481  12039   7935   -494    985     39       C  
ATOM   1277  O   THR A 248     -56.215  14.019  21.036  1.00 69.29           O  
ANISOU 1277  O   THR A 248     6386  11934   8005   -569    969    115       O  
ATOM   1278  CB  THR A 248     -54.542  16.798  21.792  1.00 68.27           C  
ANISOU 1278  CB  THR A 248     6364  11853   7723   -206    968   -444       C  
ATOM   1279  OG1 THR A 248     -54.681  17.962  22.603  1.00 68.32           O  
ANISOU 1279  OG1 THR A 248     6278  12065   7617    -43   1005   -661       O  
ATOM   1280  CG2 THR A 248     -55.076  17.103  20.401  1.00 64.64           C  
ANISOU 1280  CG2 THR A 248     5949  11150   7462   -230    907   -488       C  
ATOM   1281  N   LEU A 249     -54.180  13.523  21.905  1.00 66.43           N  
ANISOU 1281  N   LEU A 249     6188  11528   7525   -557    951    149       N  
ATOM   1282  CA  LEU A 249     -54.102  12.191  21.287  1.00 65.68           C  
ANISOU 1282  CA  LEU A 249     6158  11229   7570   -715    888    362       C  
ATOM   1283  C   LEU A 249     -55.211  11.290  21.858  1.00 72.78           C  
ANISOU 1283  C   LEU A 249     6886  12324   8445   -832    933    610       C  
ATOM   1284  O   LEU A 249     -55.888  10.598  21.089  1.00 72.88           O  
ANISOU 1284  O   LEU A 249     6885  12191   8617   -946    882    726       O  
ATOM   1285  CB  LEU A 249     -52.733  11.526  21.503  1.00 64.55           C  
ANISOU 1285  CB  LEU A 249     6148  10961   7417   -743    845    428       C  
ATOM   1286  CG  LEU A 249     -51.497  12.187  20.907  1.00 66.76           C  
ANISOU 1286  CG  LEU A 249     6601  11024   7741   -657    790    234       C  
ATOM   1287  CD1 LEU A 249     -50.245  11.507  21.411  1.00 66.06           C  
ANISOU 1287  CD1 LEU A 249     6604  10888   7607   -679    766    319       C  
ATOM   1288  CD2 LEU A 249     -51.543  12.206  19.380  1.00 66.70           C  
ANISOU 1288  CD2 LEU A 249     6696  10722   7924   -687    708    169       C  
ATOM   1289  N   ALA A 250     -55.410  11.328  23.200  1.00 70.59           N  
ANISOU 1289  N   ALA A 250     6467  12391   7965   -801   1024    689       N  
ATOM   1290  CA  ALA A 250     -56.437  10.539  23.889  1.00 73.15           C  
ANISOU 1290  CA  ALA A 250     6598  12960   8234   -907   1079    950       C  
ATOM   1291  C   ALA A 250     -57.854  10.895  23.386  1.00 77.39           C  
ANISOU 1291  C   ALA A 250     7004  13566   8835   -916   1105    923       C  
ATOM   1292  O   ALA A 250     -58.628   9.989  23.093  1.00 78.21           O  
ANISOU 1292  O   ALA A 250     7025  13641   9053  -1060   1082   1142       O  
ATOM   1293  CB  ALA A 250     -56.342  10.734  25.399  1.00 75.62           C  
ANISOU 1293  CB  ALA A 250     6778  13674   8281   -840   1180   1002       C  
ATOM   1294  N   THR A 251     -58.157  12.199  23.229  1.00 72.74           N  
ANISOU 1294  N   THR A 251     6398  13043   8198   -765   1138    656       N  
ATOM   1295  CA  THR A 251     -59.441  12.717  22.757  1.00 73.27           C  
ANISOU 1295  CA  THR A 251     6341  13178   8319   -745   1161    595       C  
ATOM   1296  C   THR A 251     -59.749  12.238  21.324  1.00 76.85           C  
ANISOU 1296  C   THR A 251     6888  13289   9024   -855   1060    636       C  
ATOM   1297  O   THR A 251     -60.900  11.885  21.032  1.00 78.19           O  
ANISOU 1297  O   THR A 251     6932  13508   9271   -940   1063    754       O  
ATOM   1298  CB  THR A 251     -59.466  14.244  22.865  1.00 78.35           C  
ANISOU 1298  CB  THR A 251     6968  13921   8881   -545   1196    283       C  
ATOM   1299  OG1 THR A 251     -59.194  14.603  24.222  1.00 79.77           O  
ANISOU 1299  OG1 THR A 251     7058  14430   8822   -440   1278    234       O  
ATOM   1300  CG2 THR A 251     -60.806  14.835  22.450  1.00 76.38           C  
ANISOU 1300  CG2 THR A 251     6573  13766   8680   -508   1222    215       C  
ATOM   1301  N   PHE A 252     -58.731  12.227  20.448  1.00 70.22           N  
ANISOU 1301  N   PHE A 252     6255  12125   8302   -852    970    536       N  
ATOM   1302  CA  PHE A 252     -58.868  11.777  19.062  1.00 68.69           C  
ANISOU 1302  CA  PHE A 252     6161  11615   8324   -938    866    547       C  
ATOM   1303  C   PHE A 252     -59.112  10.263  18.993  1.00 76.09           C  
ANISOU 1303  C   PHE A 252     7072  12467   9374  -1123    813    816       C  
ATOM   1304  O   PHE A 252     -59.944   9.835  18.196  1.00 76.43           O  
ANISOU 1304  O   PHE A 252     7075  12398   9567  -1212    756    875       O  
ATOM   1305  CB  PHE A 252     -57.620  12.146  18.235  1.00 67.27           C  
ANISOU 1305  CB  PHE A 252     6194  11156   8209   -877    791    379       C  
ATOM   1306  CG  PHE A 252     -57.665  13.460  17.488  1.00 66.64           C  
ANISOU 1306  CG  PHE A 252     6157  10999   8163   -751    776    141       C  
ATOM   1307  CD1 PHE A 252     -57.068  14.600  18.015  1.00 68.70           C  
ANISOU 1307  CD1 PHE A 252     6439  11344   8319   -603    815    -42       C  
ATOM   1308  CD2 PHE A 252     -58.252  13.546  16.231  1.00 68.02           C  
ANISOU 1308  CD2 PHE A 252     6353  11005   8488   -781    709    104       C  
ATOM   1309  CE1 PHE A 252     -57.088  15.812  17.315  1.00 68.34           C  
ANISOU 1309  CE1 PHE A 252     6427  11202   8336   -494    785   -243       C  
ATOM   1310  CE2 PHE A 252     -58.268  14.759  15.527  1.00 69.66           C  
ANISOU 1310  CE2 PHE A 252     6594  11139   8736   -669    688    -89       C  
ATOM   1311  CZ  PHE A 252     -57.690  15.886  16.076  1.00 67.02           C  
ANISOU 1311  CZ  PHE A 252     6275  10875   8315   -529    724   -253       C  
ATOM   1312  N   VAL A 253     -58.399   9.460  19.826  1.00 74.41           N  
ANISOU 1312  N   VAL A 253     6873  12298   9100  -1180    820    979       N  
ATOM   1313  CA  VAL A 253     -58.520   7.993  19.848  1.00 75.51           C  
ANISOU 1313  CA  VAL A 253     6986  12333   9371  -1356    753   1249       C  
ATOM   1314  C   VAL A 253     -59.819   7.562  20.561  1.00 82.92           C  
ANISOU 1314  C   VAL A 253     7688  13537  10280  -1453    814   1480       C  
ATOM   1315  O   VAL A 253     -60.311   6.458  20.309  1.00 83.83           O  
ANISOU 1315  O   VAL A 253     7748  13538  10563  -1612    740   1694       O  
ATOM   1316  CB  VAL A 253     -57.272   7.246  20.411  1.00 79.07           C  
ANISOU 1316  CB  VAL A 253     7536  12709   9798  -1388    723   1360       C  
ATOM   1317  CG1 VAL A 253     -55.999   7.631  19.660  1.00 76.24           C  
ANISOU 1317  CG1 VAL A 253     7399  12087   9482  -1301    659   1146       C  
ATOM   1318  CG2 VAL A 253     -57.100   7.443  21.913  1.00 80.33           C  
ANISOU 1318  CG2 VAL A 253     7587  13215   9721  -1341    836   1454       C  
ATOM   1319  N   ALA A 254     -60.369   8.432  21.434  1.00 80.96           N  
ANISOU 1319  N   ALA A 254     7292  13642   9827  -1355    940   1433       N  
ATOM   1320  CA  ALA A 254     -61.623   8.171  22.141  1.00 83.36           C  
ANISOU 1320  CA  ALA A 254     7350  14256  10069  -1425   1015   1638       C  
ATOM   1321  C   ALA A 254     -62.811   8.273  21.164  1.00 87.44           C  
ANISOU 1321  C   ALA A 254     7796  14683  10745  -1472    977   1606       C  
ATOM   1322  O   ALA A 254     -63.773   7.526  21.300  1.00 88.27           O  
ANISOU 1322  O   ALA A 254     7733  14885  10920  -1606    976   1840       O  
ATOM   1323  CB  ALA A 254     -61.792   9.150  23.296  1.00 85.01           C  
ANISOU 1323  CB  ALA A 254     7426  14878   9996  -1276   1157   1546       C  
ATOM   1324  N   ASP A 255     -62.706   9.160  20.153  1.00 82.95           N  
ANISOU 1324  N   ASP A 255     7351  13924  10241  -1369    938   1331       N  
ATOM   1325  CA  ASP A 255     -63.722   9.386  19.127  1.00 83.09           C  
ANISOU 1325  CA  ASP A 255     7324  13842  10403  -1392    892   1265       C  
ATOM   1326  C   ASP A 255     -63.162   9.073  17.721  1.00 87.44           C  
ANISOU 1326  C   ASP A 255     8078  13986  11157  -1427    752   1159       C  
ATOM   1327  O   ASP A 255     -63.596   9.682  16.747  1.00 86.02           O  
ANISOU 1327  O   ASP A 255     7927  13702  11056  -1378    714   1000       O  
ATOM   1328  CB  ASP A 255     -64.211  10.851  19.216  1.00 84.47           C  
ANISOU 1328  CB  ASP A 255     7428  14214  10451  -1214    979   1030       C  
ATOM   1329  CG  ASP A 255     -65.434  11.187  18.370  1.00 94.55           C  
ANISOU 1329  CG  ASP A 255     8611  15470  11844  -1223    954    979       C  
ATOM   1330  OD1 ASP A 255     -65.456  12.288  17.770  1.00 94.53           O  
ANISOU 1330  OD1 ASP A 255     8666  15400  11851  -1090    945    739       O  
ATOM   1331  OD2 ASP A 255     -66.357  10.333  18.281  1.00 97.15           O  
ANISOU 1331  OD2 ASP A 255     8804  15839  12269  -1368    934   1189       O  
ATOM   1332  N   TRP A 256     -62.248   8.082  17.609  1.00 86.49           N  
ANISOU 1332  N   TRP A 256     8086  13653  11125  -1513    670   1257       N  
ATOM   1333  CA  TRP A 256     -61.532   7.733  16.370  1.00 85.87           C  
ANISOU 1333  CA  TRP A 256     8202  13214  11210  -1531    539   1146       C  
ATOM   1334  C   TRP A 256     -62.402   7.557  15.108  1.00 91.01           C  
ANISOU 1334  C   TRP A 256     8837  13697  12045  -1593    440   1105       C  
ATOM   1335  O   TRP A 256     -61.966   7.986  14.043  1.00 89.01           O  
ANISOU 1335  O   TRP A 256     8724  13250  11846  -1528    374    915       O  
ATOM   1336  CB  TRP A 256     -60.643   6.498  16.543  1.00 85.28           C  
ANISOU 1336  CB  TRP A 256     8216  12963  11222  -1631    460   1296       C  
ATOM   1337  CG  TRP A 256     -59.645   6.352  15.429  1.00 84.96           C  
ANISOU 1337  CG  TRP A 256     8386  12606  11290  -1598    348   1133       C  
ATOM   1338  CD1 TRP A 256     -59.624   5.378  14.474  1.00 88.10           C  
ANISOU 1338  CD1 TRP A 256     8846  12731  11896  -1693    204   1156       C  
ATOM   1339  CD2 TRP A 256     -58.592   7.274  15.086  1.00 82.82           C  
ANISOU 1339  CD2 TRP A 256     8273  12273  10922  -1451    367    907       C  
ATOM   1340  NE1 TRP A 256     -58.592   5.604  13.590  1.00 86.03           N  
ANISOU 1340  NE1 TRP A 256     8770  12266  11651  -1608    141    960       N  
ATOM   1341  CE2 TRP A 256     -57.950   6.767  13.936  1.00 85.98           C  
ANISOU 1341  CE2 TRP A 256     8822  12383  11462  -1466    242    819       C  
ATOM   1342  CE3 TRP A 256     -58.119   8.473  15.650  1.00 83.07           C  
ANISOU 1342  CE3 TRP A 256     8325  12467  10769  -1308    471    769       C  
ATOM   1343  CZ2 TRP A 256     -56.868   7.421  13.333  1.00 83.46           C  
ANISOU 1343  CZ2 TRP A 256     8664  11953  11094  -1349    229    623       C  
ATOM   1344  CZ3 TRP A 256     -57.057   9.126  15.046  1.00 82.67           C  
ANISOU 1344  CZ3 TRP A 256     8439  12277  10696  -1201    446    577       C  
ATOM   1345  CH2 TRP A 256     -56.438   8.598  13.906  1.00 82.35           C  
ANISOU 1345  CH2 TRP A 256     8537  11967  10785  -1225    332    517       C  
ATOM   1346  N   ARG A 257     -63.600   6.949  15.211  1.00 89.90           N  
ANISOU 1346  N   ARG A 257     8522  13640  11994  -1717    428   1285       N  
ATOM   1347  CA  ARG A 257     -64.482   6.744  14.055  1.00 89.62           C  
ANISOU 1347  CA  ARG A 257     8455  13459  12135  -1783    328   1252       C  
ATOM   1348  C   ARG A 257     -64.965   8.077  13.469  1.00 92.06           C  
ANISOU 1348  C   ARG A 257     8757  13844  12376  -1647    373   1035       C  
ATOM   1349  O   ARG A 257     -65.064   8.201  12.246  1.00 91.25           O  
ANISOU 1349  O   ARG A 257     8731  13557  12384  -1639    277    907       O  
ATOM   1350  CB  ARG A 257     -65.683   5.872  14.436  1.00 92.75           C  
ANISOU 1350  CB  ARG A 257     8642  13960  12638  -1947    314   1509       C  
ATOM   1351  N   ASN A 258     -65.231   9.077  14.339  1.00 87.73           N  
ANISOU 1351  N   ASN A 258     8116  13570  11649  -1535    510    988       N  
ATOM   1352  CA  ASN A 258     -65.718  10.398  13.943  1.00 86.18           C  
ANISOU 1352  CA  ASN A 258     7890  13459  11396  -1397    554    792       C  
ATOM   1353  C   ASN A 258     -64.602  11.437  13.820  1.00 86.28           C  
ANISOU 1353  C   ASN A 258     8065  13406  11313  -1235    576    572       C  
ATOM   1354  O   ASN A 258     -64.768  12.410  13.082  1.00 84.11           O  
ANISOU 1354  O   ASN A 258     7821  13078  11058  -1136    557    402       O  
ATOM   1355  CB  ASN A 258     -66.760  10.895  14.937  1.00 89.88           C  
ANISOU 1355  CB  ASN A 258     8136  14268  11746  -1360    679    854       C  
ATOM   1356  CG  ASN A 258     -67.692  11.923  14.350  1.00116.65           C  
ANISOU 1356  CG  ASN A 258    11445  17722  15155  -1267    690    707       C  
ATOM   1357  OD1 ASN A 258     -68.742  11.591  13.789  1.00114.12           O  
ANISOU 1357  OD1 ASN A 258    11019  17387  14952  -1351    642    778       O  
ATOM   1358  ND2 ASN A 258     -67.318  13.193  14.448  1.00106.28           N  
ANISOU 1358  ND2 ASN A 258    10173  16468  13741  -1091    743    498       N  
ATOM   1359  N   SER A 259     -63.489  11.246  14.551  1.00 82.09           N  
ANISOU 1359  N   SER A 259     7624  12880  10687  -1212    609    589       N  
ATOM   1360  CA  SER A 259     -62.358  12.170  14.573  1.00 79.86           C  
ANISOU 1360  CA  SER A 259     7484  12544  10315  -1070    629    402       C  
ATOM   1361  C   SER A 259     -61.400  11.930  13.425  1.00 81.33           C  
ANISOU 1361  C   SER A 259     7867  12430  10603  -1079    519    321       C  
ATOM   1362  O   SER A 259     -60.784  12.893  12.950  1.00 79.92           O  
ANISOU 1362  O   SER A 259     7786  12176  10402   -964    511    150       O  
ATOM   1363  CB  SER A 259     -61.608  12.074  15.894  1.00 84.66           C  
ANISOU 1363  CB  SER A 259     8089  13310  10767  -1040    710    456       C  
ATOM   1364  OG  SER A 259     -62.398  12.607  16.943  1.00 98.41           O  
ANISOU 1364  OG  SER A 259     9646  15373  12374   -987    821    477       O  
ATOM   1365  N   ASN A 260     -61.249  10.660  12.980  1.00 76.88           N  
ANISOU 1365  N   ASN A 260     7353  11698  10157  -1211    430    442       N  
ATOM   1366  CA  ASN A 260     -60.366  10.328  11.860  1.00 74.94           C  
ANISOU 1366  CA  ASN A 260     7281  11189  10001  -1213    321    356       C  
ATOM   1367  C   ASN A 260     -60.992  10.840  10.566  1.00 79.56           C  
ANISOU 1367  C   ASN A 260     7866  11691  10670  -1187    256    243       C  
ATOM   1368  O   ASN A 260     -61.646  10.099   9.821  1.00 80.45           O  
ANISOU 1368  O   ASN A 260     7950  11707  10909  -1282    166    291       O  
ATOM   1369  CB  ASN A 260     -60.068   8.838  11.793  1.00 73.20           C  
ANISOU 1369  CB  ASN A 260     7102  10818   9894  -1347    234    497       C  
ATOM   1370  CG  ASN A 260     -59.053   8.467  10.749  1.00 83.34           C  
ANISOU 1370  CG  ASN A 260     8559  11857  11250  -1330    127    392       C  
ATOM   1371  OD1 ASN A 260     -58.426   9.319  10.109  1.00 74.64           O  
ANISOU 1371  OD1 ASN A 260     7556  10708  10095  -1221    126    231       O  
ATOM   1372  ND2 ASN A 260     -58.861   7.174  10.568  1.00 74.66           N  
ANISOU 1372  ND2 ASN A 260     7488  10601  10279  -1437     29    485       N  
ATOM   1373  N   ARG A 261     -60.821  12.142  10.345  1.00 75.22           N  
ANISOU 1373  N   ARG A 261     7337  11189  10054  -1057    296     96       N  
ATOM   1374  CA  ARG A 261     -61.369  12.867   9.215  1.00 74.50           C  
ANISOU 1374  CA  ARG A 261     7236  11050  10021  -1009    247     -7       C  
ATOM   1375  C   ARG A 261     -60.494  14.051   8.892  1.00 75.21           C  
ANISOU 1375  C   ARG A 261     7421  11098  10055   -874    258   -153       C  
ATOM   1376  O   ARG A 261     -59.958  14.708   9.789  1.00 73.67           O  
ANISOU 1376  O   ARG A 261     7232  10988   9770   -794    334   -195       O  
ATOM   1377  CB  ARG A 261     -62.813  13.331   9.505  1.00 76.74           C  
ANISOU 1377  CB  ARG A 261     7337  11505  10314  -1009    295     23       C  
ATOM   1378  CG  ARG A 261     -63.852  12.737   8.562  1.00 95.48           C  
ANISOU 1378  CG  ARG A 261     9643  13821  12813  -1107    208     75       C  
ATOM   1379  CD  ARG A 261     -63.916  13.452   7.213  1.00111.27           C  
ANISOU 1379  CD  ARG A 261    11691  15724  14862  -1043    132    -47       C  
ATOM   1380  NE  ARG A 261     -64.088  12.505   6.106  1.00116.29           N  
ANISOU 1380  NE  ARG A 261    12369  16215  15602  -1135      7    -31       N  
ATOM   1381  CZ  ARG A 261     -63.085  11.953   5.428  1.00118.42           C  
ANISOU 1381  CZ  ARG A 261    12784  16326  15883  -1142    -71    -80       C  
ATOM   1382  NH1 ARG A 261     -61.827  12.254   5.727  1.00 86.87           N  
ANISOU 1382  NH1 ARG A 261     8907  12293  11805  -1069    -32   -129       N  
ATOM   1383  NH2 ARG A 261     -63.332  11.093   4.448  1.00107.43           N  
ANISOU 1383  NH2 ARG A 261    11412  14821  14586  -1215   -192    -89       N  
ATOM   1384  N   TYR A 262     -60.370  14.325   7.602  1.00 70.48           N  
ANISOU 1384  N   TYR A 262     6888  10378   9513   -850    176   -224       N  
ATOM   1385  CA  TYR A 262     -59.587  15.425   7.096  1.00 69.26           C  
ANISOU 1385  CA  TYR A 262     6812  10171   9332   -738    168   -332       C  
ATOM   1386  C   TYR A 262     -60.436  16.689   6.982  1.00 74.94           C  
ANISOU 1386  C   TYR A 262     7426  10973  10074   -654    189   -391       C  
ATOM   1387  O   TYR A 262     -61.627  16.590   6.690  1.00 76.17           O  
ANISOU 1387  O   TYR A 262     7474  11185  10283   -691    174   -360       O  
ATOM   1388  CB  TYR A 262     -58.970  15.038   5.753  1.00 69.70           C  
ANISOU 1388  CB  TYR A 262     6978  10083   9422   -753     69   -361       C  
ATOM   1389  CG  TYR A 262     -57.790  14.115   5.927  1.00 70.93           C  
ANISOU 1389  CG  TYR A 262     7255  10147   9548   -787     51   -344       C  
ATOM   1390  CD1 TYR A 262     -56.536  14.615   6.260  1.00 71.69           C  
ANISOU 1390  CD1 TYR A 262     7444  10215   9578   -716     84   -387       C  
ATOM   1391  CD2 TYR A 262     -57.936  12.736   5.814  1.00 72.40           C  
ANISOU 1391  CD2 TYR A 262     7454  10266   9787   -891     -5   -284       C  
ATOM   1392  CE1 TYR A 262     -55.448  13.768   6.454  1.00 72.17           C  
ANISOU 1392  CE1 TYR A 262     7611  10198   9614   -742     68   -371       C  
ATOM   1393  CE2 TYR A 262     -56.852  11.879   5.995  1.00 73.14           C  
ANISOU 1393  CE2 TYR A 262     7654  10265   9870   -915    -30   -272       C  
ATOM   1394  CZ  TYR A 262     -55.606  12.401   6.307  1.00 80.34           C  
ANISOU 1394  CZ  TYR A 262     8660  11164  10703   -837     11   -316       C  
ATOM   1395  OH  TYR A 262     -54.528  11.573   6.507  1.00 82.63           O  
ANISOU 1395  OH  TYR A 262     9048  11365  10982   -854    -13   -304       O  
ATOM   1396  N   PRO A 263     -59.869  17.884   7.255  1.00 72.40           N  
ANISOU 1396  N   PRO A 263     7125  10656   9729   -541    218   -477       N  
ATOM   1397  CA  PRO A 263     -58.462  18.172   7.585  1.00 71.49           C  
ANISOU 1397  CA  PRO A 263     7127  10476   9562   -489    231   -521       C  
ATOM   1398  C   PRO A 263     -58.141  18.077   9.083  1.00 74.15           C  
ANISOU 1398  C   PRO A 263     7443  10920   9811   -469    318   -528       C  
ATOM   1399  O   PRO A 263     -56.993  18.306   9.459  1.00 74.00           O  
ANISOU 1399  O   PRO A 263     7510  10858   9748   -422    329   -571       O  
ATOM   1400  CB  PRO A 263     -58.277  19.616   7.067  1.00 73.23           C  
ANISOU 1400  CB  PRO A 263     7342  10646   9836   -382    197   -603       C  
ATOM   1401  CG  PRO A 263     -59.635  20.075   6.529  1.00 78.41           C  
ANISOU 1401  CG  PRO A 263     7870  11355  10566   -368    177   -605       C  
ATOM   1402  CD  PRO A 263     -60.631  19.137   7.141  1.00 74.83           C  
ANISOU 1402  CD  PRO A 263     7330  11017  10086   -450    223   -543       C  
ATOM   1403  N   ALA A 264     -59.126  17.701   9.919  1.00 69.42           N  
ANISOU 1403  N   ALA A 264     6725  10473   9180   -506    378   -477       N  
ATOM   1404  CA  ALA A 264     -59.021  17.622  11.381  1.00 69.40           C  
ANISOU 1404  CA  ALA A 264     6669  10629   9071   -483    468   -472       C  
ATOM   1405  C   ALA A 264     -57.932  16.665  11.905  1.00 70.13           C  
ANISOU 1405  C   ALA A 264     6864  10686   9096   -544    479   -397       C  
ATOM   1406  O   ALA A 264     -57.206  17.044  12.823  1.00 70.24           O  
ANISOU 1406  O   ALA A 264     6897  10771   9021   -481    527   -445       O  
ATOM   1407  CB  ALA A 264     -60.366  17.223  11.976  1.00 71.78           C  
ANISOU 1407  CB  ALA A 264     6804  11119   9351   -526    524   -397       C  
ATOM   1408  N   VAL A 265     -57.848  15.434  11.361  1.00 63.60           N  
ANISOU 1408  N   VAL A 265     6095   9753   8318   -660    427   -288       N  
ATOM   1409  CA  VAL A 265     -56.917  14.372  11.766  1.00 61.57           C  
ANISOU 1409  CA  VAL A 265     5926   9440   8027   -728    420   -201       C  
ATOM   1410  C   VAL A 265     -55.411  14.770  11.531  1.00 63.63           C  
ANISOU 1410  C   VAL A 265     6337   9579   8260   -659    395   -289       C  
ATOM   1411  O   VAL A 265     -54.524  14.144  12.125  1.00 63.17           O  
ANISOU 1411  O   VAL A 265     6345   9506   8152   -682    406   -240       O  
ATOM   1412  CB  VAL A 265     -57.301  13.040  11.067  1.00 65.04           C  
ANISOU 1412  CB  VAL A 265     6379   9768   8567   -859    345    -89       C  
ATOM   1413  CG1 VAL A 265     -56.927  13.036   9.592  1.00 63.26           C  
ANISOU 1413  CG1 VAL A 265     6256   9358   8421   -851    246   -164       C  
ATOM   1414  CG2 VAL A 265     -56.730  11.824  11.788  1.00 65.41           C  
ANISOU 1414  CG2 VAL A 265     6459   9795   8600   -944    344     41       C  
ATOM   1415  N   ILE A 266     -55.127  15.818  10.712  1.00 57.97           N  
ANISOU 1415  N   ILE A 266     5662   8786   7580   -576    361   -402       N  
ATOM   1416  CA  ILE A 266     -53.750  16.304  10.489  1.00 55.84           C  
ANISOU 1416  CA  ILE A 266     5510   8416   7292   -511    338   -472       C  
ATOM   1417  C   ILE A 266     -53.192  16.777  11.848  1.00 59.61           C  
ANISOU 1417  C   ILE A 266     5975   9000   7675   -448    406   -514       C  
ATOM   1418  O   ILE A 266     -52.018  16.526  12.165  1.00 58.29           O  
ANISOU 1418  O   ILE A 266     5899   8785   7462   -441    403   -511       O  
ATOM   1419  CB  ILE A 266     -53.696  17.411   9.391  1.00 57.37           C  
ANISOU 1419  CB  ILE A 266     5716   8527   7553   -442    286   -553       C  
ATOM   1420  CG1 ILE A 266     -53.958  16.784   8.009  1.00 56.94           C  
ANISOU 1420  CG1 ILE A 266     5697   8378   7560   -502    211   -514       C  
ATOM   1421  CG2 ILE A 266     -52.347  18.175   9.400  1.00 57.00           C  
ANISOU 1421  CG2 ILE A 266     5753   8412   7493   -366    274   -620       C  
ATOM   1422  CD1 ILE A 266     -54.454  17.717   6.965  1.00 59.60           C  
ANISOU 1422  CD1 ILE A 266     5991   8693   7962   -459    166   -550       C  
ATOM   1423  N   LEU A 267     -54.077  17.386  12.668  1.00 56.54           N  
ANISOU 1423  N   LEU A 267     5462   8771   7249   -401    464   -554       N  
ATOM   1424  CA  LEU A 267     -53.756  17.886  13.999  1.00 57.14           C  
ANISOU 1424  CA  LEU A 267     5498   8993   7221   -327    527   -617       C  
ATOM   1425  C   LEU A 267     -53.501  16.732  14.972  1.00 59.89           C  
ANISOU 1425  C   LEU A 267     5848   9442   7465   -400    574   -494       C  
ATOM   1426  O   LEU A 267     -52.734  16.909  15.910  1.00 59.47           O  
ANISOU 1426  O   LEU A 267     5816   9464   7317   -351    605   -531       O  
ATOM   1427  CB  LEU A 267     -54.841  18.845  14.519  1.00 58.67           C  
ANISOU 1427  CB  LEU A 267     5543   9347   7401   -244    570   -710       C  
ATOM   1428  CG  LEU A 267     -54.676  20.354  14.163  1.00 64.22           C  
ANISOU 1428  CG  LEU A 267     6239   9976   8187   -119    527   -879       C  
ATOM   1429  CD1 LEU A 267     -53.381  20.941  14.725  1.00 64.26           C  
ANISOU 1429  CD1 LEU A 267     6320   9937   8161    -43    512   -980       C  
ATOM   1430  CD2 LEU A 267     -54.790  20.633  12.652  1.00 66.08           C  
ANISOU 1430  CD2 LEU A 267     6519  10026   8564   -140    449   -862       C  
ATOM   1431  N   PHE A 268     -54.066  15.539  14.717  1.00 56.27           N  
ANISOU 1431  N   PHE A 268     5369   8972   7038   -519    566   -343       N  
ATOM   1432  CA  PHE A 268     -53.769  14.369  15.541  1.00 56.57           C  
ANISOU 1432  CA  PHE A 268     5409   9073   7012   -602    591   -193       C  
ATOM   1433  C   PHE A 268     -52.302  13.911  15.281  1.00 60.46           C  
ANISOU 1433  C   PHE A 268     6060   9396   7516   -611    540   -190       C  
ATOM   1434  O   PHE A 268     -51.609  13.535  16.227  1.00 60.95           O  
ANISOU 1434  O   PHE A 268     6140   9529   7489   -613    570   -138       O  
ATOM   1435  CB  PHE A 268     -54.769  13.229  15.277  1.00 58.77           C  
ANISOU 1435  CB  PHE A 268     5617   9351   7362   -734    573    -28       C  
ATOM   1436  CG  PHE A 268     -54.327  11.868  15.770  1.00 60.75           C  
ANISOU 1436  CG  PHE A 268     5895   9573   7613   -841    557    149       C  
ATOM   1437  CD1 PHE A 268     -54.470  11.513  17.105  1.00 64.95           C  
ANISOU 1437  CD1 PHE A 268     6331  10317   8029   -866    629    273       C  
ATOM   1438  CD2 PHE A 268     -53.737  10.954  14.904  1.00 62.15           C  
ANISOU 1438  CD2 PHE A 268     6187   9520   7908   -910    464    189       C  
ATOM   1439  CE1 PHE A 268     -54.063  10.256  17.559  1.00 66.42           C  
ANISOU 1439  CE1 PHE A 268     6535  10468   8235   -970    604    461       C  
ATOM   1440  CE2 PHE A 268     -53.299   9.710  15.366  1.00 65.54           C  
ANISOU 1440  CE2 PHE A 268     6639   9899   8364  -1002    433    348       C  
ATOM   1441  CZ  PHE A 268     -53.471   9.367  16.689  1.00 64.81           C  
ANISOU 1441  CZ  PHE A 268     6450  10002   8174  -1037    501    495       C  
ATOM   1442  N   TYR A 269     -51.843  13.952  14.009  1.00 55.09           N  
ANISOU 1442  N   TYR A 269     5482   8513   6935   -611    465   -243       N  
ATOM   1443  CA  TYR A 269     -50.494  13.522  13.642  1.00 54.39           C  
ANISOU 1443  CA  TYR A 269     5531   8274   6860   -611    416   -248       C  
ATOM   1444  C   TYR A 269     -49.427  14.539  14.084  1.00 57.06           C  
ANISOU 1444  C   TYR A 269     5919   8630   7130   -507    436   -362       C  
ATOM   1445  O   TYR A 269     -48.349  14.117  14.490  1.00 54.82           O  
ANISOU 1445  O   TYR A 269     5712   8311   6805   -506    430   -339       O  
ATOM   1446  CB  TYR A 269     -50.400  13.204  12.139  1.00 55.32           C  
ANISOU 1446  CB  TYR A 269     5721   8211   7087   -638    331   -271       C  
ATOM   1447  CG  TYR A 269     -51.190  11.959  11.786  1.00 57.99           C  
ANISOU 1447  CG  TYR A 269     6028   8500   7506   -749    286   -163       C  
ATOM   1448  CD1 TYR A 269     -50.780  10.701  12.223  1.00 61.03           C  
ANISOU 1448  CD1 TYR A 269     6446   8829   7913   -823    259    -52       C  
ATOM   1449  CD2 TYR A 269     -52.382  12.045  11.076  1.00 58.75           C  
ANISOU 1449  CD2 TYR A 269     6049   8603   7671   -781    264   -165       C  
ATOM   1450  CE1 TYR A 269     -51.533   9.559  11.956  1.00 63.99           C  
ANISOU 1450  CE1 TYR A 269     6780   9141   8393   -931    202     52       C  
ATOM   1451  CE2 TYR A 269     -53.151  10.914  10.815  1.00 61.01           C  
ANISOU 1451  CE2 TYR A 269     6293   8841   8047   -888    213    -67       C  
ATOM   1452  CZ  TYR A 269     -52.720   9.671  11.253  1.00 72.84           C  
ANISOU 1452  CZ  TYR A 269     7825  10269   9583   -965    178     41       C  
ATOM   1453  OH  TYR A 269     -53.469   8.547  10.996  1.00 79.33           O  
ANISOU 1453  OH  TYR A 269     8598  11018  10525  -1077    109    140       O  
ATOM   1454  N   VAL A 270     -49.748  15.859  14.047  1.00 54.01           N  
ANISOU 1454  N   VAL A 270     5482   8293   6746   -420    453   -482       N  
ATOM   1455  CA  VAL A 270     -48.895  16.952  14.524  1.00 53.06           C  
ANISOU 1455  CA  VAL A 270     5386   8187   6589   -319    459   -603       C  
ATOM   1456  C   VAL A 270     -48.655  16.730  16.023  1.00 57.70           C  
ANISOU 1456  C   VAL A 270     5934   8946   7044   -302    519   -589       C  
ATOM   1457  O   VAL A 270     -47.512  16.701  16.467  1.00 58.52           O  
ANISOU 1457  O   VAL A 270     6108   9029   7100   -276    511   -608       O  
ATOM   1458  CB  VAL A 270     -49.535  18.346  14.234  1.00 56.96           C  
ANISOU 1458  CB  VAL A 270     5807   8690   7143   -234    449   -729       C  
ATOM   1459  CG1 VAL A 270     -48.876  19.449  15.055  1.00 56.57           C  
ANISOU 1459  CG1 VAL A 270     5746   8685   7062   -128    453   -864       C  
ATOM   1460  CG2 VAL A 270     -49.480  18.684  12.748  1.00 55.93           C  
ANISOU 1460  CG2 VAL A 270     5724   8393   7131   -241    381   -733       C  
ATOM   1461  N   ASN A 271     -49.738  16.526  16.779  1.00 53.80           N  
ANISOU 1461  N   ASN A 271     5320   8636   6484   -319    579   -544       N  
ATOM   1462  CA  ASN A 271     -49.717  16.260  18.214  1.00 54.24           C  
ANISOU 1462  CA  ASN A 271     5309   8910   6389   -306    644   -507       C  
ATOM   1463  C   ASN A 271     -48.894  15.006  18.557  1.00 55.84           C  
ANISOU 1463  C   ASN A 271     5585   9081   6552   -389    637   -353       C  
ATOM   1464  O   ASN A 271     -48.155  15.032  19.543  1.00 55.45           O  
ANISOU 1464  O   ASN A 271     5540   9140   6387   -352    662   -359       O  
ATOM   1465  CB  ASN A 271     -51.146  16.129  18.744  1.00 55.21           C  
ANISOU 1465  CB  ASN A 271     5275   9245   6457   -326    709   -450       C  
ATOM   1466  CG  ASN A 271     -51.705  17.456  19.164  1.00 66.72           C  
ANISOU 1466  CG  ASN A 271     6632  10844   7877   -199    739   -632       C  
ATOM   1467  OD1 ASN A 271     -51.581  17.855  20.323  1.00 61.13           O  
ANISOU 1467  OD1 ASN A 271     5853  10345   7029   -121    787   -704       O  
ATOM   1468  ND2 ASN A 271     -52.303  18.185  18.232  1.00 54.55           N  
ANISOU 1468  ND2 ASN A 271     5074   9193   6458   -167    704   -719       N  
ATOM   1469  N   ALA A 272     -49.006  13.935  17.733  1.00 51.20           N  
ANISOU 1469  N   ALA A 272     5048   8339   6065   -495    593   -224       N  
ATOM   1470  CA  ALA A 272     -48.271  12.675  17.900  1.00 51.17           C  
ANISOU 1470  CA  ALA A 272     5115   8259   6070   -575    563    -78       C  
ATOM   1471  C   ALA A 272     -46.751  12.915  17.796  1.00 56.21           C  
ANISOU 1471  C   ALA A 272     5879   8780   6697   -518    527   -156       C  
ATOM   1472  O   ALA A 272     -45.995  12.346  18.584  1.00 57.45           O  
ANISOU 1472  O   ALA A 272     6063   8979   6787   -532    532    -78       O  
ATOM   1473  CB  ALA A 272     -48.729  11.653  16.866  1.00 51.32           C  
ANISOU 1473  CB  ALA A 272     5162   8106   6233   -678    500     20       C  
ATOM   1474  N   CYS A 273     -46.319  13.808  16.874  1.00 51.26           N  
ANISOU 1474  N   CYS A 273     5317   8025   6134   -454    490   -299       N  
ATOM   1475  CA  CYS A 273     -44.914  14.191  16.695  1.00 49.35           C  
ANISOU 1475  CA  CYS A 273     5178   7682   5892   -397    455   -374       C  
ATOM   1476  C   CYS A 273     -44.400  14.942  17.932  1.00 52.43           C  
ANISOU 1476  C   CYS A 273     5535   8222   6162   -320    494   -451       C  
ATOM   1477  O   CYS A 273     -43.320  14.621  18.433  1.00 51.32           O  
ANISOU 1477  O   CYS A 273     5453   8077   5970   -312    484   -426       O  
ATOM   1478  CB  CYS A 273     -44.737  15.032  15.440  1.00 48.44           C  
ANISOU 1478  CB  CYS A 273     5107   7426   5874   -355    409   -480       C  
ATOM   1479  SG  CYS A 273     -45.230  14.202  13.919  1.00 52.30           S  
ANISOU 1479  SG  CYS A 273     5631   7760   6479   -428    353   -420       S  
ATOM   1480  N   PHE A 274     -45.163  15.948  18.412  1.00 48.51           N  
ANISOU 1480  N   PHE A 274     4943   7862   5626   -254    531   -557       N  
ATOM   1481  CA  PHE A 274     -44.759  16.746  19.567  1.00 48.08           C  
ANISOU 1481  CA  PHE A 274     4845   7962   5460   -164    556   -669       C  
ATOM   1482  C   PHE A 274     -44.771  15.921  20.848  1.00 56.27           C  
ANISOU 1482  C   PHE A 274     5831   9209   6341   -192    610   -558       C  
ATOM   1483  O   PHE A 274     -43.898  16.143  21.688  1.00 58.06           O  
ANISOU 1483  O   PHE A 274     6068   9521   6470   -138    611   -611       O  
ATOM   1484  CB  PHE A 274     -45.597  18.016  19.705  1.00 49.11           C  
ANISOU 1484  CB  PHE A 274     4880   8178   5604    -73    568   -832       C  
ATOM   1485  CG  PHE A 274     -45.137  19.078  18.734  1.00 48.07           C  
ANISOU 1485  CG  PHE A 274     4800   7847   5618    -22    499   -954       C  
ATOM   1486  CD1 PHE A 274     -45.887  19.379  17.598  1.00 49.44           C  
ANISOU 1486  CD1 PHE A 274     4960   7908   5915    -41    476   -951       C  
ATOM   1487  CD2 PHE A 274     -43.935  19.755  18.933  1.00 46.84           C  
ANISOU 1487  CD2 PHE A 274     4699   7619   5479     38    451  -1053       C  
ATOM   1488  CE1 PHE A 274     -45.444  20.342  16.681  1.00 48.71           C  
ANISOU 1488  CE1 PHE A 274     4906   7644   5959     -1    408  -1029       C  
ATOM   1489  CE2 PHE A 274     -43.488  20.708  18.009  1.00 47.92           C  
ANISOU 1489  CE2 PHE A 274     4871   7571   5765     72    381  -1130       C  
ATOM   1490  CZ  PHE A 274     -44.241  20.990  16.888  1.00 46.12           C  
ANISOU 1490  CZ  PHE A 274     4627   7243   5656     51    361  -1109       C  
ATOM   1491  N   PHE A 275     -45.680  14.922  20.968  1.00 53.36           N  
ANISOU 1491  N   PHE A 275     5402   8917   5955   -283    646   -388       N  
ATOM   1492  CA  PHE A 275     -45.709  14.030  22.132  1.00 54.18           C  
ANISOU 1492  CA  PHE A 275     5444   9220   5921   -329    693   -230       C  
ATOM   1493  C   PHE A 275     -44.437  13.179  22.176  1.00 58.58           C  
ANISOU 1493  C   PHE A 275     6112   9655   6491   -373    648   -127       C  
ATOM   1494  O   PHE A 275     -43.747  13.168  23.205  1.00 59.80           O  
ANISOU 1494  O   PHE A 275     6255   9952   6513   -338    665   -114       O  
ATOM   1495  CB  PHE A 275     -46.953  13.123  22.132  1.00 56.59           C  
ANISOU 1495  CB  PHE A 275     5651   9609   6243   -431    727    -47       C  
ATOM   1496  CG  PHE A 275     -46.942  12.055  23.209  1.00 59.29           C  
ANISOU 1496  CG  PHE A 275     5927  10128   6474   -504    761    174       C  
ATOM   1497  CD1 PHE A 275     -47.091  12.392  24.552  1.00 63.74           C  
ANISOU 1497  CD1 PHE A 275     6375  11014   6832   -445    832    172       C  
ATOM   1498  CD2 PHE A 275     -46.785  10.712  22.880  1.00 60.94           C  
ANISOU 1498  CD2 PHE A 275     6180  10186   6789   -628    714    385       C  
ATOM   1499  CE1 PHE A 275     -47.068  11.405  25.547  1.00 66.23           C  
ANISOU 1499  CE1 PHE A 275     6616  11514   7036   -516    862    405       C  
ATOM   1500  CE2 PHE A 275     -46.783   9.725  23.872  1.00 65.27           C  
ANISOU 1500  CE2 PHE A 275     6656  10888   7257   -703    735    617       C  
ATOM   1501  CZ  PHE A 275     -46.919  10.078  25.201  1.00 64.99           C  
ANISOU 1501  CZ  PHE A 275     6502  11187   7004   -651    813    640       C  
ATOM   1502  N   VAL A 276     -44.141  12.477  21.053  1.00 52.44           N  
ANISOU 1502  N   VAL A 276     5433   8624   5867   -441    587    -64       N  
ATOM   1503  CA  VAL A 276     -42.988  11.605  20.891  1.00 51.80           C  
ANISOU 1503  CA  VAL A 276     5458   8394   5831   -478    533     21       C  
ATOM   1504  C   VAL A 276     -41.716  12.432  21.134  1.00 56.36           C  
ANISOU 1504  C   VAL A 276     6103   8958   6353   -383    518   -121       C  
ATOM   1505  O   VAL A 276     -40.904  12.023  21.958  1.00 57.09           O  
ANISOU 1505  O   VAL A 276     6213   9117   6363   -379    516    -58       O  
ATOM   1506  CB  VAL A 276     -42.987  10.860  19.524  1.00 54.93           C  
ANISOU 1506  CB  VAL A 276     5936   8534   6403   -542    465     61       C  
ATOM   1507  CG1 VAL A 276     -41.642  10.178  19.253  1.00 54.42           C  
ANISOU 1507  CG1 VAL A 276     5985   8307   6386   -543    403     88       C  
ATOM   1508  CG2 VAL A 276     -44.116   9.837  19.455  1.00 55.35           C  
ANISOU 1508  CG2 VAL A 276     5918   8590   6521   -651    461    228       C  
ATOM   1509  N   GLY A 277     -41.611  13.608  20.498  1.00 52.05           N  
ANISOU 1509  N   GLY A 277     5579   8341   5855   -310    504   -300       N  
ATOM   1510  CA  GLY A 277     -40.496  14.538  20.665  1.00 50.78           C  
ANISOU 1510  CA  GLY A 277     5465   8156   5672   -224    478   -443       C  
ATOM   1511  C   GLY A 277     -40.272  14.946  22.109  1.00 56.54           C  
ANISOU 1511  C   GLY A 277     6131   9113   6241   -163    512   -493       C  
ATOM   1512  O   GLY A 277     -39.126  15.042  22.546  1.00 57.02           O  
ANISOU 1512  O   GLY A 277     6239   9169   6259   -127    485   -525       O  
ATOM   1513  N   SER A 278     -41.370  15.154  22.869  1.00 53.79           N  
ANISOU 1513  N   SER A 278     5663   8982   5792   -147    571   -499       N  
ATOM   1514  CA  SER A 278     -41.350  15.528  24.285  1.00 54.82           C  
ANISOU 1514  CA  SER A 278     5705   9385   5738    -78    611   -557       C  
ATOM   1515  C   SER A 278     -40.757  14.417  25.126  1.00 60.12           C  
ANISOU 1515  C   SER A 278     6384  10163   6297   -130    623   -375       C  
ATOM   1516  O   SER A 278     -40.051  14.718  26.078  1.00 61.91           O  
ANISOU 1516  O   SER A 278     6596  10532   6394    -67    620   -437       O  
ATOM   1517  CB  SER A 278     -42.755  15.853  24.787  1.00 59.72           C  
ANISOU 1517  CB  SER A 278     6183  10233   6273    -53    677   -583       C  
ATOM   1518  OG  SER A 278     -43.236  17.070  24.246  1.00 67.75           O  
ANISOU 1518  OG  SER A 278     7176  11185   7379     23    660   -784       O  
ATOM   1519  N   ILE A 279     -41.024  13.135  24.780  1.00 55.80           N  
ANISOU 1519  N   ILE A 279     5855   9537   5808   -244    624   -152       N  
ATOM   1520  CA  ILE A 279     -40.458  11.982  25.492  1.00 55.99           C  
ANISOU 1520  CA  ILE A 279     5885   9623   5764   -306    619     54       C  
ATOM   1521  C   ILE A 279     -38.927  12.029  25.327  1.00 58.61           C  
ANISOU 1521  C   ILE A 279     6337   9803   6130   -270    557     -3       C  
ATOM   1522  O   ILE A 279     -38.200  11.810  26.292  1.00 59.60           O  
ANISOU 1522  O   ILE A 279     6449  10066   6129   -249    557     45       O  
ATOM   1523  CB  ILE A 279     -41.080  10.648  24.993  1.00 59.33           C  
ANISOU 1523  CB  ILE A 279     6306   9932   6304   -436    607    288       C  
ATOM   1524  CG1 ILE A 279     -42.553  10.525  25.431  1.00 61.17           C  
ANISOU 1524  CG1 ILE A 279     6393  10374   6476   -479    674    383       C  
ATOM   1525  CG2 ILE A 279     -40.269   9.421  25.437  1.00 60.64           C  
ANISOU 1525  CG2 ILE A 279     6507  10061   6473   -502    569    498       C  
ATOM   1526  CD1 ILE A 279     -43.344   9.676  24.521  1.00 69.56           C  
ANISOU 1526  CD1 ILE A 279     7457  11262   7711   -594    646    528       C  
ATOM   1527  N   GLY A 280     -38.476  12.368  24.120  1.00 52.75           N  
ANISOU 1527  N   GLY A 280     5695   8803   5544   -260    507   -106       N  
ATOM   1528  CA  GLY A 280     -37.066  12.507  23.778  1.00 51.27           C  
ANISOU 1528  CA  GLY A 280     5612   8464   5405   -225    450   -168       C  
ATOM   1529  C   GLY A 280     -36.351  13.514  24.648  1.00 53.81           C  
ANISOU 1529  C   GLY A 280     5912   8920   5613   -129    446   -323       C  
ATOM   1530  O   GLY A 280     -35.306  13.199  25.212  1.00 51.73           O  
ANISOU 1530  O   GLY A 280     5682   8683   5291   -114    420   -288       O  
ATOM   1531  N   TRP A 281     -36.954  14.706  24.808  1.00 52.06           N  
ANISOU 1531  N   TRP A 281     5627   8791   5364    -59    466   -499       N  
ATOM   1532  CA  TRP A 281     -36.443  15.802  25.625  1.00 53.21           C  
ANISOU 1532  CA  TRP A 281     5735   9062   5420     43    448   -688       C  
ATOM   1533  C   TRP A 281     -36.516  15.500  27.113  1.00 58.70           C  
ANISOU 1533  C   TRP A 281     6342  10065   5895     71    488   -645       C  
ATOM   1534  O   TRP A 281     -35.624  15.896  27.854  1.00 58.56           O  
ANISOU 1534  O   TRP A 281     6324  10136   5789    135    456   -738       O  
ATOM   1535  CB  TRP A 281     -37.216  17.086  25.329  1.00 52.61           C  
ANISOU 1535  CB  TRP A 281     5605   8982   5405    111    447   -887       C  
ATOM   1536  CG  TRP A 281     -36.767  17.756  24.066  1.00 52.83           C  
ANISOU 1536  CG  TRP A 281     5707   8735   5629    115    386   -970       C  
ATOM   1537  CD1 TRP A 281     -37.372  17.695  22.842  1.00 54.89           C  
ANISOU 1537  CD1 TRP A 281     5995   8830   6030     68    387   -928       C  
ATOM   1538  CD2 TRP A 281     -35.594  18.565  23.896  1.00 52.27           C  
ANISOU 1538  CD2 TRP A 281     5683   8541   5635    164    313  -1091       C  
ATOM   1539  NE1 TRP A 281     -36.665  18.439  21.928  1.00 53.30           N  
ANISOU 1539  NE1 TRP A 281     5850   8428   5975     87    323  -1006       N  
ATOM   1540  CE2 TRP A 281     -35.561  18.976  22.543  1.00 54.76           C  
ANISOU 1540  CE2 TRP A 281     6046   8627   6134    142    277  -1099       C  
ATOM   1541  CE3 TRP A 281     -34.562  18.983  24.759  1.00 54.20           C  
ANISOU 1541  CE3 TRP A 281     5926   8855   5811    223    269  -1186       C  
ATOM   1542  CZ2 TRP A 281     -34.548  19.799  22.033  1.00 53.36           C  
ANISOU 1542  CZ2 TRP A 281     5905   8291   6077    170    202  -1181       C  
ATOM   1543  CZ3 TRP A 281     -33.547  19.782  24.250  1.00 55.32           C  
ANISOU 1543  CZ3 TRP A 281     6111   8821   6086    249    189  -1280       C  
ATOM   1544  CH2 TRP A 281     -33.550  20.190  22.905  1.00 54.99           C  
ANISOU 1544  CH2 TRP A 281     6109   8555   6232    220    158  -1268       C  
ATOM   1545  N   LEU A 282     -37.562  14.794  27.550  1.00 57.34           N  
ANISOU 1545  N   LEU A 282     6086  10070   5631     21    555   -495       N  
ATOM   1546  CA  LEU A 282     -37.780  14.479  28.967  1.00 58.70           C  
ANISOU 1546  CA  LEU A 282     6149  10584   5571     43    604   -423       C  
ATOM   1547  C   LEU A 282     -36.994  13.257  29.484  1.00 61.61           C  
ANISOU 1547  C   LEU A 282     6547  10984   5876    -26    592   -187       C  
ATOM   1548  O   LEU A 282     -36.919  13.075  30.699  1.00 63.59           O  
ANISOU 1548  O   LEU A 282     6711  11528   5923      0    621   -126       O  
ATOM   1549  CB  LEU A 282     -39.282  14.258  29.247  1.00 59.58           C  
ANISOU 1549  CB  LEU A 282     6131  10900   5606     15    683   -339       C  
ATOM   1550  CG  LEU A 282     -40.200  15.474  29.215  1.00 64.32           C  
ANISOU 1550  CG  LEU A 282     6648  11600   6190    111    709   -574       C  
ATOM   1551  CD1 LEU A 282     -41.654  15.044  29.365  1.00 65.31           C  
ANISOU 1551  CD1 LEU A 282     6650  11906   6260     63    789   -445       C  
ATOM   1552  CD2 LEU A 282     -39.828  16.504  30.294  1.00 67.24           C  
ANISOU 1552  CD2 LEU A 282     6945  12217   6384    252    700   -804       C  
ATOM   1553  N   ALA A 283     -36.435  12.425  28.592  1.00 55.89           N  
ANISOU 1553  N   ALA A 283     5935   9979   5322   -106    547    -57       N  
ATOM   1554  CA  ALA A 283     -35.703  11.203  28.958  1.00 56.64           C  
ANISOU 1554  CA  ALA A 283     6062  10055   5402   -173    521    171       C  
ATOM   1555  C   ALA A 283     -34.569  11.459  29.963  1.00 62.59           C  
ANISOU 1555  C   ALA A 283     6816  10959   6006   -103    494    121       C  
ATOM   1556  O   ALA A 283     -34.362  10.653  30.870  1.00 63.10           O  
ANISOU 1556  O   ALA A 283     6832  11193   5950   -135    501    313       O  
ATOM   1557  CB  ALA A 283     -35.141  10.544  27.717  1.00 55.68           C  
ANISOU 1557  CB  ALA A 283     6067   9585   5503   -233    461    232       C  
ATOM   1558  N   GLN A 284     -33.861  12.596  29.805  1.00 59.04           N  
ANISOU 1558  N   GLN A 284     6410  10448   5572    -11    456   -128       N  
ATOM   1559  CA  GLN A 284     -32.755  13.048  30.653  1.00 58.89           C  
ANISOU 1559  CA  GLN A 284     6393  10549   5435     65    416   -229       C  
ATOM   1560  C   GLN A 284     -33.152  13.218  32.129  1.00 64.73           C  
ANISOU 1560  C   GLN A 284     6999  11691   5906    121    459   -233       C  
ATOM   1561  O   GLN A 284     -32.270  13.206  32.985  1.00 64.94           O  
ANISOU 1561  O   GLN A 284     7014  11858   5803    162    427   -235       O  
ATOM   1562  CB  GLN A 284     -32.199  14.390  30.130  1.00 58.48           C  
ANISOU 1562  CB  GLN A 284     6389  10351   5480    148    363   -512       C  
ATOM   1563  CG  GLN A 284     -33.189  15.551  30.218  1.00 57.69           C  
ANISOU 1563  CG  GLN A 284     6210  10348   5360    218    389   -723       C  
ATOM   1564  CD  GLN A 284     -32.672  16.810  29.595  1.00 71.34           C  
ANISOU 1564  CD  GLN A 284     7982  11891   7232    285    320   -969       C  
ATOM   1565  OE1 GLN A 284     -31.889  17.541  30.195  1.00 67.07           O  
ANISOU 1565  OE1 GLN A 284     7428  11418   6640    362    263  -1130       O  
ATOM   1566  NE2 GLN A 284     -33.136  17.119  28.391  1.00 56.87           N  
ANISOU 1566  NE2 GLN A 284     6192   9829   5587    256    316  -1000       N  
ATOM   1567  N   PHE A 285     -34.449  13.419  32.425  1.00 62.75           N  
ANISOU 1567  N   PHE A 285     6639  11641   5563    131    528   -246       N  
ATOM   1568  CA  PHE A 285     -34.869  13.685  33.798  1.00 65.40           C  
ANISOU 1568  CA  PHE A 285     6829  12398   5623    203    575   -278       C  
ATOM   1569  C   PHE A 285     -34.992  12.402  34.628  1.00 72.97           C  
ANISOU 1569  C   PHE A 285     7714  13581   6431    123    615     52       C  
ATOM   1570  O   PHE A 285     -35.039  12.495  35.855  1.00 75.20           O  
ANISOU 1570  O   PHE A 285     7875  14242   6456    182    646     60       O  
ATOM   1571  CB  PHE A 285     -36.136  14.553  33.843  1.00 67.77           C  
ANISOU 1571  CB  PHE A 285     7025  12851   5873    268    630   -454       C  
ATOM   1572  CG  PHE A 285     -35.892  15.861  33.121  1.00 68.34           C  
ANISOU 1572  CG  PHE A 285     7162  12696   6107    351    572   -770       C  
ATOM   1573  CD1 PHE A 285     -36.460  16.103  31.876  1.00 70.33           C  
ANISOU 1573  CD1 PHE A 285     7472  12668   6582    308    572   -799       C  
ATOM   1574  CD2 PHE A 285     -35.005  16.803  33.633  1.00 70.89           C  
ANISOU 1574  CD2 PHE A 285     7492  13060   6382    462    502  -1018       C  
ATOM   1575  CE1 PHE A 285     -36.182  17.281  31.173  1.00 69.85           C  
ANISOU 1575  CE1 PHE A 285     7466  12387   6687    374    508  -1053       C  
ATOM   1576  CE2 PHE A 285     -34.725  17.978  32.929  1.00 72.85           C  
ANISOU 1576  CE2 PHE A 285     7795  13067   6817    524    431  -1279       C  
ATOM   1577  CZ  PHE A 285     -35.315  18.208  31.701  1.00 69.30           C  
ANISOU 1577  CZ  PHE A 285     7397  12349   6585    477    437  -1282       C  
ATOM   1578  N   MET A 286     -34.921  11.218  33.985  1.00 70.26           N  
ANISOU 1578  N   MET A 286     7439  13006   6250     -4    601    318       N  
ATOM   1579  CA  MET A 286     -34.897   9.927  34.676  1.00 73.07           C  
ANISOU 1579  CA  MET A 286     7736  13506   6521    -93    613    660       C  
ATOM   1580  C   MET A 286     -33.545   9.779  35.422  1.00 80.29           C  
ANISOU 1580  C   MET A 286     8681  14497   7328    -51    556    679       C  
ATOM   1581  O   MET A 286     -32.550  10.387  35.009  1.00 79.41           O  
ANISOU 1581  O   MET A 286     8677  14194   7302      9    494    474       O  
ATOM   1582  CB  MET A 286     -35.128   8.777  33.692  1.00 74.87           C  
ANISOU 1582  CB  MET A 286     8036  13412   6999   -230    588    897       C  
ATOM   1583  CG  MET A 286     -36.540   8.720  33.167  1.00 79.78           C  
ANISOU 1583  CG  MET A 286     8599  14015   7697   -288    643    937       C  
ATOM   1584  SD  MET A 286     -36.757   7.444  31.906  1.00 84.59           S  
ANISOU 1584  SD  MET A 286     9298  14220   8624   -438    589   1164       S  
ATOM   1585  CE  MET A 286     -37.150   6.037  32.952  1.00 84.28           C  
ANISOU 1585  CE  MET A 286     9121  14408   8495   -553    600   1591       C  
ATOM   1586  N   ASP A 287     -33.517   9.017  36.532  1.00 79.81           N  
ANISOU 1586  N   ASP A 287     8515  14732   7076    -80    574    928       N  
ATOM   1587  CA  ASP A 287     -32.322   8.866  37.370  1.00 80.84           C  
ANISOU 1587  CA  ASP A 287     8652  14991   7073    -37    522    963       C  
ATOM   1588  C   ASP A 287     -31.087   8.376  36.595  1.00 81.05           C  
ANISOU 1588  C   ASP A 287     8839  14626   7331    -73    431    996       C  
ATOM   1589  O   ASP A 287     -31.096   7.286  36.012  1.00 80.06           O  
ANISOU 1589  O   ASP A 287     8763  14263   7394   -179    405   1234       O  
ATOM   1590  CB  ASP A 287     -32.595   7.965  38.587  1.00 86.34           C  
ANISOU 1590  CB  ASP A 287     9199  16057   7548    -84    555   1291       C  
ATOM   1591  CG  ASP A 287     -33.035   8.726  39.833  1.00106.90           C  
ANISOU 1591  CG  ASP A 287    11640  19175   9804     24    619   1171       C  
ATOM   1592  OD1 ASP A 287     -33.214   9.969  39.745  1.00107.65           O  
ANISOU 1592  OD1 ASP A 287    11736  19320   9847    139    632    815       O  
ATOM   1593  OD2 ASP A 287     -33.199   8.081  40.900  1.00117.85           O  
ANISOU 1593  OD2 ASP A 287    12888  20921  10970     -3    649   1434       O  
ATOM   1594  N   GLY A 288     -30.061   9.236  36.582  1.00 75.29           N  
ANISOU 1594  N   GLY A 288     8180  13834   6592     22    379    739       N  
ATOM   1595  CA  GLY A 288     -28.776   9.023  35.919  1.00 72.97           C  
ANISOU 1595  CA  GLY A 288     8024  13217   6484     16    296    714       C  
ATOM   1596  C   GLY A 288     -28.835   8.871  34.411  1.00 73.45           C  
ANISOU 1596  C   GLY A 288     8206  12862   6838    -38    277    681       C  
ATOM   1597  O   GLY A 288     -27.850   8.453  33.799  1.00 72.37           O  
ANISOU 1597  O   GLY A 288     8171  12463   6862    -55    214    716       O  
ATOM   1598  N   ALA A 289     -29.988   9.206  33.798  1.00 68.54           N  
ANISOU 1598  N   ALA A 289     7568  12193   6283    -58    331    609       N  
ATOM   1599  CA  ALA A 289     -30.218   9.079  32.356  1.00 65.83           C  
ANISOU 1599  CA  ALA A 289     7323  11493   6196   -107    318    576       C  
ATOM   1600  C   ALA A 289     -29.423  10.092  31.551  1.00 65.65           C  
ANISOU 1600  C   ALA A 289     7397  11259   6289    -39    275    309       C  
ATOM   1601  O   ALA A 289     -28.826   9.691  30.555  1.00 64.78           O  
ANISOU 1601  O   ALA A 289     7387  10860   6367    -69    231    333       O  
ATOM   1602  CB  ALA A 289     -31.696   9.214  32.038  1.00 66.84           C  
ANISOU 1602  CB  ALA A 289     7389  11669   6338   -145    386    579       C  
ATOM   1603  N   ARG A 290     -29.377  11.380  31.976  1.00 60.06           N  
ANISOU 1603  N   ARG A 290     6651  10692   5475     53    279     60       N  
ATOM   1604  CA  ARG A 290     -28.642  12.402  31.231  1.00 58.03           C  
ANISOU 1604  CA  ARG A 290     6468  10235   5345    110    229   -177       C  
ATOM   1605  C   ARG A 290     -27.194  11.965  30.963  1.00 62.46           C  
ANISOU 1605  C   ARG A 290     7115  10626   5992    106    159   -126       C  
ATOM   1606  O   ARG A 290     -26.775  11.992  29.798  1.00 62.44           O  
ANISOU 1606  O   ARG A 290     7195  10352   6176     90    131   -163       O  
ATOM   1607  CB  ARG A 290     -28.681  13.780  31.906  1.00 56.03           C  
ANISOU 1607  CB  ARG A 290     6148  10166   4974    213    218   -442       C  
ATOM   1608  CG  ARG A 290     -28.146  14.870  30.959  1.00 57.88           C  
ANISOU 1608  CG  ARG A 290     6445  10155   5391    253    161   -664       C  
ATOM   1609  CD  ARG A 290     -28.208  16.281  31.506  1.00 59.01           C  
ANISOU 1609  CD  ARG A 290     6522  10426   5473    355    127   -944       C  
ATOM   1610  NE  ARG A 290     -29.581  16.719  31.740  1.00 55.67           N  
ANISOU 1610  NE  ARG A 290     6014  10158   4979    384    186  -1027       N  
ATOM   1611  CZ  ARG A 290     -30.150  16.819  32.935  1.00 68.85           C  
ANISOU 1611  CZ  ARG A 290     7573  12165   6422    443    221  -1072       C  
ATOM   1612  NH1 ARG A 290     -29.461  16.524  34.034  1.00 59.82           N  
ANISOU 1612  NH1 ARG A 290     6391  11246   5091    477    201  -1041       N  
ATOM   1613  NH2 ARG A 290     -31.414  17.215  33.043  1.00 52.61           N  
ANISOU 1613  NH2 ARG A 290     5434  10241   4314    473    278  -1149       N  
ATOM   1614  N   ARG A 291     -26.467  11.495  32.008  1.00 59.55           N  
ANISOU 1614  N   ARG A 291     6716  10430   5481    120    135    -24       N  
ATOM   1615  CA  ARG A 291     -25.078  11.023  31.898  1.00 58.61           C  
ANISOU 1615  CA  ARG A 291     6663  10183   5425    122     68     38       C  
ATOM   1616  C   ARG A 291     -24.953   9.855  30.906  1.00 60.13           C  
ANISOU 1616  C   ARG A 291     6931  10110   5803     48     57    223       C  
ATOM   1617  O   ARG A 291     -23.994   9.802  30.157  1.00 57.82           O  
ANISOU 1617  O   ARG A 291     6713   9609   5647     60      9    186       O  
ATOM   1618  CB  ARG A 291     -24.510  10.611  33.265  1.00 59.94           C  
ANISOU 1618  CB  ARG A 291     6768  10614   5392    145     47    145       C  
ATOM   1619  N   GLU A 292     -25.926   8.947  30.891  1.00 57.35           N  
ANISOU 1619  N   GLU A 292     6553   9773   5463    -22     95    411       N  
ATOM   1620  CA  GLU A 292     -25.943   7.803  29.984  1.00 56.49           C  
ANISOU 1620  CA  GLU A 292     6506   9414   5544    -90     72    572       C  
ATOM   1621  C   GLU A 292     -26.253   8.265  28.546  1.00 56.74           C  
ANISOU 1621  C   GLU A 292     6605   9205   5750    -91     79    423       C  
ATOM   1622  O   GLU A 292     -25.736   7.682  27.589  1.00 53.62           O  
ANISOU 1622  O   GLU A 292     6282   8575   5516   -102     37    448       O  
ATOM   1623  CB  GLU A 292     -26.973   6.763  30.481  1.00 59.41           C  
ANISOU 1623  CB  GLU A 292     6808   9883   5883   -172    100    819       C  
ATOM   1624  CG  GLU A 292     -27.455   5.760  29.442  1.00 71.85           C  
ANISOU 1624  CG  GLU A 292     8431  11194   7676   -247     76    942       C  
ATOM   1625  CD  GLU A 292     -26.537   4.608  29.085  1.00 99.39           C  
ANISOU 1625  CD  GLU A 292    11977  14471  11316   -266     -7   1084       C  
ATOM   1626  OE1 GLU A 292     -27.068   3.565  28.642  1.00110.74           O  
ANISOU 1626  OE1 GLU A 292    13416  15755  12905   -337    -39   1242       O  
ATOM   1627  OE2 GLU A 292     -25.299   4.741  29.221  1.00 94.62           O  
ANISOU 1627  OE2 GLU A 292    11412  13844  10696   -206    -49   1029       O  
ATOM   1628  N   ILE A 293     -27.075   9.318  28.402  1.00 53.10           N  
ANISOU 1628  N   ILE A 293     6112   8814   5250    -70    126    262       N  
ATOM   1629  CA  ILE A 293     -27.455   9.819  27.083  1.00 51.99           C  
ANISOU 1629  CA  ILE A 293     6021   8473   5260    -72    133    136       C  
ATOM   1630  C   ILE A 293     -26.305  10.604  26.445  1.00 56.66           C  
ANISOU 1630  C   ILE A 293     6668   8934   5926    -15     89    -23       C  
ATOM   1631  O   ILE A 293     -25.960  10.333  25.311  1.00 55.05           O  
ANISOU 1631  O   ILE A 293     6526   8526   5866    -23     67    -27       O  
ATOM   1632  CB  ILE A 293     -28.783  10.667  27.125  1.00 54.30           C  
ANISOU 1632  CB  ILE A 293     6250   8877   5503    -70    193     33       C  
ATOM   1633  CG1 ILE A 293     -30.014   9.781  27.473  1.00 54.94           C  
ANISOU 1633  CG1 ILE A 293     6271   9057   5545   -143    239    215       C  
ATOM   1634  CG2 ILE A 293     -29.031  11.439  25.796  1.00 52.01           C  
ANISOU 1634  CG2 ILE A 293     6005   8395   5362    -60    191   -115       C  
ATOM   1635  CD1 ILE A 293     -31.228  10.548  28.019  1.00 58.73           C  
ANISOU 1635  CD1 ILE A 293     6654   9760   5902   -126    305    138       C  
ATOM   1636  N   VAL A 294     -25.726  11.551  27.165  1.00 55.34           N  
ANISOU 1636  N   VAL A 294     6469   8894   5663     44     73   -152       N  
ATOM   1637  CA  VAL A 294     -24.772  12.524  26.649  1.00 54.80           C  
ANISOU 1637  CA  VAL A 294     6429   8722   5670     93     28   -309       C  
ATOM   1638  C   VAL A 294     -23.272  12.144  26.839  1.00 57.96           C  
ANISOU 1638  C   VAL A 294     6862   9080   6078    115    -29   -262       C  
ATOM   1639  O   VAL A 294     -22.421  12.726  26.153  1.00 56.59           O  
ANISOU 1639  O   VAL A 294     6715   8782   6004    139    -67   -347       O  
ATOM   1640  CB  VAL A 294     -25.125  13.866  27.350  1.00 60.51           C  
ANISOU 1640  CB  VAL A 294     7085   9597   6307    146     26   -498       C  
ATOM   1641  CG1 VAL A 294     -24.067  14.930  27.121  1.00 61.02           C  
ANISOU 1641  CG1 VAL A 294     7159   9572   6454    192    -39   -652       C  
ATOM   1642  CG2 VAL A 294     -26.495  14.365  26.908  1.00 59.95           C  
ANISOU 1642  CG2 VAL A 294     6982   9534   6262    136     76   -565       C  
ATOM   1643  N   CYS A 295     -22.944  11.201  27.740  1.00 55.99           N  
ANISOU 1643  N   CYS A 295     6600   8942   5730    106    -39   -119       N  
ATOM   1644  CA  CYS A 295     -21.548  10.829  27.989  1.00 56.63           C  
ANISOU 1644  CA  CYS A 295     6706   8997   5816    132    -97    -73       C  
ATOM   1645  C   CYS A 295     -21.248   9.469  27.475  1.00 58.43           C  
ANISOU 1645  C   CYS A 295     6982   9080   6139    100   -113    100       C  
ATOM   1646  O   CYS A 295     -22.122   8.594  27.439  1.00 58.26           O  
ANISOU 1646  O   CYS A 295     6960   9041   6136     50    -87    231       O  
ATOM   1647  CB  CYS A 295     -21.182  10.905  29.469  1.00 59.73           C  
ANISOU 1647  CB  CYS A 295     7040   9630   6025    161   -117    -55       C  
ATOM   1648  SG  CYS A 295     -21.863  12.322  30.347  1.00 65.52           S  
ANISOU 1648  SG  CYS A 295     7694  10592   6610    209    -99   -264       S  
ATOM   1649  N   ARG A 296     -19.952   9.271  27.184  1.00 52.53           N  
ANISOU 1649  N   ARG A 296     6266   8238   5455    133   -164    102       N  
ATOM   1650  CA  ARG A 296     -19.367   8.001  26.804  1.00 50.97           C  
ANISOU 1650  CA  ARG A 296     6108   7905   5353    129   -201    241       C  
ATOM   1651  C   ARG A 296     -19.079   7.222  28.073  1.00 56.05           C  
ANISOU 1651  C   ARG A 296     6719   8683   5893    122   -230    404       C  
ATOM   1652  O   ARG A 296     -19.049   7.804  29.173  1.00 55.55           O  
ANISOU 1652  O   ARG A 296     6604   8831   5670    135   -225    379       O  
ATOM   1653  CB  ARG A 296     -18.097   8.227  25.993  1.00 47.50           C  
ANISOU 1653  CB  ARG A 296     5698   7340   5010    178   -240    162       C  
ATOM   1654  CG  ARG A 296     -18.357   8.712  24.581  1.00 48.89           C  
ANISOU 1654  CG  ARG A 296     5901   7375   5301    181   -216     55       C  
ATOM   1655  CD  ARG A 296     -17.086   8.663  23.773  1.00 52.73           C  
ANISOU 1655  CD  ARG A 296     6400   7763   5872    231   -252     18       C  
ATOM   1656  NE  ARG A 296     -17.321   9.145  22.416  1.00 58.12           N  
ANISOU 1656  NE  ARG A 296     7094   8347   6643    236   -226    -71       N  
ATOM   1657  CZ  ARG A 296     -16.380   9.308  21.497  1.00 66.43           C  
ANISOU 1657  CZ  ARG A 296     8141   9336   7762    278   -243   -112       C  
ATOM   1658  NH1 ARG A 296     -15.116   9.014  21.770  1.00 61.02           N  
ANISOU 1658  NH1 ARG A 296     7444   8662   7078    322   -285    -82       N  
ATOM   1659  NH2 ARG A 296     -16.695   9.758  20.293  1.00 53.46           N  
ANISOU 1659  NH2 ARG A 296     6495   7636   6180    279   -216   -176       N  
ATOM   1660  N   ALA A 297     -18.857   5.902  27.924  1.00 53.53           N  
ANISOU 1660  N   ALA A 297     6423   8247   5667    106   -270    568       N  
ATOM   1661  CA  ALA A 297     -18.552   4.975  29.012  1.00 53.74           C  
ANISOU 1661  CA  ALA A 297     6418   8370   5633     93   -310    766       C  
ATOM   1662  C   ALA A 297     -17.273   5.402  29.765  1.00 58.76           C  
ANISOU 1662  C   ALA A 297     7032   9128   6167    150   -351    729       C  
ATOM   1663  O   ALA A 297     -17.099   5.020  30.921  1.00 59.88           O  
ANISOU 1663  O   ALA A 297     7126   9437   6188    144   -374    867       O  
ATOM   1664  CB  ALA A 297     -18.394   3.571  28.449  1.00 54.30           C  
ANISOU 1664  CB  ALA A 297     6523   8227   5883     78   -367    914       C  
ATOM   1665  N   ASP A 298     -16.384   6.189  29.100  1.00 53.36           N  
ANISOU 1665  N   ASP A 298     6373   8370   5531    202   -364    556       N  
ATOM   1666  CA  ASP A 298     -15.142   6.694  29.679  1.00 53.23           C  
ANISOU 1666  CA  ASP A 298     6334   8448   5444    253   -410    499       C  
ATOM   1667  C   ASP A 298     -15.324   8.099  30.317  1.00 57.69           C  
ANISOU 1667  C   ASP A 298     6854   9197   5868    267   -391    331       C  
ATOM   1668  O   ASP A 298     -14.343   8.688  30.784  1.00 57.75           O  
ANISOU 1668  O   ASP A 298     6836   9283   5824    308   -437    252       O  
ATOM   1669  CB  ASP A 298     -14.017   6.713  28.626  1.00 53.89           C  
ANISOU 1669  CB  ASP A 298     6451   8353   5672    300   -444    425       C  
ATOM   1670  CG  ASP A 298     -14.145   7.721  27.483  1.00 59.63           C  
ANISOU 1670  CG  ASP A 298     7196   8982   6480    306   -409    251       C  
ATOM   1671  OD1 ASP A 298     -15.142   8.475  27.451  1.00 59.32           O  
ANISOU 1671  OD1 ASP A 298     7150   8988   6402    274   -360    171       O  
ATOM   1672  OD2 ASP A 298     -13.273   7.730  26.616  1.00 61.69           O  
ANISOU 1672  OD2 ASP A 298     7469   9130   6842    342   -429    206       O  
ATOM   1673  N   GLY A 299     -16.555   8.616  30.309  1.00 53.90           N  
ANISOU 1673  N   GLY A 299     6362   8777   5343    238   -332    268       N  
ATOM   1674  CA  GLY A 299     -16.889   9.906  30.905  1.00 54.09           C  
ANISOU 1674  CA  GLY A 299     6337   8966   5247    260   -320     93       C  
ATOM   1675  C   GLY A 299     -16.653  11.133  30.047  1.00 57.50           C  
ANISOU 1675  C   GLY A 299     6782   9279   5787    279   -327   -112       C  
ATOM   1676  O   GLY A 299     -16.776  12.256  30.548  1.00 58.48           O  
ANISOU 1676  O   GLY A 299     6862   9514   5844    306   -341   -276       O  
ATOM   1677  N   THR A 300     -16.276  10.940  28.769  1.00 51.99           N  
ANISOU 1677  N   THR A 300     6133   8363   5258    271   -327   -105       N  
ATOM   1678  CA  THR A 300     -16.051  12.048  27.828  1.00 50.98           C  
ANISOU 1678  CA  THR A 300     6006   8118   5246    280   -334   -258       C  
ATOM   1679  C   THR A 300     -17.353  12.291  27.074  1.00 55.40           C  
ANISOU 1679  C   THR A 300     6583   8610   5859    248   -273   -294       C  
ATOM   1680  O   THR A 300     -18.241  11.432  27.101  1.00 54.92           O  
ANISOU 1680  O   THR A 300     6541   8555   5772    217   -229   -187       O  
ATOM   1681  CB  THR A 300     -14.856  11.809  26.880  1.00 50.32           C  
ANISOU 1681  CB  THR A 300     5945   7882   5291    297   -365   -230       C  
ATOM   1682  OG1 THR A 300     -15.100  10.650  26.097  1.00 51.91           O  
ANISOU 1682  OG1 THR A 300     6194   7966   5562    286   -336   -113       O  
ATOM   1683  CG2 THR A 300     -13.525  11.696  27.605  1.00 45.06           C  
ANISOU 1683  CG2 THR A 300     5252   7283   4583    332   -431   -207       C  
ATOM   1684  N   MET A 301     -17.491  13.448  26.411  1.00 52.63           N  
ANISOU 1684  N   MET A 301     6215   8190   5590    250   -276   -432       N  
ATOM   1685  CA  MET A 301     -18.763  13.704  25.756  1.00 52.59           C  
ANISOU 1685  CA  MET A 301     6220   8133   5630    222   -222   -466       C  
ATOM   1686  C   MET A 301     -18.960  12.862  24.512  1.00 54.36           C  
ANISOU 1686  C   MET A 301     6494   8203   5958    198   -190   -372       C  
ATOM   1687  O   MET A 301     -17.998  12.446  23.867  1.00 52.75           O  
ANISOU 1687  O   MET A 301     6310   7909   5823    214   -213   -329       O  
ATOM   1688  CB  MET A 301     -19.025  15.190  25.477  1.00 55.27           C  
ANISOU 1688  CB  MET A 301     6519   8446   6036    233   -242   -632       C  
ATOM   1689  CG  MET A 301     -18.141  15.836  24.474  1.00 59.00           C  
ANISOU 1689  CG  MET A 301     6985   8778   6655    234   -281   -663       C  
ATOM   1690  SD  MET A 301     -18.512  17.605  24.540  1.00 64.69           S  
ANISOU 1690  SD  MET A 301     7640   9478   7459    243   -330   -849       S  
ATOM   1691  CE  MET A 301     -19.784  17.672  23.362  1.00 61.62           C  
ANISOU 1691  CE  MET A 301     7271   8994   7147    212   -265   -830       C  
ATOM   1692  N   ARG A 302     -20.234  12.557  24.236  1.00 50.96           N  
ANISOU 1692  N   ARG A 302     6077   7759   5528    166   -139   -345       N  
ATOM   1693  CA  ARG A 302     -20.627  11.791  23.065  1.00 50.44           C  
ANISOU 1693  CA  ARG A 302     6053   7556   5556    144   -115   -280       C  
ATOM   1694  C   ARG A 302     -20.496  12.666  21.851  1.00 52.36           C  
ANISOU 1694  C   ARG A 302     6291   7701   5902    152   -115   -366       C  
ATOM   1695  O   ARG A 302     -20.976  13.802  21.842  1.00 50.61           O  
ANISOU 1695  O   ARG A 302     6035   7501   5693    147   -109   -462       O  
ATOM   1696  CB  ARG A 302     -22.041  11.215  23.220  1.00 51.32           C  
ANISOU 1696  CB  ARG A 302     6168   7691   5638    100    -69   -218       C  
ATOM   1697  CG  ARG A 302     -21.994  10.109  24.222  1.00 56.55           C  
ANISOU 1697  CG  ARG A 302     6831   8429   6226     84    -78    -79       C  
ATOM   1698  CD  ARG A 302     -23.257   9.345  24.304  1.00 53.87           C  
ANISOU 1698  CD  ARG A 302     6485   8101   5880     30    -43     20       C  
ATOM   1699  NE  ARG A 302     -23.063   8.018  23.754  1.00 61.28           N  
ANISOU 1699  NE  ARG A 302     7464   8897   6920     11    -74    141       N  
ATOM   1700  CZ  ARG A 302     -23.518   6.909  24.312  1.00 73.04           C  
ANISOU 1700  CZ  ARG A 302     8943  10403   8407    -34    -84    303       C  
ATOM   1701  NH1 ARG A 302     -24.208   6.962  25.439  1.00 56.63           N  
ANISOU 1701  NH1 ARG A 302     6807   8507   6202    -66    -52    379       N  
ATOM   1702  NH2 ARG A 302     -23.307   5.740  23.734  1.00 70.26           N  
ANISOU 1702  NH2 ARG A 302     8626   9888   8182    -45   -132    393       N  
ATOM   1703  N   LEU A 303     -19.728  12.170  20.879  1.00 49.91           N  
ANISOU 1703  N   LEU A 303     6002   7296   5664    171   -129   -331       N  
ATOM   1704  CA  LEU A 303     -19.415  12.843  19.616  1.00 49.69           C  
ANISOU 1704  CA  LEU A 303     5958   7197   5724    182   -130   -376       C  
ATOM   1705  C   LEU A 303     -19.369  11.833  18.506  1.00 53.46           C  
ANISOU 1705  C   LEU A 303     6469   7596   6249    197   -120   -329       C  
ATOM   1706  O   LEU A 303     -18.901  10.711  18.732  1.00 53.47           O  
ANISOU 1706  O   LEU A 303     6500   7577   6241    219   -139   -270       O  
ATOM   1707  CB  LEU A 303     -18.039  13.564  19.674  1.00 49.82           C  
ANISOU 1707  CB  LEU A 303     5934   7229   5766    209   -174   -400       C  
ATOM   1708  CG  LEU A 303     -17.764  14.577  20.786  1.00 53.81           C  
ANISOU 1708  CG  LEU A 303     6400   7806   6241    207   -211   -469       C  
ATOM   1709  CD1 LEU A 303     -16.300  14.891  20.853  1.00 52.91           C  
ANISOU 1709  CD1 LEU A 303     6250   7698   6156    231   -263   -464       C  
ATOM   1710  CD2 LEU A 303     -18.575  15.851  20.590  1.00 55.30           C  
ANISOU 1710  CD2 LEU A 303     6551   7979   6482    186   -212   -560       C  
ATOM   1711  N   GLY A 304     -19.801  12.251  17.312  1.00 48.32           N  
ANISOU 1711  N   GLY A 304     5807   6904   5650    194   -100   -359       N  
ATOM   1712  CA  GLY A 304     -19.758  11.430  16.111  1.00 47.03           C  
ANISOU 1712  CA  GLY A 304     5662   6685   5523    222    -97   -346       C  
ATOM   1713  C   GLY A 304     -20.389  10.075  16.303  1.00 49.90           C  
ANISOU 1713  C   GLY A 304     6076   6994   5890    214   -102   -309       C  
ATOM   1714  O   GLY A 304     -19.789   9.057  15.976  1.00 50.56           O  
ANISOU 1714  O   GLY A 304     6180   7030   6000    257   -131   -293       O  
ATOM   1715  N   GLU A 305     -21.589  10.072  16.864  1.00 45.66           N  
ANISOU 1715  N   GLU A 305     5550   6462   5335    161    -81   -295       N  
ATOM   1716  CA  GLU A 305     -22.392   8.896  17.146  1.00 46.05           C  
ANISOU 1716  CA  GLU A 305     5632   6461   5403    131    -89   -236       C  
ATOM   1717  C   GLU A 305     -23.183   8.535  15.885  1.00 51.19           C  
ANISOU 1717  C   GLU A 305     6295   7038   6119    128    -88   -274       C  
ATOM   1718  O   GLU A 305     -23.529   9.455  15.143  1.00 50.13           O  
ANISOU 1718  O   GLU A 305     6137   6928   5983    126    -61   -332       O  
ATOM   1719  CB  GLU A 305     -23.306   9.241  18.327  1.00 47.85           C  
ANISOU 1719  CB  GLU A 305     5843   6768   5568     75    -60   -201       C  
ATOM   1720  CG  GLU A 305     -23.840   8.077  19.129  1.00 61.58           C  
ANISOU 1720  CG  GLU A 305     7594   8499   7305     35    -73    -88       C  
ATOM   1721  CD  GLU A 305     -22.879   7.322  20.018  1.00 69.60           C  
ANISOU 1721  CD  GLU A 305     8618   9529   8299     54   -113      0       C  
ATOM   1722  OE1 GLU A 305     -22.814   6.081  19.866  1.00 69.27           O  
ANISOU 1722  OE1 GLU A 305     8599   9385   8334     52   -158     77       O  
ATOM   1723  OE2 GLU A 305     -22.208   7.952  20.869  1.00 53.78           O  
ANISOU 1723  OE2 GLU A 305     6593   7631   6210     72   -109     -9       O  
ATOM   1724  N   PRO A 306     -23.444   7.250  15.533  1.00 49.83           N  
ANISOU 1724  N   PRO A 306     6151   6769   6012    132   -127   -249       N  
ATOM   1725  CA  PRO A 306     -23.126   5.985  16.238  1.00 50.78           C  
ANISOU 1725  CA  PRO A 306     6294   6824   6174    131   -178   -164       C  
ATOM   1726  C   PRO A 306     -21.630   5.689  16.318  1.00 58.02           C  
ANISOU 1726  C   PRO A 306     7217   7737   7092    205   -214   -168       C  
ATOM   1727  O   PRO A 306     -20.967   5.542  15.286  1.00 56.89           O  
ANISOU 1727  O   PRO A 306     7071   7564   6979    274   -233   -245       O  
ATOM   1728  CB  PRO A 306     -23.833   4.913  15.385  1.00 51.99           C  
ANISOU 1728  CB  PRO A 306     6467   6850   6436    126   -225   -179       C  
ATOM   1729  CG  PRO A 306     -24.816   5.648  14.544  1.00 55.42           C  
ANISOU 1729  CG  PRO A 306     6887   7312   6857    102   -184   -252       C  
ATOM   1730  CD  PRO A 306     -24.202   6.986  14.296  1.00 50.11           C  
ANISOU 1730  CD  PRO A 306     6191   6745   6104    135   -136   -309       C  
ATOM   1731  N   THR A 307     -21.103   5.620  17.556  1.00 57.93           N  
ANISOU 1731  N   THR A 307     7201   7774   7035    193   -222    -84       N  
ATOM   1732  CA  THR A 307     -19.700   5.284  17.849  1.00 58.78           C  
ANISOU 1732  CA  THR A 307     7308   7883   7143    256   -261    -66       C  
ATOM   1733  C   THR A 307     -19.632   3.861  18.337  1.00 64.04           C  
ANISOU 1733  C   THR A 307     7994   8448   7892    256   -329     33       C  
ATOM   1734  O   THR A 307     -20.498   3.424  19.100  1.00 64.00           O  
ANISOU 1734  O   THR A 307     7989   8435   7894    186   -333    139       O  
ATOM   1735  CB  THR A 307     -19.034   6.232  18.866  1.00 68.61           C  
ANISOU 1735  CB  THR A 307     8527   9258   8285    250   -237    -47       C  
ATOM   1736  OG1 THR A 307     -19.987   6.732  19.789  1.00 67.79           O  
ANISOU 1736  OG1 THR A 307     8412   9236   8111    182   -201     -5       O  
ATOM   1737  CG2 THR A 307     -18.337   7.384  18.214  1.00 71.38           C  
ANISOU 1737  CG2 THR A 307     8848   9665   8607    284   -210   -141       C  
ATOM   1738  N   SER A 308     -18.607   3.139  17.889  1.00 61.62           N  
ANISOU 1738  N   SER A 308     7693   8067   7652    336   -386      6       N  
ATOM   1739  CA  SER A 308     -18.377   1.748  18.240  1.00 62.94           C  
ANISOU 1739  CA  SER A 308     7873   8107   7932    353   -472     91       C  
ATOM   1740  C   SER A 308     -18.148   1.570  19.748  1.00 66.38           C  
ANISOU 1740  C   SER A 308     8297   8604   8319    306   -484    255       C  
ATOM   1741  O   SER A 308     -17.537   2.420  20.407  1.00 64.17           O  
ANISOU 1741  O   SER A 308     7998   8463   7919    310   -446    260       O  
ATOM   1742  CB  SER A 308     -17.188   1.193  17.461  1.00 67.91           C  
ANISOU 1742  CB  SER A 308     8501   8672   8631    469   -527      4       C  
ATOM   1743  OG  SER A 308     -15.976   1.807  17.870  1.00 79.61           O  
ANISOU 1743  OG  SER A 308     9958  10266  10023    512   -504      3       O  
ATOM   1744  N   ASN A 309     -18.702   0.460  20.278  1.00 64.27           N  
ANISOU 1744  N   ASN A 309     8032   8237   8149    258   -545    393       N  
ATOM   1745  CA  ASN A 309     -18.607  -0.017  21.660  1.00 64.84           C  
ANISOU 1745  CA  ASN A 309     8081   8359   8195    209   -574    588       C  
ATOM   1746  C   ASN A 309     -19.160   0.994  22.669  1.00 67.07           C  
ANISOU 1746  C   ASN A 309     8336   8853   8296    139   -489    644       C  
ATOM   1747  O   ASN A 309     -18.767   1.007  23.840  1.00 69.18           O  
ANISOU 1747  O   ASN A 309     8573   9239   8472    123   -494    767       O  
ATOM   1748  CB  ASN A 309     -17.170  -0.437  21.981  1.00 67.42           C  
ANISOU 1748  CB  ASN A 309     8404   8672   8541    289   -633    615       C  
ATOM   1749  CG  ASN A 309     -16.675  -1.437  20.961  1.00 99.47           C  
ANISOU 1749  CG  ASN A 309    12482  12530  12784    373   -721    538       C  
ATOM   1750  OD1 ASN A 309     -15.884  -1.111  20.062  1.00 89.70           O  
ANISOU 1750  OD1 ASN A 309    11249  11293  11541    467   -713    382       O  
ATOM   1751  ND2 ASN A 309     -17.281  -2.620  20.965  1.00 95.34           N  
ANISOU 1751  ND2 ASN A 309    11961  11833  12430    340   -806    632       N  
ATOM   1752  N   GLU A 310     -20.107   1.814  22.207  1.00 59.31           N  
ANISOU 1752  N   GLU A 310     7355   7921   7261    104   -417    549       N  
ATOM   1753  CA  GLU A 310     -20.848   2.756  23.025  1.00 57.60           C  
ANISOU 1753  CA  GLU A 310     7105   7891   6890     46   -341    570       C  
ATOM   1754  C   GLU A 310     -22.277   2.285  23.015  1.00 61.47           C  
ANISOU 1754  C   GLU A 310     7578   8348   7428    -37   -330    656       C  
ATOM   1755  O   GLU A 310     -22.684   1.564  22.100  1.00 61.57           O  
ANISOU 1755  O   GLU A 310     7614   8186   7592    -44   -372    638       O  
ATOM   1756  CB  GLU A 310     -20.710   4.211  22.538  1.00 57.01           C  
ANISOU 1756  CB  GLU A 310     7032   7903   6726     79   -275    389       C  
ATOM   1757  CG  GLU A 310     -19.337   4.832  22.742  1.00 61.79           C  
ANISOU 1757  CG  GLU A 310     7634   8569   7273    145   -285    322       C  
ATOM   1758  CD  GLU A 310     -18.769   4.918  24.150  1.00 79.94           C  
ANISOU 1758  CD  GLU A 310     9901  11018   9455    145   -298    409       C  
ATOM   1759  OE1 GLU A 310     -19.542   4.957  25.135  1.00 71.08           O  
ANISOU 1759  OE1 GLU A 310     8745  10026   8235     93   -273    493       O  
ATOM   1760  OE2 GLU A 310     -17.525   4.982  24.258  1.00 75.11           O  
ANISOU 1760  OE2 GLU A 310     9288  10411   8838    200   -334    388       O  
ATOM   1761  N   THR A 311     -23.024   2.637  24.048  1.00 58.30           N  
ANISOU 1761  N   THR A 311     7127   8121   6902    -97   -280    751       N  
ATOM   1762  CA  THR A 311     -24.423   2.257  24.200  1.00 58.74           C  
ANISOU 1762  CA  THR A 311     7147   8187   6986   -184   -261    857       C  
ATOM   1763  C   THR A 311     -25.301   3.007  23.145  1.00 60.85           C  
ANISOU 1763  C   THR A 311     7431   8414   7275   -190   -209    693       C  
ATOM   1764  O   THR A 311     -24.881   4.037  22.608  1.00 59.47           O  
ANISOU 1764  O   THR A 311     7281   8265   7052   -133   -174    519       O  
ATOM   1765  CB  THR A 311     -24.822   2.493  25.656  1.00 68.37           C  
ANISOU 1765  CB  THR A 311     8292   9651   8033   -230   -216   1001       C  
ATOM   1766  OG1 THR A 311     -25.869   1.600  26.003  1.00 77.40           O  
ANISOU 1766  OG1 THR A 311     9385  10784   9239   -322   -229   1194       O  
ATOM   1767  CG2 THR A 311     -25.202   3.922  25.946  1.00 64.03           C  
ANISOU 1767  CG2 THR A 311     7716   9306   7306   -207   -128    853       C  
ATOM   1768  N   LEU A 312     -26.488   2.468  22.824  1.00 57.36           N  
ANISOU 1768  N   LEU A 312     6970   7903   6922   -260   -214    760       N  
ATOM   1769  CA  LEU A 312     -27.373   3.066  21.812  1.00 55.74           C  
ANISOU 1769  CA  LEU A 312     6775   7657   6748   -269   -175    623       C  
ATOM   1770  C   LEU A 312     -28.271   4.178  22.369  1.00 58.07           C  
ANISOU 1770  C   LEU A 312     7017   8157   6892   -295    -81    589       C  
ATOM   1771  O   LEU A 312     -29.004   4.788  21.593  1.00 57.41           O  
ANISOU 1771  O   LEU A 312     6935   8053   6825   -299    -47    477       O  
ATOM   1772  CB  LEU A 312     -28.250   1.995  21.151  1.00 56.81           C  
ANISOU 1772  CB  LEU A 312     6908   7617   7060   -331   -234    694       C  
ATOM   1773  CG  LEU A 312     -27.548   1.019  20.211  1.00 62.65           C  
ANISOU 1773  CG  LEU A 312     7701   8123   7980   -286   -336    650       C  
ATOM   1774  CD1 LEU A 312     -28.229  -0.340  20.243  1.00 64.76           C  
ANISOU 1774  CD1 LEU A 312     7943   8233   8432   -363   -426    806       C  
ATOM   1775  CD2 LEU A 312     -27.517   1.554  18.778  1.00 63.87           C  
ANISOU 1775  CD2 LEU A 312     7900   8202   8168   -224   -330    433       C  
ATOM   1776  N   SER A 313     -28.201   4.462  23.686  1.00 54.45           N  
ANISOU 1776  N   SER A 313     6506   7903   6281   -303    -45    675       N  
ATOM   1777  CA  SER A 313     -29.033   5.467  24.378  1.00 54.21           C  
ANISOU 1777  CA  SER A 313     6410   8096   6093   -311     37    635       C  
ATOM   1778  C   SER A 313     -28.997   6.848  23.700  1.00 55.26           C  
ANISOU 1778  C   SER A 313     6565   8233   6197   -252     76    405       C  
ATOM   1779  O   SER A 313     -30.037   7.492  23.580  1.00 53.42           O  
ANISOU 1779  O   SER A 313     6293   8070   5934   -268    126    344       O  
ATOM   1780  CB  SER A 313     -28.623   5.599  25.842  1.00 57.24           C  
ANISOU 1780  CB  SER A 313     6738   8710   6302   -298     55    722       C  
ATOM   1781  OG  SER A 313     -28.560   4.325  26.459  1.00 62.68           O  
ANISOU 1781  OG  SER A 313     7398   9391   7025   -355     10    960       O  
ATOM   1782  N   CYS A 314     -27.812   7.267  23.237  1.00 51.73           N  
ANISOU 1782  N   CYS A 314     6173   7708   5775   -187     46    292       N  
ATOM   1783  CA  CYS A 314     -27.585   8.526  22.542  1.00 50.87           C  
ANISOU 1783  CA  CYS A 314     6081   7581   5668   -135     65    104       C  
ATOM   1784  C   CYS A 314     -28.338   8.556  21.203  1.00 55.24           C  
ANISOU 1784  C   CYS A 314     6656   7994   6337   -154     70     45       C  
ATOM   1785  O   CYS A 314     -29.042   9.533  20.942  1.00 55.02           O  
ANISOU 1785  O   CYS A 314     6602   8012   6292   -149    108    -52       O  
ATOM   1786  CB  CYS A 314     -26.090   8.746  22.338  1.00 51.04           C  
ANISOU 1786  CB  CYS A 314     6142   7547   5703    -74     24     44       C  
ATOM   1787  SG  CYS A 314     -25.661  10.302  21.508  1.00 54.52           S  
ANISOU 1787  SG  CYS A 314     6587   7960   6170    -22     32   -149       S  
ATOM   1788  N   VAL A 315     -28.193   7.496  20.354  1.00 51.15           N  
ANISOU 1788  N   VAL A 315     6182   7312   5940   -167     23     95       N  
ATOM   1789  CA  VAL A 315     -28.843   7.488  19.043  1.00 50.30           C  
ANISOU 1789  CA  VAL A 315     6093   7088   5932   -177     18     28       C  
ATOM   1790  C   VAL A 315     -30.353   7.263  19.183  1.00 53.73           C  
ANISOU 1790  C   VAL A 315     6483   7555   6378   -248     46     87       C  
ATOM   1791  O   VAL A 315     -31.092   7.737  18.327  1.00 54.12           O  
ANISOU 1791  O   VAL A 315     6526   7573   6463   -253     63      8       O  
ATOM   1792  CB  VAL A 315     -28.209   6.556  17.964  1.00 54.25           C  
ANISOU 1792  CB  VAL A 315     6644   7416   6552   -149    -49     15       C  
ATOM   1793  CG1 VAL A 315     -26.773   6.963  17.652  1.00 53.03           C  
ANISOU 1793  CG1 VAL A 315     6517   7254   6379    -71    -64    -63       C  
ATOM   1794  CG2 VAL A 315     -28.289   5.089  18.342  1.00 55.29           C  
ANISOU 1794  CG2 VAL A 315     6783   7462   6764   -188   -108    152       C  
ATOM   1795  N   ILE A 316     -30.819   6.595  20.249  1.00 49.52           N  
ANISOU 1795  N   ILE A 316     5909   7099   5810   -303     51    235       N  
ATOM   1796  CA  ILE A 316     -32.258   6.416  20.454  1.00 50.21           C  
ANISOU 1796  CA  ILE A 316     5935   7243   5900   -375     83    310       C  
ATOM   1797  C   ILE A 316     -32.884   7.804  20.715  1.00 52.78           C  
ANISOU 1797  C   ILE A 316     6212   7728   6113   -350    158    198       C  
ATOM   1798  O   ILE A 316     -33.875   8.146  20.080  1.00 52.73           O  
ANISOU 1798  O   ILE A 316     6184   7705   6147   -371    179    148       O  
ATOM   1799  CB  ILE A 316     -32.573   5.384  21.586  1.00 55.07           C  
ANISOU 1799  CB  ILE A 316     6497   7930   6497   -445     72    526       C  
ATOM   1800  CG1 ILE A 316     -32.253   3.945  21.104  1.00 56.65           C  
ANISOU 1800  CG1 ILE A 316     6737   7917   6872   -480    -24    632       C  
ATOM   1801  CG2 ILE A 316     -34.039   5.495  22.080  1.00 53.98           C  
ANISOU 1801  CG2 ILE A 316     6267   7932   6312   -514    127    610       C  
ATOM   1802  CD1 ILE A 316     -32.090   2.898  22.227  1.00 63.48           C  
ANISOU 1802  CD1 ILE A 316     7561   8822   7737   -531    -59    860       C  
ATOM   1803  N   ILE A 317     -32.256   8.611  21.584  1.00 48.13           N  
ANISOU 1803  N   ILE A 317     5607   7281   5399   -297    185    144       N  
ATOM   1804  CA  ILE A 317     -32.720   9.955  21.963  1.00 47.23           C  
ANISOU 1804  CA  ILE A 317     5441   7314   5189   -257    237     15       C  
ATOM   1805  C   ILE A 317     -32.675  10.879  20.752  1.00 49.80           C  
ANISOU 1805  C   ILE A 317     5801   7520   5601   -219    228   -139       C  
ATOM   1806  O   ILE A 317     -33.630  11.614  20.519  1.00 49.37           O  
ANISOU 1806  O   ILE A 317     5703   7506   5548   -218    260   -210       O  
ATOM   1807  CB  ILE A 317     -31.917  10.497  23.191  1.00 49.86           C  
ANISOU 1807  CB  ILE A 317     5750   7814   5381   -203    245    -19       C  
ATOM   1808  CG1 ILE A 317     -32.346   9.762  24.482  1.00 50.29           C  
ANISOU 1808  CG1 ILE A 317     5735   8061   5312   -242    272    144       C  
ATOM   1809  CG2 ILE A 317     -32.021  12.020  23.361  1.00 50.50           C  
ANISOU 1809  CG2 ILE A 317     5795   7984   5407   -135    266   -210       C  
ATOM   1810  CD1 ILE A 317     -33.881   9.607  24.660  1.00 51.55           C  
ANISOU 1810  CD1 ILE A 317     5811   8327   5447   -297    325    218       C  
ATOM   1811  N   PHE A 318     -31.618  10.771  19.942  1.00 44.81           N  
ANISOU 1811  N   PHE A 318     5236   6746   5043   -192    183   -173       N  
ATOM   1812  CA  PHE A 318     -31.495  11.545  18.722  1.00 42.20           C  
ANISOU 1812  CA  PHE A 318     4927   6316   4790   -162    171   -283       C  
ATOM   1813  C   PHE A 318     -32.636  11.242  17.776  1.00 46.73           C  
ANISOU 1813  C   PHE A 318     5495   6820   5440   -203    177   -272       C  
ATOM   1814  O   PHE A 318     -33.238  12.170  17.262  1.00 46.01           O  
ANISOU 1814  O   PHE A 318     5375   6735   5371   -191    194   -352       O  
ATOM   1815  CB  PHE A 318     -30.152  11.266  18.025  1.00 42.39           C  
ANISOU 1815  CB  PHE A 318     5010   6231   4864   -126    126   -295       C  
ATOM   1816  CG  PHE A 318     -30.168  11.644  16.562  1.00 41.20           C  
ANISOU 1816  CG  PHE A 318     4875   5984   4796   -109    111   -359       C  
ATOM   1817  CD1 PHE A 318     -30.174  12.978  16.173  1.00 41.83           C  
ANISOU 1817  CD1 PHE A 318     4925   6080   4889    -82    119   -445       C  
ATOM   1818  CD2 PHE A 318     -30.237  10.667  15.579  1.00 42.48           C  
ANISOU 1818  CD2 PHE A 318     5071   6044   5024   -120     82   -332       C  
ATOM   1819  CE1 PHE A 318     -30.233  13.327  14.829  1.00 42.52           C  
ANISOU 1819  CE1 PHE A 318     5013   6103   5041    -71    107   -477       C  
ATOM   1820  CE2 PHE A 318     -30.315  11.016  14.234  1.00 45.49           C  
ANISOU 1820  CE2 PHE A 318     5454   6374   5455    -99     71   -391       C  
ATOM   1821  CZ  PHE A 318     -30.337  12.345  13.870  1.00 43.49           C  
ANISOU 1821  CZ  PHE A 318     5167   6158   5200    -79     88   -450       C  
ATOM   1822  N   VAL A 319     -32.882   9.949  17.492  1.00 45.04           N  
ANISOU 1822  N   VAL A 319     5304   6525   5283   -249    150   -177       N  
ATOM   1823  CA  VAL A 319     -33.901   9.505  16.545  1.00 44.45           C  
ANISOU 1823  CA  VAL A 319     5224   6370   5295   -291    137   -170       C  
ATOM   1824  C   VAL A 319     -35.253  10.027  17.006  1.00 49.46           C  
ANISOU 1824  C   VAL A 319     5786   7114   5893   -327    189   -163       C  
ATOM   1825  O   VAL A 319     -35.928  10.685  16.225  1.00 49.24           O  
ANISOU 1825  O   VAL A 319     5739   7069   5899   -321    198   -235       O  
ATOM   1826  CB  VAL A 319     -33.896   7.971  16.321  1.00 48.29           C  
ANISOU 1826  CB  VAL A 319     5739   6738   5869   -334     79    -74       C  
ATOM   1827  CG1 VAL A 319     -35.149   7.514  15.566  1.00 48.12           C  
ANISOU 1827  CG1 VAL A 319     5695   6652   5937   -389     60    -63       C  
ATOM   1828  CG2 VAL A 319     -32.635   7.533  15.579  1.00 47.27           C  
ANISOU 1828  CG2 VAL A 319     5676   6497   5788   -278     23   -121       C  
ATOM   1829  N   ILE A 320     -35.608   9.811  18.278  1.00 46.89           N  
ANISOU 1829  N   ILE A 320     5410   6919   5486   -355    223    -77       N  
ATOM   1830  CA  ILE A 320     -36.880  10.290  18.833  1.00 47.05           C  
ANISOU 1830  CA  ILE A 320     5344   7082   5451   -380    279    -69       C  
ATOM   1831  C   ILE A 320     -37.005  11.830  18.644  1.00 50.31           C  
ANISOU 1831  C   ILE A 320     5733   7549   5833   -312    307   -231       C  
ATOM   1832  O   ILE A 320     -38.016  12.279  18.134  1.00 51.21           O  
ANISOU 1832  O   ILE A 320     5806   7665   5985   -321    324   -273       O  
ATOM   1833  CB  ILE A 320     -37.068   9.860  20.323  1.00 50.69           C  
ANISOU 1833  CB  ILE A 320     5741   7722   5796   -407    315     54       C  
ATOM   1834  CG1 ILE A 320     -37.178   8.319  20.465  1.00 50.65           C  
ANISOU 1834  CG1 ILE A 320     5738   7646   5859   -492    277    247       C  
ATOM   1835  CG2 ILE A 320     -38.277  10.559  20.963  1.00 51.26           C  
ANISOU 1835  CG2 ILE A 320     5708   7990   5779   -405    383     30       C  
ATOM   1836  CD1 ILE A 320     -37.050   7.812  21.968  1.00 50.83           C  
ANISOU 1836  CD1 ILE A 320     5702   7849   5764   -518    300    407       C  
ATOM   1837  N   VAL A 321     -35.986  12.605  18.988  1.00 46.09           N  
ANISOU 1837  N   VAL A 321     5220   7039   5254   -247    300   -318       N  
ATOM   1838  CA  VAL A 321     -36.071  14.068  18.880  1.00 46.26           C  
ANISOU 1838  CA  VAL A 321     5210   7090   5277   -184    307   -467       C  
ATOM   1839  C   VAL A 321     -35.995  14.531  17.411  1.00 49.43           C  
ANISOU 1839  C   VAL A 321     5646   7338   5798   -176    273   -521       C  
ATOM   1840  O   VAL A 321     -36.828  15.332  16.988  1.00 49.13           O  
ANISOU 1840  O   VAL A 321     5563   7303   5802   -165    282   -584       O  
ATOM   1841  CB  VAL A 321     -35.044  14.834  19.776  1.00 49.10           C  
ANISOU 1841  CB  VAL A 321     5568   7522   5566   -120    295   -550       C  
ATOM   1842  CG1 VAL A 321     -35.160  16.351  19.576  1.00 48.46           C  
ANISOU 1842  CG1 VAL A 321     5450   7431   5534    -58    278   -708       C  
ATOM   1843  CG2 VAL A 321     -35.240  14.490  21.253  1.00 49.46           C  
ANISOU 1843  CG2 VAL A 321     5560   7767   5466   -117    331   -507       C  
ATOM   1844  N   TYR A 322     -35.013  14.049  16.652  1.00 45.49           N  
ANISOU 1844  N   TYR A 322     5214   6723   5345   -176    235   -493       N  
ATOM   1845  CA  TYR A 322     -34.841  14.496  15.278  1.00 43.25           C  
ANISOU 1845  CA  TYR A 322     4951   6334   5148   -162    205   -533       C  
ATOM   1846  C   TYR A 322     -36.000  14.066  14.383  1.00 47.37           C  
ANISOU 1846  C   TYR A 322     5459   6816   5722   -203    207   -507       C  
ATOM   1847  O   TYR A 322     -36.517  14.914  13.655  1.00 46.75           O  
ANISOU 1847  O   TYR A 322     5350   6721   5692   -190    202   -555       O  
ATOM   1848  CB  TYR A 322     -33.505  14.051  14.689  1.00 42.37           C  
ANISOU 1848  CB  TYR A 322     4900   6144   5055   -142    168   -513       C  
ATOM   1849  CG  TYR A 322     -33.306  14.599  13.291  1.00 41.73           C  
ANISOU 1849  CG  TYR A 322     4820   5999   5038   -121    143   -542       C  
ATOM   1850  CD1 TYR A 322     -33.019  15.947  13.084  1.00 42.25           C  
ANISOU 1850  CD1 TYR A 322     4848   6067   5140    -90    131   -591       C  
ATOM   1851  CD2 TYR A 322     -33.478  13.787  12.174  1.00 41.71           C  
ANISOU 1851  CD2 TYR A 322     4843   5942   5065   -133    123   -519       C  
ATOM   1852  CE1 TYR A 322     -32.891  16.466  11.801  1.00 40.58           C  
ANISOU 1852  CE1 TYR A 322     4619   5816   4984    -79    108   -586       C  
ATOM   1853  CE2 TYR A 322     -33.358  14.298  10.887  1.00 42.41           C  
ANISOU 1853  CE2 TYR A 322     4917   6011   5187   -111    103   -538       C  
ATOM   1854  CZ  TYR A 322     -33.049  15.636  10.706  1.00 45.99           C  
ANISOU 1854  CZ  TYR A 322     5327   6479   5667    -87    100   -556       C  
ATOM   1855  OH  TYR A 322     -32.940  16.149   9.442  1.00 46.17           O  
ANISOU 1855  OH  TYR A 322     5321   6500   5720    -71     80   -544       O  
ATOM   1856  N   TYR A 323     -36.399  12.773  14.423  1.00 44.77           N  
ANISOU 1856  N   TYR A 323     5149   6465   5398   -254    202   -427       N  
ATOM   1857  CA  TYR A 323     -37.505  12.270  13.605  1.00 45.07           C  
ANISOU 1857  CA  TYR A 323     5171   6459   5496   -299    190   -406       C  
ATOM   1858  C   TYR A 323     -38.798  12.996  13.934  1.00 50.45           C  
ANISOU 1858  C   TYR A 323     5774   7225   6169   -314    231   -426       C  
ATOM   1859  O   TYR A 323     -39.501  13.380  13.008  1.00 51.36           O  
ANISOU 1859  O   TYR A 323     5867   7310   6337   -317    220   -460       O  
ATOM   1860  CB  TYR A 323     -37.706  10.746  13.755  1.00 46.47           C  
ANISOU 1860  CB  TYR A 323     5369   6581   5706   -358    162   -313       C  
ATOM   1861  CG  TYR A 323     -38.713  10.171  12.782  1.00 47.74           C  
ANISOU 1861  CG  TYR A 323     5517   6674   5949   -403    128   -307       C  
ATOM   1862  CD1 TYR A 323     -40.068  10.110  13.102  1.00 49.61           C  
ANISOU 1862  CD1 TYR A 323     5686   6965   6201   -461    152   -260       C  
ATOM   1863  CD2 TYR A 323     -38.312   9.688  11.536  1.00 48.72           C  
ANISOU 1863  CD2 TYR A 323     5687   6695   6130   -381     67   -356       C  
ATOM   1864  CE1 TYR A 323     -41.003   9.619  12.195  1.00 49.99           C  
ANISOU 1864  CE1 TYR A 323     5715   6948   6331   -505    112   -260       C  
ATOM   1865  CE2 TYR A 323     -39.240   9.183  10.624  1.00 49.49           C  
ANISOU 1865  CE2 TYR A 323     5767   6737   6300   -416     24   -371       C  
ATOM   1866  CZ  TYR A 323     -40.583   9.159  10.956  1.00 55.26           C  
ANISOU 1866  CZ  TYR A 323     6433   7505   7057   -482     44   -321       C  
ATOM   1867  OH  TYR A 323     -41.482   8.620  10.079  1.00 57.39           O  
ANISOU 1867  OH  TYR A 323     6682   7716   7407   -521     -7   -336       O  
ATOM   1868  N   ALA A 324     -39.131  13.148  15.228  1.00 47.51           N  
ANISOU 1868  N   ALA A 324     5354   6974   5725   -318    276   -406       N  
ATOM   1869  CA  ALA A 324     -40.360  13.823  15.650  1.00 48.33           C  
ANISOU 1869  CA  ALA A 324     5369   7187   5808   -318    320   -435       C  
ATOM   1870  C   ALA A 324     -40.380  15.269  15.179  1.00 52.86           C  
ANISOU 1870  C   ALA A 324     5919   7748   6417   -253    313   -557       C  
ATOM   1871  O   ALA A 324     -41.404  15.706  14.648  1.00 52.79           O  
ANISOU 1871  O   ALA A 324     5859   7744   6455   -257    318   -583       O  
ATOM   1872  CB  ALA A 324     -40.505  13.758  17.153  1.00 49.87           C  
ANISOU 1872  CB  ALA A 324     5510   7547   5892   -316    368   -401       C  
ATOM   1873  N   LEU A 325     -39.236  15.993  15.327  1.00 49.18           N  
ANISOU 1873  N   LEU A 325     5486   7256   5945   -197    292   -621       N  
ATOM   1874  CA  LEU A 325     -39.067  17.384  14.877  1.00 48.81           C  
ANISOU 1874  CA  LEU A 325     5414   7168   5964   -140    265   -719       C  
ATOM   1875  C   LEU A 325     -39.285  17.499  13.357  1.00 52.53           C  
ANISOU 1875  C   LEU A 325     5898   7534   6527   -155    231   -697       C  
ATOM   1876  O   LEU A 325     -40.002  18.394  12.908  1.00 53.50           O  
ANISOU 1876  O   LEU A 325     5966   7647   6714   -136    221   -741       O  
ATOM   1877  CB  LEU A 325     -37.657  17.922  15.248  1.00 48.37           C  
ANISOU 1877  CB  LEU A 325     5391   7085   5901    -95    235   -764       C  
ATOM   1878  CG  LEU A 325     -37.306  19.356  14.808  1.00 51.49           C  
ANISOU 1878  CG  LEU A 325     5755   7414   6395    -44    187   -848       C  
ATOM   1879  CD1 LEU A 325     -38.094  20.383  15.593  1.00 51.41           C  
ANISOU 1879  CD1 LEU A 325     5663   7474   6396      7    191   -964       C  
ATOM   1880  CD2 LEU A 325     -35.827  19.621  14.949  1.00 51.88           C  
ANISOU 1880  CD2 LEU A 325     5843   7416   6454    -22    149   -855       C  
ATOM   1881  N   MET A 326     -38.673  16.592  12.582  1.00 47.26           N  
ANISOU 1881  N   MET A 326     5295   6800   5861   -183    210   -635       N  
ATOM   1882  CA  MET A 326     -38.768  16.606  11.134  1.00 46.70           C  
ANISOU 1882  CA  MET A 326     5233   6664   5846   -189    176   -617       C  
ATOM   1883  C   MET A 326     -40.160  16.191  10.659  1.00 49.28           C  
ANISOU 1883  C   MET A 326     5525   7002   6197   -231    182   -600       C  
ATOM   1884  O   MET A 326     -40.698  16.859   9.775  1.00 48.96           O  
ANISOU 1884  O   MET A 326     5447   6948   6209   -221    163   -613       O  
ATOM   1885  CB  MET A 326     -37.667  15.762  10.484  1.00 49.10           C  
ANISOU 1885  CB  MET A 326     5605   6918   6132   -188    149   -583       C  
ATOM   1886  CG  MET A 326     -36.304  16.414  10.552  1.00 53.43           C  
ANISOU 1886  CG  MET A 326     6171   7454   6678   -145    134   -593       C  
ATOM   1887  SD  MET A 326     -36.130  18.037   9.725  1.00 59.52           S  
ANISOU 1887  SD  MET A 326     6882   8205   7528   -111    102   -604       S  
ATOM   1888  CE  MET A 326     -35.947  19.108  11.149  1.00 55.79           C  
ANISOU 1888  CE  MET A 326     6376   7743   7079    -83    105   -672       C  
ATOM   1889  N   ALA A 327     -40.772  15.165  11.273  1.00 44.79           N  
ANISOU 1889  N   ALA A 327     4956   6462   5599   -280    204   -559       N  
ATOM   1890  CA  ALA A 327     -42.132  14.748  10.916  1.00 45.30           C  
ANISOU 1890  CA  ALA A 327     4976   6539   5697   -328    206   -534       C  
ATOM   1891  C   ALA A 327     -43.134  15.874  11.195  1.00 49.58           C  
ANISOU 1891  C   ALA A 327     5432   7151   6257   -306    235   -578       C  
ATOM   1892  O   ALA A 327     -43.971  16.165  10.342  1.00 49.87           O  
ANISOU 1892  O   ALA A 327     5429   7174   6344   -315    217   -585       O  
ATOM   1893  CB  ALA A 327     -42.524  13.480  11.666  1.00 46.76           C  
ANISOU 1893  CB  ALA A 327     5162   6742   5863   -393    218   -457       C  
ATOM   1894  N   GLY A 328     -42.996  16.524  12.352  1.00 46.55           N  
ANISOU 1894  N   GLY A 328     5016   6843   5829   -269    272   -618       N  
ATOM   1895  CA  GLY A 328     -43.832  17.643  12.778  1.00 46.43           C  
ANISOU 1895  CA  GLY A 328     4912   6899   5829   -225    294   -690       C  
ATOM   1896  C   GLY A 328     -43.886  18.797  11.797  1.00 49.07           C  
ANISOU 1896  C   GLY A 328     5225   7159   6259   -182    250   -742       C  
ATOM   1897  O   GLY A 328     -44.981  19.245  11.452  1.00 49.05           O  
ANISOU 1897  O   GLY A 328     5154   7176   6307   -177    250   -760       O  
ATOM   1898  N   VAL A 329     -42.717  19.252  11.288  1.00 45.16           N  
ANISOU 1898  N   VAL A 329     4780   6582   5797   -155    209   -747       N  
ATOM   1899  CA  VAL A 329     -42.673  20.375  10.339  1.00 44.52           C  
ANISOU 1899  CA  VAL A 329     4667   6430   5817   -121    159   -761       C  
ATOM   1900  C   VAL A 329     -43.204  19.957   8.936  1.00 49.22           C  
ANISOU 1900  C   VAL A 329     5264   6998   6438   -159    135   -694       C  
ATOM   1901  O   VAL A 329     -43.669  20.818   8.189  1.00 49.22           O  
ANISOU 1901  O   VAL A 329     5211   6974   6518   -140    101   -690       O  
ATOM   1902  CB  VAL A 329     -41.296  21.091  10.248  1.00 47.48           C  
ANISOU 1902  CB  VAL A 329     5072   6739   6229    -87    118   -767       C  
ATOM   1903  CG1 VAL A 329     -40.918  21.741  11.572  1.00 47.31           C  
ANISOU 1903  CG1 VAL A 329     5030   6741   6206    -39    122   -862       C  
ATOM   1904  CG2 VAL A 329     -40.191  20.170   9.741  1.00 46.77           C  
ANISOU 1904  CG2 VAL A 329     5063   6629   6079   -114    115   -701       C  
ATOM   1905  N   VAL A 330     -43.141  18.655   8.586  1.00 45.68           N  
ANISOU 1905  N   VAL A 330     4872   6556   5930   -207    142   -647       N  
ATOM   1906  CA  VAL A 330     -43.681  18.156   7.320  1.00 45.92           C  
ANISOU 1906  CA  VAL A 330     4899   6575   5972   -236    111   -610       C  
ATOM   1907  C   VAL A 330     -45.217  18.057   7.468  1.00 51.96           C  
ANISOU 1907  C   VAL A 330     5597   7381   6764   -267    127   -616       C  
ATOM   1908  O   VAL A 330     -45.951  18.398   6.531  1.00 50.76           O  
ANISOU 1908  O   VAL A 330     5401   7231   6655   -269     97   -605       O  
ATOM   1909  CB  VAL A 330     -43.035  16.825   6.844  1.00 49.39           C  
ANISOU 1909  CB  VAL A 330     5415   6993   6359   -263     94   -585       C  
ATOM   1910  CG1 VAL A 330     -43.634  16.378   5.512  1.00 49.80           C  
ANISOU 1910  CG1 VAL A 330     5454   7047   6420   -282     50   -576       C  
ATOM   1911  CG2 VAL A 330     -41.521  16.973   6.702  1.00 47.96           C  
ANISOU 1911  CG2 VAL A 330     5284   6788   6148   -226     82   -579       C  
ATOM   1912  N   TRP A 331     -45.694  17.657   8.668  1.00 50.72           N  
ANISOU 1912  N   TRP A 331     5420   7275   6575   -287    175   -625       N  
ATOM   1913  CA  TRP A 331     -47.127  17.567   8.941  1.00 52.75           C  
ANISOU 1913  CA  TRP A 331     5598   7596   6850   -316    200   -621       C  
ATOM   1914  C   TRP A 331     -47.730  18.964   9.007  1.00 57.10           C  
ANISOU 1914  C   TRP A 331     6065   8172   7458   -256    201   -679       C  
ATOM   1915  O   TRP A 331     -48.918  19.119   8.737  1.00 58.75           O  
ANISOU 1915  O   TRP A 331     6201   8418   7705   -267    202   -678       O  
ATOM   1916  CB  TRP A 331     -47.439  16.750  10.205  1.00 52.64           C  
ANISOU 1916  CB  TRP A 331     5569   7658   6775   -356    253   -591       C  
ATOM   1917  CG  TRP A 331     -47.644  15.290   9.919  1.00 53.83           C  
ANISOU 1917  CG  TRP A 331     5751   7775   6927   -439    233   -513       C  
ATOM   1918  CD1 TRP A 331     -46.789  14.274  10.215  1.00 56.56           C  
ANISOU 1918  CD1 TRP A 331     6171   8076   7245   -470    222   -469       C  
ATOM   1919  CD2 TRP A 331     -48.753  14.692   9.218  1.00 54.19           C  
ANISOU 1919  CD2 TRP A 331     5754   7810   7027   -499    204   -477       C  
ATOM   1920  NE1 TRP A 331     -47.293  13.079   9.753  1.00 56.50           N  
ANISOU 1920  NE1 TRP A 331     6167   8018   7284   -544    182   -412       N  
ATOM   1921  CE2 TRP A 331     -48.499  13.306   9.139  1.00 58.16           C  
ANISOU 1921  CE2 TRP A 331     6306   8249   7543   -566    169   -418       C  
ATOM   1922  CE3 TRP A 331     -49.940  15.195   8.649  1.00 55.64           C  
ANISOU 1922  CE3 TRP A 331     5856   8026   7260   -502    195   -492       C  
ATOM   1923  CZ2 TRP A 331     -49.390  12.413   8.528  1.00 57.67           C  
ANISOU 1923  CZ2 TRP A 331     6215   8148   7550   -639    119   -380       C  
ATOM   1924  CZ3 TRP A 331     -50.810  14.314   8.028  1.00 57.41           C  
ANISOU 1924  CZ3 TRP A 331     6053   8227   7535   -575    154   -449       C  
ATOM   1925  CH2 TRP A 331     -50.534  12.940   7.972  1.00 58.32           C  
ANISOU 1925  CH2 TRP A 331     6218   8272   7670   -644    114   -398       C  
ATOM   1926  N   PHE A 332     -46.895  19.980   9.291  1.00 51.43           N  
ANISOU 1926  N   PHE A 332     5355   7421   6763   -192    189   -730       N  
ATOM   1927  CA  PHE A 332     -47.281  21.390   9.265  1.00 50.66           C  
ANISOU 1927  CA  PHE A 332     5182   7309   6758   -126    164   -793       C  
ATOM   1928  C   PHE A 332     -47.526  21.827   7.795  1.00 53.65           C  
ANISOU 1928  C   PHE A 332     5542   7623   7219   -131    104   -739       C  
ATOM   1929  O   PHE A 332     -48.488  22.552   7.530  1.00 54.55           O  
ANISOU 1929  O   PHE A 332     5574   7742   7411   -106     85   -757       O  
ATOM   1930  CB  PHE A 332     -46.217  22.276   9.943  1.00 51.69           C  
ANISOU 1930  CB  PHE A 332     5327   7400   6912    -64    147   -860       C  
ATOM   1931  CG  PHE A 332     -46.278  23.724   9.524  1.00 53.18           C  
ANISOU 1931  CG  PHE A 332     5455   7508   7243     -5     82   -899       C  
ATOM   1932  CD1 PHE A 332     -47.374  24.522   9.863  1.00 56.80           C  
ANISOU 1932  CD1 PHE A 332     5814   7991   7775     48     76   -979       C  
ATOM   1933  CD2 PHE A 332     -45.264  24.284   8.759  1.00 53.88           C  
ANISOU 1933  CD2 PHE A 332     5574   7497   7403     -1     23   -845       C  
ATOM   1934  CE1 PHE A 332     -47.450  25.847   9.435  1.00 57.90           C  
ANISOU 1934  CE1 PHE A 332     5892   8031   8076    103     -1  -1007       C  
ATOM   1935  CE2 PHE A 332     -45.332  25.616   8.349  1.00 56.99           C  
ANISOU 1935  CE2 PHE A 332     5900   7801   7953     44    -51   -853       C  
ATOM   1936  CZ  PHE A 332     -46.429  26.383   8.677  1.00 56.49           C  
ANISOU 1936  CZ  PHE A 332     5745   7738   7981     96    -67   -935       C  
ATOM   1937  N   VAL A 333     -46.663  21.391   6.854  1.00 47.73           N  
ANISOU 1937  N   VAL A 333     4860   6830   6445   -158     74   -672       N  
ATOM   1938  CA  VAL A 333     -46.828  21.689   5.425  1.00 46.88           C  
ANISOU 1938  CA  VAL A 333     4730   6701   6381   -163     20   -607       C  
ATOM   1939  C   VAL A 333     -48.180  21.101   4.919  1.00 51.64           C  
ANISOU 1939  C   VAL A 333     5291   7354   6977   -201     21   -595       C  
ATOM   1940  O   VAL A 333     -48.894  21.773   4.177  1.00 51.55           O  
ANISOU 1940  O   VAL A 333     5211   7343   7031   -187    -17   -569       O  
ATOM   1941  CB  VAL A 333     -45.635  21.179   4.595  1.00 48.68           C  
ANISOU 1941  CB  VAL A 333     5029   6917   6549   -175     -3   -549       C  
ATOM   1942  CG1 VAL A 333     -45.903  21.286   3.102  1.00 47.82           C  
ANISOU 1942  CG1 VAL A 333     4888   6836   6445   -180    -52   -481       C  
ATOM   1943  CG2 VAL A 333     -44.361  21.919   4.968  1.00 48.50           C  
ANISOU 1943  CG2 VAL A 333     5028   6847   6555   -140    -13   -545       C  
ATOM   1944  N   VAL A 334     -48.516  19.862   5.348  1.00 49.16           N  
ANISOU 1944  N   VAL A 334     5009   7074   6595   -253     56   -603       N  
ATOM   1945  CA  VAL A 334     -49.750  19.142   5.021  1.00 49.69           C  
ANISOU 1945  CA  VAL A 334     5035   7180   6664   -304     52   -590       C  
ATOM   1946  C   VAL A 334     -50.960  19.960   5.514  1.00 56.17           C  
ANISOU 1946  C   VAL A 334     5751   8046   7547   -280     73   -618       C  
ATOM   1947  O   VAL A 334     -51.946  20.079   4.785  1.00 56.67           O  
ANISOU 1947  O   VAL A 334     5752   8129   7653   -292     43   -600       O  
ATOM   1948  CB  VAL A 334     -49.735  17.695   5.595  1.00 52.95           C  
ANISOU 1948  CB  VAL A 334     5496   7601   7020   -369     77   -579       C  
ATOM   1949  CG1 VAL A 334     -51.072  16.988   5.358  1.00 53.27           C  
ANISOU 1949  CG1 VAL A 334     5477   7674   7088   -431     65   -558       C  
ATOM   1950  CG2 VAL A 334     -48.607  16.885   4.975  1.00 51.91           C  
ANISOU 1950  CG2 VAL A 334     5460   7419   6843   -378     43   -569       C  
ATOM   1951  N   LEU A 335     -50.852  20.548   6.726  1.00 54.65           N  
ANISOU 1951  N   LEU A 335     5532   7876   7356   -236    118   -673       N  
ATOM   1952  CA  LEU A 335     -51.852  21.421   7.350  1.00 56.29           C  
ANISOU 1952  CA  LEU A 335     5633   8137   7617   -187    139   -730       C  
ATOM   1953  C   LEU A 335     -52.137  22.623   6.432  1.00 60.87           C  
ANISOU 1953  C   LEU A 335     6158   8659   8312   -136     75   -731       C  
ATOM   1954  O   LEU A 335     -53.304  22.889   6.144  1.00 62.12           O  
ANISOU 1954  O   LEU A 335     6228   8853   8522   -131     65   -732       O  
ATOM   1955  CB  LEU A 335     -51.350  21.900   8.742  1.00 56.73           C  
ANISOU 1955  CB  LEU A 335     5683   8230   7642   -129    183   -814       C  
ATOM   1956  CG  LEU A 335     -52.370  22.492   9.734  1.00 62.97           C  
ANISOU 1956  CG  LEU A 335     6358   9131   8435    -75    227   -898       C  
ATOM   1957  CD1 LEU A 335     -51.739  22.694  11.096  1.00 63.73           C  
ANISOU 1957  CD1 LEU A 335     6462   9297   8457    -26    272   -980       C  
ATOM   1958  CD2 LEU A 335     -52.888  23.848   9.285  1.00 66.74           C  
ANISOU 1958  CD2 LEU A 335     6751   9560   9046      6    175   -963       C  
ATOM   1959  N   THR A 336     -51.076  23.330   5.967  1.00 56.29           N  
ANISOU 1959  N   THR A 336     5620   7991   7778   -104     26   -713       N  
ATOM   1960  CA  THR A 336     -51.188  24.515   5.103  1.00 56.26           C  
ANISOU 1960  CA  THR A 336     5558   7920   7899    -62    -46   -680       C  
ATOM   1961  C   THR A 336     -51.773  24.122   3.745  1.00 61.72           C  
ANISOU 1961  C   THR A 336     6233   8638   8581   -106    -84   -589       C  
ATOM   1962  O   THR A 336     -52.542  24.898   3.164  1.00 62.41           O  
ANISOU 1962  O   THR A 336     6236   8714   8762    -80   -130   -563       O  
ATOM   1963  CB  THR A 336     -49.836  25.245   4.938  1.00 56.96           C  
ANISOU 1963  CB  THR A 336     5687   7918   8039    -33    -90   -654       C  
ATOM   1964  OG1 THR A 336     -48.934  24.448   4.178  1.00 52.41           O  
ANISOU 1964  OG1 THR A 336     5194   7351   7370    -82    -92   -572       O  
ATOM   1965  CG2 THR A 336     -49.207  25.648   6.264  1.00 53.12           C  
ANISOU 1965  CG2 THR A 336     5214   7404   7564     14    -67   -758       C  
ATOM   1966  N   TYR A 337     -51.399  22.913   3.247  1.00 57.19           N  
ANISOU 1966  N   TYR A 337     5736   8098   7896   -167    -72   -550       N  
ATOM   1967  CA  TYR A 337     -51.885  22.341   1.997  1.00 56.64           C  
ANISOU 1967  CA  TYR A 337     5658   8071   7791   -206   -112   -491       C  
ATOM   1968  C   TYR A 337     -53.397  22.070   2.113  1.00 60.27           C  
ANISOU 1968  C   TYR A 337     6040   8581   8278   -231   -103   -514       C  
ATOM   1969  O   TYR A 337     -54.147  22.400   1.190  1.00 59.66           O  
ANISOU 1969  O   TYR A 337     5898   8528   8242   -228   -152   -474       O  
ATOM   1970  CB  TYR A 337     -51.118  21.045   1.646  1.00 57.25           C  
ANISOU 1970  CB  TYR A 337     5833   8166   7754   -252   -106   -486       C  
ATOM   1971  CG  TYR A 337     -51.663  20.326   0.426  1.00 59.29           C  
ANISOU 1971  CG  TYR A 337     6081   8477   7968   -286   -156   -462       C  
ATOM   1972  CD1 TYR A 337     -52.622  19.321   0.552  1.00 61.43           C  
ANISOU 1972  CD1 TYR A 337     6341   8770   8229   -342   -154   -495       C  
ATOM   1973  CD2 TYR A 337     -51.254  20.680  -0.855  1.00 60.31           C  
ANISOU 1973  CD2 TYR A 337     6197   8647   8069   -263   -212   -402       C  
ATOM   1974  CE1 TYR A 337     -53.154  18.684  -0.569  1.00 62.79           C  
ANISOU 1974  CE1 TYR A 337     6498   8988   8373   -369   -215   -493       C  
ATOM   1975  CE2 TYR A 337     -51.746  20.022  -1.980  1.00 62.13           C  
ANISOU 1975  CE2 TYR A 337     6413   8951   8244   -283   -265   -399       C  
ATOM   1976  CZ  TYR A 337     -52.704  19.029  -1.835  1.00 72.62           C  
ANISOU 1976  CZ  TYR A 337     7737  10283   9571   -334   -271   -457       C  
ATOM   1977  OH  TYR A 337     -53.217  18.414  -2.958  1.00 76.24           O  
ANISOU 1977  OH  TYR A 337     8173  10809   9985   -351   -337   -472       O  
ATOM   1978  N   ALA A 338     -53.825  21.452   3.234  1.00 56.38           N  
ANISOU 1978  N   ALA A 338     5547   8118   7757   -256    -41   -565       N  
ATOM   1979  CA  ALA A 338     -55.228  21.128   3.484  1.00 57.52           C  
ANISOU 1979  CA  ALA A 338     5605   8327   7921   -287    -22   -576       C  
ATOM   1980  C   ALA A 338     -56.067  22.381   3.530  1.00 62.97           C  
ANISOU 1980  C   ALA A 338     6185   9028   8712   -221    -36   -599       C  
ATOM   1981  O   ALA A 338     -57.166  22.381   2.990  1.00 65.02           O  
ANISOU 1981  O   ALA A 338     6367   9328   9010   -237    -62   -577       O  
ATOM   1982  CB  ALA A 338     -55.374  20.361   4.781  1.00 58.55           C  
ANISOU 1982  CB  ALA A 338     5742   8506   7998   -321     52   -603       C  
ATOM   1983  N   TRP A 339     -55.535  23.461   4.125  1.00 58.22           N  
ANISOU 1983  N   TRP A 339     5573   8383   8168   -144    -31   -647       N  
ATOM   1984  CA  TRP A 339     -56.200  24.751   4.198  1.00 57.98           C  
ANISOU 1984  CA  TRP A 339     5435   8333   8261    -65    -61   -686       C  
ATOM   1985  C   TRP A 339     -56.430  25.322   2.791  1.00 62.25           C  
ANISOU 1985  C   TRP A 339     5940   8829   8883    -60   -148   -598       C  
ATOM   1986  O   TRP A 339     -57.566  25.653   2.458  1.00 61.88           O  
ANISOU 1986  O   TRP A 339     5794   8813   8904    -44   -173   -592       O  
ATOM   1987  CB  TRP A 339     -55.404  25.739   5.076  1.00 56.14           C  
ANISOU 1987  CB  TRP A 339     5207   8036   8087     16    -61   -768       C  
ATOM   1988  CG  TRP A 339     -56.231  26.899   5.539  1.00 57.63           C  
ANISOU 1988  CG  TRP A 339     5276   8218   8404    110    -83   -857       C  
ATOM   1989  CD1 TRP A 339     -57.373  26.846   6.289  1.00 61.25           C  
ANISOU 1989  CD1 TRP A 339     5638   8784   8849    142    -33   -937       C  
ATOM   1990  CD2 TRP A 339     -55.995  28.281   5.264  1.00 57.65           C  
ANISOU 1990  CD2 TRP A 339     5230   8097   8577    189   -169   -874       C  
ATOM   1991  NE1 TRP A 339     -57.876  28.111   6.476  1.00 61.36           N  
ANISOU 1991  NE1 TRP A 339     5548   8754   9012    247    -83  -1023       N  
ATOM   1992  CE2 TRP A 339     -57.047  29.014   5.864  1.00 62.59           C  
ANISOU 1992  CE2 TRP A 339     5733   8752   9295    276   -173   -986       C  
ATOM   1993  CE3 TRP A 339     -54.991  28.977   4.572  1.00 58.47           C  
ANISOU 1993  CE3 TRP A 339     5371   8070   8776    194   -248   -798       C  
ATOM   1994  CZ2 TRP A 339     -57.123  30.409   5.794  1.00 62.81           C  
ANISOU 1994  CZ2 TRP A 339     5681   8658   9524    372   -265  -1038       C  
ATOM   1995  CZ3 TRP A 339     -55.058  30.362   4.520  1.00 60.95           C  
ANISOU 1995  CZ3 TRP A 339     5603   8264   9293    276   -339   -825       C  
ATOM   1996  CH2 TRP A 339     -56.116  31.063   5.121  1.00 62.83           C  
ANISOU 1996  CH2 TRP A 339     5726   8509   9637    366   -352   -951       C  
ATOM   1997  N   HIS A 340     -55.377  25.383   1.952  1.00 59.42           N  
ANISOU 1997  N   HIS A 340     5652   8420   8506    -76   -192   -519       N  
ATOM   1998  CA  HIS A 340     -55.488  25.901   0.584  1.00 60.14           C  
ANISOU 1998  CA  HIS A 340     5702   8501   8649    -74   -273   -411       C  
ATOM   1999  C   HIS A 340     -56.430  25.039  -0.311  1.00 63.50           C  
ANISOU 1999  C   HIS A 340     6103   9020   9005   -130   -289   -373       C  
ATOM   2000  O   HIS A 340     -57.311  25.597  -0.971  1.00 64.82           O  
ANISOU 2000  O   HIS A 340     6177   9205   9245   -112   -342   -327       O  
ATOM   2001  CB  HIS A 340     -54.089  26.021  -0.057  1.00 60.98           C  
ANISOU 2001  CB  HIS A 340     5879   8571   8720    -81   -305   -327       C  
ATOM   2002  CG  HIS A 340     -54.102  26.207  -1.546  1.00 65.29           C  
ANISOU 2002  CG  HIS A 340     6391   9165   9252    -94   -375   -197       C  
ATOM   2003  ND1 HIS A 340     -53.428  25.335  -2.385  1.00 66.99           N  
ANISOU 2003  ND1 HIS A 340     6672   9459   9321   -134   -377   -152       N  
ATOM   2004  CD2 HIS A 340     -54.753  27.126  -2.302  1.00 68.39           C  
ANISOU 2004  CD2 HIS A 340     6681   9554   9749    -68   -447   -107       C  
ATOM   2005  CE1 HIS A 340     -53.665  25.762  -3.616  1.00 67.27           C  
ANISOU 2005  CE1 HIS A 340     6643   9558   9360   -129   -444    -37       C  
ATOM   2006  NE2 HIS A 340     -54.456  26.838  -3.618  1.00 68.50           N  
ANISOU 2006  NE2 HIS A 340     6696   9663   9667    -95   -489      6       N  
ATOM   2007  N   THR A 341     -56.247  23.704  -0.326  1.00 57.62           N  
ANISOU 2007  N   THR A 341     5434   8324   8134   -194   -256   -395       N  
ATOM   2008  CA  THR A 341     -57.011  22.808  -1.192  1.00 56.86           C  
ANISOU 2008  CA  THR A 341     5322   8301   7979   -250   -287   -377       C  
ATOM   2009  C   THR A 341     -58.472  22.598  -0.747  1.00 58.80           C  
ANISOU 2009  C   THR A 341     5478   8589   8274   -271   -270   -413       C  
ATOM   2010  O   THR A 341     -59.302  22.338  -1.618  1.00 57.96           O  
ANISOU 2010  O   THR A 341     5317   8536   8169   -298   -321   -384       O  
ATOM   2011  CB  THR A 341     -56.297  21.484  -1.374  1.00 66.27           C  
ANISOU 2011  CB  THR A 341     6619   9508   9053   -305   -277   -401       C  
ATOM   2012  OG1 THR A 341     -56.276  20.790  -0.131  1.00 69.06           O  
ANISOU 2012  OG1 THR A 341     7011   9835   9394   -334   -206   -460       O  
ATOM   2013  CG2 THR A 341     -54.890  21.666  -1.928  1.00 64.20           C  
ANISOU 2013  CG2 THR A 341     6430   9234   8728   -279   -297   -362       C  
ATOM   2014  N   SER A 342     -58.801  22.737   0.562  1.00 54.21           N  
ANISOU 2014  N   SER A 342     4869   8003   7726   -256   -200   -474       N  
ATOM   2015  CA  SER A 342     -60.192  22.603   1.030  1.00 54.44           C  
ANISOU 2015  CA  SER A 342     4790   8098   7795   -271   -174   -500       C  
ATOM   2016  C   SER A 342     -61.051  23.749   0.504  1.00 59.53           C  
ANISOU 2016  C   SER A 342     5319   8749   8552   -208   -225   -482       C  
ATOM   2017  O   SER A 342     -62.228  23.538   0.211  1.00 60.09           O  
ANISOU 2017  O   SER A 342     5300   8882   8650   -232   -242   -470       O  
ATOM   2018  CB  SER A 342     -60.274  22.538   2.548  1.00 56.82           C  
ANISOU 2018  CB  SER A 342     5074   8432   8083   -256    -84   -565       C  
ATOM   2019  OG  SER A 342     -59.549  21.427   3.050  1.00 63.70           O  
ANISOU 2019  OG  SER A 342     6042   9301   8860   -321    -43   -561       O  
ATOM   2020  N   PHE A 343     -60.455  24.952   0.357  1.00 56.27           N  
ANISOU 2020  N   PHE A 343     4902   8261   8217   -130   -260   -471       N  
ATOM   2021  CA  PHE A 343     -61.116  26.103  -0.241  1.00 56.82           C  
ANISOU 2021  CA  PHE A 343     4865   8307   8416    -68   -328   -433       C  
ATOM   2022  C   PHE A 343     -61.210  25.892  -1.768  1.00 60.58           C  
ANISOU 2022  C   PHE A 343     5341   8818   8861   -108   -409   -322       C  
ATOM   2023  O   PHE A 343     -62.271  26.108  -2.360  1.00 60.46           O  
ANISOU 2023  O   PHE A 343     5227   8848   8896   -104   -456   -287       O  
ATOM   2024  CB  PHE A 343     -60.359  27.402   0.079  1.00 59.00           C  
ANISOU 2024  CB  PHE A 343     5135   8471   8809     18   -357   -445       C  
ATOM   2025  CG  PHE A 343     -60.470  27.951   1.481  1.00 61.11           C  
ANISOU 2025  CG  PHE A 343     5364   8715   9140     92   -306   -578       C  
ATOM   2026  CD1 PHE A 343     -61.710  28.174   2.061  1.00 65.34           C  
ANISOU 2026  CD1 PHE A 343     5783   9317   9728    137   -282   -655       C  
ATOM   2027  CD2 PHE A 343     -59.338  28.332   2.185  1.00 63.08           C  
ANISOU 2027  CD2 PHE A 343     5681   8886   9401    128   -292   -631       C  
ATOM   2028  CE1 PHE A 343     -61.812  28.703   3.351  1.00 67.14           C  
ANISOU 2028  CE1 PHE A 343     5962   9553   9996    223   -237   -796       C  
ATOM   2029  CE2 PHE A 343     -59.442  28.865   3.470  1.00 66.57           C  
ANISOU 2029  CE2 PHE A 343     6079   9323   9890    209   -255   -774       C  
ATOM   2030  CZ  PHE A 343     -60.680  29.053   4.045  1.00 65.39           C  
ANISOU 2030  CZ  PHE A 343     5812   9259   9776    261   -226   -862       C  
ATOM   2031  N   LYS A 344     -60.092  25.446  -2.394  1.00 56.92           N  
ANISOU 2031  N   LYS A 344     4979   8350   8299   -142   -425   -272       N  
ATOM   2032  CA  LYS A 344     -59.995  25.172  -3.833  1.00 56.74           C  
ANISOU 2032  CA  LYS A 344     4960   8394   8206   -171   -497   -179       C  
ATOM   2033  C   LYS A 344     -61.052  24.196  -4.284  1.00 60.30           C  
ANISOU 2033  C   LYS A 344     5377   8936   8599   -229   -514   -205       C  
ATOM   2034  O   LYS A 344     -61.578  24.355  -5.382  1.00 61.09           O  
ANISOU 2034  O   LYS A 344     5416   9104   8692   -229   -588   -140       O  
ATOM   2035  CB  LYS A 344     -58.604  24.616  -4.202  1.00 58.51           C  
ANISOU 2035  CB  LYS A 344     5300   8624   8308   -192   -490   -159       C  
ATOM   2036  CG  LYS A 344     -57.622  25.656  -4.740  1.00 79.72           C  
ANISOU 2036  CG  LYS A 344     7980  11278  11030   -148   -533    -47       C  
ATOM   2037  CD  LYS A 344     -57.748  25.851  -6.256  1.00 94.95           C  
ANISOU 2037  CD  LYS A 344     9852  13318  12909   -147   -615     78       C  
ATOM   2038  CE  LYS A 344     -56.787  26.879  -6.814  1.00107.39           C  
ANISOU 2038  CE  LYS A 344    11402  14880  14521   -114   -660    227       C  
ATOM   2039  NZ  LYS A 344     -57.120  28.268  -6.389  1.00115.48           N  
ANISOU 2039  NZ  LYS A 344    12337  15780  15758    -67   -697    287       N  
ATOM   2040  N   ALA A 345     -61.355  23.179  -3.440  1.00 55.49           N  
ANISOU 2040  N   ALA A 345     4801   8329   7953   -282   -454   -291       N  
ATOM   2041  CA  ALA A 345     -62.330  22.128  -3.716  1.00 54.76           C  
ANISOU 2041  CA  ALA A 345     4676   8301   7829   -352   -475   -319       C  
ATOM   2042  C   ALA A 345     -63.758  22.682  -3.789  1.00 59.83           C  
ANISOU 2042  C   ALA A 345     5177   8988   8570   -337   -499   -301       C  
ATOM   2043  O   ALA A 345     -64.593  22.091  -4.469  1.00 59.73           O  
ANISOU 2043  O   ALA A 345     5115   9039   8543   -385   -553   -295       O  
ATOM   2044  CB  ALA A 345     -62.235  21.038  -2.665  1.00 54.68           C  
ANISOU 2044  CB  ALA A 345     4721   8268   7786   -414   -406   -383       C  
ATOM   2045  N   LEU A 346     -64.027  23.831  -3.142  1.00 57.53           N  
ANISOU 2045  N   LEU A 346     4815   8660   8382   -264   -469   -302       N  
ATOM   2046  CA  LEU A 346     -65.349  24.466  -3.176  1.00 59.29           C  
ANISOU 2046  CA  LEU A 346     4894   8922   8711   -230   -492   -294       C  
ATOM   2047  C   LEU A 346     -65.567  25.305  -4.431  1.00 65.18           C  
ANISOU 2047  C   LEU A 346     5578   9680   9508   -189   -592   -200       C  
ATOM   2048  O   LEU A 346     -66.712  25.539  -4.808  1.00 64.89           O  
ANISOU 2048  O   LEU A 346     5426   9695   9534   -182   -634   -178       O  
ATOM   2049  CB  LEU A 346     -65.551  25.366  -1.945  1.00 59.81           C  
ANISOU 2049  CB  LEU A 346     4901   8949   8875   -151   -429   -357       C  
ATOM   2050  CG  LEU A 346     -65.762  24.681  -0.597  1.00 63.97           C  
ANISOU 2050  CG  LEU A 346     5430   9519   9357   -179   -326   -439       C  
ATOM   2051  CD1 LEU A 346     -65.631  25.691   0.536  1.00 64.28           C  
ANISOU 2051  CD1 LEU A 346     5431   9528   9466    -77   -273   -521       C  
ATOM   2052  CD2 LEU A 346     -67.124  23.997  -0.538  1.00 66.25           C  
ANISOU 2052  CD2 LEU A 346     5609   9912   9651   -235   -314   -436       C  
ATOM   2053  N   GLY A 347     -64.482  25.743  -5.065  1.00 64.28           N  
ANISOU 2053  N   GLY A 347     5528   9529   9365   -166   -631   -131       N  
ATOM   2054  CA  GLY A 347     -64.561  26.629  -6.218  1.00 66.60           C  
ANISOU 2054  CA  GLY A 347     5755   9844   9707   -126   -726     -9       C  
ATOM   2055  C   GLY A 347     -64.227  26.134  -7.604  1.00 74.97           C  
ANISOU 2055  C   GLY A 347     6840  11009  10635   -162   -797     73       C  
ATOM   2056  O   GLY A 347     -64.532  26.840  -8.566  1.00 76.85           O  
ANISOU 2056  O   GLY A 347     6993  11300  10907   -134   -878    186       O  
ATOM   2057  N   THR A 348     -63.590  24.963  -7.741  1.00 73.73           N  
ANISOU 2057  N   THR A 348     6790  10894  10329   -216   -773     17       N  
ATOM   2058  CA  THR A 348     -63.166  24.452  -9.057  1.00 75.91           C  
ANISOU 2058  CA  THR A 348     7091  11295  10458   -234   -841     65       C  
ATOM   2059  C   THR A 348     -62.919  22.935  -9.030  1.00 83.15           C  
ANISOU 2059  C   THR A 348     8102  12245  11247   -296   -824    -57       C  
ATOM   2060  O   THR A 348     -63.017  22.325  -7.969  1.00 82.24           O  
ANISOU 2060  O   THR A 348     8033  12047  11166   -333   -758   -149       O  
ATOM   2061  CB  THR A 348     -61.888  25.206  -9.540  1.00 85.63           C  
ANISOU 2061  CB  THR A 348     8353  12529  11653   -190   -854    182       C  
ATOM   2062  OG1 THR A 348     -61.581  24.815 -10.883  1.00 88.82           O  
ANISOU 2062  OG1 THR A 348     8750  13098  11898   -193   -921    238       O  
ATOM   2063  CG2 THR A 348     -60.670  25.007  -8.606  1.00 80.10           C  
ANISOU 2063  CG2 THR A 348     7771  11728  10936   -192   -773    126       C  
ATOM   2064  N   THR A 349     -62.577  22.347 -10.203  1.00 83.13           N  
ANISOU 2064  N   THR A 349     8118  12369  11100   -302   -892    -57       N  
ATOM   2065  CA  THR A 349     -62.254  20.932 -10.384  1.00 84.25           C  
ANISOU 2065  CA  THR A 349     8343  12540  11129   -346   -906   -184       C  
ATOM   2066  C   THR A 349     -60.943  20.723  -9.610  1.00 90.00           C  
ANISOU 2066  C   THR A 349     9192  13177  11827   -340   -827   -217       C  
ATOM   2067  O   THR A 349     -59.869  21.149 -10.049  1.00 90.57           O  
ANISOU 2067  O   THR A 349     9298  13295  11819   -296   -824   -157       O  
ATOM   2068  CB  THR A 349     -62.279  20.564 -11.901  1.00 95.37           C  
ANISOU 2068  CB  THR A 349     9717  14131  12390   -328  -1010   -187       C  
ATOM   2069  OG1 THR A 349     -63.429  19.754 -12.159  1.00 97.84           O  
ANISOU 2069  OG1 THR A 349     9979  14472  12724   -378  -1076   -276       O  
ATOM   2070  CG2 THR A 349     -61.022  19.842 -12.402  1.00 94.49           C  
ANISOU 2070  CG2 THR A 349     9699  14087  12116   -307  -1019   -254       C  
ATOM   2071  N   TYR A 350     -61.090  20.204  -8.380  1.00 86.93           N  
ANISOU 2071  N   TYR A 350     8849  12665  11514   -384   -760   -291       N  
ATOM   2072  CA  TYR A 350     -60.029  19.949  -7.408  1.00 86.45           C  
ANISOU 2072  CA  TYR A 350     8896  12507  11446   -387   -680   -327       C  
ATOM   2073  C   TYR A 350     -60.563  19.067  -6.290  1.00 91.70           C  
ANISOU 2073  C   TYR A 350     9582  13085  12176   -454   -634   -405       C  
ATOM   2074  O   TYR A 350     -61.492  19.469  -5.589  1.00 91.70           O  
ANISOU 2074  O   TYR A 350     9506  13061  12274   -468   -602   -388       O  
ATOM   2075  CB  TYR A 350     -59.466  21.263  -6.822  1.00 87.60           C  
ANISOU 2075  CB  TYR A 350     9035  12591  11658   -333   -623   -244       C  
ATOM   2076  CG  TYR A 350     -58.020  21.129  -6.408  1.00 89.88           C  
ANISOU 2076  CG  TYR A 350     9431  12832  11888   -316   -574   -254       C  
ATOM   2077  CD1 TYR A 350     -56.992  21.563  -7.242  1.00 92.13           C  
ANISOU 2077  CD1 TYR A 350     9731  13180  12094   -273   -601   -179       C  
ATOM   2078  CD2 TYR A 350     -57.671  20.501  -5.215  1.00 90.35           C  
ANISOU 2078  CD2 TYR A 350     9567  12798  11962   -346   -504   -329       C  
ATOM   2079  CE1 TYR A 350     -55.654  21.403  -6.885  1.00 92.71           C  
ANISOU 2079  CE1 TYR A 350     9895  13218  12113   -258   -557   -187       C  
ATOM   2080  CE2 TYR A 350     -56.338  20.304  -4.864  1.00 90.70           C  
ANISOU 2080  CE2 TYR A 350     9709  12804  11950   -331   -465   -341       C  
ATOM   2081  CZ  TYR A 350     -55.332  20.770  -5.694  1.00 99.83           C  
ANISOU 2081  CZ  TYR A 350    10879  14015  13036   -286   -491   -275       C  
ATOM   2082  OH  TYR A 350     -54.018  20.592  -5.330  1.00102.11           O  
ANISOU 2082  OH  TYR A 350    11254  14269  13273   -270   -452   -284       O  
ATOM   2083  N   GLN A 351     -59.986  17.864  -6.124  1.00 89.02           N  
ANISOU 2083  N   GLN A 351     9333  12706  11784   -493   -636   -482       N  
ATOM   2084  CA  GLN A 351     -60.421  16.923  -5.088  1.00 89.07           C  
ANISOU 2084  CA  GLN A 351     9355  12632  11857   -568   -601   -527       C  
ATOM   2085  C   GLN A 351     -59.850  17.344  -3.723  1.00 91.46           C  
ANISOU 2085  C   GLN A 351     9699  12864  12188   -555   -492   -503       C  
ATOM   2086  O   GLN A 351     -58.657  17.654  -3.634  1.00 89.88           O  
ANISOU 2086  O   GLN A 351     9577  12640  11932   -509   -463   -498       O  
ATOM   2087  CB  GLN A 351     -60.057  15.455  -5.414  1.00 90.97           C  
ANISOU 2087  CB  GLN A 351     9665  12838  12063   -617   -665   -616       C  
ATOM   2088  CG  GLN A 351     -59.487  15.188  -6.811  1.00110.30           C  
ANISOU 2088  CG  GLN A 351    12145  15366  14400   -569   -756   -674       C  
ATOM   2089  CD  GLN A 351     -57.979  15.291  -6.840  1.00130.05           C  
ANISOU 2089  CD  GLN A 351    14743  17863  16805   -509   -718   -681       C  
ATOM   2090  OE1 GLN A 351     -57.262  14.479  -6.242  1.00123.66           O  
ANISOU 2090  OE1 GLN A 351    14018  16966  16000   -529   -697   -731       O  
ATOM   2091  NE2 GLN A 351     -57.461  16.279  -7.560  1.00123.00           N  
ANISOU 2091  NE2 GLN A 351    13833  17070  15833   -438   -715   -618       N  
ATOM   2092  N   PRO A 352     -60.684  17.392  -2.656  1.00 88.32           N  
ANISOU 2092  N   PRO A 352     9238  12450  11868   -589   -433   -486       N  
ATOM   2093  CA  PRO A 352     -60.160  17.799  -1.338  1.00 91.54           C  
ANISOU 2093  CA  PRO A 352     9676  12819  12285   -567   -333   -478       C  
ATOM   2094  C   PRO A 352     -59.238  16.741  -0.731  1.00134.45           C  
ANISOU 2094  C   PRO A 352    15216  18192  17677   -610   -308   -502       C  
ATOM   2095  O   PRO A 352     -59.367  15.555  -1.030  1.00101.01           O  
ANISOU 2095  O   PRO A 352    11007  13930  13445   -675   -362   -524       O  
ATOM   2096  CB  PRO A 352     -61.422  17.983  -0.495  1.00 93.34           C  
ANISOU 2096  CB  PRO A 352     9788  13090  12586   -590   -285   -460       C  
ATOM   2097  CG  PRO A 352     -62.429  17.075  -1.118  1.00 97.23           C  
ANISOU 2097  CG  PRO A 352    10221  13608  13113   -669   -355   -455       C  
ATOM   2098  CD  PRO A 352     -62.125  17.059  -2.588  1.00 91.91           C  
ANISOU 2098  CD  PRO A 352     9582  12941  12397   -648   -455   -476       C  
ATOM   2099  N   GLY A 355     -56.506  16.094   2.134  1.00 94.22           N  
ANISOU 2099  N   GLY A 355    10337  12981  12482   -598   -128   -508       N  
ATOM   2100  CA  GLY A 355     -57.916  15.755   2.296  1.00 95.13           C  
ANISOU 2100  CA  GLY A 355    10347  13142  12656   -659   -131   -480       C  
ATOM   2101  C   GLY A 355     -58.321  14.423   1.690  1.00100.09           C  
ANISOU 2101  C   GLY A 355    10982  13729  13321   -747   -212   -476       C  
ATOM   2102  O   GLY A 355     -57.645  13.922   0.787  1.00 99.54           O  
ANISOU 2102  O   GLY A 355    10988  13608  13226   -739   -284   -521       O  
ATOM   2103  N   LYS A 356     -59.441  13.844   2.186  1.00 98.52           N  
ANISOU 2103  N   LYS A 356    10692  13557  13185   -828   -207   -427       N  
ATOM   2104  CA  LYS A 356     -60.058  12.571   1.755  1.00 99.80           C  
ANISOU 2104  CA  LYS A 356    10830  13668  13423   -928   -295   -412       C  
ATOM   2105  C   LYS A 356     -59.053  11.382   1.750  1.00104.77           C  
ANISOU 2105  C   LYS A 356    11569  14180  14059   -965   -348   -431       C  
ATOM   2106  O   LYS A 356     -58.119  11.373   2.554  1.00103.90           O  
ANISOU 2106  O   LYS A 356    11528  14049  13901   -943   -286   -413       O  
ATOM   2107  CB  LYS A 356     -60.724  12.729   0.372  1.00102.73           C  
ANISOU 2107  CB  LYS A 356    11159  14054  13818   -918   -391   -464       C  
ATOM   2108  N   THR A 357     -59.267  10.376   0.866  1.00102.49           N  
ANISOU 2108  N   THR A 357    11290  13813  13837  -1017   -469   -477       N  
ATOM   2109  CA  THR A 357     -58.402   9.198   0.754  1.00102.63           C  
ANISOU 2109  CA  THR A 357    11402  13705  13889  -1043   -543   -517       C  
ATOM   2110  C   THR A 357     -57.172   9.538  -0.119  1.00106.00           C  
ANISOU 2110  C   THR A 357    11936  14130  14210   -934   -565   -625       C  
ATOM   2111  O   THR A 357     -57.101   9.182  -1.302  1.00105.61           O  
ANISOU 2111  O   THR A 357    11906  14069  14154   -908   -669   -727       O  
ATOM   2112  CB  THR A 357     -59.174   7.961   0.256  1.00112.34           C  
ANISOU 2112  CB  THR A 357    12585  14841  15258  -1139   -678   -536       C  
ATOM   2113  OG1 THR A 357     -59.896   8.285  -0.934  1.00112.41           O  
ANISOU 2113  OG1 THR A 357    12544  14906  15263  -1116   -753   -614       O  
ATOM   2114  CG2 THR A 357     -60.114   7.389   1.311  1.00112.47           C  
ANISOU 2114  CG2 THR A 357    12501  14841  15391  -1263   -656   -392       C  
ATOM   2115  N   SER A 358     -56.217  10.258   0.494  1.00101.77           N  
ANISOU 2115  N   SER A 358    11458  13626  13585   -870   -466   -601       N  
ATOM   2116  CA  SER A 358     -54.934  10.665  -0.081  1.00100.54           C  
ANISOU 2116  CA  SER A 358    11393  13481  13327   -773   -463   -668       C  
ATOM   2117  C   SER A 358     -53.843  10.317   0.918  1.00102.04           C  
ANISOU 2117  C   SER A 358    11664  13608  13498   -769   -409   -640       C  
ATOM   2118  O   SER A 358     -53.946  10.662   2.098  1.00101.14           O  
ANISOU 2118  O   SER A 358    11528  13515  13385   -790   -318   -559       O  
ATOM   2119  CB  SER A 358     -54.935  12.151  -0.428  1.00104.47           C  
ANISOU 2119  CB  SER A 358    11860  14085  13750   -697   -405   -652       C  
ATOM   2120  OG  SER A 358     -55.885  12.429  -1.445  1.00115.26           O  
ANISOU 2120  OG  SER A 358    13154  15514  15125   -694   -467   -675       O  
ATOM   2121  N   TYR A 359     -52.836   9.569   0.464  1.00 98.03           N  
ANISOU 2121  N   TYR A 359    11239  13033  12973   -739   -469   -711       N  
ATOM   2122  CA  TYR A 359     -51.779   9.094   1.339  1.00 96.88           C  
ANISOU 2122  CA  TYR A 359    11170  12818  12822   -736   -434   -686       C  
ATOM   2123  C   TYR A 359     -50.476   9.852   1.116  1.00 95.82           C  
ANISOU 2123  C   TYR A 359    11104  12732  12572   -637   -387   -719       C  
ATOM   2124  O   TYR A 359     -49.506   9.331   0.556  1.00 95.41           O  
ANISOU 2124  O   TYR A 359    11117  12648  12485   -587   -436   -794       O  
ATOM   2125  CB  TYR A 359     -51.602   7.570   1.214  1.00100.16           C  
ANISOU 2125  CB  TYR A 359    11622  13098  13338   -782   -542   -729       C  
ATOM   2126  CG  TYR A 359     -52.758   6.807   1.830  1.00104.82           C  
ANISOU 2126  CG  TYR A 359    12138  13623  14067   -903   -575   -643       C  
ATOM   2127  CD1 TYR A 359     -52.735   6.428   3.171  1.00107.42           C  
ANISOU 2127  CD1 TYR A 359    12455  13918  14441   -970   -517   -512       C  
ATOM   2128  CD2 TYR A 359     -53.897   6.506   1.086  1.00106.89           C  
ANISOU 2128  CD2 TYR A 359    12327  13875  14409   -951   -662   -678       C  
ATOM   2129  CE1 TYR A 359     -53.812   5.759   3.754  1.00109.82           C  
ANISOU 2129  CE1 TYR A 359    12672  14186  14869  -1088   -542   -402       C  
ATOM   2130  CE2 TYR A 359     -54.981   5.841   1.659  1.00109.20           C  
ANISOU 2130  CE2 TYR A 359    12536  14114  14839  -1071   -693   -579       C  
ATOM   2131  CZ  TYR A 359     -54.932   5.464   2.993  1.00118.43           C  
ANISOU 2131  CZ  TYR A 359    13689  15256  16054  -1142   -631   -433       C  
ATOM   2132  OH  TYR A 359     -55.994   4.795   3.557  1.00122.18           O  
ANISOU 2132  OH  TYR A 359    14064  15696  16663  -1266   -661   -308       O  
ATOM   2133  N   PHE A 360     -50.468  11.108   1.611  1.00 87.96           N  
ANISOU 2133  N   PHE A 360    10083  11813  11524   -607   -293   -664       N  
ATOM   2134  CA  PHE A 360     -49.307  11.997   1.667  1.00 84.32           C  
ANISOU 2134  CA  PHE A 360     9668  11390  10978   -529   -239   -664       C  
ATOM   2135  C   PHE A 360     -48.423  11.498   2.804  1.00 83.58           C  
ANISOU 2135  C   PHE A 360     9638  11237  10881   -539   -198   -636       C  
ATOM   2136  O   PHE A 360     -47.256  11.887   2.894  1.00 83.90           O  
ANISOU 2136  O   PHE A 360     9731  11286  10861   -481   -170   -645       O  
ATOM   2137  CB  PHE A 360     -49.696  13.483   1.859  1.00 85.22           C  
ANISOU 2137  CB  PHE A 360     9723  11580  11077   -497   -176   -622       C  
ATOM   2138  CG  PHE A 360     -51.022  13.756   2.525  1.00 86.65           C  
ANISOU 2138  CG  PHE A 360     9819  11786  11317   -547   -142   -581       C  
ATOM   2139  CD1 PHE A 360     -51.234  13.417   3.856  1.00 89.45           C  
ANISOU 2139  CD1 PHE A 360    10163  12133  11691   -590    -84   -538       C  
ATOM   2140  CD2 PHE A 360     -52.053  14.371   1.826  1.00 89.42           C  
ANISOU 2140  CD2 PHE A 360    10090  12189  11696   -545   -166   -580       C  
ATOM   2141  CE1 PHE A 360     -52.471  13.650   4.464  1.00 91.06           C  
ANISOU 2141  CE1 PHE A 360    10271  12392  11935   -629    -47   -499       C  
ATOM   2142  CE2 PHE A 360     -53.285  14.621   2.439  1.00 92.77           C  
ANISOU 2142  CE2 PHE A 360    10425  12650  12175   -583   -133   -547       C  
ATOM   2143  CZ  PHE A 360     -53.483  14.260   3.753  1.00 90.87           C  
ANISOU 2143  CZ  PHE A 360    10169  12413  11945   -623    -70   -509       C  
ATOM   2144  N   HIS A 361     -48.993  10.594   3.655  1.00 74.84           N  
ANISOU 2144  N   HIS A 361     8518  10075   9845   -618   -201   -589       N  
ATOM   2145  CA  HIS A 361     -48.345   9.855   4.739  1.00 71.81           C  
ANISOU 2145  CA  HIS A 361     8179   9633   9474   -647   -180   -539       C  
ATOM   2146  C   HIS A 361     -46.988   9.322   4.280  1.00 70.60           C  
ANISOU 2146  C   HIS A 361     8117   9417   9292   -591   -224   -601       C  
ATOM   2147  O   HIS A 361     -46.041   9.299   5.055  1.00 69.52           O  
ANISOU 2147  O   HIS A 361     8027   9266   9120   -571   -184   -572       O  
ATOM   2148  CB  HIS A 361     -49.236   8.673   5.176  1.00 72.92           C  
ANISOU 2148  CB  HIS A 361     8278   9706   9722   -750   -225   -474       C  
ATOM   2149  CG  HIS A 361     -50.278   9.036   6.181  1.00 76.32           C  
ANISOU 2149  CG  HIS A 361     8618  10219  10161   -809   -151   -375       C  
ATOM   2150  ND1 HIS A 361     -50.039   8.920   7.541  1.00 77.97           N  
ANISOU 2150  ND1 HIS A 361     8817  10466  10343   -837    -83   -279       N  
ATOM   2151  CD2 HIS A 361     -51.534   9.501   5.994  1.00 78.08           C  
ANISOU 2151  CD2 HIS A 361     8748  10512  10408   -838   -138   -360       C  
ATOM   2152  CE1 HIS A 361     -51.151   9.318   8.135  1.00 77.73           C  
ANISOU 2152  CE1 HIS A 361     8683  10539  10309   -876    -27   -215       C  
ATOM   2153  NE2 HIS A 361     -52.077   9.681   7.246  1.00 78.23           N  
ANISOU 2153  NE2 HIS A 361     8695  10619  10410   -878    -57   -262       N  
ATOM   2154  N   LEU A 362     -46.911   8.913   3.002  1.00 65.32           N  
ANISOU 2154  N   LEU A 362     7463   8727   8630   -559   -310   -694       N  
ATOM   2155  CA  LEU A 362     -45.721   8.401   2.352  1.00 65.20           C  
ANISOU 2155  CA  LEU A 362     7515   8680   8579   -489   -361   -779       C  
ATOM   2156  C   LEU A 362     -44.605   9.438   2.407  1.00 67.84           C  
ANISOU 2156  C   LEU A 362     7879   9094   8803   -412   -289   -770       C  
ATOM   2157  O   LEU A 362     -43.522   9.102   2.857  1.00 67.16           O  
ANISOU 2157  O   LEU A 362     7849   8971   8697   -382   -280   -772       O  
ATOM   2158  CB  LEU A 362     -46.037   8.000   0.909  1.00 66.35           C  
ANISOU 2158  CB  LEU A 362     7644   8843   8724   -455   -459   -895       C  
ATOM   2159  CG  LEU A 362     -45.243   6.825   0.349  1.00 72.64           C  
ANISOU 2159  CG  LEU A 362     8492   9567   9542   -405   -556  -1011       C  
ATOM   2160  CD1 LEU A 362     -45.593   5.524   1.063  1.00 74.03           C  
ANISOU 2160  CD1 LEU A 362     8681   9572   9875   -482   -626   -992       C  
ATOM   2161  CD2 LEU A 362     -45.508   6.668  -1.129  1.00 77.27           C  
ANISOU 2161  CD2 LEU A 362     9048  10224  10085   -348   -643  -1143       C  
ATOM   2162  N   LEU A 363     -44.890  10.706   2.054  1.00 63.82           N  
ANISOU 2162  N   LEU A 363     7325   8684   8241   -388   -241   -745       N  
ATOM   2163  CA  LEU A 363     -43.907  11.778   2.141  1.00 62.85           C  
ANISOU 2163  CA  LEU A 363     7214   8622   8044   -328   -184   -718       C  
ATOM   2164  C   LEU A 363     -43.606  12.173   3.606  1.00 63.98           C  
ANISOU 2164  C   LEU A 363     7372   8740   8199   -350   -109   -655       C  
ATOM   2165  O   LEU A 363     -42.441  12.403   3.951  1.00 63.82           O  
ANISOU 2165  O   LEU A 363     7392   8720   8137   -309    -83   -648       O  
ATOM   2166  CB  LEU A 363     -44.376  13.022   1.357  1.00 63.31           C  
ANISOU 2166  CB  LEU A 363     7207   8775   8074   -301   -174   -697       C  
ATOM   2167  CG  LEU A 363     -43.308  14.130   1.180  1.00 68.27           C  
ANISOU 2167  CG  LEU A 363     7832   9460   8648   -242   -138   -656       C  
ATOM   2168  CD1 LEU A 363     -42.184  13.676   0.268  1.00 69.33           C  
ANISOU 2168  CD1 LEU A 363     7994   9648   8700   -180   -172   -692       C  
ATOM   2169  CD2 LEU A 363     -43.911  15.424   0.675  1.00 69.75           C  
ANISOU 2169  CD2 LEU A 363     7943   9709   8852   -234   -131   -603       C  
ATOM   2170  N   THR A 364     -44.653  12.275   4.444  1.00 57.15           N  
ANISOU 2170  N   THR A 364     6463   7871   7381   -408    -76   -613       N  
ATOM   2171  CA  THR A 364     -44.554  12.747   5.829  1.00 55.23           C  
ANISOU 2171  CA  THR A 364     6211   7644   7128   -419     -5   -566       C  
ATOM   2172  C   THR A 364     -43.721  11.849   6.725  1.00 55.20           C  
ANISOU 2172  C   THR A 364     6267   7593   7114   -434      2   -540       C  
ATOM   2173  O   THR A 364     -43.080  12.349   7.633  1.00 52.12           O  
ANISOU 2173  O   THR A 364     5890   7231   6684   -412     51   -522       O  
ATOM   2174  CB  THR A 364     -45.940  12.962   6.449  1.00 62.65           C  
ANISOU 2174  CB  THR A 364     7073   8625   8105   -470     28   -531       C  
ATOM   2175  OG1 THR A 364     -46.559  11.701   6.733  1.00 65.47           O  
ANISOU 2175  OG1 THR A 364     7424   8940   8511   -546      1   -491       O  
ATOM   2176  CG2 THR A 364     -46.826  13.824   5.588  1.00 60.10           C  
ANISOU 2176  CG2 THR A 364     6686   8344   7806   -455     16   -553       C  
ATOM   2177  N   TRP A 365     -43.754  10.542   6.506  1.00 53.22           N  
ANISOU 2177  N   TRP A 365     6046   7266   6909   -470    -57   -539       N  
ATOM   2178  CA  TRP A 365     -42.975   9.640   7.341  1.00 52.95           C  
ANISOU 2178  CA  TRP A 365     6062   7173   6883   -485    -63   -499       C  
ATOM   2179  C   TRP A 365     -41.607   9.321   6.680  1.00 55.52           C  
ANISOU 2179  C   TRP A 365     6459   7455   7182   -416   -104   -563       C  
ATOM   2180  O   TRP A 365     -40.631   9.112   7.402  1.00 54.57           O  
ANISOU 2180  O   TRP A 365     6380   7316   7037   -398    -88   -536       O  
ATOM   2181  CB  TRP A 365     -43.790   8.369   7.676  1.00 52.70           C  
ANISOU 2181  CB  TRP A 365     6009   7067   6948   -573   -112   -439       C  
ATOM   2182  CG  TRP A 365     -45.122   8.679   8.327  1.00 54.32           C  
ANISOU 2182  CG  TRP A 365     6128   7341   7169   -641    -65   -364       C  
ATOM   2183  CD1 TRP A 365     -46.361   8.451   7.801  1.00 57.94           C  
ANISOU 2183  CD1 TRP A 365     6526   7791   7699   -697   -101   -359       C  
ATOM   2184  CD2 TRP A 365     -45.340   9.364   9.581  1.00 53.71           C  
ANISOU 2184  CD2 TRP A 365     6005   7376   7027   -650     27   -297       C  
ATOM   2185  NE1 TRP A 365     -47.337   8.946   8.642  1.00 57.68           N  
ANISOU 2185  NE1 TRP A 365     6408   7859   7648   -740    -32   -283       N  
ATOM   2186  CE2 TRP A 365     -46.740   9.507   9.742  1.00 58.26           C  
ANISOU 2186  CE2 TRP A 365     6488   8015   7634   -707     47   -251       C  
ATOM   2187  CE3 TRP A 365     -44.489   9.879  10.576  1.00 53.87           C  
ANISOU 2187  CE3 TRP A 365     6046   7461   6960   -608     89   -283       C  
ATOM   2188  CZ2 TRP A 365     -47.308  10.107  10.875  1.00 57.24           C  
ANISOU 2188  CZ2 TRP A 365     6282   8023   7442   -717    132   -196       C  
ATOM   2189  CZ3 TRP A 365     -45.052  10.496  11.683  1.00 55.35           C  
ANISOU 2189  CZ3 TRP A 365     6163   7780   7087   -616    166   -239       C  
ATOM   2190  CH2 TRP A 365     -46.445  10.601  11.829  1.00 56.70           C  
ANISOU 2190  CH2 TRP A 365     6237   8025   7281   -666    190   -198       C  
ATOM   2191  N   SER A 366     -41.527   9.361   5.330  1.00 51.28           N  
ANISOU 2191  N   SER A 366     5924   6925   6634   -370   -154   -645       N  
ATOM   2192  CA  SER A 366     -40.320   9.043   4.547  1.00 51.23           C  
ANISOU 2192  CA  SER A 366     5965   6913   6588   -292   -194   -716       C  
ATOM   2193  C   SER A 366     -39.240  10.108   4.603  1.00 53.69           C  
ANISOU 2193  C   SER A 366     6284   7303   6813   -231   -137   -702       C  
ATOM   2194  O   SER A 366     -38.064   9.755   4.726  1.00 52.55           O  
ANISOU 2194  O   SER A 366     6182   7143   6641   -186   -143   -717       O  
ATOM   2195  CB  SER A 366     -40.665   8.812   3.075  1.00 55.88           C  
ANISOU 2195  CB  SER A 366     6534   7527   7169   -256   -264   -811       C  
ATOM   2196  OG  SER A 366     -41.327   7.571   2.904  1.00 71.30           O  
ANISOU 2196  OG  SER A 366     8489   9379   9222   -300   -347   -851       O  
ATOM   2197  N   LEU A 367     -39.617  11.387   4.383  1.00 50.44           N  
ANISOU 2197  N   LEU A 367     5825   6970   6372   -227    -94   -676       N  
ATOM   2198  CA  LEU A 367     -38.686  12.512   4.374  1.00 50.65           C  
ANISOU 2198  CA  LEU A 367     5841   7056   6347   -179    -54   -650       C  
ATOM   2199  C   LEU A 367     -37.908  12.559   5.726  1.00 54.72           C  
ANISOU 2199  C   LEU A 367     6392   7538   6859   -185    -14   -616       C  
ATOM   2200  O   LEU A 367     -36.677  12.536   5.666  1.00 55.78           O  
ANISOU 2200  O   LEU A 367     6555   7682   6957   -139    -15   -619       O  
ATOM   2201  CB  LEU A 367     -39.419  13.829   4.071  1.00 51.30           C  
ANISOU 2201  CB  LEU A 367     5857   7193   6441   -186    -32   -619       C  
ATOM   2202  CG  LEU A 367     -38.564  15.028   3.646  1.00 57.41           C  
ANISOU 2202  CG  LEU A 367     6600   8024   7189   -140    -20   -581       C  
ATOM   2203  CD1 LEU A 367     -39.231  15.784   2.508  1.00 58.16           C  
ANISOU 2203  CD1 LEU A 367     6627   8185   7286   -131    -43   -556       C  
ATOM   2204  CD2 LEU A 367     -38.314  15.974   4.828  1.00 60.77           C  
ANISOU 2204  CD2 LEU A 367     7016   8421   7653   -148     20   -552       C  
ATOM   2205  N   PRO A 368     -38.558  12.504   6.928  1.00 50.10           N  
ANISOU 2205  N   PRO A 368     5803   6931   6302   -235     19   -583       N  
ATOM   2206  CA  PRO A 368     -37.784  12.462   8.182  1.00 49.48           C  
ANISOU 2206  CA  PRO A 368     5754   6847   6200   -234     51   -554       C  
ATOM   2207  C   PRO A 368     -36.977  11.172   8.357  1.00 51.81           C  
ANISOU 2207  C   PRO A 368     6107   7080   6496   -229     17   -548       C  
ATOM   2208  O   PRO A 368     -35.909  11.221   8.971  1.00 50.38           O  
ANISOU 2208  O   PRO A 368     5955   6903   6283   -201     29   -535       O  
ATOM   2209  CB  PRO A 368     -38.868  12.549   9.258  1.00 51.29           C  
ANISOU 2209  CB  PRO A 368     5944   7101   6441   -286     89   -520       C  
ATOM   2210  CG  PRO A 368     -40.046  13.063   8.563  1.00 55.07           C  
ANISOU 2210  CG  PRO A 368     6368   7602   6953   -303     87   -537       C  
ATOM   2211  CD  PRO A 368     -40.002  12.501   7.229  1.00 50.68           C  
ANISOU 2211  CD  PRO A 368     5832   7011   6416   -293     31   -566       C  
ATOM   2212  N   PHE A 369     -37.473  10.029   7.809  1.00 47.80           N  
ANISOU 2212  N   PHE A 369     5612   6509   6039   -253    -37   -563       N  
ATOM   2213  CA  PHE A 369     -36.785   8.733   7.902  1.00 47.85           C  
ANISOU 2213  CA  PHE A 369     5669   6432   6081   -244    -91   -567       C  
ATOM   2214  C   PHE A 369     -35.446   8.753   7.143  1.00 51.36           C  
ANISOU 2214  C   PHE A 369     6143   6891   6480   -157   -112   -631       C  
ATOM   2215  O   PHE A 369     -34.408   8.351   7.673  1.00 51.81           O  
ANISOU 2215  O   PHE A 369     6236   6923   6528   -128   -117   -616       O  
ATOM   2216  CB  PHE A 369     -37.670   7.599   7.375  1.00 50.19           C  
ANISOU 2216  CB  PHE A 369     5960   6641   6469   -286   -163   -588       C  
ATOM   2217  CG  PHE A 369     -37.067   6.225   7.564  1.00 52.85           C  
ANISOU 2217  CG  PHE A 369     6340   6860   6881   -280   -237   -590       C  
ATOM   2218  CD1 PHE A 369     -36.347   5.615   6.541  1.00 55.78           C  
ANISOU 2218  CD1 PHE A 369     6738   7188   7266   -204   -308   -701       C  
ATOM   2219  CD2 PHE A 369     -37.236   5.530   8.758  1.00 56.31           C  
ANISOU 2219  CD2 PHE A 369     6781   7237   7378   -346   -241   -480       C  
ATOM   2220  CE1 PHE A 369     -35.783   4.349   6.720  1.00 57.86           C  
ANISOU 2220  CE1 PHE A 369     7036   7326   7621   -189   -390   -717       C  
ATOM   2221  CE2 PHE A 369     -36.670   4.260   8.935  1.00 60.13           C  
ANISOU 2221  CE2 PHE A 369     7297   7592   7956   -342   -322   -468       C  
ATOM   2222  CZ  PHE A 369     -35.951   3.678   7.914  1.00 58.02           C  
ANISOU 2222  CZ  PHE A 369     7063   7259   7723   -261   -400   -595       C  
ATOM   2223  N   VAL A 370     -35.493   9.240   5.915  1.00 46.11           N  
ANISOU 2223  N   VAL A 370     5453   6287   5780   -114   -124   -691       N  
ATOM   2224  CA  VAL A 370     -34.386   9.329   4.990  1.00 45.42           C  
ANISOU 2224  CA  VAL A 370     5367   6257   5632    -28   -140   -746       C  
ATOM   2225  C   VAL A 370     -33.356  10.314   5.543  1.00 48.41           C  
ANISOU 2225  C   VAL A 370     5742   6691   5959     -6    -84   -690       C  
ATOM   2226  O   VAL A 370     -32.172  10.003   5.481  1.00 47.69           O  
ANISOU 2226  O   VAL A 370     5671   6611   5839     49    -94   -706       O  
ATOM   2227  CB  VAL A 370     -34.947   9.678   3.580  1.00 49.03           C  
ANISOU 2227  CB  VAL A 370     5778   6800   6051      1   -162   -800       C  
ATOM   2228  CG1 VAL A 370     -33.928  10.338   2.695  1.00 48.77           C  
ANISOU 2228  CG1 VAL A 370     5715   6889   5925     82   -152   -813       C  
ATOM   2229  CG2 VAL A 370     -35.513   8.439   2.899  1.00 49.42           C  
ANISOU 2229  CG2 VAL A 370     5838   6790   6151      5   -243   -892       C  
ATOM   2230  N   LEU A 371     -33.796  11.439   6.162  1.00 44.78           N  
ANISOU 2230  N   LEU A 371     5254   6258   5502    -47    -34   -634       N  
ATOM   2231  CA  LEU A 371     -32.885  12.410   6.779  1.00 43.93           C  
ANISOU 2231  CA  LEU A 371     5136   6185   5370    -32      2   -592       C  
ATOM   2232  C   LEU A 371     -32.178  11.823   8.028  1.00 47.05           C  
ANISOU 2232  C   LEU A 371     5578   6534   5766    -37      9   -572       C  
ATOM   2233  O   LEU A 371     -30.958  11.936   8.146  1.00 47.12           O  
ANISOU 2233  O   LEU A 371     5595   6561   5746      4      9   -565       O  
ATOM   2234  CB  LEU A 371     -33.624  13.709   7.142  1.00 43.79           C  
ANISOU 2234  CB  LEU A 371     5071   6189   5377    -66     35   -563       C  
ATOM   2235  CG  LEU A 371     -33.935  14.653   5.977  1.00 47.93           C  
ANISOU 2235  CG  LEU A 371     5535   6770   5906    -52     27   -550       C  
ATOM   2236  CD1 LEU A 371     -34.870  15.769   6.422  1.00 48.06           C  
ANISOU 2236  CD1 LEU A 371     5506   6779   5976    -84     45   -535       C  
ATOM   2237  CD2 LEU A 371     -32.650  15.240   5.378  1.00 48.44           C  
ANISOU 2237  CD2 LEU A 371     5572   6891   5942     -6     21   -514       C  
ATOM   2238  N   THR A 372     -32.936  11.152   8.911  1.00 43.52           N  
ANISOU 2238  N   THR A 372     5151   6037   5347    -89     10   -551       N  
ATOM   2239  CA  THR A 372     -32.442  10.503  10.133  1.00 42.92           C  
ANISOU 2239  CA  THR A 372     5108   5930   5267   -103     13   -508       C  
ATOM   2240  C   THR A 372     -31.386   9.420   9.805  1.00 45.07           C  
ANISOU 2240  C   THR A 372     5423   6149   5551    -56    -35   -525       C  
ATOM   2241  O   THR A 372     -30.352   9.365  10.478  1.00 44.87           O  
ANISOU 2241  O   THR A 372     5417   6130   5501    -31    -32   -500       O  
ATOM   2242  CB  THR A 372     -33.629   9.899  10.940  1.00 48.46           C  
ANISOU 2242  CB  THR A 372     5802   6609   6001   -175     19   -457       C  
ATOM   2243  OG1 THR A 372     -34.585  10.925  11.245  1.00 45.57           O  
ANISOU 2243  OG1 THR A 372     5388   6309   5620   -203     65   -458       O  
ATOM   2244  CG2 THR A 372     -33.185   9.251  12.248  1.00 47.21           C  
ANISOU 2244  CG2 THR A 372     5664   6445   5829   -196     23   -384       C  
ATOM   2245  N   VAL A 373     -31.637   8.583   8.780  1.00 39.84           N  
ANISOU 2245  N   VAL A 373     4771   5438   4929    -37    -87   -578       N  
ATOM   2246  CA  VAL A 373     -30.722   7.504   8.409  1.00 40.53           C  
ANISOU 2246  CA  VAL A 373     4890   5467   5041     22   -145   -621       C  
ATOM   2247  C   VAL A 373     -29.400   8.092   7.818  1.00 46.51           C  
ANISOU 2247  C   VAL A 373     5635   6312   5726    105   -129   -657       C  
ATOM   2248  O   VAL A 373     -28.322   7.517   8.043  1.00 47.35           O  
ANISOU 2248  O   VAL A 373     5763   6396   5833    155   -153   -663       O  
ATOM   2249  CB  VAL A 373     -31.410   6.455   7.466  1.00 44.48           C  
ANISOU 2249  CB  VAL A 373     5395   5893   5613     30   -220   -698       C  
ATOM   2250  CG1 VAL A 373     -30.414   5.425   6.937  1.00 44.57           C  
ANISOU 2250  CG1 VAL A 373     5430   5851   5653    116   -291   -779       C  
ATOM   2251  CG2 VAL A 373     -32.562   5.739   8.185  1.00 44.12           C  
ANISOU 2251  CG2 VAL A 373     5354   5749   5663    -63   -246   -635       C  
ATOM   2252  N   ALA A 374     -29.478   9.245   7.111  1.00 42.85           N  
ANISOU 2252  N   ALA A 374     5126   5947   5208    117    -93   -663       N  
ATOM   2253  CA  ALA A 374     -28.298   9.873   6.513  1.00 42.20           C  
ANISOU 2253  CA  ALA A 374     5009   5962   5060    182    -77   -666       C  
ATOM   2254  C   ALA A 374     -27.368  10.354   7.606  1.00 46.40           C  
ANISOU 2254  C   ALA A 374     5549   6495   5584    175    -50   -605       C  
ATOM   2255  O   ALA A 374     -26.169  10.100   7.515  1.00 47.27           O  
ANISOU 2255  O   ALA A 374     5656   6634   5668    233    -60   -612       O  
ATOM   2256  CB  ALA A 374     -28.700  11.020   5.597  1.00 42.67           C  
ANISOU 2256  CB  ALA A 374     5008   6120   5085    178    -51   -650       C  
ATOM   2257  N   ILE A 375     -27.936  10.944   8.688  1.00 41.67           N  
ANISOU 2257  N   ILE A 375     4957   5871   5007    109    -21   -558       N  
ATOM   2258  CA  ILE A 375     -27.211  11.451   9.857  1.00 40.35           C  
ANISOU 2258  CA  ILE A 375     4792   5711   4827     99     -3   -517       C  
ATOM   2259  C   ILE A 375     -26.526  10.294  10.566  1.00 47.08           C  
ANISOU 2259  C   ILE A 375     5692   6514   5684    118    -30   -505       C  
ATOM   2260  O   ILE A 375     -25.329  10.389  10.866  1.00 49.35           O  
ANISOU 2260  O   ILE A 375     5977   6825   5950    155    -35   -491       O  
ATOM   2261  CB  ILE A 375     -28.140  12.250  10.817  1.00 41.68           C  
ANISOU 2261  CB  ILE A 375     4947   5882   5006     39     26   -498       C  
ATOM   2262  CG1 ILE A 375     -28.733  13.484  10.096  1.00 40.70           C  
ANISOU 2262  CG1 ILE A 375     4770   5792   4902     29     40   -507       C  
ATOM   2263  CG2 ILE A 375     -27.381  12.646  12.102  1.00 39.84           C  
ANISOU 2263  CG2 ILE A 375     4717   5669   4750     39     33   -477       C  
ATOM   2264  CD1 ILE A 375     -29.866  14.153  10.798  1.00 42.88           C  
ANISOU 2264  CD1 ILE A 375     5026   6068   5198    -16     62   -515       C  
ATOM   2265  N   LEU A 376     -27.269   9.196  10.807  1.00 42.61           N  
ANISOU 2265  N   LEU A 376     5159   5872   5157     90    -55   -500       N  
ATOM   2266  CA  LEU A 376     -26.720   7.995  11.428  1.00 42.20           C  
ANISOU 2266  CA  LEU A 376     5146   5751   5137    103    -96   -471       C  
ATOM   2267  C   LEU A 376     -25.609   7.397  10.590  1.00 46.51           C  
ANISOU 2267  C   LEU A 376     5698   6285   5690    191   -136   -528       C  
ATOM   2268  O   LEU A 376     -24.639   6.916  11.149  1.00 47.83           O  
ANISOU 2268  O   LEU A 376     5881   6432   5862    223   -158   -504       O  
ATOM   2269  CB  LEU A 376     -27.812   6.942  11.655  1.00 42.66           C  
ANISOU 2269  CB  LEU A 376     5224   5717   5268     48   -129   -443       C  
ATOM   2270  CG  LEU A 376     -28.901   7.285  12.706  1.00 46.24           C  
ANISOU 2270  CG  LEU A 376     5661   6201   5708    -38    -89   -365       C  
ATOM   2271  CD1 LEU A 376     -29.953   6.203  12.740  1.00 47.05           C  
ANISOU 2271  CD1 LEU A 376     5766   6213   5897    -96   -129   -322       C  
ATOM   2272  CD2 LEU A 376     -28.308   7.492  14.117  1.00 45.42           C  
ANISOU 2272  CD2 LEU A 376     5557   6153   5548    -50    -65   -289       C  
ATOM   2273  N   ALA A 377     -25.734   7.424   9.254  1.00 42.94           N  
ANISOU 2273  N   ALA A 377     5224   5863   5228    236   -147   -607       N  
ATOM   2274  CA  ALA A 377     -24.722   6.840   8.384  1.00 42.55           C  
ANISOU 2274  CA  ALA A 377     5165   5835   5168    336   -184   -681       C  
ATOM   2275  C   ALA A 377     -23.444   7.677   8.365  1.00 45.61           C  
ANISOU 2275  C   ALA A 377     5513   6332   5484    381   -148   -655       C  
ATOM   2276  O   ALA A 377     -22.367   7.095   8.284  1.00 43.90           O  
ANISOU 2276  O   ALA A 377     5294   6122   5263    455   -175   -681       O  
ATOM   2277  CB  ALA A 377     -25.265   6.675   6.978  1.00 43.48           C  
ANISOU 2277  CB  ALA A 377     5258   5992   5273    377   -206   -777       C  
ATOM   2278  N   VAL A 378     -23.561   9.036   8.477  1.00 41.42           N  
ANISOU 2278  N   VAL A 378     4946   5877   4913    335    -95   -600       N  
ATOM   2279  CA  VAL A 378     -22.404   9.942   8.439  1.00 39.92           C  
ANISOU 2279  CA  VAL A 378     4706   5783   4680    362    -70   -560       C  
ATOM   2280  C   VAL A 378     -21.860  10.168   9.871  1.00 45.13           C  
ANISOU 2280  C   VAL A 378     5387   6405   5354    327    -67   -504       C  
ATOM   2281  O   VAL A 378     -20.857  10.863  10.053  1.00 44.70           O  
ANISOU 2281  O   VAL A 378     5293   6410   5282    342    -59   -469       O  
ATOM   2282  CB  VAL A 378     -22.678  11.273   7.671  1.00 41.76           C  
ANISOU 2282  CB  VAL A 378     4871   6108   4888    338    -37   -526       C  
ATOM   2283  CG1 VAL A 378     -23.263  10.994   6.283  1.00 41.55           C  
ANISOU 2283  CG1 VAL A 378     4817   6142   4828    374    -43   -578       C  
ATOM   2284  CG2 VAL A 378     -23.569  12.235   8.461  1.00 40.08           C  
ANISOU 2284  CG2 VAL A 378     4663   5850   4714    252    -17   -487       C  
ATOM   2285  N   ALA A 379     -22.506   9.529  10.862  1.00 42.87           N  
ANISOU 2285  N   ALA A 379     5157   6034   5099    284    -79   -489       N  
ATOM   2286  CA  ALA A 379     -22.168   9.525  12.286  1.00 42.99           C  
ANISOU 2286  CA  ALA A 379     5193   6031   5109    254    -82   -437       C  
ATOM   2287  C   ALA A 379     -21.899  10.948  12.815  1.00 48.10           C  
ANISOU 2287  C   ALA A 379     5800   6743   5732    224    -55   -418       C  
ATOM   2288  O   ALA A 379     -20.783  11.251  13.236  1.00 49.13           O  
ANISOU 2288  O   ALA A 379     5911   6908   5850    248    -66   -400       O  
ATOM   2289  CB  ALA A 379     -20.966   8.611  12.537  1.00 43.70           C  
ANISOU 2289  CB  ALA A 379     5299   6101   5206    315   -119   -427       C  
ATOM   2290  N   GLN A 380     -22.909  11.825  12.764  1.00 43.54           N  
ANISOU 2290  N   GLN A 380     5204   6175   5163    176    -30   -429       N  
ATOM   2291  CA  GLN A 380     -22.745  13.211  13.212  1.00 42.06           C  
ANISOU 2291  CA  GLN A 380     4973   6026   4983    153    -23   -431       C  
ATOM   2292  C   GLN A 380     -23.700  13.567  14.346  1.00 46.87           C  
ANISOU 2292  C   GLN A 380     5591   6637   5580    108    -10   -447       C  
ATOM   2293  O   GLN A 380     -24.004  14.740  14.582  1.00 48.05           O  
ANISOU 2293  O   GLN A 380     5701   6802   5753     90     -9   -478       O  
ATOM   2294  CB  GLN A 380     -22.857  14.207  12.043  1.00 42.04           C  
ANISOU 2294  CB  GLN A 380     4912   6046   5015    153    -18   -430       C  
ATOM   2295  CG  GLN A 380     -21.579  14.301  11.202  1.00 41.53           C  
ANISOU 2295  CG  GLN A 380     4803   6031   4945    199    -29   -397       C  
ATOM   2296  CD  GLN A 380     -20.270  14.568  11.944  1.00 51.09           C  
ANISOU 2296  CD  GLN A 380     5994   7260   6158    214    -53   -374       C  
ATOM   2297  OE1 GLN A 380     -20.194  15.248  12.972  1.00 41.33           O  
ANISOU 2297  OE1 GLN A 380     4752   6007   4943    185    -69   -385       O  
ATOM   2298  NE2 GLN A 380     -19.190  14.082  11.384  1.00 42.03           N  
ANISOU 2298  NE2 GLN A 380     4823   6159   4986    266    -58   -351       N  
ATOM   2299  N   VAL A 381     -24.122  12.549  15.087  1.00 42.63           N  
ANISOU 2299  N   VAL A 381     5096   6091   5011     93     -5   -423       N  
ATOM   2300  CA  VAL A 381     -24.956  12.704  16.272  1.00 41.90           C  
ANISOU 2300  CA  VAL A 381     5001   6042   4879     57     13   -422       C  
ATOM   2301  C   VAL A 381     -24.013  12.986  17.444  1.00 47.04           C  
ANISOU 2301  C   VAL A 381     5642   6753   5479     75     -6   -423       C  
ATOM   2302  O   VAL A 381     -23.005  12.280  17.593  1.00 46.08           O  
ANISOU 2302  O   VAL A 381     5543   6620   5347    100    -30   -382       O  
ATOM   2303  CB  VAL A 381     -25.804  11.438  16.516  1.00 44.97           C  
ANISOU 2303  CB  VAL A 381     5422   6406   5259     24     21   -363       C  
ATOM   2304  CG1 VAL A 381     -26.564  11.519  17.841  1.00 45.41           C  
ANISOU 2304  CG1 VAL A 381     5457   6549   5249    -11     46   -337       C  
ATOM   2305  CG2 VAL A 381     -26.733  11.158  15.349  1.00 43.81           C  
ANISOU 2305  CG2 VAL A 381     5280   6199   5168      7     27   -377       C  
ATOM   2306  N   ASP A 382     -24.300  14.038  18.234  1.00 44.29           N  
ANISOU 2306  N   ASP A 382     5255   6468   5104     70     -3   -482       N  
ATOM   2307  CA  ASP A 382     -23.482  14.383  19.396  1.00 44.39           C  
ANISOU 2307  CA  ASP A 382     5251   6553   5061     91    -30   -506       C  
ATOM   2308  C   ASP A 382     -24.346  14.651  20.598  1.00 48.22           C  
ANISOU 2308  C   ASP A 382     5710   7151   5463     83    -10   -544       C  
ATOM   2309  O   ASP A 382     -25.483  15.088  20.450  1.00 46.33           O  
ANISOU 2309  O   ASP A 382     5448   6923   5234     68     18   -586       O  
ATOM   2310  CB  ASP A 382     -22.626  15.617  19.124  1.00 46.23           C  
ANISOU 2310  CB  ASP A 382     5443   6761   5360    112    -71   -572       C  
ATOM   2311  CG  ASP A 382     -22.022  15.676  17.752  1.00 51.89           C  
ANISOU 2311  CG  ASP A 382     6158   7399   6160    118    -79   -536       C  
ATOM   2312  OD1 ASP A 382     -21.101  14.884  17.481  1.00 53.76           O  
ANISOU 2312  OD1 ASP A 382     6417   7625   6385    139    -87   -480       O  
ATOM   2313  OD2 ASP A 382     -22.463  16.520  16.954  1.00 53.09           O  
ANISOU 2313  OD2 ASP A 382     6276   7512   6384    106    -80   -560       O  
ATOM   2314  N   GLY A 383     -23.780  14.441  21.779  1.00 46.26           N  
ANISOU 2314  N   GLY A 383     5453   7000   5123    100    -27   -535       N  
ATOM   2315  CA  GLY A 383     -24.477  14.696  23.029  1.00 46.43           C  
ANISOU 2315  CA  GLY A 383     5434   7177   5032    106    -10   -576       C  
ATOM   2316  C   GLY A 383     -24.144  16.064  23.565  1.00 50.29           C  
ANISOU 2316  C   GLY A 383     5873   7716   5520    149    -53   -730       C  
ATOM   2317  O   GLY A 383     -23.057  16.584  23.303  1.00 51.07           O  
ANISOU 2317  O   GLY A 383     5971   7748   5687    167   -106   -766       O  
ATOM   2318  N   ASP A 384     -25.073  16.665  24.300  1.00 46.85           N  
ANISOU 2318  N   ASP A 384     5385   7398   5017    169    -37   -826       N  
ATOM   2319  CA  ASP A 384     -24.827  17.943  24.954  1.00 47.91           C  
ANISOU 2319  CA  ASP A 384     5462   7590   5152    222    -92  -1002       C  
ATOM   2320  C   ASP A 384     -25.476  17.932  26.340  1.00 53.44           C  
ANISOU 2320  C   ASP A 384     6108   8524   5674    260    -69  -1062       C  
ATOM   2321  O   ASP A 384     -26.677  17.679  26.474  1.00 53.80           O  
ANISOU 2321  O   ASP A 384     6129   8655   5658    249     -7  -1039       O  
ATOM   2322  CB  ASP A 384     -25.285  19.139  24.111  1.00 49.20           C  
ANISOU 2322  CB  ASP A 384     5597   7624   5472    230   -119  -1114       C  
ATOM   2323  CG  ASP A 384     -25.395  20.427  24.889  1.00 59.17           C  
ANISOU 2323  CG  ASP A 384     6789   8945   6748    292   -183  -1317       C  
ATOM   2324  OD1 ASP A 384     -24.380  20.857  25.471  1.00 60.74           O  
ANISOU 2324  OD1 ASP A 384     6971   9150   6957    320   -257  -1389       O  
ATOM   2325  OD2 ASP A 384     -26.498  20.992  24.936  1.00 68.69           O  
ANISOU 2325  OD2 ASP A 384     7951  10191   7958    317   -167  -1415       O  
ATOM   2326  N   SER A 385     -24.659  18.166  27.368  1.00 50.46           N  
ANISOU 2326  N   SER A 385     5702   8266   5204    304   -119  -1132       N  
ATOM   2327  CA  SER A 385     -25.098  18.154  28.765  1.00 51.85           C  
ANISOU 2327  CA  SER A 385     5813   8709   5178    352   -104  -1193       C  
ATOM   2328  C   SER A 385     -26.107  19.279  29.093  1.00 58.26           C  
ANISOU 2328  C   SER A 385     6549   9608   5979    413   -108  -1399       C  
ATOM   2329  O   SER A 385     -26.959  19.070  29.961  1.00 59.66           O  
ANISOU 2329  O   SER A 385     6667  10018   5984    441    -55  -1409       O  
ATOM   2330  CB  SER A 385     -23.893  18.248  29.701  1.00 53.86           C  
ANISOU 2330  CB  SER A 385     6052   9062   5348    394   -174  -1244       C  
ATOM   2331  OG  SER A 385     -23.052  19.344  29.373  1.00 56.51           O  
ANISOU 2331  OG  SER A 385     6382   9251   5836    422   -268  -1398       O  
ATOM   2332  N   VAL A 386     -26.018  20.458  28.427  1.00 55.11           N  
ANISOU 2332  N   VAL A 386     6141   9034   5765    436   -173  -1555       N  
ATOM   2333  CA  VAL A 386     -26.920  21.563  28.769  1.00 56.93           C  
ANISOU 2333  CA  VAL A 386     6293   9327   6011    507   -195  -1771       C  
ATOM   2334  C   VAL A 386     -28.340  21.278  28.192  1.00 60.34           C  
ANISOU 2334  C   VAL A 386     6719   9758   6450    477   -104  -1699       C  
ATOM   2335  O   VAL A 386     -29.314  21.482  28.916  1.00 61.08           O  
ANISOU 2335  O   VAL A 386     6738  10048   6421    530    -67  -1794       O  
ATOM   2336  CB  VAL A 386     -26.386  23.013  28.486  1.00 61.70           C  
ANISOU 2336  CB  VAL A 386     6868   9754   6823    551   -319  -1976       C  
ATOM   2337  CG1 VAL A 386     -24.967  23.029  27.943  1.00 60.45           C  
ANISOU 2337  CG1 VAL A 386     6760   9412   6797    505   -386  -1898       C  
ATOM   2338  CG2 VAL A 386     -27.323  23.841  27.618  1.00 61.52           C  
ANISOU 2338  CG2 VAL A 386     6820   9576   6977    554   -325  -2046       C  
ATOM   2339  N   SER A 387     -28.449  20.749  26.950  1.00 54.38           N  
ANISOU 2339  N   SER A 387     6032   8809   5819    395    -68  -1534       N  
ATOM   2340  CA  SER A 387     -29.741  20.381  26.369  1.00 53.46           C  
ANISOU 2340  CA  SER A 387     5913   8686   5715    358     11  -1454       C  
ATOM   2341  C   SER A 387     -30.232  19.044  26.932  1.00 57.86           C  
ANISOU 2341  C   SER A 387     6471   9421   6092    316     98  -1278       C  
ATOM   2342  O   SER A 387     -31.436  18.804  26.980  1.00 57.61           O  
ANISOU 2342  O   SER A 387     6397   9483   6008    304    164  -1244       O  
ATOM   2343  CB  SER A 387     -29.662  20.310  24.849  1.00 54.07           C  
ANISOU 2343  CB  SER A 387     6053   8510   5981    294      7  -1355       C  
ATOM   2344  OG  SER A 387     -28.664  19.393  24.444  1.00 60.91           O  
ANISOU 2344  OG  SER A 387     6994   9299   6851    241      9  -1196       O  
ATOM   2345  N   GLY A 388     -29.293  18.186  27.324  1.00 55.13           N  
ANISOU 2345  N   GLY A 388     6166   9112   5667    290     93  -1155       N  
ATOM   2346  CA  GLY A 388     -29.571  16.872  27.895  1.00 55.33           C  
ANISOU 2346  CA  GLY A 388     6190   9286   5546    243    155   -958       C  
ATOM   2347  C   GLY A 388     -30.028  15.850  26.879  1.00 55.86           C  
ANISOU 2347  C   GLY A 388     6315   9201   5710    154    197   -770       C  
ATOM   2348  O   GLY A 388     -30.593  14.815  27.243  1.00 54.28           O  
ANISOU 2348  O   GLY A 388     6095   9102   5425    104    247   -603       O  
ATOM   2349  N   ILE A 389     -29.811  16.151  25.593  1.00 50.40           N  
ANISOU 2349  N   ILE A 389     5682   8270   5198    134    170   -796       N  
ATOM   2350  CA  ILE A 389     -30.157  15.256  24.493  1.00 48.65           C  
ANISOU 2350  CA  ILE A 389     5516   7891   5080     63    194   -655       C  
ATOM   2351  C   ILE A 389     -28.942  15.050  23.589  1.00 51.95           C  
ANISOU 2351  C   ILE A 389     6012   8113   5614     54    145   -624       C  
ATOM   2352  O   ILE A 389     -27.912  15.702  23.734  1.00 49.73           O  
ANISOU 2352  O   ILE A 389     5735   7805   5353     94     96   -709       O  
ATOM   2353  CB  ILE A 389     -31.383  15.756  23.651  1.00 50.68           C  
ANISOU 2353  CB  ILE A 389     5747   8084   5423     50    223   -708       C  
ATOM   2354  CG1 ILE A 389     -31.095  17.103  22.931  1.00 49.97           C  
ANISOU 2354  CG1 ILE A 389     5657   7868   5462     95    174   -868       C  
ATOM   2355  CG2 ILE A 389     -32.685  15.772  24.460  1.00 51.69           C  
ANISOU 2355  CG2 ILE A 389     5789   8415   5435     54    281   -712       C  
ATOM   2356  CD1 ILE A 389     -31.791  17.305  21.625  1.00 52.15           C  
ANISOU 2356  CD1 ILE A 389     5949   7993   5872     64    180   -855       C  
ATOM   2357  N   CYS A 390     -29.103  14.136  22.641  1.00 49.87           N  
ANISOU 2357  N   CYS A 390     5798   7721   5429      3    155   -508       N  
ATOM   2358  CA  CYS A 390     -28.192  13.870  21.556  1.00 49.17           C  
ANISOU 2358  CA  CYS A 390     5773   7462   5450      0    119   -483       C  
ATOM   2359  C   CYS A 390     -28.869  14.458  20.332  1.00 50.37           C  
ANISOU 2359  C   CYS A 390     5923   7507   5709     -9    126   -538       C  
ATOM   2360  O   CYS A 390     -30.091  14.331  20.191  1.00 50.01           O  
ANISOU 2360  O   CYS A 390     5853   7482   5664    -38    161   -524       O  
ATOM   2361  CB  CYS A 390     -27.911  12.375  21.416  1.00 50.10           C  
ANISOU 2361  CB  CYS A 390     5936   7522   5575    -36    113   -334       C  
ATOM   2362  SG  CYS A 390     -26.674  11.734  22.581  1.00 54.72           S  
ANISOU 2362  SG  CYS A 390     6533   8188   6071    -16     81   -257       S  
ATOM   2363  N   PHE A 391     -28.129  15.205  19.519  1.00 45.19           N  
ANISOU 2363  N   PHE A 391     5275   6756   5137     15     91   -597       N  
ATOM   2364  CA  PHE A 391     -28.721  15.868  18.355  1.00 43.66           C  
ANISOU 2364  CA  PHE A 391     5068   6477   5042      9     91   -636       C  
ATOM   2365  C   PHE A 391     -27.707  15.913  17.231  1.00 46.26           C  
ANISOU 2365  C   PHE A 391     5423   6707   5448     19     59   -611       C  
ATOM   2366  O   PHE A 391     -26.582  15.466  17.418  1.00 47.87           O  
ANISOU 2366  O   PHE A 391     5651   6905   5630     35     38   -578       O  
ATOM   2367  CB  PHE A 391     -29.227  17.292  18.748  1.00 45.25           C  
ANISOU 2367  CB  PHE A 391     5206   6715   5271     37     80   -757       C  
ATOM   2368  CG  PHE A 391     -30.275  17.899  17.829  1.00 45.81           C  
ANISOU 2368  CG  PHE A 391     5247   6730   5427     26     88   -785       C  
ATOM   2369  CD1 PHE A 391     -31.574  17.398  17.797  1.00 47.03           C  
ANISOU 2369  CD1 PHE A 391     5391   6926   5551     -2    135   -759       C  
ATOM   2370  CD2 PHE A 391     -29.959  18.972  16.998  1.00 46.59           C  
ANISOU 2370  CD2 PHE A 391     5319   6737   5645     39     45   -822       C  
ATOM   2371  CE1 PHE A 391     -32.533  17.957  16.955  1.00 47.02           C  
ANISOU 2371  CE1 PHE A 391     5359   6879   5629     -9    139   -784       C  
ATOM   2372  CE2 PHE A 391     -30.925  19.538  16.163  1.00 47.99           C  
ANISOU 2372  CE2 PHE A 391     5463   6868   5903     30     47   -834       C  
ATOM   2373  CZ  PHE A 391     -32.207  19.033  16.155  1.00 46.18           C  
ANISOU 2373  CZ  PHE A 391     5229   6683   5634      9     95   -822       C  
ATOM   2374  N   VAL A 392     -28.105  16.416  16.057  1.00 41.76           N  
ANISOU 2374  N   VAL A 392     4837   6073   4957     12     57   -618       N  
ATOM   2375  CA  VAL A 392     -27.255  16.528  14.878  1.00 40.77           C  
ANISOU 2375  CA  VAL A 392     4713   5889   4889     24     33   -584       C  
ATOM   2376  C   VAL A 392     -26.573  17.914  14.835  1.00 46.50           C  
ANISOU 2376  C   VAL A 392     5384   6594   5690     39    -10   -619       C  
ATOM   2377  O   VAL A 392     -27.191  18.962  15.092  1.00 47.27           O  
ANISOU 2377  O   VAL A 392     5436   6681   5842     39    -26   -681       O  
ATOM   2378  CB  VAL A 392     -28.029  16.195  13.548  1.00 44.08           C  
ANISOU 2378  CB  VAL A 392     5136   6274   5340      9     49   -554       C  
ATOM   2379  CG1 VAL A 392     -29.296  17.037  13.369  1.00 43.70           C  
ANISOU 2379  CG1 VAL A 392     5046   6224   5335    -10     60   -592       C  
ATOM   2380  CG2 VAL A 392     -27.136  16.300  12.311  1.00 43.32           C  
ANISOU 2380  CG2 VAL A 392     5023   6160   5275     30     29   -516       C  
ATOM   2381  N   GLY A 393     -25.283  17.877  14.526  1.00 43.49           N  
ANISOU 2381  N   GLY A 393     5000   6203   5322     55    -35   -579       N  
ATOM   2382  CA  GLY A 393     -24.476  19.062  14.297  1.00 43.33           C  
ANISOU 2382  CA  GLY A 393     4918   6152   5394     58    -86   -578       C  
ATOM   2383  C   GLY A 393     -24.085  19.878  15.495  1.00 47.46           C  
ANISOU 2383  C   GLY A 393     5413   6674   5945     68   -133   -656       C  
ATOM   2384  O   GLY A 393     -23.868  21.085  15.358  1.00 47.26           O  
ANISOU 2384  O   GLY A 393     5325   6596   6038     63   -189   -678       O  
ATOM   2385  N   TYR A 394     -23.952  19.231  16.660  1.00 44.35           N  
ANISOU 2385  N   TYR A 394     5058   6341   5452     83   -120   -695       N  
ATOM   2386  CA  TYR A 394     -23.477  19.910  17.858  1.00 45.25           C  
ANISOU 2386  CA  TYR A 394     5143   6482   5566    103   -171   -785       C  
ATOM   2387  C   TYR A 394     -21.984  20.199  17.709  1.00 50.68           C  
ANISOU 2387  C   TYR A 394     5806   7141   6308    107   -225   -747       C  
ATOM   2388  O   TYR A 394     -21.551  21.332  17.898  1.00 52.12           O  
ANISOU 2388  O   TYR A 394     5929   7278   6597    107   -296   -800       O  
ATOM   2389  CB  TYR A 394     -23.765  19.081  19.123  1.00 46.41           C  
ANISOU 2389  CB  TYR A 394     5328   6737   5568    118   -139   -816       C  
ATOM   2390  CG  TYR A 394     -25.155  19.256  19.708  1.00 46.95           C  
ANISOU 2390  CG  TYR A 394     5382   6868   5588    123   -106   -889       C  
ATOM   2391  CD1 TYR A 394     -25.895  20.414  19.473  1.00 49.69           C  
ANISOU 2391  CD1 TYR A 394     5677   7171   6033    132   -132   -980       C  
ATOM   2392  CD2 TYR A 394     -25.685  18.313  20.584  1.00 47.35           C  
ANISOU 2392  CD2 TYR A 394     5458   7034   5500    123    -58   -865       C  
ATOM   2393  CE1 TYR A 394     -27.142  20.613  20.073  1.00 52.21           C  
ANISOU 2393  CE1 TYR A 394     5970   7566   6301    149   -102  -1062       C  
ATOM   2394  CE2 TYR A 394     -26.934  18.495  21.178  1.00 48.48           C  
ANISOU 2394  CE2 TYR A 394     5570   7266   5585    130    -23   -926       C  
ATOM   2395  CZ  TYR A 394     -27.649  19.655  20.936  1.00 56.08           C  
ANISOU 2395  CZ  TYR A 394     6480   8192   6635    149    -44  -1035       C  
ATOM   2396  OH  TYR A 394     -28.873  19.830  21.525  1.00 56.98           O  
ANISOU 2396  OH  TYR A 394     6554   8411   6687    167     -8  -1103       O  
ATOM   2397  N   LYS A 395     -21.215  19.196  17.277  1.00 46.16           N  
ANISOU 2397  N   LYS A 395     5270   6588   5680    110   -197   -654       N  
ATOM   2398  CA  LYS A 395     -19.786  19.328  17.077  1.00 46.07           C  
ANISOU 2398  CA  LYS A 395     5229   6570   5707    116   -239   -605       C  
ATOM   2399  C   LYS A 395     -19.490  20.110  15.804  1.00 50.16           C  
ANISOU 2399  C   LYS A 395     5681   7034   6344     95   -259   -535       C  
ATOM   2400  O   LYS A 395     -18.637  20.987  15.825  1.00 49.21           O  
ANISOU 2400  O   LYS A 395     5494   6884   6321     84   -323   -521       O  
ATOM   2401  CB  LYS A 395     -19.115  17.934  17.027  1.00 48.73           C  
ANISOU 2401  CB  LYS A 395     5618   6951   5945    139   -204   -536       C  
ATOM   2402  CG  LYS A 395     -17.700  17.901  17.616  1.00 61.62           C  
ANISOU 2402  CG  LYS A 395     7229   8611   7572    158   -250   -522       C  
ATOM   2403  CD  LYS A 395     -16.626  18.018  16.554  1.00 77.79           C  
ANISOU 2403  CD  LYS A 395     9228  10652   9678    164   -260   -437       C  
ATOM   2404  CE  LYS A 395     -15.221  17.995  17.113  1.00 88.03           C  
ANISOU 2404  CE  LYS A 395    10494  11979  10973    181   -306   -417       C  
ATOM   2405  NZ  LYS A 395     -14.904  19.201  17.926  1.00 95.85           N  
ANISOU 2405  NZ  LYS A 395    11429  12948  12043    158   -383   -480       N  
ATOM   2406  N   ASN A 396     -20.176  19.769  14.694  1.00 47.95           N  
ANISOU 2406  N   ASN A 396     5411   6750   6056     88   -210   -481       N  
ATOM   2407  CA  ASN A 396     -19.954  20.367  13.381  1.00 47.37           C  
ANISOU 2407  CA  ASN A 396     5269   6665   6066     71   -219   -389       C  
ATOM   2408  C   ASN A 396     -21.225  21.001  12.912  1.00 51.52           C  
ANISOU 2408  C   ASN A 396     5778   7147   6652     48   -214   -404       C  
ATOM   2409  O   ASN A 396     -22.135  20.287  12.497  1.00 51.91           O  
ANISOU 2409  O   ASN A 396     5874   7218   6630     55   -160   -410       O  
ATOM   2410  CB  ASN A 396     -19.449  19.307  12.413  1.00 45.83           C  
ANISOU 2410  CB  ASN A 396     5090   6540   5786     99   -171   -312       C  
ATOM   2411  CG  ASN A 396     -18.111  18.762  12.831  1.00 57.84           C  
ANISOU 2411  CG  ASN A 396     6612   8102   7263    128   -183   -292       C  
ATOM   2412  OD1 ASN A 396     -17.102  19.475  12.843  1.00 48.87           O  
ANISOU 2412  OD1 ASN A 396     5404   6971   6195    117   -228   -244       O  
ATOM   2413  ND2 ASN A 396     -18.087  17.506  13.241  1.00 45.51           N  
ANISOU 2413  ND2 ASN A 396     5126   6562   5602    163   -152   -323       N  
ATOM   2414  N   TYR A 397     -21.300  22.356  13.007  1.00 48.05           N  
ANISOU 2414  N   TYR A 397     5266   6633   6358     23   -282   -415       N  
ATOM   2415  CA  TYR A 397     -22.490  23.167  12.718  1.00 46.87           C  
ANISOU 2415  CA  TYR A 397     5087   6423   6300      6   -297   -441       C  
ATOM   2416  C   TYR A 397     -23.087  22.884  11.318  1.00 49.68           C  
ANISOU 2416  C   TYR A 397     5432   6815   6631     -4   -250   -341       C  
ATOM   2417  O   TYR A 397     -24.310  22.930  11.180  1.00 49.97           O  
ANISOU 2417  O   TYR A 397     5484   6833   6667     -6   -229   -382       O  
ATOM   2418  CB  TYR A 397     -22.200  24.678  12.905  1.00 48.35           C  
ANISOU 2418  CB  TYR A 397     5179   6505   6685    -17   -401   -447       C  
ATOM   2419  CG  TYR A 397     -21.452  25.337  11.762  1.00 50.58           C  
ANISOU 2419  CG  TYR A 397     5365   6770   7082    -56   -441   -278       C  
ATOM   2420  CD1 TYR A 397     -20.069  25.232  11.654  1.00 51.73           C  
ANISOU 2420  CD1 TYR A 397     5473   6955   7226    -65   -459   -193       C  
ATOM   2421  CD2 TYR A 397     -22.137  26.024  10.758  1.00 52.30           C  
ANISOU 2421  CD2 TYR A 397     5518   6951   7402    -83   -458   -185       C  
ATOM   2422  CE1 TYR A 397     -19.382  25.794  10.576  1.00 53.53           C  
ANISOU 2422  CE1 TYR A 397     5595   7200   7545   -103   -488    -13       C  
ATOM   2423  CE2 TYR A 397     -21.465  26.579   9.670  1.00 54.07           C  
ANISOU 2423  CE2 TYR A 397     5639   7191   7715   -122   -490      2       C  
ATOM   2424  CZ  TYR A 397     -20.086  26.466   9.585  1.00 63.32           C  
ANISOU 2424  CZ  TYR A 397     6767   8414   8877   -133   -503     91       C  
ATOM   2425  OH  TYR A 397     -19.431  27.026   8.512  1.00 64.32           O  
ANISOU 2425  OH  TYR A 397     6773   8582   9084   -174   -530    295       O  
ATOM   2426  N   ARG A 398     -22.255  22.567  10.303  1.00 46.40           N  
ANISOU 2426  N   ARG A 398     4981   6467   6182     -5   -233   -218       N  
ATOM   2427  CA  ARG A 398     -22.744  22.291   8.933  1.00 46.69           C  
ANISOU 2427  CA  ARG A 398     4995   6572   6173     -4   -193   -129       C  
ATOM   2428  C   ARG A 398     -23.833  21.204   8.888  1.00 48.26           C  
ANISOU 2428  C   ARG A 398     5284   6799   6254     18   -131   -208       C  
ATOM   2429  O   ARG A 398     -24.715  21.269   8.029  1.00 48.50           O  
ANISOU 2429  O   ARG A 398     5297   6848   6281     11   -116   -179       O  
ATOM   2430  CB  ARG A 398     -21.594  21.896   7.991  1.00 47.46           C  
ANISOU 2430  CB  ARG A 398     5043   6784   6208     13   -176    -12       C  
ATOM   2431  CG  ARG A 398     -20.788  23.096   7.500  1.00 58.46           C  
ANISOU 2431  CG  ARG A 398     6307   8173   7731    -26   -235    130       C  
ATOM   2432  CD  ARG A 398     -19.696  22.715   6.511  1.00 58.93           C  
ANISOU 2432  CD  ARG A 398     6298   8385   7706     -5   -207    256       C  
ATOM   2433  NE  ARG A 398     -18.877  23.875   6.151  1.00 78.61           N  
ANISOU 2433  NE  ARG A 398     8654  10880  10335    -54   -268    420       N  
ATOM   2434  CZ  ARG A 398     -17.793  24.269   6.820  1.00 99.72           C  
ANISOU 2434  CZ  ARG A 398    11286  13512  13092    -75   -318    444       C  
ATOM   2435  NH1 ARG A 398     -17.383  23.599   7.893  1.00 90.58           N  
ANISOU 2435  NH1 ARG A 398    10216  12320  11881    -44   -310    312       N  
ATOM   2436  NH2 ARG A 398     -17.114  25.339   6.424  1.00 85.03           N  
ANISOU 2436  NH2 ARG A 398     9287  11645  11376   -130   -382    612       N  
ATOM   2437  N   TYR A 399     -23.792  20.239   9.827  1.00 42.62           N  
ANISOU 2437  N   TYR A 399     4656   6083   5455     39   -104   -296       N  
ATOM   2438  CA  TYR A 399     -24.753  19.135   9.856  1.00 41.82           C  
ANISOU 2438  CA  TYR A 399     4631   5995   5262     50    -57   -354       C  
ATOM   2439  C   TYR A 399     -26.082  19.631  10.401  1.00 45.22           C  
ANISOU 2439  C   TYR A 399     5069   6374   5738     26    -56   -419       C  
ATOM   2440  O   TYR A 399     -27.122  19.276   9.864  1.00 43.88           O  
ANISOU 2440  O   TYR A 399     4915   6213   5544     19    -30   -426       O  
ATOM   2441  CB  TYR A 399     -24.185  17.901  10.599  1.00 41.69           C  
ANISOU 2441  CB  TYR A 399     4689   5995   5158     76    -38   -392       C  
ATOM   2442  CG  TYR A 399     -23.010  17.340   9.823  1.00 40.99           C  
ANISOU 2442  CG  TYR A 399     4584   5966   5022    114    -36   -338       C  
ATOM   2443  CD1 TYR A 399     -21.727  17.877   9.976  1.00 41.99           C  
ANISOU 2443  CD1 TYR A 399     4660   6114   5180    121    -63   -291       C  
ATOM   2444  CD2 TYR A 399     -23.198  16.371   8.840  1.00 41.05           C  
ANISOU 2444  CD2 TYR A 399     4611   6022   4964    147    -13   -339       C  
ATOM   2445  CE1 TYR A 399     -20.663  17.447   9.191  1.00 40.66           C  
ANISOU 2445  CE1 TYR A 399     4456   6027   4965    161    -57   -236       C  
ATOM   2446  CE2 TYR A 399     -22.130  15.913   8.061  1.00 42.08           C  
ANISOU 2446  CE2 TYR A 399     4711   6234   5045    198    -12   -307       C  
ATOM   2447  CZ  TYR A 399     -20.868  16.468   8.232  1.00 47.72           C  
ANISOU 2447  CZ  TYR A 399     5370   6984   5779    206    -28   -249       C  
ATOM   2448  OH  TYR A 399     -19.811  16.059   7.460  1.00 43.39           O  
ANISOU 2448  OH  TYR A 399     4775   6538   5174    261    -22   -213       O  
ATOM   2449  N   ARG A 400     -26.045  20.561  11.345  1.00 43.47           N  
ANISOU 2449  N   ARG A 400     4821   6105   5590     18    -93   -469       N  
ATOM   2450  CA  ARG A 400     -27.260  21.208  11.823  1.00 43.34           C  
ANISOU 2450  CA  ARG A 400     4789   6050   5626     10   -100   -543       C  
ATOM   2451  C   ARG A 400     -27.831  22.114  10.706  1.00 46.49           C  
ANISOU 2451  C   ARG A 400     5121   6414   6131     -7   -125   -484       C  
ATOM   2452  O   ARG A 400     -29.041  22.147  10.502  1.00 46.75           O  
ANISOU 2452  O   ARG A 400     5152   6442   6169    -12   -106   -511       O  
ATOM   2453  CB  ARG A 400     -26.970  22.001  13.096  1.00 43.13           C  
ANISOU 2453  CB  ARG A 400     4742   5993   5652     23   -146   -638       C  
ATOM   2454  CG  ARG A 400     -28.224  22.493  13.767  1.00 48.39           C  
ANISOU 2454  CG  ARG A 400     5394   6652   6340     35   -145   -745       C  
ATOM   2455  CD  ARG A 400     -27.902  23.067  15.106  1.00 54.20           C  
ANISOU 2455  CD  ARG A 400     6111   7391   7093     65   -189   -866       C  
ATOM   2456  NE  ARG A 400     -29.061  23.731  15.691  1.00 54.70           N  
ANISOU 2456  NE  ARG A 400     6137   7457   7189     92   -198   -986       N  
ATOM   2457  CZ  ARG A 400     -29.101  24.173  16.937  1.00 65.56           C  
ANISOU 2457  CZ  ARG A 400     7491   8874   8545    135   -228  -1128       C  
ATOM   2458  NH1 ARG A 400     -28.050  24.021  17.737  1.00 52.95           N  
ANISOU 2458  NH1 ARG A 400     5909   7312   6897    149   -254  -1160       N  
ATOM   2459  NH2 ARG A 400     -30.188  24.773  17.397  1.00 54.71           N  
ANISOU 2459  NH2 ARG A 400     6072   7520   7196    172   -234  -1247       N  
ATOM   2460  N   ALA A 401     -26.960  22.788   9.945  1.00 42.54           N  
ANISOU 2460  N   ALA A 401     4556   5900   5709    -17   -167   -385       N  
ATOM   2461  CA  ALA A 401     -27.394  23.653   8.846  1.00 42.87           C  
ANISOU 2461  CA  ALA A 401     4518   5920   5851    -38   -198   -291       C  
ATOM   2462  C   ALA A 401     -28.090  22.838   7.733  1.00 48.01           C  
ANISOU 2462  C   ALA A 401     5189   6654   6398    -35   -143   -243       C  
ATOM   2463  O   ALA A 401     -29.220  23.155   7.346  1.00 48.25           O  
ANISOU 2463  O   ALA A 401     5199   6666   6466    -44   -145   -248       O  
ATOM   2464  CB  ALA A 401     -26.208  24.419   8.292  1.00 44.20           C  
ANISOU 2464  CB  ALA A 401     4601   6082   6110    -57   -251   -164       C  
ATOM   2465  N   GLY A 402     -27.452  21.748   7.305  1.00 43.77           N  
ANISOU 2465  N   GLY A 402     4692   6204   5733    -16   -102   -219       N  
ATOM   2466  CA  GLY A 402     -27.998  20.885   6.275  1.00 42.63           C  
ANISOU 2466  CA  GLY A 402     4567   6141   5488     -3    -64   -202       C  
ATOM   2467  C   GLY A 402     -29.216  20.081   6.671  1.00 46.13           C  
ANISOU 2467  C   GLY A 402     5083   6563   5882     -5    -32   -299       C  
ATOM   2468  O   GLY A 402     -30.118  19.912   5.848  1.00 45.92           O  
ANISOU 2468  O   GLY A 402     5045   6569   5834     -8    -24   -290       O  
ATOM   2469  N   PHE A 403     -29.266  19.580   7.926  1.00 41.43           N  
ANISOU 2469  N   PHE A 403     4551   5924   5265     -5    -16   -383       N  
ATOM   2470  CA  PHE A 403     -30.333  18.681   8.364  1.00 40.06           C  
ANISOU 2470  CA  PHE A 403     4437   5743   5043    -15     16   -450       C  
ATOM   2471  C   PHE A 403     -31.446  19.304   9.186  1.00 44.45           C  
ANISOU 2471  C   PHE A 403     4977   6261   5652    -34     19   -506       C  
ATOM   2472  O   PHE A 403     -32.494  18.668   9.348  1.00 42.60           O  
ANISOU 2472  O   PHE A 403     4766   6035   5385    -50     46   -537       O  
ATOM   2473  CB  PHE A 403     -29.734  17.519   9.154  1.00 40.90           C  
ANISOU 2473  CB  PHE A 403     4615   5852   5075     -4     34   -480       C  
ATOM   2474  CG  PHE A 403     -28.928  16.578   8.285  1.00 41.69           C  
ANISOU 2474  CG  PHE A 403     4735   5990   5113     27     32   -455       C  
ATOM   2475  CD1 PHE A 403     -29.562  15.676   7.434  1.00 43.45           C  
ANISOU 2475  CD1 PHE A 403     4979   6231   5301     34     34   -473       C  
ATOM   2476  CD2 PHE A 403     -27.534  16.588   8.323  1.00 42.85           C  
ANISOU 2476  CD2 PHE A 403     4877   6161   5243     57     22   -427       C  
ATOM   2477  CE1 PHE A 403     -28.817  14.781   6.655  1.00 44.57           C  
ANISOU 2477  CE1 PHE A 403     5134   6414   5385     80     23   -481       C  
ATOM   2478  CE2 PHE A 403     -26.789  15.705   7.535  1.00 45.45           C  
ANISOU 2478  CE2 PHE A 403     5216   6541   5510    101     20   -421       C  
ATOM   2479  CZ  PHE A 403     -27.435  14.811   6.700  1.00 43.73           C  
ANISOU 2479  CZ  PHE A 403     5018   6342   5254    118     19   -457       C  
ATOM   2480  N   VAL A 404     -31.245  20.529   9.700  1.00 42.96           N  
ANISOU 2480  N   VAL A 404     4739   6032   5551    -29    -14   -525       N  
ATOM   2481  CA  VAL A 404     -32.241  21.183  10.547  1.00 42.73           C  
ANISOU 2481  CA  VAL A 404     4685   5980   5572    -27    -17   -606       C  
ATOM   2482  C   VAL A 404     -32.615  22.526   9.954  1.00 45.75           C  
ANISOU 2482  C   VAL A 404     4986   6306   6093    -26    -68   -586       C  
ATOM   2483  O   VAL A 404     -33.779  22.741   9.677  1.00 46.51           O  
ANISOU 2483  O   VAL A 404     5054   6398   6218    -29    -61   -604       O  
ATOM   2484  CB  VAL A 404     -31.748  21.307  12.029  1.00 47.11           C  
ANISOU 2484  CB  VAL A 404     5254   6542   6103     -7    -21   -690       C  
ATOM   2485  CG1 VAL A 404     -32.805  21.962  12.926  1.00 47.21           C  
ANISOU 2485  CG1 VAL A 404     5227   6564   6146     12    -22   -796       C  
ATOM   2486  CG2 VAL A 404     -31.363  19.945  12.587  1.00 46.65           C  
ANISOU 2486  CG2 VAL A 404     5269   6540   5917    -13     22   -680       C  
ATOM   2487  N   LEU A 405     -31.654  23.431   9.782  1.00 43.11           N  
ANISOU 2487  N   LEU A 405     4605   5921   5855    -23   -125   -543       N  
ATOM   2488  CA  LEU A 405     -31.910  24.765   9.245  1.00 43.72           C  
ANISOU 2488  CA  LEU A 405     4593   5921   6098    -27   -192   -503       C  
ATOM   2489  C   LEU A 405     -32.502  24.726   7.819  1.00 47.22           C  
ANISOU 2489  C   LEU A 405     5002   6397   6544    -47   -185   -389       C  
ATOM   2490  O   LEU A 405     -33.565  25.318   7.607  1.00 47.79           O  
ANISOU 2490  O   LEU A 405     5030   6433   6696    -45   -205   -403       O  
ATOM   2491  CB  LEU A 405     -30.625  25.615   9.263  1.00 44.37           C  
ANISOU 2491  CB  LEU A 405     4624   5941   6293    -34   -263   -447       C  
ATOM   2492  CG  LEU A 405     -30.811  27.083   8.847  1.00 49.48           C  
ANISOU 2492  CG  LEU A 405     5167   6477   7155    -43   -357   -395       C  
ATOM   2493  CD1 LEU A 405     -31.550  27.850   9.905  1.00 49.31           C  
ANISOU 2493  CD1 LEU A 405     5124   6368   7243     -7   -405   -559       C  
ATOM   2494  CD2 LEU A 405     -29.490  27.738   8.544  1.00 50.38           C  
ANISOU 2494  CD2 LEU A 405     5220   6545   7376    -70   -424   -281       C  
ATOM   2495  N   ALA A 406     -31.831  24.046   6.858  1.00 42.48           N  
ANISOU 2495  N   ALA A 406     4413   5875   5850    -57   -160   -285       N  
ATOM   2496  CA  ALA A 406     -32.315  23.979   5.476  1.00 42.66           C  
ANISOU 2496  CA  ALA A 406     4396   5964   5849    -67   -157   -182       C  
ATOM   2497  C   ALA A 406     -33.706  23.318   5.392  1.00 49.87           C  
ANISOU 2497  C   ALA A 406     5347   6904   6698    -66   -117   -253       C  
ATOM   2498  O   ALA A 406     -34.588  23.974   4.832  1.00 50.65           O  
ANISOU 2498  O   ALA A 406     5386   6988   6869    -73   -144   -214       O  
ATOM   2499  CB  ALA A 406     -31.322  23.266   4.587  1.00 43.05           C  
ANISOU 2499  CB  ALA A 406     4451   6125   5782    -60   -133    -95       C  
ATOM   2500  N   PRO A 407     -33.982  22.117   6.007  1.00 46.99           N  
ANISOU 2500  N   PRO A 407     5066   6564   6222    -62    -65   -346       N  
ATOM   2501  CA  PRO A 407     -35.342  21.552   5.947  1.00 46.73           C  
ANISOU 2501  CA  PRO A 407     5053   6550   6153    -72    -37   -397       C  
ATOM   2502  C   PRO A 407     -36.435  22.472   6.513  1.00 51.12           C  
ANISOU 2502  C   PRO A 407     5561   7050   6813    -72    -52   -450       C  
ATOM   2503  O   PRO A 407     -37.452  22.625   5.850  1.00 50.80           O  
ANISOU 2503  O   PRO A 407     5483   7023   6796    -79    -58   -432       O  
ATOM   2504  CB  PRO A 407     -35.209  20.276   6.778  1.00 47.56           C  
ANISOU 2504  CB  PRO A 407     5243   6670   6157    -75      7   -467       C  
ATOM   2505  CG  PRO A 407     -33.802  19.883   6.554  1.00 51.37           C  
ANISOU 2505  CG  PRO A 407     5754   7175   6590    -59      3   -430       C  
ATOM   2506  CD  PRO A 407     -33.081  21.168   6.692  1.00 47.03           C  
ANISOU 2506  CD  PRO A 407     5146   6587   6138    -53    -35   -389       C  
ATOM   2507  N   ILE A 408     -36.226  23.103   7.689  1.00 48.19           N  
ANISOU 2507  N   ILE A 408     5182   6624   6502    -54    -64   -523       N  
ATOM   2508  CA  ILE A 408     -37.212  24.021   8.295  1.00 48.91           C  
ANISOU 2508  CA  ILE A 408     5217   6671   6694    -34    -85   -603       C  
ATOM   2509  C   ILE A 408     -37.422  25.223   7.362  1.00 55.14           C  
ANISOU 2509  C   ILE A 408     5921   7397   7635    -31   -154   -527       C  
ATOM   2510  O   ILE A 408     -38.560  25.662   7.197  1.00 57.72           O  
ANISOU 2510  O   ILE A 408     6197   7708   8026    -21   -166   -551       O  
ATOM   2511  CB  ILE A 408     -36.828  24.457   9.746  1.00 52.08           C  
ANISOU 2511  CB  ILE A 408     5622   7048   7116     -1    -94   -721       C  
ATOM   2512  CG1 ILE A 408     -36.898  23.268  10.728  1.00 51.91           C  
ANISOU 2512  CG1 ILE A 408     5669   7113   6940     -6    -23   -778       C  
ATOM   2513  CG2 ILE A 408     -37.692  25.622  10.256  1.00 52.62           C  
ANISOU 2513  CG2 ILE A 408     5614   7065   7316     41   -139   -820       C  
ATOM   2514  CD1 ILE A 408     -36.293  23.558  12.111  1.00 55.08           C  
ANISOU 2514  CD1 ILE A 408     6078   7528   7321     28    -30   -877       C  
ATOM   2515  N   GLY A 409     -36.344  25.718   6.752  1.00 51.00           N  
ANISOU 2515  N   GLY A 409     5369   6841   7168    -42   -200   -422       N  
ATOM   2516  CA  GLY A 409     -36.410  26.816   5.793  1.00 51.63           C  
ANISOU 2516  CA  GLY A 409     5355   6867   7395    -51   -272   -304       C  
ATOM   2517  C   GLY A 409     -37.260  26.465   4.585  1.00 57.11           C  
ANISOU 2517  C   GLY A 409     6028   7640   8032    -67   -254   -217       C  
ATOM   2518  O   GLY A 409     -38.047  27.291   4.131  1.00 57.53           O  
ANISOU 2518  O   GLY A 409     6006   7650   8204    -64   -302   -173       O  
ATOM   2519  N   LEU A 410     -37.135  25.217   4.083  1.00 53.91           N  
ANISOU 2519  N   LEU A 410     5686   7346   7450    -78   -193   -205       N  
ATOM   2520  CA  LEU A 410     -37.915  24.685   2.967  1.00 54.56           C  
ANISOU 2520  CA  LEU A 410     5757   7521   7451    -88   -177   -154       C  
ATOM   2521  C   LEU A 410     -39.407  24.583   3.375  1.00 56.95           C  
ANISOU 2521  C   LEU A 410     6060   7803   7777    -86   -162   -247       C  
ATOM   2522  O   LEU A 410     -40.280  24.897   2.549  1.00 54.92           O  
ANISOU 2522  O   LEU A 410     5745   7570   7554    -90   -187   -193       O  
ATOM   2523  CB  LEU A 410     -37.330  23.308   2.530  1.00 55.05           C  
ANISOU 2523  CB  LEU A 410     5893   7690   7335    -88   -129   -162       C  
ATOM   2524  CG  LEU A 410     -38.088  22.329   1.550  1.00 61.70           C  
ANISOU 2524  CG  LEU A 410     6746   8637   8060    -90   -114   -163       C  
ATOM   2525  CD1 LEU A 410     -39.153  21.450   2.275  1.00 62.94           C  
ANISOU 2525  CD1 LEU A 410     6961   8767   8187   -104    -80   -284       C  
ATOM   2526  CD2 LEU A 410     -38.582  23.003   0.246  1.00 64.11           C  
ANISOU 2526  CD2 LEU A 410     6956   9012   8392    -91   -157    -44       C  
ATOM   2527  N   VAL A 411     -39.696  24.160   4.649  1.00 53.26           N  
ANISOU 2527  N   VAL A 411     5644   7306   7286    -79   -121   -376       N  
ATOM   2528  CA  VAL A 411     -41.084  24.033   5.115  1.00 52.73           C  
ANISOU 2528  CA  VAL A 411     5563   7244   7229    -77    -98   -459       C  
ATOM   2529  C   VAL A 411     -41.711  25.430   5.246  1.00 56.21           C  
ANISOU 2529  C   VAL A 411     5912   7608   7837    -47   -153   -472       C  
ATOM   2530  O   VAL A 411     -42.921  25.561   5.049  1.00 56.18           O  
ANISOU 2530  O   VAL A 411     5863   7619   7865    -43   -153   -492       O  
ATOM   2531  CB  VAL A 411     -41.351  23.152   6.379  1.00 55.66           C  
ANISOU 2531  CB  VAL A 411     5994   7642   7514    -80    -35   -567       C  
ATOM   2532  CG1 VAL A 411     -40.625  21.817   6.327  1.00 53.78           C  
ANISOU 2532  CG1 VAL A 411     5842   7448   7145   -107      1   -550       C  
ATOM   2533  CG2 VAL A 411     -41.118  23.891   7.692  1.00 56.02           C  
ANISOU 2533  CG2 VAL A 411     6024   7645   7616    -43    -40   -661       C  
ATOM   2534  N   LEU A 412     -40.894  26.465   5.524  1.00 52.39           N  
ANISOU 2534  N   LEU A 412     5393   7036   7476    -26   -209   -459       N  
ATOM   2535  CA  LEU A 412     -41.409  27.827   5.631  1.00 53.04           C  
ANISOU 2535  CA  LEU A 412     5383   7017   7753      8   -284   -477       C  
ATOM   2536  C   LEU A 412     -41.795  28.378   4.277  1.00 58.53           C  
ANISOU 2536  C   LEU A 412     6004   7703   8532     -9   -339   -325       C  
ATOM   2537  O   LEU A 412     -42.848  29.010   4.185  1.00 59.40           O  
ANISOU 2537  O   LEU A 412     6044   7772   8752     15   -375   -347       O  
ATOM   2538  CB  LEU A 412     -40.438  28.780   6.328  1.00 53.07           C  
ANISOU 2538  CB  LEU A 412     5364   6908   7892     33   -349   -513       C  
ATOM   2539  CG  LEU A 412     -40.329  28.641   7.853  1.00 56.99           C  
ANISOU 2539  CG  LEU A 412     5897   7404   8352     74   -322   -699       C  
ATOM   2540  CD1 LEU A 412     -39.182  29.457   8.365  1.00 57.44           C  
ANISOU 2540  CD1 LEU A 412     5935   7355   8533     90   -397   -723       C  
ATOM   2541  CD2 LEU A 412     -41.623  29.076   8.573  1.00 57.40           C  
ANISOU 2541  CD2 LEU A 412     5894   7454   8460    131   -323   -847       C  
ATOM   2542  N   ILE A 413     -40.990  28.116   3.223  1.00 55.62           N  
ANISOU 2542  N   ILE A 413     5640   7392   8102    -45   -345   -172       N  
ATOM   2543  CA  ILE A 413     -41.313  28.621   1.886  1.00 56.61           C  
ANISOU 2543  CA  ILE A 413     5682   7545   8281    -62   -396     -5       C  
ATOM   2544  C   ILE A 413     -42.543  27.869   1.314  1.00 58.91           C  
ANISOU 2544  C   ILE A 413     5981   7940   8462    -67   -356    -23       C  
ATOM   2545  O   ILE A 413     -43.422  28.526   0.776  1.00 58.85           O  
ANISOU 2545  O   ILE A 413     5894   7915   8551    -61   -404     36       O  
ATOM   2546  CB  ILE A 413     -40.112  28.676   0.881  1.00 60.69           C  
ANISOU 2546  CB  ILE A 413     6174   8128   8758    -91   -418    179       C  
ATOM   2547  CG1 ILE A 413     -39.835  27.353   0.162  1.00 61.85           C  
ANISOU 2547  CG1 ILE A 413     6385   8446   8668   -103   -347    196       C  
ATOM   2548  CG2 ILE A 413     -38.831  29.277   1.491  1.00 61.02           C  
ANISOU 2548  CG2 ILE A 413     6207   8071   8908    -95   -457    199       C  
ATOM   2549  CD1 ILE A 413     -40.290  27.353  -1.298  1.00 73.85           C  
ANISOU 2549  CD1 ILE A 413     7837  10101  10122   -112   -367    338       C  
ATOM   2550  N   VAL A 414     -42.624  26.521   1.475  1.00 53.73           N  
ANISOU 2550  N   VAL A 414     5415   7377   7624    -80   -279   -105       N  
ATOM   2551  CA  VAL A 414     -43.725  25.704   0.947  1.00 52.54           C  
ANISOU 2551  CA  VAL A 414     5273   7316   7375    -93   -251   -130       C  
ATOM   2552  C   VAL A 414     -45.010  25.918   1.790  1.00 55.87           C  
ANISOU 2552  C   VAL A 414     5669   7686   7871    -78   -239   -244       C  
ATOM   2553  O   VAL A 414     -46.076  26.137   1.214  1.00 54.49           O  
ANISOU 2553  O   VAL A 414     5434   7536   7733    -77   -263   -217       O  
ATOM   2554  CB  VAL A 414     -43.343  24.202   0.812  1.00 55.55           C  
ANISOU 2554  CB  VAL A 414     5747   7789   7570   -112   -195   -176       C  
ATOM   2555  CG1 VAL A 414     -44.512  23.385   0.256  1.00 55.28           C  
ANISOU 2555  CG1 VAL A 414     5713   7827   7463   -130   -185   -211       C  
ATOM   2556  CG2 VAL A 414     -42.122  24.035  -0.091  1.00 55.05           C  
ANISOU 2556  CG2 VAL A 414     5688   7803   7424   -111   -208    -74       C  
ATOM   2557  N   GLY A 415     -44.890  25.872   3.119  1.00 53.14           N  
ANISOU 2557  N   GLY A 415     5360   7290   7539    -60   -204   -365       N  
ATOM   2558  CA  GLY A 415     -46.010  26.120   4.025  1.00 53.39           C  
ANISOU 2558  CA  GLY A 415     5356   7305   7626    -34   -185   -480       C  
ATOM   2559  C   GLY A 415     -46.536  27.536   3.871  1.00 58.25           C  
ANISOU 2559  C   GLY A 415     5867   7834   8431     10   -259   -469       C  
ATOM   2560  O   GLY A 415     -47.747  27.739   3.783  1.00 59.44           O  
ANISOU 2560  O   GLY A 415     5956   8002   8627     27   -264   -499       O  
ATOM   2561  N   GLY A 416     -45.616  28.503   3.787  1.00 54.93           N  
ANISOU 2561  N   GLY A 416     5419   7315   8136     27   -326   -416       N  
ATOM   2562  CA  GLY A 416     -45.921  29.917   3.580  1.00 55.51           C  
ANISOU 2562  CA  GLY A 416     5389   7271   8432     66   -423   -385       C  
ATOM   2563  C   GLY A 416     -46.632  30.152   2.265  1.00 58.85           C  
ANISOU 2563  C   GLY A 416     5744   7726   8892     47   -465   -239       C  
ATOM   2564  O   GLY A 416     -47.608  30.902   2.220  1.00 59.96           O  
ANISOU 2564  O   GLY A 416     5799   7813   9171     83   -514   -258       O  
ATOM   2565  N   TYR A 417     -46.172  29.471   1.194  1.00 54.15           N  
ANISOU 2565  N   TYR A 417     5180   7233   8162     -4   -447   -102       N  
ATOM   2566  CA  TYR A 417     -46.769  29.513  -0.144  1.00 54.12           C  
ANISOU 2566  CA  TYR A 417     5115   7307   8142    -24   -481     43       C  
ATOM   2567  C   TYR A 417     -48.246  29.080  -0.077  1.00 57.88           C  
ANISOU 2567  C   TYR A 417     5573   7836   8581    -15   -451    -46       C  
ATOM   2568  O   TYR A 417     -49.109  29.761  -0.627  1.00 58.29           O  
ANISOU 2568  O   TYR A 417     5535   7872   8741      0   -508     16       O  
ATOM   2569  CB  TYR A 417     -45.979  28.602  -1.130  1.00 54.76           C  
ANISOU 2569  CB  TYR A 417     5242   7530   8032    -65   -451    151       C  
ATOM   2570  CG  TYR A 417     -46.667  28.376  -2.467  1.00 56.93           C  
ANISOU 2570  CG  TYR A 417     5464   7935   8229    -80   -473    262       C  
ATOM   2571  CD1 TYR A 417     -46.526  29.288  -3.509  1.00 59.99           C  
ANISOU 2571  CD1 TYR A 417     5748   8345   8698    -84   -550    460       C  
ATOM   2572  CD2 TYR A 417     -47.486  27.264  -2.677  1.00 56.78           C  
ANISOU 2572  CD2 TYR A 417     5490   8021   8064    -93   -427    175       C  
ATOM   2573  CE1 TYR A 417     -47.180  29.102  -4.727  1.00 62.05           C  
ANISOU 2573  CE1 TYR A 417     5953   8751   8873    -92   -574    562       C  
ATOM   2574  CE2 TYR A 417     -48.147  27.070  -3.890  1.00 57.78           C  
ANISOU 2574  CE2 TYR A 417     5562   8272   8118   -101   -458    258       C  
ATOM   2575  CZ  TYR A 417     -47.976  27.983  -4.919  1.00 67.64           C  
ANISOU 2575  CZ  TYR A 417     6711   9565   9424    -98   -528    449       C  
ATOM   2576  OH  TYR A 417     -48.609  27.801  -6.126  1.00 70.17           O  
ANISOU 2576  OH  TYR A 417     6972  10035   9655   -102   -562    534       O  
ATOM   2577  N   PHE A 418     -48.520  27.932   0.566  1.00 53.54           N  
ANISOU 2577  N   PHE A 418     5104   7352   7886    -30   -367   -173       N  
ATOM   2578  CA  PHE A 418     -49.868  27.396   0.677  1.00 53.95           C  
ANISOU 2578  CA  PHE A 418     5136   7464   7897    -35   -334   -247       C  
ATOM   2579  C   PHE A 418     -50.755  28.285   1.532  1.00 59.23           C  
ANISOU 2579  C   PHE A 418     5728   8059   8717     21   -349   -344       C  
ATOM   2580  O   PHE A 418     -51.937  28.424   1.209  1.00 60.29           O  
ANISOU 2580  O   PHE A 418     5794   8227   8889     29   -363   -346       O  
ATOM   2581  CB  PHE A 418     -49.862  25.955   1.197  1.00 55.19           C  
ANISOU 2581  CB  PHE A 418     5387   7697   7886    -73   -251   -335       C  
ATOM   2582  CG  PHE A 418     -49.401  24.960   0.164  1.00 56.68           C  
ANISOU 2582  CG  PHE A 418     5632   7974   7931   -116   -248   -268       C  
ATOM   2583  CD1 PHE A 418     -49.968  24.940  -1.113  1.00 61.24           C  
ANISOU 2583  CD1 PHE A 418     6157   8627   8484   -128   -295   -185       C  
ATOM   2584  CD2 PHE A 418     -48.430  24.016   0.471  1.00 57.56           C  
ANISOU 2584  CD2 PHE A 418     5840   8103   7927   -137   -206   -301       C  
ATOM   2585  CE1 PHE A 418     -49.543  24.018  -2.071  1.00 62.05           C  
ANISOU 2585  CE1 PHE A 418     6303   8830   8444   -153   -300   -152       C  
ATOM   2586  CE2 PHE A 418     -48.011  23.089  -0.485  1.00 60.75           C  
ANISOU 2586  CE2 PHE A 418     6288   8590   8204   -161   -212   -267       C  
ATOM   2587  CZ  PHE A 418     -48.555  23.109  -1.754  1.00 60.44           C  
ANISOU 2587  CZ  PHE A 418     6195   8635   8136   -165   -260   -200       C  
ATOM   2588  N   LEU A 419     -50.193  28.929   2.576  1.00 55.15           N  
ANISOU 2588  N   LEU A 419     5213   7448   8292     66   -357   -431       N  
ATOM   2589  CA  LEU A 419     -50.966  29.856   3.403  1.00 55.44           C  
ANISOU 2589  CA  LEU A 419     5167   7419   8480    140   -384   -552       C  
ATOM   2590  C   LEU A 419     -51.410  31.065   2.576  1.00 60.17           C  
ANISOU 2590  C   LEU A 419     5658   7921   9282    172   -493   -457       C  
ATOM   2591  O   LEU A 419     -52.608  31.335   2.556  1.00 61.32           O  
ANISOU 2591  O   LEU A 419     5722   8079   9496    209   -506   -502       O  
ATOM   2592  CB  LEU A 419     -50.218  30.293   4.675  1.00 55.25           C  
ANISOU 2592  CB  LEU A 419     5167   7326   8501    190   -380   -688       C  
ATOM   2593  CG  LEU A 419     -50.253  29.297   5.851  1.00 58.00           C  
ANISOU 2593  CG  LEU A 419     5580   7784   8675    185   -274   -818       C  
ATOM   2594  CD1 LEU A 419     -49.345  29.753   6.995  1.00 57.54           C  
ANISOU 2594  CD1 LEU A 419     5547   7671   8646    234   -282   -938       C  
ATOM   2595  CD2 LEU A 419     -51.677  29.062   6.354  1.00 57.75           C  
ANISOU 2595  CD2 LEU A 419     5480   7852   8611    215   -224   -915       C  
ATOM   2596  N   ILE A 420     -50.492  31.703   1.805  1.00 56.95           N  
ANISOU 2596  N   ILE A 420     5239   7434   8965    152   -569   -305       N  
ATOM   2597  CA  ILE A 420     -50.798  32.858   0.932  1.00 58.30           C  
ANISOU 2597  CA  ILE A 420     5299   7510   9341    170   -685   -167       C  
ATOM   2598  C   ILE A 420     -51.842  32.468  -0.151  1.00 63.29           C  
ANISOU 2598  C   ILE A 420     5888   8259   9901    142   -681    -64       C  
ATOM   2599  O   ILE A 420     -52.779  33.231  -0.403  1.00 64.82           O  
ANISOU 2599  O   ILE A 420     5979   8401  10247    182   -747    -45       O  
ATOM   2600  CB  ILE A 420     -49.513  33.463   0.292  1.00 61.40           C  
ANISOU 2600  CB  ILE A 420     5684   7825   9820    135   -758     12       C  
ATOM   2601  CG1 ILE A 420     -48.577  34.059   1.374  1.00 61.19           C  
ANISOU 2601  CG1 ILE A 420     5678   7655   9916    169   -789    -99       C  
ATOM   2602  CG2 ILE A 420     -49.862  34.524  -0.777  1.00 63.66           C  
ANISOU 2602  CG2 ILE A 420     5845   8040  10302    137   -879    209       C  
ATOM   2603  CD1 ILE A 420     -47.072  34.085   1.002  1.00 56.85           C  
ANISOU 2603  CD1 ILE A 420     5165   7086   9350    114   -809     45       C  
ATOM   2604  N   ARG A 421     -51.668  31.285  -0.770  1.00 58.46           N  
ANISOU 2604  N   ARG A 421     5350   7800   9063     80   -613    -10       N  
ATOM   2605  CA  ARG A 421     -52.559  30.735  -1.788  1.00 57.97           C  
ANISOU 2605  CA  ARG A 421     5258   7867   8903     50   -610     65       C  
ATOM   2606  C   ARG A 421     -53.901  30.431  -1.177  1.00 61.82           C  
ANISOU 2606  C   ARG A 421     5716   8382   9389     74   -570    -78       C  
ATOM   2607  O   ARG A 421     -54.936  30.608  -1.835  1.00 62.27           O  
ANISOU 2607  O   ARG A 421     5694   8484   9482     78   -606    -28       O  
ATOM   2608  CB  ARG A 421     -51.960  29.470  -2.412  1.00 57.63           C  
ANISOU 2608  CB  ARG A 421     5305   7968   8624    -10   -553    106       C  
ATOM   2609  CG  ARG A 421     -51.245  29.744  -3.726  1.00 72.89           C  
ANISOU 2609  CG  ARG A 421     7203   9971  10522    -33   -611    310       C  
ATOM   2610  CD  ARG A 421     -51.453  28.583  -4.669  1.00 88.98           C  
ANISOU 2610  CD  ARG A 421     9278  12191  12341    -69   -581    327       C  
ATOM   2611  NE  ARG A 421     -51.702  29.017  -6.042  1.00 99.61           N  
ANISOU 2611  NE  ARG A 421    10531  13646  13668    -73   -651    507       N  
ATOM   2612  CZ  ARG A 421     -52.648  28.507  -6.823  1.00117.21           C  
ANISOU 2612  CZ  ARG A 421    12725  15999  15811    -82   -668    510       C  
ATOM   2613  NH1 ARG A 421     -53.444  27.545  -6.372  1.00103.63           N  
ANISOU 2613  NH1 ARG A 421    11052  14293  14030    -95   -621    349       N  
ATOM   2614  NH2 ARG A 421     -52.805  28.951  -8.062  1.00108.43           N  
ANISOU 2614  NH2 ARG A 421    11522  15006  14671    -81   -735    684       N  
ATOM   2615  N   GLY A 422     -53.860  30.002   0.088  1.00 56.43           N  
ANISOU 2615  N   GLY A 422     5087   7688   8665     91   -496   -246       N  
ATOM   2616  CA  GLY A 422     -55.035  29.702   0.888  1.00 55.49           C  
ANISOU 2616  CA  GLY A 422     4931   7616   8535    116   -444   -385       C  
ATOM   2617  C   GLY A 422     -55.862  30.940   1.156  1.00 57.68           C  
ANISOU 2617  C   GLY A 422     5086   7810   9019    199   -509   -432       C  
ATOM   2618  O   GLY A 422     -57.087  30.856   1.090  1.00 56.90           O  
ANISOU 2618  O   GLY A 422     4915   7774   8931    213   -500   -462       O  
ATOM   2619  N   VAL A 423     -55.207  32.110   1.428  1.00 54.82           N  
ANISOU 2619  N   VAL A 423     4692   7298   8840    256   -585   -438       N  
ATOM   2620  CA  VAL A 423     -55.966  33.338   1.669  1.00 56.71           C  
ANISOU 2620  CA  VAL A 423     4807   7428   9311    348   -668   -497       C  
ATOM   2621  C   VAL A 423     -56.529  33.843   0.324  1.00 61.78           C  
ANISOU 2621  C   VAL A 423     5365   8055  10054    332   -758   -311       C  
ATOM   2622  O   VAL A 423     -57.687  34.271   0.295  1.00 62.11           O  
ANISOU 2622  O   VAL A 423     5306   8096  10199    385   -790   -350       O  
ATOM   2623  CB  VAL A 423     -55.295  34.466   2.512  1.00 61.88           C  
ANISOU 2623  CB  VAL A 423     5436   7908  10166    427   -742   -597       C  
ATOM   2624  CG1 VAL A 423     -54.507  33.903   3.687  1.00 60.59           C  
ANISOU 2624  CG1 VAL A 423     5364   7786   9872    434   -657   -758       C  
ATOM   2625  CG2 VAL A 423     -54.442  35.410   1.678  1.00 62.71           C  
ANISOU 2625  CG2 VAL A 423     5524   7865  10438    401   -859   -413       C  
ATOM   2626  N   MET A 424     -55.762  33.698  -0.788  1.00 58.29           N  
ANISOU 2626  N   MET A 424     4959   7632   9556    261   -789   -110       N  
ATOM   2627  CA  MET A 424     -56.214  34.088  -2.135  1.00 59.15           C  
ANISOU 2627  CA  MET A 424     4987   7768   9719    238   -870     92       C  
ATOM   2628  C   MET A 424     -57.502  33.338  -2.504  1.00 61.94           C  
ANISOU 2628  C   MET A 424     5312   8270   9952    222   -826     66       C  
ATOM   2629  O   MET A 424     -58.481  33.964  -2.924  1.00 62.37           O  
ANISOU 2629  O   MET A 424     5256   8306  10135    258   -895    115       O  
ATOM   2630  CB  MET A 424     -55.127  33.825  -3.185  1.00 61.27           C  
ANISOU 2630  CB  MET A 424     5302   8098   9879    165   -885    294       C  
ATOM   2631  CG  MET A 424     -54.001  34.833  -3.161  1.00 66.34           C  
ANISOU 2631  CG  MET A 424     5920   8587  10698    172   -968    401       C  
ATOM   2632  SD  MET A 424     -52.657  34.357  -4.286  1.00 71.13           S  
ANISOU 2632  SD  MET A 424     6575   9318  11131     89   -959    630       S  
ATOM   2633  CE  MET A 424     -53.443  34.655  -5.899  1.00 68.78           C  
ANISOU 2633  CE  MET A 424     6156   9142  10836     69  -1041    877       C  
ATOM   2634  N   THR A 425     -57.508  32.004  -2.278  1.00 57.45           N  
ANISOU 2634  N   THR A 425     4838   7835   9155    169   -720    -16       N  
ATOM   2635  CA  THR A 425     -58.649  31.123  -2.536  1.00 56.86           C  
ANISOU 2635  CA  THR A 425     4745   7897   8961    138   -677    -51       C  
ATOM   2636  C   THR A 425     -59.799  31.454  -1.582  1.00 61.38           C  
ANISOU 2636  C   THR A 425     5235   8450   9637    203   -656   -200       C  
ATOM   2637  O   THR A 425     -60.943  31.502  -2.035  1.00 62.80           O  
ANISOU 2637  O   THR A 425     5326   8688   9848    210   -682   -177       O  
ATOM   2638  CB  THR A 425     -58.252  29.647  -2.458  1.00 61.49           C  
ANISOU 2638  CB  THR A 425     5449   8598   9316     63   -587    -97       C  
ATOM   2639  OG1 THR A 425     -56.974  29.475  -3.074  1.00 62.22           O  
ANISOU 2639  OG1 THR A 425     5618   8694   9328     29   -600      4       O  
ATOM   2640  CG2 THR A 425     -59.260  28.757  -3.152  1.00 58.44           C  
ANISOU 2640  CG2 THR A 425     5040   8345   8820     14   -582    -79       C  
ATOM   2641  N   LEU A 426     -59.501  31.702  -0.281  1.00 56.97           N  
ANISOU 2641  N   LEU A 426     4695   7827   9125    257   -611   -356       N  
ATOM   2642  CA  LEU A 426     -60.506  32.092   0.715  1.00 57.07           C  
ANISOU 2642  CA  LEU A 426     4616   7844   9223    339   -588   -518       C  
ATOM   2643  C   LEU A 426     -61.282  33.327   0.205  1.00 61.22           C  
ANISOU 2643  C   LEU A 426     5004   8278   9979    417   -700   -476       C  
ATOM   2644  O   LEU A 426     -62.506  33.275   0.157  1.00 62.12           O  
ANISOU 2644  O   LEU A 426     5023   8464  10114    445   -693   -515       O  
ATOM   2645  CB  LEU A 426     -59.851  32.358   2.102  1.00 56.83           C  
ANISOU 2645  CB  LEU A 426     4623   7762   9209    399   -544   -687       C  
ATOM   2646  CG  LEU A 426     -60.626  33.225   3.138  1.00 63.36           C  
ANISOU 2646  CG  LEU A 426     5334   8568  10172    526   -553   -875       C  
ATOM   2647  CD1 LEU A 426     -61.996  32.626   3.498  1.00 63.97           C  
ANISOU 2647  CD1 LEU A 426     5337   8821  10149    530   -470   -948       C  
ATOM   2648  CD2 LEU A 426     -59.812  33.412   4.407  1.00 66.20           C  
ANISOU 2648  CD2 LEU A 426     5738   8886  10529    584   -524  -1038       C  
ATOM   2649  N   PHE A 427     -60.572  34.391  -0.230  1.00 57.14           N  
ANISOU 2649  N   PHE A 427     4468   7601   9640    446   -809   -380       N  
ATOM   2650  CA  PHE A 427     -61.192  35.609  -0.753  1.00 58.83           C  
ANISOU 2650  CA  PHE A 427     4549   7700  10104    516   -935   -313       C  
ATOM   2651  C   PHE A 427     -61.977  35.344  -2.040  1.00 62.40           C  
ANISOU 2651  C   PHE A 427     4946   8250  10511    464   -970   -138       C  
ATOM   2652  O   PHE A 427     -63.075  35.884  -2.197  1.00 64.74           O  
ANISOU 2652  O   PHE A 427     5121   8534  10942    524  -1026   -145       O  
ATOM   2653  CB  PHE A 427     -60.153  36.719  -0.981  1.00 61.73           C  
ANISOU 2653  CB  PHE A 427     4907   7866  10682    539  -1053   -217       C  
ATOM   2654  CG  PHE A 427     -59.662  37.373   0.292  1.00 64.08           C  
ANISOU 2654  CG  PHE A 427     5207   8024  11115    626  -1068   -419       C  
ATOM   2655  CD1 PHE A 427     -60.545  38.040   1.140  1.00 69.26           C  
ANISOU 2655  CD1 PHE A 427     5762   8630  11925    751  -1095   -622       C  
ATOM   2656  CD2 PHE A 427     -58.313  37.364   0.621  1.00 64.80           C  
ANISOU 2656  CD2 PHE A 427     5392   8041  11189    594  -1066   -411       C  
ATOM   2657  CE1 PHE A 427     -60.087  38.636   2.323  1.00 71.02           C  
ANISOU 2657  CE1 PHE A 427     5981   8742  12262    844  -1117   -835       C  
ATOM   2658  CE2 PHE A 427     -57.856  37.967   1.798  1.00 68.25           C  
ANISOU 2658  CE2 PHE A 427     5827   8355  11750    678  -1091   -611       C  
ATOM   2659  CZ  PHE A 427     -58.741  38.602   2.637  1.00 68.08           C  
ANISOU 2659  CZ  PHE A 427     5707   8293  11868    805  -1119   -827       C  
ATOM   2660  N   SER A 428     -61.449  34.478  -2.916  1.00 55.80           N  
ANISOU 2660  N   SER A 428     4195   7527   9478    361   -938      0       N  
ATOM   2661  CA  SER A 428     -62.075  34.090  -4.176  1.00 55.47           C  
ANISOU 2661  CA  SER A 428     4113   7612   9351    307   -970    155       C  
ATOM   2662  C   SER A 428     -63.423  33.378  -3.931  1.00 60.21           C  
ANISOU 2662  C   SER A 428     4670   8340   9868    305   -910     44       C  
ATOM   2663  O   SER A 428     -64.405  33.686  -4.623  1.00 60.41           O  
ANISOU 2663  O   SER A 428     4590   8406   9957    319   -972    120       O  
ATOM   2664  CB  SER A 428     -61.130  33.199  -4.982  1.00 58.23           C  
ANISOU 2664  CB  SER A 428     4569   8070   9485    214   -940    272       C  
ATOM   2665  OG  SER A 428     -61.684  32.892  -6.251  1.00 72.83           O  
ANISOU 2665  OG  SER A 428     6370  10054  11247    173   -985    414       O  
ATOM   2666  N   ILE A 429     -63.478  32.443  -2.938  1.00 56.01           N  
ANISOU 2666  N   ILE A 429     4207   7874   9201    285   -794   -121       N  
ATOM   2667  CA  ILE A 429     -64.729  31.739  -2.592  1.00 55.28           C  
ANISOU 2667  CA  ILE A 429     4061   7906   9037    273   -733   -215       C  
ATOM   2668  C   ILE A 429     -65.720  32.754  -2.050  1.00 58.63           C  
ANISOU 2668  C   ILE A 429     4342   8279   9657    383   -768   -302       C  
ATOM   2669  O   ILE A 429     -66.859  32.766  -2.494  1.00 59.80           O  
ANISOU 2669  O   ILE A 429     4387   8498   9835    390   -794   -276       O  
ATOM   2670  CB  ILE A 429     -64.547  30.536  -1.598  1.00 56.88           C  
ANISOU 2670  CB  ILE A 429     4355   8195   9062    220   -605   -341       C  
ATOM   2671  CG1 ILE A 429     -63.591  29.444  -2.127  1.00 55.68           C  
ANISOU 2671  CG1 ILE A 429     4343   8087   8727    118   -578   -272       C  
ATOM   2672  CG2 ILE A 429     -65.899  29.936  -1.180  1.00 57.32           C  
ANISOU 2672  CG2 ILE A 429     4326   8378   9074    206   -549   -415       C  
ATOM   2673  CD1 ILE A 429     -63.894  28.841  -3.497  1.00 62.09           C  
ANISOU 2673  CD1 ILE A 429     5153   8990   9449     48   -633   -149       C  
ATOM   2674  N   LYS A 430     -65.290  33.619  -1.117  1.00 55.63           N  
ANISOU 2674  N   LYS A 430     3948   7774   9415    477   -778   -414       N  
ATOM   2675  CA  LYS A 430     -66.169  34.641  -0.524  1.00 57.36           C  
ANISOU 2675  CA  LYS A 430     4025   7935   9834    605   -821   -533       C  
ATOM   2676  C   LYS A 430     -66.754  35.539  -1.611  1.00 63.86           C  
ANISOU 2676  C   LYS A 430     4736   8683  10844    638   -954   -388       C  
ATOM   2677  O   LYS A 430     -67.933  35.883  -1.555  1.00 64.10           O  
ANISOU 2677  O   LYS A 430     4637   8749  10970    705   -977   -439       O  
ATOM   2678  CB  LYS A 430     -65.423  35.479   0.535  1.00 59.54           C  
ANISOU 2678  CB  LYS A 430     4312   8070  10240    704   -837   -683       C  
ATOM   2679  CG  LYS A 430     -65.056  34.716   1.813  1.00 64.66           C  
ANISOU 2679  CG  LYS A 430     5035   8818  10714    700   -706   -855       C  
ATOM   2680  CD  LYS A 430     -66.104  34.861   2.908  1.00 71.44           C  
ANISOU 2680  CD  LYS A 430     5775   9778  11591    809   -651  -1061       C  
ATOM   2681  CE  LYS A 430     -65.538  34.547   4.271  1.00 82.12           C  
ANISOU 2681  CE  LYS A 430     7183  11207  12811    835   -549  -1232       C  
ATOM   2682  NZ  LYS A 430     -66.574  34.649   5.331  1.00 94.75           N  
ANISOU 2682  NZ  LYS A 430     8652  12958  14392    943   -484  -1425       N  
ATOM   2683  N   SER A 431     -65.938  35.848  -2.635  1.00 62.58           N  
ANISOU 2683  N   SER A 431     4618   8440  10721    587  -1039   -191       N  
ATOM   2684  CA  SER A 431     -66.324  36.687  -3.767  1.00 64.45           C  
ANISOU 2684  CA  SER A 431     4751   8613  11123    604  -1173     -5       C  
ATOM   2685  C   SER A 431     -67.257  35.934  -4.738  1.00 67.53           C  
ANISOU 2685  C   SER A 431     5104   9184  11371    536  -1165    101       C  
ATOM   2686  O   SER A 431     -68.353  36.420  -5.012  1.00 67.48           O  
ANISOU 2686  O   SER A 431     4966   9185  11487    590  -1225    116       O  
ATOM   2687  CB  SER A 431     -65.078  37.195  -4.499  1.00 69.05           C  
ANISOU 2687  CB  SER A 431     5385   9086  11767    563  -1256    189       C  
ATOM   2688  OG  SER A 431     -65.419  38.053  -5.576  1.00 84.37           O  
ANISOU 2688  OG  SER A 431     7213  10972  13873    576  -1392    400       O  
ATOM   2689  N   ASN A 432     -66.834  34.747  -5.235  1.00 63.26           N  
ANISOU 2689  N   ASN A 432     4673   8784  10580    423  -1100    162       N  
ATOM   2690  CA  ASN A 432     -67.592  33.978  -6.230  1.00 63.02           C  
ANISOU 2690  CA  ASN A 432     4615   8923  10404    352  -1108    254       C  
ATOM   2691  C   ASN A 432     -68.771  33.169  -5.674  1.00 65.89           C  
ANISOU 2691  C   ASN A 432     4938   9408  10689    341  -1029    110       C  
ATOM   2692  O   ASN A 432     -69.697  32.879  -6.439  1.00 67.57           O  
ANISOU 2692  O   ASN A 432     5077   9730  10865    311  -1067    175       O  
ATOM   2693  CB  ASN A 432     -66.665  33.074  -7.021  1.00 62.65           C  
ANISOU 2693  CB  ASN A 432     4691   8975  10138    252  -1086    352       C  
ATOM   2694  CG  ASN A 432     -65.798  33.869  -7.961  1.00 85.29           C  
ANISOU 2694  CG  ASN A 432     7549  11793  13063    251  -1182    561       C  
ATOM   2695  OD1 ASN A 432     -66.284  34.546  -8.867  1.00 82.24           O  
ANISOU 2695  OD1 ASN A 432     7056  11426  12768    270  -1285    721       O  
ATOM   2696  ND2 ASN A 432     -64.501  33.856  -7.732  1.00 79.28           N  
ANISOU 2696  ND2 ASN A 432     6891  10975  12257    230  -1154    578       N  
ATOM   2697  N   HIS A 433     -68.780  32.833  -4.372  1.00 59.65           N  
ANISOU 2697  N   HIS A 433     4179   8613   9873    363   -926    -71       N  
ATOM   2698  CA  HIS A 433     -69.909  32.099  -3.761  1.00 58.22           C  
ANISOU 2698  CA  HIS A 433     3938   8560   9624    349   -846   -188       C  
ATOM   2699  C   HIS A 433     -70.451  32.916  -2.579  1.00 64.50           C  
ANISOU 2699  C   HIS A 433     4631   9306  10569    474   -819   -346       C  
ATOM   2700  O   HIS A 433     -70.172  32.569  -1.427  1.00 64.29           O  
ANISOU 2700  O   HIS A 433     4648   9304  10476    487   -721   -485       O  
ATOM   2701  CB  HIS A 433     -69.471  30.690  -3.330  1.00 56.21           C  
ANISOU 2701  CB  HIS A 433     3806   8397   9154    244   -739   -242       C  
ATOM   2702  CG  HIS A 433     -68.898  29.882  -4.446  1.00 57.79           C  
ANISOU 2702  CG  HIS A 433     4106   8642   9210    141   -771   -125       C  
ATOM   2703  ND1 HIS A 433     -67.550  29.922  -4.744  1.00 58.38           N  
ANISOU 2703  ND1 HIS A 433     4300   8648   9233    124   -783    -69       N  
ATOM   2704  CD2 HIS A 433     -69.511  29.057  -5.317  1.00 58.76           C  
ANISOU 2704  CD2 HIS A 433     4214   8879   9231     61   -800    -70       C  
ATOM   2705  CE1 HIS A 433     -67.386  29.112  -5.776  1.00 56.92           C  
ANISOU 2705  CE1 HIS A 433     4167   8552   8906     43   -812     12       C  
ATOM   2706  NE2 HIS A 433     -68.540  28.572  -6.156  1.00 57.79           N  
ANISOU 2706  NE2 HIS A 433     4203   8769   8985      4   -829      7       N  
ATOM   2707  N   PRO A 434     -71.161  34.046  -2.841  1.00 63.64           N  
ANISOU 2707  N   PRO A 434     4382   9129  10669    577   -912   -332       N  
ATOM   2708  CA  PRO A 434     -71.626  34.909  -1.737  1.00 64.70           C  
ANISOU 2708  CA  PRO A 434     4411   9212  10959    719   -901   -510       C  
ATOM   2709  C   PRO A 434     -72.452  34.207  -0.659  1.00 68.35           C  
ANISOU 2709  C   PRO A 434     4814   9849  11307    730   -774   -669       C  
ATOM   2710  O   PRO A 434     -73.472  33.567  -0.949  1.00 67.88           O  
ANISOU 2710  O   PRO A 434     4680   9934  11177    678   -748   -631       O  
ATOM   2711  CB  PRO A 434     -72.475  35.975  -2.450  1.00 68.02           C  
ANISOU 2711  CB  PRO A 434     4681   9556  11608    806  -1033   -439       C  
ATOM   2712  CG  PRO A 434     -72.809  35.382  -3.793  1.00 72.32           C  
ANISOU 2712  CG  PRO A 434     5228  10192  12057    696  -1076   -243       C  
ATOM   2713  CD  PRO A 434     -71.570  34.614  -4.143  1.00 66.38           C  
ANISOU 2713  CD  PRO A 434     4651   9448  11122    577  -1040   -158       C  
ATOM   2714  N   GLY A 435     -71.980  34.350   0.579  1.00 64.66           N  
ANISOU 2714  N   GLY A 435     4371   9376  10821    798   -701   -838       N  
ATOM   2715  CA  GLY A 435     -72.617  33.825   1.782  1.00 64.76           C  
ANISOU 2715  CA  GLY A 435     4315   9570  10720    828   -576   -993       C  
ATOM   2716  C   GLY A 435     -72.465  32.339   2.039  1.00 67.11           C  
ANISOU 2716  C   GLY A 435     4704  10020  10774    681   -456   -948       C  
ATOM   2717  O   GLY A 435     -73.033  31.833   3.010  1.00 68.86           O  
ANISOU 2717  O   GLY A 435     4857  10413  10893    691   -349  -1042       O  
ATOM   2718  N   LEU A 436     -71.727  31.617   1.171  1.00 60.23           N  
ANISOU 2718  N   LEU A 436     3975   9099   9811    548   -477   -802       N  
ATOM   2719  CA  LEU A 436     -71.507  30.171   1.309  1.00 57.63           C  
ANISOU 2719  CA  LEU A 436     3740   8879   9277    404   -388   -754       C  
ATOM   2720  C   LEU A 436     -70.727  29.894   2.601  1.00 60.20           C  
ANISOU 2720  C   LEU A 436     4136   9235   9501    421   -286   -866       C  
ATOM   2721  O   LEU A 436     -71.205  29.125   3.434  1.00 59.94           O  
ANISOU 2721  O   LEU A 436     4059   9363   9353    385   -185   -904       O  
ATOM   2722  CB  LEU A 436     -70.804  29.583   0.068  1.00 55.75           C  
ANISOU 2722  CB  LEU A 436     3635   8570   8978    287   -450   -603       C  
ATOM   2723  CG  LEU A 436     -70.420  28.092   0.112  1.00 58.49           C  
ANISOU 2723  CG  LEU A 436     4093   8990   9141    143   -385   -562       C  
ATOM   2724  CD1 LEU A 436     -71.647  27.181   0.008  1.00 57.89           C  
ANISOU 2724  CD1 LEU A 436     3920   9057   9020     62   -364   -528       C  
ATOM   2725  CD2 LEU A 436     -69.411  27.756  -0.973  1.00 58.39           C  
ANISOU 2725  CD2 LEU A 436     4221   8891   9071     72   -448   -460       C  
ATOM   2726  N   LEU A 437     -69.573  30.557   2.790  1.00 55.55           N  
ANISOU 2726  N   LEU A 437     3641   8503   8961    478   -316   -911       N  
ATOM   2727  CA  LEU A 437     -68.782  30.394   4.007  1.00 54.59           C  
ANISOU 2727  CA  LEU A 437     3584   8408   8749    506   -232  -1026       C  
ATOM   2728  C   LEU A 437     -69.310  31.340   5.083  1.00 64.71           C  
ANISOU 2728  C   LEU A 437     4730   9742  10117    670   -214  -1214       C  
ATOM   2729  O   LEU A 437     -68.800  32.457   5.256  1.00 66.19           O  
ANISOU 2729  O   LEU A 437     4916   9787  10449    784   -285  -1309       O  
ATOM   2730  CB  LEU A 437     -67.277  30.615   3.748  1.00 52.15           C  
ANISOU 2730  CB  LEU A 437     3435   7932   8447    486   -275   -993       C  
ATOM   2731  CG  LEU A 437     -66.592  29.642   2.789  1.00 52.92           C  
ANISOU 2731  CG  LEU A 437     3672   8002   8434    341   -284   -837       C  
ATOM   2732  CD1 LEU A 437     -65.188  30.116   2.477  1.00 52.71           C  
ANISOU 2732  CD1 LEU A 437     3766   7815   8445    347   -339   -801       C  
ATOM   2733  CD2 LEU A 437     -66.577  28.226   3.342  1.00 49.66           C  
ANISOU 2733  CD2 LEU A 437     3316   7722   7833    237   -178   -830       C  
ATOM   2734  N   SER A 438     -70.380  30.899   5.770  1.00 63.62           N  
ANISOU 2734  N   SER A 438     4464   9814   9897    684   -126  -1268       N  
ATOM   2735  CA  SER A 438     -71.052  31.619   6.855  1.00 65.74           C  
ANISOU 2735  CA  SER A 438     4575  10203  10201    843    -87  -1459       C  
ATOM   2736  C   SER A 438     -71.847  30.632   7.744  1.00 73.09           C  
ANISOU 2736  C   SER A 438     5410  11418  10943    798     52  -1463       C  
ATOM   2737  O   SER A 438     -71.932  29.443   7.422  1.00 71.58           O  
ANISOU 2737  O   SER A 438     5272  11291  10635    637     98  -1307       O  
ATOM   2738  CB  SER A 438     -71.962  32.715   6.298  1.00 68.99           C  
ANISOU 2738  CB  SER A 438     4844  10544  10824    960   -188  -1500       C  
ATOM   2739  OG  SER A 438     -73.237  32.241   5.898  1.00 79.45           O  
ANISOU 2739  OG  SER A 438     6059  11998  12132    901   -171  -1401       O  
ATOM   2740  N   GLU A 439     -72.433  31.140   8.849  1.00 72.91           N  
ANISOU 2740  N   GLU A 439     5234  11569  10898    943    110  -1639       N  
ATOM   2741  CA  GLU A 439     -73.246  30.378   9.802  1.00 73.64           C  
ANISOU 2741  CA  GLU A 439     5196  11971  10814    924    245  -1644       C  
ATOM   2742  C   GLU A 439     -74.652  30.119   9.240  1.00 78.85           C  
ANISOU 2742  C   GLU A 439     5702  12741  11517    883    245  -1548       C  
ATOM   2743  O   GLU A 439     -75.417  29.335   9.814  1.00 79.88           O  
ANISOU 2743  O   GLU A 439     5716  13121  11513    827    349  -1491       O  
ATOM   2744  CB  GLU A 439     -73.327  31.136  11.135  1.00 76.53           C  
ANISOU 2744  CB  GLU A 439     5440  12504  11134   1117    299  -1887       C  
ATOM   2745  N   LYS A 440     -74.985  30.789   8.119  1.00 74.51           N  
ANISOU 2745  N   LYS A 440     5142  12009  11158    909    125  -1516       N  
ATOM   2746  CA  LYS A 440     -76.257  30.693   7.407  1.00 73.98           C  
ANISOU 2746  CA  LYS A 440     4937  12007  11163    879     96  -1426       C  
ATOM   2747  C   LYS A 440     -76.218  29.539   6.399  1.00 74.29           C  
ANISOU 2747  C   LYS A 440     5081  11995  11151    664     77  -1202       C  
ATOM   2748  O   LYS A 440     -77.257  28.914   6.147  1.00 74.43           O  
ANISOU 2748  O   LYS A 440     4986  12153  11141    583    103  -1106       O  
ATOM   2749  CB  LYS A 440     -76.533  32.032   6.688  1.00 77.47           C  
ANISOU 2749  CB  LYS A 440     5324  12267  11843   1017    -40  -1496       C  
ATOM   2750  CG  LYS A 440     -77.836  32.105   5.880  1.00 96.76           C  
ANISOU 2750  CG  LYS A 440     7620  14760  14386   1005    -89  -1411       C  
ATOM   2751  CD  LYS A 440     -77.565  32.150   4.371  1.00107.69           C  
ANISOU 2751  CD  LYS A 440     9113  15923  15882    911   -219  -1245       C  
ATOM   2752  CE  LYS A 440     -78.810  31.950   3.539  1.00120.97           C  
ANISOU 2752  CE  LYS A 440    10666  17678  17620    861   -262  -1133       C  
ATOM   2753  NZ  LYS A 440     -79.132  30.511   3.351  1.00129.28           N  
ANISOU 2753  NZ  LYS A 440    11739  18871  18511    671   -193   -993       N  
ATOM   2754  N   ALA A 441     -75.034  29.287   5.788  1.00 66.73           N  
ANISOU 2754  N   ALA A 441     4327  10838  10188    579     23  -1128       N  
ATOM   2755  CA  ALA A 441     -74.900  28.254   4.770  1.00 64.60           C  
ANISOU 2755  CA  ALA A 441     4163  10508   9875    397    -12   -949       C  
ATOM   2756  C   ALA A 441     -73.977  27.111   5.229  1.00 66.35           C  
ANISOU 2756  C   ALA A 441     4529  10744   9935    272     60   -894       C  
ATOM   2757  O   ALA A 441     -74.376  26.346   6.107  1.00 67.02           O  
ANISOU 2757  O   ALA A 441     4545  11013   9906    223    161   -879       O  
ATOM   2758  CB  ALA A 441     -74.422  28.864   3.462  1.00 64.27           C  
ANISOU 2758  CB  ALA A 441     4215  10247   9958    400   -147   -889       C  
ATOM   2759  N   ALA A 442     -72.772  26.972   4.636  1.00 59.87           N  
ANISOU 2759  N   ALA A 442     3898   9744   9106    219      7   -850       N  
ATOM   2760  CA  ALA A 442     -71.822  25.905   4.968  1.00 57.14           C  
ANISOU 2760  CA  ALA A 442     3698   9388   8626    106     60   -798       C  
ATOM   2761  C   ALA A 442     -71.103  26.209   6.300  1.00 61.26           C  
ANISOU 2761  C   ALA A 442     4243   9963   9072    192    145   -916       C  
ATOM   2762  O   ALA A 442     -69.908  26.479   6.320  1.00 60.65           O  
ANISOU 2762  O   ALA A 442     4303   9753   8988    217    123   -952       O  
ATOM   2763  CB  ALA A 442     -70.835  25.718   3.827  1.00 55.69           C  
ANISOU 2763  CB  ALA A 442     3687   9015   8457     39    -29   -724       C  
ATOM   2764  N   SER A 443     -71.856  26.151   7.413  1.00 59.55           N  
ANISOU 2764  N   SER A 443     3878   9961   8787    239    241   -974       N  
ATOM   2765  CA  SER A 443     -71.395  26.467   8.768  1.00 59.72           C  
ANISOU 2765  CA  SER A 443     3879  10098   8715    338    327  -1101       C  
ATOM   2766  C   SER A 443     -70.305  25.522   9.297  1.00 61.23           C  
ANISOU 2766  C   SER A 443     4216  10284   8765    239    382  -1041       C  
ATOM   2767  O   SER A 443     -69.390  25.996   9.968  1.00 60.00           O  
ANISOU 2767  O   SER A 443     4128  10099   8571    321    400  -1150       O  
ATOM   2768  CB  SER A 443     -72.568  26.511   9.745  1.00 65.02           C  
ANISOU 2768  CB  SER A 443     4334  11050   9321    401    422  -1153       C  
ATOM   2769  OG  SER A 443     -73.318  25.310   9.728  1.00 77.00           O  
ANISOU 2769  OG  SER A 443     5792  12709  10754    245    478   -985       O  
ATOM   2770  N   LYS A 444     -70.389  24.214   9.010  1.00 57.27           N  
ANISOU 2770  N   LYS A 444     3757   9802   8200     68    400   -876       N  
ATOM   2771  CA  LYS A 444     -69.374  23.257   9.467  1.00 56.15           C  
ANISOU 2771  CA  LYS A 444     3748   9642   7943    -31    441   -806       C  
ATOM   2772  C   LYS A 444     -68.054  23.461   8.707  1.00 60.91           C  
ANISOU 2772  C   LYS A 444     4553  10000   8589    -36    362   -821       C  
ATOM   2773  O   LYS A 444     -66.985  23.423   9.330  1.00 60.55           O  
ANISOU 2773  O   LYS A 444     4608   9930   8470    -17    394   -861       O  
ATOM   2774  CB  LYS A 444     -69.877  21.815   9.345  1.00 57.70           C  
ANISOU 2774  CB  LYS A 444     3922   9902   8100   -210    460   -627       C  
ATOM   2775  CG  LYS A 444     -71.067  21.535  10.264  1.00 66.50           C  
ANISOU 2775  CG  LYS A 444     4828  11291   9149   -218    554   -581       C  
ATOM   2776  CD  LYS A 444     -71.986  20.455   9.704  1.00 81.39           C  
ANISOU 2776  CD  LYS A 444     6641  13201  11082   -382    527   -409       C  
ATOM   2777  CE  LYS A 444     -73.365  20.474  10.338  1.00 97.31           C  
ANISOU 2777  CE  LYS A 444     8415  15482  13074   -369    601   -371       C  
ATOM   2778  NZ  LYS A 444     -74.244  21.542   9.774  1.00102.92           N  
ANISOU 2778  NZ  LYS A 444     9015  16204  13884   -250    562   -477       N  
ATOM   2779  N   ILE A 445     -68.127  23.708   7.373  1.00 58.13           N  
ANISOU 2779  N   ILE A 445     4250   9488   8350    -58    261   -785       N  
ATOM   2780  CA  ILE A 445     -66.950  23.989   6.540  1.00 56.90           C  
ANISOU 2780  CA  ILE A 445     4259   9127   8233    -57    183   -784       C  
ATOM   2781  C   ILE A 445     -66.362  25.334   6.983  1.00 60.71           C  
ANISOU 2781  C   ILE A 445     4747   9547   8773     95    170   -920       C  
ATOM   2782  O   ILE A 445     -65.160  25.407   7.218  1.00 58.70           O  
ANISOU 2782  O   ILE A 445     4614   9206   8483    105    170   -947       O  
ATOM   2783  CB  ILE A 445     -67.258  23.964   5.014  1.00 59.91           C  
ANISOU 2783  CB  ILE A 445     4663   9398   8702   -109     78   -704       C  
ATOM   2784  CG1 ILE A 445     -67.668  22.547   4.547  1.00 60.57           C  
ANISOU 2784  CG1 ILE A 445     4762   9514   8737   -263     70   -591       C  
ATOM   2785  CG2 ILE A 445     -66.036  24.477   4.199  1.00 59.06           C  
ANISOU 2785  CG2 ILE A 445     4697   9114   8631    -83      3   -701       C  
ATOM   2786  CD1 ILE A 445     -68.321  22.473   3.116  1.00 68.74           C  
ANISOU 2786  CD1 ILE A 445     5770  10501   9845   -309    -32   -529       C  
ATOM   2787  N   ASN A 446     -67.217  26.374   7.161  1.00 59.01           N  
ANISOU 2787  N   ASN A 446     4390   9378   8655    215    155  -1014       N  
ATOM   2788  CA  ASN A 446     -66.770  27.698   7.605  1.00 59.66           C  
ANISOU 2788  CA  ASN A 446     4454   9385   8827    370    122  -1163       C  
ATOM   2789  C   ASN A 446     -65.957  27.597   8.921  1.00 65.19           C  
ANISOU 2789  C   ASN A 446     5195  10163   9410    414    200  -1267       C  
ATOM   2790  O   ASN A 446     -64.805  28.035   8.962  1.00 63.21           O  
ANISOU 2790  O   ASN A 446     5052   9776   9190    449    160  -1315       O  
ATOM   2791  CB  ASN A 446     -67.965  28.642   7.779  1.00 57.12           C  
ANISOU 2791  CB  ASN A 446     3951   9135   8618    495    103  -1263       C  
ATOM   2792  CG  ASN A 446     -67.595  30.082   8.047  1.00 69.84           C  
ANISOU 2792  CG  ASN A 446     5532  10628  10375    661     34  -1423       C  
ATOM   2793  OD1 ASN A 446     -66.849  30.716   7.299  1.00 60.54           O  
ANISOU 2793  OD1 ASN A 446     4435   9239   9327    672    -67  -1393       O  
ATOM   2794  ND2 ASN A 446     -68.146  30.644   9.100  1.00 63.07           N  
ANISOU 2794  ND2 ASN A 446     4543   9910   9510    795     79  -1597       N  
ATOM   2795  N   GLU A 447     -66.543  26.947   9.952  1.00 63.53           N  
ANISOU 2795  N   GLU A 447     4895  10184   9060    401    308  -1281       N  
ATOM   2796  CA  GLU A 447     -65.961  26.766  11.276  1.00 63.90           C  
ANISOU 2796  CA  GLU A 447     4951  10365   8965    443    391  -1366       C  
ATOM   2797  C   GLU A 447     -64.627  26.005  11.241  1.00 66.82           C  
ANISOU 2797  C   GLU A 447     5504  10632   9251    340    396  -1282       C  
ATOM   2798  O   GLU A 447     -63.663  26.464  11.863  1.00 65.71           O  
ANISOU 2798  O   GLU A 447     5427  10458   9084    411    396  -1386       O  
ATOM   2799  CB  GLU A 447     -66.950  26.065  12.226  1.00 66.68           C  
ANISOU 2799  CB  GLU A 447     5152  11012   9171    424    507  -1341       C  
ATOM   2800  CG  GLU A 447     -66.599  26.209  13.702  1.00 83.46           C  
ANISOU 2800  CG  GLU A 447     7231  13335  11144    515    592  -1464       C  
ATOM   2801  CD  GLU A 447     -66.180  27.600  14.151  1.00117.68           C  
ANISOU 2801  CD  GLU A 447    11543  17618  15551    708    543  -1707       C  
ATOM   2802  OE1 GLU A 447     -65.002  27.760  14.551  1.00113.00           O  
ANISOU 2802  OE1 GLU A 447    11065  16947  14923    732    528  -1773       O  
ATOM   2803  OE2 GLU A 447     -67.007  28.537  14.052  1.00118.93           O  
ANISOU 2803  OE2 GLU A 447    11571  17795  15822    833    506  -1834       O  
ATOM   2804  N   THR A 448     -64.576  24.857  10.533  1.00 62.78           N  
ANISOU 2804  N   THR A 448     5072  10073   8708    183    393  -1107       N  
ATOM   2805  CA  THR A 448     -63.367  24.026  10.429  1.00 61.12           C  
ANISOU 2805  CA  THR A 448     5030   9767   8428     85    393  -1023       C  
ATOM   2806  C   THR A 448     -62.257  24.793   9.698  1.00 65.08           C  
ANISOU 2806  C   THR A 448     5659  10046   9025    128    304  -1065       C  
ATOM   2807  O   THR A 448     -61.101  24.684  10.084  1.00 64.40           O  
ANISOU 2807  O   THR A 448     5680   9906   8883    127    312  -1084       O  
ATOM   2808  CB  THR A 448     -63.690  22.690   9.728  1.00 63.66           C  
ANISOU 2808  CB  THR A 448     5387  10075   8725    -78    388   -851       C  
ATOM   2809  OG1 THR A 448     -64.758  22.050  10.413  1.00 59.94           O  
ANISOU 2809  OG1 THR A 448     4777   9808   8191   -122    461   -795       O  
ATOM   2810  CG2 THR A 448     -62.499  21.748   9.662  1.00 61.79           C  
ANISOU 2810  CG2 THR A 448     5309   9749   8419   -172    386   -774       C  
ATOM   2811  N   MET A 449     -62.612  25.557   8.646  1.00 62.41           N  
ANISOU 2811  N   MET A 449     5297   9587   8830    162    218  -1064       N  
ATOM   2812  CA  MET A 449     -61.662  26.328   7.847  1.00 61.58           C  
ANISOU 2812  CA  MET A 449     5285   9283   8831    195    127  -1066       C  
ATOM   2813  C   MET A 449     -61.137  27.514   8.623  1.00 66.88           C  
ANISOU 2813  C   MET A 449     5933   9907   9571    330    106  -1220       C  
ATOM   2814  O   MET A 449     -59.972  27.877   8.446  1.00 66.99           O  
ANISOU 2814  O   MET A 449     6047   9782   9624    338     58  -1222       O  
ATOM   2815  CB  MET A 449     -62.275  26.781   6.512  1.00 64.07           C  
ANISOU 2815  CB  MET A 449     5560   9509   9275    188     38   -994       C  
ATOM   2816  CG  MET A 449     -62.540  25.627   5.540  1.00 67.44           C  
ANISOU 2816  CG  MET A 449     6033   9950   9642     55     29   -854       C  
ATOM   2817  SD  MET A 449     -61.194  24.411   5.455  1.00 70.70           S  
ANISOU 2817  SD  MET A 449     6624  10315   9924    -54     51   -781       S  
ATOM   2818  CE  MET A 449     -59.988  25.363   4.552  1.00 66.25           C  
ANISOU 2818  CE  MET A 449     6147   9580   9444     -7    -39   -760       C  
ATOM   2819  N   LEU A 450     -61.970  28.097   9.498  1.00 64.39           N  
ANISOU 2819  N   LEU A 450     5480   9712   9272    438    137  -1356       N  
ATOM   2820  CA  LEU A 450     -61.556  29.218  10.325  1.00 65.28           C  
ANISOU 2820  CA  LEU A 450     5556   9791   9458    583    107  -1541       C  
ATOM   2821  C   LEU A 450     -60.507  28.771  11.334  1.00 69.60           C  
ANISOU 2821  C   LEU A 450     6190  10393   9863    576    164  -1594       C  
ATOM   2822  O   LEU A 450     -59.448  29.402  11.398  1.00 69.98           O  
ANISOU 2822  O   LEU A 450     6310  10295   9985    619    100  -1654       O  
ATOM   2823  CB  LEU A 450     -62.748  29.896  11.038  1.00 67.09           C  
ANISOU 2823  CB  LEU A 450     5604  10168   9721    714    128  -1696       C  
ATOM   2824  CG  LEU A 450     -62.406  30.988  12.083  1.00 72.78           C  
ANISOU 2824  CG  LEU A 450     6263  10892  10496    885     99  -1937       C  
ATOM   2825  CD1 LEU A 450     -61.713  32.199  11.444  1.00 72.57           C  
ANISOU 2825  CD1 LEU A 450     6272  10586  10714    952    -48  -1984       C  
ATOM   2826  CD2 LEU A 450     -63.645  31.424  12.844  1.00 76.10           C  
ANISOU 2826  CD2 LEU A 450     6494  11520  10899   1013    142  -2092       C  
ATOM   2827  N   ARG A 451     -60.764  27.687  12.099  1.00 65.54           N  
ANISOU 2827  N   ARG A 451     5663  10085   9154    517    275  -1555       N  
ATOM   2828  CA  ARG A 451     -59.757  27.321  13.085  1.00 65.16           C  
ANISOU 2828  CA  ARG A 451     5688  10100   8969    518    324  -1600       C  
ATOM   2829  C   ARG A 451     -58.540  26.619  12.470  1.00 67.88           C  
ANISOU 2829  C   ARG A 451     6207  10295   9288    399    303  -1462       C  
ATOM   2830  O   ARG A 451     -57.449  26.768  13.017  1.00 68.27           O  
ANISOU 2830  O   ARG A 451     6333  10310   9297    423    299  -1518       O  
ATOM   2831  CB  ARG A 451     -60.306  26.570  14.295  1.00 64.40           C  
ANISOU 2831  CB  ARG A 451     5502  10291   8675    514    444  -1610       C  
ATOM   2832  CG  ARG A 451     -61.086  25.303  14.080  1.00 69.82           C  
ANISOU 2832  CG  ARG A 451     6162  11095   9271    376    513  -1422       C  
ATOM   2833  CD  ARG A 451     -61.072  24.500  15.377  1.00 78.34           C  
ANISOU 2833  CD  ARG A 451     7191  12431  10143    354    623  -1394       C  
ATOM   2834  NE  ARG A 451     -60.926  25.357  16.559  1.00 88.61           N  
ANISOU 2834  NE  ARG A 451     8406  13890  11370    513    651  -1599       N  
ATOM   2835  CZ  ARG A 451     -60.607  24.927  17.774  1.00 99.69           C  
ANISOU 2835  CZ  ARG A 451     9782  15512  12585    527    730  -1614       C  
ATOM   2836  NH1 ARG A 451     -60.402  23.637  17.994  1.00 91.65           N  
ANISOU 2836  NH1 ARG A 451     8813  14565  11446    386    789  -1415       N  
ATOM   2837  NH2 ARG A 451     -60.492  25.785  18.780  1.00 72.87           N  
ANISOU 2837  NH2 ARG A 451     6302  12265   9121    688    742  -1829       N  
ATOM   2838  N   LEU A 452     -58.680  25.975  11.305  1.00 62.96           N  
ANISOU 2838  N   LEU A 452     5642   9581   8700    286    278  -1301       N  
ATOM   2839  CA  LEU A 452     -57.532  25.365  10.633  1.00 61.84           C  
ANISOU 2839  CA  LEU A 452     5654   9302   8539    192    249  -1189       C  
ATOM   2840  C   LEU A 452     -56.526  26.460  10.187  1.00 64.23           C  
ANISOU 2840  C   LEU A 452     6016   9416   8972    255    158  -1239       C  
ATOM   2841  O   LEU A 452     -55.324  26.285  10.356  1.00 62.22           O  
ANISOU 2841  O   LEU A 452     5866   9097   8678    234    151  -1227       O  
ATOM   2842  CB  LEU A 452     -57.987  24.519   9.447  1.00 61.79           C  
ANISOU 2842  CB  LEU A 452     5677   9258   8542     78    231  -1037       C  
ATOM   2843  CG  LEU A 452     -56.958  23.564   8.864  1.00 66.52           C  
ANISOU 2843  CG  LEU A 452     6421   9770   9086    -22    217   -929       C  
ATOM   2844  CD1 LEU A 452     -56.887  22.278   9.677  1.00 67.35           C  
ANISOU 2844  CD1 LEU A 452     6555   9983   9053   -101    293   -877       C  
ATOM   2845  CD2 LEU A 452     -57.308  23.232   7.431  1.00 70.49           C  
ANISOU 2845  CD2 LEU A 452     6942  10200   9642    -89    157   -829       C  
ATOM   2846  N   GLY A 453     -57.047  27.595   9.715  1.00 61.76           N  
ANISOU 2846  N   GLY A 453     5621   9023   8821    334     85  -1293       N  
ATOM   2847  CA  GLY A 453     -56.264  28.755   9.310  1.00 61.19           C  
ANISOU 2847  CA  GLY A 453     5571   8766   8913    395    -17  -1327       C  
ATOM   2848  C   GLY A 453     -55.584  29.457  10.468  1.00 65.23           C  
ANISOU 2848  C   GLY A 453     6075   9268   9441    494    -27  -1497       C  
ATOM   2849  O   GLY A 453     -54.423  29.857  10.350  1.00 65.13           O  
ANISOU 2849  O   GLY A 453     6138   9122   9488    493    -83  -1490       O  
ATOM   2850  N   ILE A 454     -56.282  29.591  11.607  1.00 61.84           N  
ANISOU 2850  N   ILE A 454     5549   8998   8951    581     27  -1652       N  
ATOM   2851  CA  ILE A 454     -55.701  30.226  12.790  1.00 61.99           C  
ANISOU 2851  CA  ILE A 454     5548   9044   8962    689     16  -1844       C  
ATOM   2852  C   ILE A 454     -54.546  29.343  13.291  1.00 64.65           C  
ANISOU 2852  C   ILE A 454     6008   9422   9134    617     71  -1793       C  
ATOM   2853  O   ILE A 454     -53.471  29.867  13.582  1.00 63.10           O  
ANISOU 2853  O   ILE A 454     5864   9119   8993    653     13  -1864       O  
ATOM   2854  CB  ILE A 454     -56.769  30.521  13.877  1.00 66.46           C  
ANISOU 2854  CB  ILE A 454     5966   9821   9464    807     70  -2025       C  
ATOM   2855  CG1 ILE A 454     -57.760  31.606  13.377  1.00 67.62           C  
ANISOU 2855  CG1 ILE A 454     5989   9884   9820    906    -13  -2108       C  
ATOM   2856  CG2 ILE A 454     -56.117  30.945  15.219  1.00 67.82           C  
ANISOU 2856  CG2 ILE A 454     6123  10086   9561    915     77  -2231       C  
ATOM   2857  CD1 ILE A 454     -59.098  31.707  14.147  1.00 72.94           C  
ANISOU 2857  CD1 ILE A 454     6499  10792  10421    998     56  -2230       C  
ATOM   2858  N   PHE A 455     -54.743  28.003  13.292  1.00 60.18           N  
ANISOU 2858  N   PHE A 455     5487   8988   8391    507    168  -1657       N  
ATOM   2859  CA  PHE A 455     -53.732  27.038  13.722  1.00 57.72           C  
ANISOU 2859  CA  PHE A 455     5287   8717   7928    432    220  -1586       C  
ATOM   2860  C   PHE A 455     -52.534  27.017  12.750  1.00 60.98           C  
ANISOU 2860  C   PHE A 455     5828   8923   8417    364    153  -1478       C  
ATOM   2861  O   PHE A 455     -51.390  27.050  13.215  1.00 60.70           O  
ANISOU 2861  O   PHE A 455     5866   8850   8348    371    142  -1508       O  
ATOM   2862  CB  PHE A 455     -54.359  25.651  13.907  1.00 58.70           C  
ANISOU 2862  CB  PHE A 455     5407   9010   7887    331    321  -1457       C  
ATOM   2863  CG  PHE A 455     -55.005  25.481  15.266  1.00 61.42           C  
ANISOU 2863  CG  PHE A 455     5643   9611   8084    388    408  -1545       C  
ATOM   2864  CD1 PHE A 455     -54.440  24.650  16.221  1.00 64.18           C  
ANISOU 2864  CD1 PHE A 455     6029  10099   8258    351    477  -1506       C  
ATOM   2865  CD2 PHE A 455     -56.155  26.193  15.609  1.00 65.11           C  
ANISOU 2865  CD2 PHE A 455     5960  10196   8583    488    419  -1666       C  
ATOM   2866  CE1 PHE A 455     -55.018  24.527  17.489  1.00 66.84           C  
ANISOU 2866  CE1 PHE A 455     6250  10708   8440    407    558  -1573       C  
ATOM   2867  CE2 PHE A 455     -56.744  26.048  16.866  1.00 68.79           C  
ANISOU 2867  CE2 PHE A 455     6309  10938   8891    549    504  -1747       C  
ATOM   2868  CZ  PHE A 455     -56.170  25.220  17.799  1.00 66.84           C  
ANISOU 2868  CZ  PHE A 455     6095  10845   8456    507    575  -1694       C  
ATOM   2869  N   GLY A 456     -52.803  27.051  11.439  1.00 56.47           N  
ANISOU 2869  N   GLY A 456     5272   8237   7948    311    106  -1361       N  
ATOM   2870  CA  GLY A 456     -51.779  27.089  10.396  1.00 55.03           C  
ANISOU 2870  CA  GLY A 456     5186   7893   7831    256     44  -1247       C  
ATOM   2871  C   GLY A 456     -50.938  28.351  10.402  1.00 60.62           C  
ANISOU 2871  C   GLY A 456     5890   8449   8696    326    -50  -1316       C  
ATOM   2872  O   GLY A 456     -49.723  28.271  10.202  1.00 60.62           O  
ANISOU 2872  O   GLY A 456     5974   8367   8691    292    -75  -1261       O  
ATOM   2873  N   PHE A 457     -51.569  29.531  10.652  1.00 58.17           N  
ANISOU 2873  N   PHE A 457     5471   8092   8537    427   -111  -1439       N  
ATOM   2874  CA  PHE A 457     -50.860  30.817  10.744  1.00 58.07           C  
ANISOU 2874  CA  PHE A 457     5435   7912   8717    501   -223  -1520       C  
ATOM   2875  C   PHE A 457     -50.083  30.916  12.059  1.00 62.93           C  
ANISOU 2875  C   PHE A 457     6071   8572   9266    560   -210  -1682       C  
ATOM   2876  O   PHE A 457     -48.974  31.449  12.071  1.00 62.75           O  
ANISOU 2876  O   PHE A 457     6087   8416   9340    567   -285  -1692       O  
ATOM   2877  CB  PHE A 457     -51.807  32.014  10.567  1.00 60.88           C  
ANISOU 2877  CB  PHE A 457     5663   8187   9281    595   -308  -1606       C  
ATOM   2878  CG  PHE A 457     -51.998  32.365   9.109  1.00 61.80           C  
ANISOU 2878  CG  PHE A 457     5766   8175   9542    543   -380  -1424       C  
ATOM   2879  CD1 PHE A 457     -50.978  32.978   8.384  1.00 64.76           C  
ANISOU 2879  CD1 PHE A 457     6168   8372  10065    514   -479  -1313       C  
ATOM   2880  CD2 PHE A 457     -53.165  32.019   8.441  1.00 62.96           C  
ANISOU 2880  CD2 PHE A 457     5864   8396   9663    517   -349  -1347       C  
ATOM   2881  CE1 PHE A 457     -51.143  33.279   7.028  1.00 65.32           C  
ANISOU 2881  CE1 PHE A 457     6213   8359  10248    465   -543  -1123       C  
ATOM   2882  CE2 PHE A 457     -53.326  32.309   7.083  1.00 65.80           C  
ANISOU 2882  CE2 PHE A 457     6205   8662  10133    470   -418  -1174       C  
ATOM   2883  CZ  PHE A 457     -52.313  32.939   6.387  1.00 64.18           C  
ANISOU 2883  CZ  PHE A 457     6024   8298  10064    447   -512  -1059       C  
ATOM   2884  N   LEU A 458     -50.628  30.347  13.141  1.00 60.74           N  
ANISOU 2884  N   LEU A 458     5765   8498   8817    595   -116  -1792       N  
ATOM   2885  CA  LEU A 458     -49.965  30.295  14.442  1.00 62.23           C  
ANISOU 2885  CA  LEU A 458     5967   8782   8897    651    -92  -1940       C  
ATOM   2886  C   LEU A 458     -48.724  29.408  14.369  1.00 65.14           C  
ANISOU 2886  C   LEU A 458     6467   9139   9146    554    -57  -1813       C  
ATOM   2887  O   LEU A 458     -47.655  29.817  14.835  1.00 65.11           O  
ANISOU 2887  O   LEU A 458     6498   9068   9171    583   -108  -1885       O  
ATOM   2888  CB  LEU A 458     -50.934  29.771  15.513  1.00 64.04           C  
ANISOU 2888  CB  LEU A 458     6117   9274   8942    702     12  -2043       C  
ATOM   2889  CG  LEU A 458     -50.593  30.047  16.981  1.00 71.11           C  
ANISOU 2889  CG  LEU A 458     6971  10317   9729    807     26  -2251       C  
ATOM   2890  CD1 LEU A 458     -50.406  31.548  17.249  1.00 73.31           C  
ANISOU 2890  CD1 LEU A 458     7176  10465  10216    948   -104  -2479       C  
ATOM   2891  CD2 LEU A 458     -51.685  29.506  17.884  1.00 73.49           C  
ANISOU 2891  CD2 LEU A 458     7178  10917   9829    843    142  -2303       C  
ATOM   2892  N   ALA A 459     -48.865  28.204  13.750  1.00 59.44           N  
ANISOU 2892  N   ALA A 459     5812   8470   8303    440     18  -1631       N  
ATOM   2893  CA  ALA A 459     -47.786  27.234  13.585  1.00 56.44           C  
ANISOU 2893  CA  ALA A 459     5552   8079   7813    350     51  -1506       C  
ATOM   2894  C   ALA A 459     -46.670  27.815  12.713  1.00 59.44           C  
ANISOU 2894  C   ALA A 459     5989   8263   8333    327    -40  -1437       C  
ATOM   2895  O   ALA A 459     -45.501  27.643  13.063  1.00 58.68           O  
ANISOU 2895  O   ALA A 459     5960   8141   8194    313    -47  -1432       O  
ATOM   2896  CB  ALA A 459     -48.314  25.934  13.000  1.00 55.88           C  
ANISOU 2896  CB  ALA A 459     5521   8081   7628    247    125  -1349       C  
ATOM   2897  N   PHE A 460     -47.025  28.566  11.634  1.00 55.54           N  
ANISOU 2897  N   PHE A 460     5453   7641   8011    328   -112  -1377       N  
ATOM   2898  CA  PHE A 460     -46.053  29.240  10.755  1.00 54.20           C  
ANISOU 2898  CA  PHE A 460     5306   7298   7990    307   -205  -1284       C  
ATOM   2899  C   PHE A 460     -45.188  30.209  11.548  1.00 58.51           C  
ANISOU 2899  C   PHE A 460     5832   7749   8651    374   -284  -1413       C  
ATOM   2900  O   PHE A 460     -43.974  30.234  11.347  1.00 58.26           O  
ANISOU 2900  O   PHE A 460     5855   7640   8642    338   -320  -1344       O  
ATOM   2901  CB  PHE A 460     -46.750  29.984   9.601  1.00 55.73           C  
ANISOU 2901  CB  PHE A 460     5429   7394   8351    306   -274  -1198       C  
ATOM   2902  CG  PHE A 460     -45.805  30.776   8.725  1.00 56.02           C  
ANISOU 2902  CG  PHE A 460     5463   7270   8552    283   -375  -1077       C  
ATOM   2903  CD1 PHE A 460     -45.556  32.123   8.981  1.00 59.50           C  
ANISOU 2903  CD1 PHE A 460     5829   7556   9222    347   -492  -1149       C  
ATOM   2904  CD2 PHE A 460     -45.149  30.172   7.659  1.00 55.81           C  
ANISOU 2904  CD2 PHE A 460     5496   7253   8456    200   -360   -890       C  
ATOM   2905  CE1 PHE A 460     -44.657  32.848   8.193  1.00 60.03           C  
ANISOU 2905  CE1 PHE A 460     5880   7475   9455    313   -591  -1007       C  
ATOM   2906  CE2 PHE A 460     -44.269  30.900   6.859  1.00 58.51           C  
ANISOU 2906  CE2 PHE A 460     5816   7478   8935    176   -448   -756       C  
ATOM   2907  CZ  PHE A 460     -44.014  32.228   7.143  1.00 58.04           C  
ANISOU 2907  CZ  PHE A 460     5681   7261   9112    225   -562   -801       C  
ATOM   2908  N   GLY A 461     -45.825  30.998  12.416  1.00 56.35           N  
ANISOU 2908  N   GLY A 461     5473   7488   8451    476   -317  -1605       N  
ATOM   2909  CA  GLY A 461     -45.168  31.968  13.288  1.00 57.05           C  
ANISOU 2909  CA  GLY A 461     5526   7492   8659    559   -407  -1777       C  
ATOM   2910  C   GLY A 461     -44.165  31.328  14.228  1.00 60.67           C  
ANISOU 2910  C   GLY A 461     6059   8044   8948    549   -359  -1829       C  
ATOM   2911  O   GLY A 461     -43.065  31.852  14.396  1.00 60.48           O  
ANISOU 2911  O   GLY A 461     6054   7905   9021    553   -439  -1852       O  
ATOM   2912  N   PHE A 462     -44.516  30.160  14.805  1.00 57.68           N  
ANISOU 2912  N   PHE A 462     5719   7871   8324    525   -233  -1824       N  
ATOM   2913  CA  PHE A 462     -43.645  29.406  15.713  1.00 57.69           C  
ANISOU 2913  CA  PHE A 462     5789   7986   8143    510   -177  -1847       C  
ATOM   2914  C   PHE A 462     -42.486  28.730  14.972  1.00 60.41           C  
ANISOU 2914  C   PHE A 462     6241   8254   8459    408   -170  -1660       C  
ATOM   2915  O   PHE A 462     -41.352  28.802  15.454  1.00 61.19           O  
ANISOU 2915  O   PHE A 462     6381   8327   8543    411   -200  -1690       O  
ATOM   2916  CB  PHE A 462     -44.437  28.367  16.520  1.00 59.90           C  
ANISOU 2916  CB  PHE A 462     6061   8509   8188    508    -52  -1863       C  
ATOM   2917  CG  PHE A 462     -45.285  28.912  17.654  1.00 63.30           C  
ANISOU 2917  CG  PHE A 462     6381   9095   8574    627    -41  -2078       C  
ATOM   2918  CD1 PHE A 462     -44.709  29.632  18.694  1.00 67.29           C  
ANISOU 2918  CD1 PHE A 462     6852   9628   9086    726   -100  -2281       C  
ATOM   2919  CD2 PHE A 462     -46.644  28.634  17.721  1.00 66.43           C  
ANISOU 2919  CD2 PHE A 462     6703   9635   8903    642     30  -2082       C  
ATOM   2920  CE1 PHE A 462     -45.488  30.113  19.750  1.00 70.34           C  
ANISOU 2920  CE1 PHE A 462     7127  10190   9409    851    -90  -2501       C  
ATOM   2921  CE2 PHE A 462     -47.423  29.118  18.777  1.00 71.16           C  
ANISOU 2921  CE2 PHE A 462     7185  10410   9440    762     47  -2284       C  
ATOM   2922  CZ  PHE A 462     -46.839  29.850  19.787  1.00 70.21           C  
ANISOU 2922  CZ  PHE A 462     7031  10328   9319    871    -11  -2499       C  
ATOM   2923  N   VAL A 463     -42.750  28.099  13.811  1.00 55.20           N  
ANISOU 2923  N   VAL A 463     5619   7565   7789    325   -137  -1480       N  
ATOM   2924  CA  VAL A 463     -41.719  27.455  12.988  1.00 54.31           C  
ANISOU 2924  CA  VAL A 463     5595   7396   7645    242   -131  -1312       C  
ATOM   2925  C   VAL A 463     -40.698  28.542  12.532  1.00 59.02           C  
ANISOU 2925  C   VAL A 463     6173   7820   8431    251   -244  -1289       C  
ATOM   2926  O   VAL A 463     -39.488  28.294  12.574  1.00 58.20           O  
ANISOU 2926  O   VAL A 463     6125   7692   8298    221   -254  -1238       O  
ATOM   2927  CB  VAL A 463     -42.318  26.649  11.790  1.00 57.70           C  
ANISOU 2927  CB  VAL A 463     6052   7845   8027    169    -85  -1154       C  
ATOM   2928  CG1 VAL A 463     -41.227  26.072  10.893  1.00 56.45           C  
ANISOU 2928  CG1 VAL A 463     5967   7640   7840    105    -91  -1005       C  
ATOM   2929  CG2 VAL A 463     -43.218  25.522  12.280  1.00 57.57           C  
ANISOU 2929  CG2 VAL A 463     6051   7981   7843    145     13  -1159       C  
ATOM   2930  N   LEU A 464     -41.190  29.755  12.167  1.00 55.80           N  
ANISOU 2930  N   LEU A 464     5678   7294   8231    293   -334  -1326       N  
ATOM   2931  CA  LEU A 464     -40.350  30.887  11.756  1.00 55.12           C  
ANISOU 2931  CA  LEU A 464     5550   7028   8365    297   -458  -1290       C  
ATOM   2932  C   LEU A 464     -39.418  31.328  12.897  1.00 57.75           C  
ANISOU 2932  C   LEU A 464     5886   7328   8730    344   -512  -1440       C  
ATOM   2933  O   LEU A 464     -38.264  31.671  12.622  1.00 57.35           O  
ANISOU 2933  O   LEU A 464     5845   7176   8768    309   -577  -1361       O  
ATOM   2934  CB  LEU A 464     -41.217  32.070  11.269  1.00 56.27           C  
ANISOU 2934  CB  LEU A 464     5590   7047   8742    340   -553  -1310       C  
ATOM   2935  CG  LEU A 464     -40.494  33.373  10.865  1.00 61.65           C  
ANISOU 2935  CG  LEU A 464     6204   7517   9703    341   -705  -1258       C  
ATOM   2936  CD1 LEU A 464     -39.451  33.135   9.745  1.00 60.72           C  
ANISOU 2936  CD1 LEU A 464     6118   7368   9586    243   -710  -1005       C  
ATOM   2937  CD2 LEU A 464     -41.485  34.443  10.480  1.00 64.50           C  
ANISOU 2937  CD2 LEU A 464     6458   7757  10294    392   -799  -1288       C  
ATOM   2938  N   ILE A 465     -39.909  31.318  14.166  1.00 54.15           N  
ANISOU 2938  N   ILE A 465     5411   6975   8191    424   -487  -1652       N  
ATOM   2939  CA  ILE A 465     -39.114  31.682  15.356  1.00 54.01           C  
ANISOU 2939  CA  ILE A 465     5390   6963   8170    482   -537  -1824       C  
ATOM   2940  C   ILE A 465     -38.013  30.614  15.536  1.00 56.51           C  
ANISOU 2940  C   ILE A 465     5806   7367   8298    416   -465  -1724       C  
ATOM   2941  O   ILE A 465     -36.841  30.953  15.706  1.00 56.09           O  
ANISOU 2941  O   ILE A 465     5766   7232   8315    406   -534  -1726       O  
ATOM   2942  CB  ILE A 465     -40.008  31.876  16.625  1.00 57.77           C  
ANISOU 2942  CB  ILE A 465     5806   7576   8568    595   -518  -2076       C  
ATOM   2943  CG1 ILE A 465     -40.938  33.098  16.462  1.00 58.75           C  
ANISOU 2943  CG1 ILE A 465     5820   7583   8921    678   -616  -2201       C  
ATOM   2944  CG2 ILE A 465     -39.148  32.032  17.896  1.00 58.59           C  
ANISOU 2944  CG2 ILE A 465     5913   7738   8611    655   -557  -2255       C  
ATOM   2945  CD1 ILE A 465     -42.126  33.147  17.416  1.00 63.74           C  
ANISOU 2945  CD1 ILE A 465     6379   8390   9449    787   -568  -2413       C  
ATOM   2946  N   THR A 466     -38.406  29.334  15.415  1.00 52.78           N  
ANISOU 2946  N   THR A 466     5398   7043   7611    367   -337  -1626       N  
ATOM   2947  CA  THR A 466     -37.576  28.121  15.450  1.00 51.47           C  
ANISOU 2947  CA  THR A 466     5328   6962   7267    303   -262  -1512       C  
ATOM   2948  C   THR A 466     -36.436  28.281  14.391  1.00 53.86           C  
ANISOU 2948  C   THR A 466     5661   7129   7677    240   -315  -1351       C  
ATOM   2949  O   THR A 466     -35.255  28.179  14.748  1.00 54.07           O  
ANISOU 2949  O   THR A 466     5721   7143   7679    230   -337  -1344       O  
ATOM   2950  CB  THR A 466     -38.542  26.903  15.266  1.00 59.32           C  
ANISOU 2950  CB  THR A 466     6360   8094   8084    262   -143  -1430       C  
ATOM   2951  OG1 THR A 466     -39.096  26.541  16.539  1.00 60.69           O  
ANISOU 2951  OG1 THR A 466     6509   8436   8115    312    -86  -1557       O  
ATOM   2952  CG2 THR A 466     -37.926  25.701  14.616  1.00 55.60           C  
ANISOU 2952  CG2 THR A 466     5981   7647   7497    183    -85  -1266       C  
ATOM   2953  N   PHE A 467     -36.790  28.647  13.141  1.00 49.02           N  
ANISOU 2953  N   PHE A 467     5017   6425   7184    206   -343  -1226       N  
ATOM   2954  CA  PHE A 467     -35.845  28.849  12.032  1.00 47.64           C  
ANISOU 2954  CA  PHE A 467     4845   6157   7100    149   -389  -1051       C  
ATOM   2955  C   PHE A 467     -34.845  29.940  12.339  1.00 53.25           C  
ANISOU 2955  C   PHE A 467     5504   6734   7993    164   -506  -1087       C  
ATOM   2956  O   PHE A 467     -33.638  29.738  12.125  1.00 52.05           O  
ANISOU 2956  O   PHE A 467     5378   6569   7828    125   -518   -993       O  
ATOM   2957  CB  PHE A 467     -36.576  29.180  10.723  1.00 48.87           C  
ANISOU 2957  CB  PHE A 467     4953   6265   7350    120   -405   -920       C  
ATOM   2958  CG  PHE A 467     -35.647  29.473   9.569  1.00 49.50           C  
ANISOU 2958  CG  PHE A 467     5010   6282   7517     67   -454   -727       C  
ATOM   2959  CD1 PHE A 467     -35.041  28.437   8.860  1.00 50.54           C  
ANISOU 2959  CD1 PHE A 467     5202   6509   7493     20   -386   -595       C  
ATOM   2960  CD2 PHE A 467     -35.371  30.781   9.193  1.00 52.14           C  
ANISOU 2960  CD2 PHE A 467     5250   6467   8093     66   -574   -672       C  
ATOM   2961  CE1 PHE A 467     -34.170  28.707   7.802  1.00 51.25           C  
ANISOU 2961  CE1 PHE A 467     5253   6580   7639    -21   -424   -414       C  
ATOM   2962  CE2 PHE A 467     -34.484  31.051   8.143  1.00 55.30           C  
ANISOU 2962  CE2 PHE A 467     5612   6835   8566     10   -616   -465       C  
ATOM   2963  CZ  PHE A 467     -33.896  30.010   7.450  1.00 52.02           C  
ANISOU 2963  CZ  PHE A 467     5251   6550   7964    -31   -534   -337       C  
ATOM   2964  N   SER A 468     -35.347  31.105  12.820  1.00 50.91           N  
ANISOU 2964  N   SER A 468     5128   6335   7879    224   -600  -1227       N  
ATOM   2965  CA  SER A 468     -34.518  32.256  13.193  1.00 51.46           C  
ANISOU 2965  CA  SER A 468     5135   6249   8168    245   -739  -1293       C  
ATOM   2966  C   SER A 468     -33.463  31.887  14.255  1.00 55.01           C  
ANISOU 2966  C   SER A 468     5633   6756   8511    259   -736  -1393       C  
ATOM   2967  O   SER A 468     -32.344  32.398  14.205  1.00 55.37           O  
ANISOU 2967  O   SER A 468     5654   6697   8686    232   -824  -1347       O  
ATOM   2968  CB  SER A 468     -35.393  33.398  13.699  1.00 54.79           C  
ANISOU 2968  CB  SER A 468     5468   6569   8780    329   -837  -1481       C  
ATOM   2969  OG  SER A 468     -36.303  33.796  12.688  1.00 61.67           O  
ANISOU 2969  OG  SER A 468     6287   7373   9771    315   -855  -1373       O  
ATOM   2970  N   CYS A 469     -33.815  30.988  15.189  1.00 51.28           N  
ANISOU 2970  N   CYS A 469     5220   6456   7807    296   -636  -1512       N  
ATOM   2971  CA  CYS A 469     -32.940  30.535  16.269  1.00 51.57           C  
ANISOU 2971  CA  CYS A 469     5301   6581   7711    315   -623  -1606       C  
ATOM   2972  C   CYS A 469     -31.893  29.557  15.751  1.00 55.57           C  
ANISOU 2972  C   CYS A 469     5884   7130   8101    239   -562  -1419       C  
ATOM   2973  O   CYS A 469     -30.755  29.616  16.212  1.00 55.78           O  
ANISOU 2973  O   CYS A 469     5918   7137   8137    233   -609  -1434       O  
ATOM   2974  CB  CYS A 469     -33.758  29.925  17.400  1.00 51.85           C  
ANISOU 2974  CB  CYS A 469     5356   6807   7536    377   -537  -1764       C  
ATOM   2975  SG  CYS A 469     -34.762  31.126  18.301  1.00 57.37           S  
ANISOU 2975  SG  CYS A 469     5951   7495   8352    499   -619  -2044       S  
ATOM   2976  N   HIS A 470     -32.270  28.653  14.807  1.00 50.38           N  
ANISOU 2976  N   HIS A 470     5276   6533   7335    186   -466  -1257       N  
ATOM   2977  CA  HIS A 470     -31.312  27.720  14.207  1.00 48.51           C  
ANISOU 2977  CA  HIS A 470     5101   6337   6993    127   -413  -1092       C  
ATOM   2978  C   HIS A 470     -30.381  28.505  13.269  1.00 55.06           C  
ANISOU 2978  C   HIS A 470     5876   7042   8003     86   -498   -955       C  
ATOM   2979  O   HIS A 470     -29.220  28.118  13.085  1.00 54.52           O  
ANISOU 2979  O   HIS A 470     5830   6992   7892     55   -493   -861       O  
ATOM   2980  CB  HIS A 470     -32.016  26.566  13.452  1.00 47.25           C  
ANISOU 2980  CB  HIS A 470     4998   6270   6686     94   -305   -984       C  
ATOM   2981  CG  HIS A 470     -32.725  25.570  14.327  1.00 49.58           C  
ANISOU 2981  CG  HIS A 470     5346   6697   6796    112   -217  -1064       C  
ATOM   2982  ND1 HIS A 470     -32.034  24.765  15.220  1.00 50.70           N  
ANISOU 2982  ND1 HIS A 470     5542   6924   6797    117   -182  -1091       N  
ATOM   2983  CD2 HIS A 470     -34.040  25.249  14.379  1.00 50.98           C  
ANISOU 2983  CD2 HIS A 470     5519   6937   6916    120   -162  -1096       C  
ATOM   2984  CE1 HIS A 470     -32.951  24.013  15.812  1.00 49.84           C  
ANISOU 2984  CE1 HIS A 470     5456   6928   6555    125   -109  -1129       C  
ATOM   2985  NE2 HIS A 470     -34.173  24.265  15.333  1.00 50.49           N  
ANISOU 2985  NE2 HIS A 470     5501   7001   6681    125    -92  -1135       N  
ATOM   2986  N   PHE A 471     -30.892  29.626  12.700  1.00 53.76           N  
ANISOU 2986  N   PHE A 471     5627   6754   8045     85   -581   -933       N  
ATOM   2987  CA  PHE A 471     -30.141  30.496  11.795  1.00 54.80           C  
ANISOU 2987  CA  PHE A 471     5682   6765   8375     39   -674   -775       C  
ATOM   2988  C   PHE A 471     -29.071  31.255  12.558  1.00 58.04           C  
ANISOU 2988  C   PHE A 471     6051   7074   8928     46   -784   -847       C  
ATOM   2989  O   PHE A 471     -27.966  31.385  12.042  1.00 57.75           O  
ANISOU 2989  O   PHE A 471     5983   7007   8954     -5   -820   -698       O  
ATOM   2990  CB  PHE A 471     -31.054  31.470  11.008  1.00 58.26           C  
ANISOU 2990  CB  PHE A 471     6034   7093   9009     35   -740   -717       C  
ATOM   2991  CG  PHE A 471     -30.341  32.044   9.807  1.00 61.48           C  
ANISOU 2991  CG  PHE A 471     6363   7433   9563    -31   -803   -478       C  
ATOM   2992  CD1 PHE A 471     -30.339  31.367   8.591  1.00 64.27           C  
ANISOU 2992  CD1 PHE A 471     6729   7904   9789    -74   -724   -283       C  
ATOM   2993  CD2 PHE A 471     -29.589  33.216   9.914  1.00 65.95           C  
ANISOU 2993  CD2 PHE A 471     6835   7834  10390    -51   -947   -443       C  
ATOM   2994  CE1 PHE A 471     -29.622  31.865   7.494  1.00 66.12           C  
ANISOU 2994  CE1 PHE A 471     6875   8119  10128   -132   -774    -46       C  
ATOM   2995  CE2 PHE A 471     -28.866  33.709   8.819  1.00 69.59           C  
ANISOU 2995  CE2 PHE A 471     7208   8253  10981   -122  -1002   -187       C  
ATOM   2996  CZ  PHE A 471     -28.889  33.032   7.616  1.00 66.86           C  
ANISOU 2996  CZ  PHE A 471     6868   8055  10479   -160   -910     16       C  
ATOM   2997  N   TYR A 472     -29.389  31.760  13.771  1.00 54.75           N  
ANISOU 2997  N   TYR A 472     5625   6620   8559    112   -840  -1079       N  
ATOM   2998  CA  TYR A 472     -28.424  32.460  14.633  1.00 54.90           C  
ANISOU 2998  CA  TYR A 472     5604   6549   8706    130   -956  -1193       C  
ATOM   2999  C   TYR A 472     -27.247  31.517  14.929  1.00 56.94           C  
ANISOU 2999  C   TYR A 472     5930   6920   8784    103   -894  -1137       C  
ATOM   3000  O   TYR A 472     -26.091  31.903  14.779  1.00 56.64           O  
ANISOU 3000  O   TYR A 472     5850   6809   8860     63   -970  -1056       O  
ATOM   3001  CB  TYR A 472     -29.109  32.931  15.933  1.00 56.79           C  
ANISOU 3001  CB  TYR A 472     5829   6788   8961    227  -1005  -1485       C  
ATOM   3002  CG  TYR A 472     -28.168  33.543  16.953  1.00 59.97           C  
ANISOU 3002  CG  TYR A 472     6197   7125   9465    260  -1127  -1646       C  
ATOM   3003  CD1 TYR A 472     -27.549  32.756  17.920  1.00 61.40           C  
ANISOU 3003  CD1 TYR A 472     6442   7457   9431    283  -1073  -1736       C  
ATOM   3004  CD2 TYR A 472     -27.937  34.916  16.983  1.00 62.56           C  
ANISOU 3004  CD2 TYR A 472     6421   7235  10115    271  -1309  -1713       C  
ATOM   3005  CE1 TYR A 472     -26.662  33.308  18.840  1.00 63.91           C  
ANISOU 3005  CE1 TYR A 472     6724   7725   9834    315  -1191  -1888       C  
ATOM   3006  CE2 TYR A 472     -27.075  35.484  17.918  1.00 64.67           C  
ANISOU 3006  CE2 TYR A 472     6651   7434  10488    302  -1437  -1878       C  
ATOM   3007  CZ  TYR A 472     -26.437  34.675  18.846  1.00 72.77           C  
ANISOU 3007  CZ  TYR A 472     7744   8629  11278    325  -1375  -1969       C  
ATOM   3008  OH  TYR A 472     -25.581  35.220  19.777  1.00 76.82           O  
ANISOU 3008  OH  TYR A 472     8217   9088  11884    359  -1506  -2138       O  
ATOM   3009  N   ASP A 473     -27.568  30.266  15.302  1.00 52.50           N  
ANISOU 3009  N   ASP A 473     5463   6533   7952    120   -759  -1165       N  
ATOM   3010  CA  ASP A 473     -26.624  29.205  15.640  1.00 51.65           C  
ANISOU 3010  CA  ASP A 473     5427   6542   7655    105   -690  -1120       C  
ATOM   3011  C   ASP A 473     -25.710  28.839  14.457  1.00 53.98           C  
ANISOU 3011  C   ASP A 473     5719   6835   7956     38   -666   -887       C  
ATOM   3012  O   ASP A 473     -24.506  28.684  14.653  1.00 53.56           O  
ANISOU 3012  O   ASP A 473     5666   6794   7892     21   -689   -845       O  
ATOM   3013  CB  ASP A 473     -27.387  27.973  16.156  1.00 52.48           C  
ANISOU 3013  CB  ASP A 473     5621   6814   7506    132   -560  -1174       C  
ATOM   3014  CG  ASP A 473     -27.759  28.070  17.628  1.00 63.82           C  
ANISOU 3014  CG  ASP A 473     7060   8328   8863    202   -572  -1393       C  
ATOM   3015  OD1 ASP A 473     -27.548  29.152  18.231  1.00 64.94           O  
ANISOU 3015  OD1 ASP A 473     7134   8385   9154    243   -686  -1540       O  
ATOM   3016  OD2 ASP A 473     -28.205  27.053  18.192  1.00 71.26           O  
ANISOU 3016  OD2 ASP A 473     8062   9421   9595    218   -475  -1416       O  
ATOM   3017  N   PHE A 474     -26.272  28.763  13.243  1.00 49.95           N  
ANISOU 3017  N   PHE A 474     5194   6322   7462      6   -626   -743       N  
ATOM   3018  CA  PHE A 474     -25.555  28.472  12.001  1.00 50.19           C  
ANISOU 3018  CA  PHE A 474     5203   6386   7482    -46   -600   -525       C  
ATOM   3019  C   PHE A 474     -24.581  29.594  11.660  1.00 55.59           C  
ANISOU 3019  C   PHE A 474     5778   6954   8390    -88   -719   -417       C  
ATOM   3020  O   PHE A 474     -23.453  29.344  11.216  1.00 55.18           O  
ANISOU 3020  O   PHE A 474     5702   6950   8314   -121   -713   -281       O  
ATOM   3021  CB  PHE A 474     -26.567  28.294  10.853  1.00 52.50           C  
ANISOU 3021  CB  PHE A 474     5491   6714   7744    -59   -544   -423       C  
ATOM   3022  CG  PHE A 474     -26.046  28.577   9.459  1.00 55.90           C  
ANISOU 3022  CG  PHE A 474     5844   7157   8239   -108   -560   -197       C  
ATOM   3023  CD1 PHE A 474     -25.142  27.713   8.845  1.00 59.77           C  
ANISOU 3023  CD1 PHE A 474     6351   7772   8588   -120   -498    -78       C  
ATOM   3024  CD2 PHE A 474     -26.466  29.702   8.757  1.00 59.72           C  
ANISOU 3024  CD2 PHE A 474     6227   7542   8922   -135   -640    -99       C  
ATOM   3025  CE1 PHE A 474     -24.675  27.966   7.553  1.00 61.69           C  
ANISOU 3025  CE1 PHE A 474     6507   8071   8863   -156   -506    133       C  
ATOM   3026  CE2 PHE A 474     -26.009  29.947   7.461  1.00 63.57           C  
ANISOU 3026  CE2 PHE A 474     6629   8074   9451   -182   -651    134       C  
ATOM   3027  CZ  PHE A 474     -25.121  29.075   6.865  1.00 61.78           C  
ANISOU 3027  CZ  PHE A 474     6415   8001   9057   -191   -580    248       C  
ATOM   3028  N   PHE A 475     -25.061  30.835  11.818  1.00 52.04           N  
ANISOU 3028  N   PHE A 475     5251   6350   8172    -86   -832   -472       N  
ATOM   3029  CA  PHE A 475     -24.341  32.055  11.536  1.00 52.49           C  
ANISOU 3029  CA  PHE A 475     5188   6255   8499   -132   -973   -373       C  
ATOM   3030  C   PHE A 475     -23.171  32.260  12.500  1.00 56.28           C  
ANISOU 3030  C   PHE A 475     5657   6692   9034   -130  -1049   -461       C  
ATOM   3031  O   PHE A 475     -22.209  32.935  12.138  1.00 56.69           O  
ANISOU 3031  O   PHE A 475     5614   6661   9263   -186  -1143   -324       O  
ATOM   3032  CB  PHE A 475     -25.323  33.237  11.634  1.00 55.27           C  
ANISOU 3032  CB  PHE A 475     5473   6438   9091   -113  -1082   -456       C  
ATOM   3033  CG  PHE A 475     -24.851  34.521  11.004  1.00 58.54           C  
ANISOU 3033  CG  PHE A 475     5746   6673   9823   -173  -1234   -296       C  
ATOM   3034  CD1 PHE A 475     -24.156  35.465  11.749  1.00 63.54           C  
ANISOU 3034  CD1 PHE A 475     6311   7138  10694   -176  -1390   -388       C  
ATOM   3035  CD2 PHE A 475     -25.102  34.790   9.665  1.00 60.45           C  
ANISOU 3035  CD2 PHE A 475     5914   6916  10136   -227  -1230    -46       C  
ATOM   3036  CE1 PHE A 475     -23.720  36.658  11.167  1.00 66.05           C  
ANISOU 3036  CE1 PHE A 475     6487   7269  11340   -242  -1547   -222       C  
ATOM   3037  CE2 PHE A 475     -24.667  35.983   9.083  1.00 65.14           C  
ANISOU 3037  CE2 PHE A 475     6365   7347  11040   -292  -1377    136       C  
ATOM   3038  CZ  PHE A 475     -23.989  36.916   9.839  1.00 64.87           C  
ANISOU 3038  CZ  PHE A 475     6262   7123  11264   -302  -1538     51       C  
ATOM   3039  N   ASN A 476     -23.244  31.685  13.713  1.00 51.81           N  
ANISOU 3039  N   ASN A 476     5178   6193   8315    -70  -1012   -676       N  
ATOM   3040  CA  ASN A 476     -22.229  31.927  14.720  1.00 52.24           C  
ANISOU 3040  CA  ASN A 476     5219   6214   8416    -59  -1095   -788       C  
ATOM   3041  C   ASN A 476     -21.395  30.714  15.191  1.00 57.09           C  
ANISOU 3041  C   ASN A 476     5919   6992   8782    -48   -999   -790       C  
ATOM   3042  O   ASN A 476     -20.375  30.954  15.848  1.00 57.80           O  
ANISOU 3042  O   ASN A 476     5982   7056   8923    -51  -1076   -843       O  
ATOM   3043  CB  ASN A 476     -22.902  32.536  15.944  1.00 52.78           C  
ANISOU 3043  CB  ASN A 476     5286   6214   8553     14  -1176  -1069       C  
ATOM   3044  CG  ASN A 476     -23.507  33.898  15.731  1.00 66.54           C  
ANISOU 3044  CG  ASN A 476     6930   7756  10596     17  -1315  -1111       C  
ATOM   3045  OD1 ASN A 476     -22.813  34.877  15.489  1.00 61.76           O  
ANISOU 3045  OD1 ASN A 476     6224   6985  10258    -29  -1458  -1037       O  
ATOM   3046  ND2 ASN A 476     -24.817  34.002  15.861  1.00 56.67           N  
ANISOU 3046  ND2 ASN A 476     5697   6511   9322     74  -1286  -1234       N  
ATOM   3047  N   GLN A 477     -21.792  29.445  14.904  1.00 52.04           N  
ANISOU 3047  N   GLN A 477     5372   6506   7893    -36   -849   -740       N  
ATOM   3048  CA  GLN A 477     -21.052  28.310  15.475  1.00 50.22           C  
ANISOU 3048  CA  GLN A 477     5220   6411   7450    -17   -775   -756       C  
ATOM   3049  C   GLN A 477     -19.635  28.106  14.926  1.00 54.75           C  
ANISOU 3049  C   GLN A 477     5756   7011   8037    -59   -784   -589       C  
ATOM   3050  O   GLN A 477     -18.797  27.621  15.688  1.00 55.43           O  
ANISOU 3050  O   GLN A 477     5872   7156   8032    -42   -783   -637       O  
ATOM   3051  CB  GLN A 477     -21.827  27.007  15.409  1.00 49.58           C  
ANISOU 3051  CB  GLN A 477     5242   6463   7133      9   -635   -760       C  
ATOM   3052  CG  GLN A 477     -21.287  25.980  16.399  1.00 49.63           C  
ANISOU 3052  CG  GLN A 477     5326   6584   6948     41   -585   -828       C  
ATOM   3053  CD  GLN A 477     -22.169  24.792  16.535  1.00 65.56           C  
ANISOU 3053  CD  GLN A 477     7433   8708   8770     64   -471   -844       C  
ATOM   3054  OE1 GLN A 477     -23.369  24.911  16.764  1.00 65.08           O  
ANISOU 3054  OE1 GLN A 477     7384   8653   8692     82   -449   -930       O  
ATOM   3055  NE2 GLN A 477     -21.592  23.619  16.394  1.00 56.29           N  
ANISOU 3055  NE2 GLN A 477     6316   7615   7457     63   -403   -760       N  
ATOM   3056  N   ALA A 478     -19.321  28.509  13.674  1.00 50.18           N  
ANISOU 3056  N   ALA A 478     5097   6401   7568   -112   -797   -390       N  
ATOM   3057  CA  ALA A 478     -17.929  28.375  13.214  1.00 48.51           C  
ANISOU 3057  CA  ALA A 478     4827   6237   7368   -148   -807   -230       C  
ATOM   3058  C   ALA A 478     -16.991  29.116  14.194  1.00 54.91           C  
ANISOU 3058  C   ALA A 478     5583   6956   8325   -160   -934   -311       C  
ATOM   3059  O   ALA A 478     -15.954  28.563  14.577  1.00 55.27           O  
ANISOU 3059  O   ALA A 478     5640   7077   8285   -155   -922   -296       O  
ATOM   3060  CB  ALA A 478     -17.762  28.896  11.798  1.00 48.66           C  
ANISOU 3060  CB  ALA A 478     4739   6251   7499   -204   -818      1       C  
ATOM   3061  N   GLU A 479     -17.428  30.305  14.692  1.00 52.72           N  
ANISOU 3061  N   GLU A 479     5253   6518   8262   -165  -1060   -425       N  
ATOM   3062  CA  GLU A 479     -16.692  31.086  15.686  1.00 53.86           C  
ANISOU 3062  CA  GLU A 479     5341   6556   8566   -168  -1204   -547       C  
ATOM   3063  C   GLU A 479     -16.656  30.373  17.032  1.00 57.47           C  
ANISOU 3063  C   GLU A 479     5896   7110   8830    -98  -1174   -765       C  
ATOM   3064  O   GLU A 479     -15.564  30.202  17.586  1.00 58.14           O  
ANISOU 3064  O   GLU A 479     5967   7225   8898   -101  -1217   -782       O  
ATOM   3065  CB  GLU A 479     -17.262  32.500  15.849  1.00 56.80           C  
ANISOU 3065  CB  GLU A 479     5629   6723   9228   -178  -1357   -636       C  
ATOM   3066  CG  GLU A 479     -16.436  33.549  15.122  1.00 72.06           C  
ANISOU 3066  CG  GLU A 479     7413   8511  11456   -266  -1489   -441       C  
ATOM   3067  CD  GLU A 479     -14.947  33.537  15.431  1.00109.71           C  
ANISOU 3067  CD  GLU A 479    12127  13293  16264   -304  -1551   -385       C  
ATOM   3068  OE1 GLU A 479     -14.154  33.487  14.465  1.00111.02           O  
ANISOU 3068  OE1 GLU A 479    12215  13508  16459   -372  -1528   -126       O  
ATOM   3069  OE2 GLU A 479     -14.572  33.510  16.627  1.00109.27           O  
ANISOU 3069  OE2 GLU A 479    12104  13229  16185   -260  -1613   -597       O  
ATOM   3070  N   TRP A 480     -17.828  29.919  17.535  1.00 52.51           N  
ANISOU 3070  N   TRP A 480     5357   6546   8048    -37  -1097   -912       N  
ATOM   3071  CA  TRP A 480     -17.949  29.176  18.792  1.00 52.57           C  
ANISOU 3071  CA  TRP A 480     5449   6679   7845     30  -1054  -1092       C  
ATOM   3072  C   TRP A 480     -17.055  27.930  18.802  1.00 56.05           C  
ANISOU 3072  C   TRP A 480     5950   7261   8083     26   -962   -986       C  
ATOM   3073  O   TRP A 480     -16.398  27.669  19.810  1.00 56.68           O  
ANISOU 3073  O   TRP A 480     6047   7405   8083     55   -993  -1082       O  
ATOM   3074  CB  TRP A 480     -19.403  28.774  19.056  1.00 51.17           C  
ANISOU 3074  CB  TRP A 480     5342   6570   7531     80   -966  -1200       C  
ATOM   3075  CG  TRP A 480     -20.365  29.924  19.157  1.00 53.30           C  
ANISOU 3075  CG  TRP A 480     5555   6718   7980    104  -1053  -1335       C  
ATOM   3076  CD1 TRP A 480     -20.082  31.207  19.528  1.00 57.79           C  
ANISOU 3076  CD1 TRP A 480     6032   7133   8792    110  -1218  -1453       C  
ATOM   3077  CD2 TRP A 480     -21.778  29.872  18.936  1.00 52.94           C  
ANISOU 3077  CD2 TRP A 480     5535   6688   7892    132   -988  -1382       C  
ATOM   3078  NE1 TRP A 480     -21.221  31.970  19.504  1.00 58.19           N  
ANISOU 3078  NE1 TRP A 480     6048   7097   8963    146  -1262  -1570       N  
ATOM   3079  CE2 TRP A 480     -22.283  31.175  19.147  1.00 58.48           C  
ANISOU 3079  CE2 TRP A 480     6156   7244   8821    160  -1117  -1526       C  
ATOM   3080  CE3 TRP A 480     -22.673  28.849  18.573  1.00 53.09           C  
ANISOU 3080  CE3 TRP A 480     5631   6824   7716    137   -842  -1318       C  
ATOM   3081  CZ2 TRP A 480     -23.645  31.478  19.031  1.00 57.46           C  
ANISOU 3081  CZ2 TRP A 480     6021   7097   8715    199  -1096  -1609       C  
ATOM   3082  CZ3 TRP A 480     -24.018  29.154  18.438  1.00 54.59           C  
ANISOU 3082  CZ3 TRP A 480     5814   6996   7931    165   -821  -1389       C  
ATOM   3083  CH2 TRP A 480     -24.491  30.453  18.669  1.00 56.59           C  
ANISOU 3083  CH2 TRP A 480     5986   7117   8398    198   -942  -1532       C  
ATOM   3084  N   GLU A 481     -17.010  27.180  17.680  1.00 50.67           N  
ANISOU 3084  N   GLU A 481     5295   6632   7326     -2   -858   -797       N  
ATOM   3085  CA  GLU A 481     -16.164  25.994  17.534  1.00 48.94           C  
ANISOU 3085  CA  GLU A 481     5124   6533   6939      3   -776   -694       C  
ATOM   3086  C   GLU A 481     -14.669  26.363  17.661  1.00 54.99           C  
ANISOU 3086  C   GLU A 481     5814   7280   7801    -24   -861   -634       C  
ATOM   3087  O   GLU A 481     -13.939  25.668  18.363  1.00 54.99           O  
ANISOU 3087  O   GLU A 481     5850   7365   7680      3   -848   -662       O  
ATOM   3088  CB  GLU A 481     -16.443  25.315  16.200  1.00 48.44           C  
ANISOU 3088  CB  GLU A 481     5079   6518   6809    -13   -672   -530       C  
ATOM   3089  CG  GLU A 481     -17.669  24.428  16.236  1.00 52.40           C  
ANISOU 3089  CG  GLU A 481     5678   7078   7152     20   -570   -584       C  
ATOM   3090  CD  GLU A 481     -18.127  23.939  14.877  1.00 63.96           C  
ANISOU 3090  CD  GLU A 481     7151   8573   8578      7   -489   -453       C  
ATOM   3091  OE1 GLU A 481     -17.271  23.743  13.982  1.00 65.03           O  
ANISOU 3091  OE1 GLU A 481     7243   8750   8716     -6   -474   -315       O  
ATOM   3092  OE2 GLU A 481     -19.349  23.728  14.716  1.00 51.65           O  
ANISOU 3092  OE2 GLU A 481     5637   7013   6975     16   -441   -496       O  
ATOM   3093  N   ARG A 482     -14.242  27.482  17.021  1.00 52.79           N  
ANISOU 3093  N   ARG A 482     5421   6887   7750    -80   -955   -543       N  
ATOM   3094  CA  ARG A 482     -12.885  28.021  17.090  1.00 53.75           C  
ANISOU 3094  CA  ARG A 482     5444   6971   8009   -121  -1054   -471       C  
ATOM   3095  C   ARG A 482     -12.546  28.465  18.513  1.00 59.20           C  
ANISOU 3095  C   ARG A 482     6131   7618   8742    -95  -1168   -673       C  
ATOM   3096  O   ARG A 482     -11.430  28.208  18.957  1.00 59.73           O  
ANISOU 3096  O   ARG A 482     6180   7738   8778    -95  -1199   -660       O  
ATOM   3097  CB  ARG A 482     -12.730  29.202  16.130  1.00 56.58           C  
ANISOU 3097  CB  ARG A 482     5670   7202   8626   -196  -1141   -319       C  
ATOM   3098  CG  ARG A 482     -11.306  29.403  15.603  1.00 73.65           C  
ANISOU 3098  CG  ARG A 482     7718   9388  10880   -253  -1182   -125       C  
ATOM   3099  CD  ARG A 482     -11.273  30.194  14.295  1.00 93.35           C  
ANISOU 3099  CD  ARG A 482    10081  11823  13563   -329  -1216    105       C  
ATOM   3100  NE  ARG A 482     -11.969  29.500  13.201  1.00107.03           N  
ANISOU 3100  NE  ARG A 482    11852  13673  15142   -314  -1076    226       N  
ATOM   3101  CZ  ARG A 482     -13.174  29.829  12.737  1.00116.96           C  
ANISOU 3101  CZ  ARG A 482    13129  14872  16437   -314  -1060    216       C  
ATOM   3102  NH1 ARG A 482     -13.833  30.862  13.250  1.00103.34           N  
ANISOU 3102  NH1 ARG A 482    11389  12969  14908   -325  -1172     93       N  
ATOM   3103  NH2 ARG A 482     -13.728  29.128  11.757  1.00 98.78           N  
ANISOU 3103  NH2 ARG A 482    10859  12693  13981   -297   -937    319       N  
ATOM   3104  N   SER A 483     -13.495  29.127  19.224  1.00 56.34           N  
ANISOU 3104  N   SER A 483     5783   7179   8445    -63  -1232   -869       N  
ATOM   3105  CA  SER A 483     -13.316  29.579  20.607  1.00 57.79           C  
ANISOU 3105  CA  SER A 483     5961   7347   8651    -20  -1344  -1100       C  
ATOM   3106  C   SER A 483     -13.198  28.395  21.568  1.00 63.31           C  
ANISOU 3106  C   SER A 483     6759   8232   9064     42  -1257  -1184       C  
ATOM   3107  O   SER A 483     -12.364  28.428  22.483  1.00 64.37           O  
ANISOU 3107  O   SER A 483     6875   8407   9175     61  -1332  -1275       O  
ATOM   3108  CB  SER A 483     -14.449  30.498  21.038  1.00 61.87           C  
ANISOU 3108  CB  SER A 483     6462   7761   9285     16  -1420  -1297       C  
ATOM   3109  OG  SER A 483     -14.301  31.743  20.380  1.00 74.35           O  
ANISOU 3109  OG  SER A 483     7929   9139  11182    -43  -1550  -1233       O  
ATOM   3110  N   PHE A 484     -13.999  27.343  21.334  1.00 59.37           N  
ANISOU 3110  N   PHE A 484     6358   7844   8358     69  -1106  -1137       N  
ATOM   3111  CA  PHE A 484     -13.983  26.095  22.104  1.00 59.12           C  
ANISOU 3111  CA  PHE A 484     6417   7982   8062    117  -1014  -1166       C  
ATOM   3112  C   PHE A 484     -12.605  25.416  21.964  1.00 60.94           C  
ANISOU 3112  C   PHE A 484     6641   8269   8245    101  -1005  -1033       C  
ATOM   3113  O   PHE A 484     -11.960  25.152  22.971  1.00 61.05           O  
ANISOU 3113  O   PHE A 484     6662   8363   8171    131  -1045  -1109       O  
ATOM   3114  CB  PHE A 484     -15.107  25.177  21.607  1.00 60.30           C  
ANISOU 3114  CB  PHE A 484     6653   8196   8062    129   -870  -1103       C  
ATOM   3115  CG  PHE A 484     -15.329  23.907  22.380  1.00 62.57           C  
ANISOU 3115  CG  PHE A 484     7028   8641   8104    172   -781  -1119       C  
ATOM   3116  CD1 PHE A 484     -16.358  23.813  23.308  1.00 67.57           C  
ANISOU 3116  CD1 PHE A 484     7693   9362   8617    216   -760  -1258       C  
ATOM   3117  CD2 PHE A 484     -14.583  22.767  22.103  1.00 64.86           C  
ANISOU 3117  CD2 PHE A 484     7362   8996   8287    169   -716   -979       C  
ATOM   3118  CE1 PHE A 484     -16.598  22.621  23.994  1.00 68.82           C  
ANISOU 3118  CE1 PHE A 484     7919   9673   8556    245   -679  -1236       C  
ATOM   3119  CE2 PHE A 484     -14.814  21.577  22.793  1.00 68.51           C  
ANISOU 3119  CE2 PHE A 484     7898   9584   8550    202   -646   -971       C  
ATOM   3120  CZ  PHE A 484     -15.817  21.512  23.739  1.00 67.72           C  
ANISOU 3120  CZ  PHE A 484     7823   9571   8335    233   -628  -1086       C  
ATOM   3121  N   ARG A 485     -12.137  25.204  20.720  1.00 56.20           N  
ANISOU 3121  N   ARG A 485     6014   7637   7703     58   -959   -839       N  
ATOM   3122  CA  ARG A 485     -10.847  24.580  20.422  1.00 56.13           C  
ANISOU 3122  CA  ARG A 485     5983   7687   7657     49   -943   -704       C  
ATOM   3123  C   ARG A 485      -9.680  25.364  21.047  1.00 62.04           C  
ANISOU 3123  C   ARG A 485     6640   8395   8538     27  -1081   -744       C  
ATOM   3124  O   ARG A 485      -8.871  24.761  21.756  1.00 61.42           O  
ANISOU 3124  O   ARG A 485     6577   8405   8355     54  -1089   -756       O  
ATOM   3125  CB  ARG A 485     -10.645  24.439  18.904  1.00 55.01           C  
ANISOU 3125  CB  ARG A 485     5801   7533   7567     13   -878   -507       C  
ATOM   3126  CG  ARG A 485      -9.470  23.537  18.524  1.00 63.04           C  
ANISOU 3126  CG  ARG A 485     6804   8649   8501     27   -832   -376       C  
ATOM   3127  CD  ARG A 485      -9.252  23.499  17.028  1.00 71.99           C  
ANISOU 3127  CD  ARG A 485     7876   9803   9674      2   -775   -196       C  
ATOM   3128  NE  ARG A 485      -7.977  22.867  16.684  1.00 81.04           N  
ANISOU 3128  NE  ARG A 485     8975  11049  10766     21   -751    -82       N  
ATOM   3129  CZ  ARG A 485      -6.843  23.521  16.443  1.00 92.34           C  
ANISOU 3129  CZ  ARG A 485    10279  12481  12323    -21   -820     20       C  
ATOM   3130  NH1 ARG A 485      -6.806  24.847  16.503  1.00 81.04           N  
ANISOU 3130  NH1 ARG A 485     8756  10935  11099    -91   -930     28       N  
ATOM   3131  NH2 ARG A 485      -5.738  22.854  16.145  1.00 77.14           N  
ANISOU 3131  NH2 ARG A 485     8311  10668  10330      8   -787    115       N  
ATOM   3132  N   ASP A 486      -9.616  26.696  20.802  1.00 60.66           N  
ANISOU 3132  N   ASP A 486     6366   8078   8603    -23  -1198   -763       N  
ATOM   3133  CA  ASP A 486      -8.571  27.590  21.316  1.00 62.37           C  
ANISOU 3133  CA  ASP A 486     6479   8222   8995    -55  -1354   -804       C  
ATOM   3134  C   ASP A 486      -8.508  27.571  22.841  1.00 69.03           C  
ANISOU 3134  C   ASP A 486     7358   9123   9746      3  -1426  -1029       C  
ATOM   3135  O   ASP A 486      -7.406  27.550  23.388  1.00 69.84           O  
ANISOU 3135  O   ASP A 486     7417   9260   9857      0  -1499  -1037       O  
ATOM   3136  CB  ASP A 486      -8.773  29.032  20.826  1.00 65.16           C  
ANISOU 3136  CB  ASP A 486     6724   8387   9648   -117  -1480   -798       C  
ATOM   3137  CG  ASP A 486      -8.602  29.250  19.334  1.00 76.63           C  
ANISOU 3137  CG  ASP A 486     8099   9794  11221   -187  -1439   -545       C  
ATOM   3138  OD1 ASP A 486      -8.253  28.274  18.622  1.00 76.46           O  
ANISOU 3138  OD1 ASP A 486     8105   9901  11043   -181  -1311   -385       O  
ATOM   3139  OD2 ASP A 486      -8.883  30.381  18.864  1.00 83.90           O  
ANISOU 3139  OD2 ASP A 486     8930  10558  12390   -242  -1538   -509       O  
ATOM   3140  N   TYR A 487      -9.675  27.559  23.521  1.00 66.34           N  
ANISOU 3140  N   TYR A 487     7089   8815   9304     59  -1404  -1207       N  
ATOM   3141  CA  TYR A 487      -9.757  27.503  24.978  1.00 67.86           C  
ANISOU 3141  CA  TYR A 487     7309   9107   9368    126  -1460  -1426       C  
ATOM   3142  C   TYR A 487      -9.208  26.168  25.483  1.00 72.77           C  
ANISOU 3142  C   TYR A 487     8002   9913   9736    162  -1369  -1361       C  
ATOM   3143  O   TYR A 487      -8.319  26.173  26.328  1.00 72.27           O  
ANISOU 3143  O   TYR A 487     7910   9916   9634    182  -1450  -1432       O  
ATOM   3144  CB  TYR A 487     -11.208  27.722  25.456  1.00 69.56           C  
ANISOU 3144  CB  TYR A 487     7569   9344   9515    181  -1436  -1606       C  
ATOM   3145  CG  TYR A 487     -11.448  27.456  26.932  1.00 72.43           C  
ANISOU 3145  CG  TYR A 487     7965   9880   9675    264  -1456  -1813       C  
ATOM   3146  CD1 TYR A 487     -10.966  28.328  27.907  1.00 75.87           C  
ANISOU 3146  CD1 TYR A 487     8328  10306  10192    299  -1620  -2028       C  
ATOM   3147  CD2 TYR A 487     -12.215  26.371  27.349  1.00 72.23           C  
ANISOU 3147  CD2 TYR A 487     8030  10035   9380    309  -1318  -1796       C  
ATOM   3148  CE1 TYR A 487     -11.203  28.100  29.262  1.00 77.49           C  
ANISOU 3148  CE1 TYR A 487     8551  10708  10185    384  -1638  -2224       C  
ATOM   3149  CE2 TYR A 487     -12.459  26.133  28.701  1.00 73.81           C  
ANISOU 3149  CE2 TYR A 487     8242  10426   9376    384  -1332  -1961       C  
ATOM   3150  CZ  TYR A 487     -11.952  27.001  29.654  1.00 83.00           C  
ANISOU 3150  CZ  TYR A 487     9333  11607  10596    426  -1488  -2179       C  
ATOM   3151  OH  TYR A 487     -12.195  26.769  30.987  1.00 83.68           O  
ANISOU 3151  OH  TYR A 487     9421  11919  10457    508  -1500  -2346       O  
ATOM   3152  N   VAL A 488      -9.709  25.036  24.933  1.00 70.35           N  
ANISOU 3152  N   VAL A 488     7781   9678   9271    169  -1213  -1223       N  
ATOM   3153  CA  VAL A 488      -9.324  23.669  25.314  1.00 70.29           C  
ANISOU 3153  CA  VAL A 488     7843   9820   9043    203  -1125  -1141       C  
ATOM   3154  C   VAL A 488      -7.790  23.457  25.167  1.00 75.99           C  
ANISOU 3154  C   VAL A 488     8511  10549   9812    183  -1171  -1029       C  
ATOM   3155  O   VAL A 488      -7.147  22.995  26.114  1.00 75.53           O  
ANISOU 3155  O   VAL A 488     8460  10599   9639    217  -1204  -1065       O  
ATOM   3156  CB  VAL A 488     -10.138  22.609  24.517  1.00 72.38           C  
ANISOU 3156  CB  VAL A 488     8195  10111   9196    205   -971  -1011       C  
ATOM   3157  CG1 VAL A 488      -9.576  21.210  24.710  1.00 71.79           C  
ANISOU 3157  CG1 VAL A 488     8177  10145   8955    233   -900   -898       C  
ATOM   3158  CG2 VAL A 488     -11.612  22.639  24.902  1.00 71.90           C  
ANISOU 3158  CG2 VAL A 488     8186  10084   9050    230   -923  -1120       C  
ATOM   3159  N   LEU A 489      -7.222  23.803  23.998  1.00 74.19           N  
ANISOU 3159  N   LEU A 489     8219  10223   9746    130  -1173   -887       N  
ATOM   3160  CA  LEU A 489      -5.790  23.645  23.714  1.00 74.82           C  
ANISOU 3160  CA  LEU A 489     8230  10319   9881    110  -1208   -764       C  
ATOM   3161  C   LEU A 489      -4.923  24.558  24.580  1.00 83.55           C  
ANISOU 3161  C   LEU A 489     9245  11394  11107     93  -1370   -869       C  
ATOM   3162  O   LEU A 489      -3.800  24.173  24.914  1.00 83.76           O  
ANISOU 3162  O   LEU A 489     9237  11487  11102    100  -1402   -818       O  
ATOM   3163  CB  LEU A 489      -5.476  23.896  22.225  1.00 73.92           C  
ANISOU 3163  CB  LEU A 489     8047  10137   9902     57  -1169   -580       C  
ATOM   3164  CG  LEU A 489      -6.031  22.892  21.210  1.00 76.71           C  
ANISOU 3164  CG  LEU A 489     8470  10541  10135     81  -1016   -461       C  
ATOM   3165  CD1 LEU A 489      -5.602  23.258  19.812  1.00 76.29           C  
ANISOU 3165  CD1 LEU A 489     8325  10456  10205     35   -993   -291       C  
ATOM   3166  CD2 LEU A 489      -5.602  21.468  21.523  1.00 78.91           C  
ANISOU 3166  CD2 LEU A 489     8815  10939  10227    143   -945   -419       C  
ATOM   3167  N   CYS A 490      -5.428  25.764  24.925  1.00 83.67           N  
ANISOU 3167  N   CYS A 490     9216  11303  11271     74  -1481  -1024       N  
ATOM   3168  CA  CYS A 490      -4.716  26.729  25.763  1.00 86.66           C  
ANISOU 3168  CA  CYS A 490     9504  11631  11790     61  -1659  -1162       C  
ATOM   3169  C   CYS A 490      -4.464  26.144  27.157  1.00 90.62           C  
ANISOU 3169  C   CYS A 490    10053  12296  12081    132  -1684  -1303       C  
ATOM   3170  O   CYS A 490      -3.352  26.270  27.677  1.00 91.73           O  
ANISOU 3170  O   CYS A 490    10130  12466  12256    127  -1783  -1319       O  
ATOM   3171  CB  CYS A 490      -5.470  28.050  25.846  1.00 89.17           C  
ANISOU 3171  CB  CYS A 490     9772  11793  12315     43  -1775  -1320       C  
ATOM   3172  SG  CYS A 490      -4.831  29.179  27.102  1.00 96.35           S  
ANISOU 3172  SG  CYS A 490    10587  12648  13372     56  -2011  -1573       S  
ATOM   3173  N   GLN A 491      -5.486  25.485  27.736  1.00 85.93           N  
ANISOU 3173  N   GLN A 491     9561  11820  11267    195  -1592  -1387       N  
ATOM   3174  CA  GLN A 491      -5.432  24.816  29.040  1.00 86.26           C  
ANISOU 3174  CA  GLN A 491     9648  12053  11072    265  -1594  -1492       C  
ATOM   3175  C   GLN A 491      -4.443  23.634  29.014  1.00 90.84           C  
ANISOU 3175  C   GLN A 491    10252  12738  11526    273  -1534  -1316       C  
ATOM   3176  O   GLN A 491      -3.895  23.277  30.060  1.00 92.08           O  
ANISOU 3176  O   GLN A 491    10404  13031  11550    314  -1585  -1374       O  
ATOM   3177  CB  GLN A 491      -6.828  24.338  29.464  1.00 86.79           C  
ANISOU 3177  CB  GLN A 491     9805  12226  10946    317  -1491  -1565       C  
ATOM   3178  CG  GLN A 491      -7.855  25.462  29.648  1.00 99.16           C  
ANISOU 3178  CG  GLN A 491    11345  13721  12610    333  -1554  -1771       C  
ATOM   3179  CD  GLN A 491      -7.688  26.242  30.931  1.00121.97           C  
ANISOU 3179  CD  GLN A 491    14172  16682  15489    388  -1707  -2031       C  
ATOM   3180  OE1 GLN A 491      -7.343  27.427  30.921  1.00120.18           O  
ANISOU 3180  OE1 GLN A 491    13859  16308  15495    368  -1860  -2156       O  
ATOM   3181  NE2 GLN A 491      -7.967  25.610  32.063  1.00114.53           N  
ANISOU 3181  NE2 GLN A 491    13264  15972  14282    460  -1678  -2119       N  
ATOM   3182  N   ALA A 492      -4.194  23.055  27.818  1.00 86.08           N  
ANISOU 3182  N   ALA A 492     9665  12077  10966    239  -1433  -1109       N  
ATOM   3183  CA  ALA A 492      -3.227  21.971  27.622  1.00 85.35           C  
ANISOU 3183  CA  ALA A 492     9582  12059  10787    254  -1380   -944       C  
ATOM   3184  C   ALA A 492      -1.793  22.551  27.542  1.00 89.68           C  
ANISOU 3184  C   ALA A 492    10014  12567  11494    217  -1495   -906       C  
ATOM   3185  O   ALA A 492      -0.907  22.100  28.274  1.00 89.91           O  
ANISOU 3185  O   ALA A 492    10025  12696  11442    246  -1544   -905       O  
ATOM   3186  CB  ALA A 492      -3.568  21.172  26.365  1.00 84.41           C  
ANISOU 3186  CB  ALA A 492     9514  11903  10654    247  -1238   -773       C  
ATOM   3187  N   ASN A 493      -1.588  23.571  26.674  1.00 85.89           N  
ANISOU 3187  N   ASN A 493     9447  11945  11243    150  -1544   -863       N  
ATOM   3188  CA  ASN A 493      -0.323  24.278  26.442  1.00112.14           C  
ANISOU 3188  CA  ASN A 493    12638  15211  14759     96  -1656   -801       C  
ATOM   3189  C   ASN A 493      -0.582  25.539  25.621  1.00139.09           C  
ANISOU 3189  C   ASN A 493    15963  18451  18432     17  -1724   -788       C  
ATOM   3190  O   ASN A 493       0.196  26.488  25.665  1.00101.33           O  
ANISOU 3190  O   ASN A 493    11059  13583  13857    -40  -1863   -790       O  
ATOM   3191  CB  ASN A 493       0.693  23.378  25.729  1.00112.31           C  
ANISOU 3191  CB  ASN A 493    12630  15302  14738    101  -1575   -592       C  
ATOM   3192  N   CYS A 507      -6.817  29.860  29.296  1.00 94.75           N  
ANISOU 3192  N   CYS A 507    10460  12576  12967    233  -2102  -2158       N  
ATOM   3193  CA  CYS A 507      -7.230  31.132  28.706  1.00 95.02           C  
ANISOU 3193  CA  CYS A 507    10418  12369  13318    192  -2217  -2218       C  
ATOM   3194  C   CYS A 507      -8.635  31.508  29.164  1.00 97.09           C  
ANISOU 3194  C   CYS A 507    10714  12648  13527    271  -2209  -2444       C  
ATOM   3195  O   CYS A 507      -9.094  31.086  30.228  1.00 97.60           O  
ANISOU 3195  O   CYS A 507    10828  12917  13340    364  -2176  -2621       O  
ATOM   3196  CB  CYS A 507      -7.155  31.070  27.180  1.00 94.22           C  
ANISOU 3196  CB  CYS A 507    10302  12130  13368     95  -2133  -1922       C  
ATOM   3197  SG  CYS A 507      -5.473  31.011  26.515  1.00 98.26           S  
ANISOU 3197  SG  CYS A 507    10718  12588  14027     -3  -2183  -1672       S  
ATOM   3198  N   GLU A 508      -9.293  32.331  28.341  1.00 91.17           N  
ANISOU 3198  N   GLU A 508     9927  11693  13021    235  -2245  -2426       N  
ATOM   3199  CA  GLU A 508     -10.662  32.796  28.467  1.00 90.07           C  
ANISOU 3199  CA  GLU A 508     9806  11526  12891    299  -2239  -2605       C  
ATOM   3200  C   GLU A 508     -11.437  32.335  27.234  1.00 88.28           C  
ANISOU 3200  C   GLU A 508     9635  11254  12654    249  -2074  -2371       C  
ATOM   3201  O   GLU A 508     -10.823  32.018  26.204  1.00 86.53           O  
ANISOU 3201  O   GLU A 508     9404  10961  12512    159  -2020  -2100       O  
ATOM   3202  CB  GLU A 508     -10.691  34.329  28.601  1.00 93.74           C  
ANISOU 3202  CB  GLU A 508    10155  11754  13707    305  -2472  -2816       C  
ATOM   3203  N   ILE A 509     -12.777  32.262  27.346  1.00 81.13           N  
ANISOU 3203  N   ILE A 509     8782  10410  11634    312  -1991  -2478       N  
ATOM   3204  CA  ILE A 509     -13.655  31.887  26.236  1.00 77.03           C  
ANISOU 3204  CA  ILE A 509     8313   9852  11102    274  -1845  -2290       C  
ATOM   3205  C   ILE A 509     -14.013  33.203  25.513  1.00 77.19           C  
ANISOU 3205  C   ILE A 509     8244   9607  11478    237  -1974  -2308       C  
ATOM   3206  O   ILE A 509     -14.580  34.104  26.140  1.00 77.81           O  
ANISOU 3206  O   ILE A 509     8275   9616  11675    305  -2098  -2566       O  
ATOM   3207  CB  ILE A 509     -14.889  31.085  26.748  1.00 79.25           C  
ANISOU 3207  CB  ILE A 509     8684  10339  11087    353  -1693  -2375       C  
ATOM   3208  CG1 ILE A 509     -14.459  29.801  27.497  1.00 78.94           C  
ANISOU 3208  CG1 ILE A 509     8719  10548  10724    380  -1585  -2327       C  
ATOM   3209  CG2 ILE A 509     -15.845  30.742  25.604  1.00 78.05           C  
ANISOU 3209  CG2 ILE A 509     8579  10137  10939    313  -1558  -2197       C  
ATOM   3210  CD1 ILE A 509     -15.491  29.276  28.531  1.00 87.01           C  
ANISOU 3210  CD1 ILE A 509     9789  11808  11465    475  -1503  -2487       C  
ATOM   3211  N   LYS A 510     -13.597  33.343  24.234  1.00 70.05           N  
ANISOU 3211  N   LYS A 510     7303   8562  10751    134  -1961  -2035       N  
ATOM   3212  CA  LYS A 510     -13.814  34.548  23.417  1.00 70.20           C  
ANISOU 3212  CA  LYS A 510     7224   8327  11124     78  -2083  -1979       C  
ATOM   3213  C   LYS A 510     -15.318  34.831  23.199  1.00 73.05           C  
ANISOU 3213  C   LYS A 510     7612   8652  11491    129  -2037  -2069       C  
ATOM   3214  O   LYS A 510     -15.787  35.961  23.368  1.00 74.55           O  
ANISOU 3214  O   LYS A 510     7729   8669  11927    159  -2188  -2239       O  
ATOM   3215  CB  LYS A 510     -13.096  34.409  22.064  1.00 71.75           C  
ANISOU 3215  CB  LYS A 510     7377   8458  11429    -39  -2038  -1627       C  
ATOM   3216  CG  LYS A 510     -11.744  35.100  22.028  1.00 93.84           C  
ANISOU 3216  CG  LYS A 510    10058  11132  14466   -113  -2199  -1551       C  
ATOM   3217  CD  LYS A 510     -10.783  34.471  21.021  1.00105.90           C  
ANISOU 3217  CD  LYS A 510    11561  12724  15954   -204  -2103  -1215       C  
ATOM   3218  CE  LYS A 510      -9.788  33.539  21.675  1.00119.26           C  
ANISOU 3218  CE  LYS A 510    13299  14597  17417   -184  -2044  -1215       C  
ATOM   3219  NZ  LYS A 510      -8.403  33.760  21.173  1.00129.14           N  
ANISOU 3219  NZ  LYS A 510    14436  15803  18828   -275  -2115  -1004       N  
ATOM   3220  N   ASN A 511     -16.054  33.792  22.827  1.00 66.41           N  
ANISOU 3220  N   ASN A 511     6870   7970  10392    140  -1837  -1959       N  
ATOM   3221  CA  ASN A 511     -17.490  33.803  22.572  1.00 65.16           C  
ANISOU 3221  CA  ASN A 511     6749   7822  10187    183  -1759  -2012       C  
ATOM   3222  C   ASN A 511     -17.996  32.410  22.809  1.00 65.65           C  
ANISOU 3222  C   ASN A 511     6930   8130   9883    220  -1558  -1982       C  
ATOM   3223  O   ASN A 511     -17.203  31.474  22.846  1.00 64.25           O  
ANISOU 3223  O   ASN A 511     6804   8074   9533    193  -1476  -1856       O  
ATOM   3224  CB  ASN A 511     -17.815  34.286  21.141  1.00 62.86           C  
ANISOU 3224  CB  ASN A 511     6409   7365  10111    103  -1757  -1781       C  
ATOM   3225  CG  ASN A 511     -16.908  33.710  20.085  1.00 73.78           C  
ANISOU 3225  CG  ASN A 511     7789   8773  11471      6  -1681  -1465       C  
ATOM   3226  OD1 ASN A 511     -15.945  34.347  19.647  1.00 68.83           O  
ANISOU 3226  OD1 ASN A 511     7066   8017  11068    -67  -1793  -1336       O  
ATOM   3227  ND2 ASN A 511     -17.153  32.470  19.697  1.00 63.53           N  
ANISOU 3227  ND2 ASN A 511     6587   7649   9902      7  -1495  -1340       N  
ATOM   3228  N   ARG A 512     -19.305  32.265  22.967  1.00 61.05           N  
ANISOU 3228  N   ARG A 512     6386   7618   9195    282  -1486  -2094       N  
ATOM   3229  CA  ARG A 512     -19.942  30.977  23.209  1.00 58.79           C  
ANISOU 3229  CA  ARG A 512     6200   7554   8584    312  -1305  -2063       C  
ATOM   3230  C   ARG A 512     -21.410  31.040  22.761  1.00 61.75           C  
ANISOU 3230  C   ARG A 512     6589   7924   8951    335  -1231  -2077       C  
ATOM   3231  O   ARG A 512     -21.923  32.147  22.594  1.00 61.09           O  
ANISOU 3231  O   ARG A 512     6433   7685   9092    354  -1336  -2179       O  
ATOM   3232  CB  ARG A 512     -19.828  30.607  24.712  1.00 57.88           C  
ANISOU 3232  CB  ARG A 512     6104   7636   8252    397  -1311  -2275       C  
ATOM   3233  CG  ARG A 512     -20.560  31.556  25.630  1.00 61.70           C  
ANISOU 3233  CG  ARG A 512     6524   8123   8797    496  -1417  -2581       C  
ATOM   3234  CD  ARG A 512     -20.713  31.024  27.022  1.00 67.02           C  
ANISOU 3234  CD  ARG A 512     7217   9061   9185    587  -1378  -2762       C  
ATOM   3235  NE  ARG A 512     -21.724  31.794  27.746  1.00 69.98           N  
ANISOU 3235  NE  ARG A 512     7532   9485   9572    697  -1440  -3049       N  
ATOM   3236  CZ  ARG A 512     -22.127  31.529  28.981  1.00 82.72           C  
ANISOU 3236  CZ  ARG A 512     9134  11356  10938    798  -1414  -3244       C  
ATOM   3237  NH1 ARG A 512     -21.597  30.515  29.655  1.00 70.40           N  
ANISOU 3237  NH1 ARG A 512     7622  10018   9108    794  -1333  -3170       N  
ATOM   3238  NH2 ARG A 512     -23.054  32.278  29.557  1.00 72.17           N  
ANISOU 3238  NH2 ARG A 512     7730  10070   9621    908  -1472  -3515       N  
ATOM   3239  N   PRO A 513     -22.116  29.882  22.606  1.00 57.93           N  
ANISOU 3239  N   PRO A 513     6187   7598   8224    335  -1063  -1984       N  
ATOM   3240  CA  PRO A 513     -23.548  29.920  22.245  1.00 56.50           C  
ANISOU 3240  CA  PRO A 513     6012   7425   8030    357   -995  -2005       C  
ATOM   3241  C   PRO A 513     -24.434  30.679  23.233  1.00 61.71           C  
ANISOU 3241  C   PRO A 513     6619   8129   8701    458  -1058  -2285       C  
ATOM   3242  O   PRO A 513     -24.109  30.788  24.419  1.00 62.49           O  
ANISOU 3242  O   PRO A 513     6699   8341   8704    525  -1109  -2472       O  
ATOM   3243  CB  PRO A 513     -23.935  28.449  22.246  1.00 56.71           C  
ANISOU 3243  CB  PRO A 513     6131   7636   7779    342   -824  -1881       C  
ATOM   3244  CG  PRO A 513     -22.660  27.729  21.972  1.00 61.12           C  
ANISOU 3244  CG  PRO A 513     6731   8210   8281    289   -803  -1721       C  
ATOM   3245  CD  PRO A 513     -21.649  28.487  22.739  1.00 58.07           C  
ANISOU 3245  CD  PRO A 513     6290   7784   7991    313   -939  -1852       C  
ATOM   3246  N   SER A 514     -25.561  31.203  22.733  1.00 59.01           N  
ANISOU 3246  N   SER A 514     6243   7709   8469    477  -1058  -2320       N  
ATOM   3247  CA  SER A 514     -26.541  31.923  23.546  1.00 60.24           C  
ANISOU 3247  CA  SER A 514     6338   7909   8642    585  -1111  -2588       C  
ATOM   3248  C   SER A 514     -27.616  30.945  24.019  1.00 63.66           C  
ANISOU 3248  C   SER A 514     6814   8591   8783    624   -952  -2603       C  
ATOM   3249  O   SER A 514     -28.259  30.302  23.185  1.00 62.75           O  
ANISOU 3249  O   SER A 514     6743   8483   8614    569   -838  -2424       O  
ATOM   3250  CB  SER A 514     -27.155  33.075  22.755  1.00 63.13           C  
ANISOU 3250  CB  SER A 514     6632   8046   9309    587  -1211  -2613       C  
ATOM   3251  OG  SER A 514     -28.332  33.564  23.377  1.00 72.48           O  
ANISOU 3251  OG  SER A 514     7762   9293  10483    696  -1229  -2852       O  
ATOM   3252  N   LEU A 515     -27.793  30.817  25.350  1.00 60.62           N  
ANISOU 3252  N   LEU A 515     6406   8419   8207    717   -947  -2809       N  
ATOM   3253  CA  LEU A 515     -28.804  29.930  25.934  1.00 60.52           C  
ANISOU 3253  CA  LEU A 515     6410   8671   7912    755   -803  -2817       C  
ATOM   3254  C   LEU A 515     -30.198  30.554  25.851  1.00 65.78           C  
ANISOU 3254  C   LEU A 515     7010   9339   8643    824   -799  -2951       C  
ATOM   3255  O   LEU A 515     -31.189  29.824  25.918  1.00 66.21           O  
ANISOU 3255  O   LEU A 515     7076   9564   8518    825   -668  -2888       O  
ATOM   3256  CB  LEU A 515     -28.471  29.543  27.389  1.00 61.73           C  
ANISOU 3256  CB  LEU A 515     6547   9093   7814    830   -794  -2963       C  
ATOM   3257  CG  LEU A 515     -27.250  28.615  27.613  1.00 65.84           C  
ANISOU 3257  CG  LEU A 515     7136   9677   8201    767   -765  -2807       C  
ATOM   3258  CD1 LEU A 515     -27.190  28.139  29.055  1.00 67.34           C  
ANISOU 3258  CD1 LEU A 515     7299  10174   8112    845   -741  -2932       C  
ATOM   3259  CD2 LEU A 515     -27.231  27.402  26.633  1.00 64.36           C  
ANISOU 3259  CD2 LEU A 515     7045   9465   7946    652   -630  -2491       C  
ATOM   3260  N   LEU A 516     -30.268  31.898  25.704  1.00 61.93           N  
ANISOU 3260  N   LEU A 516     6447   8656   8428    879   -949  -3129       N  
ATOM   3261  CA  LEU A 516     -31.503  32.646  25.534  1.00 62.16           C  
ANISOU 3261  CA  LEU A 516     6403   8641   8574    951   -974  -3267       C  
ATOM   3262  C   LEU A 516     -32.100  32.317  24.175  1.00 65.71           C  
ANISOU 3262  C   LEU A 516     6895   8965   9108    854   -892  -3013       C  
ATOM   3263  O   LEU A 516     -33.296  32.029  24.088  1.00 66.38           O  
ANISOU 3263  O   LEU A 516     6963   9159   9098    879   -798  -3011       O  
ATOM   3264  CB  LEU A 516     -31.254  34.157  25.673  1.00 64.06           C  
ANISOU 3264  CB  LEU A 516     6553   8661   9128   1028  -1183  -3507       C  
ATOM   3265  CG  LEU A 516     -32.438  35.090  25.358  1.00 69.34           C  
ANISOU 3265  CG  LEU A 516     7136   9218   9992   1105  -1244  -3649       C  
ATOM   3266  CD1 LEU A 516     -33.630  34.828  26.269  1.00 69.80           C  
ANISOU 3266  CD1 LEU A 516     7143   9572   9807   1230  -1153  -3849       C  
ATOM   3267  CD2 LEU A 516     -32.014  36.525  25.453  1.00 73.80           C  
ANISOU 3267  CD2 LEU A 516     7614   9519  10906   1165  -1473  -3856       C  
ATOM   3268  N   VAL A 517     -31.259  32.325  23.121  1.00 60.85           N  
ANISOU 3268  N   VAL A 517     6325   8142   8652    744   -924  -2795       N  
ATOM   3269  CA  VAL A 517     -31.657  31.974  21.759  1.00 58.89           C  
ANISOU 3269  CA  VAL A 517     6116   7789   8470    649   -853  -2542       C  
ATOM   3270  C   VAL A 517     -32.237  30.551  21.794  1.00 63.49           C  
ANISOU 3270  C   VAL A 517     6772   8592   8759    613   -670  -2407       C  
ATOM   3271  O   VAL A 517     -33.285  30.315  21.185  1.00 63.27           O  
ANISOU 3271  O   VAL A 517     6744   8577   8720    595   -598  -2329       O  
ATOM   3272  CB  VAL A 517     -30.478  32.133  20.759  1.00 60.96           C  
ANISOU 3272  CB  VAL A 517     6404   7852   8908    547   -915  -2335       C  
ATOM   3273  CG1 VAL A 517     -30.736  31.393  19.442  1.00 58.88           C  
ANISOU 3273  CG1 VAL A 517     6195   7564   8615    450   -811  -2060       C  
ATOM   3274  CG2 VAL A 517     -30.190  33.609  20.500  1.00 61.77           C  
ANISOU 3274  CG2 VAL A 517     6414   7703   9353    566  -1103  -2424       C  
ATOM   3275  N   GLU A 518     -31.608  29.645  22.592  1.00 59.99           N  
ANISOU 3275  N   GLU A 518     6381   8323   8091    607   -608  -2392       N  
ATOM   3276  CA  GLU A 518     -32.040  28.254  22.770  1.00 58.52           C  
ANISOU 3276  CA  GLU A 518     6255   8338   7641    569   -454  -2259       C  
ATOM   3277  C   GLU A 518     -33.378  28.151  23.481  1.00 62.12           C  
ANISOU 3277  C   GLU A 518     6655   8992   7955    641   -386  -2382       C  
ATOM   3278  O   GLU A 518     -34.190  27.312  23.090  1.00 61.50           O  
ANISOU 3278  O   GLU A 518     6602   8992   7772    595   -275  -2245       O  
ATOM   3279  CB  GLU A 518     -30.998  27.419  23.528  1.00 59.74           C  
ANISOU 3279  CB  GLU A 518     6463   8620   7616    552   -426  -2214       C  
ATOM   3280  CG  GLU A 518     -29.633  27.302  22.866  1.00 66.12           C  
ANISOU 3280  CG  GLU A 518     7322   9269   8532    482   -479  -2080       C  
ATOM   3281  CD  GLU A 518     -29.532  27.337  21.354  1.00 75.70           C  
ANISOU 3281  CD  GLU A 518     8564  10293   9904    399   -475  -1888       C  
ATOM   3282  OE1 GLU A 518     -28.550  27.934  20.854  1.00 75.52           O  
ANISOU 3282  OE1 GLU A 518     8530  10114  10052    369   -565  -1845       O  
ATOM   3283  OE2 GLU A 518     -30.414  26.767  20.671  1.00 56.36           O  
ANISOU 3283  OE2 GLU A 518     6141   7864   7407    364   -387  -1777       O  
ATOM   3284  N   LYS A 519     -33.613  28.998  24.509  1.00 58.64           N  
ANISOU 3284  N   LYS A 519     6130   8637   7514    757   -457  -2646       N  
ATOM   3285  CA  LYS A 519     -34.866  29.025  25.269  1.00 59.51           C  
ANISOU 3285  CA  LYS A 519     6161   8966   7483    848   -400  -2794       C  
ATOM   3286  C   LYS A 519     -36.019  29.501  24.389  1.00 64.91           C  
ANISOU 3286  C   LYS A 519     6806   9534   8324    850   -394  -2784       C  
ATOM   3287  O   LYS A 519     -37.108  28.942  24.470  1.00 65.39           O  
ANISOU 3287  O   LYS A 519     6840   9758   8246    854   -287  -2742       O  
ATOM   3288  CB  LYS A 519     -34.738  29.912  26.505  1.00 63.41           C  
ANISOU 3288  CB  LYS A 519     6565   9574   7954    988   -497  -3107       C  
ATOM   3289  CG  LYS A 519     -34.066  29.228  27.672  1.00 61.66           C  
ANISOU 3289  CG  LYS A 519     6353   9609   7464   1012   -457  -3134       C  
ATOM   3290  CD  LYS A 519     -34.077  30.134  28.866  1.00 66.00           C  
ANISOU 3290  CD  LYS A 519     6803  10291   7982   1164   -559  -3470       C  
ATOM   3291  CE  LYS A 519     -33.408  29.497  30.046  1.00 69.45           C  
ANISOU 3291  CE  LYS A 519     7240  11005   8142   1192   -527  -3495       C  
ATOM   3292  NZ  LYS A 519     -33.009  30.526  31.030  1.00 77.35           N  
ANISOU 3292  NZ  LYS A 519     8156  12074   9162   1333   -668  -3835       N  
ATOM   3293  N   ILE A 520     -35.759  30.506  23.524  1.00 61.59           N  
ANISOU 3293  N   ILE A 520     6373   8833   8195    840   -512  -2799       N  
ATOM   3294  CA  ILE A 520     -36.708  31.055  22.542  1.00 60.52           C  
ANISOU 3294  CA  ILE A 520     6200   8548   8247    835   -529  -2764       C  
ATOM   3295  C   ILE A 520     -37.016  29.965  21.503  1.00 60.82           C  
ANISOU 3295  C   ILE A 520     6316   8585   8206    713   -407  -2479       C  
ATOM   3296  O   ILE A 520     -38.158  29.839  21.073  1.00 61.05           O  
ANISOU 3296  O   ILE A 520     6316   8650   8229    712   -349  -2441       O  
ATOM   3297  CB  ILE A 520     -36.147  32.366  21.899  1.00 63.69           C  
ANISOU 3297  CB  ILE A 520     6565   8645   8990    842   -701  -2815       C  
ATOM   3298  CG1 ILE A 520     -36.041  33.495  22.960  1.00 65.10           C  
ANISOU 3298  CG1 ILE A 520     6650   8814   9270    980   -840  -3143       C  
ATOM   3299  CG2 ILE A 520     -37.003  32.824  20.695  1.00 63.40           C  
ANISOU 3299  CG2 ILE A 520     6497   8440   9150    812   -718  -2711       C  
ATOM   3300  CD1 ILE A 520     -35.179  34.665  22.581  1.00 66.95           C  
ANISOU 3300  CD1 ILE A 520     6854   8754   9830    974  -1028  -3189       C  
ATOM   3301  N   ASN A 521     -36.019  29.158  21.134  1.00 56.07           N  
ANISOU 3301  N   ASN A 521     5808   7955   7542    618   -373  -2292       N  
ATOM   3302  CA  ASN A 521     -36.212  28.041  20.200  1.00 54.46           C  
ANISOU 3302  CA  ASN A 521     5679   7756   7257    512   -269  -2046       C  
ATOM   3303  C   ASN A 521     -37.142  27.019  20.842  1.00 58.96           C  
ANISOU 3303  C   ASN A 521     6248   8564   7591    515   -143  -2026       C  
ATOM   3304  O   ASN A 521     -38.153  26.643  20.238  1.00 57.10           O  
ANISOU 3304  O   ASN A 521     6004   8344   7348    481    -81  -1938       O  
ATOM   3305  CB  ASN A 521     -34.866  27.382  19.820  1.00 53.44           C  
ANISOU 3305  CB  ASN A 521     5639   7566   7101    433   -267  -1887       C  
ATOM   3306  CG  ASN A 521     -34.880  26.544  18.548  1.00 62.75           C  
ANISOU 3306  CG  ASN A 521     6885   8681   8275    336   -206  -1656       C  
ATOM   3307  OD1 ASN A 521     -33.948  26.589  17.739  1.00 64.40           O  
ANISOU 3307  OD1 ASN A 521     7130   8767   8573    285   -243  -1541       O  
ATOM   3308  ND2 ASN A 521     -35.902  25.746  18.336  1.00 41.31           N  
ANISOU 3308  ND2 ASN A 521     4182   6061   5454    309   -113  -1586       N  
ATOM   3309  N   LEU A 522     -36.816  26.614  22.095  1.00 57.15           N  
ANISOU 3309  N   LEU A 522     6012   8529   7173    554   -111  -2104       N  
ATOM   3310  CA  LEU A 522     -37.592  25.641  22.850  1.00 57.84           C  
ANISOU 3310  CA  LEU A 522     6081   8870   7027    553      3  -2064       C  
ATOM   3311  C   LEU A 522     -39.005  26.167  23.168  1.00 63.75           C  
ANISOU 3311  C   LEU A 522     6721   9738   7762    631     29  -2198       C  
ATOM   3312  O   LEU A 522     -39.950  25.376  23.181  1.00 63.24           O  
ANISOU 3312  O   LEU A 522     6637   9816   7576    595    128  -2095       O  
ATOM   3313  CB  LEU A 522     -36.858  25.216  24.123  1.00 58.61           C  
ANISOU 3313  CB  LEU A 522     6180   9159   6929    586     17  -2113       C  
ATOM   3314  CG  LEU A 522     -35.634  24.319  23.905  1.00 62.56           C  
ANISOU 3314  CG  LEU A 522     6783   9597   7389    503     23  -1942       C  
ATOM   3315  CD1 LEU A 522     -34.876  24.112  25.194  1.00 63.68           C  
ANISOU 3315  CD1 LEU A 522     6911   9920   7363    552     12  -2020       C  
ATOM   3316  CD2 LEU A 522     -36.005  22.990  23.266  1.00 63.40           C  
ANISOU 3316  CD2 LEU A 522     6952   9713   7426    398    117  -1702       C  
ATOM   3317  N   PHE A 523     -39.149  27.493  23.372  1.00 61.39           N  
ANISOU 3317  N   PHE A 523     6347   9373   7605    735    -69  -2425       N  
ATOM   3318  CA  PHE A 523     -40.437  28.127  23.621  1.00 62.63           C  
ANISOU 3318  CA  PHE A 523     6392   9624   7779    827    -61  -2579       C  
ATOM   3319  C   PHE A 523     -41.352  27.942  22.393  1.00 64.95           C  
ANISOU 3319  C   PHE A 523     6696   9796   8187    756    -24  -2425       C  
ATOM   3320  O   PHE A 523     -42.500  27.537  22.553  1.00 65.28           O  
ANISOU 3320  O   PHE A 523     6679  10000   8124    764     61  -2404       O  
ATOM   3321  CB  PHE A 523     -40.270  29.626  23.973  1.00 66.21           C  
ANISOU 3321  CB  PHE A 523     6768   9976   8412    957   -202  -2862       C  
ATOM   3322  CG  PHE A 523     -41.540  30.430  23.804  1.00 69.58           C  
ANISOU 3322  CG  PHE A 523     7090  10394   8954   1044   -224  -3002       C  
ATOM   3323  CD1 PHE A 523     -42.532  30.408  24.779  1.00 74.63           C  
ANISOU 3323  CD1 PHE A 523     7621  11321   9416   1149   -159  -3157       C  
ATOM   3324  CD2 PHE A 523     -41.771  31.161  22.642  1.00 71.91           C  
ANISOU 3324  CD2 PHE A 523     7385  10412   9528   1021   -307  -2962       C  
ATOM   3325  CE1 PHE A 523     -43.723  31.122  24.605  1.00 77.03           C  
ANISOU 3325  CE1 PHE A 523     7819  11622   9826   1236   -178  -3289       C  
ATOM   3326  CE2 PHE A 523     -42.967  31.864  22.463  1.00 76.21           C  
ANISOU 3326  CE2 PHE A 523     7828  10942  10185   1102   -331  -3081       C  
ATOM   3327  CZ  PHE A 523     -43.932  31.845  23.449  1.00 75.96           C  
ANISOU 3327  CZ  PHE A 523     7691  11187   9982   1213   -267  -3253       C  
ATOM   3328  N   ALA A 524     -40.844  28.257  21.186  1.00 59.12           N  
ANISOU 3328  N   ALA A 524     6019   8788   7654    690    -91  -2317       N  
ATOM   3329  CA  ALA A 524     -41.603  28.156  19.939  1.00 57.29           C  
ANISOU 3329  CA  ALA A 524     5796   8435   7536    625    -72  -2172       C  
ATOM   3330  C   ALA A 524     -41.763  26.716  19.475  1.00 58.88           C  
ANISOU 3330  C   ALA A 524     6073   8710   7590    509     38  -1943       C  
ATOM   3331  O   ALA A 524     -42.726  26.416  18.768  1.00 57.34           O  
ANISOU 3331  O   ALA A 524     5860   8511   7415    469     81  -1852       O  
ATOM   3332  CB  ALA A 524     -40.930  28.972  18.850  1.00 57.31           C  
ANISOU 3332  CB  ALA A 524     5826   8161   7787    595   -183  -2120       C  
ATOM   3333  N   MET A 525     -40.800  25.839  19.817  1.00 55.23           N  
ANISOU 3333  N   MET A 525     5690   8295   7000    456     72  -1850       N  
ATOM   3334  CA  MET A 525     -40.838  24.433  19.424  1.00 54.31           C  
ANISOU 3334  CA  MET A 525     5644   8225   6765    351    157  -1643       C  
ATOM   3335  C   MET A 525     -41.888  23.714  20.276  1.00 58.85           C  
ANISOU 3335  C   MET A 525     6157   9041   7161    355    253  -1633       C  
ATOM   3336  O   MET A 525     -42.827  23.158  19.712  1.00 58.81           O  
ANISOU 3336  O   MET A 525     6139   9051   7154    300    303  -1527       O  
ATOM   3337  CB  MET A 525     -39.445  23.798  19.546  1.00 56.26           C  
ANISOU 3337  CB  MET A 525     5985   8436   6955    305    148  -1558       C  
ATOM   3338  CG  MET A 525     -39.323  22.431  18.907  1.00 59.39           C  
ANISOU 3338  CG  MET A 525     6462   8815   7288    202    205  -1354       C  
ATOM   3339  SD  MET A 525     -39.968  21.126  19.983  1.00 65.54           S  
ANISOU 3339  SD  MET A 525     7218   9834   7849    170    305  -1271       S  
ATOM   3340  CE  MET A 525     -38.802  21.230  21.384  1.00 62.59           C  
ANISOU 3340  CE  MET A 525     6851   9584   7347    227    288  -1355       C  
ATOM   3341  N   PHE A 526     -41.760  23.757  21.620  1.00 55.74           N  
ANISOU 3341  N   PHE A 526     5714   8848   6617    422    275  -1740       N  
ATOM   3342  CA  PHE A 526     -42.734  23.149  22.536  1.00 56.50           C  
ANISOU 3342  CA  PHE A 526     5726   9217   6524    433    368  -1721       C  
ATOM   3343  C   PHE A 526     -44.081  23.882  22.458  1.00 62.79           C  
ANISOU 3343  C   PHE A 526     6408  10078   7370    500    379  -1836       C  
ATOM   3344  O   PHE A 526     -45.126  23.244  22.586  1.00 62.64           O  
ANISOU 3344  O   PHE A 526     6328  10214   7259    465    461  -1744       O  
ATOM   3345  CB  PHE A 526     -42.215  23.151  23.988  1.00 59.09           C  
ANISOU 3345  CB  PHE A 526     6014   9773   6667    504    380  -1821       C  
ATOM   3346  CG  PHE A 526     -41.132  22.146  24.307  1.00 59.08           C  
ANISOU 3346  CG  PHE A 526     6100   9789   6561    432    396  -1670       C  
ATOM   3347  CD1 PHE A 526     -41.385  20.778  24.236  1.00 60.76           C  
ANISOU 3347  CD1 PHE A 526     6340  10066   6682    325    470  -1437       C  
ATOM   3348  CD2 PHE A 526     -39.882  22.563  24.748  1.00 60.11           C  
ANISOU 3348  CD2 PHE A 526     6274   9877   6690    475    330  -1765       C  
ATOM   3349  CE1 PHE A 526     -40.392  19.848  24.564  1.00 60.97           C  
ANISOU 3349  CE1 PHE A 526     6439  10101   6626    267    475  -1299       C  
ATOM   3350  CE2 PHE A 526     -38.900  21.630  25.107  1.00 62.22           C  
ANISOU 3350  CE2 PHE A 526     6612  10176   6855    417    343  -1627       C  
ATOM   3351  CZ  PHE A 526     -39.157  20.280  25.001  1.00 59.68           C  
ANISOU 3351  CZ  PHE A 526     6319   9906   6450    316    415  -1394       C  
ATOM   3352  N   GLY A 527     -44.022  25.206  22.244  1.00 59.93           N  
ANISOU 3352  N   GLY A 527     6013   9589   7170    593    290  -2027       N  
ATOM   3353  CA  GLY A 527     -45.170  26.095  22.094  1.00 60.61           C  
ANISOU 3353  CA  GLY A 527     5991   9689   7349    675    274  -2164       C  
ATOM   3354  C   GLY A 527     -46.075  25.706  20.949  1.00 64.62           C  
ANISOU 3354  C   GLY A 527     6505  10102   7946    590    306  -2006       C  
ATOM   3355  O   GLY A 527     -47.293  25.858  21.062  1.00 65.38           O  
ANISOU 3355  O   GLY A 527     6499  10320   8024    630    346  -2050       O  
ATOM   3356  N   THR A 528     -45.494  25.164  19.847  1.00 60.07           N  
ANISOU 3356  N   THR A 528     6043   9327   7454    478    289  -1826       N  
ATOM   3357  CA  THR A 528     -46.271  24.664  18.707  1.00 59.02           C  
ANISOU 3357  CA  THR A 528     5924   9112   7390    392    313  -1671       C  
ATOM   3358  C   THR A 528     -47.058  23.458  19.187  1.00 63.87           C  
ANISOU 3358  C   THR A 528     6504   9932   7831    329    418  -1548       C  
ATOM   3359  O   THR A 528     -48.261  23.383  18.935  1.00 65.81           O  
ANISOU 3359  O   THR A 528     6673  10242   8090    319    453  -1522       O  
ATOM   3360  CB  THR A 528     -45.394  24.316  17.507  1.00 62.10           C  
ANISOU 3360  CB  THR A 528     6434   9283   7878    301    269  -1526       C  
ATOM   3361  OG1 THR A 528     -44.462  25.362  17.278  1.00 64.47           O  
ANISOU 3361  OG1 THR A 528     6759   9422   8315    351    175  -1615       O  
ATOM   3362  CG2 THR A 528     -46.208  24.051  16.242  1.00 57.36           C  
ANISOU 3362  CG2 THR A 528     5835   8591   7370    237    269  -1410       C  
ATOM   3363  N   GLY A 529     -46.384  22.565  19.917  1.00 57.50           N  
ANISOU 3363  N   GLY A 529     5743   9231   6875    287    461  -1470       N  
ATOM   3364  CA  GLY A 529     -46.998  21.387  20.508  1.00 56.71           C  
ANISOU 3364  CA  GLY A 529     5602   9330   6617    220    550  -1327       C  
ATOM   3365  C   GLY A 529     -48.158  21.747  21.410  1.00 61.04           C  
ANISOU 3365  C   GLY A 529     5995  10139   7060    295    610  -1419       C  
ATOM   3366  O   GLY A 529     -49.228  21.144  21.299  1.00 61.42           O  
ANISOU 3366  O   GLY A 529     5974  10289   7074    238    669  -1304       O  
ATOM   3367  N   ILE A 530     -47.963  22.767  22.282  1.00 57.63           N  
ANISOU 3367  N   ILE A 530     5497   9817   6582    431    589  -1637       N  
ATOM   3368  CA  ILE A 530     -48.981  23.240  23.231  1.00 58.71           C  
ANISOU 3368  CA  ILE A 530     5471  10233   6602    537    641  -1773       C  
ATOM   3369  C   ILE A 530     -50.111  23.961  22.452  1.00 62.71           C  
ANISOU 3369  C   ILE A 530     5905  10658   7263    576    620  -1845       C  
ATOM   3370  O   ILE A 530     -51.284  23.682  22.720  1.00 63.72           O  
ANISOU 3370  O   ILE A 530     5913  10986   7310    578    693  -1808       O  
ATOM   3371  CB  ILE A 530     -48.396  24.110  24.404  1.00 62.40           C  
ANISOU 3371  CB  ILE A 530     5889  10845   6975    686    608  -2017       C  
ATOM   3372  CG1 ILE A 530     -47.210  23.396  25.116  1.00 61.93           C  
ANISOU 3372  CG1 ILE A 530     5904  10859   6766    645    621  -1934       C  
ATOM   3373  CG2 ILE A 530     -49.489  24.451  25.436  1.00 63.99           C  
ANISOU 3373  CG2 ILE A 530     5906  11386   7020    806    671  -2160       C  
ATOM   3374  CD1 ILE A 530     -46.255  24.310  25.979  1.00 61.60           C  
ANISOU 3374  CD1 ILE A 530     5863  10848   6695    773    547  -2177       C  
ATOM   3375  N   ALA A 531     -49.766  24.842  21.480  1.00 57.46           N  
ANISOU 3375  N   ALA A 531     5304   9709   6819    599    521  -1927       N  
ATOM   3376  CA  ALA A 531     -50.759  25.559  20.674  1.00 57.41           C  
ANISOU 3376  CA  ALA A 531     5234   9600   6979    634    487  -1982       C  
ATOM   3377  C   ALA A 531     -51.601  24.593  19.824  1.00 61.22           C  
ANISOU 3377  C   ALA A 531     5722  10065   7473    506    540  -1763       C  
ATOM   3378  O   ALA A 531     -52.831  24.638  19.919  1.00 61.98           O  
ANISOU 3378  O   ALA A 531     5699  10298   7554    532    583  -1777       O  
ATOM   3379  CB  ALA A 531     -50.089  26.591  19.783  1.00 57.39           C  
ANISOU 3379  CB  ALA A 531     5301   9294   7211    666    364  -2063       C  
ATOM   3380  N   MET A 532     -50.953  23.692  19.039  1.00 55.90           N  
ANISOU 3380  N   MET A 532     5178   9237   6823    373    533  -1571       N  
ATOM   3381  CA  MET A 532     -51.660  22.717  18.190  1.00 55.09           C  
ANISOU 3381  CA  MET A 532     5088   9098   6743    249    564  -1377       C  
ATOM   3382  C   MET A 532     -52.520  21.738  19.012  1.00 62.28           C  
ANISOU 3382  C   MET A 532     5903  10271   7490    198    664  -1266       C  
ATOM   3383  O   MET A 532     -53.496  21.218  18.472  1.00 63.55           O  
ANISOU 3383  O   MET A 532     6017  10444   7684    124    686  -1151       O  
ATOM   3384  CB  MET A 532     -50.700  21.944  17.261  1.00 55.25           C  
ANISOU 3384  CB  MET A 532     5262   8912   6818    137    525  -1228       C  
ATOM   3385  CG  MET A 532     -49.917  22.837  16.273  1.00 56.69           C  
ANISOU 3385  CG  MET A 532     5525   8851   7165    168    430  -1288       C  
ATOM   3386  SD  MET A 532     -50.926  23.869  15.172  1.00 59.66           S  
ANISOU 3386  SD  MET A 532     5831   9110   7728    209    370  -1338       S  
ATOM   3387  CE  MET A 532     -50.912  25.489  16.064  1.00 56.60           C  
ANISOU 3387  CE  MET A 532     5349   8748   7406    378    324  -1589       C  
ATOM   3388  N   SER A 533     -52.200  21.530  20.312  1.00 59.15           N  
ANISOU 3388  N   SER A 533     5464  10094   6918    238    718  -1295       N  
ATOM   3389  CA  SER A 533     -52.962  20.649  21.209  1.00 60.04           C  
ANISOU 3389  CA  SER A 533     5463  10491   6858    193    814  -1170       C  
ATOM   3390  C   SER A 533     -54.298  21.279  21.635  1.00 66.09           C  
ANISOU 3390  C   SER A 533     6048  11480   7584    283    863  -1275       C  
ATOM   3391  O   SER A 533     -55.167  20.564  22.135  1.00 66.48           O  
ANISOU 3391  O   SER A 533     5981  11759   7519    232    943  -1142       O  
ATOM   3392  CB  SER A 533     -52.142  20.291  22.448  1.00 62.75           C  
ANISOU 3392  CB  SER A 533     5809  11018   7014    215    852  -1161       C  
ATOM   3393  OG  SER A 533     -52.094  21.348  23.394  1.00 66.45           O  
ANISOU 3393  OG  SER A 533     6193  11665   7391    376    857  -1396       O  
ATOM   3394  N   THR A 534     -54.458  22.611  21.457  1.00 63.77           N  
ANISOU 3394  N   THR A 534     5720  11118   7393    419    810  -1506       N  
ATOM   3395  CA  THR A 534     -55.685  23.323  21.840  1.00 65.41           C  
ANISOU 3395  CA  THR A 534     5752  11522   7580    531    844  -1642       C  
ATOM   3396  C   THR A 534     -56.790  23.115  20.786  1.00 70.81           C  
ANISOU 3396  C   THR A 534     6396  12111   8396    456    841  -1531       C  
ATOM   3397  O   THR A 534     -57.915  23.583  20.991  1.00 72.44           O  
ANISOU 3397  O   THR A 534     6451  12474   8599    533    872  -1614       O  
ATOM   3398  CB  THR A 534     -55.424  24.816  22.111  1.00 68.47           C  
ANISOU 3398  CB  THR A 534     6108  11864   8043    715    772  -1946       C  
ATOM   3399  OG1 THR A 534     -55.067  25.482  20.900  1.00 65.15           O  
ANISOU 3399  OG1 THR A 534     5790  11097   7867    708    664  -1982       O  
ATOM   3400  CG2 THR A 534     -54.381  25.050  23.195  1.00 63.55           C  
ANISOU 3400  CG2 THR A 534     5510  11351   7285    797    765  -2078       C  
ATOM   3401  N   TRP A 535     -56.479  22.384  19.681  1.00 66.22           N  
ANISOU 3401  N   TRP A 535     5945  11292   7925    310    804  -1348       N  
ATOM   3402  CA  TRP A 535     -57.416  22.027  18.608  1.00 65.87           C  
ANISOU 3402  CA  TRP A 535     5879  11148   8000    220    790  -1226       C  
ATOM   3403  C   TRP A 535     -58.610  21.253  19.175  1.00 72.35           C  
ANISOU 3403  C   TRP A 535     6546  12239   8706    161    883  -1092       C  
ATOM   3404  O   TRP A 535     -59.726  21.335  18.661  1.00 71.72           O  
ANISOU 3404  O   TRP A 535     6371  12180   8699    147    886  -1065       O  
ATOM   3405  CB  TRP A 535     -56.701  21.181  17.536  1.00 62.58           C  
ANISOU 3405  CB  TRP A 535     5630  10472   7677     80    734  -1066       C  
ATOM   3406  CG  TRP A 535     -57.615  20.703  16.449  1.00 63.17           C  
ANISOU 3406  CG  TRP A 535     5685  10456   7860    -17    712   -944       C  
ATOM   3407  CD1 TRP A 535     -58.305  19.528  16.420  1.00 66.41           C  
ANISOU 3407  CD1 TRP A 535     6050  10944   8238   -145    748   -758       C  
ATOM   3408  CD2 TRP A 535     -58.047  21.453  15.307  1.00 62.76           C  
ANISOU 3408  CD2 TRP A 535     5635  10240   7969     12    642  -1002       C  
ATOM   3409  NE1 TRP A 535     -59.115  19.484  15.313  1.00 65.80           N  
ANISOU 3409  NE1 TRP A 535     5953  10757   8289   -196    703   -714       N  
ATOM   3410  CE2 TRP A 535     -58.979  20.653  14.611  1.00 66.57           C  
ANISOU 3410  CE2 TRP A 535     6080  10716   8497   -100    641   -858       C  
ATOM   3411  CE3 TRP A 535     -57.708  22.713  14.780  1.00 63.94           C  
ANISOU 3411  CE3 TRP A 535     5813  10238   8241    117    569  -1149       C  
ATOM   3412  CZ2 TRP A 535     -59.576  21.067  13.414  1.00 65.71           C  
ANISOU 3412  CZ2 TRP A 535     5963  10475   8529   -104    575   -864       C  
ATOM   3413  CZ3 TRP A 535     -58.298  23.119  13.591  1.00 65.26           C  
ANISOU 3413  CZ3 TRP A 535     5970  10271   8556    108    506  -1134       C  
ATOM   3414  CH2 TRP A 535     -59.243  22.313  12.937  1.00 65.92           C  
ANISOU 3414  CH2 TRP A 535     6014  10375   8658      3    513   -998       C  
ATOM   3415  N   VAL A 536     -58.347  20.491  20.228  1.00 71.65           N  
ANISOU 3415  N   VAL A 536     6425  12358   8440    123    954   -994       N  
ATOM   3416  CA  VAL A 536     -59.302  19.643  20.906  1.00 73.74           C  
ANISOU 3416  CA  VAL A 536     6537  12902   8579     52   1044   -824       C  
ATOM   3417  C   VAL A 536     -59.968  20.422  22.093  1.00 80.51           C  
ANISOU 3417  C   VAL A 536     7199  14117   9274    210   1123   -982       C  
ATOM   3418  O   VAL A 536     -60.916  19.914  22.680  1.00 81.77           O  
ANISOU 3418  O   VAL A 536     7191  14553   9323    175   1206   -861       O  
ATOM   3419  CB  VAL A 536     -58.534  18.339  21.291  1.00 77.55           C  
ANISOU 3419  CB  VAL A 536     7097  13391   8978    -85   1063   -602       C  
ATOM   3420  CG1 VAL A 536     -58.622  17.972  22.759  1.00 79.40           C  
ANISOU 3420  CG1 VAL A 536     7194  13997   8980    -64   1161   -529       C  
ATOM   3421  CG2 VAL A 536     -58.927  17.174  20.390  1.00 76.74           C  
ANISOU 3421  CG2 VAL A 536     7035  13117   9004   -266   1028   -370       C  
ATOM   3422  N   TRP A 537     -59.551  21.676  22.382  1.00 77.40           N  
ANISOU 3422  N   TRP A 537     6813  13714   8880    385   1089  -1258       N  
ATOM   3423  CA  TRP A 537     -60.168  22.423  23.490  1.00 79.90           C  
ANISOU 3423  CA  TRP A 537     6941  14372   9044    554   1151  -1446       C  
ATOM   3424  C   TRP A 537     -61.480  23.111  23.030  1.00 84.84           C  
ANISOU 3424  C   TRP A 537     7426  15034   9773    627   1151  -1542       C  
ATOM   3425  O   TRP A 537     -61.509  24.326  22.795  1.00 84.14           O  
ANISOU 3425  O   TRP A 537     7329  14837   9801    776   1084  -1791       O  
ATOM   3426  CB  TRP A 537     -59.193  23.440  24.127  1.00 78.73           C  
ANISOU 3426  CB  TRP A 537     6842  14213   8859    721   1102  -1723       C  
ATOM   3427  CG  TRP A 537     -57.928  22.883  24.728  1.00 78.88           C  
ANISOU 3427  CG  TRP A 537     6974  14243   8754    676   1106  -1658       C  
ATOM   3428  CD1 TRP A 537     -57.417  21.624  24.580  1.00 80.64           C  
ANISOU 3428  CD1 TRP A 537     7295  14404   8942    500   1127  -1384       C  
ATOM   3429  CD2 TRP A 537     -56.978  23.610  25.519  1.00 79.16           C  
ANISOU 3429  CD2 TRP A 537     7039  14329   8707    812   1070  -1882       C  
ATOM   3430  NE1 TRP A 537     -56.213  21.520  25.237  1.00 79.73           N  
ANISOU 3430  NE1 TRP A 537     7267  14308   8720    520   1114  -1415       N  
ATOM   3431  CE2 TRP A 537     -55.911  22.728  25.809  1.00 82.01           C  
ANISOU 3431  CE2 TRP A 537     7518  14666   8976    707   1079  -1719       C  
ATOM   3432  CE3 TRP A 537     -56.923  24.927  26.012  1.00 81.43           C  
ANISOU 3432  CE3 TRP A 537     7260  14672   9006   1018   1020  -2217       C  
ATOM   3433  CZ2 TRP A 537     -54.810  23.117  26.578  1.00 81.39           C  
ANISOU 3433  CZ2 TRP A 537     7491  14633   8801    796   1047  -1870       C  
ATOM   3434  CZ3 TRP A 537     -55.828  25.312  26.768  1.00 83.04           C  
ANISOU 3434  CZ3 TRP A 537     7517  14911   9124   1105    980  -2378       C  
ATOM   3435  CH2 TRP A 537     -54.789  24.413  27.048  1.00 82.73           C  
ANISOU 3435  CH2 TRP A 537     7594  14862   8979    993    997  -2201       C  
ATOM   3436  N   THR A 538     -62.556  22.300  22.885  1.00 81.97           N  
ANISOU 3436  N   THR A 538     6948  14813   9384    515   1216  -1330       N  
ATOM   3437  CA  THR A 538     -63.909  22.708  22.466  1.00 82.53           C  
ANISOU 3437  CA  THR A 538     6867  14953   9537    556   1228  -1365       C  
ATOM   3438  C   THR A 538     -64.950  22.046  23.364  1.00 89.27           C  
ANISOU 3438  C   THR A 538     7496  16228  10195    528   1353  -1219       C  
ATOM   3439  O   THR A 538     -64.593  21.173  24.163  1.00 89.68           O  
ANISOU 3439  O   THR A 538     7526  16481  10067    454   1421  -1057       O  
ATOM   3440  CB  THR A 538     -64.201  22.324  20.991  1.00 85.87           C  
ANISOU 3440  CB  THR A 538     7391  15048  10188    412   1154  -1218       C  
ATOM   3441  OG1 THR A 538     -64.331  20.904  20.887  1.00 81.77           O  
ANISOU 3441  OG1 THR A 538     6896  14540   9634    209   1188   -919       O  
ATOM   3442  CG2 THR A 538     -63.173  22.859  19.995  1.00 84.43           C  
ANISOU 3442  CG2 THR A 538     7416  14469  10194    427   1034  -1323       C  
ATOM   3443  N   LYS A 539     -66.245  22.409  23.183  1.00 87.21           N  
ANISOU 3443  N   LYS A 539     7061  16100   9976    577   1381  -1252       N  
ATOM   3444  CA  LYS A 539     -67.359  21.828  23.935  1.00 89.49           C  
ANISOU 3444  CA  LYS A 539     7109  16798  10095    548   1499  -1101       C  
ATOM   3445  C   LYS A 539     -67.555  20.357  23.539  1.00 92.54           C  
ANISOU 3445  C   LYS A 539     7517  17128  10514    294   1516   -728       C  
ATOM   3446  O   LYS A 539     -67.831  19.526  24.405  1.00 93.48           O  
ANISOU 3446  O   LYS A 539     7499  17562  10456    219   1610   -522       O  
ATOM   3447  CB  LYS A 539     -68.652  22.635  23.719  1.00 93.65           C  
ANISOU 3447  CB  LYS A 539     7452  17445  10687    672   1510  -1246       C  
ATOM   3448  N   ALA A 540     -67.356  20.032  22.242  1.00 87.19           N  
ANISOU 3448  N   ALA A 540     7011  16051  10067    164   1417   -641       N  
ATOM   3449  CA  ALA A 540     -67.476  18.675  21.691  1.00 86.67           C  
ANISOU 3449  CA  ALA A 540     6992  15855  10086    -72   1397   -326       C  
ATOM   3450  C   ALA A 540     -66.545  17.660  22.396  1.00 90.36           C  
ANISOU 3450  C   ALA A 540     7530  16372  10430   -182   1424   -135       C  
ATOM   3451  O   ALA A 540     -66.906  16.488  22.496  1.00 91.27           O  
ANISOU 3451  O   ALA A 540     7581  16550  10547   -356   1445    152       O  
ATOM   3452  CB  ALA A 540     -67.191  18.691  20.199  1.00 85.20           C  
ANISOU 3452  CB  ALA A 540     6995  15230  10145   -145   1272   -344       C  
ATOM   3453  N   THR A 541     -65.382  18.117  22.911  1.00 85.50           N  
ANISOU 3453  N   THR A 541     7034  15732   9721    -80   1418   -288       N  
ATOM   3454  CA  THR A 541     -64.405  17.298  23.643  1.00 85.28           C  
ANISOU 3454  CA  THR A 541     7077  15760   9566   -155   1440   -139       C  
ATOM   3455  C   THR A 541     -64.979  16.892  25.007  1.00 91.88           C  
ANISOU 3455  C   THR A 541     7680  17077  10152   -148   1565      3       C  
ATOM   3456  O   THR A 541     -64.814  15.736  25.406  1.00 91.39           O  
ANISOU 3456  O   THR A 541     7597  17089  10036   -301   1589    290       O  
ATOM   3457  CB  THR A 541     -63.083  18.054  23.745  1.00 90.03           C  
ANISOU 3457  CB  THR A 541     7855  16204  10148    -30   1391   -374       C  
ATOM   3458  OG1 THR A 541     -62.547  18.145  22.424  1.00 86.49           O  
ANISOU 3458  OG1 THR A 541     7612  15321   9928    -86   1279   -413       O  
ATOM   3459  CG2 THR A 541     -62.062  17.393  24.688  1.00 85.70           C  
ANISOU 3459  CG2 THR A 541     7355  15778   9430    -64   1424   -265       C  
ATOM   3460  N   LEU A 542     -65.672  17.828  25.699  1.00 91.47           N  
ANISOU 3460  N   LEU A 542     7444  17356   9954     31   1639   -190       N  
ATOM   3461  CA  LEU A 542     -66.365  17.567  26.974  1.00 94.85           C  
ANISOU 3461  CA  LEU A 542     7614  18305  10121     64   1768    -76       C  
ATOM   3462  C   LEU A 542     -67.407  16.466  26.772  1.00101.35           C  
ANISOU 3462  C   LEU A 542     8290  19219  11000   -135   1804    275       C  
ATOM   3463  O   LEU A 542     -67.538  15.584  27.619  1.00102.35           O  
ANISOU 3463  O   LEU A 542     8283  19635  10970   -233   1877    547       O  
ATOM   3464  CB  LEU A 542     -67.050  18.845  27.521  1.00 96.46           C  
ANISOU 3464  CB  LEU A 542     7644  18812  10197    309   1825   -390       C  
ATOM   3465  CG  LEU A 542     -66.252  19.808  28.417  1.00101.70           C  
ANISOU 3465  CG  LEU A 542     8325  19636  10679    530   1834   -704       C  
ATOM   3466  CD1 LEU A 542     -65.856  19.165  29.748  1.00103.89           C  
ANISOU 3466  CD1 LEU A 542     8508  20305  10660    513   1925   -545       C  
ATOM   3467  CD2 LEU A 542     -65.084  20.464  27.683  1.00100.35           C  
ANISOU 3467  CD2 LEU A 542     8424  19008  10697    582   1707   -931       C  
ATOM   3468  N   LEU A 543     -68.108  16.506  25.612  1.00 98.67           N  
ANISOU 3468  N   LEU A 543     7978  18615  10897   -202   1739    279       N  
ATOM   3469  CA  LEU A 543     -69.124  15.533  25.200  1.00100.05           C  
ANISOU 3469  CA  LEU A 543     8030  18800  11185   -396   1742    583       C  
ATOM   3470  C   LEU A 543     -68.484  14.171  24.901  1.00103.91           C  
ANISOU 3470  C   LEU A 543     8653  19036  11790   -626   1675    883       C  
ATOM   3471  O   LEU A 543     -69.071  13.141  25.243  1.00105.21           O  
ANISOU 3471  O   LEU A 543     8670  19353  11952   -792   1705   1206       O  
ATOM   3472  CB  LEU A 543     -69.908  16.045  23.964  1.00 99.09           C  
ANISOU 3472  CB  LEU A 543     7927  18433  11291   -385   1672    459       C  
ATOM   3473  CG  LEU A 543     -71.215  16.846  24.193  1.00105.42           C  
ANISOU 3473  CG  LEU A 543     8483  19542  12029   -253   1746    338       C  
ATOM   3474  CD1 LEU A 543     -72.260  16.039  24.962  1.00107.85           C  
ANISOU 3474  CD1 LEU A 543     8511  20254  12213   -361   1849    637       C  
ATOM   3475  CD2 LEU A 543     -70.959  18.217  24.832  1.00108.30           C  
ANISOU 3475  CD2 LEU A 543     8816  20093  12240     19   1789    -22       C  
ATOM   3476  N   ILE A 544     -67.280  14.173  24.279  1.00 98.20           N  
ANISOU 3476  N   ILE A 544     8199  17932  11181   -633   1578    778       N  
ATOM   3477  CA  ILE A 544     -66.516  12.964  23.956  1.00 97.22           C  
ANISOU 3477  CA  ILE A 544     8225  17534  11179   -821   1499   1009       C  
ATOM   3478  C   ILE A 544     -66.108  12.260  25.261  1.00104.05           C  
ANISOU 3478  C   ILE A 544     8999  18694  11840   -869   1573   1232       C  
ATOM   3479  O   ILE A 544     -66.312  11.050  25.379  1.00104.73           O  
ANISOU 3479  O   ILE A 544     9024  18775  11993  -1060   1555   1561       O  
ATOM   3480  CB  ILE A 544     -65.289  13.289  23.039  1.00 97.21           C  
ANISOU 3480  CB  ILE A 544     8518  17100  11318   -782   1389    807       C  
ATOM   3481  CG1 ILE A 544     -65.740  13.457  21.573  1.00 96.02           C  
ANISOU 3481  CG1 ILE A 544     8452  16620  11412   -822   1291    725       C  
ATOM   3482  CG2 ILE A 544     -64.175  12.224  23.144  1.00 96.73           C  
ANISOU 3482  CG2 ILE A 544     8608  16853  11292   -908   1333    986       C  
ATOM   3483  CD1 ILE A 544     -64.884  14.377  20.732  1.00 99.52           C  
ANISOU 3483  CD1 ILE A 544     9110  16759  11944   -706   1215    446       C  
ATOM   3484  N   TRP A 545     -65.571  13.021  26.241  1.00101.58           N  
ANISOU 3484  N   TRP A 545     8664  18645  11286   -697   1649   1058       N  
ATOM   3485  CA  TRP A 545     -65.109  12.451  27.502  1.00103.33           C  
ANISOU 3485  CA  TRP A 545     8801  19175  11286   -721   1719   1249       C  
ATOM   3486  C   TRP A 545     -66.248  12.055  28.434  1.00112.11           C  
ANISOU 3486  C   TRP A 545     9602  20773  12222   -764   1835   1493       C  
ATOM   3487  O   TRP A 545     -66.075  11.084  29.170  1.00113.37           O  
ANISOU 3487  O   TRP A 545     9677  21113  12286   -884   1866   1802       O  
ATOM   3488  CB  TRP A 545     -64.107  13.366  28.209  1.00101.37           C  
ANISOU 3488  CB  TRP A 545     8634  19043  10837   -522   1747    970       C  
ATOM   3489  CG  TRP A 545     -62.763  13.353  27.536  1.00 99.37           C  
ANISOU 3489  CG  TRP A 545     8670  18355  10729   -533   1638    857       C  
ATOM   3490  CD1 TRP A 545     -62.184  14.379  26.849  1.00100.21           C  
ANISOU 3490  CD1 TRP A 545     8950  18196  10929   -400   1575    528       C  
ATOM   3491  CD2 TRP A 545     -61.892  12.221  27.375  1.00 98.16           C  
ANISOU 3491  CD2 TRP A 545     8658  17968  10670   -694   1571   1090       C  
ATOM   3492  NE1 TRP A 545     -60.981  13.974  26.316  1.00 97.70           N  
ANISOU 3492  NE1 TRP A 545     8865  17525  10732   -465   1484    541       N  
ATOM   3493  CE2 TRP A 545     -60.776  12.654  26.624  1.00 99.63           C  
ANISOU 3493  CE2 TRP A 545     9098  17778  10979   -637   1479    871       C  
ATOM   3494  CE3 TRP A 545     -61.932  10.887  27.817  1.00100.57           C  
ANISOU 3494  CE3 TRP A 545     8889  18346  10976   -877   1573   1470       C  
ATOM   3495  CZ2 TRP A 545     -59.707  11.805  26.314  1.00 97.50           C  
ANISOU 3495  CZ2 TRP A 545     9007  17222  10815   -746   1398    999       C  
ATOM   3496  CZ3 TRP A 545     -60.880  10.043  27.497  1.00100.79           C  
ANISOU 3496  CZ3 TRP A 545     9103  18062  11132   -987   1481   1595       C  
ATOM   3497  CH2 TRP A 545     -59.781  10.503  26.758  1.00 98.85           C  
ANISOU 3497  CH2 TRP A 545     9106  17460  10990   -915   1398   1351       C  
ATOM   3498  N   ARG A 546     -67.410  12.755  28.386  1.00110.74           N  
ANISOU 3498  N   ARG A 546     9249  20811  12014   -675   1896   1377       N  
ATOM   3499  CA  ARG A 546     -68.582  12.404  29.198  1.00114.02           C  
ANISOU 3499  CA  ARG A 546     9347  21708  12267   -714   2011   1611       C  
ATOM   3500  C   ARG A 546     -69.125  11.044  28.746  1.00119.64           C  
ANISOU 3500  C   ARG A 546     9998  22274  13185   -988   1960   2025       C  
ATOM   3501  O   ARG A 546     -69.363  10.175  29.584  1.00121.35           O  
ANISOU 3501  O   ARG A 546    10030  22791  13286  -1107   2019   2370       O  
ATOM   3502  CB  ARG A 546     -69.669  13.488  29.114  1.00114.89           C  
ANISOU 3502  CB  ARG A 546     9294  22039  12322   -544   2074   1361       C  
ATOM   3503  N   ARG A 547     -69.242  10.844  27.412  1.00115.55           N  
ANISOU 3503  N   ARG A 547     9639  21284  12979  -1089   1838   1993       N  
ATOM   3504  CA  ARG A 547     -69.690   9.598  26.781  1.00116.46           C  
ANISOU 3504  CA  ARG A 547     9735  21168  13348  -1343   1751   2326       C  
ATOM   3505  C   ARG A 547     -68.627   8.483  26.920  1.00122.27           C  
ANISOU 3505  C   ARG A 547    10610  21689  14159  -1495   1674   2564       C  
ATOM   3506  O   ARG A 547     -68.973   7.305  26.812  1.00123.31           O  
ANISOU 3506  O   ARG A 547    10659  21750  14445  -1710   1620   2915       O  
ATOM   3507  CB  ARG A 547     -70.039   9.829  25.304  1.00114.49           C  
ANISOU 3507  CB  ARG A 547     9626  20489  13384  -1371   1635   2160       C  
ATOM   3508  N   THR A 548     -67.346   8.852  27.157  1.00118.77           N  
ANISOU 3508  N   THR A 548    10369  21136  13623  -1384   1661   2376       N  
ATOM   3509  CA  THR A 548     -66.245   7.905  27.373  1.00118.67           C  
ANISOU 3509  CA  THR A 548    10492  20939  13657  -1494   1593   2564       C  
ATOM   3510  C   THR A 548     -66.185   7.521  28.862  1.00126.80           C  
ANISOU 3510  C   THR A 548    11324  22440  14413  -1505   1702   2821       C  
ATOM   3511  O   THR A 548     -65.712   6.432  29.193  1.00127.25           O  
ANISOU 3511  O   THR A 548    11387  22431  14529  -1660   1654   3131       O  
ATOM   3512  CB  THR A 548     -64.916   8.479  26.873  1.00120.92           C  
ANISOU 3512  CB  THR A 548    11071  20905  13968  -1371   1529   2251       C  
ATOM   3513  N   TRP A 549     -66.709   8.402  29.749  1.00126.15           N  
ANISOU 3513  N   TRP A 549    11052  22846  14035  -1338   1844   2697       N  
ATOM   3514  CA  TRP A 549     -66.797   8.214  31.205  1.00129.53           C  
ANISOU 3514  CA  TRP A 549    11252  23820  14145  -1313   1968   2906       C  
ATOM   3515  C   TRP A 549     -67.959   7.221  31.536  1.00136.34           C  
ANISOU 3515  C   TRP A 549    11829  24928  15045  -1515   2004   3358       C  
ATOM   3516  O   TRP A 549     -68.415   7.144  32.679  1.00139.16           O  
ANISOU 3516  O   TRP A 549    11927  25818  15131  -1497   2127   3556       O  
ATOM   3517  CB  TRP A 549     -66.984   9.594  31.886  1.00129.34           C  
ANISOU 3517  CB  TRP A 549    11128  24206  13811  -1041   2091   2551       C  
ATOM   3518  CG  TRP A 549     -66.918   9.616  33.389  1.00133.47           C  
ANISOU 3518  CG  TRP A 549    11436  25320  13956   -960   2220   2670       C  
ATOM   3519  CD1 TRP A 549     -67.953   9.838  34.249  1.00139.52           C  
ANISOU 3519  CD1 TRP A 549    11885  26658  14470   -897   2356   2759       C  
ATOM   3520  CD2 TRP A 549     -65.744   9.472  34.202  1.00133.55           C  
ANISOU 3520  CD2 TRP A 549    11527  25436  13780   -915   2224   2692       C  
ATOM   3521  NE1 TRP A 549     -67.506   9.804  35.549  1.00141.19           N  
ANISOU 3521  NE1 TRP A 549    11969  27338  14339   -819   2446   2844       N  
ATOM   3522  CE2 TRP A 549     -66.152   9.587  35.551  1.00140.84           C  
ANISOU 3522  CE2 TRP A 549    12167  27014  14330   -830   2365   2805       C  
ATOM   3523  CE3 TRP A 549     -64.385   9.242  33.924  1.00132.68           C  
ANISOU 3523  CE3 TRP A 549    11693  24945  13775   -937   2122   2631       C  
ATOM   3524  CZ2 TRP A 549     -65.251   9.484  36.619  1.00141.28           C  
ANISOU 3524  CZ2 TRP A 549    12211  27353  14115   -768   2402   2857       C  
ATOM   3525  CZ3 TRP A 549     -63.493   9.139  34.983  1.00135.24           C  
ANISOU 3525  CZ3 TRP A 549    12007  25533  13846   -880   2158   2686       C  
ATOM   3526  CH2 TRP A 549     -63.927   9.259  36.311  1.00139.18           C  
ANISOU 3526  CH2 TRP A 549    12226  26683  13974   -797   2294   2798       C  
ATOM   3527  N   CYS A 550     -68.393   6.434  30.516  1.00131.76           N  
ANISOU 3527  N   CYS A 550    11297  23954  14811  -1711   1888   3525       N  
ATOM   3528  CA  CYS A 550     -69.441   5.405  30.531  1.00151.73           C  
ANISOU 3528  CA  CYS A 550    13598  26567  17486  -1937   1873   3948       C  
ATOM   3529  C   CYS A 550     -70.784   6.009  30.928  1.00160.17           C  
ANISOU 3529  C   CYS A 550    14373  28105  18380  -1860   2008   3937       C  
ATOM   3530  O   CYS A 550     -71.332   6.812  30.175  1.00113.48           O  
ANISOU 3530  O   CYS A 550     8495  22073  12548  -1765   2002   3652       O  
ATOM   3531  CB  CYS A 550     -69.063   4.229  31.431  1.00154.26           C  
ANISOU 3531  CB  CYS A 550    13808  27036  17766  -2107   1866   4404       C  
ATOM   3532  SG  CYS A 550     -67.420   3.533  31.097  1.00155.80           S  
ANISOU 3532  SG  CYS A 550    14333  26710  18152  -2179   1710   4417       S  
TER    3533      CYS A 550                                                      
ATOM   3534  N   THR B   0      16.234  25.634 -26.971  1.00 95.90           N  
ANISOU 3534  N   THR B   0    10508  13826  12103      6   2180    805       N  
ATOM   3535  CA  THR B   0      17.646  26.002 -27.101  1.00 97.60           C  
ANISOU 3535  CA  THR B   0    10445  14023  12616      4   2428    760       C  
ATOM   3536  C   THR B   0      18.314  25.988 -25.716  1.00 99.30           C  
ANISOU 3536  C   THR B   0    10317  14224  13190     82   2207    724       C  
ATOM   3537  O   THR B   0      19.375  25.378 -25.565  1.00100.91           O  
ANISOU 3537  O   THR B   0    10280  14390  13674    187   2297    619       O  
ATOM   3538  CB  THR B   0      17.809  27.355 -27.814  1.00108.08           C  
ANISOU 3538  CB  THR B   0    11819  15360  13885   -157   2627    854       C  
ATOM   3539  OG1 THR B   0      17.127  28.369 -27.077  1.00106.00           O  
ANISOU 3539  OG1 THR B   0    11552  15119  13602   -229   2361    962       O  
ATOM   3540  CG2 THR B   0      17.307  27.326 -29.256  1.00109.15           C  
ANISOU 3540  CG2 THR B   0    12335  15483  13651   -223   2850    886       C  
ATOM   3541  N   ALA B   1      17.683  26.639 -24.710  1.00 91.74           N  
ANISOU 3541  N   ALA B   1     9352  13283  12223     39   1910    804       N  
ATOM   3542  CA  ALA B   1      18.175  26.673 -23.331  1.00 90.19           C  
ANISOU 3542  CA  ALA B   1     8913  13057  12298    102   1645    780       C  
ATOM   3543  C   ALA B   1      17.452  25.622 -22.487  1.00 90.27           C  
ANISOU 3543  C   ALA B   1     9067  13037  12193    211   1373    761       C  
ATOM   3544  O   ALA B   1      16.365  25.175 -22.864  1.00 88.56           O  
ANISOU 3544  O   ALA B   1     9119  12838  11693    194   1362    788       O  
ATOM   3545  CB  ALA B   1      17.985  28.058 -22.734  1.00 89.90           C  
ANISOU 3545  CB  ALA B   1     8822  13033  12302    -21   1517    871       C  
ATOM   3546  N   ASP B   2      18.059  25.212 -21.362  1.00 85.74           N  
ANISOU 3546  N   ASP B   2     8328  12405  11845    317   1149    712       N  
ATOM   3547  CA  ASP B   2      17.482  24.209 -20.462  1.00 83.72           C  
ANISOU 3547  CA  ASP B   2     8237  12089  11484    416    900    700       C  
ATOM   3548  C   ASP B   2      16.303  24.800 -19.671  1.00 82.10           C  
ANISOU 3548  C   ASP B   2     8224  11898  11072    323    706    790       C  
ATOM   3549  O   ASP B   2      16.323  25.980 -19.319  1.00 80.97           O  
ANISOU 3549  O   ASP B   2     8004  11780  10981    232    653    844       O  
ATOM   3550  CB  ASP B   2      18.551  23.613 -19.521  1.00 87.67           C  
ANISOU 3550  CB  ASP B   2     8539  12496  12275    570    698    625       C  
ATOM   3551  CG  ASP B   2      19.360  24.627 -18.730  1.00101.84           C  
ANISOU 3551  CG  ASP B   2    10082  14279  14332    537    531    633       C  
ATOM   3552  OD1 ASP B   2      19.176  24.697 -17.495  1.00102.32           O  
ANISOU 3552  OD1 ASP B   2    10224  14279  14374    562    222    658       O  
ATOM   3553  OD2 ASP B   2      20.199  25.333 -19.344  1.00108.96           O  
ANISOU 3553  OD2 ASP B   2    10721  15220  15458    478    717    608       O  
ATOM   3554  N   LEU B   3      15.271  23.974 -19.415  1.00 75.44           N  
ANISOU 3554  N   LEU B   3     7629  11029  10007    340    625    798       N  
ATOM   3555  CA  LEU B   3      14.044  24.348 -18.702  1.00 72.59           C  
ANISOU 3555  CA  LEU B   3     7454  10670   9455    259    490    864       C  
ATOM   3556  C   LEU B   3      14.331  25.025 -17.351  1.00 75.90           C  
ANISOU 3556  C   LEU B   3     7823  11038   9976    258    270    889       C  
ATOM   3557  O   LEU B   3      13.699  26.031 -17.031  1.00 74.55           O  
ANISOU 3557  O   LEU B   3     7698  10896   9731    163    237    947       O  
ATOM   3558  CB  LEU B   3      13.168  23.100 -18.499  1.00 71.69           C  
ANISOU 3558  CB  LEU B   3     7571  10500   9166    291    445    841       C  
ATOM   3559  CG  LEU B   3      11.827  23.274 -17.793  1.00 73.71           C  
ANISOU 3559  CG  LEU B   3     8015  10746   9244    203    355    888       C  
ATOM   3560  CD1 LEU B   3      10.835  24.044 -18.650  1.00 72.06           C  
ANISOU 3560  CD1 LEU B   3     7830  10637   8912     88    463    931       C  
ATOM   3561  CD2 LEU B   3      11.258  21.929 -17.412  1.00 76.14           C  
ANISOU 3561  CD2 LEU B   3     8528  10963   9440    235    313    853       C  
ATOM   3562  N   GLU B   4      15.298  24.488 -16.591  1.00 73.58           N  
ANISOU 3562  N   GLU B   4     7445  10657   9856    373    108    840       N  
ATOM   3563  CA  GLU B   4      15.732  24.991 -15.282  1.00 73.88           C  
ANISOU 3563  CA  GLU B   4     7463  10620   9990    391   -150    848       C  
ATOM   3564  C   GLU B   4      16.250  26.429 -15.403  1.00 75.68           C  
ANISOU 3564  C   GLU B   4     7481  10902  10374    297   -129    869       C  
ATOM   3565  O   GLU B   4      15.928  27.267 -14.558  1.00 74.71           O  
ANISOU 3565  O   GLU B   4     7437  10749  10200    232   -269    904       O  
ATOM   3566  CB  GLU B   4      16.807  24.071 -14.667  1.00 77.75           C  
ANISOU 3566  CB  GLU B   4     7878  10996  10665    555   -350    781       C  
ATOM   3567  CG  GLU B   4      16.352  22.635 -14.408  1.00 92.37           C  
ANISOU 3567  CG  GLU B   4     9981  12753  12362    653   -401    766       C  
ATOM   3568  CD  GLU B   4      16.188  21.719 -15.612  1.00117.28           C  
ANISOU 3568  CD  GLU B   4    13137  15943  15480    692   -165    727       C  
ATOM   3569  OE1 GLU B   4      16.965  21.851 -16.586  1.00110.35           O  
ANISOU 3569  OE1 GLU B   4    12013  15126  14788    723      4    678       O  
ATOM   3570  OE2 GLU B   4      15.274  20.863 -15.579  1.00113.76           O  
ANISOU 3570  OE2 GLU B   4    12954  15452  14817    681   -136    738       O  
ATOM   3571  N   ASP B   5      17.011  26.720 -16.475  1.00 71.51           N  
ANISOU 3571  N   ASP B   5     6711  10439  10022    278     72    845       N  
ATOM   3572  CA  ASP B   5      17.528  28.061 -16.751  1.00 71.10           C  
ANISOU 3572  CA  ASP B   5     6463  10425  10126    165    144    867       C  
ATOM   3573  C   ASP B   5      16.394  28.983 -17.156  1.00 69.51           C  
ANISOU 3573  C   ASP B   5     6433  10284   9696     35    261    955       C  
ATOM   3574  O   ASP B   5      16.311  30.094 -16.644  1.00 68.72           O  
ANISOU 3574  O   ASP B   5     6325  10165   9621    -50    177    992       O  
ATOM   3575  CB  ASP B   5      18.613  28.027 -17.836  1.00 75.34           C  
ANISOU 3575  CB  ASP B   5     6723  10999  10904    171    385    815       C  
ATOM   3576  CG  ASP B   5      20.021  27.980 -17.296  1.00 91.38           C  
ANISOU 3576  CG  ASP B   5     8434  12970  13318    243    243    730       C  
ATOM   3577  OD1 ASP B   5      20.917  28.567 -17.935  1.00 95.39           O  
ANISOU 3577  OD1 ASP B   5     8662  13501  14080    178    430    698       O  
ATOM   3578  OD2 ASP B   5      20.226  27.371 -16.218  1.00 98.44           O  
ANISOU 3578  OD2 ASP B   5     9358  13780  14263    361    -60    693       O  
ATOM   3579  N   ASN B   6      15.490  28.504 -18.025  1.00 63.50           N  
ANISOU 3579  N   ASN B   6     5834   9577   8715     27    425    981       N  
ATOM   3580  CA  ASN B   6      14.314  29.256 -18.465  1.00 61.73           C  
ANISOU 3580  CA  ASN B   6     5773   9401   8280    -69    500   1058       C  
ATOM   3581  C   ASN B   6      13.455  29.658 -17.268  1.00 64.84           C  
ANISOU 3581  C   ASN B   6     6307   9753   8576    -87    309   1085       C  
ATOM   3582  O   ASN B   6      12.991  30.792 -17.216  1.00 65.06           O  
ANISOU 3582  O   ASN B   6     6366   9786   8568   -164    312   1139       O  
ATOM   3583  CB  ASN B   6      13.493  28.448 -19.470  1.00 59.95           C  
ANISOU 3583  CB  ASN B   6     5703   9224   7851    -56    635   1060       C  
ATOM   3584  CG  ASN B   6      14.125  28.317 -20.832  1.00 74.52           C  
ANISOU 3584  CG  ASN B   6     7492  11108   9717    -65    875   1045       C  
ATOM   3585  OD1 ASN B   6      14.562  29.302 -21.436  1.00 64.32           O  
ANISOU 3585  OD1 ASN B   6     6130   9831   8476   -145   1011   1086       O  
ATOM   3586  ND2 ASN B   6      14.138  27.097 -21.371  1.00 67.31           N  
ANISOU 3586  ND2 ASN B   6     6643  10192   8738      7    953    985       N  
ATOM   3587  N   TRP B   7      13.293  28.743 -16.286  1.00 60.85           N  
ANISOU 3587  N   TRP B   7     5903   9187   8029    -13    157   1047       N  
ATOM   3588  CA  TRP B   7      12.544  28.956 -15.040  1.00 59.29           C  
ANISOU 3588  CA  TRP B   7     5880   8926   7722    -27      7   1059       C  
ATOM   3589  C   TRP B   7      13.215  30.028 -14.185  1.00 63.92           C  
ANISOU 3589  C   TRP B   7     6401   9454   8432    -58   -140   1060       C  
ATOM   3590  O   TRP B   7      12.519  30.875 -13.625  1.00 63.66           O  
ANISOU 3590  O   TRP B   7     6483   9394   8312   -114   -171   1086       O  
ATOM   3591  CB  TRP B   7      12.433  27.644 -14.243  1.00 57.60           C  
ANISOU 3591  CB  TRP B   7     5822   8633   7430     55   -103   1020       C  
ATOM   3592  CG  TRP B   7      11.356  27.644 -13.195  1.00 57.44           C  
ANISOU 3592  CG  TRP B   7     6042   8547   7233     20   -162   1034       C  
ATOM   3593  CD1 TRP B   7      11.528  27.582 -11.845  1.00 60.88           C  
ANISOU 3593  CD1 TRP B   7     6639   8865   7627     44   -339   1021       C  
ATOM   3594  CD2 TRP B   7       9.938  27.657 -13.418  1.00 55.89           C  
ANISOU 3594  CD2 TRP B   7     5961   8387   6887    -47    -30   1054       C  
ATOM   3595  NE1 TRP B   7      10.307  27.568 -11.212  1.00 59.18           N  
ANISOU 3595  NE1 TRP B   7     6648   8608   7228    -12   -279   1033       N  
ATOM   3596  CE2 TRP B   7       9.314  27.610 -12.154  1.00 59.32           C  
ANISOU 3596  CE2 TRP B   7     6610   8724   7206    -68    -89   1049       C  
ATOM   3597  CE3 TRP B   7       9.133  27.698 -14.566  1.00 56.72           C  
ANISOU 3597  CE3 TRP B   7     6012   8588   6949    -92    121   1070       C  
ATOM   3598  CZ2 TRP B   7       7.923  27.580 -12.002  1.00 58.17           C  
ANISOU 3598  CZ2 TRP B   7     6579   8579   6943   -135     36   1051       C  
ATOM   3599  CZ3 TRP B   7       7.755  27.711 -14.414  1.00 57.86           C  
ANISOU 3599  CZ3 TRP B   7     6256   8737   6990   -151    189   1074       C  
ATOM   3600  CH2 TRP B   7       7.164  27.622 -13.142  1.00 58.40           C  
ANISOU 3600  CH2 TRP B   7     6494   8713   6984   -173    165   1059       C  
ATOM   3601  N   GLU B   8      14.563  30.000 -14.102  1.00 60.88           N  
ANISOU 3601  N   GLU B   8     5821   9042   8269    -21   -229   1019       N  
ATOM   3602  CA  GLU B   8      15.330  30.983 -13.349  1.00 61.39           C  
ANISOU 3602  CA  GLU B   8     5793   9043   8491    -62   -397   1004       C  
ATOM   3603  C   GLU B   8      15.281  32.355 -14.038  1.00 65.63           C  
ANISOU 3603  C   GLU B   8     6227   9623   9086   -184   -252   1051       C  
ATOM   3604  O   GLU B   8      15.194  33.361 -13.336  1.00 65.36           O  
ANISOU 3604  O   GLU B   8     6246   9528   9060   -247   -362   1059       O  
ATOM   3605  CB  GLU B   8      16.773  30.522 -13.123  1.00 64.71           C  
ANISOU 3605  CB  GLU B   8     5988   9418   9181     14   -550    935       C  
ATOM   3606  CG  GLU B   8      17.297  30.882 -11.738  1.00 77.47           C  
ANISOU 3606  CG  GLU B   8     7655  10914  10866     26   -880    898       C  
ATOM   3607  CD  GLU B   8      16.385  30.580 -10.556  1.00102.98           C  
ANISOU 3607  CD  GLU B   8    11257  14053  13817     60  -1040    912       C  
ATOM   3608  OE1 GLU B   8      16.097  31.522  -9.783  1.00100.88           O  
ANISOU 3608  OE1 GLU B   8    11140  13724  13465    -11  -1144    919       O  
ATOM   3609  OE2 GLU B   8      15.934  29.418 -10.420  1.00 95.61           O  
ANISOU 3609  OE2 GLU B   8    10487  13100  12742    147  -1035    913       O  
ATOM   3610  N   THR B   9      15.256  32.392 -15.398  1.00 61.94           N  
ANISOU 3610  N   THR B   9     5664   9243   8628   -218     -5   1084       N  
ATOM   3611  CA  THR B   9      15.112  33.627 -16.183  1.00 61.79           C  
ANISOU 3611  CA  THR B   9     5609   9248   8619   -331    154   1146       C  
ATOM   3612  C   THR B   9      13.753  34.275 -15.834  1.00 65.20           C  
ANISOU 3612  C   THR B   9     6265   9665   8843   -359    125   1201       C  
ATOM   3613  O   THR B   9      13.694  35.499 -15.668  1.00 65.60           O  
ANISOU 3613  O   THR B   9     6330   9667   8928   -435    109   1233       O  
ATOM   3614  CB  THR B   9      15.267  33.350 -17.697  1.00 66.72           C  
ANISOU 3614  CB  THR B   9     6171   9949   9230   -348    421   1171       C  
ATOM   3615  OG1 THR B   9      16.555  32.792 -17.946  1.00 70.42           O  
ANISOU 3615  OG1 THR B   9     6411  10420   9924   -312    474   1102       O  
ATOM   3616  CG2 THR B   9      15.125  34.601 -18.541  1.00 60.66           C  
ANISOU 3616  CG2 THR B   9     5419   9181   8448   -467    584   1248       C  
ATOM   3617  N   LEU B  10      12.684  33.449 -15.678  1.00 60.32           N  
ANISOU 3617  N   LEU B  10     5810   9074   8034   -296    120   1200       N  
ATOM   3618  CA  LEU B  10      11.359  33.930 -15.285  1.00 59.34           C  
ANISOU 3618  CA  LEU B  10     5859   8934   7754   -307    107   1229       C  
ATOM   3619  C   LEU B  10      11.433  34.542 -13.887  1.00 64.55           C  
ANISOU 3619  C   LEU B  10     6603   9491   8431   -319    -52   1199       C  
ATOM   3620  O   LEU B  10      10.991  35.678 -13.715  1.00 65.51           O  
ANISOU 3620  O   LEU B  10     6780   9570   8540   -363    -45   1226       O  
ATOM   3621  CB  LEU B  10      10.284  32.825 -15.347  1.00 58.48           C  
ANISOU 3621  CB  LEU B  10     5869   8864   7486   -256    143   1214       C  
ATOM   3622  CG  LEU B  10       9.971  32.223 -16.730  1.00 62.52           C  
ANISOU 3622  CG  LEU B  10     6356   9464   7934   -248    277   1235       C  
ATOM   3623  CD1 LEU B  10       9.137  30.968 -16.592  1.00 61.82           C  
ANISOU 3623  CD1 LEU B  10     6368   9390   7731   -209    275   1196       C  
ATOM   3624  CD2 LEU B  10       9.298  33.238 -17.665  1.00 63.00           C  
ANISOU 3624  CD2 LEU B  10     6439   9557   7943   -292    353   1302       C  
ATOM   3625  N   ASN B  11      12.072  33.839 -12.921  1.00 61.18           N  
ANISOU 3625  N   ASN B  11     6203   9008   8036   -274   -210   1143       N  
ATOM   3626  CA  ASN B  11      12.276  34.323 -11.550  1.00 61.80           C  
ANISOU 3626  CA  ASN B  11     6409   8969   8103   -283   -397   1105       C  
ATOM   3627  C   ASN B  11      13.048  35.656 -11.531  1.00 67.88           C  
ANISOU 3627  C   ASN B  11     7064   9690   9037   -364   -460   1107       C  
ATOM   3628  O   ASN B  11      12.579  36.615 -10.918  1.00 68.39           O  
ANISOU 3628  O   ASN B  11     7266   9678   9043   -405   -497   1105       O  
ATOM   3629  CB  ASN B  11      13.037  33.285 -10.716  1.00 62.39           C  
ANISOU 3629  CB  ASN B  11     6531   8981   8192   -210   -593   1051       C  
ATOM   3630  CG  ASN B  11      12.278  32.042 -10.327  1.00 81.35           C  
ANISOU 3630  CG  ASN B  11     9135  11370  10405   -146   -569   1044       C  
ATOM   3631  OD1 ASN B  11      11.125  31.822 -10.716  1.00 78.67           O  
ANISOU 3631  OD1 ASN B  11     8870  11082   9937   -161   -392   1069       O  
ATOM   3632  ND2 ASN B  11      12.935  31.181  -9.553  1.00 71.16           N  
ANISOU 3632  ND2 ASN B  11     7933   9996   9110    -74   -762   1007       N  
ATOM   3633  N   ASP B  12      14.209  35.711 -12.220  1.00 65.44           N  
ANISOU 3633  N   ASP B  12     6504   9416   8943   -393   -449   1103       N  
ATOM   3634  CA  ASP B  12      15.099  36.871 -12.319  1.00 67.35           C  
ANISOU 3634  CA  ASP B  12     6592   9608   9390   -496   -487   1099       C  
ATOM   3635  C   ASP B  12      14.413  38.119 -12.893  1.00 71.04           C  
ANISOU 3635  C   ASP B  12     7128  10065   9800   -579   -332   1168       C  
ATOM   3636  O   ASP B  12      14.548  39.204 -12.323  1.00 71.91           O  
ANISOU 3636  O   ASP B  12     7296  10074   9954   -650   -424   1157       O  
ATOM   3637  CB  ASP B  12      16.329  36.538 -13.193  1.00 71.10           C  
ANISOU 3637  CB  ASP B  12     6760  10138  10118   -516   -408   1082       C  
ATOM   3638  CG  ASP B  12      17.305  35.518 -12.628  1.00 89.17           C  
ANISOU 3638  CG  ASP B  12     8911  12406  12564   -429   -604   1000       C  
ATOM   3639  OD1 ASP B  12      18.304  35.207 -13.322  1.00 92.00           O  
ANISOU 3639  OD1 ASP B  12     8989  12805  13162   -430   -518    970       O  
ATOM   3640  OD2 ASP B  12      17.053  34.999 -11.510  1.00 96.81           O  
ANISOU 3640  OD2 ASP B  12    10064  13306  13414   -353   -834    965       O  
ATOM   3641  N   ASN B  13      13.708  37.971 -14.027  1.00 65.72           N  
ANISOU 3641  N   ASN B  13     6465   9478   9026   -567   -120   1235       N  
ATOM   3642  CA  ASN B  13      13.045  39.087 -14.678  1.00 65.09           C  
ANISOU 3642  CA  ASN B  13     6465   9378   8888   -622      4   1311       C  
ATOM   3643  C   ASN B  13      11.833  39.581 -13.883  1.00 67.77           C  
ANISOU 3643  C   ASN B  13     7016   9656   9077   -579    -56   1308       C  
ATOM   3644  O   ASN B  13      11.565  40.783 -13.908  1.00 68.32           O  
ANISOU 3644  O   ASN B  13     7156   9646   9158   -625    -39   1342       O  
ATOM   3645  CB  ASN B  13      12.683  38.741 -16.105  1.00 64.61           C  
ANISOU 3645  CB  ASN B  13     6386   9412   8750   -611    203   1379       C  
ATOM   3646  CG  ASN B  13      13.891  38.782 -17.010  1.00 77.59           C  
ANISOU 3646  CG  ASN B  13     7850  11078  10552   -690    339   1392       C  
ATOM   3647  OD1 ASN B  13      14.450  39.851 -17.294  1.00 71.74           O  
ANISOU 3647  OD1 ASN B  13     7065  10267   9924   -801    403   1428       O  
ATOM   3648  ND2 ASN B  13      14.352  37.617 -17.450  1.00 61.80           N  
ANISOU 3648  ND2 ASN B  13     5744   9159   8577   -639    406   1355       N  
ATOM   3649  N   LEU B  14      11.153  38.688 -13.131  1.00 62.44           N  
ANISOU 3649  N   LEU B  14     6448   8999   8275   -496   -112   1262       N  
ATOM   3650  CA  LEU B  14      10.032  39.043 -12.250  1.00 61.27           C  
ANISOU 3650  CA  LEU B  14     6494   8784   8002   -458   -128   1237       C  
ATOM   3651  C   LEU B  14      10.499  39.992 -11.128  1.00 65.27           C  
ANISOU 3651  C   LEU B  14     7105   9148   8547   -506   -266   1189       C  
ATOM   3652  O   LEU B  14       9.768  40.916 -10.764  1.00 64.33           O  
ANISOU 3652  O   LEU B  14     7116   8946   8382   -503   -234   1185       O  
ATOM   3653  CB  LEU B  14       9.380  37.782 -11.641  1.00 60.38           C  
ANISOU 3653  CB  LEU B  14     6482   8704   7756   -388   -130   1192       C  
ATOM   3654  CG  LEU B  14       8.185  37.225 -12.415  1.00 63.80           C  
ANISOU 3654  CG  LEU B  14     6904   9228   8109   -344     13   1220       C  
ATOM   3655  CD1 LEU B  14       8.019  35.734 -12.190  1.00 63.60           C  
ANISOU 3655  CD1 LEU B  14     6915   9250   8002   -307     18   1186       C  
ATOM   3656  CD2 LEU B  14       6.904  37.974 -12.077  1.00 64.42           C  
ANISOU 3656  CD2 LEU B  14     7080   9253   8142   -320     84   1211       C  
ATOM   3657  N   LYS B  15      11.726  39.764 -10.604  1.00 62.76           N  
ANISOU 3657  N   LYS B  15     6725   8792   8328   -543   -431   1143       N  
ATOM   3658  CA  LYS B  15      12.366  40.584  -9.571  1.00 64.43           C  
ANISOU 3658  CA  LYS B  15     7027   8861   8591   -602   -617   1084       C  
ATOM   3659  C   LYS B  15      12.645  41.999 -10.119  1.00 69.75           C  
ANISOU 3659  C   LYS B  15     7629   9473   9399   -702   -567   1122       C  
ATOM   3660  O   LYS B  15      12.426  42.986  -9.417  1.00 70.36           O  
ANISOU 3660  O   LYS B  15     7870   9417   9446   -737   -631   1089       O  
ATOM   3661  CB  LYS B  15      13.672  39.911  -9.108  1.00 68.13           C  
ANISOU 3661  CB  LYS B  15     7385   9318   9185   -610   -837   1028       C  
ATOM   3662  CG  LYS B  15      14.236  40.441  -7.797  1.00 88.54           C  
ANISOU 3662  CG  LYS B  15    10120  11743  11778   -653  -1105    947       C  
ATOM   3663  CD  LYS B  15      15.694  39.998  -7.601  1.00105.23           C  
ANISOU 3663  CD  LYS B  15    12024  13844  14115   -673  -1351    894       C  
ATOM   3664  CE  LYS B  15      16.721  41.076  -7.917  1.00122.78           C  
ANISOU 3664  CE  LYS B  15    14020  16014  16619   -811  -1415    876       C  
ATOM   3665  NZ  LYS B  15      16.801  41.402  -9.372  1.00131.29           N  
ANISOU 3665  NZ  LYS B  15    14854  17194  17837   -874  -1124    956       N  
ATOM   3666  N   VAL B  16      13.099  42.081 -11.386  1.00 65.91           N  
ANISOU 3666  N   VAL B  16     6934   9068   9043   -751   -434   1190       N  
ATOM   3667  CA  VAL B  16      13.419  43.325 -12.081  1.00 66.81           C  
ANISOU 3667  CA  VAL B  16     6993   9116   9277   -860   -350   1245       C  
ATOM   3668  C   VAL B  16      12.131  44.154 -12.253  1.00 70.09           C  
ANISOU 3668  C   VAL B  16     7603   9475   9552   -815   -249   1297       C  
ATOM   3669  O   VAL B  16      12.156  45.341 -11.943  1.00 70.65           O  
ANISOU 3669  O   VAL B  16     7774   9405   9666   -877   -285   1294       O  
ATOM   3670  CB  VAL B  16      14.159  43.056 -13.427  1.00 71.20           C  
ANISOU 3670  CB  VAL B  16     7323   9767   9964   -921   -186   1308       C  
ATOM   3671  CG1 VAL B  16      14.356  44.334 -14.230  1.00 72.34           C  
ANISOU 3671  CG1 VAL B  16     7471   9824  10191  -1044    -58   1384       C  
ATOM   3672  CG2 VAL B  16      15.508  42.381 -13.188  1.00 72.10           C  
ANISOU 3672  CG2 VAL B  16     7199   9911  10283   -960   -286   1237       C  
ATOM   3673  N   ILE B  17      11.006  43.524 -12.673  1.00 65.85           N  
ANISOU 3673  N   ILE B  17     7117   9033   8870   -702   -144   1331       N  
ATOM   3674  CA  ILE B  17       9.711  44.205 -12.871  1.00 65.19           C  
ANISOU 3674  CA  ILE B  17     7171   8904   8696   -631    -65   1370       C  
ATOM   3675  C   ILE B  17       9.233  44.867 -11.561  1.00 71.50           C  
ANISOU 3675  C   ILE B  17     8156   9561   9450   -603   -139   1289       C  
ATOM   3676  O   ILE B  17       8.933  46.065 -11.570  1.00 72.74           O  
ANISOU 3676  O   ILE B  17     8412   9590   9637   -613   -124   1308       O  
ATOM   3677  CB  ILE B  17       8.605  43.287 -13.473  1.00 66.13           C  
ANISOU 3677  CB  ILE B  17     7269   9152   8705   -520     26   1397       C  
ATOM   3678  CG1 ILE B  17       9.032  42.717 -14.838  1.00 65.73           C  
ANISOU 3678  CG1 ILE B  17     7092   9220   8664   -547    107   1473       C  
ATOM   3679  CG2 ILE B  17       7.278  44.049 -13.616  1.00 66.27           C  
ANISOU 3679  CG2 ILE B  17     7387   9110   8685   -432     74   1421       C  
ATOM   3680  CD1 ILE B  17       8.412  41.384 -15.217  1.00 65.60           C  
ANISOU 3680  CD1 ILE B  17     7031   9342   8551   -470    147   1463       C  
ATOM   3681  N   GLU B  18       9.200  44.108 -10.447  1.00 68.22           N  
ANISOU 3681  N   GLU B  18     7821   9147   8951   -570   -212   1201       N  
ATOM   3682  CA  GLU B  18       8.706  44.621  -9.170  1.00 68.79           C  
ANISOU 3682  CA  GLU B  18     8122   9079   8936   -543   -251   1114       C  
ATOM   3683  C   GLU B  18       9.590  45.731  -8.556  1.00 74.94           C  
ANISOU 3683  C   GLU B  18     8998   9689   9786   -644   -393   1071       C  
ATOM   3684  O   GLU B  18       9.038  46.591  -7.869  1.00 75.95           O  
ANISOU 3684  O   GLU B  18     9328   9672   9859   -621   -377   1019       O  
ATOM   3685  CB  GLU B  18       8.434  43.500  -8.152  1.00 69.52           C  
ANISOU 3685  CB  GLU B  18     8338   9195   8882   -495   -277   1038       C  
ATOM   3686  CG  GLU B  18       9.607  42.644  -7.740  1.00 78.17           C  
ANISOU 3686  CG  GLU B  18     9395  10320   9987   -541   -458   1012       C  
ATOM   3687  CD  GLU B  18       9.195  41.595  -6.729  1.00106.42           C  
ANISOU 3687  CD  GLU B  18    13167  13885  13382   -486   -478    951       C  
ATOM   3688  OE1 GLU B  18       8.756  40.501  -7.153  1.00104.42           O  
ANISOU 3688  OE1 GLU B  18    12838  13751  13086   -437   -383    979       O  
ATOM   3689  OE2 GLU B  18       9.263  41.884  -5.513  1.00105.25           O  
ANISOU 3689  OE2 GLU B  18    13282  13592  13116   -499   -579    875       O  
ATOM   3690  N   LYS B  19      10.915  45.754  -8.817  1.00 72.31           N  
ANISOU 3690  N   LYS B  19     8516   9364   9595   -756   -519   1083       N  
ATOM   3691  CA  LYS B  19      11.747  46.830  -8.266  1.00 74.00           C  
ANISOU 3691  CA  LYS B  19     8798   9410   9908   -874   -669   1034       C  
ATOM   3692  C   LYS B  19      12.140  47.874  -9.343  1.00 78.95           C  
ANISOU 3692  C   LYS B  19     9300   9993  10703   -977   -583   1120       C  
ATOM   3693  O   LYS B  19      13.013  48.711  -9.087  1.00 81.17           O  
ANISOU 3693  O   LYS B  19     9573  10146  11122  -1113   -696   1089       O  
ATOM   3694  CB  LYS B  19      12.978  46.306  -7.499  1.00 77.49           C  
ANISOU 3694  CB  LYS B  19     9188   9835  10420   -945   -919    955       C  
ATOM   3695  CG  LYS B  19      14.000  45.513  -8.297  1.00 88.61           C  
ANISOU 3695  CG  LYS B  19    10274  11383  12013   -990   -940    993       C  
ATOM   3696  CD  LYS B  19      15.265  45.207  -7.475  1.00100.82           C  
ANISOU 3696  CD  LYS B  19    11741  12872  13693  -1056  -1236    900       C  
ATOM   3697  CE  LYS B  19      15.112  44.130  -6.419  1.00111.42           C  
ANISOU 3697  CE  LYS B  19    13254  14221  14861   -947  -1413    834       C  
ATOM   3698  NZ  LYS B  19      14.836  44.701  -5.074  1.00122.63           N  
ANISOU 3698  NZ  LYS B  19    15034  15459  16101   -952  -1586    746       N  
ATOM   3699  N   ALA B  20      11.445  47.866 -10.507  1.00 73.53           N  
ANISOU 3699  N   ALA B  20     8553   9391   9995   -918   -391   1226       N  
ATOM   3700  CA  ALA B  20      11.672  48.814 -11.604  1.00 73.65           C  
ANISOU 3700  CA  ALA B  20     8521   9348  10114  -1002   -286   1328       C  
ATOM   3701  C   ALA B  20      10.910  50.121 -11.384  1.00 76.64           C  
ANISOU 3701  C   ALA B  20     9123   9541  10457   -968   -263   1338       C  
ATOM   3702  O   ALA B  20       9.767  50.097 -10.923  1.00 75.13           O  
ANISOU 3702  O   ALA B  20     9063   9337  10147   -822   -232   1306       O  
ATOM   3703  CB  ALA B  20      11.249  48.196 -12.923  1.00 73.23           C  
ANISOU 3703  CB  ALA B  20     8355   9451  10018   -945   -127   1436       C  
ATOM   3704  N   ASP B  21      11.530  51.256 -11.733  1.00 74.62           N  
ANISOU 3704  N   ASP B  21     8903   9130  10319  -1104   -261   1378       N  
ATOM   3705  CA  ASP B  21      10.877  52.563 -11.599  1.00 75.64           C  
ANISOU 3705  CA  ASP B  21     9260   9051  10430  -1073   -243   1393       C  
ATOM   3706  C   ASP B  21      10.307  53.041 -12.942  1.00 79.29           C  
ANISOU 3706  C   ASP B  21     9754   9498  10874  -1025   -105   1544       C  
ATOM   3707  O   ASP B  21       9.354  53.821 -12.946  1.00 79.97           O  
ANISOU 3707  O   ASP B  21    10014   9456  10914   -905    -87   1565       O  
ATOM   3708  CB  ASP B  21      11.792  53.645 -10.981  1.00 79.84           C  
ANISOU 3708  CB  ASP B  21     9881   9367  11086  -1251   -352   1334       C  
ATOM   3709  CG  ASP B  21      13.280  53.347 -10.956  1.00 94.45           C  
ANISOU 3709  CG  ASP B  21    11514  11262  13109  -1452   -436   1302       C  
ATOM   3710  OD1 ASP B  21      13.757  52.795  -9.937  1.00 96.19           O  
ANISOU 3710  OD1 ASP B  21    11697  11512  13340  -1468   -611   1182       O  
ATOM   3711  OD2 ASP B  21      13.976  53.714 -11.932  1.00101.07           O  
ANISOU 3711  OD2 ASP B  21    12232  12090  14083  -1595   -327   1393       O  
ATOM   3712  N   ASN B  22      10.857  52.547 -14.071  1.00 74.43           N  
ANISOU 3712  N   ASN B  22     8990   9004  10286  -1104    -10   1643       N  
ATOM   3713  CA  ASN B  22      10.425  52.938 -15.418  1.00 74.27           C  
ANISOU 3713  CA  ASN B  22     9049   8961  10210  -1075    108   1795       C  
ATOM   3714  C   ASN B  22       9.908  51.748 -16.239  1.00 75.75           C  
ANISOU 3714  C   ASN B  22     9128   9370  10283   -962    169   1845       C  
ATOM   3715  O   ASN B  22      10.299  50.602 -16.007  1.00 73.31           O  
ANISOU 3715  O   ASN B  22     8639   9237   9978   -970    166   1782       O  
ATOM   3716  CB  ASN B  22      11.558  53.646 -16.169  1.00 75.23           C  
ANISOU 3716  CB  ASN B  22     9174   8973  10438  -1299    209   1880       C  
ATOM   3717  CG  ASN B  22      12.831  52.844 -16.254  1.00 97.02           C  
ANISOU 3717  CG  ASN B  22    11675  11868  13322  -1459    261   1837       C  
ATOM   3718  OD1 ASN B  22      13.644  52.819 -15.326  1.00 93.81           O  
ANISOU 3718  OD1 ASN B  22    11146  11438  13060  -1560    154   1722       O  
ATOM   3719  ND2 ASN B  22      13.012  52.144 -17.355  1.00 87.43           N  
ANISOU 3719  ND2 ASN B  22    10374  10788  12056  -1472    412   1919       N  
ATOM   3720  N   ALA B  23       9.054  52.054 -17.230  1.00 72.80           N  
ANISOU 3720  N   ALA B  23     8884   8968   9808   -857    204   1959       N  
ATOM   3721  CA  ALA B  23       8.400  51.094 -18.116  1.00 71.44           C  
ANISOU 3721  CA  ALA B  23     8662   8970   9512   -743    230   2012       C  
ATOM   3722  C   ALA B  23       9.351  50.440 -19.134  1.00 74.94           C  
ANISOU 3722  C   ALA B  23     9027   9526   9922   -877    364   2077       C  
ATOM   3723  O   ALA B  23       8.978  49.417 -19.707  1.00 73.70           O  
ANISOU 3723  O   ALA B  23     8803   9534   9665   -802    382   2084       O  
ATOM   3724  CB  ALA B  23       7.252  51.768 -18.841  1.00 73.10           C  
ANISOU 3724  CB  ALA B  23     9058   9078   9639   -592    175   2109       C  
ATOM   3725  N   ALA B  24      10.556  51.011 -19.366  1.00 72.09           N  
ANISOU 3725  N   ALA B  24     8670   9066   9654  -1078    475   2115       N  
ATOM   3726  CA  ALA B  24      11.545  50.437 -20.291  1.00 71.66           C  
ANISOU 3726  CA  ALA B  24     8525   9101   9602  -1218    658   2160       C  
ATOM   3727  C   ALA B  24      12.198  49.189 -19.677  1.00 73.24           C  
ANISOU 3727  C   ALA B  24     8438   9489   9902  -1231    650   2034       C  
ATOM   3728  O   ALA B  24      12.464  48.222 -20.390  1.00 71.30           O  
ANISOU 3728  O   ALA B  24     8106   9386   9600  -1228    761   2044       O  
ATOM   3729  CB  ALA B  24      12.603  51.467 -20.638  1.00 74.64           C  
ANISOU 3729  CB  ALA B  24     8960   9303  10096  -1443    802   2220       C  
ATOM   3730  N   GLN B  25      12.451  49.229 -18.347  1.00 69.91           N  
ANISOU 3730  N   GLN B  25     7901   9048   9614  -1238    507   1914       N  
ATOM   3731  CA  GLN B  25      13.038  48.155 -17.535  1.00 68.52           C  
ANISOU 3731  CA  GLN B  25     7494   9007   9534  -1232    432   1790       C  
ATOM   3732  C   GLN B  25      12.026  47.009 -17.418  1.00 69.28           C  
ANISOU 3732  C   GLN B  25     7592   9261   9471  -1044    374   1760       C  
ATOM   3733  O   GLN B  25      12.395  45.839 -17.504  1.00 67.31           O  
ANISOU 3733  O   GLN B  25     7190   9156   9229  -1022    398   1715       O  
ATOM   3734  CB  GLN B  25      13.417  48.707 -16.150  1.00 70.56           C  
ANISOU 3734  CB  GLN B  25     7731   9153   9925  -1282    256   1682       C  
ATOM   3735  CG  GLN B  25      14.557  47.962 -15.455  1.00 93.09           C  
ANISOU 3735  CG  GLN B  25    10340  12076  12954  -1354    167   1570       C  
ATOM   3736  CD  GLN B  25      14.734  48.385 -14.010  1.00115.97           C  
ANISOU 3736  CD  GLN B  25    13283  14862  15920  -1373    -64   1457       C  
ATOM   3737  OE1 GLN B  25      14.613  47.573 -13.083  1.00111.77           O  
ANISOU 3737  OE1 GLN B  25    12734  14393  15340  -1280   -218   1366       O  
ATOM   3738  NE2 GLN B  25      15.013  49.667 -13.776  1.00107.21           N  
ANISOU 3738  NE2 GLN B  25    12270  13563  14903  -1497    -97   1458       N  
ATOM   3739  N   VAL B  26      10.740  47.370 -17.262  1.00 65.68           N  
ANISOU 3739  N   VAL B  26     7301   8763   8892   -910    309   1783       N  
ATOM   3740  CA  VAL B  26       9.597  46.461 -17.192  1.00 63.82           C  
ANISOU 3740  CA  VAL B  26     7070   8649   8530   -745    265   1756       C  
ATOM   3741  C   VAL B  26       9.441  45.787 -18.571  1.00 68.88           C  
ANISOU 3741  C   VAL B  26     7709   9403   9060   -724    366   1838       C  
ATOM   3742  O   VAL B  26       9.431  44.559 -18.637  1.00 68.46           O  
ANISOU 3742  O   VAL B  26     7553   9495   8962   -680    376   1793       O  
ATOM   3743  CB  VAL B  26       8.310  47.201 -16.729  1.00 67.22           C  
ANISOU 3743  CB  VAL B  26     7643   8980   8918   -618    189   1749       C  
ATOM   3744  CG1 VAL B  26       7.089  46.302 -16.814  1.00 65.50           C  
ANISOU 3744  CG1 VAL B  26     7393   8883   8612   -467    167   1721       C  
ATOM   3745  CG2 VAL B  26       8.463  47.733 -15.308  1.00 67.62           C  
ANISOU 3745  CG2 VAL B  26     7735   8914   9042   -638    109   1649       C  
ATOM   3746  N   LYS B  27       9.382  46.590 -19.658  1.00 66.84           N  
ANISOU 3746  N   LYS B  27     7596   9057   8741   -761    437   1958       N  
ATOM   3747  CA  LYS B  27       9.264  46.141 -21.055  1.00 67.81           C  
ANISOU 3747  CA  LYS B  27     7802   9245   8716   -755    529   2047       C  
ATOM   3748  C   LYS B  27      10.351  45.107 -21.411  1.00 71.61           C  
ANISOU 3748  C   LYS B  27     8132   9852   9223   -844    675   2010       C  
ATOM   3749  O   LYS B  27      10.034  44.074 -21.998  1.00 70.42           O  
ANISOU 3749  O   LYS B  27     7977   9824   8955   -780    697   2002       O  
ATOM   3750  CB  LYS B  27       9.346  47.347 -22.021  1.00 72.60           C  
ANISOU 3750  CB  LYS B  27     8641   9687   9256   -821    596   2186       C  
ATOM   3751  CG  LYS B  27       9.080  47.029 -23.490  1.00 89.10           C  
ANISOU 3751  CG  LYS B  27    10912  11805  11138   -807    669   2291       C  
ATOM   3752  CD  LYS B  27       9.321  48.259 -24.350  1.00105.08           C  
ANISOU 3752  CD  LYS B  27    13213  13629  13082   -891    744   2436       C  
ATOM   3753  CE  LYS B  27       9.319  47.959 -25.829  1.00118.34           C  
ANISOU 3753  CE  LYS B  27    15129  15310  14524   -919    859   2543       C  
ATOM   3754  NZ  LYS B  27       9.231  49.207 -26.634  1.00131.05           N  
ANISOU 3754  NZ  LYS B  27    17087  16695  16009   -964    879   2700       N  
ATOM   3755  N   ASP B  28      11.612  45.385 -21.036  1.00 68.94           N  
ANISOU 3755  N   ASP B  28     7662   9473   9060   -987    765   1976       N  
ATOM   3756  CA  ASP B  28      12.752  44.511 -21.307  1.00 69.13           C  
ANISOU 3756  CA  ASP B  28     7497   9594   9177  -1067    912   1926       C  
ATOM   3757  C   ASP B  28      12.677  43.223 -20.507  1.00 69.88           C  
ANISOU 3757  C   ASP B  28     7419   9826   9305   -964    800   1809       C  
ATOM   3758  O   ASP B  28      12.954  42.159 -21.067  1.00 69.33           O  
ANISOU 3758  O   ASP B  28     7281   9867   9196   -938    898   1785       O  
ATOM   3759  CB  ASP B  28      14.066  45.230 -21.011  1.00 73.23           C  
ANISOU 3759  CB  ASP B  28     7874  10015   9934  -1246   1002   1904       C  
ATOM   3760  CG  ASP B  28      15.290  44.380 -21.267  1.00 87.52           C  
ANISOU 3760  CG  ASP B  28     9431  11914  11909  -1318   1154   1834       C  
ATOM   3761  OD1 ASP B  28      15.604  44.131 -22.457  1.00 90.05           O  
ANISOU 3761  OD1 ASP B  28     9797  12260  12156  -1369   1398   1885       O  
ATOM   3762  OD2 ASP B  28      15.977  44.024 -20.285  1.00 94.01           O  
ANISOU 3762  OD2 ASP B  28    10019  12759  12942  -1327   1033   1724       O  
ATOM   3763  N   ALA B  29      12.320  43.315 -19.206  1.00 64.04           N  
ANISOU 3763  N   ALA B  29     6642   9063   8626   -908    609   1737       N  
ATOM   3764  CA  ALA B  29      12.199  42.148 -18.339  1.00 62.35           C  
ANISOU 3764  CA  ALA B  29     6325   8946   8419   -815    494   1635       C  
ATOM   3765  C   ALA B  29      11.080  41.227 -18.844  1.00 64.71           C  
ANISOU 3765  C   ALA B  29     6708   9350   8529   -694    497   1648       C  
ATOM   3766  O   ALA B  29      11.327  40.027 -18.996  1.00 63.48           O  
ANISOU 3766  O   ALA B  29     6469   9295   8357   -656    524   1600       O  
ATOM   3767  CB  ALA B  29      11.961  42.567 -16.899  1.00 62.68           C  
ANISOU 3767  CB  ALA B  29     6394   8910   8512   -793    313   1567       C  
ATOM   3768  N   LEU B  30       9.896  41.802 -19.196  1.00 60.81           N  
ANISOU 3768  N   LEU B  30     6372   8821   7913   -635    466   1710       N  
ATOM   3769  CA  LEU B  30       8.767  41.072 -19.790  1.00 59.85           C  
ANISOU 3769  CA  LEU B  30     6318   8783   7641   -534    444   1722       C  
ATOM   3770  C   LEU B  30       9.142  40.417 -21.129  1.00 65.56           C  
ANISOU 3770  C   LEU B  30     7073   9578   8261   -561    569   1765       C  
ATOM   3771  O   LEU B  30       8.706  39.295 -21.377  1.00 65.47           O  
ANISOU 3771  O   LEU B  30     7051   9662   8164   -501    555   1726       O  
ATOM   3772  CB  LEU B  30       7.560  41.993 -20.024  1.00 60.04           C  
ANISOU 3772  CB  LEU B  30     6475   8730   7606   -465    365   1781       C  
ATOM   3773  CG  LEU B  30       6.762  42.451 -18.803  1.00 63.76           C  
ANISOU 3773  CG  LEU B  30     6939   9140   8146   -396    264   1720       C  
ATOM   3774  CD1 LEU B  30       5.880  43.623 -19.169  1.00 64.66           C  
ANISOU 3774  CD1 LEU B  30     7172   9142   8256   -334    207   1787       C  
ATOM   3775  CD2 LEU B  30       5.934  41.305 -18.198  1.00 63.47           C  
ANISOU 3775  CD2 LEU B  30     6832   9199   8084   -318    228   1631       C  
ATOM   3776  N   THR B  31       9.928  41.115 -21.990  1.00 63.26           N  
ANISOU 3776  N   THR B  31     6843   9224   7967   -659    707   1842       N  
ATOM   3777  CA  THR B  31      10.363  40.604 -23.302  1.00 64.26           C  
ANISOU 3777  CA  THR B  31     7049   9394   7974   -700    876   1883       C  
ATOM   3778  C   THR B  31      11.221  39.347 -23.100  1.00 69.18           C  
ANISOU 3778  C   THR B  31     7487  10117   8682   -703    966   1784       C  
ATOM   3779  O   THR B  31      11.010  38.352 -23.799  1.00 69.53           O  
ANISOU 3779  O   THR B  31     7585  10237   8597   -658   1017   1763       O  
ATOM   3780  CB  THR B  31      11.103  41.692 -24.125  1.00 69.17           C  
ANISOU 3780  CB  THR B  31     7793   9901   8588   -828   1048   1984       C  
ATOM   3781  OG1 THR B  31      10.261  42.835 -24.254  1.00 66.35           O  
ANISOU 3781  OG1 THR B  31     7629   9429   8151   -801    932   2077       O  
ATOM   3782  CG2 THR B  31      11.486  41.217 -25.521  1.00 67.06           C  
ANISOU 3782  CG2 THR B  31     7671   9656   8154   -875   1261   2027       C  
ATOM   3783  N   LYS B  32      12.159  39.391 -22.129  1.00 65.90           N  
ANISOU 3783  N   LYS B  32     6865   9687   8488   -746    957   1717       N  
ATOM   3784  CA  LYS B  32      13.035  38.272 -21.777  1.00 65.52           C  
ANISOU 3784  CA  LYS B  32     6616   9709   8571   -726    994   1617       C  
ATOM   3785  C   LYS B  32      12.214  37.120 -21.163  1.00 67.94           C  
ANISOU 3785  C   LYS B  32     6932  10090   8791   -602    840   1551       C  
ATOM   3786  O   LYS B  32      12.509  35.955 -21.429  1.00 68.33           O  
ANISOU 3786  O   LYS B  32     6928  10203   8829   -555    896   1494       O  
ATOM   3787  CB  LYS B  32      14.153  38.722 -20.834  1.00 68.35           C  
ANISOU 3787  CB  LYS B  32     6761  10011   9198   -795    949   1563       C  
ATOM   3788  CG  LYS B  32      15.196  39.584 -21.511  1.00 81.38           C  
ANISOU 3788  CG  LYS B  32     8333  11596  10991   -943   1160   1600       C  
ATOM   3789  CD  LYS B  32      16.497  39.574 -20.734  1.00 94.40           C  
ANISOU 3789  CD  LYS B  32     9687  13219  12963  -1000   1118   1507       C  
ATOM   3790  CE  LYS B  32      16.896  40.942 -20.246  1.00107.18           C  
ANISOU 3790  CE  LYS B  32    11276  14715  14734  -1135   1070   1532       C  
ATOM   3791  NZ  LYS B  32      15.961  41.462 -19.205  1.00115.20           N  
ANISOU 3791  NZ  LYS B  32    12443  15678  15650  -1080    813   1540       N  
ATOM   3792  N   MET B  33      11.157  37.445 -20.398  1.00 62.68           N  
ANISOU 3792  N   MET B  33     6347   9402   8066   -553    673   1557       N  
ATOM   3793  CA  MET B  33      10.230  36.451 -19.832  1.00 60.75           C  
ANISOU 3793  CA  MET B  33     6135   9211   7738   -460    561   1501       C  
ATOM   3794  C   MET B  33       9.451  35.736 -20.934  1.00 64.51           C  
ANISOU 3794  C   MET B  33     6718   9753   8042   -423    609   1520       C  
ATOM   3795  O   MET B  33       9.296  34.520 -20.869  1.00 63.81           O  
ANISOU 3795  O   MET B  33     6615   9718   7911   -377    599   1459       O  
ATOM   3796  CB  MET B  33       9.243  37.098 -18.855  1.00 61.99           C  
ANISOU 3796  CB  MET B  33     6353   9314   7887   -430    429   1500       C  
ATOM   3797  CG  MET B  33       9.839  37.344 -17.510  1.00 65.60           C  
ANISOU 3797  CG  MET B  33     6753   9710   8461   -443    336   1443       C  
ATOM   3798  SD  MET B  33       8.627  37.848 -16.287  1.00 68.88           S  
ANISOU 3798  SD  MET B  33     7281  10056   8834   -397    232   1413       S  
ATOM   3799  CE  MET B  33       7.803  36.280 -15.999  1.00 64.45           C  
ANISOU 3799  CE  MET B  33     6750   9569   8170   -330    229   1352       C  
ATOM   3800  N   ARG B  34       8.980  36.484 -21.952  1.00 62.22           N  
ANISOU 3800  N   ARG B  34     6556   9441   7642   -444    644   1604       N  
ATOM   3801  CA  ARG B  34       8.213  35.932 -23.072  1.00 62.78           C  
ANISOU 3801  CA  ARG B  34     6767   9556   7531   -414    644   1624       C  
ATOM   3802  C   ARG B  34       9.045  34.907 -23.849  1.00 67.51           C  
ANISOU 3802  C   ARG B  34     7374  10203   8073   -431    800   1586       C  
ATOM   3803  O   ARG B  34       8.514  33.858 -24.241  1.00 67.01           O  
ANISOU 3803  O   ARG B  34     7370  10191   7901   -390    771   1539       O  
ATOM   3804  CB  ARG B  34       7.725  37.044 -24.012  1.00 62.79           C  
ANISOU 3804  CB  ARG B  34     6943   9494   7419   -431    626   1732       C  
ATOM   3805  CG  ARG B  34       6.461  36.662 -24.750  1.00 66.57           C  
ANISOU 3805  CG  ARG B  34     7557   9998   7737   -370    493   1743       C  
ATOM   3806  CD  ARG B  34       6.244  37.539 -25.960  1.00 69.75           C  
ANISOU 3806  CD  ARG B  34     8192  10325   7985   -381    471   1856       C  
ATOM   3807  NE  ARG B  34       4.977  37.233 -26.624  1.00 69.13           N  
ANISOU 3807  NE  ARG B  34     8230  10260   7776   -311    274   1858       N  
ATOM   3808  CZ  ARG B  34       4.854  36.500 -27.727  1.00 84.81           C  
ANISOU 3808  CZ  ARG B  34    10392  12271   9560   -318    270   1853       C  
ATOM   3809  NH1 ARG B  34       5.932  36.002 -28.327  1.00 73.75           N  
ANISOU 3809  NH1 ARG B  34     9081  10884   8056   -385    495   1846       N  
ATOM   3810  NH2 ARG B  34       3.655  36.270 -28.247  1.00 72.67           N  
ANISOU 3810  NH2 ARG B  34     8940  10736   7934   -256     39   1845       N  
ATOM   3811  N   ALA B  35      10.350  35.214 -24.039  1.00 64.03           N  
ANISOU 3811  N   ALA B  35     6861   9737   7731   -494    974   1594       N  
ATOM   3812  CA  ALA B  35      11.328  34.377 -24.734  1.00 64.11           C  
ANISOU 3812  CA  ALA B  35     6841   9776   7741   -507   1174   1546       C  
ATOM   3813  C   ALA B  35      11.611  33.092 -23.951  1.00 66.22           C  
ANISOU 3813  C   ALA B  35     6955  10089   8116   -433   1121   1436       C  
ATOM   3814  O   ALA B  35      11.644  32.014 -24.546  1.00 66.54           O  
ANISOU 3814  O   ALA B  35     7054  10162   8066   -392   1195   1382       O  
ATOM   3815  CB  ALA B  35      12.616  35.155 -24.942  1.00 66.20           C  
ANISOU 3815  CB  ALA B  35     7007   9990   8157   -603   1377   1572       C  
ATOM   3816  N   ALA B  36      11.806  33.216 -22.621  1.00 60.36           N  
ANISOU 3816  N   ALA B  36     6057   9330   7547   -412    982   1403       N  
ATOM   3817  CA  ALA B  36      12.089  32.115 -21.708  1.00 58.86           C  
ANISOU 3817  CA  ALA B  36     5759   9152   7453   -337    891   1313       C  
ATOM   3818  C   ALA B  36      10.858  31.243 -21.484  1.00 60.57           C  
ANISOU 3818  C   ALA B  36     6104   9393   7515   -282    774   1288       C  
ATOM   3819  O   ALA B  36      11.013  30.039 -21.320  1.00 59.69           O  
ANISOU 3819  O   ALA B  36     5986   9289   7405   -224    768   1220       O  
ATOM   3820  CB  ALA B  36      12.603  32.648 -20.389  1.00 59.38           C  
ANISOU 3820  CB  ALA B  36     5689   9168   7705   -343    752   1296       C  
ATOM   3821  N   ALA B  37       9.643  31.828 -21.499  1.00 57.13           N  
ANISOU 3821  N   ALA B  37     5775   8961   6969   -301    688   1337       N  
ATOM   3822  CA  ALA B  37       8.393  31.068 -21.368  1.00 56.21           C  
ANISOU 3822  CA  ALA B  37     5747   8867   6744   -271    594   1306       C  
ATOM   3823  C   ALA B  37       8.187  30.181 -22.606  1.00 62.60           C  
ANISOU 3823  C   ALA B  37     6667   9712   7405   -266    662   1285       C  
ATOM   3824  O   ALA B  37       7.963  28.979 -22.461  1.00 63.31           O  
ANISOU 3824  O   ALA B  37     6786   9808   7462   -238    642   1217       O  
ATOM   3825  CB  ALA B  37       7.208  32.003 -21.184  1.00 56.07           C  
ANISOU 3825  CB  ALA B  37     5767   8837   6698   -285    496   1353       C  
ATOM   3826  N   LEU B  38       8.323  30.765 -23.814  1.00 59.65           N  
ANISOU 3826  N   LEU B  38     6389   9345   6929   -298    746   1341       N  
ATOM   3827  CA  LEU B  38       8.189  30.056 -25.088  1.00 60.53           C  
ANISOU 3827  CA  LEU B  38     6665   9473   6860   -301    814   1321       C  
ATOM   3828  C   LEU B  38       9.203  28.919 -25.236  1.00 66.12           C  
ANISOU 3828  C   LEU B  38     7342  10181   7599   -268    966   1239       C  
ATOM   3829  O   LEU B  38       8.832  27.840 -25.701  1.00 66.97           O  
ANISOU 3829  O   LEU B  38     7561  10294   7592   -247    961   1177       O  
ATOM   3830  CB  LEU B  38       8.328  31.021 -26.272  1.00 61.73           C  
ANISOU 3830  CB  LEU B  38     6975   9603   6875   -346    896   1408       C  
ATOM   3831  CG  LEU B  38       7.140  31.945 -26.528  1.00 65.98           C  
ANISOU 3831  CG  LEU B  38     7615  10123   7330   -352    714   1485       C  
ATOM   3832  CD1 LEU B  38       7.435  32.891 -27.677  1.00 67.09           C  
ANISOU 3832  CD1 LEU B  38     7954  10210   7325   -395    803   1586       C  
ATOM   3833  CD2 LEU B  38       5.821  31.153 -26.739  1.00 65.67           C  
ANISOU 3833  CD2 LEU B  38     7653  10110   7189   -325    526   1436       C  
ATOM   3834  N   ASP B  39      10.470  29.158 -24.840  1.00 62.44           N  
ANISOU 3834  N   ASP B  39     6714   9699   7310   -260   1088   1230       N  
ATOM   3835  CA  ASP B  39      11.536  28.159 -24.904  1.00 63.10           C  
ANISOU 3835  CA  ASP B  39     6715   9772   7489   -205   1227   1144       C  
ATOM   3836  C   ASP B  39      11.299  27.066 -23.854  1.00 65.97           C  
ANISOU 3836  C   ASP B  39     7025  10118   7920   -131   1078   1073       C  
ATOM   3837  O   ASP B  39      11.631  25.901 -24.103  1.00 66.37           O  
ANISOU 3837  O   ASP B  39     7111  10148   7960    -69   1142    995       O  
ATOM   3838  CB  ASP B  39      12.909  28.819 -24.712  1.00 66.57           C  
ANISOU 3838  CB  ASP B  39     6946  10193   8155   -221   1367   1148       C  
ATOM   3839  CG  ASP B  39      14.093  27.889 -24.911  1.00 84.78           C  
ANISOU 3839  CG  ASP B  39     9125  12481  10607   -151   1538   1050       C  
ATOM   3840  OD1 ASP B  39      14.930  27.789 -23.987  1.00 86.12           O  
ANISOU 3840  OD1 ASP B  39     9061  12628  11031   -100   1474   1006       O  
ATOM   3841  OD2 ASP B  39      14.181  27.256 -25.991  1.00 93.14           O  
ANISOU 3841  OD2 ASP B  39    10324  13537  11526   -140   1725   1011       O  
ATOM   3842  N   ALA B  40      10.711  27.441 -22.691  1.00 60.33           N  
ANISOU 3842  N   ALA B  40     6263   9397   7264   -138    895   1101       N  
ATOM   3843  CA  ALA B  40      10.389  26.504 -21.617  1.00 59.49           C  
ANISOU 3843  CA  ALA B  40     6164   9252   7188    -88    761   1050       C  
ATOM   3844  C   ALA B  40       9.264  25.584 -22.071  1.00 64.57           C  
ANISOU 3844  C   ALA B  40     6973   9899   7660   -104    732   1018       C  
ATOM   3845  O   ALA B  40       9.300  24.390 -21.773  1.00 64.04           O  
ANISOU 3845  O   ALA B  40     6961   9785   7588    -59    711    955       O  
ATOM   3846  CB  ALA B  40       9.999  27.252 -20.348  1.00 58.99           C  
ANISOU 3846  CB  ALA B  40     6055   9167   7191   -109    617   1088       C  
ATOM   3847  N   GLN B  41       8.302  26.139 -22.862  1.00 61.85           N  
ANISOU 3847  N   GLN B  41     6716   9598   7186   -167    717   1059       N  
ATOM   3848  CA  GLN B  41       7.161  25.430 -23.454  1.00 61.18           C  
ANISOU 3848  CA  GLN B  41     6771   9520   6956   -202    658   1025       C  
ATOM   3849  C   GLN B  41       7.624  24.313 -24.408  1.00 66.31           C  
ANISOU 3849  C   GLN B  41     7544  10148   7502   -174    762    954       C  
ATOM   3850  O   GLN B  41       6.952  23.286 -24.524  1.00 66.61           O  
ANISOU 3850  O   GLN B  41     7686  10156   7466   -189    709    891       O  
ATOM   3851  CB  GLN B  41       6.263  26.416 -24.205  1.00 62.14           C  
ANISOU 3851  CB  GLN B  41     6944   9680   6986   -254    588   1086       C  
ATOM   3852  CG  GLN B  41       4.827  25.930 -24.353  1.00 65.97           C  
ANISOU 3852  CG  GLN B  41     7492  10169   7406   -297    446   1049       C  
ATOM   3853  CD  GLN B  41       3.987  26.791 -25.254  1.00 68.86           C  
ANISOU 3853  CD  GLN B  41     7917  10560   7688   -323    334   1102       C  
ATOM   3854  OE1 GLN B  41       4.407  27.216 -26.334  1.00 69.13           O  
ANISOU 3854  OE1 GLN B  41     8083  10595   7587   -319    377   1145       O  
ATOM   3855  NE2 GLN B  41       2.738  26.973 -24.879  1.00 56.69           N  
ANISOU 3855  NE2 GLN B  41     6296   9023   6219   -347    187   1092       N  
ATOM   3856  N   LYS B  42       8.771  24.518 -25.072  1.00 63.99           N  
ANISOU 3856  N   LYS B  42     7239   9857   7216   -140    929    956       N  
ATOM   3857  CA  LYS B  42       9.372  23.570 -26.018  1.00 65.56           C  
ANISOU 3857  CA  LYS B  42     7557  10025   7327   -101   1085    881       C  
ATOM   3858  C   LYS B  42      10.036  22.403 -25.288  1.00 71.26           C  
ANISOU 3858  C   LYS B  42     8211  10685   8180    -10   1104    798       C  
ATOM   3859  O   LYS B  42      10.180  21.320 -25.867  1.00 71.50           O  
ANISOU 3859  O   LYS B  42     8372  10665   8128     29   1178    715       O  
ATOM   3860  CB  LYS B  42      10.406  24.275 -26.917  1.00 68.28           C  
ANISOU 3860  CB  LYS B  42     7892  10382   7667   -103   1309    907       C  
ATOM   3861  CG  LYS B  42       9.849  25.384 -27.794  1.00 67.87           C  
ANISOU 3861  CG  LYS B  42     7986  10360   7442   -186   1305    996       C  
ATOM   3862  CD  LYS B  42      10.941  25.950 -28.688  1.00 74.05           C  
ANISOU 3862  CD  LYS B  42     8799  11129   8208   -206   1581   1019       C  
ATOM   3863  CE  LYS B  42      10.726  27.392 -29.076  1.00 89.16           C  
ANISOU 3863  CE  LYS B  42    10782  13050  10044   -286   1573   1141       C  
ATOM   3864  NZ  LYS B  42       9.617  27.549 -30.054  1.00104.57           N  
ANISOU 3864  NZ  LYS B  42    13041  14990  11700   -325   1448   1180       N  
ATOM   3865  N   ALA B  43      10.460  22.639 -24.024  1.00 68.46           N  
ANISOU 3865  N   ALA B  43     7677  10315   8018     32   1023    820       N  
ATOM   3866  CA  ALA B  43      11.149  21.657 -23.193  1.00 69.01           C  
ANISOU 3866  CA  ALA B  43     7689  10305   8226    136    989    757       C  
ATOM   3867  C   ALA B  43      10.201  20.602 -22.667  1.00 74.48           C  
ANISOU 3867  C   ALA B  43     8539  10934   8826    123    862    725       C  
ATOM   3868  O   ALA B  43       8.998  20.827 -22.591  1.00 73.53           O  
ANISOU 3868  O   ALA B  43     8493  10842   8602     24    775    758       O  
ATOM   3869  CB  ALA B  43      11.848  22.344 -22.037  1.00 69.13           C  
ANISOU 3869  CB  ALA B  43     7507  10313   8447    174    898    796       C  
ATOM   3870  N   THR B  44      10.745  19.444 -22.321  1.00 73.80           N  
ANISOU 3870  N   THR B  44     8498  10748   8796    222    858    657       N  
ATOM   3871  CA  THR B  44       9.978  18.341 -21.765  1.00 74.49           C  
ANISOU 3871  CA  THR B  44     8758  10738   8805    205    758    627       C  
ATOM   3872  C   THR B  44      10.362  18.244 -20.277  1.00 79.20           C  
ANISOU 3872  C   THR B  44     9316  11253   9524    271    619    656       C  
ATOM   3873  O   THR B  44      11.546  18.053 -19.980  1.00 79.05           O  
ANISOU 3873  O   THR B  44     9193  11184   9659    406    604    633       O  
ATOM   3874  CB  THR B  44      10.227  17.042 -22.569  1.00 88.73           C  
ANISOU 3874  CB  THR B  44    10715  12456  10542    266    849    528       C  
ATOM   3875  OG1 THR B  44       9.999  17.286 -23.961  1.00 91.20           O  
ANISOU 3875  OG1 THR B  44    11094  12840  10719    208    973    501       O  
ATOM   3876  CG2 THR B  44       9.361  15.871 -22.093  1.00 88.06           C  
ANISOU 3876  CG2 THR B  44    10836  12253  10369    219    758    495       C  
ATOM   3877  N   PRO B  45       9.398  18.396 -19.330  1.00 76.35           N  
ANISOU 3877  N   PRO B  45     9040  10867   9102    180    516    702       N  
ATOM   3878  CA  PRO B  45       9.743  18.286 -17.900  1.00 77.06           C  
ANISOU 3878  CA  PRO B  45     9169  10855   9254    237    381    732       C  
ATOM   3879  C   PRO B  45      10.421  16.950 -17.570  1.00 85.64           C  
ANISOU 3879  C   PRO B  45    10385  11782  10372    370    325    682       C  
ATOM   3880  O   PRO B  45      10.087  15.938 -18.195  1.00 85.49           O  
ANISOU 3880  O   PRO B  45    10500  11706  10276    363    396    627       O  
ATOM   3881  CB  PRO B  45       8.390  18.415 -17.203  1.00 77.59           C  
ANISOU 3881  CB  PRO B  45     9366  10907   9207     95    359    769       C  
ATOM   3882  CG  PRO B  45       7.550  19.155 -18.164  1.00 80.59           C  
ANISOU 3882  CG  PRO B  45     9651  11424   9544    -17    440    775       C  
ATOM   3883  CD  PRO B  45       7.953  18.643 -19.502  1.00 76.77           C  
ANISOU 3883  CD  PRO B  45     9162  10970   9037     25    521    720       C  
ATOM   3884  N   PRO B  46      11.411  16.938 -16.635  1.00 85.94           N  
ANISOU 3884  N   PRO B  46    10391  11732  10530    499    178    696       N  
ATOM   3885  CA  PRO B  46      12.143  15.686 -16.329  1.00 87.79           C  
ANISOU 3885  CA  PRO B  46    10744  11794  10818    660     90    649       C  
ATOM   3886  C   PRO B  46      11.253  14.498 -15.940  1.00 91.37           C  
ANISOU 3886  C   PRO B  46    11527  12093  11096    603     82    647       C  
ATOM   3887  O   PRO B  46      11.593  13.352 -16.250  1.00 92.27           O  
ANISOU 3887  O   PRO B  46    11759  12079  11220    705     87    591       O  
ATOM   3888  CB  PRO B  46      13.051  16.086 -15.156  1.00 90.58           C  
ANISOU 3888  CB  PRO B  46    11038  12077  11301    773   -134    683       C  
ATOM   3889  CG  PRO B  46      12.466  17.373 -14.615  1.00 93.54           C  
ANISOU 3889  CG  PRO B  46    11374  12554  11614    632   -154    752       C  
ATOM   3890  CD  PRO B  46      11.931  18.061 -15.827  1.00 87.76           C  
ANISOU 3890  CD  PRO B  46    10484  12002  10860    513     55    747       C  
ATOM   3891  N   LYS B  47      10.112  14.777 -15.290  1.00 86.56           N  
ANISOU 3891  N   LYS B  47    11062  11485  10341    435     91    701       N  
ATOM   3892  CA  LYS B  47       9.138  13.777 -14.846  1.00 86.81           C  
ANISOU 3892  CA  LYS B  47    11398  11369  10217    332    122    703       C  
ATOM   3893  C   LYS B  47       8.382  13.138 -16.017  1.00 89.19           C  
ANISOU 3893  C   LYS B  47    11722  11704  10461    229    273    638       C  
ATOM   3894  O   LYS B  47       7.945  11.990 -15.898  1.00 90.47           O  
ANISOU 3894  O   LYS B  47    12126  11708  10539    185    294    611       O  
ATOM   3895  CB  LYS B  47       8.120  14.417 -13.878  1.00 89.16           C  
ANISOU 3895  CB  LYS B  47    11795  11673  10410    168    140    767       C  
ATOM   3896  CG  LYS B  47       8.690  14.772 -12.503  1.00112.36           C  
ANISOU 3896  CG  LYS B  47    14845  14513  13331    247    -24    827       C  
ATOM   3897  CD  LYS B  47       7.717  15.614 -11.666  1.00124.25           C  
ANISOU 3897  CD  LYS B  47    16432  16044  14734     84     46    875       C  
ATOM   3898  CE  LYS B  47       8.273  15.932 -10.295  1.00133.60           C  
ANISOU 3898  CE  LYS B  47    17797  17109  15855    154   -124    928       C  
ATOM   3899  NZ  LYS B  47       7.352  16.788  -9.503  1.00138.81           N  
ANISOU 3899  NZ  LYS B  47    18558  17781  16403     -1    -15    960       N  
ATOM   3900  N   LEU B  48       8.228  13.874 -17.136  1.00 83.19           N  
ANISOU 3900  N   LEU B  48    10741  11131   9734    184    363    613       N  
ATOM   3901  CA  LEU B  48       7.439  13.443 -18.297  1.00 82.13           C  
ANISOU 3901  CA  LEU B  48    10639  11041   9526     74    467    549       C  
ATOM   3902  C   LEU B  48       8.274  12.945 -19.493  1.00 85.45           C  
ANISOU 3902  C   LEU B  48    11027  11468   9971    197    533    470       C  
ATOM   3903  O   LEU B  48       7.778  13.006 -20.622  1.00 84.31           O  
ANISOU 3903  O   LEU B  48    10864  11412   9757    118    609    425       O  
ATOM   3904  CB  LEU B  48       6.520  14.604 -18.759  1.00 80.63           C  
ANISOU 3904  CB  LEU B  48    10285  11033   9318    -75    505    576       C  
ATOM   3905  CG  LEU B  48       5.669  15.323 -17.690  1.00 83.87           C  
ANISOU 3905  CG  LEU B  48    10677  11461   9730   -192    485    640       C  
ATOM   3906  CD1 LEU B  48       4.940  16.497 -18.281  1.00 82.63           C  
ANISOU 3906  CD1 LEU B  48    10325  11476   9593   -287    506    659       C  
ATOM   3907  CD2 LEU B  48       4.669  14.380 -17.031  1.00 86.81           C  
ANISOU 3907  CD2 LEU B  48    11260  11686  10039   -327    519    622       C  
ATOM   3908  N   GLU B  49       9.499  12.409 -19.260  1.00 83.26           N  
ANISOU 3908  N   GLU B  49    10761  11083   9792    393    501    445       N  
ATOM   3909  CA  GLU B  49      10.357  11.925 -20.359  1.00 84.40           C  
ANISOU 3909  CA  GLU B  49    10865  11217   9985    527    607    354       C  
ATOM   3910  C   GLU B  49       9.792  10.634 -21.006  1.00 88.60           C  
ANISOU 3910  C   GLU B  49    11657  11618  10389    482    665    266       C  
ATOM   3911  O   GLU B  49       9.971  10.425 -22.208  1.00 88.08           O  
ANISOU 3911  O   GLU B  49    11605  11581  10279    505    791    183       O  
ATOM   3912  CB  GLU B  49      11.833  11.741 -19.925  1.00 87.30           C  
ANISOU 3912  CB  GLU B  49    11112  11505  10553    765    553    338       C  
ATOM   3913  CG  GLU B  49      12.105  10.658 -18.891  1.00101.44           C  
ANISOU 3913  CG  GLU B  49    13107  13066  12370    881    399    341       C  
ATOM   3914  CD  GLU B  49      13.184   9.658 -19.270  1.00125.31           C  
ANISOU 3914  CD  GLU B  49    16136  15942  15532   1116    418    246       C  
ATOM   3915  OE1 GLU B  49      14.383  10.019 -19.216  1.00120.77           O  
ANISOU 3915  OE1 GLU B  49    15307  15395  15184   1293    389    226       O  
ATOM   3916  OE2 GLU B  49      12.830   8.501 -19.591  1.00118.82           O  
ANISOU 3916  OE2 GLU B  49    15565  14966  14615   1125    461    183       O  
ATOM   3917  N   ASP B  50       9.079   9.809 -20.220  1.00 86.00           N  
ANISOU 3917  N   ASP B  50    11555  11134   9987    400    586    282       N  
ATOM   3918  CA  ASP B  50       8.468   8.556 -20.680  1.00 87.33           C  
ANISOU 3918  CA  ASP B  50    11990  11147  10045    328    623    200       C  
ATOM   3919  C   ASP B  50       7.084   8.787 -21.320  1.00 88.27           C  
ANISOU 3919  C   ASP B  50    12133  11363  10043     77    654    180       C  
ATOM   3920  O   ASP B  50       6.527   7.862 -21.920  1.00 89.33           O  
ANISOU 3920  O   ASP B  50    12460  11395  10087    -10    679     95       O  
ATOM   3921  CB  ASP B  50       8.346   7.565 -19.503  1.00 90.92           C  
ANISOU 3921  CB  ASP B  50    12698  11361  10486    344    532    232       C  
ATOM   3922  CG  ASP B  50       7.529   8.069 -18.320  1.00107.22           C  
ANISOU 3922  CG  ASP B  50    14793  13433  12513    187    474    336       C  
ATOM   3923  OD1 ASP B  50       6.595   7.350 -17.895  1.00109.23           O  
ANISOU 3923  OD1 ASP B  50    15269  13553  12678     17    495    335       O  
ATOM   3924  OD2 ASP B  50       7.837   9.178 -17.806  1.00113.88           O  
ANISOU 3924  OD2 ASP B  50    15447  14405  13420    227    423    411       O  
ATOM   3925  N   LYS B  51       6.552  10.022 -21.205  1.00 80.92           N  
ANISOU 3925  N   LYS B  51    11002  10619   9127    -30    634    251       N  
ATOM   3926  CA  LYS B  51       5.226  10.420 -21.688  1.00 79.36           C  
ANISOU 3926  CA  LYS B  51    10765  10522   8865   -248    623    240       C  
ATOM   3927  C   LYS B  51       5.233  10.936 -23.132  1.00 81.34           C  
ANISOU 3927  C   LYS B  51    10946  10913   9044   -252    650    190       C  
ATOM   3928  O   LYS B  51       6.201  11.561 -23.574  1.00 81.36           O  
ANISOU 3928  O   LYS B  51    10840  11003   9068   -113    711    205       O  
ATOM   3929  CB  LYS B  51       4.620  11.506 -20.770  1.00 80.52           C  
ANISOU 3929  CB  LYS B  51    10741  10778   9076   -340    587    337       C  
ATOM   3930  CG  LYS B  51       4.612  11.162 -19.271  1.00 96.56           C  
ANISOU 3930  CG  LYS B  51    12880  12670  11138   -344    573    398       C  
ATOM   3931  CD  LYS B  51       3.380  10.367 -18.821  1.00109.29           C  
ANISOU 3931  CD  LYS B  51    14656  14153  12718   -552    607    372       C  
ATOM   3932  CE  LYS B  51       3.580   9.698 -17.478  1.00122.42           C  
ANISOU 3932  CE  LYS B  51    16549  15611  14355   -534    617    425       C  
ATOM   3933  NZ  LYS B  51       3.706  10.679 -16.365  1.00132.88           N  
ANISOU 3933  NZ  LYS B  51    17794  16990  15703   -504    603    521       N  
ATOM   3934  N   SER B  52       4.114  10.687 -23.843  1.00 76.18           N  
ANISOU 3934  N   SER B  52    10364  10270   8309   -425    600    130       N  
ATOM   3935  CA  SER B  52       3.825  11.106 -25.218  1.00 75.24           C  
ANISOU 3935  CA  SER B  52    10253  10259   8077   -467    575     81       C  
ATOM   3936  C   SER B  52       3.763  12.639 -25.304  1.00 76.42           C  
ANISOU 3936  C   SER B  52    10174  10603   8261   -462    547    176       C  
ATOM   3937  O   SER B  52       3.304  13.258 -24.347  1.00 74.68           O  
ANISOU 3937  O   SER B  52     9791  10431   8153   -511    507    252       O  
ATOM   3938  CB  SER B  52       2.493  10.499 -25.669  1.00 78.19           C  
ANISOU 3938  CB  SER B  52    10735  10578   8396   -672    461     -1       C  
ATOM   3939  OG  SER B  52       1.909  11.148 -26.789  1.00 81.81           O  
ANISOU 3939  OG  SER B  52    11179  11150   8756   -741    359    -27       O  
ATOM   3940  N   PRO B  53       4.177  13.294 -26.416  1.00 72.54           N  
ANISOU 3940  N   PRO B  53     9691  10209   7664   -410    578    175       N  
ATOM   3941  CA  PRO B  53       4.059  14.769 -26.470  1.00 70.76           C  
ANISOU 3941  CA  PRO B  53     9274  10142   7469   -414    542    275       C  
ATOM   3942  C   PRO B  53       2.598  15.232 -26.583  1.00 73.44           C  
ANISOU 3942  C   PRO B  53     9544  10541   7818   -572    362    284       C  
ATOM   3943  O   PRO B  53       2.290  16.378 -26.253  1.00 71.60           O  
ANISOU 3943  O   PRO B  53     9130  10413   7664   -581    312    369       O  
ATOM   3944  CB  PRO B  53       4.879  15.166 -27.704  1.00 73.30           C  
ANISOU 3944  CB  PRO B  53     9693  10510   7648   -331    649    264       C  
ATOM   3945  CG  PRO B  53       5.515  13.907 -28.209  1.00 79.08           C  
ANISOU 3945  CG  PRO B  53    10643  11112   8292   -265    763    150       C  
ATOM   3946  CD  PRO B  53       4.754  12.753 -27.663  1.00 75.25           C  
ANISOU 3946  CD  PRO B  53    10249  10504   7841   -350    664     85       C  
ATOM   3947  N   ASP B  54       1.699  14.323 -27.003  1.00 71.00           N  
ANISOU 3947  N   ASP B  54     9365  10155   7457   -694    257    188       N  
ATOM   3948  CA  ASP B  54       0.266  14.588 -27.146  1.00 71.27           C  
ANISOU 3948  CA  ASP B  54     9303  10227   7550   -849     64    168       C  
ATOM   3949  C   ASP B  54      -0.522  14.072 -25.913  1.00 74.17           C  
ANISOU 3949  C   ASP B  54     9543  10528   8109   -967     72    155       C  
ATOM   3950  O   ASP B  54      -1.759  14.158 -25.892  1.00 74.31           O  
ANISOU 3950  O   ASP B  54     9433  10562   8239  -1110    -58    120       O  
ATOM   3951  CB  ASP B  54      -0.274  13.976 -28.460  1.00 75.16           C  
ANISOU 3951  CB  ASP B  54    10011  10669   7878   -932    -84     57       C  
ATOM   3952  CG  ASP B  54       0.361  14.532 -29.724  1.00 84.35           C  
ANISOU 3952  CG  ASP B  54    11353  11883   8812   -841    -86     70       C  
ATOM   3953  OD1 ASP B  54       0.763  13.725 -30.589  1.00 87.45           O  
ANISOU 3953  OD1 ASP B  54    12024  12188   9015   -825    -44    -20       O  
ATOM   3954  OD2 ASP B  54       0.454  15.773 -29.848  1.00 87.97           O  
ANISOU 3954  OD2 ASP B  54    11700  12453   9270   -791   -116    168       O  
ATOM   3955  N   SER B  55       0.202  13.582 -24.873  1.00 69.23           N  
ANISOU 3955  N   SER B  55     8954   9821   7530   -904    227    185       N  
ATOM   3956  CA  SER B  55      -0.385  13.111 -23.615  1.00 68.79           C  
ANISOU 3956  CA  SER B  55     8850   9677   7612  -1007    283    189       C  
ATOM   3957  C   SER B  55      -1.025  14.296 -22.847  1.00 74.14           C  
ANISOU 3957  C   SER B  55     9270  10461   8439  -1045    278    264       C  
ATOM   3958  O   SER B  55      -0.565  15.434 -23.023  1.00 73.00           O  
ANISOU 3958  O   SER B  55     9014  10440   8285   -937    260    337       O  
ATOM   3959  CB  SER B  55       0.662  12.407 -22.752  1.00 69.63           C  
ANISOU 3959  CB  SER B  55     9105   9657   7693   -897    413    218       C  
ATOM   3960  OG  SER B  55       1.600  13.302 -22.176  1.00 71.04           O  
ANISOU 3960  OG  SER B  55     9184   9913   7896   -742    464    315       O  
ATOM   3961  N   PRO B  56      -2.074  14.067 -22.007  1.00 71.87           N  
ANISOU 3961  N   PRO B  56     8893  10118   8296  -1201    317    242       N  
ATOM   3962  CA  PRO B  56      -2.711  15.193 -21.291  1.00 71.25           C  
ANISOU 3962  CA  PRO B  56     8573  10129   8369  -1227    344    296       C  
ATOM   3963  C   PRO B  56      -1.766  16.015 -20.404  1.00 73.33           C  
ANISOU 3963  C   PRO B  56     8829  10428   8605  -1080    437    403       C  
ATOM   3964  O   PRO B  56      -1.987  17.217 -20.270  1.00 72.16           O  
ANISOU 3964  O   PRO B  56     8500  10389   8530  -1040    413    453       O  
ATOM   3965  CB  PRO B  56      -3.779  14.505 -20.429  1.00 74.35           C  
ANISOU 3965  CB  PRO B  56     8938  10407   8904  -1422    451    241       C  
ATOM   3966  CG  PRO B  56      -4.065  13.238 -21.118  1.00 80.35           C  
ANISOU 3966  CG  PRO B  56     9849  11059   9621  -1535    392    141       C  
ATOM   3967  CD  PRO B  56      -2.758  12.794 -21.700  1.00 75.09           C  
ANISOU 3967  CD  PRO B  56     9420  10366   8746  -1370    365    159       C  
ATOM   3968  N   GLU B  57      -0.730  15.376 -19.806  1.00 69.35           N  
ANISOU 3968  N   GLU B  57     8524   9821   8006   -994    518    433       N  
ATOM   3969  CA  GLU B  57       0.252  16.022 -18.922  1.00 67.74           C  
ANISOU 3969  CA  GLU B  57     8332   9627   7781   -856    565    522       C  
ATOM   3970  C   GLU B  57       1.102  17.026 -19.693  1.00 68.53           C  
ANISOU 3970  C   GLU B  57     8323   9863   7852   -714    498    567       C  
ATOM   3971  O   GLU B  57       1.370  18.124 -19.197  1.00 65.30           O  
ANISOU 3971  O   GLU B  57     7799   9523   7488   -656    502    634       O  
ATOM   3972  CB  GLU B  57       1.165  14.982 -18.242  1.00 69.67           C  
ANISOU 3972  CB  GLU B  57     8819   9709   7944   -784    610    531       C  
ATOM   3973  CG  GLU B  57       0.464  14.070 -17.246  1.00 80.24           C  
ANISOU 3973  CG  GLU B  57    10327  10878   9283   -923    705    513       C  
ATOM   3974  CD  GLU B  57       0.374  12.612 -17.660  1.00 98.44           C  
ANISOU 3974  CD  GLU B  57    12838  13032  11532   -985    711    442       C  
ATOM   3975  OE1 GLU B  57      -0.035  12.338 -18.814  1.00 99.91           O  
ANISOU 3975  OE1 GLU B  57    12967  13267  11727  -1045    654    367       O  
ATOM   3976  OE2 GLU B  57       0.682  11.740 -16.815  1.00 79.61           O  
ANISOU 3976  OE2 GLU B  57    10702  10463   9085   -977    762    460       O  
ATOM   3977  N   MET B  58       1.512  16.646 -20.913  1.00 66.14           N  
ANISOU 3977  N   MET B  58     8080   9585   7467   -669    453    526       N  
ATOM   3978  CA  MET B  58       2.316  17.484 -21.804  1.00 64.88           C  
ANISOU 3978  CA  MET B  58     7858   9535   7260   -557    432    562       C  
ATOM   3979  C   MET B  58       1.468  18.620 -22.363  1.00 66.56           C  
ANISOU 3979  C   MET B  58     7921   9867   7501   -611    347    590       C  
ATOM   3980  O   MET B  58       1.937  19.758 -22.415  1.00 65.05           O  
ANISOU 3980  O   MET B  58     7635   9758   7323   -539    348    661       O  
ATOM   3981  CB  MET B  58       2.939  16.648 -22.930  1.00 68.39           C  
ANISOU 3981  CB  MET B  58     8459   9942   7584   -504    450    498       C  
ATOM   3982  CG  MET B  58       4.157  15.851 -22.489  1.00 72.71           C  
ANISOU 3982  CG  MET B  58     9106  10388   8134   -376    533    486       C  
ATOM   3983  SD  MET B  58       5.569  16.857 -21.946  1.00 76.49           S  
ANISOU 3983  SD  MET B  58     9428  10928   8706   -217    580    570       S  
ATOM   3984  CE  MET B  58       6.061  17.629 -23.507  1.00 73.74           C  
ANISOU 3984  CE  MET B  58     9046  10694   8276   -179    649    565       C  
ATOM   3985  N   LYS B  59       0.205  18.328 -22.721  1.00 63.46           N  
ANISOU 3985  N   LYS B  59     7499   9472   7142   -738    260    531       N  
ATOM   3986  CA  LYS B  59      -0.721  19.339 -23.230  1.00 63.37           C  
ANISOU 3986  CA  LYS B  59     7334   9554   7191   -777    135    547       C  
ATOM   3987  C   LYS B  59      -1.046  20.363 -22.130  1.00 65.08           C  
ANISOU 3987  C   LYS B  59     7364   9806   7557   -768    181    609       C  
ATOM   3988  O   LYS B  59      -1.052  21.563 -22.419  1.00 64.51           O  
ANISOU 3988  O   LYS B  59     7191   9813   7507   -710    119    668       O  
ATOM   3989  CB  LYS B  59      -1.998  18.700 -23.799  1.00 67.87           C  
ANISOU 3989  CB  LYS B  59     7883  10096   7808   -916      4    451       C  
ATOM   3990  CG  LYS B  59      -1.762  17.956 -25.111  1.00 81.79           C  
ANISOU 3990  CG  LYS B  59     9851  11832   9392   -922    -90    387       C  
ATOM   3991  CD  LYS B  59      -3.064  17.582 -25.796  1.00 96.08           C  
ANISOU 3991  CD  LYS B  59    11615  13631  11259  -1054   -296    296       C  
ATOM   3992  CE  LYS B  59      -2.840  17.177 -27.237  1.00112.25           C  
ANISOU 3992  CE  LYS B  59    13906  15659  13085  -1046   -428    241       C  
ATOM   3993  NZ  LYS B  59      -4.101  17.208 -28.029  1.00124.38           N  
ANISOU 3993  NZ  LYS B  59    15386  17200  14672  -1153   -709    166       N  
ATOM   3994  N   ASP B  60      -1.232  19.904 -20.862  1.00 59.97           N  
ANISOU 3994  N   ASP B  60     6714   9082   6990   -819    301    597       N  
ATOM   3995  CA  ASP B  60      -1.498  20.804 -19.732  1.00 58.94           C  
ANISOU 3995  CA  ASP B  60     6460   8961   6973   -813    377    642       C  
ATOM   3996  C   ASP B  60      -0.261  21.654 -19.449  1.00 62.30           C  
ANISOU 3996  C   ASP B  60     6912   9421   7338   -679    399    729       C  
ATOM   3997  O   ASP B  60      -0.394  22.860 -19.248  1.00 61.92           O  
ANISOU 3997  O   ASP B  60     6743   9426   7356   -641    386    776       O  
ATOM   3998  CB  ASP B  60      -1.953  20.039 -18.469  1.00 61.07           C  
ANISOU 3998  CB  ASP B  60     6794   9115   7295   -913    524    607       C  
ATOM   3999  CG  ASP B  60      -2.442  20.931 -17.332  1.00 68.72           C  
ANISOU 3999  CG  ASP B  60     7659  10079   8373   -929    632    631       C  
ATOM   4000  OD1 ASP B  60      -1.772  20.970 -16.275  1.00 68.70           O  
ANISOU 4000  OD1 ASP B  60     7794  10008   8301   -887    724    674       O  
ATOM   4001  OD2 ASP B  60      -3.489  21.602 -17.506  1.00 74.21           O  
ANISOU 4001  OD2 ASP B  60     8143  10828   9226   -974    613    600       O  
ATOM   4002  N   PHE B  61       0.942  21.038 -19.504  1.00 58.84           N  
ANISOU 4002  N   PHE B  61     6617   8944   6796   -604    424    742       N  
ATOM   4003  CA  PHE B  61       2.220  21.721 -19.319  1.00 57.92           C  
ANISOU 4003  CA  PHE B  61     6498   8851   6658   -486    435    807       C  
ATOM   4004  C   PHE B  61       2.348  22.904 -20.292  1.00 63.31           C  
ANISOU 4004  C   PHE B  61     7078   9640   7337   -446    382    854       C  
ATOM   4005  O   PHE B  61       2.609  24.032 -19.861  1.00 62.80           O  
ANISOU 4005  O   PHE B  61     6931   9605   7326   -407    383    913       O  
ATOM   4006  CB  PHE B  61       3.390  20.737 -19.506  1.00 59.76           C  
ANISOU 4006  CB  PHE B  61     6860   9022   6823   -409    460    787       C  
ATOM   4007  CG  PHE B  61       4.746  21.401 -19.577  1.00 60.91           C  
ANISOU 4007  CG  PHE B  61     6951   9203   6990   -292    467    833       C  
ATOM   4008  CD1 PHE B  61       5.326  21.959 -18.442  1.00 63.07           C  
ANISOU 4008  CD1 PHE B  61     7190   9444   7328   -244    450    876       C  
ATOM   4009  CD2 PHE B  61       5.422  21.509 -20.785  1.00 63.32           C  
ANISOU 4009  CD2 PHE B  61     7243   9561   7253   -243    499    828       C  
ATOM   4010  CE1 PHE B  61       6.568  22.584 -18.509  1.00 63.77           C  
ANISOU 4010  CE1 PHE B  61     7191   9559   7478   -155    444    907       C  
ATOM   4011  CE2 PHE B  61       6.661  22.149 -20.853  1.00 66.35           C  
ANISOU 4011  CE2 PHE B  61     7543   9972   7696   -157    540    862       C  
ATOM   4012  CZ  PHE B  61       7.234  22.666 -19.713  1.00 63.87           C  
ANISOU 4012  CZ  PHE B  61     7154   9630   7485   -116    502    898       C  
ATOM   4013  N   ARG B  62       2.140  22.634 -21.597  1.00 60.57           N  
ANISOU 4013  N   ARG B  62     6774   9330   6910   -462    332    828       N  
ATOM   4014  CA  ARG B  62       2.201  23.623 -22.671  1.00 60.74           C  
ANISOU 4014  CA  ARG B  62     6776   9426   6879   -433    277    876       C  
ATOM   4015  C   ARG B  62       1.103  24.672 -22.529  1.00 66.23           C  
ANISOU 4015  C   ARG B  62     7340  10158   7668   -461    181    907       C  
ATOM   4016  O   ARG B  62       1.349  25.842 -22.806  1.00 65.94           O  
ANISOU 4016  O   ARG B  62     7267  10155   7632   -415    158    979       O  
ATOM   4017  CB  ARG B  62       2.117  22.943 -24.047  1.00 60.05           C  
ANISOU 4017  CB  ARG B  62     6832   9340   6643   -452    233    829       C  
ATOM   4018  CG  ARG B  62       3.380  22.150 -24.410  1.00 59.94           C  
ANISOU 4018  CG  ARG B  62     6947   9291   6538   -392    360    801       C  
ATOM   4019  CD  ARG B  62       3.467  21.790 -25.882  1.00 63.54           C  
ANISOU 4019  CD  ARG B  62     7585   9748   6811   -398    352    764       C  
ATOM   4020  NE  ARG B  62       2.345  20.963 -26.333  1.00 71.26           N  
ANISOU 4020  NE  ARG B  62     8649  10692   7732   -484    219    683       N  
ATOM   4021  CZ  ARG B  62       2.359  19.636 -26.399  1.00 78.13           C  
ANISOU 4021  CZ  ARG B  62     9640  11486   8559   -509    248    591       C  
ATOM   4022  NH1 ARG B  62       3.448  18.960 -26.062  1.00 62.77           N  
ANISOU 4022  NH1 ARG B  62     7745   9487   6619   -432    403    570       N  
ATOM   4023  NH2 ARG B  62       1.285  18.976 -26.805  1.00 66.97           N  
ANISOU 4023  NH2 ARG B  62     8292  10037   7116   -610    110    514       N  
ATOM   4024  N   HIS B  63      -0.088  24.265 -22.063  1.00 64.76           N  
ANISOU 4024  N   HIS B  63     7074   9950   7582   -536    139    849       N  
ATOM   4025  CA  HIS B  63      -1.218  25.176 -21.874  1.00 65.44           C  
ANISOU 4025  CA  HIS B  63     6993  10060   7811   -550     59    855       C  
ATOM   4026  C   HIS B  63      -0.928  26.258 -20.812  1.00 68.13           C  
ANISOU 4026  C   HIS B  63     7255  10394   8238   -499    145    912       C  
ATOM   4027  O   HIS B  63      -1.266  27.425 -21.041  1.00 67.57           O  
ANISOU 4027  O   HIS B  63     7097  10347   8232   -453     76    956       O  
ATOM   4028  CB  HIS B  63      -2.503  24.416 -21.521  1.00 67.36           C  
ANISOU 4028  CB  HIS B  63     7134  10272   8187   -656     41    761       C  
ATOM   4029  CG  HIS B  63      -3.692  25.317 -21.433  1.00 72.00           C  
ANISOU 4029  CG  HIS B  63     7508  10882   8969   -658    -41    747       C  
ATOM   4030  ND1 HIS B  63      -4.077  26.109 -22.504  1.00 74.92           N  
ANISOU 4030  ND1 HIS B  63     7830  11293   9343   -602   -247    776       N  
ATOM   4031  CD2 HIS B  63      -4.512  25.563 -20.389  1.00 74.29           C  
ANISOU 4031  CD2 HIS B  63     7633  11141   9453   -697     65    708       C  
ATOM   4032  CE1 HIS B  63      -5.126  26.792 -22.080  1.00 75.37           C  
ANISOU 4032  CE1 HIS B  63     7664  11347   9625   -595   -281    748       C  
ATOM   4033  NE2 HIS B  63      -5.429  26.490 -20.818  1.00 75.42           N  
ANISOU 4033  NE2 HIS B  63     7583  11314   9759   -655    -76    700       N  
ATOM   4034  N   GLY B  64      -0.299  25.865 -19.695  1.00 63.00           N  
ANISOU 4034  N   GLY B  64     6664   9693   7578   -502    275    909       N  
ATOM   4035  CA  GLY B  64       0.098  26.771 -18.618  1.00 61.96           C  
ANISOU 4035  CA  GLY B  64     6512   9535   7495   -461    344    952       C  
ATOM   4036  C   GLY B  64       0.994  27.903 -19.100  1.00 65.97           C  
ANISOU 4036  C   GLY B  64     7015  10079   7971   -385    301   1032       C  
ATOM   4037  O   GLY B  64       0.912  29.024 -18.589  1.00 66.32           O  
ANISOU 4037  O   GLY B  64     7005  10110   8085   -356    305   1066       O  
ATOM   4038  N   PHE B  65       1.833  27.629 -20.116  1.00 61.56           N  
ANISOU 4038  N   PHE B  65     6526   9553   7310   -362    279   1057       N  
ATOM   4039  CA  PHE B  65       2.690  28.642 -20.717  1.00 61.22           C  
ANISOU 4039  CA  PHE B  65     6491   9533   7235   -316    274   1133       C  
ATOM   4040  C   PHE B  65       1.906  29.508 -21.712  1.00 66.63           C  
ANISOU 4040  C   PHE B  65     7165  10246   7906   -308    170   1175       C  
ATOM   4041  O   PHE B  65       2.270  30.671 -21.885  1.00 66.35           O  
ANISOU 4041  O   PHE B  65     7129  10202   7880   -279    164   1247       O  
ATOM   4042  CB  PHE B  65       3.916  28.019 -21.385  1.00 62.65           C  
ANISOU 4042  CB  PHE B  65     6752   9725   7326   -298    340   1134       C  
ATOM   4043  CG  PHE B  65       4.995  27.673 -20.399  1.00 63.15           C  
ANISOU 4043  CG  PHE B  65     6797   9749   7447   -269    403   1119       C  
ATOM   4044  CD1 PHE B  65       5.782  28.667 -19.828  1.00 65.99           C  
ANISOU 4044  CD1 PHE B  65     7094  10093   7888   -250    413   1164       C  
ATOM   4045  CD2 PHE B  65       5.222  26.353 -20.030  1.00 65.00           C  
ANISOU 4045  CD2 PHE B  65     7089   9947   7662   -260    425   1057       C  
ATOM   4046  CE1 PHE B  65       6.781  28.344 -18.904  1.00 66.70           C  
ANISOU 4046  CE1 PHE B  65     7162  10136   8045   -217    417   1143       C  
ATOM   4047  CE2 PHE B  65       6.231  26.030 -19.123  1.00 67.27           C  
ANISOU 4047  CE2 PHE B  65     7372  10179   8007   -213    435   1046       C  
ATOM   4048  CZ  PHE B  65       6.996  27.026 -18.556  1.00 65.35           C  
ANISOU 4048  CZ  PHE B  65     7051   9928   7851   -190    416   1086       C  
ATOM   4049  N   ASP B  66       0.836  28.960 -22.349  1.00 64.03           N  
ANISOU 4049  N   ASP B  66     6834   9934   7561   -335     69   1129       N  
ATOM   4050  CA  ASP B  66      -0.033  29.725 -23.258  1.00 65.14           C  
ANISOU 4050  CA  ASP B  66     6967  10084   7701   -312    -92   1162       C  
ATOM   4051  C   ASP B  66      -0.727  30.836 -22.467  1.00 69.02           C  
ANISOU 4051  C   ASP B  66     7311  10550   8365   -272   -122   1181       C  
ATOM   4052  O   ASP B  66      -0.728  31.986 -22.906  1.00 70.33           O  
ANISOU 4052  O   ASP B  66     7502  10695   8526   -217   -199   1255       O  
ATOM   4053  CB  ASP B  66      -1.076  28.827 -23.960  1.00 67.96           C  
ANISOU 4053  CB  ASP B  66     7322  10454   8045   -355   -232   1086       C  
ATOM   4054  CG  ASP B  66      -0.542  27.882 -25.024  1.00 76.00           C  
ANISOU 4054  CG  ASP B  66     8534  11480   8861   -384   -238   1064       C  
ATOM   4055  OD1 ASP B  66       0.437  28.256 -25.724  1.00 75.84           O  
ANISOU 4055  OD1 ASP B  66     8670  11460   8685   -354   -179   1130       O  
ATOM   4056  OD2 ASP B  66      -1.136  26.787 -25.196  1.00 79.73           O  
ANISOU 4056  OD2 ASP B  66     9011  11948   9335   -445   -291    975       O  
ATOM   4057  N   ILE B  67      -1.266  30.494 -21.276  1.00 63.77           N  
ANISOU 4057  N   ILE B  67     6524   9868   7840   -299    -37   1113       N  
ATOM   4058  CA  ILE B  67      -1.896  31.428 -20.334  1.00 62.98           C  
ANISOU 4058  CA  ILE B  67     6295   9728   7907   -263     -5   1106       C  
ATOM   4059  C   ILE B  67      -0.852  32.493 -19.929  1.00 66.33           C  
ANISOU 4059  C   ILE B  67     6795  10118   8291   -219     56   1185       C  
ATOM   4060  O   ILE B  67      -1.142  33.694 -19.987  1.00 67.24           O  
ANISOU 4060  O   ILE B  67     6876  10197   8476   -158      2   1229       O  
ATOM   4061  CB  ILE B  67      -2.473  30.675 -19.093  1.00 65.48           C  
ANISOU 4061  CB  ILE B  67     6532  10017   8332   -325    137   1013       C  
ATOM   4062  CG1 ILE B  67      -3.600  29.679 -19.490  1.00 67.14           C  
ANISOU 4062  CG1 ILE B  67     6640  10247   8622   -395     84    926       C  
ATOM   4063  CG2 ILE B  67      -2.971  31.656 -18.023  1.00 66.27           C  
ANISOU 4063  CG2 ILE B  67     6536  10061   8583   -286    225    996       C  
ATOM   4064  CD1 ILE B  67      -3.908  28.573 -18.431  1.00 75.42           C  
ANISOU 4064  CD1 ILE B  67     7689  11255   9711   -497    261    844       C  
ATOM   4065  N   LEU B  68       0.374  32.034 -19.572  1.00 60.07           N  
ANISOU 4065  N   LEU B  68     6098   9325   7399   -248    151   1199       N  
ATOM   4066  CA  LEU B  68       1.485  32.873 -19.134  1.00 58.54           C  
ANISOU 4066  CA  LEU B  68     5955   9096   7190   -231    200   1255       C  
ATOM   4067  C   LEU B  68       1.915  33.867 -20.217  1.00 62.05           C  
ANISOU 4067  C   LEU B  68     6451   9540   7584   -206    142   1347       C  
ATOM   4068  O   LEU B  68       2.078  35.040 -19.904  1.00 62.15           O  
ANISOU 4068  O   LEU B  68     6466   9498   7652   -182    139   1393       O  
ATOM   4069  CB  LEU B  68       2.680  32.010 -18.687  1.00 57.53           C  
ANISOU 4069  CB  LEU B  68     5887   8971   7000   -259    273   1236       C  
ATOM   4070  CG  LEU B  68       3.705  32.687 -17.753  1.00 60.70           C  
ANISOU 4070  CG  LEU B  68     6306   9318   7438   -254    302   1256       C  
ATOM   4071  CD1 LEU B  68       3.200  32.752 -16.312  1.00 59.88           C  
ANISOU 4071  CD1 LEU B  68     6228   9149   7376   -258    332   1203       C  
ATOM   4072  CD2 LEU B  68       5.033  31.964 -17.794  1.00 61.78           C  
ANISOU 4072  CD2 LEU B  68     6465   9467   7544   -260    326   1252       C  
ATOM   4073  N   VAL B  69       2.053  33.416 -21.479  1.00 58.97           N  
ANISOU 4073  N   VAL B  69     6138   9193   7077   -216    104   1372       N  
ATOM   4074  CA  VAL B  69       2.459  34.251 -22.618  1.00 59.78           C  
ANISOU 4074  CA  VAL B  69     6354   9276   7082   -207     73   1466       C  
ATOM   4075  C   VAL B  69       1.395  35.344 -22.877  1.00 66.58           C  
ANISOU 4075  C   VAL B  69     7209  10088   8000   -147    -73   1510       C  
ATOM   4076  O   VAL B  69       1.765  36.500 -23.117  1.00 68.16           O  
ANISOU 4076  O   VAL B  69     7484  10223   8189   -131    -75   1595       O  
ATOM   4077  CB  VAL B  69       2.790  33.417 -23.888  1.00 63.99           C  
ANISOU 4077  CB  VAL B  69     7022   9851   7442   -233     82   1468       C  
ATOM   4078  CG1 VAL B  69       2.986  34.313 -25.117  1.00 65.59           C  
ANISOU 4078  CG1 VAL B  69     7404  10012   7504   -228     43   1569       C  
ATOM   4079  CG2 VAL B  69       4.034  32.555 -23.665  1.00 62.64           C  
ANISOU 4079  CG2 VAL B  69     6850   9705   7246   -269    248   1433       C  
ATOM   4080  N   GLY B  70       0.113  34.978 -22.772  1.00 63.18           N  
ANISOU 4080  N   GLY B  70     6674   9675   7656   -114   -187   1447       N  
ATOM   4081  CA  GLY B  70      -1.011  35.898 -22.914  1.00 63.94           C  
ANISOU 4081  CA  GLY B  70     6707   9720   7867    -32   -345   1463       C  
ATOM   4082  C   GLY B  70      -0.974  36.985 -21.856  1.00 67.21           C  
ANISOU 4082  C   GLY B  70     7052  10062   8421      9   -273   1473       C  
ATOM   4083  O   GLY B  70      -1.121  38.170 -22.168  1.00 68.64           O  
ANISOU 4083  O   GLY B  70     7289  10163   8627     76   -357   1545       O  
ATOM   4084  N   GLN B  71      -0.702  36.586 -20.607  1.00 61.59           N  
ANISOU 4084  N   GLN B  71     6264   9359   7777    -32   -119   1404       N  
ATOM   4085  CA  GLN B  71      -0.574  37.495 -19.472  1.00 60.85           C  
ANISOU 4085  CA  GLN B  71     6148   9188   7785     -7    -34   1395       C  
ATOM   4086  C   GLN B  71       0.676  38.365 -19.589  1.00 65.06           C  
ANISOU 4086  C   GLN B  71     6813   9667   8241    -32     -1   1483       C  
ATOM   4087  O   GLN B  71       0.631  39.510 -19.139  1.00 66.25           O  
ANISOU 4087  O   GLN B  71     6983   9722   8465      7     -3   1506       O  
ATOM   4088  CB  GLN B  71      -0.526  36.723 -18.163  1.00 60.80           C  
ANISOU 4088  CB  GLN B  71     6095   9191   7814    -56    109   1301       C  
ATOM   4089  CG  GLN B  71      -1.821  36.098 -17.713  1.00 64.51           C  
ANISOU 4089  CG  GLN B  71     6424   9674   8413    -48    144   1202       C  
ATOM   4090  CD  GLN B  71      -1.552  35.430 -16.393  1.00 78.57           C  
ANISOU 4090  CD  GLN B  71     8247  11437  10170   -112    310   1131       C  
ATOM   4091  OE1 GLN B  71      -1.896  35.939 -15.325  1.00 74.39           O  
ANISOU 4091  OE1 GLN B  71     7718  10833   9712    -97    421   1080       O  
ATOM   4092  NE2 GLN B  71      -0.803  34.348 -16.433  1.00 67.35           N  
ANISOU 4092  NE2 GLN B  71     6902  10063   8626   -178    329   1132       N  
ATOM   4093  N   ILE B  72       1.792  37.829 -20.166  1.00 60.40           N  
ANISOU 4093  N   ILE B  72     6301   9126   7523   -103     45   1522       N  
ATOM   4094  CA  ILE B  72       3.020  38.607 -20.407  1.00 60.93           C  
ANISOU 4094  CA  ILE B  72     6460   9142   7547   -151    100   1600       C  
ATOM   4095  C   ILE B  72       2.693  39.685 -21.471  1.00 68.50           C  
ANISOU 4095  C   ILE B  72     7537  10030   8461   -113     15   1704       C  
ATOM   4096  O   ILE B  72       3.117  40.837 -21.331  1.00 68.99           O  
ANISOU 4096  O   ILE B  72     7664   9991   8559   -124     32   1762       O  
ATOM   4097  CB  ILE B  72       4.258  37.734 -20.800  1.00 62.76           C  
ANISOU 4097  CB  ILE B  72     6711   9440   7693   -227    199   1601       C  
ATOM   4098  CG1 ILE B  72       4.890  37.074 -19.558  1.00 61.04           C  
ANISOU 4098  CG1 ILE B  72     6410   9240   7542   -254    255   1519       C  
ATOM   4099  CG2 ILE B  72       5.333  38.560 -21.534  1.00 63.60           C  
ANISOU 4099  CG2 ILE B  72     6907   9496   7762   -288    273   1691       C  
ATOM   4100  CD1 ILE B  72       5.533  35.694 -19.805  1.00 58.73           C  
ANISOU 4100  CD1 ILE B  72     6097   9025   7194   -278    311   1476       C  
ATOM   4101  N   ASP B  73       1.916  39.300 -22.507  1.00 66.56           N  
ANISOU 4101  N   ASP B  73     7339   9818   8132    -70    -98   1725       N  
ATOM   4102  CA  ASP B  73       1.480  40.184 -23.584  1.00 68.59           C  
ANISOU 4102  CA  ASP B  73     7752   9996   8315    -16   -231   1826       C  
ATOM   4103  C   ASP B  73       0.538  41.271 -23.049  1.00 72.35           C  
ANISOU 4103  C   ASP B  73     8167  10370   8952     92   -345   1827       C  
ATOM   4104  O   ASP B  73       0.657  42.430 -23.455  1.00 73.02           O  
ANISOU 4104  O   ASP B  73     8399  10333   9014    125   -398   1924       O  
ATOM   4105  CB  ASP B  73       0.819  39.378 -24.717  1.00 71.63           C  
ANISOU 4105  CB  ASP B  73     8208  10439   8570      9   -370   1825       C  
ATOM   4106  CG  ASP B  73       1.816  38.606 -25.574  1.00 80.81           C  
ANISOU 4106  CG  ASP B  73     9519  11657   9529    -85   -248   1847       C  
ATOM   4107  OD1 ASP B  73       3.010  38.986 -25.589  1.00 80.85           O  
ANISOU 4107  OD1 ASP B  73     9602  11629   9487   -161    -71   1901       O  
ATOM   4108  OD2 ASP B  73       1.397  37.635 -26.246  1.00 86.66           O  
ANISOU 4108  OD2 ASP B  73    10294  12463  10171    -85   -323   1803       O  
ATOM   4109  N   ASP B  74      -0.346  40.912 -22.104  1.00 67.80           N  
ANISOU 4109  N   ASP B  74     7389   9829   8545    145   -354   1716       N  
ATOM   4110  CA  ASP B  74      -1.245  41.869 -21.469  1.00 68.94           C  
ANISOU 4110  CA  ASP B  74     7443   9875   8876    256   -412   1686       C  
ATOM   4111  C   ASP B  74      -0.416  42.895 -20.681  1.00 71.77           C  
ANISOU 4111  C   ASP B  74     7882  10127   9262    227   -293   1714       C  
ATOM   4112  O   ASP B  74      -0.680  44.095 -20.771  1.00 73.72           O  
ANISOU 4112  O   ASP B  74     8196  10239   9575    308   -362   1762       O  
ATOM   4113  CB  ASP B  74      -2.267  41.157 -20.557  1.00 71.03           C  
ANISOU 4113  CB  ASP B  74     7474  10200   9315    289   -372   1546       C  
ATOM   4114  CG  ASP B  74      -3.291  40.267 -21.255  1.00 84.59           C  
ANISOU 4114  CG  ASP B  74     9067  11996  11079    322   -520   1499       C  
ATOM   4115  OD1 ASP B  74      -3.558  40.490 -22.461  1.00 86.52           O  
ANISOU 4115  OD1 ASP B  74     9406  12219  11247    373   -725   1573       O  
ATOM   4116  OD2 ASP B  74      -3.850  39.364 -20.584  1.00 90.56           O  
ANISOU 4116  OD2 ASP B  74     9646  12817  11945    291   -438   1384       O  
ATOM   4117  N   ALA B  75       0.618  42.424 -19.960  1.00 64.97           N  
ANISOU 4117  N   ALA B  75     7023   9312   8353    112   -140   1682       N  
ATOM   4118  CA  ALA B  75       1.524  43.279 -19.194  1.00 63.93           C  
ANISOU 4118  CA  ALA B  75     6962   9081   8246     58    -52   1693       C  
ATOM   4119  C   ALA B  75       2.380  44.164 -20.134  1.00 67.60           C  
ANISOU 4119  C   ALA B  75     7599   9462   8626      0    -62   1823       C  
ATOM   4120  O   ALA B  75       2.681  45.312 -19.797  1.00 67.63           O  
ANISOU 4120  O   ALA B  75     7688   9327   8682    -10    -50   1856       O  
ATOM   4121  CB  ALA B  75       2.411  42.429 -18.298  1.00 62.95           C  
ANISOU 4121  CB  ALA B  75     6788   9029   8102    -41     61   1620       C  
ATOM   4122  N   LEU B  76       2.725  43.647 -21.327  1.00 63.92           N  
ANISOU 4122  N   LEU B  76     7206   9061   8020    -43    -70   1894       N  
ATOM   4123  CA  LEU B  76       3.504  44.386 -22.314  1.00 64.59           C  
ANISOU 4123  CA  LEU B  76     7485   9061   7996   -115    -34   2021       C  
ATOM   4124  C   LEU B  76       2.717  45.557 -22.894  1.00 69.57           C  
ANISOU 4124  C   LEU B  76     8278   9537   8617    -14   -176   2115       C  
ATOM   4125  O   LEU B  76       3.313  46.621 -23.067  1.00 69.68           O  
ANISOU 4125  O   LEU B  76     8447   9409   8620    -71   -129   2200       O  
ATOM   4126  CB  LEU B  76       4.022  43.481 -23.434  1.00 64.76           C  
ANISOU 4126  CB  LEU B  76     7579   9180   7846   -182     25   2059       C  
ATOM   4127  CG  LEU B  76       5.418  42.881 -23.198  1.00 68.80           C  
ANISOU 4127  CG  LEU B  76     8018   9761   8363   -319    221   2026       C  
ATOM   4128  CD1 LEU B  76       5.719  41.762 -24.205  1.00 69.30           C  
ANISOU 4128  CD1 LEU B  76     8129   9931   8270   -351    289   2027       C  
ATOM   4129  CD2 LEU B  76       6.509  43.952 -23.227  1.00 70.36           C  
ANISOU 4129  CD2 LEU B  76     8300   9836   8600   -436    344   2099       C  
ATOM   4130  N   LYS B  77       1.378  45.403 -23.145  1.00 66.63           N  
ANISOU 4130  N   LYS B  77     7862   9177   8277    136   -360   2094       N  
ATOM   4131  CA  LYS B  77       0.587  46.521 -23.679  1.00 68.04           C  
ANISOU 4131  CA  LYS B  77     8184   9193   8473    266   -542   2178       C  
ATOM   4132  C   LYS B  77       0.439  47.626 -22.616  1.00 69.74           C  
ANISOU 4132  C   LYS B  77     8359   9267   8872    324   -517   2144       C  
ATOM   4133  O   LYS B  77       0.416  48.806 -22.974  1.00 71.36           O  
ANISOU 4133  O   LYS B  77     8754   9288   9071    373   -589   2240       O  
ATOM   4134  CB  LYS B  77      -0.768  46.098 -24.288  1.00 72.22           C  
ANISOU 4134  CB  LYS B  77     8650   9764   9027    417   -783   2156       C  
ATOM   4135  CG  LYS B  77      -1.772  45.443 -23.361  1.00 94.88           C  
ANISOU 4135  CG  LYS B  77    11203  12730  12117    502   -806   2000       C  
ATOM   4136  CD  LYS B  77      -2.885  44.766 -24.153  1.00110.10           C  
ANISOU 4136  CD  LYS B  77    13046  14720  14066    601  -1041   1972       C  
ATOM   4137  CE  LYS B  77      -3.831  43.996 -23.263  1.00123.06           C  
ANISOU 4137  CE  LYS B  77    14354  16462  15943    646  -1015   1810       C  
ATOM   4138  NZ  LYS B  77      -4.916  43.343 -24.041  1.00132.08           N  
ANISOU 4138  NZ  LYS B  77    15382  17663  17140    718  -1257   1769       N  
ATOM   4139  N   LEU B  78       0.439  47.249 -21.326  1.00 63.09           N  
ANISOU 4139  N   LEU B  78     7316   8491   8166    307   -402   2011       N  
ATOM   4140  CA  LEU B  78       0.394  48.194 -20.208  1.00 62.80           C  
ANISOU 4140  CA  LEU B  78     7266   8320   8274    344   -347   1954       C  
ATOM   4141  C   LEU B  78       1.744  48.937 -20.069  1.00 65.74           C  
ANISOU 4141  C   LEU B  78     7802   8588   8587    189   -237   2018       C  
ATOM   4142  O   LEU B  78       1.742  50.158 -19.931  1.00 66.28           O  
ANISOU 4142  O   LEU B  78     8005   8465   8711    220   -261   2057       O  
ATOM   4143  CB  LEU B  78       0.025  47.487 -18.889  1.00 61.36           C  
ANISOU 4143  CB  LEU B  78     6878   8230   8205    355   -244   1793       C  
ATOM   4144  CG  LEU B  78      -1.414  46.947 -18.765  1.00 66.28           C  
ANISOU 4144  CG  LEU B  78     7302   8916   8965    502   -307   1701       C  
ATOM   4145  CD1 LEU B  78      -1.502  45.890 -17.681  1.00 64.84           C  
ANISOU 4145  CD1 LEU B  78     6963   8858   8814    443   -157   1566       C  
ATOM   4146  CD2 LEU B  78      -2.416  48.069 -18.492  1.00 69.19           C  
ANISOU 4146  CD2 LEU B  78     7652   9117   9521    678   -369   1671       C  
ATOM   4147  N   ALA B  79       2.885  48.206 -20.126  1.00 60.40           N  
ANISOU 4147  N   ALA B  79     7102   8025   7823     22   -121   2021       N  
ATOM   4148  CA  ALA B  79       4.230  48.788 -20.040  1.00 60.39           C  
ANISOU 4148  CA  ALA B  79     7195   7942   7810   -148    -11   2067       C  
ATOM   4149  C   ALA B  79       4.474  49.773 -21.191  1.00 67.27           C  
ANISOU 4149  C   ALA B  79     8306   8659   8593   -184    -24   2224       C  
ATOM   4150  O   ALA B  79       4.966  50.877 -20.952  1.00 67.85           O  
ANISOU 4150  O   ALA B  79     8503   8557   8719   -254     11   2262       O  
ATOM   4151  CB  ALA B  79       5.281  47.692 -20.053  1.00 59.78           C  
ANISOU 4151  CB  ALA B  79     6999   8026   7688   -287    101   2032       C  
ATOM   4152  N   ASN B  80       4.043  49.404 -22.425  1.00 65.08           N  
ANISOU 4152  N   ASN B  80     8131   8425   8171   -131    -88   2313       N  
ATOM   4153  CA  ASN B  80       4.156  50.233 -23.633  1.00 66.63           C  
ANISOU 4153  CA  ASN B  80     8624   8464   8227   -151   -113   2476       C  
ATOM   4154  C   ASN B  80       3.245  51.466 -23.571  1.00 72.38           C  
ANISOU 4154  C   ASN B  80     9501   8977   9021      5   -282   2528       C  
ATOM   4155  O   ASN B  80       3.450  52.420 -24.329  1.00 75.01           O  
ANISOU 4155  O   ASN B  80    10122   9118   9259    -24   -297   2667       O  
ATOM   4156  CB  ASN B  80       3.864  49.404 -24.877  1.00 65.76           C  
ANISOU 4156  CB  ASN B  80     8613   8457   7918   -123   -167   2539       C  
ATOM   4157  CG  ASN B  80       4.964  48.413 -25.156  1.00 86.00           C  
ANISOU 4157  CG  ASN B  80    11114  11169  10394   -293     44   2518       C  
ATOM   4158  OD1 ASN B  80       6.142  48.763 -25.205  1.00 86.95           O  
ANISOU 4158  OD1 ASN B  80    11300  11229  10509   -466    243   2562       O  
ATOM   4159  ND2 ASN B  80       4.616  47.153 -25.327  1.00 73.26           N  
ANISOU 4159  ND2 ASN B  80     9359   9742   8734   -251     14   2442       N  
ATOM   4160  N   GLU B  81       2.269  51.461 -22.645  1.00 67.74           N  
ANISOU 4160  N   GLU B  81     8727   8406   8604    168   -388   2412       N  
ATOM   4161  CA  GLU B  81       1.366  52.580 -22.395  1.00 68.93           C  
ANISOU 4161  CA  GLU B  81     8959   8357   8876    346   -531   2421       C  
ATOM   4162  C   GLU B  81       1.960  53.486 -21.306  1.00 72.03           C  
ANISOU 4162  C   GLU B  81     9376   8602   9389    270   -413   2367       C  
ATOM   4163  O   GLU B  81       1.414  54.550 -21.020  1.00 74.29           O  
ANISOU 4163  O   GLU B  81     9765   8684   9777    395   -493   2372       O  
ATOM   4164  CB  GLU B  81      -0.032  52.073 -22.003  1.00 69.97           C  
ANISOU 4164  CB  GLU B  81     8852   8578   9156    560   -671   2306       C  
ATOM   4165  CG  GLU B  81      -0.933  51.835 -23.202  1.00 82.97           C  
ANISOU 4165  CG  GLU B  81    10559  10234  10732    704   -907   2384       C  
ATOM   4166  CD  GLU B  81      -2.117  50.907 -22.997  1.00108.57           C  
ANISOU 4166  CD  GLU B  81    13501  13634  14117    846  -1021   2259       C  
ATOM   4167  OE1 GLU B  81      -2.701  50.907 -21.888  1.00105.20           O  
ANISOU 4167  OE1 GLU B  81    12843  13218  13910    929   -958   2118       O  
ATOM   4168  OE2 GLU B  81      -2.481  50.200 -23.964  1.00103.27           O  
ANISOU 4168  OE2 GLU B  81    12840  13061  13338    867  -1169   2297       O  
ATOM   4169  N   GLY B  82       3.095  53.071 -20.750  1.00 65.75           N  
ANISOU 4169  N   GLY B  82     8498   7897   8586     69   -243   2314       N  
ATOM   4170  CA  GLY B  82       3.797  53.796 -19.701  1.00 65.71           C  
ANISOU 4170  CA  GLY B  82     8514   7768   8684    -38   -155   2248       C  
ATOM   4171  C   GLY B  82       3.186  53.588 -18.333  1.00 69.71           C  
ANISOU 4171  C   GLY B  82     8857   8310   9318     64   -156   2076       C  
ATOM   4172  O   GLY B  82       3.450  54.360 -17.412  1.00 69.78           O  
ANISOU 4172  O   GLY B  82     8936   8171   9406     29   -125   2009       O  
ATOM   4173  N   LYS B  83       2.365  52.536 -18.194  1.00 66.36           N  
ANISOU 4173  N   LYS B  83     8238   8070   8905    179   -181   1999       N  
ATOM   4174  CA  LYS B  83       1.661  52.201 -16.962  1.00 65.25           C  
ANISOU 4174  CA  LYS B  83     7953   7970   8868    275   -141   1836       C  
ATOM   4175  C   LYS B  83       2.484  51.162 -16.213  1.00 67.86           C  
ANISOU 4175  C   LYS B  83     8173   8464   9146    125    -44   1750       C  
ATOM   4176  O   LYS B  83       2.206  49.962 -16.298  1.00 66.98           O  
ANISOU 4176  O   LYS B  83     7907   8543   8999    138    -27   1714       O  
ATOM   4177  CB  LYS B  83       0.218  51.732 -17.265  1.00 67.40           C  
ANISOU 4177  CB  LYS B  83     8072   8318   9218    480   -216   1800       C  
ATOM   4178  CG  LYS B  83      -0.591  52.754 -18.072  1.00 79.34           C  
ANISOU 4178  CG  LYS B  83     9690   9655  10799    655   -368   1889       C  
ATOM   4179  CD  LYS B  83      -2.064  52.773 -17.689  1.00 90.39           C  
ANISOU 4179  CD  LYS B  83    10909  11036  12397    886   -415   1781       C  
ATOM   4180  CE  LYS B  83      -2.965  52.090 -18.690  1.00 94.64           C  
ANISOU 4180  CE  LYS B  83    11301  11694  12963   1000   -581   1818       C  
ATOM   4181  NZ  LYS B  83      -3.334  52.993 -19.806  1.00100.98           N  
ANISOU 4181  NZ  LYS B  83    12280  12334  13754   1126   -807   1961       N  
ATOM   4182  N   VAL B  84       3.542  51.637 -15.518  1.00 63.72           N  
ANISOU 4182  N   VAL B  84     7739   7850   8622    -22     -3   1721       N  
ATOM   4183  CA  VAL B  84       4.482  50.809 -14.739  1.00 61.60           C  
ANISOU 4183  CA  VAL B  84     7392   7693   8319   -164     39   1641       C  
ATOM   4184  C   VAL B  84       3.748  50.110 -13.590  1.00 65.14           C  
ANISOU 4184  C   VAL B  84     7776   8208   8765    -76     80   1498       C  
ATOM   4185  O   VAL B  84       3.867  48.892 -13.465  1.00 63.08           O  
ANISOU 4185  O   VAL B  84     7399   8120   8450   -105    103   1465       O  
ATOM   4186  CB  VAL B  84       5.719  51.602 -14.205  1.00 65.43           C  
ANISOU 4186  CB  VAL B  84     7986   8034   8841   -334     27   1628       C  
ATOM   4187  CG1 VAL B  84       6.761  50.665 -13.585  1.00 64.00           C  
ANISOU 4187  CG1 VAL B  84     7696   7977   8646   -470     18   1559       C  
ATOM   4188  CG2 VAL B  84       6.353  52.471 -15.290  1.00 65.89           C  
ANISOU 4188  CG2 VAL B  84     8138   7979   8917   -434     31   1768       C  
ATOM   4189  N   LYS B  85       2.992  50.869 -12.760  1.00 64.29           N  
ANISOU 4189  N   LYS B  85     7765   7950   8712     29    110   1413       N  
ATOM   4190  CA  LYS B  85       2.253  50.334 -11.602  1.00 64.20           C  
ANISOU 4190  CA  LYS B  85     7739   7964   8691    104    203   1269       C  
ATOM   4191  C   LYS B  85       1.288  49.200 -12.029  1.00 67.64           C  
ANISOU 4191  C   LYS B  85     7976   8581   9141    195    251   1262       C  
ATOM   4192  O   LYS B  85       1.310  48.139 -11.402  1.00 66.48           O  
ANISOU 4192  O   LYS B  85     7787   8545   8928    154    317   1189       O  
ATOM   4193  CB  LYS B  85       1.506  51.459 -10.861  1.00 68.41           C  
ANISOU 4193  CB  LYS B  85     8410   8284   9299    221    263   1183       C  
ATOM   4194  CG  LYS B  85       0.962  51.053  -9.495  1.00 82.48           C  
ANISOU 4194  CG  LYS B  85    10256  10044  11038    258    406   1021       C  
ATOM   4195  CD  LYS B  85       0.615  52.264  -8.614  1.00 92.18           C  
ANISOU 4195  CD  LYS B  85    11693  11026  12306    331    475    922       C  
ATOM   4196  CE  LYS B  85      -0.589  52.035  -7.716  1.00101.17           C  
ANISOU 4196  CE  LYS B  85    12829  12131  13479    462    688    773       C  
ATOM   4197  NZ  LYS B  85      -0.370  50.972  -6.691  1.00104.53           N  
ANISOU 4197  NZ  LYS B  85    13346  12635  13734    363    787    681       N  
ATOM   4198  N   GLU B  86       0.500  49.404 -13.116  1.00 64.97           N  
ANISOU 4198  N   GLU B  86     7536   8263   8886    308    195   1339       N  
ATOM   4199  CA  GLU B  86      -0.428  48.403 -13.663  1.00 64.51           C  
ANISOU 4199  CA  GLU B  86     7279   8365   8868    386    197   1333       C  
ATOM   4200  C   GLU B  86       0.330  47.209 -14.279  1.00 67.89           C  
ANISOU 4200  C   GLU B  86     7642   8982   9173    262    163   1393       C  
ATOM   4201  O   GLU B  86      -0.117  46.067 -14.126  1.00 66.85           O  
ANISOU 4201  O   GLU B  86     7385   8984   9030    262    213   1336       O  
ATOM   4202  CB  GLU B  86      -1.366  49.021 -14.710  1.00 67.51           C  
ANISOU 4202  CB  GLU B  86     7594   8690   9369    543     82   1402       C  
ATOM   4203  CG  GLU B  86      -2.473  49.888 -14.132  1.00 79.62           C  
ANISOU 4203  CG  GLU B  86     9096  10070  11086    719    133   1308       C  
ATOM   4204  CD  GLU B  86      -3.716  49.982 -14.998  1.00106.79           C  
ANISOU 4204  CD  GLU B  86    12365  13511  14700    903      8   1329       C  
ATOM   4205  OE1 GLU B  86      -4.037  51.102 -15.456  1.00100.10           O  
ANISOU 4205  OE1 GLU B  86    11597  12492  13942   1034   -106   1384       O  
ATOM   4206  OE2 GLU B  86      -4.380  48.939 -15.206  1.00104.94           O  
ANISOU 4206  OE2 GLU B  86    11919  13432  14522    920      5   1286       O  
ATOM   4207  N   ALA B  87       1.480  47.466 -14.960  1.00 64.65           N  
ANISOU 4207  N   ALA B  87     7317   8567   8680    151     99   1499       N  
ATOM   4208  CA  ALA B  87       2.306  46.405 -15.554  1.00 63.63           C  
ANISOU 4208  CA  ALA B  87     7131   8597   8450     40     93   1546       C  
ATOM   4209  C   ALA B  87       2.916  45.526 -14.470  1.00 67.84           C  
ANISOU 4209  C   ALA B  87     7644   9197   8936    -45    155   1452       C  
ATOM   4210  O   ALA B  87       2.994  44.310 -14.651  1.00 67.27           O  
ANISOU 4210  O   ALA B  87     7483   9267   8809    -72    171   1439       O  
ATOM   4211  CB  ALA B  87       3.396  46.985 -16.434  1.00 64.79           C  
ANISOU 4211  CB  ALA B  87     7371   8697   8551    -64     63   1665       C  
ATOM   4212  N   GLN B  88       3.306  46.132 -13.329  1.00 64.61           N  
ANISOU 4212  N   GLN B  88     7345   8665   8539    -79    173   1384       N  
ATOM   4213  CA  GLN B  88       3.857  45.422 -12.175  1.00 63.18           C  
ANISOU 4213  CA  GLN B  88     7207   8506   8293   -147    191   1293       C  
ATOM   4214  C   GLN B  88       2.768  44.549 -11.570  1.00 66.07           C  
ANISOU 4214  C   GLN B  88     7542   8929   8633    -73    289   1205       C  
ATOM   4215  O   GLN B  88       3.027  43.384 -11.253  1.00 64.84           O  
ANISOU 4215  O   GLN B  88     7373   8866   8400   -118    303   1172       O  
ATOM   4216  CB  GLN B  88       4.443  46.402 -11.145  1.00 65.48           C  
ANISOU 4216  CB  GLN B  88     7667   8623   8587   -199    156   1237       C  
ATOM   4217  CG  GLN B  88       5.797  46.968 -11.590  1.00 75.45           C  
ANISOU 4217  CG  GLN B  88     8932   9842   9893   -326     62   1305       C  
ATOM   4218  CD  GLN B  88       6.242  48.233 -10.888  1.00 88.83           C  
ANISOU 4218  CD  GLN B  88    10790  11334  11625   -380      9   1264       C  
ATOM   4219  OE1 GLN B  88       5.452  49.146 -10.608  1.00 85.44           O  
ANISOU 4219  OE1 GLN B  88    10478  10768  11216   -297     51   1237       O  
ATOM   4220  NE2 GLN B  88       7.549  48.349 -10.667  1.00 74.87           N  
ANISOU 4220  NE2 GLN B  88     9020   9534   9893   -522    -91   1256       N  
ATOM   4221  N   ALA B  89       1.526  45.090 -11.489  1.00 63.24           N  
ANISOU 4221  N   ALA B  89     7161   8508   8358     42    364   1168       N  
ATOM   4222  CA  ALA B  89       0.353  44.377 -10.970  1.00 62.26           C  
ANISOU 4222  CA  ALA B  89     6971   8422   8261    106    501   1075       C  
ATOM   4223  C   ALA B  89       0.030  43.158 -11.847  1.00 64.73           C  
ANISOU 4223  C   ALA B  89     7108   8910   8577     97    483   1111       C  
ATOM   4224  O   ALA B  89      -0.152  42.070 -11.311  1.00 64.65           O  
ANISOU 4224  O   ALA B  89     7092   8963   8511     57    571   1050       O  
ATOM   4225  CB  ALA B  89      -0.841  45.312 -10.886  1.00 64.13           C  
ANISOU 4225  CB  ALA B  89     7167   8550   8651    240    576   1026       C  
ATOM   4226  N   ALA B  90       0.030  43.326 -13.184  1.00 60.97           N  
ANISOU 4226  N   ALA B  90     6531   8495   8142    124    366   1210       N  
ATOM   4227  CA  ALA B  90      -0.201  42.248 -14.149  1.00 60.43           C  
ANISOU 4227  CA  ALA B  90     6331   8577   8054    111    318   1246       C  
ATOM   4228  C   ALA B  90       0.904  41.179 -14.059  1.00 64.66           C  
ANISOU 4228  C   ALA B  90     6911   9204   8454     -1    318   1259       C  
ATOM   4229  O   ALA B  90       0.605  39.988 -14.149  1.00 63.95           O  
ANISOU 4229  O   ALA B  90     6753   9212   8332    -24    348   1228       O  
ATOM   4230  CB  ALA B  90      -0.275  42.813 -15.557  1.00 61.80           C  
ANISOU 4230  CB  ALA B  90     6475   8757   8250    160    179   1355       C  
ATOM   4231  N   ALA B  91       2.167  41.610 -13.838  1.00 61.79           N  
ANISOU 4231  N   ALA B  91     6651   8793   8034    -70    281   1294       N  
ATOM   4232  CA  ALA B  91       3.333  40.736 -13.676  1.00 60.66           C  
ANISOU 4232  CA  ALA B  91     6528   8712   7807   -157    260   1296       C  
ATOM   4233  C   ALA B  91       3.240  39.902 -12.398  1.00 64.77           C  
ANISOU 4233  C   ALA B  91     7126   9218   8265   -175    314   1203       C  
ATOM   4234  O   ALA B  91       3.699  38.765 -12.393  1.00 63.49           O  
ANISOU 4234  O   ALA B  91     6954   9127   8040   -210    301   1195       O  
ATOM   4235  CB  ALA B  91       4.603  41.557 -13.657  1.00 61.46           C  
ANISOU 4235  CB  ALA B  91     6683   8744   7924   -225    198   1340       C  
ATOM   4236  N   GLU B  92       2.631  40.453 -11.329  1.00 62.76           N  
ANISOU 4236  N   GLU B  92     6975   8854   8016   -145    384   1132       N  
ATOM   4237  CA  GLU B  92       2.430  39.756 -10.053  1.00 63.15           C  
ANISOU 4237  CA  GLU B  92     7168   8857   7970   -166    466   1044       C  
ATOM   4238  C   GLU B  92       1.427  38.583 -10.233  1.00 66.55           C  
ANISOU 4238  C   GLU B  92     7509   9375   8403   -159    581   1013       C  
ATOM   4239  O   GLU B  92       1.524  37.583  -9.519  1.00 66.50           O  
ANISOU 4239  O   GLU B  92     7614   9362   8289   -202    628    973       O  
ATOM   4240  CB  GLU B  92       1.960  40.740  -8.961  1.00 65.83           C  
ANISOU 4240  CB  GLU B  92     7667   9041   8305   -138    553    969       C  
ATOM   4241  CG  GLU B  92       2.056  40.204  -7.535  1.00 78.89           C  
ANISOU 4241  CG  GLU B  92     9570  10604   9800   -178    619    886       C  
ATOM   4242  CD  GLU B  92       3.437  39.968  -6.942  1.00 96.23           C  
ANISOU 4242  CD  GLU B  92    11932  12756  11874   -241    436    894       C  
ATOM   4243  OE1 GLU B  92       4.425  40.550  -7.448  1.00 92.73           O  
ANISOU 4243  OE1 GLU B  92    11416  12318  11499   -264    273    945       O  
ATOM   4244  OE2 GLU B  92       3.521  39.228  -5.936  1.00 85.51           O  
ANISOU 4244  OE2 GLU B  92    10788  11341  10360   -269    454    846       O  
ATOM   4245  N   GLN B  93       0.514  38.693 -11.225  1.00 61.84           N  
ANISOU 4245  N   GLN B  93     6722   8847   7928   -109    600   1034       N  
ATOM   4246  CA  GLN B  93      -0.449  37.656 -11.584  1.00 61.13           C  
ANISOU 4246  CA  GLN B  93     6503   8840   7882   -115    675   1001       C  
ATOM   4247  C   GLN B  93       0.253  36.490 -12.339  1.00 61.99           C  
ANISOU 4247  C   GLN B  93     6588   9060   7907   -167    586   1050       C  
ATOM   4248  O   GLN B  93      -0.301  35.388 -12.407  1.00 61.86           O  
ANISOU 4248  O   GLN B  93     6528   9092   7883   -202    647   1013       O  
ATOM   4249  CB  GLN B  93      -1.589  38.251 -12.423  1.00 63.65           C  
ANISOU 4249  CB  GLN B  93     6623   9183   8379    -35    660   1003       C  
ATOM   4250  CG  GLN B  93      -2.947  37.579 -12.209  1.00 87.26           C  
ANISOU 4250  CG  GLN B  93     9467  12195  11492    -37    796    913       C  
ATOM   4251  CD  GLN B  93      -3.981  37.947 -13.260  1.00112.59           C  
ANISOU 4251  CD  GLN B  93    12436  15444  14898     45    701    917       C  
ATOM   4252  OE1 GLN B  93      -3.874  38.957 -13.973  1.00109.45           O  
ANISOU 4252  OE1 GLN B  93    12016  15025  14546    129    555    984       O  
ATOM   4253  NE2 GLN B  93      -5.026  37.136 -13.369  1.00105.16           N  
ANISOU 4253  NE2 GLN B  93    11318  14549  14088     19    768    843       N  
ATOM   4254  N   LEU B  94       1.482  36.717 -12.868  1.00 56.04           N  
ANISOU 4254  N   LEU B  94     5862   8331   7101   -179    463   1122       N  
ATOM   4255  CA  LEU B  94       2.269  35.671 -13.537  1.00 54.38           C  
ANISOU 4255  CA  LEU B  94     5633   8207   6821   -214    404   1156       C  
ATOM   4256  C   LEU B  94       2.729  34.630 -12.523  1.00 57.38           C  
ANISOU 4256  C   LEU B  94     6142   8554   7106   -251    431   1108       C  
ATOM   4257  O   LEU B  94       2.864  33.456 -12.874  1.00 56.97           O  
ANISOU 4257  O   LEU B  94     6080   8556   7008   -270    429   1104       O  
ATOM   4258  CB  LEU B  94       3.487  36.238 -14.285  1.00 54.14           C  
ANISOU 4258  CB  LEU B  94     5584   8194   6791   -222    313   1231       C  
ATOM   4259  CG  LEU B  94       3.225  37.161 -15.476  1.00 59.05           C  
ANISOU 4259  CG  LEU B  94     6140   8838   7460   -195    276   1304       C  
ATOM   4260  CD1 LEU B  94       4.494  37.844 -15.900  1.00 59.45           C  
ANISOU 4260  CD1 LEU B  94     6209   8863   7516   -232    242   1369       C  
ATOM   4261  CD2 LEU B  94       2.637  36.411 -16.652  1.00 59.80           C  
ANISOU 4261  CD2 LEU B  94     6172   9028   7522   -185    258   1321       C  
ATOM   4262  N   LYS B  95       2.951  35.061 -11.264  1.00 53.09           N  
ANISOU 4262  N   LYS B  95     5751   7902   6518   -258    446   1072       N  
ATOM   4263  CA  LYS B  95       3.343  34.192 -10.156  1.00 53.20           C  
ANISOU 4263  CA  LYS B  95     5959   7845   6410   -285    447   1031       C  
ATOM   4264  C   LYS B  95       2.230  33.202  -9.872  1.00 58.55           C  
ANISOU 4264  C   LYS B  95     6677   8519   7049   -315    603    983       C  
ATOM   4265  O   LYS B  95       2.493  32.002  -9.760  1.00 59.27           O  
ANISOU 4265  O   LYS B  95     6852   8610   7059   -340    594    979       O  
ATOM   4266  CB  LYS B  95       3.686  35.007  -8.896  1.00 55.78           C  
ANISOU 4266  CB  LYS B  95     6485   8036   6671   -288    418    997       C  
ATOM   4267  CG  LYS B  95       4.970  35.810  -9.021  1.00 58.48           C  
ANISOU 4267  CG  LYS B  95     6798   8360   7060   -285    239   1032       C  
ATOM   4268  CD  LYS B  95       5.187  36.671  -7.806  1.00 66.89           C  
ANISOU 4268  CD  LYS B  95     8075   9278   8061   -296    195    985       C  
ATOM   4269  CE  LYS B  95       6.303  37.660  -8.024  1.00 68.16           C  
ANISOU 4269  CE  LYS B  95     8169   9413   8316   -314     29   1011       C  
ATOM   4270  NZ  LYS B  95       6.452  38.581  -6.863  1.00 74.97           N  
ANISOU 4270  NZ  LYS B  95     9258  10117   9111   -333    -31    954       N  
ATOM   4271  N   THR B  96       0.976  33.696  -9.846  1.00 54.96           N  
ANISOU 4271  N   THR B  96     6141   8059   6683   -313    748    944       N  
ATOM   4272  CA  THR B  96      -0.237  32.908  -9.611  1.00 54.76           C  
ANISOU 4272  CA  THR B  96     6096   8027   6685   -361    932    883       C  
ATOM   4273  C   THR B  96      -0.369  31.794 -10.651  1.00 56.77           C  
ANISOU 4273  C   THR B  96     6217   8385   6969   -390    886    901       C  
ATOM   4274  O   THR B  96      -0.550  30.638 -10.275  1.00 55.30           O  
ANISOU 4274  O   THR B  96     6135   8166   6710   -454    966    873       O  
ATOM   4275  CB  THR B  96      -1.464  33.828  -9.590  1.00 64.16           C  
ANISOU 4275  CB  THR B  96     7137   9200   8039   -330   1068    832       C  
ATOM   4276  OG1 THR B  96      -1.184  34.962  -8.753  1.00 70.37           O  
ANISOU 4276  OG1 THR B  96     8062   9884   8790   -290   1088    818       O  
ATOM   4277  CG2 THR B  96      -2.725  33.117  -9.105  1.00 58.51           C  
ANISOU 4277  CG2 THR B  96     6392   8451   7389   -396   1307    747       C  
ATOM   4278  N   THR B  97      -0.243  32.138 -11.944  1.00 54.54           N  
ANISOU 4278  N   THR B  97     5746   8207   6771   -349    757    949       N  
ATOM   4279  CA  THR B  97      -0.348  31.193 -13.056  1.00 54.90           C  
ANISOU 4279  CA  THR B  97     5689   8344   6826   -371    694    961       C  
ATOM   4280  C   THR B  97       0.772  30.161 -12.998  1.00 60.77           C  
ANISOU 4280  C   THR B  97     6571   9082   7435   -386    637    983       C  
ATOM   4281  O   THR B  97       0.509  28.967 -13.162  1.00 61.51           O  
ANISOU 4281  O   THR B  97     6694   9180   7495   -434    670    955       O  
ATOM   4282  CB  THR B  97      -0.320  31.960 -14.372  1.00 62.42           C  
ANISOU 4282  CB  THR B  97     6488   9381   7850   -316    564   1015       C  
ATOM   4283  OG1 THR B  97      -1.495  32.762 -14.448  1.00 67.10           O  
ANISOU 4283  OG1 THR B  97     6941   9964   8592   -285    594    985       O  
ATOM   4284  CG2 THR B  97      -0.204  31.047 -15.604  1.00 57.72           C  
ANISOU 4284  CG2 THR B  97     5845   8869   7217   -335    480   1029       C  
ATOM   4285  N   ARG B  98       2.014  30.627 -12.778  1.00 57.25           N  
ANISOU 4285  N   ARG B  98     6197   8616   6938   -343    544   1026       N  
ATOM   4286  CA  ARG B  98       3.206  29.788 -12.707  1.00 57.19           C  
ANISOU 4286  CA  ARG B  98     6284   8595   6852   -328    463   1041       C  
ATOM   4287  C   ARG B  98       3.062  28.748 -11.602  1.00 62.70           C  
ANISOU 4287  C   ARG B  98     7189   9189   7446   -361    517   1002       C  
ATOM   4288  O   ARG B  98       3.366  27.573 -11.825  1.00 64.25           O  
ANISOU 4288  O   ARG B  98     7443   9377   7592   -362    494    996       O  
ATOM   4289  CB  ARG B  98       4.454  30.660 -12.475  1.00 56.28           C  
ANISOU 4289  CB  ARG B  98     6171   8458   6754   -286    351   1077       C  
ATOM   4290  CG  ARG B  98       5.406  30.672 -13.667  1.00 69.71           C  
ANISOU 4290  CG  ARG B  98     7735  10243   8509   -259    289   1118       C  
ATOM   4291  CD  ARG B  98       6.287  31.910 -13.811  1.00 80.95           C  
ANISOU 4291  CD  ARG B  98     9084  11662  10010   -250    228   1158       C  
ATOM   4292  NE  ARG B  98       6.912  32.370 -12.565  1.00 88.78           N  
ANISOU 4292  NE  ARG B  98    10175  12554  11002   -248    141   1137       N  
ATOM   4293  CZ  ARG B  98       8.096  31.974 -12.103  1.00 97.09           C  
ANISOU 4293  CZ  ARG B  98    11245  13565  12081   -225     22   1123       C  
ATOM   4294  NH1 ARG B  98       8.800  31.054 -12.753  1.00 75.57           N  
ANISOU 4294  NH1 ARG B  98     8429  10889   9396   -192     10   1122       N  
ATOM   4295  NH2 ARG B  98       8.572  32.473 -10.973  1.00 85.71           N  
ANISOU 4295  NH2 ARG B  98     9916  12021  10630   -227    -96   1100       N  
ATOM   4296  N   ASN B  99       2.523  29.171 -10.445  1.00 58.09           N  
ANISOU 4296  N   ASN B  99     6743   8510   6818   -390    606    974       N  
ATOM   4297  CA  ASN B  99       2.354  28.331  -9.266  1.00 58.50           C  
ANISOU 4297  CA  ASN B  99     7064   8431   6732   -432    680    945       C  
ATOM   4298  C   ASN B  99       1.138  27.417  -9.308  1.00 62.57           C  
ANISOU 4298  C   ASN B  99     7588   8932   7255   -522    868    902       C  
ATOM   4299  O   ASN B  99       1.209  26.316  -8.751  1.00 62.83           O  
ANISOU 4299  O   ASN B  99     7839   8865   7168   -563    906    896       O  
ATOM   4300  CB  ASN B  99       2.305  29.197  -8.017  1.00 56.81           C  
ANISOU 4300  CB  ASN B  99     7042   8103   6439   -435    722    925       C  
ATOM   4301  CG  ASN B  99       3.631  29.828  -7.755  1.00 65.44           C  
ANISOU 4301  CG  ASN B  99     8183   9172   7509   -368    504    956       C  
ATOM   4302  OD1 ASN B  99       4.674  29.321  -8.183  1.00 56.09           O  
ANISOU 4302  OD1 ASN B  99     6951   8019   6343   -321    333    986       O  
ATOM   4303  ND2 ASN B  99       3.622  30.959  -7.079  1.00 60.78           N  
ANISOU 4303  ND2 ASN B  99     7669   8520   6904   -364    508    938       N  
ATOM   4304  N   ALA B 100       0.025  27.870  -9.912  1.00 59.00           N  
ANISOU 4304  N   ALA B 100     6906   8558   6952   -555    975    871       N  
ATOM   4305  CA  ALA B 100      -1.177  27.055  -9.976  1.00 60.03           C  
ANISOU 4305  CA  ALA B 100     6987   8675   7145   -658   1149    815       C  
ATOM   4306  C   ALA B 100      -1.150  26.103 -11.171  1.00 64.76           C  
ANISOU 4306  C   ALA B 100     7462   9357   7785   -677   1055    819       C  
ATOM   4307  O   ALA B 100      -1.692  25.004 -11.057  1.00 65.08           O  
ANISOU 4307  O   ALA B 100     7572   9343   7813   -773   1156    781       O  
ATOM   4308  CB  ALA B 100      -2.414  27.933 -10.031  1.00 61.25           C  
ANISOU 4308  CB  ALA B 100     6928   8860   7482   -677   1289    761       C  
ATOM   4309  N   TYR B 101      -0.496  26.482 -12.292  1.00 60.65           N  
ANISOU 4309  N   TYR B 101     6796   8950   7300   -597    877    861       N  
ATOM   4310  CA  TYR B 101      -0.541  25.618 -13.467  1.00 61.05           C  
ANISOU 4310  CA  TYR B 101     6762   9068   7367   -616    800    852       C  
ATOM   4311  C   TYR B 101       0.766  24.939 -13.881  1.00 64.90           C  
ANISOU 4311  C   TYR B 101     7358   9556   7744   -553    685    888       C  
ATOM   4312  O   TYR B 101       0.687  23.813 -14.377  1.00 65.44           O  
ANISOU 4312  O   TYR B 101     7473   9610   7779   -590    681    860       O  
ATOM   4313  CB  TYR B 101      -1.088  26.388 -14.691  1.00 63.10           C  
ANISOU 4313  CB  TYR B 101     6780   9446   7748   -589    710    856       C  
ATOM   4314  CG  TYR B 101      -2.435  27.053 -14.481  1.00 67.52           C  
ANISOU 4314  CG  TYR B 101     7168  10010   8477   -624    792    808       C  
ATOM   4315  CD1 TYR B 101      -3.610  26.311 -14.483  1.00 71.55           C  
ANISOU 4315  CD1 TYR B 101     7578  10505   9104   -729    877    730       C  
ATOM   4316  CD2 TYR B 101      -2.536  28.434 -14.316  1.00 68.73           C  
ANISOU 4316  CD2 TYR B 101     7238  10174   8702   -550    782    833       C  
ATOM   4317  CE1 TYR B 101      -4.854  26.921 -14.307  1.00 75.62           C  
ANISOU 4317  CE1 TYR B 101     7881  11021   9829   -751    958    671       C  
ATOM   4318  CE2 TYR B 101      -3.770  29.053 -14.117  1.00 71.02           C  
ANISOU 4318  CE2 TYR B 101     7350  10457   9179   -558    862    778       C  
ATOM   4319  CZ  TYR B 101      -4.929  28.293 -14.126  1.00 83.27           C  
ANISOU 4319  CZ  TYR B 101     8768  12001  10872   -653    950    694       C  
ATOM   4320  OH  TYR B 101      -6.159  28.887 -13.949  1.00 88.88           O  
ANISOU 4320  OH  TYR B 101     9251  12701  11819   -653   1035    625       O  
ATOM   4321  N   ILE B 102       1.938  25.599 -13.757  1.00 61.21           N  
ANISOU 4321  N   ILE B 102     6910   9100   7245   -461    593    938       N  
ATOM   4322  CA  ILE B 102       3.182  25.039 -14.318  1.00 60.64           C  
ANISOU 4322  CA  ILE B 102     6869   9041   7131   -389    496    959       C  
ATOM   4323  C   ILE B 102       4.098  24.365 -13.294  1.00 62.95           C  
ANISOU 4323  C   ILE B 102     7356   9214   7347   -344    449    962       C  
ATOM   4324  O   ILE B 102       4.665  23.310 -13.596  1.00 61.79           O  
ANISOU 4324  O   ILE B 102     7277   9031   7167   -307    412    949       O  
ATOM   4325  CB  ILE B 102       3.972  26.120 -15.103  1.00 63.49           C  
ANISOU 4325  CB  ILE B 102     7084   9494   7548   -324    424   1005       C  
ATOM   4326  CG1 ILE B 102       3.055  26.874 -16.114  1.00 63.52           C  
ANISOU 4326  CG1 ILE B 102     6942   9590   7602   -353    434   1016       C  
ATOM   4327  CG2 ILE B 102       5.208  25.497 -15.807  1.00 63.37           C  
ANISOU 4327  CG2 ILE B 102     7062   9495   7523   -257    377   1008       C  
ATOM   4328  CD1 ILE B 102       3.562  28.300 -16.515  1.00 67.50           C  
ANISOU 4328  CD1 ILE B 102     7352  10139   8156   -312    392   1075       C  
ATOM   4329  N   GLN B 103       4.272  24.992 -12.123  1.00 59.58           N  
ANISOU 4329  N   GLN B 103     7034   8714   6890   -336    431    977       N  
ATOM   4330  CA  GLN B 103       5.122  24.564 -11.003  1.00 59.61           C  
ANISOU 4330  CA  GLN B 103     7259   8583   6806   -286    332    985       C  
ATOM   4331  C   GLN B 103       5.127  23.055 -10.741  1.00 63.96           C  
ANISOU 4331  C   GLN B 103     8018   9022   7263   -289    339    970       C  
ATOM   4332  O   GLN B 103       6.187  22.508 -10.447  1.00 64.08           O  
ANISOU 4332  O   GLN B 103     8138   8955   7252   -195    191    980       O  
ATOM   4333  CB  GLN B 103       4.659  25.257  -9.726  1.00 61.31           C  
ANISOU 4333  CB  GLN B 103     7642   8709   6944   -328    378    984       C  
ATOM   4334  CG  GLN B 103       5.806  25.672  -8.840  1.00 70.32           C  
ANISOU 4334  CG  GLN B 103     8912   9763   8042   -253    190   1002       C  
ATOM   4335  CD  GLN B 103       5.423  25.796  -7.394  1.00 73.65           C  
ANISOU 4335  CD  GLN B 103     9657  10029   8298   -293    224    992       C  
ATOM   4336  OE1 GLN B 103       6.300  25.805  -6.530  1.00 71.47           O  
ANISOU 4336  OE1 GLN B 103     9576   9640   7938   -236     36   1001       O  
ATOM   4337  NE2 GLN B 103       4.121  25.854  -7.082  1.00 53.44           N  
ANISOU 4337  NE2 GLN B 103     7172   7446   5687   -394    462    967       N  
ATOM   4338  N   LYS B 104       3.951  22.390 -10.850  1.00 60.73           N  
ANISOU 4338  N   LYS B 104     7659   8593   6821   -397    498    942       N  
ATOM   4339  CA  LYS B 104       3.786  20.956 -10.604  1.00 61.43           C  
ANISOU 4339  CA  LYS B 104     7970   8553   6817   -430    535    926       C  
ATOM   4340  C   LYS B 104       4.649  20.087 -11.539  1.00 65.81           C  
ANISOU 4340  C   LYS B 104     8473   9125   7408   -336    426    917       C  
ATOM   4341  O   LYS B 104       4.938  18.941 -11.189  1.00 66.89           O  
ANISOU 4341  O   LYS B 104     8830   9119   7465   -310    393    914       O  
ATOM   4342  CB  LYS B 104       2.301  20.538 -10.670  1.00 63.93           C  
ANISOU 4342  CB  LYS B 104     8292   8856   7143   -593    744    885       C  
ATOM   4343  CG  LYS B 104       1.594  20.690 -12.017  1.00 65.58           C  
ANISOU 4343  CG  LYS B 104     8208   9221   7488   -642    778    848       C  
ATOM   4344  CD  LYS B 104       0.109  20.364 -11.858  1.00 67.48           C  
ANISOU 4344  CD  LYS B 104     8426   9430   7781   -810    964    795       C  
ATOM   4345  CE  LYS B 104      -0.763  21.590 -11.939  1.00 75.40           C  
ANISOU 4345  CE  LYS B 104     9196  10533   8917   -847   1041    776       C  
ATOM   4346  NZ  LYS B 104      -1.133  21.916 -13.355  1.00 86.31           N  
ANISOU 4346  NZ  LYS B 104    10294  12071  10430   -833    944    756       N  
ATOM   4347  N   TYR B 105       5.087  20.640 -12.690  1.00 61.32           N  
ANISOU 4347  N   TYR B 105     7642   8708   6948   -280    385    912       N  
ATOM   4348  CA  TYR B 105       5.936  19.941 -13.652  1.00 61.23           C  
ANISOU 4348  CA  TYR B 105     7569   8718   6978   -187    327    890       C  
ATOM   4349  C   TYR B 105       7.423  20.245 -13.408  1.00 68.77           C  
ANISOU 4349  C   TYR B 105     8465   9659   8006    -36    180    909       C  
ATOM   4350  O   TYR B 105       8.271  19.609 -14.031  1.00 69.30           O  
ANISOU 4350  O   TYR B 105     8479   9718   8133     65    144    881       O  
ATOM   4351  CB  TYR B 105       5.527  20.286 -15.100  1.00 60.32           C  
ANISOU 4351  CB  TYR B 105     7250   8756   6915   -227    394    868       C  
ATOM   4352  CG  TYR B 105       4.073  19.979 -15.385  1.00 59.88           C  
ANISOU 4352  CG  TYR B 105     7208   8712   6831   -371    490    835       C  
ATOM   4353  CD1 TYR B 105       3.642  18.671 -15.578  1.00 61.93           C  
ANISOU 4353  CD1 TYR B 105     7611   8881   7040   -430    530    787       C  
ATOM   4354  CD2 TYR B 105       3.118  20.992 -15.415  1.00 59.26           C  
ANISOU 4354  CD2 TYR B 105     6991   8722   6804   -450    533    845       C  
ATOM   4355  CE1 TYR B 105       2.300  18.378 -15.802  1.00 61.68           C  
ANISOU 4355  CE1 TYR B 105     7561   8852   7021   -582    608    745       C  
ATOM   4356  CE2 TYR B 105       1.776  20.712 -15.666  1.00 59.79           C  
ANISOU 4356  CE2 TYR B 105     7020   8797   6900   -579    604    801       C  
ATOM   4357  CZ  TYR B 105       1.373  19.403 -15.852  1.00 64.72           C  
ANISOU 4357  CZ  TYR B 105     7767   9337   7487   -654    640    749       C  
ATOM   4358  OH  TYR B 105       0.058  19.107 -16.070  1.00 65.66           O  
ANISOU 4358  OH  TYR B 105     7820   9457   7671   -799    702    694       O  
ATOM   4359  N   LEU B 106       7.733  21.173 -12.476  1.00 67.97           N  
ANISOU 4359  N   LEU B 106     8371   9540   7915    -22     96    943       N  
ATOM   4360  CA  LEU B 106       9.096  21.587 -12.089  1.00 69.84           C  
ANISOU 4360  CA  LEU B 106     8532   9752   8251    100    -80    952       C  
ATOM   4361  C   LEU B 106       9.228  21.596 -10.570  1.00 76.13           C  
ANISOU 4361  C   LEU B 106     9584  10395   8947    115   -221    974       C  
ATOM   4362  O   LEU B 106       9.385  22.672  -9.975  1.00 75.76           O  
ANISOU 4362  O   LEU B 106     9512  10362   8911     94   -284    991       O  
ATOM   4363  CB  LEU B 106       9.377  23.003 -12.630  1.00 69.42           C  
ANISOU 4363  CB  LEU B 106     8214   9844   8320     80    -59    968       C  
ATOM   4364  CG  LEU B 106       9.790  23.123 -14.074  1.00 74.19           C  
ANISOU 4364  CG  LEU B 106     8587  10573   9027     98     39    953       C  
ATOM   4365  CD1 LEU B 106       8.632  23.625 -14.930  1.00 72.44           C  
ANISOU 4365  CD1 LEU B 106     8321  10460   8741    -12    187    967       C  
ATOM   4366  CD2 LEU B 106      11.004  24.038 -14.192  1.00 78.48           C  
ANISOU 4366  CD2 LEU B 106     8911  11165   9741    147    -25    960       C  
ATOM   4367  N   SER B 190       9.124  20.426  -9.921  1.00 72.38           N  
ANISOU 4367  N   SER B 190     7032  10558   9912   -770    541    -98       N  
ATOM   4368  CA  SER B 190       9.121  20.457  -8.465  1.00 71.35           C  
ANISOU 4368  CA  SER B 190     6926  10331   9852   -727    392    -70       C  
ATOM   4369  C   SER B 190      10.236  19.665  -7.758  1.00 76.21           C  
ANISOU 4369  C   SER B 190     7389  10926  10641   -683    343   -109       C  
ATOM   4370  O   SER B 190      11.094  20.273  -7.110  1.00 76.71           O  
ANISOU 4370  O   SER B 190     7386  10974  10785   -730    276    -78       O  
ATOM   4371  CB  SER B 190       7.767  20.000  -7.943  1.00 72.70           C  
ANISOU 4371  CB  SER B 190     7230  10453   9939   -653    329    -66       C  
ATOM   4372  OG  SER B 190       7.659  20.228  -6.551  1.00 79.51           O  
ANISOU 4372  OG  SER B 190     8135  11241  10835   -630    191    -34       O  
ATOM   4373  N   GLY B 191      10.153  18.342  -7.755  1.00 72.45           N  
ANISOU 4373  N   GLY B 191     6859  10438  10229   -593    358   -167       N  
ATOM   4374  CA  GLY B 191      11.094  17.556  -6.963  1.00 73.69           C  
ANISOU 4374  CA  GLY B 191     6873  10558  10570   -536    291   -177       C  
ATOM   4375  C   GLY B 191      10.627  17.454  -5.513  1.00 77.08           C  
ANISOU 4375  C   GLY B 191     7373  10919  10993   -494    120   -111       C  
ATOM   4376  O   GLY B 191      10.896  16.449  -4.852  1.00 78.60           O  
ANISOU 4376  O   GLY B 191     7487  11072  11306   -418     55   -103       O  
ATOM   4377  N   GLN B 192       9.889  18.487  -5.015  1.00 70.17           N  
ANISOU 4377  N   GLN B 192     6648  10032   9983   -545     53    -61       N  
ATOM   4378  CA  GLN B 192       9.263  18.531  -3.687  1.00 67.88           C  
ANISOU 4378  CA  GLN B 192     6454   9696   9641   -526    -91    -12       C  
ATOM   4379  C   GLN B 192       8.164  17.481  -3.568  1.00 67.09           C  
ANISOU 4379  C   GLN B 192     6433   9560   9497   -436    -92    -21       C  
ATOM   4380  O   GLN B 192       8.070  16.824  -2.536  1.00 67.42           O  
ANISOU 4380  O   GLN B 192     6472   9571   9573   -390   -197     17       O  
ATOM   4381  CB  GLN B 192       8.666  19.920  -3.389  1.00 68.16           C  
ANISOU 4381  CB  GLN B 192     6627   9719   9551   -607   -120     13       C  
ATOM   4382  CG  GLN B 192       9.183  20.551  -2.089  1.00 80.22           C  
ANISOU 4382  CG  GLN B 192     8149  11237  11093   -664   -257     42       C  
ATOM   4383  CD  GLN B 192       8.378  20.211  -0.858  1.00 94.80           C  
ANISOU 4383  CD  GLN B 192    10097  13061  12864   -630   -367     62       C  
ATOM   4384  OE1 GLN B 192       7.158  20.060  -0.894  1.00 92.43           O  
ANISOU 4384  OE1 GLN B 192     9921  12732  12467   -590   -339     56       O  
ATOM   4385  NE2 GLN B 192       9.036  20.167   0.285  1.00 84.68           N  
ANISOU 4385  NE2 GLN B 192     8761  11801  11612   -657   -497     89       N  
ATOM   4386  N   CYS B 193       7.328  17.334  -4.608  1.00 60.01           N  
ANISOU 4386  N   CYS B 193     5604   8676   8521   -421     20    -63       N  
ATOM   4387  CA  CYS B 193       6.226  16.369  -4.597  1.00 57.77           C  
ANISOU 4387  CA  CYS B 193     5393   8361   8195   -347     32    -83       C  
ATOM   4388  C   CYS B 193       6.498  15.245  -5.561  1.00 63.18           C  
ANISOU 4388  C   CYS B 193     5977   9058   8972   -299    145   -162       C  
ATOM   4389  O   CYS B 193       7.074  15.463  -6.627  1.00 64.21           O  
ANISOU 4389  O   CYS B 193     6039   9246   9111   -341    255   -213       O  
ATOM   4390  CB  CYS B 193       4.891  17.038  -4.906  1.00 55.65           C  
ANISOU 4390  CB  CYS B 193     5284   8099   7761   -370     58    -76       C  
ATOM   4391  SG  CYS B 193       4.625  18.598  -4.032  1.00 58.98           S  
ANISOU 4391  SG  CYS B 193     5814   8498   8095   -442    -30    -14       S  
ATOM   4392  N   GLU B 194       6.061  14.048  -5.188  1.00 59.64           N  
ANISOU 4392  N   GLU B 194     5518   8552   8590   -219    124   -175       N  
ATOM   4393  CA  GLU B 194       6.184  12.854  -5.995  1.00 60.21           C  
ANISOU 4393  CA  GLU B 194     5499   8609   8768   -167    233   -268       C  
ATOM   4394  C   GLU B 194       4.806  12.310  -6.281  1.00 63.33           C  
ANISOU 4394  C   GLU B 194     6008   8988   9067   -139    268   -307       C  
ATOM   4395  O   GLU B 194       3.957  12.280  -5.389  1.00 62.10           O  
ANISOU 4395  O   GLU B 194     5955   8789   8852   -116    175   -242       O  
ATOM   4396  CB  GLU B 194       7.046  11.803  -5.285  1.00 62.88           C  
ANISOU 4396  CB  GLU B 194     5692   8870   9329    -94    179   -247       C  
ATOM   4397  N   VAL B 195       4.585  11.888  -7.539  1.00 59.78           N  
ANISOU 4397  N   VAL B 195     5536   8583   8595   -150    407   -419       N  
ATOM   4398  CA  VAL B 195       3.360  11.272  -8.055  1.00 58.33           C  
ANISOU 4398  CA  VAL B 195     5434   8401   8328   -135    460   -484       C  
ATOM   4399  C   VAL B 195       2.906  10.198  -7.024  1.00 59.57           C  
ANISOU 4399  C   VAL B 195     5599   8437   8596    -53    382   -451       C  
ATOM   4400  O   VAL B 195       3.755   9.479  -6.502  1.00 59.71           O  
ANISOU 4400  O   VAL B 195     5502   8379   8807      1    355   -437       O  
ATOM   4401  CB  VAL B 195       3.618  10.692  -9.493  1.00 63.80           C  
ANISOU 4401  CB  VAL B 195     6045   9159   9035   -162    627   -638       C  
ATOM   4402  CG1 VAL B 195       2.371  10.033 -10.094  1.00 63.44           C  
ANISOU 4402  CG1 VAL B 195     6076   9131   8899   -162    683   -723       C  
ATOM   4403  CG2 VAL B 195       4.140  11.775 -10.438  1.00 63.99           C  
ANISOU 4403  CG2 VAL B 195     6059   9314   8942   -254    700   -645       C  
ATOM   4404  N   PRO B 196       1.619  10.134  -6.624  1.00 54.15           N  
ANISOU 4404  N   PRO B 196     5040   7731   7802    -42    334   -418       N  
ATOM   4405  CA  PRO B 196       0.462  10.897  -7.131  1.00 52.61           C  
ANISOU 4405  CA  PRO B 196     4976   7612   7402    -92    351   -420       C  
ATOM   4406  C   PRO B 196       0.262  12.290  -6.499  1.00 54.37           C  
ANISOU 4406  C   PRO B 196     5294   7862   7503   -131    261   -311       C  
ATOM   4407  O   PRO B 196      -0.812  12.870  -6.676  1.00 52.92           O  
ANISOU 4407  O   PRO B 196     5217   7712   7180   -154    255   -291       O  
ATOM   4408  CB  PRO B 196      -0.712   9.961  -6.834  1.00 53.73           C  
ANISOU 4408  CB  PRO B 196     5178   7693   7544    -50    340   -439       C  
ATOM   4409  CG  PRO B 196      -0.305   9.222  -5.604  1.00 58.48           C  
ANISOU 4409  CG  PRO B 196     5736   8183   8300     13    255   -370       C  
ATOM   4410  CD  PRO B 196       1.205   9.109  -5.646  1.00 55.15           C  
ANISOU 4410  CD  PRO B 196     5173   7748   8035     26    267   -375       C  
ATOM   4411  N   LEU B 197       1.275  12.848  -5.799  1.00 50.77           N  
ANISOU 4411  N   LEU B 197     4791   7391   7107   -142    195   -247       N  
ATOM   4412  CA  LEU B 197       1.118  14.198  -5.231  1.00 49.71           C  
ANISOU 4412  CA  LEU B 197     4743   7275   6871   -189    123   -168       C  
ATOM   4413  C   LEU B 197       1.555  15.211  -6.265  1.00 52.81           C  
ANISOU 4413  C   LEU B 197     5120   7742   7203   -258    193   -178       C  
ATOM   4414  O   LEU B 197       2.235  14.847  -7.212  1.00 53.84           O  
ANISOU 4414  O   LEU B 197     5156   7919   7381   -272    282   -239       O  
ATOM   4415  CB  LEU B 197       1.818  14.417  -3.870  1.00 49.35           C  
ANISOU 4415  CB  LEU B 197     4675   7186   6890   -187      5    -96       C  
ATOM   4416  CG  LEU B 197       1.277  13.602  -2.699  1.00 53.28           C  
ANISOU 4416  CG  LEU B 197     5211   7625   7409   -136    -81    -51       C  
ATOM   4417  CD1 LEU B 197       2.049  13.889  -1.440  1.00 54.78           C  
ANISOU 4417  CD1 LEU B 197     5368   7807   7640   -153   -201     24       C  
ATOM   4418  CD2 LEU B 197      -0.197  13.863  -2.462  1.00 53.96           C  
ANISOU 4418  CD2 LEU B 197     5438   7704   7359   -139    -90    -42       C  
ATOM   4419  N   VAL B 198       1.106  16.451  -6.139  1.00 48.22           N  
ANISOU 4419  N   VAL B 198     4630   7171   6519   -304    163   -120       N  
ATOM   4420  CA  VAL B 198       1.349  17.471  -7.152  1.00 48.74           C  
ANISOU 4420  CA  VAL B 198     4696   7302   6522   -373    226   -102       C  
ATOM   4421  C   VAL B 198       1.579  18.810  -6.445  1.00 52.76           C  
ANISOU 4421  C   VAL B 198     5249   7772   7027   -420    158    -31       C  
ATOM   4422  O   VAL B 198       0.885  19.141  -5.488  1.00 52.84           O  
ANISOU 4422  O   VAL B 198     5343   7724   7012   -405     85     -4       O  
ATOM   4423  CB  VAL B 198       0.123  17.415  -8.139  1.00 52.79           C  
ANISOU 4423  CB  VAL B 198     5280   7870   6909   -378    283   -110       C  
ATOM   4424  CG1 VAL B 198      -0.613  18.733  -8.326  1.00 52.34           C  
ANISOU 4424  CG1 VAL B 198     5306   7821   6759   -424    269    -24       C  
ATOM   4425  CG2 VAL B 198       0.512  16.785  -9.467  1.00 53.09           C  
ANISOU 4425  CG2 VAL B 198     5239   8002   6930   -399    395   -188       C  
ATOM   4426  N   ARG B 199       2.607  19.528  -6.871  1.00 50.52           N  
ANISOU 4426  N   ARG B 199     4900   7517   6777   -484    191    -14       N  
ATOM   4427  CA  ARG B 199       3.038  20.811  -6.307  1.00 50.67           C  
ANISOU 4427  CA  ARG B 199     4940   7496   6817   -545    142     39       C  
ATOM   4428  C   ARG B 199       1.984  21.903  -6.552  1.00 54.65           C  
ANISOU 4428  C   ARG B 199     5556   7971   7238   -571    147     98       C  
ATOM   4429  O   ARG B 199       1.537  22.129  -7.680  1.00 54.96           O  
ANISOU 4429  O   ARG B 199     5611   8062   7208   -590    216    131       O  
ATOM   4430  CB  ARG B 199       4.421  21.193  -6.884  1.00 49.99           C  
ANISOU 4430  CB  ARG B 199     4739   7454   6800   -611    193     40       C  
ATOM   4431  CG  ARG B 199       5.032  22.533  -6.451  1.00 52.59           C  
ANISOU 4431  CG  ARG B 199     5068   7741   7172   -690    154     85       C  
ATOM   4432  CD  ARG B 199       5.798  22.512  -5.129  1.00 49.16           C  
ANISOU 4432  CD  ARG B 199     4594   7265   6821   -693     48     64       C  
ATOM   4433  NE  ARG B 199       4.958  23.088  -4.092  1.00 63.66           N  
ANISOU 4433  NE  ARG B 199     6547   9031   8610   -695    -28     74       N  
ATOM   4434  CZ  ARG B 199       5.077  24.315  -3.608  1.00 68.93           C  
ANISOU 4434  CZ  ARG B 199     7251   9645   9295   -769    -58     86       C  
ATOM   4435  NH1 ARG B 199       6.084  25.091  -3.986  1.00 39.17           N  
ANISOU 4435  NH1 ARG B 199     3407   5882   5594   -849    -31    101       N  
ATOM   4436  NH2 ARG B 199       4.216  24.763  -2.709  1.00 71.14           N  
ANISOU 4436  NH2 ARG B 199     7636   9861   9532   -767   -109     73       N  
ATOM   4437  N   THR B 200       1.571  22.544  -5.459  1.00 50.46           N  
ANISOU 4437  N   THR B 200     5097   7359   6715   -572     73    110       N  
ATOM   4438  CA  THR B 200       0.583  23.622  -5.429  1.00 49.49           C  
ANISOU 4438  CA  THR B 200     5072   7176   6556   -587     71    157       C  
ATOM   4439  C   THR B 200       0.834  24.486  -4.190  1.00 51.42           C  
ANISOU 4439  C   THR B 200     5349   7335   6854   -627      6    140       C  
ATOM   4440  O   THR B 200       1.148  23.953  -3.129  1.00 51.06           O  
ANISOU 4440  O   THR B 200     5293   7288   6820   -614    -60     90       O  
ATOM   4441  CB  THR B 200      -0.878  23.063  -5.489  1.00 57.37           C  
ANISOU 4441  CB  THR B 200     6147   8173   7478   -517     72    155       C  
ATOM   4442  OG1 THR B 200      -1.790  24.150  -5.352  1.00 62.74           O  
ANISOU 4442  OG1 THR B 200     6904   8779   8153   -526     66    200       O  
ATOM   4443  CG2 THR B 200      -1.185  21.989  -4.429  1.00 50.84           C  
ANISOU 4443  CG2 THR B 200     5337   7334   6647   -458     16     95       C  
ATOM   4444  N   ASP B 201       0.712  25.804  -4.324  1.00 48.30           N  
ANISOU 4444  N   ASP B 201     4988   6871   6492   -680     24    180       N  
ATOM   4445  CA  ASP B 201       0.904  26.713  -3.192  1.00 49.20           C  
ANISOU 4445  CA  ASP B 201     5135   6897   6662   -731    -24    140       C  
ATOM   4446  C   ASP B 201      -0.377  26.851  -2.367  1.00 53.56           C  
ANISOU 4446  C   ASP B 201     5787   7384   7181   -688    -47    104       C  
ATOM   4447  O   ASP B 201      -0.323  27.387  -1.266  1.00 53.56           O  
ANISOU 4447  O   ASP B 201     5819   7329   7202   -727    -86     39       O  
ATOM   4448  CB  ASP B 201       1.350  28.093  -3.675  1.00 52.04           C  
ANISOU 4448  CB  ASP B 201     5482   7188   7102   -811     16    191       C  
ATOM   4449  CG  ASP B 201       2.815  28.228  -4.074  1.00 63.05           C  
ANISOU 4449  CG  ASP B 201     6774   8628   8553   -884     28    202       C  
ATOM   4450  OD1 ASP B 201       3.607  27.296  -3.784  1.00 59.38           O  
ANISOU 4450  OD1 ASP B 201     6239   8241   8082   -874     -6    157       O  
ATOM   4451  OD2 ASP B 201       3.174  29.285  -4.639  1.00 72.06           O  
ANISOU 4451  OD2 ASP B 201     7900   9720   9760   -953     72    261       O  
ATOM   4452  N   ASN B 202      -1.517  26.382  -2.913  1.00 49.86           N  
ANISOU 4452  N   ASN B 202     5360   6929   6657   -617    -17    138       N  
ATOM   4453  CA  ASN B 202      -2.844  26.468  -2.307  1.00 50.07           C  
ANISOU 4453  CA  ASN B 202     5468   6899   6657   -570    -23    111       C  
ATOM   4454  C   ASN B 202      -2.982  25.510  -1.092  1.00 51.86           C  
ANISOU 4454  C   ASN B 202     5719   7160   6826   -545    -78     32       C  
ATOM   4455  O   ASN B 202      -3.078  24.293  -1.275  1.00 49.06           O  
ANISOU 4455  O   ASN B 202     5343   6878   6421   -495    -89     37       O  
ATOM   4456  CB  ASN B 202      -3.923  26.185  -3.371  1.00 53.00           C  
ANISOU 4456  CB  ASN B 202     5855   7298   6986   -509     18    180       C  
ATOM   4457  CG  ASN B 202      -5.367  26.432  -2.967  1.00 76.65           C  
ANISOU 4457  CG  ASN B 202     8917  10227   9979   -459     24    172       C  
ATOM   4458  OD1 ASN B 202      -5.725  26.678  -1.799  1.00 66.16           O  
ANISOU 4458  OD1 ASN B 202     7635   8836   8666   -461      8     97       O  
ATOM   4459  ND2 ASN B 202      -6.238  26.348  -3.953  1.00 72.41           N  
ANISOU 4459  ND2 ASN B 202     8380   9716   9417   -418     50    246       N  
ATOM   4460  N   PRO B 203      -3.031  26.075   0.148  1.00 49.02           N  
ANISOU 4460  N   PRO B 203     5403   6748   6474   -586   -109    -40       N  
ATOM   4461  CA  PRO B 203      -3.145  25.232   1.354  1.00 48.76           C  
ANISOU 4461  CA  PRO B 203     5395   6765   6367   -579   -166    -97       C  
ATOM   4462  C   PRO B 203      -4.434  24.426   1.434  1.00 54.98           C  
ANISOU 4462  C   PRO B 203     6233   7566   7091   -503   -149    -94       C  
ATOM   4463  O   PRO B 203      -4.428  23.350   2.036  1.00 55.23           O  
ANISOU 4463  O   PRO B 203     6263   7658   7063   -482   -192   -101       O  
ATOM   4464  CB  PRO B 203      -3.080  26.241   2.502  1.00 50.99           C  
ANISOU 4464  CB  PRO B 203     5721   6993   6659   -656   -183   -184       C  
ATOM   4465  CG  PRO B 203      -2.485  27.470   1.913  1.00 55.65           C  
ANISOU 4465  CG  PRO B 203     6284   7508   7355   -712   -149   -173       C  
ATOM   4466  CD  PRO B 203      -2.947  27.507   0.507  1.00 50.84           C  
ANISOU 4466  CD  PRO B 203     5659   6876   6781   -652    -90    -76       C  
ATOM   4467  N   LYS B 204      -5.532  24.933   0.827  1.00 52.78           N  
ANISOU 4467  N   LYS B 204     5989   7230   6835   -464    -90    -73       N  
ATOM   4468  CA  LYS B 204      -6.821  24.229   0.778  1.00 52.19           C  
ANISOU 4468  CA  LYS B 204     5951   7168   6712   -395    -69    -68       C  
ATOM   4469  C   LYS B 204      -6.723  22.979  -0.135  1.00 56.28           C  
ANISOU 4469  C   LYS B 204     6422   7764   7196   -345    -71    -17       C  
ATOM   4470  O   LYS B 204      -7.571  22.087  -0.044  1.00 55.37           O  
ANISOU 4470  O   LYS B 204     6327   7675   7037   -297    -66    -22       O  
ATOM   4471  CB  LYS B 204      -7.937  25.167   0.315  1.00 54.29           C  
ANISOU 4471  CB  LYS B 204     6245   7352   7032   -368    -14    -50       C  
ATOM   4472  CG  LYS B 204      -8.443  26.073   1.445  1.00 77.17           C  
ANISOU 4472  CG  LYS B 204     9195  10163   9963   -399      6   -136       C  
ATOM   4473  CD  LYS B 204      -9.197  27.302   0.934  1.00 93.20           C  
ANISOU 4473  CD  LYS B 204    11229  12077  12107   -381     62   -109       C  
ATOM   4474  CE  LYS B 204      -9.578  28.240   2.059  1.00109.84           C  
ANISOU 4474  CE  LYS B 204    13379  14085  14272   -417     98   -221       C  
ATOM   4475  NZ  LYS B 204      -9.993  29.579   1.555  1.00120.58           N  
ANISOU 4475  NZ  LYS B 204    14725  15301  15790   -407    152   -189       N  
ATOM   4476  N   SER B 205      -5.661  22.904  -0.979  1.00 51.99           N  
ANISOU 4476  N   SER B 205     5815   7259   6680   -364    -70     20       N  
ATOM   4477  CA  SER B 205      -5.417  21.780  -1.878  1.00 50.83           C  
ANISOU 4477  CA  SER B 205     5614   7186   6514   -329    -56     42       C  
ATOM   4478  C   SER B 205      -4.481  20.763  -1.293  1.00 52.36           C  
ANISOU 4478  C   SER B 205     5759   7417   6717   -328   -100     19       C  
ATOM   4479  O   SER B 205      -4.415  19.668  -1.838  1.00 51.44           O  
ANISOU 4479  O   SER B 205     5600   7343   6601   -291    -84     18       O  
ATOM   4480  CB  SER B 205      -4.829  22.255  -3.203  1.00 56.26           C  
ANISOU 4480  CB  SER B 205     6251   7904   7223   -356    -14     91       C  
ATOM   4481  OG  SER B 205      -5.621  23.239  -3.844  1.00 69.42           O  
ANISOU 4481  OG  SER B 205     7949   9536   8892   -359     18    145       O  
ATOM   4482  N   TRP B 206      -3.746  21.091  -0.210  1.00 49.55           N  
ANISOU 4482  N   TRP B 206     5403   7049   6376   -372   -157      0       N  
ATOM   4483  CA  TRP B 206      -2.731  20.178   0.322  1.00 50.41           C  
ANISOU 4483  CA  TRP B 206     5446   7197   6509   -373   -214      3       C  
ATOM   4484  C   TRP B 206      -3.318  18.897   0.882  1.00 57.60           C  
ANISOU 4484  C   TRP B 206     6373   8121   7393   -321   -241      9       C  
ATOM   4485  O   TRP B 206      -4.410  18.894   1.435  1.00 57.15           O  
ANISOU 4485  O   TRP B 206     6393   8047   7276   -310   -239     -3       O  
ATOM   4486  CB  TRP B 206      -1.790  20.843   1.338  1.00 49.56           C  
ANISOU 4486  CB  TRP B 206     5327   7091   6413   -444   -283    -11       C  
ATOM   4487  CG  TRP B 206      -0.991  21.988   0.768  1.00 50.01           C  
ANISOU 4487  CG  TRP B 206     5349   7130   6525   -504   -259    -14       C  
ATOM   4488  CD1 TRP B 206      -0.756  22.256  -0.553  1.00 52.69           C  
ANISOU 4488  CD1 TRP B 206     5645   7470   6904   -500   -191     13       C  
ATOM   4489  CD2 TRP B 206      -0.348  23.033   1.508  1.00 50.02           C  
ANISOU 4489  CD2 TRP B 206     5353   7112   6542   -588   -299    -46       C  
ATOM   4490  NE1 TRP B 206      -0.037  23.423  -0.679  1.00 52.55           N  
ANISOU 4490  NE1 TRP B 206     5607   7426   6935   -572   -184     14       N  
ATOM   4491  CE2 TRP B 206       0.220  23.927   0.569  1.00 53.94           C  
ANISOU 4491  CE2 TRP B 206     5808   7581   7105   -627   -249    -29       C  
ATOM   4492  CE3 TRP B 206      -0.246  23.336   2.875  1.00 51.33           C  
ANISOU 4492  CE3 TRP B 206     5554   7287   6663   -645   -369    -92       C  
ATOM   4493  CZ2 TRP B 206       0.923  25.071   0.955  1.00 53.56           C  
ANISOU 4493  CZ2 TRP B 206     5749   7498   7103   -717   -266    -59       C  
ATOM   4494  CZ3 TRP B 206       0.466  24.464   3.256  1.00 53.27           C  
ANISOU 4494  CZ3 TRP B 206     5788   7510   6941   -739   -388   -136       C  
ATOM   4495  CH2 TRP B 206       1.033  25.321   2.302  1.00 54.00           C  
ANISOU 4495  CH2 TRP B 206     5837   7558   7122   -771   -336   -120       C  
ATOM   4496  N   TYR B 207      -2.602  17.790   0.643  1.00 56.91           N  
ANISOU 4496  N   TYR B 207     6204   8056   7365   -288   -254     28       N  
ATOM   4497  CA  TYR B 207      -2.994  16.459   1.062  1.00 57.05           C  
ANISOU 4497  CA  TYR B 207     6216   8070   7392   -236   -276     47       C  
ATOM   4498  C   TYR B 207      -2.553  16.219   2.483  1.00 64.03           C  
ANISOU 4498  C   TYR B 207     7100   8969   8259   -262   -376     88       C  
ATOM   4499  O   TYR B 207      -1.358  16.141   2.755  1.00 65.25           O  
ANISOU 4499  O   TYR B 207     7175   9145   8472   -283   -435    116       O  
ATOM   4500  CB  TYR B 207      -2.402  15.413   0.116  1.00 58.57           C  
ANISOU 4500  CB  TYR B 207     6308   8262   7682   -190   -237     42       C  
ATOM   4501  CG  TYR B 207      -2.868  14.010   0.410  1.00 60.42           C  
ANISOU 4501  CG  TYR B 207     6532   8468   7957   -134   -245     59       C  
ATOM   4502  CD1 TYR B 207      -4.179  13.620   0.142  1.00 61.24           C  
ANISOU 4502  CD1 TYR B 207     6701   8556   8013   -107   -196     35       C  
ATOM   4503  CD2 TYR B 207      -2.006  13.070   0.962  1.00 62.59           C  
ANISOU 4503  CD2 TYR B 207     6723   8725   8333   -109   -303    107       C  
ATOM   4504  CE1 TYR B 207      -4.622  12.331   0.426  1.00 61.77           C  
ANISOU 4504  CE1 TYR B 207     6757   8585   8129    -64   -199     51       C  
ATOM   4505  CE2 TYR B 207      -2.440  11.778   1.260  1.00 64.25           C  
ANISOU 4505  CE2 TYR B 207     6921   8890   8603    -59   -310    137       C  
ATOM   4506  CZ  TYR B 207      -3.747  11.411   0.979  1.00 70.43           C  
ANISOU 4506  CZ  TYR B 207     7775   9651   9335    -40   -254    104       C  
ATOM   4507  OH  TYR B 207      -4.181  10.140   1.250  1.00 71.48           O  
ANISOU 4507  OH  TYR B 207     7893   9729   9539      2   -254    133       O  
ATOM   4508  N   GLU B 208      -3.535  16.140   3.397  1.00 62.05           N  
ANISOU 4508  N   GLU B 208     6936   8718   7921   -269   -396     94       N  
ATOM   4509  CA  GLU B 208      -3.389  15.909   4.834  1.00 62.33           C  
ANISOU 4509  CA  GLU B 208     6996   8791   7897   -308   -487    137       C  
ATOM   4510  C   GLU B 208      -2.373  16.899   5.431  1.00 68.54           C  
ANISOU 4510  C   GLU B 208     7763   9619   8659   -388   -553    124       C  
ATOM   4511  O   GLU B 208      -2.608  18.107   5.340  1.00 69.17           O  
ANISOU 4511  O   GLU B 208     7896   9687   8698   -434   -515     57       O  
ATOM   4512  CB  GLU B 208      -3.038  14.441   5.119  1.00 63.88           C  
ANISOU 4512  CB  GLU B 208     7124   8984   8163   -261   -539    222       C  
ATOM   4513  CG  GLU B 208      -4.061  13.487   4.514  1.00 70.65           C  
ANISOU 4513  CG  GLU B 208     7998   9790   9055   -193   -467    219       C  
ATOM   4514  CD  GLU B 208      -4.358  12.179   5.220  1.00 73.39           C  
ANISOU 4514  CD  GLU B 208     8337  10120   9428   -165   -510    303       C  
ATOM   4515  OE1 GLU B 208      -3.506  11.698   5.999  1.00 61.00           O  
ANISOU 4515  OE1 GLU B 208     6709   8571   7897   -175   -604    394       O  
ATOM   4516  OE2 GLU B 208      -5.440  11.610   4.952  1.00 63.52           O  
ANISOU 4516  OE2 GLU B 208     7130   8833   8170   -133   -450    288       O  
ATOM   4517  N   ASP B 209      -1.250  16.414   5.989  1.00 65.70           N  
ANISOU 4517  N   ASP B 209     7320   9302   8341   -405   -649    189       N  
ATOM   4518  CA  ASP B 209      -0.233  17.269   6.604  1.00 66.25           C  
ANISOU 4518  CA  ASP B 209     7358   9427   8388   -491   -726    178       C  
ATOM   4519  C   ASP B 209       0.940  17.576   5.655  1.00 66.60           C  
ANISOU 4519  C   ASP B 209     7292   9455   8558   -486   -712    169       C  
ATOM   4520  O   ASP B 209       1.863  18.287   6.064  1.00 67.32           O  
ANISOU 4520  O   ASP B 209     7342   9588   8651   -561   -773    156       O  
ATOM   4521  CB  ASP B 209       0.290  16.612   7.898  1.00 70.67           C  
ANISOU 4521  CB  ASP B 209     7885  10066   8901   -528   -860    268       C  
ATOM   4522  CG  ASP B 209      -0.636  16.730   9.098  1.00 94.37           C  
ANISOU 4522  CG  ASP B 209    11001  13124  11733   -586   -886    260       C  
ATOM   4523  OD1 ASP B 209      -0.126  16.979  10.221  1.00 98.50           O  
ANISOU 4523  OD1 ASP B 209    11522  13743  12159   -677   -990    282       O  
ATOM   4524  OD2 ASP B 209      -1.872  16.542   8.925  1.00103.29           O  
ANISOU 4524  OD2 ASP B 209    12215  14211  12820   -548   -803    231       O  
ATOM   4525  N   VAL B 210       0.906  17.056   4.400  1.00 59.55           N  
ANISOU 4525  N   VAL B 210     6350   8512   7765   -410   -627    166       N  
ATOM   4526  CA  VAL B 210       1.966  17.276   3.396  1.00 58.37           C  
ANISOU 4526  CA  VAL B 210     6092   8355   7730   -407   -591    152       C  
ATOM   4527  C   VAL B 210       1.843  18.710   2.852  1.00 61.03           C  
ANISOU 4527  C   VAL B 210     6482   8678   8031   -466   -526     88       C  
ATOM   4528  O   VAL B 210       0.910  19.007   2.102  1.00 62.22           O  
ANISOU 4528  O   VAL B 210     6701   8792   8147   -442   -438     57       O  
ATOM   4529  CB  VAL B 210       1.969  16.227   2.245  1.00 60.43           C  
ANISOU 4529  CB  VAL B 210     6281   8581   8097   -320   -510    154       C  
ATOM   4530  CG1 VAL B 210       3.205  16.386   1.366  1.00 60.34           C  
ANISOU 4530  CG1 VAL B 210     6142   8582   8203   -328   -474    137       C  
ATOM   4531  CG2 VAL B 210       1.867  14.796   2.777  1.00 60.14           C  
ANISOU 4531  CG2 VAL B 210     6206   8527   8118   -255   -560    218       C  
ATOM   4532  N   GLU B 211       2.766  19.590   3.246  1.00 55.04           N  
ANISOU 4532  N   GLU B 211     5684   7944   7286   -547   -576     74       N  
ATOM   4533  CA  GLU B 211       2.752  20.987   2.816  1.00 54.30           C  
ANISOU 4533  CA  GLU B 211     5630   7819   7183   -612   -520     22       C  
ATOM   4534  C   GLU B 211       3.354  21.143   1.427  1.00 57.89           C  
ANISOU 4534  C   GLU B 211     6006   8262   7729   -600   -435     28       C  
ATOM   4535  O   GLU B 211       4.417  20.591   1.139  1.00 59.46           O  
ANISOU 4535  O   GLU B 211     6082   8494   8017   -590   -451     50       O  
ATOM   4536  CB  GLU B 211       3.485  21.887   3.819  1.00 56.46           C  
ANISOU 4536  CB  GLU B 211     5895   8121   7438   -718   -603     -8       C  
ATOM   4537  CG  GLU B 211       2.767  22.041   5.147  1.00 64.12           C  
ANISOU 4537  CG  GLU B 211     6963   9114   8286   -758   -665    -39       C  
ATOM   4538  CD  GLU B 211       3.593  22.636   6.272  1.00 86.62           C  
ANISOU 4538  CD  GLU B 211     9792  12023  11098   -873   -765    -76       C  
ATOM   4539  OE1 GLU B 211       4.806  22.873   6.071  1.00 67.94           O  
ANISOU 4539  OE1 GLU B 211     7318   9684   8814   -918   -806    -64       O  
ATOM   4540  OE2 GLU B 211       3.012  22.896   7.350  1.00 89.62           O  
ANISOU 4540  OE2 GLU B 211    10261  12430  11361   -928   -797   -126       O  
ATOM   4541  N   GLY B 212       2.661  21.893   0.583  1.00 53.01           N  
ANISOU 4541  N   GLY B 212     5452   7602   7088   -603   -345     13       N  
ATOM   4542  CA  GLY B 212       3.073  22.185  -0.784  1.00 52.81           C  
ANISOU 4542  CA  GLY B 212     5371   7579   7115   -608   -255     27       C  
ATOM   4543  C   GLY B 212       2.619  21.177  -1.817  1.00 56.34           C  
ANISOU 4543  C   GLY B 212     5799   8052   7556   -532   -183     36       C  
ATOM   4544  O   GLY B 212       2.834  21.410  -3.009  1.00 55.72           O  
ANISOU 4544  O   GLY B 212     5685   7996   7490   -545    -99     45       O  
ATOM   4545  N   CYS B 213       1.992  20.044  -1.375  1.00 52.01           N  
ANISOU 4545  N   CYS B 213     5272   7506   6984   -462   -211     32       N  
ATOM   4546  CA  CYS B 213       1.559  18.956  -2.249  1.00 51.33           C  
ANISOU 4546  CA  CYS B 213     5163   7437   6903   -394   -145     20       C  
ATOM   4547  C   CYS B 213       0.112  18.578  -2.041  1.00 54.31           C  
ANISOU 4547  C   CYS B 213     5644   7790   7200   -347   -140     16       C  
ATOM   4548  O   CYS B 213      -0.298  18.300  -0.917  1.00 53.89           O  
ANISOU 4548  O   CYS B 213     5640   7715   7121   -334   -208     26       O  
ATOM   4549  CB  CYS B 213       2.442  17.726  -2.081  1.00 52.57           C  
ANISOU 4549  CB  CYS B 213     5204   7606   7163   -350   -170     16       C  
ATOM   4550  SG  CYS B 213       4.209  18.065  -2.112  1.00 58.17           S  
ANISOU 4550  SG  CYS B 213     5767   8346   7990   -401   -191     23       S  
ATOM   4551  N   GLY B 214      -0.606  18.460  -3.155  1.00 51.09           N  
ANISOU 4551  N   GLY B 214     5257   7401   6753   -327    -60      3       N  
ATOM   4552  CA  GLY B 214      -1.986  18.005  -3.210  1.00 50.96           C  
ANISOU 4552  CA  GLY B 214     5318   7373   6671   -283    -43     -5       C  
ATOM   4553  C   GLY B 214      -2.119  16.764  -4.073  1.00 55.64           C  
ANISOU 4553  C   GLY B 214     5859   7997   7284   -240     16    -47       C  
ATOM   4554  O   GLY B 214      -1.227  16.463  -4.865  1.00 56.28           O  
ANISOU 4554  O   GLY B 214     5853   8117   7415   -251     68    -75       O  
ATOM   4555  N   ILE B 215      -3.232  16.043  -3.944  1.00 52.61           N  
ANISOU 4555  N   ILE B 215     5526   7597   6867   -198     18    -62       N  
ATOM   4556  CA  ILE B 215      -3.489  14.833  -4.732  1.00 52.27           C  
ANISOU 4556  CA  ILE B 215     5439   7573   6847   -165     79   -119       C  
ATOM   4557  C   ILE B 215      -3.803  15.237  -6.182  1.00 53.15           C  
ANISOU 4557  C   ILE B 215     5548   7765   6882   -199    158   -145       C  
ATOM   4558  O   ILE B 215      -4.627  16.119  -6.399  1.00 51.29           O  
ANISOU 4558  O   ILE B 215     5380   7547   6560   -220    152   -103       O  
ATOM   4559  CB  ILE B 215      -4.603  13.937  -4.089  1.00 55.03           C  
ANISOU 4559  CB  ILE B 215     5839   7878   7192   -119     56   -126       C  
ATOM   4560  CG1 ILE B 215      -4.972  12.722  -4.958  1.00 55.81           C  
ANISOU 4560  CG1 ILE B 215     5893   7987   7324    -95    126   -202       C  
ATOM   4561  CG2 ILE B 215      -5.840  14.723  -3.699  1.00 55.56           C  
ANISOU 4561  CG2 ILE B 215     6010   7940   7162   -126     33    -94       C  
ATOM   4562  CD1 ILE B 215      -3.894  11.616  -4.999  1.00 69.13           C  
ANISOU 4562  CD1 ILE B 215     7471   9636   9159    -65    148   -244       C  
ATOM   4563  N   GLN B 216      -3.117  14.620  -7.163  1.00 49.62           N  
ANISOU 4563  N   GLN B 216     5016   7369   6469   -210    233   -211       N  
ATOM   4564  CA  GLN B 216      -3.346  14.897  -8.596  1.00 49.83           C  
ANISOU 4564  CA  GLN B 216     5032   7500   6399   -260    313   -240       C  
ATOM   4565  C   GLN B 216      -4.820  14.621  -8.969  1.00 55.49           C  
ANISOU 4565  C   GLN B 216     5815   8248   7021   -252    317   -253       C  
ATOM   4566  O   GLN B 216      -5.459  13.721  -8.400  1.00 53.42           O  
ANISOU 4566  O   GLN B 216     5572   7929   6798   -206    297   -287       O  
ATOM   4567  CB  GLN B 216      -2.397  14.072  -9.499  1.00 50.82           C  
ANISOU 4567  CB  GLN B 216     5050   7679   6580   -276    407   -341       C  
ATOM   4568  CG  GLN B 216      -2.548  12.563  -9.285  1.00 55.35           C  
ANISOU 4568  CG  GLN B 216     5581   8196   7255   -222    432   -437       C  
ATOM   4569  CD  GLN B 216      -1.794  11.699 -10.239  1.00 63.01           C  
ANISOU 4569  CD  GLN B 216     6443   9209   8289   -238    544   -563       C  
ATOM   4570  OE1 GLN B 216      -0.614  11.895 -10.486  1.00 59.10           O  
ANISOU 4570  OE1 GLN B 216     5865   8735   7857   -257    584   -577       O  
ATOM   4571  NE2 GLN B 216      -2.446  10.655 -10.715  1.00 56.29           N  
ANISOU 4571  NE2 GLN B 216     5582   8362   7443   -229    601   -670       N  
ATOM   4572  N   CYS B 217      -5.343  15.387  -9.930  1.00 55.40           N  
ANISOU 4572  N   CYS B 217     5830   8330   6888   -301    339   -215       N  
ATOM   4573  CA  CYS B 217      -6.721  15.243 -10.390  1.00 56.14           C  
ANISOU 4573  CA  CYS B 217     5972   8474   6887   -303    334   -215       C  
ATOM   4574  C   CYS B 217      -7.043  13.820 -10.902  1.00 58.65           C  
ANISOU 4574  C   CYS B 217     6250   8828   7207   -299    390   -344       C  
ATOM   4575  O   CYS B 217      -8.132  13.309 -10.625  1.00 58.06           O  
ANISOU 4575  O   CYS B 217     6210   8726   7122   -272    366   -362       O  
ATOM   4576  CB  CYS B 217      -7.050  16.276 -11.453  1.00 57.83           C  
ANISOU 4576  CB  CYS B 217     6200   8797   6975   -364    343   -134       C  
ATOM   4577  SG  CYS B 217      -8.743  16.133 -12.066  1.00 62.38           S  
ANISOU 4577  SG  CYS B 217     6814   9452   7434   -370    321   -118       S  
ATOM   4578  N   GLN B 218      -6.131  13.218 -11.678  1.00 53.91           N  
ANISOU 4578  N   GLN B 218     5572   8286   6626   -333    473   -441       N  
ATOM   4579  CA  GLN B 218      -6.315  11.872 -12.218  1.00 53.75           C  
ANISOU 4579  CA  GLN B 218     5503   8290   6631   -337    545   -590       C  
ATOM   4580  C   GLN B 218      -6.253  10.854 -11.111  1.00 55.77           C  
ANISOU 4580  C   GLN B 218     5745   8392   7054   -260    521   -626       C  
ATOM   4581  O   GLN B 218      -5.243  10.794 -10.404  1.00 55.48           O  
ANISOU 4581  O   GLN B 218     5668   8270   7140   -223    505   -602       O  
ATOM   4582  CB  GLN B 218      -5.253  11.556 -13.276  1.00 56.22           C  
ANISOU 4582  CB  GLN B 218     5727   8696   6938   -394    655   -696       C  
ATOM   4583  CG  GLN B 218      -5.785  11.663 -14.685  1.00 72.63           C  
ANISOU 4583  CG  GLN B 218     7806  10960   8831   -487    714   -747       C  
ATOM   4584  CD  GLN B 218      -5.614  10.380 -15.448  1.00 89.20           C  
ANISOU 4584  CD  GLN B 218     9834  13106  10954   -520    825   -950       C  
ATOM   4585  OE1 GLN B 218      -4.575   9.698 -15.376  1.00 81.91           O  
ANISOU 4585  OE1 GLN B 218     8828  12117  10177   -498    902  -1056       O  
ATOM   4586  NE2 GLN B 218      -6.620  10.059 -16.243  1.00 80.60           N  
ANISOU 4586  NE2 GLN B 218     8767  12135   9724   -580    840  -1012       N  
ATOM   4587  N   ASN B 219      -7.348  10.090 -10.927  1.00 51.76           N  
ANISOU 4587  N   ASN B 219     5268   7851   6549   -241    510   -669       N  
ATOM   4588  CA  ASN B 219      -7.467   9.044  -9.914  1.00 51.26           C  
ANISOU 4588  CA  ASN B 219     5196   7643   6639   -176    489   -689       C  
ATOM   4589  C   ASN B 219      -6.241   8.149 -10.025  1.00 57.02           C  
ANISOU 4589  C   ASN B 219     5822   8311   7531   -156    557   -780       C  
ATOM   4590  O   ASN B 219      -6.040   7.540 -11.083  1.00 59.71           O  
ANISOU 4590  O   ASN B 219     6101   8712   7873   -195    657   -920       O  
ATOM   4591  CB  ASN B 219      -8.778   8.256 -10.090  1.00 50.40           C  
ANISOU 4591  CB  ASN B 219     5114   7532   6503   -183    499   -753       C  
ATOM   4592  CG  ASN B 219      -9.119   7.310  -8.963  1.00 72.38           C  
ANISOU 4592  CG  ASN B 219     7909  10167   9425   -123    464   -734       C  
ATOM   4593  OD1 ASN B 219      -8.262   6.651  -8.361  1.00 65.21           O  
ANISOU 4593  OD1 ASN B 219     6951   9150   8677    -78    467   -733       O  
ATOM   4594  ND2 ASN B 219     -10.403   7.191  -8.678  1.00 68.43           N  
ANISOU 4594  ND2 ASN B 219     7466   9662   8870   -124    431   -711       N  
ATOM   4595  N   PRO B 220      -5.354   8.141  -8.997  1.00 52.37           N  
ANISOU 4595  N   PRO B 220     5205   7618   7075   -101    505   -704       N  
ATOM   4596  CA  PRO B 220      -4.095   7.379  -9.117  1.00 53.25           C  
ANISOU 4596  CA  PRO B 220     5197   7669   7365    -75    565   -775       C  
ATOM   4597  C   PRO B 220      -4.213   5.844  -9.090  1.00 58.25           C  
ANISOU 4597  C   PRO B 220     5768   8190   8175    -36    621   -879       C  
ATOM   4598  O   PRO B 220      -3.229   5.161  -9.405  1.00 59.35           O  
ANISOU 4598  O   PRO B 220     5793   8279   8477    -16    696   -968       O  
ATOM   4599  CB  PRO B 220      -3.295   7.849  -7.906  1.00 55.03           C  
ANISOU 4599  CB  PRO B 220     5416   7822   7671    -30    466   -638       C  
ATOM   4600  CG  PRO B 220      -4.305   8.320  -6.918  1.00 57.69           C  
ANISOU 4600  CG  PRO B 220     5867   8135   7916    -19    364   -524       C  
ATOM   4601  CD  PRO B 220      -5.418   8.887  -7.718  1.00 52.73           C  
ANISOU 4601  CD  PRO B 220     5316   7610   7110    -69    392   -554       C  
ATOM   4602  N   LEU B 221      -5.381   5.299  -8.713  1.00 53.67           N  
ANISOU 4602  N   LEU B 221     5250   7558   7583    -24    592   -871       N  
ATOM   4603  CA  LEU B 221      -5.587   3.845  -8.617  1.00 53.77           C  
ANISOU 4603  CA  LEU B 221     5210   7443   7779      9    641   -958       C  
ATOM   4604  C   LEU B 221      -5.974   3.206  -9.957  1.00 55.32           C  
ANISOU 4604  C   LEU B 221     5367   7702   7948    -50    769  -1163       C  
ATOM   4605  O   LEU B 221      -6.061   1.981 -10.043  1.00 54.95           O  
ANISOU 4605  O   LEU B 221     5261   7544   8074    -32    834  -1271       O  
ATOM   4606  CB  LEU B 221      -6.688   3.535  -7.575  1.00 53.24           C  
ANISOU 4606  CB  LEU B 221     5224   7295   7708     36    559   -856       C  
ATOM   4607  CG  LEU B 221      -6.601   4.219  -6.222  1.00 57.16           C  
ANISOU 4607  CG  LEU B 221     5782   7759   8178     72    432   -664       C  
ATOM   4608  CD1 LEU B 221      -7.826   3.923  -5.422  1.00 57.92           C  
ANISOU 4608  CD1 LEU B 221     5958   7804   8245     79    382   -597       C  
ATOM   4609  CD2 LEU B 221      -5.338   3.829  -5.461  1.00 57.56           C  
ANISOU 4609  CD2 LEU B 221     5746   7707   8418    129    394   -589       C  
ATOM   4610  N   PHE B 222      -6.245   4.027 -10.979  1.00 50.54           N  
ANISOU 4610  N   PHE B 222     4797   7276   7129   -127    802  -1213       N  
ATOM   4611  CA  PHE B 222      -6.690   3.552 -12.289  1.00 51.08           C  
ANISOU 4611  CA  PHE B 222     4839   7449   7118   -207    912  -1404       C  
ATOM   4612  C   PHE B 222      -5.824   4.151 -13.378  1.00 59.08           C  
ANISOU 4612  C   PHE B 222     5804   8616   8027   -270    993  -1479       C  
ATOM   4613  O   PHE B 222      -5.523   5.349 -13.360  1.00 58.75           O  
ANISOU 4613  O   PHE B 222     5802   8666   7855   -285    939  -1354       O  
ATOM   4614  CB  PHE B 222      -8.197   3.859 -12.524  1.00 50.94           C  
ANISOU 4614  CB  PHE B 222     4915   7530   6909   -258    864  -1386       C  
ATOM   4615  CG  PHE B 222      -9.085   3.274 -11.443  1.00 50.78           C  
ANISOU 4615  CG  PHE B 222     4940   7366   6986   -204    795  -1314       C  
ATOM   4616  CD1 PHE B 222      -9.374   1.912 -11.416  1.00 53.90           C  
ANISOU 4616  CD1 PHE B 222     5288   7640   7551   -197    856  -1437       C  
ATOM   4617  CD2 PHE B 222      -9.572   4.070 -10.413  1.00 50.27           C  
ANISOU 4617  CD2 PHE B 222     4960   7279   6860   -165    678  -1127       C  
ATOM   4618  CE1 PHE B 222     -10.132   1.358 -10.378  1.00 53.24           C  
ANISOU 4618  CE1 PHE B 222     5244   7420   7566   -152    797  -1354       C  
ATOM   4619  CE2 PHE B 222     -10.365   3.524  -9.402  1.00 51.71           C  
ANISOU 4619  CE2 PHE B 222     5181   7342   7123   -124    625  -1061       C  
ATOM   4620  CZ  PHE B 222     -10.633   2.168  -9.389  1.00 50.62           C  
ANISOU 4620  CZ  PHE B 222     4997   7089   7146   -119    683  -1165       C  
ATOM   4621  N   THR B 223      -5.403   3.296 -14.311  1.00 58.87           N  
ANISOU 4621  N   THR B 223     5688   8611   8069   -313   1132  -1690       N  
ATOM   4622  CA  THR B 223      -4.538   3.645 -15.439  1.00 60.56           C  
ANISOU 4622  CA  THR B 223     5840   8977   8194   -387   1242  -1800       C  
ATOM   4623  C   THR B 223      -5.292   4.484 -16.471  1.00 66.78           C  
ANISOU 4623  C   THR B 223     6699  10007   8669   -501   1238  -1799       C  
ATOM   4624  O   THR B 223      -6.524   4.429 -16.525  1.00 66.13           O  
ANISOU 4624  O   THR B 223     6687   9965   8474   -528   1182  -1784       O  
ATOM   4625  CB  THR B 223      -3.996   2.358 -16.091  1.00 65.56           C  
ANISOU 4625  CB  THR B 223     6352   9550   9006   -402   1406  -2053       C  
ATOM   4626  OG1 THR B 223      -5.078   1.638 -16.703  1.00 64.42           O  
ANISOU 4626  OG1 THR B 223     6234   9448   8797   -467   1452  -2207       O  
ATOM   4627  CG2 THR B 223      -3.254   1.465 -15.100  1.00 61.61           C  
ANISOU 4627  CG2 THR B 223     5762   8799   8846   -283   1408  -2038       C  
ATOM   4628  N   GLU B 224      -4.546   5.203 -17.329  1.00 65.75           N  
ANISOU 4628  N   GLU B 224     6539  10039   8404   -573   1301  -1814       N  
ATOM   4629  CA  GLU B 224      -5.095   6.004 -18.422  1.00 66.38           C  
ANISOU 4629  CA  GLU B 224     6670  10367   8185   -693   1304  -1799       C  
ATOM   4630  C   GLU B 224      -5.986   5.119 -19.286  1.00 70.36           C  
ANISOU 4630  C   GLU B 224     7170  10972   8593   -780   1372  -1995       C  
ATOM   4631  O   GLU B 224      -7.088   5.536 -19.643  1.00 70.13           O  
ANISOU 4631  O   GLU B 224     7211  11076   8359   -839   1299  -1932       O  
ATOM   4632  CB  GLU B 224      -3.957   6.630 -19.252  1.00 69.31           C  
ANISOU 4632  CB  GLU B 224     6984  10881   8470   -763   1397  -1820       C  
ATOM   4633  CG  GLU B 224      -4.422   7.531 -20.394  1.00 86.57           C  
ANISOU 4633  CG  GLU B 224     9219  13335  10338   -895   1395  -1768       C  
ATOM   4634  CD  GLU B 224      -4.668   9.001 -20.092  1.00114.69           C  
ANISOU 4634  CD  GLU B 224    12864  16940  13772   -887   1260  -1496       C  
ATOM   4635  OE1 GLU B 224      -4.926   9.353 -18.916  1.00107.87           O  
ANISOU 4635  OE1 GLU B 224    12052  15908  13025   -783   1141  -1346       O  
ATOM   4636  OE2 GLU B 224      -4.620   9.805 -21.052  1.00110.64           O  
ANISOU 4636  OE2 GLU B 224    12365  16634  13041   -993   1278  -1433       O  
ATOM   4637  N   ALA B 225      -5.528   3.872 -19.566  1.00 67.05           N  
ANISOU 4637  N   ALA B 225     6659  10475   8344   -784   1509  -2235       N  
ATOM   4638  CA  ALA B 225      -6.265   2.876 -20.349  1.00 67.35           C  
ANISOU 4638  CA  ALA B 225     6676  10581   8332   -871   1595  -2468       C  
ATOM   4639  C   ALA B 225      -7.613   2.522 -19.683  1.00 68.52           C  
ANISOU 4639  C   ALA B 225     6896  10635   8506   -832   1481  -2405       C  
ATOM   4640  O   ALA B 225      -8.614   2.405 -20.387  1.00 68.59           O  
ANISOU 4640  O   ALA B 225     6935  10795   8333   -930   1474  -2482       O  
ATOM   4641  CB  ALA B 225      -5.422   1.625 -20.545  1.00 69.42           C  
ANISOU 4641  CB  ALA B 225     6818  10716   8842   -858   1765  -2725       C  
ATOM   4642  N   GLU B 226      -7.648   2.397 -18.339  1.00 63.39           N  
ANISOU 4642  N   GLU B 226     6268   9752   8064   -699   1389  -2257       N  
ATOM   4643  CA  GLU B 226      -8.889   2.103 -17.601  1.00 62.07           C  
ANISOU 4643  CA  GLU B 226     6167   9486   7931   -659   1285  -2179       C  
ATOM   4644  C   GLU B 226      -9.816   3.328 -17.570  1.00 61.90           C  
ANISOU 4644  C   GLU B 226     6244   9609   7665   -683   1148  -1976       C  
ATOM   4645  O   GLU B 226     -11.029   3.144 -17.624  1.00 61.23           O  
ANISOU 4645  O   GLU B 226     6199   9560   7506   -713   1094  -1978       O  
ATOM   4646  CB  GLU B 226      -8.608   1.599 -16.184  1.00 62.81           C  
ANISOU 4646  CB  GLU B 226     6252   9307   8304   -522   1235  -2075       C  
ATOM   4647  CG  GLU B 226      -7.968   0.217 -16.149  1.00 70.58           C  
ANISOU 4647  CG  GLU B 226     7134  10110   9573   -490   1356  -2265       C  
ATOM   4648  CD  GLU B 226      -7.336  -0.127 -14.816  1.00 82.60           C  
ANISOU 4648  CD  GLU B 226     8628  11384  11372   -356   1305  -2130       C  
ATOM   4649  OE1 GLU B 226      -6.737   0.777 -14.189  1.00 70.21           O  
ANISOU 4649  OE1 GLU B 226     7082   9814   9781   -299   1221  -1944       O  
ATOM   4650  OE2 GLU B 226      -7.456  -1.297 -14.386  1.00 69.91           O  
ANISOU 4650  OE2 GLU B 226     6973   9585  10004   -313   1344  -2205       O  
ATOM   4651  N   HIS B 227      -9.246   4.567 -17.553  1.00 55.81           N  
ANISOU 4651  N   HIS B 227     5502   8921   6784   -674   1097  -1810       N  
ATOM   4652  CA  HIS B 227     -10.002   5.827 -17.635  1.00 53.43           C  
ANISOU 4652  CA  HIS B 227     5279   8750   6270   -697    979  -1614       C  
ATOM   4653  C   HIS B 227     -10.724   5.921 -18.990  1.00 60.88           C  
ANISOU 4653  C   HIS B 227     6222   9947   6962   -833   1001  -1697       C  
ATOM   4654  O   HIS B 227     -11.948   6.053 -19.028  1.00 61.02           O  
ANISOU 4654  O   HIS B 227     6281  10024   6881   -855    919  -1642       O  
ATOM   4655  CB  HIS B 227      -9.081   7.047 -17.452  1.00 52.27           C  
ANISOU 4655  CB  HIS B 227     5148   8625   6088   -671    946  -1447       C  
ATOM   4656  CG  HIS B 227      -8.822   7.436 -16.031  1.00 53.49           C  
ANISOU 4656  CG  HIS B 227     5338   8584   6404   -552    859  -1288       C  
ATOM   4657  ND1 HIS B 227      -7.927   6.734 -15.242  1.00 55.06           N  
ANISOU 4657  ND1 HIS B 227     5486   8604   6831   -475    895  -1334       N  
ATOM   4658  CD2 HIS B 227      -9.302   8.483 -15.318  1.00 54.00           C  
ANISOU 4658  CD2 HIS B 227     5475   8619   6424   -508    743  -1089       C  
ATOM   4659  CE1 HIS B 227      -7.913   7.352 -14.070  1.00 53.27           C  
ANISOU 4659  CE1 HIS B 227     5310   8263   6669   -396    792  -1162       C  
ATOM   4660  NE2 HIS B 227      -8.737   8.398 -14.060  1.00 52.88           N  
ANISOU 4660  NE2 HIS B 227     5337   8292   6464   -413    707  -1024       N  
ATOM   4661  N   GLN B 228      -9.962   5.785 -20.095  1.00 60.51           N  
ANISOU 4661  N   GLN B 228     6120  10056   6816   -931   1117  -1838       N  
ATOM   4662  CA  GLN B 228     -10.437   5.848 -21.485  1.00 62.08           C  
ANISOU 4662  CA  GLN B 228     6309  10531   6748  -1084   1153  -1932       C  
ATOM   4663  C   GLN B 228     -11.495   4.770 -21.788  1.00 65.70           C  
ANISOU 4663  C   GLN B 228     6754  11014   7197  -1141   1170  -2115       C  
ATOM   4664  O   GLN B 228     -12.505   5.091 -22.427  1.00 66.11           O  
ANISOU 4664  O   GLN B 228     6829  11258   7033  -1230   1101  -2078       O  
ATOM   4665  CB  GLN B 228      -9.264   5.771 -22.480  1.00 64.93           C  
ANISOU 4665  CB  GLN B 228     6605  11032   7034  -1176   1301  -2079       C  
ATOM   4666  CG  GLN B 228      -8.380   7.025 -22.438  1.00 87.71           C  
ANISOU 4666  CG  GLN B 228     9505  13964   9859  -1160   1275  -1879       C  
ATOM   4667  CD  GLN B 228      -7.335   7.068 -23.528  1.00122.01           C  
ANISOU 4667  CD  GLN B 228    13785  18484  14091  -1272   1423  -2010       C  
ATOM   4668  OE1 GLN B 228      -7.538   7.663 -24.596  1.00120.16           O  
ANISOU 4668  OE1 GLN B 228    13562  18515  13580  -1405   1429  -1976       O  
ATOM   4669  NE2 GLN B 228      -6.173   6.474 -23.268  1.00117.19           N  
ANISOU 4669  NE2 GLN B 228    13099  17735  13694  -1221   1545  -2150       N  
ATOM   4670  N   ASP B 229     -11.300   3.523 -21.299  1.00 60.49           N  
ANISOU 4670  N   ASP B 229     6049  10151   6782  -1089   1252  -2295       N  
ATOM   4671  CA  ASP B 229     -12.284   2.453 -21.488  1.00 60.39           C  
ANISOU 4671  CA  ASP B 229     6019  10123   6801  -1140   1274  -2475       C  
ATOM   4672  C   ASP B 229     -13.615   2.862 -20.806  1.00 63.74           C  
ANISOU 4672  C   ASP B 229     6510  10513   7194  -1094   1115  -2289       C  
ATOM   4673  O   ASP B 229     -14.666   2.790 -21.435  1.00 64.60           O  
ANISOU 4673  O   ASP B 229     6622  10778   7144  -1188   1076  -2339       O  
ATOM   4674  CB  ASP B 229     -11.750   1.104 -20.961  1.00 62.09           C  
ANISOU 4674  CB  ASP B 229     6173  10086   7334  -1076   1391  -2670       C  
ATOM   4675  CG  ASP B 229     -12.805   0.017 -20.826  1.00 67.71           C  
ANISOU 4675  CG  ASP B 229     6873  10709   8143  -1103   1399  -2816       C  
ATOM   4676  OD1 ASP B 229     -13.121  -0.633 -21.841  1.00 70.60           O  
ANISOU 4676  OD1 ASP B 229     7200  11221   8405  -1236   1485  -3052       O  
ATOM   4677  OD2 ASP B 229     -13.327  -0.162 -19.717  1.00 68.97           O  
ANISOU 4677  OD2 ASP B 229     7064  10668   8474  -1000   1320  -2695       O  
ATOM   4678  N   MET B 230     -13.541   3.367 -19.562  1.00 58.29           N  
ANISOU 4678  N   MET B 230     5867   9639   6641   -957   1025  -2076       N  
ATOM   4679  CA  MET B 230     -14.689   3.841 -18.791  1.00 56.70           C  
ANISOU 4679  CA  MET B 230     5725   9388   6431   -901    888  -1893       C  
ATOM   4680  C   MET B 230     -15.401   5.011 -19.493  1.00 62.11           C  
ANISOU 4680  C   MET B 230     6440  10308   6850   -968    789  -1742       C  
ATOM   4681  O   MET B 230     -16.631   5.014 -19.552  1.00 61.05           O  
ANISOU 4681  O   MET B 230     6317  10237   6644   -995    710  -1706       O  
ATOM   4682  CB  MET B 230     -14.245   4.253 -17.372  1.00 56.70           C  
ANISOU 4682  CB  MET B 230     5765   9163   6615   -755    832  -1713       C  
ATOM   4683  CG  MET B 230     -15.399   4.567 -16.438  1.00 58.50           C  
ANISOU 4683  CG  MET B 230     6047   9311   6869   -693    717  -1558       C  
ATOM   4684  SD  MET B 230     -16.711   3.312 -16.316  1.00 62.49           S  
ANISOU 4684  SD  MET B 230     6533   9756   7457   -727    727  -1697       S  
ATOM   4685  CE  MET B 230     -15.862   2.018 -15.466  1.00 58.89           C  
ANISOU 4685  CE  MET B 230     6047   9024   7306   -647    815  -1795       C  
ATOM   4686  N   HIS B 231     -14.629   5.985 -20.036  1.00 60.46           N  
ANISOU 4686  N   HIS B 231     6237  10228   6506   -996    792  -1649       N  
ATOM   4687  CA  HIS B 231     -15.169   7.159 -20.738  1.00 60.59           C  
ANISOU 4687  CA  HIS B 231     6276  10462   6283  -1059    698  -1476       C  
ATOM   4688  C   HIS B 231     -15.941   6.747 -21.997  1.00 64.97           C  
ANISOU 4688  C   HIS B 231     6795  11271   6622  -1210    705  -1605       C  
ATOM   4689  O   HIS B 231     -17.044   7.250 -22.214  1.00 64.89           O  
ANISOU 4689  O   HIS B 231     6794  11375   6488  -1238    591  -1480       O  
ATOM   4690  CB  HIS B 231     -14.062   8.173 -21.079  1.00 61.59           C  
ANISOU 4690  CB  HIS B 231     6410  10661   6331  -1069    720  -1362       C  
ATOM   4691  CG  HIS B 231     -13.357   8.740 -19.876  1.00 63.37           C  
ANISOU 4691  CG  HIS B 231     6669  10665   6742   -935    694  -1220       C  
ATOM   4692  ND1 HIS B 231     -12.085   9.280 -19.976  1.00 65.14           N  
ANISOU 4692  ND1 HIS B 231     6883  10885   6983   -931    750  -1186       N  
ATOM   4693  CD2 HIS B 231     -13.754   8.800 -18.581  1.00 63.19           C  
ANISOU 4693  CD2 HIS B 231     6687  10436   6888   -816    622  -1119       C  
ATOM   4694  CE1 HIS B 231     -11.759   9.655 -18.751  1.00 62.68           C  
ANISOU 4694  CE1 HIS B 231     6604  10368   6845   -812    702  -1067       C  
ATOM   4695  NE2 HIS B 231     -12.732   9.387 -17.879  1.00 61.96           N  
ANISOU 4695  NE2 HIS B 231     6547  10154   6841   -742    627  -1025       N  
ATOM   4696  N   SER B 232     -15.408   5.782 -22.776  1.00 61.72           N  
ANISOU 4696  N   SER B 232     6334  10938   6180  -1308    838  -1865       N  
ATOM   4697  CA  SER B 232     -16.092   5.256 -23.969  1.00 62.90           C  
ANISOU 4697  CA  SER B 232     6445  11336   6120  -1471    859  -2032       C  
ATOM   4698  C   SER B 232     -17.402   4.560 -23.571  1.00 66.22           C  
ANISOU 4698  C   SER B 232     6859  11687   6615  -1462    795  -2087       C  
ATOM   4699  O   SER B 232     -18.412   4.708 -24.262  1.00 66.44           O  
ANISOU 4699  O   SER B 232     6872  11925   6449  -1563    715  -2070       O  
ATOM   4700  CB  SER B 232     -15.188   4.295 -24.733  1.00 66.27           C  
ANISOU 4700  CB  SER B 232     6817  11822   6541  -1569   1038  -2333       C  
ATOM   4701  OG  SER B 232     -14.355   5.029 -25.612  1.00 76.97           O  
ANISOU 4701  OG  SER B 232     8166  13378   7701  -1648   1084  -2288       O  
ATOM   4702  N   TYR B 233     -17.383   3.857 -22.415  1.00 61.12           N  
ANISOU 4702  N   TYR B 233     6221  10750   6251  -1342    821  -2129       N  
ATOM   4703  CA  TYR B 233     -18.524   3.143 -21.847  1.00 60.30           C  
ANISOU 4703  CA  TYR B 233     6113  10535   6264  -1320    776  -2173       C  
ATOM   4704  C   TYR B 233     -19.633   4.133 -21.442  1.00 63.28           C  
ANISOU 4704  C   TYR B 233     6522  10956   6566  -1273    610  -1914       C  
ATOM   4705  O   TYR B 233     -20.794   3.891 -21.774  1.00 64.48           O  
ANISOU 4705  O   TYR B 233     6647  11215   6637  -1342    548  -1944       O  
ATOM   4706  CB  TYR B 233     -18.068   2.282 -20.652  1.00 59.74           C  
ANISOU 4706  CB  TYR B 233     6047  10139   6513  -1198    843  -2235       C  
ATOM   4707  CG  TYR B 233     -19.153   1.402 -20.071  1.00 60.45           C  
ANISOU 4707  CG  TYR B 233     6127  10101   6743  -1187    821  -2299       C  
ATOM   4708  CD1 TYR B 233     -19.440   0.155 -20.625  1.00 63.18           C  
ANISOU 4708  CD1 TYR B 233     6417  10450   7137  -1287    915  -2571       C  
ATOM   4709  CD2 TYR B 233     -19.880   1.804 -18.950  1.00 58.97           C  
ANISOU 4709  CD2 TYR B 233     5980   9779   6648  -1082    718  -2099       C  
ATOM   4710  CE1 TYR B 233     -20.427  -0.666 -20.081  1.00 63.76           C  
ANISOU 4710  CE1 TYR B 233     6478  10395   7353  -1284    899  -2627       C  
ATOM   4711  CE2 TYR B 233     -20.885   1.001 -18.411  1.00 58.92           C  
ANISOU 4711  CE2 TYR B 233     5960   9659   6767  -1080    705  -2152       C  
ATOM   4712  CZ  TYR B 233     -21.138  -0.244 -18.962  1.00 65.35           C  
ANISOU 4712  CZ  TYR B 233     6720  10471   7638  -1179    794  -2410       C  
ATOM   4713  OH  TYR B 233     -22.103  -1.044 -18.407  1.00 60.59           O  
ANISOU 4713  OH  TYR B 233     6101   9743   7176  -1180    786  -2458       O  
ATOM   4714  N   ILE B 234     -19.278   5.244 -20.747  1.00 56.99           N  
ANISOU 4714  N   ILE B 234     5774  10074   5805  -1161    544  -1672       N  
ATOM   4715  CA  ILE B 234     -20.240   6.282 -20.337  1.00 55.02           C  
ANISOU 4715  CA  ILE B 234     5547   9843   5513  -1104    402  -1426       C  
ATOM   4716  C   ILE B 234     -20.741   7.026 -21.585  1.00 61.51           C  
ANISOU 4716  C   ILE B 234     6341  10969   6062  -1221    323  -1341       C  
ATOM   4717  O   ILE B 234     -21.938   7.275 -21.680  1.00 61.11           O  
ANISOU 4717  O   ILE B 234     6267  11001   5953  -1238    218  -1252       O  
ATOM   4718  CB  ILE B 234     -19.665   7.264 -19.264  1.00 55.49           C  
ANISOU 4718  CB  ILE B 234     5664   9724   5695   -963    367  -1217       C  
ATOM   4719  CG1 ILE B 234     -19.267   6.507 -17.959  1.00 53.82           C  
ANISOU 4719  CG1 ILE B 234     5478   9231   5739   -855    424  -1278       C  
ATOM   4720  CG2 ILE B 234     -20.663   8.419 -18.954  1.00 54.22           C  
ANISOU 4720  CG2 ILE B 234     5517   9590   5493   -912    233   -974       C  
ATOM   4721  CD1 ILE B 234     -18.186   7.175 -17.122  1.00 51.47           C  
ANISOU 4721  CD1 ILE B 234     5224   8785   5548   -754    436  -1161       C  
ATOM   4722  N   ALA B 235     -19.838   7.386 -22.532  1.00 60.64           N  
ANISOU 4722  N   ALA B 235     6226  11028   5786  -1304    371  -1359       N  
ATOM   4723  CA  ALA B 235     -20.225   8.076 -23.773  1.00 62.44           C  
ANISOU 4723  CA  ALA B 235     6426  11566   5732  -1431    297  -1264       C  
ATOM   4724  C   ALA B 235     -21.334   7.302 -24.469  1.00 70.25           C  
ANISOU 4724  C   ALA B 235     7360  12735   6595  -1555    264  -1408       C  
ATOM   4725  O   ALA B 235     -22.414   7.857 -24.643  1.00 71.21           O  
ANISOU 4725  O   ALA B 235     7456  12978   6621  -1573    128  -1246       O  
ATOM   4726  CB  ALA B 235     -19.025   8.250 -24.705  1.00 63.79           C  
ANISOU 4726  CB  ALA B 235     6596  11895   5747  -1525    392  -1325       C  
ATOM   4727  N   ALA B 236     -21.100   5.992 -24.748  1.00 68.75           N  
ANISOU 4727  N   ALA B 236     7145  12535   6440  -1632    386  -1713       N  
ATOM   4728  CA  ALA B 236     -22.024   5.065 -25.408  1.00 70.71           C  
ANISOU 4728  CA  ALA B 236     7339  12938   6589  -1767    381  -1911       C  
ATOM   4729  C   ALA B 236     -23.373   4.975 -24.686  1.00 74.99           C  
ANISOU 4729  C   ALA B 236     7865  13378   7252  -1702    270  -1824       C  
ATOM   4730  O   ALA B 236     -24.377   5.392 -25.256  1.00 76.54           O  
ANISOU 4730  O   ALA B 236     8018  13782   7282  -1777    146  -1726       O  
ATOM   4731  CB  ALA B 236     -21.393   3.682 -25.507  1.00 72.17           C  
ANISOU 4731  CB  ALA B 236     7505  13034   6882  -1823    555  -2255       C  
ATOM   4732  N   PHE B 237     -23.387   4.483 -23.430  1.00 70.20           N  
ANISOU 4732  N   PHE B 237     7284  12459   6927  -1566    310  -1843       N  
ATOM   4733  CA  PHE B 237     -24.593   4.316 -22.616  1.00 69.59           C  
ANISOU 4733  CA  PHE B 237     7192  12257   6990  -1500    230  -1776       C  
ATOM   4734  C   PHE B 237     -25.325   5.642 -22.356  1.00 71.59           C  
ANISOU 4734  C   PHE B 237     7447  12559   7196  -1424     77  -1466       C  
ATOM   4735  O   PHE B 237     -26.555   5.657 -22.304  1.00 70.52           O  
ANISOU 4735  O   PHE B 237     7263  12470   7060  -1436    -17  -1412       O  
ATOM   4736  CB  PHE B 237     -24.252   3.649 -21.276  1.00 70.15           C  
ANISOU 4736  CB  PHE B 237     7302  11991   7360  -1369    314  -1830       C  
ATOM   4737  CG  PHE B 237     -24.621   2.188 -21.186  1.00 72.96           C  
ANISOU 4737  CG  PHE B 237     7622  12252   7846  -1429    397  -2086       C  
ATOM   4738  CD1 PHE B 237     -25.926   1.799 -20.911  1.00 76.98           C  
ANISOU 4738  CD1 PHE B 237     8093  12749   8408  -1448    335  -2091       C  
ATOM   4739  CD2 PHE B 237     -23.663   1.200 -21.371  1.00 75.71           C  
ANISOU 4739  CD2 PHE B 237     7967  12513   8288  -1465    545  -2323       C  
ATOM   4740  CE1 PHE B 237     -26.267   0.445 -20.826  1.00 78.80           C  
ANISOU 4740  CE1 PHE B 237     8287  12879   8773  -1511    416  -2326       C  
ATOM   4741  CE2 PHE B 237     -24.003  -0.153 -21.282  1.00 79.29           C  
ANISOU 4741  CE2 PHE B 237     8382  12853   8891  -1519    628  -2559       C  
ATOM   4742  CZ  PHE B 237     -25.298  -0.521 -21.005  1.00 77.90           C  
ANISOU 4742  CZ  PHE B 237     8175  12664   8760  -1545    562  -2557       C  
ATOM   4743  N   GLY B 238     -24.561   6.724 -22.216  1.00 66.99           N  
ANISOU 4743  N   GLY B 238     6910  11957   6588  -1351     57  -1276       N  
ATOM   4744  CA  GLY B 238     -25.077   8.063 -21.951  1.00 65.92           C  
ANISOU 4744  CA  GLY B 238     6776  11835   6438  -1270    -71   -982       C  
ATOM   4745  C   GLY B 238     -25.780   8.670 -23.140  1.00 69.47           C  
ANISOU 4745  C   GLY B 238     7162  12589   6645  -1383   -192   -865       C  
ATOM   4746  O   GLY B 238     -26.845   9.277 -22.984  1.00 69.14           O  
ANISOU 4746  O   GLY B 238     7076  12575   6621  -1345   -314   -689       O  
ATOM   4747  N   ALA B 239     -25.187   8.496 -24.339  1.00 65.99           N  
ANISOU 4747  N   ALA B 239     6711  12386   5976  -1528   -156   -959       N  
ATOM   4748  CA  ALA B 239     -25.732   8.983 -25.612  1.00 66.91           C  
ANISOU 4748  CA  ALA B 239     6767  12839   5815  -1667   -268   -856       C  
ATOM   4749  C   ALA B 239     -27.051   8.286 -25.927  1.00 71.03           C  
ANISOU 4749  C   ALA B 239     7210  13491   6286  -1756   -342   -958       C  
ATOM   4750  O   ALA B 239     -28.033   8.965 -26.237  1.00 70.97           O  
ANISOU 4750  O   ALA B 239     7140  13630   6197  -1771   -495   -758       O  
ATOM   4751  CB  ALA B 239     -24.730   8.761 -26.741  1.00 68.84           C  
ANISOU 4751  CB  ALA B 239     7024  13306   5827  -1815   -183   -981       C  
ATOM   4752  N   VAL B 240     -27.079   6.934 -25.790  1.00 67.96           N  
ANISOU 4752  N   VAL B 240     6818  13032   5974  -1809   -234  -1262       N  
ATOM   4753  CA  VAL B 240     -28.238   6.074 -26.058  1.00 69.00           C  
ANISOU 4753  CA  VAL B 240     6874  13264   6079  -1909   -277  -1414       C  
ATOM   4754  C   VAL B 240     -29.386   6.452 -25.124  1.00 72.92           C  
ANISOU 4754  C   VAL B 240     7335  13611   6761  -1783   -385  -1235       C  
ATOM   4755  O   VAL B 240     -30.495   6.680 -25.611  1.00 74.68           O  
ANISOU 4755  O   VAL B 240     7472  14022   6881  -1848   -520  -1144       O  
ATOM   4756  CB  VAL B 240     -27.898   4.553 -25.993  1.00 72.38           C  
ANISOU 4756  CB  VAL B 240     7310  13589   6601  -1978   -117  -1780       C  
ATOM   4757  CG1 VAL B 240     -29.160   3.681 -26.086  1.00 72.83           C  
ANISOU 4757  CG1 VAL B 240     7290  13695   6687  -2064   -160  -1927       C  
ATOM   4758  CG2 VAL B 240     -26.909   4.167 -27.093  1.00 73.29           C  
ANISOU 4758  CG2 VAL B 240     7435  13904   6507  -2131    -11  -1983       C  
ATOM   4759  N   THR B 241     -29.121   6.547 -23.807  1.00 68.18           N  
ANISOU 4759  N   THR B 241     6793  12688   6424  -1610   -328  -1179       N  
ATOM   4760  CA  THR B 241     -30.127   6.919 -22.798  1.00 66.88           C  
ANISOU 4760  CA  THR B 241     6602  12360   6451  -1483   -402  -1023       C  
ATOM   4761  C   THR B 241     -30.666   8.320 -23.087  1.00 70.83           C  
ANISOU 4761  C   THR B 241     7057  12984   6871  -1439   -556   -712       C  
ATOM   4762  O   THR B 241     -31.873   8.499 -23.078  1.00 71.27           O  
ANISOU 4762  O   THR B 241     7025  13101   6951  -1437   -665   -617       O  
ATOM   4763  CB  THR B 241     -29.551   6.820 -21.375  1.00 71.84           C  
ANISOU 4763  CB  THR B 241     7311  12644   7339  -1322   -301  -1025       C  
ATOM   4764  OG1 THR B 241     -28.932   5.548 -21.227  1.00 69.19           O  
ANISOU 4764  OG1 THR B 241     7010  12202   7078  -1366   -163  -1290       O  
ATOM   4765  CG2 THR B 241     -30.618   6.992 -20.289  1.00 71.06           C  
ANISOU 4765  CG2 THR B 241     7185  12379   7437  -1212   -347   -919       C  
ATOM   4766  N   GLY B 242     -29.770   9.271 -23.365  1.00 67.15           N  
ANISOU 4766  N   GLY B 242     6640  12550   6323  -1410   -561   -559       N  
ATOM   4767  CA  GLY B 242     -30.117  10.653 -23.681  1.00 67.60           C  
ANISOU 4767  CA  GLY B 242     6659  12706   6320  -1368   -696   -250       C  
ATOM   4768  C   GLY B 242     -31.069  10.789 -24.855  1.00 74.42           C  
ANISOU 4768  C   GLY B 242     7414  13893   6970  -1502   -844   -166       C  
ATOM   4769  O   GLY B 242     -32.101  11.455 -24.732  1.00 74.90           O  
ANISOU 4769  O   GLY B 242     7393  13971   7095  -1445   -974     42       O  
ATOM   4770  N   LEU B 243     -30.737  10.136 -25.996  1.00 71.91           N  
ANISOU 4770  N   LEU B 243     7085  13837   6399  -1685   -824   -335       N  
ATOM   4771  CA  LEU B 243     -31.536  10.159 -27.228  1.00 73.56           C  
ANISOU 4771  CA  LEU B 243     7193  14403   6354  -1849   -964   -281       C  
ATOM   4772  C   LEU B 243     -32.872   9.421 -27.048  1.00 76.65           C  
ANISOU 4772  C   LEU B 243     7488  14818   6818  -1882  -1027   -385       C  
ATOM   4773  O   LEU B 243     -33.890   9.927 -27.524  1.00 77.16           O  
ANISOU 4773  O   LEU B 243     7444  15071   6803  -1920  -1194   -204       O  
ATOM   4774  CB  LEU B 243     -30.763   9.581 -28.432  1.00 75.12           C  
ANISOU 4774  CB  LEU B 243     7414  14877   6251  -2049   -901   -471       C  
ATOM   4775  CG  LEU B 243     -29.525  10.359 -28.919  1.00 80.23           C  
ANISOU 4775  CG  LEU B 243     8132  15595   6757  -2063   -858   -349       C  
ATOM   4776  CD1 LEU B 243     -28.692   9.515 -29.868  1.00 81.88           C  
ANISOU 4776  CD1 LEU B 243     8372  16008   6731  -2247   -734   -629       C  
ATOM   4777  CD2 LEU B 243     -29.895  11.677 -29.590  1.00 83.70           C  
ANISOU 4777  CD2 LEU B 243     8515  16243   7044  -2082  -1036     18       C  
ATOM   4778  N   CYS B 244     -32.879   8.246 -26.364  1.00 72.08           N  
ANISOU 4778  N   CYS B 244     6940  14049   6400  -1870   -899   -663       N  
ATOM   4779  CA  CYS B 244     -34.111   7.479 -26.091  1.00 72.58           C  
ANISOU 4779  CA  CYS B 244     6915  14101   6561  -1902   -939   -778       C  
ATOM   4780  C   CYS B 244     -35.078   8.318 -25.271  1.00 74.50           C  
ANISOU 4780  C   CYS B 244     7094  14205   7008  -1746  -1043   -525       C  
ATOM   4781  O   CYS B 244     -36.222   8.509 -25.684  1.00 76.44           O  
ANISOU 4781  O   CYS B 244     7216  14620   7209  -1796  -1185   -430       O  
ATOM   4782  CB  CYS B 244     -33.814   6.155 -25.390  1.00 72.02           C  
ANISOU 4782  CB  CYS B 244     6900  13807   6658  -1900   -768  -1091       C  
ATOM   4783  SG  CYS B 244     -33.227   4.845 -26.490  1.00 78.13           S  
ANISOU 4783  SG  CYS B 244     7683  14782   7220  -2130   -660  -1464       S  
ATOM   4784  N   THR B 245     -34.603   8.849 -24.132  1.00 67.30           N  
ANISOU 4784  N   THR B 245     6259  12994   6317  -1561   -972   -420       N  
ATOM   4785  CA  THR B 245     -35.423   9.644 -23.224  1.00 66.01           C  
ANISOU 4785  CA  THR B 245     6046  12662   6374  -1403  -1037   -209       C  
ATOM   4786  C   THR B 245     -35.873  10.951 -23.891  1.00 71.25           C  
ANISOU 4786  C   THR B 245     6623  13501   6949  -1387  -1209    107       C  
ATOM   4787  O   THR B 245     -37.016  11.348 -23.679  1.00 72.13           O  
ANISOU 4787  O   THR B 245     6619  13618   7171  -1336  -1314    246       O  
ATOM   4788  CB  THR B 245     -34.720   9.877 -21.874  1.00 63.40           C  
ANISOU 4788  CB  THR B 245     5826  11988   6275  -1231   -910   -199       C  
ATOM   4789  OG1 THR B 245     -33.465  10.523 -22.087  1.00 65.74           O  
ANISOU 4789  OG1 THR B 245     6217  12271   6490  -1207   -870   -123       O  
ATOM   4790  CG2 THR B 245     -34.534   8.583 -21.084  1.00 53.07           C  
ANISOU 4790  CG2 THR B 245     4577  10490   5098  -1233   -764   -465       C  
ATOM   4791  N   LEU B 246     -35.014  11.591 -24.706  1.00 68.13           N  
ANISOU 4791  N   LEU B 246     6271  13248   6365  -1434  -1237    224       N  
ATOM   4792  CA  LEU B 246     -35.363  12.821 -25.427  1.00 69.94           C  
ANISOU 4792  CA  LEU B 246     6421  13652   6502  -1431  -1403    546       C  
ATOM   4793  C   LEU B 246     -36.550  12.564 -26.386  1.00 78.10           C  
ANISOU 4793  C   LEU B 246     7303  14997   7374  -1568  -1569    586       C  
ATOM   4794  O   LEU B 246     -37.478  13.380 -26.433  1.00 79.61           O  
ANISOU 4794  O   LEU B 246     7375  15229   7645  -1507  -1717    844       O  
ATOM   4795  CB  LEU B 246     -34.139  13.368 -26.194  1.00 70.34           C  
ANISOU 4795  CB  LEU B 246     6554  13823   6347  -1492  -1383    629       C  
ATOM   4796  CG  LEU B 246     -34.292  14.667 -27.007  1.00 76.48           C  
ANISOU 4796  CG  LEU B 246     7265  14782   7012  -1502  -1546    984       C  
ATOM   4797  CD1 LEU B 246     -34.681  15.861 -26.126  1.00 75.72           C  
ANISOU 4797  CD1 LEU B 246     7137  14426   7207  -1299  -1591   1253       C  
ATOM   4798  CD2 LEU B 246     -33.014  14.977 -27.755  1.00 78.15           C  
ANISOU 4798  CD2 LEU B 246     7567  15128   7000  -1593  -1497   1012       C  
ATOM   4799  N   PHE B 247     -36.545  11.407 -27.096  1.00 75.49           N  
ANISOU 4799  N   PHE B 247     6968  14876   6839  -1752  -1540    322       N  
ATOM   4800  CA  PHE B 247     -37.625  11.023 -28.010  1.00 77.62           C  
ANISOU 4800  CA  PHE B 247     7098  15460   6936  -1910  -1690    313       C  
ATOM   4801  C   PHE B 247     -38.934  10.910 -27.244  1.00 82.49           C  
ANISOU 4801  C   PHE B 247     7597  15944   7801  -1818  -1748    342       C  
ATOM   4802  O   PHE B 247     -39.929  11.472 -27.690  1.00 84.87           O  
ANISOU 4802  O   PHE B 247     7753  16414   8082  -1830  -1928    560       O  
ATOM   4803  CB  PHE B 247     -37.310   9.704 -28.752  1.00 79.97           C  
ANISOU 4803  CB  PHE B 247     7427  15957   7003  -2123  -1611    -36       C  
ATOM   4804  CG  PHE B 247     -38.444   9.156 -29.595  1.00 83.55           C  
ANISOU 4804  CG  PHE B 247     7737  16724   7286  -2302  -1750   -105       C  
ATOM   4805  CD1 PHE B 247     -39.233   8.105 -29.134  1.00 86.07           C  
ANISOU 4805  CD1 PHE B 247     8004  16961   7739  -2336  -1706   -347       C  
ATOM   4806  CD2 PHE B 247     -38.731   9.697 -30.845  1.00 87.76           C  
ANISOU 4806  CD2 PHE B 247     8182  17639   7521  -2446  -1929     80       C  
ATOM   4807  CE1 PHE B 247     -40.292   7.610 -29.907  1.00 89.12           C  
ANISOU 4807  CE1 PHE B 247     8250  17640   7973  -2510  -1839   -418       C  
ATOM   4808  CE2 PHE B 247     -39.795   9.206 -31.614  1.00 92.85           C  
ANISOU 4808  CE2 PHE B 247     8687  18591   8001  -2620  -2070     19       C  
ATOM   4809  CZ  PHE B 247     -40.569   8.166 -31.140  1.00 90.51           C  
ANISOU 4809  CZ  PHE B 247     8338  18205   7848  -2651  -2024   -237       C  
ATOM   4810  N   THR B 248     -38.919  10.210 -26.087  1.00 76.66           N  
ANISOU 4810  N   THR B 248     6918  14907   7302  -1726  -1596    140       N  
ATOM   4811  CA  THR B 248     -40.071   9.981 -25.205  1.00 75.78           C  
ANISOU 4811  CA  THR B 248     6712  14637   7444  -1639  -1608    130       C  
ATOM   4812  C   THR B 248     -40.616  11.306 -24.663  1.00 79.21           C  
ANISOU 4812  C   THR B 248     7072  14944   8081  -1458  -1699    455       C  
ATOM   4813  O   THR B 248     -41.838  11.480 -24.613  1.00 79.58           O  
ANISOU 4813  O   THR B 248     6963  15044   8230  -1438  -1813    561       O  
ATOM   4814  CB  THR B 248     -39.686   9.024 -24.079  1.00 80.68           C  
ANISOU 4814  CB  THR B 248     7439  14959   8256  -1580  -1409   -131       C  
ATOM   4815  OG1 THR B 248     -39.062   7.885 -24.666  1.00 84.83           O  
ANISOU 4815  OG1 THR B 248     8032  15591   8610  -1742  -1320   -419       O  
ATOM   4816  CG2 THR B 248     -40.881   8.572 -23.261  1.00 77.54           C  
ANISOU 4816  CG2 THR B 248     6945  14433   8085  -1532  -1405   -184       C  
ATOM   4817  N   LEU B 249     -39.721  12.239 -24.288  1.00 74.41           N  
ANISOU 4817  N   LEU B 249     6565  14171   7539  -1331  -1649    608       N  
ATOM   4818  CA  LEU B 249     -40.124  13.560 -23.808  1.00 74.40           C  
ANISOU 4818  CA  LEU B 249     6500  14029   7741  -1160  -1720    908       C  
ATOM   4819  C   LEU B 249     -40.796  14.347 -24.947  1.00 80.82           C  
ANISOU 4819  C   LEU B 249     7161  15127   8421  -1220  -1941   1190       C  
ATOM   4820  O   LEU B 249     -41.911  14.841 -24.759  1.00 81.01           O  
ANISOU 4820  O   LEU B 249     7032  15132   8617  -1140  -2048   1364       O  
ATOM   4821  CB  LEU B 249     -38.931  14.338 -23.228  1.00 72.73           C  
ANISOU 4821  CB  LEU B 249     6433  13588   7611  -1036  -1614    986       C  
ATOM   4822  CG  LEU B 249     -38.318  13.803 -21.926  1.00 74.91           C  
ANISOU 4822  CG  LEU B 249     6846  13553   8063   -942  -1415    775       C  
ATOM   4823  CD1 LEU B 249     -37.038  14.523 -21.604  1.00 73.38           C  
ANISOU 4823  CD1 LEU B 249     6790  13204   7889   -862  -1332    846       C  
ATOM   4824  CD2 LEU B 249     -39.285  13.913 -20.762  1.00 76.37           C  
ANISOU 4824  CD2 LEU B 249     6963  13516   8536   -808  -1382    785       C  
ATOM   4825  N   ALA B 250     -40.151  14.390 -26.142  1.00 78.59           N  
ANISOU 4825  N   ALA B 250     6912  15121   7827  -1370  -2006   1228       N  
ATOM   4826  CA  ALA B 250     -40.668  15.065 -27.342  1.00 81.31           C  
ANISOU 4826  CA  ALA B 250     7125  15783   7986  -1459  -2222   1503       C  
ATOM   4827  C   ALA B 250     -42.040  14.501 -27.757  1.00 87.96           C  
ANISOU 4827  C   ALA B 250     7786  16844   8791  -1557  -2366   1475       C  
ATOM   4828  O   ALA B 250     -42.926  15.272 -28.136  1.00 90.03           O  
ANISOU 4828  O   ALA B 250     7885  17229   9093  -1531  -2553   1763       O  
ATOM   4829  CB  ALA B 250     -39.681  14.931 -28.487  1.00 83.04           C  
ANISOU 4829  CB  ALA B 250     7433  16272   7847  -1633  -2228   1475       C  
ATOM   4830  N   THR B 251     -42.218  13.165 -27.656  1.00 83.56           N  
ANISOU 4830  N   THR B 251     7249  16321   8178  -1667  -2278   1136       N  
ATOM   4831  CA  THR B 251     -43.472  12.476 -27.965  1.00 84.92           C  
ANISOU 4831  CA  THR B 251     7257  16681   8326  -1774  -2390   1056       C  
ATOM   4832  C   THR B 251     -44.559  12.907 -26.974  1.00 87.88           C  
ANISOU 4832  C   THR B 251     7502  16830   9058  -1596  -2418   1183       C  
ATOM   4833  O   THR B 251     -45.701  13.121 -27.382  1.00 89.27           O  
ANISOU 4833  O   THR B 251     7485  17179   9256  -1624  -2594   1336       O  
ATOM   4834  CB  THR B 251     -43.271  10.957 -27.941  1.00 91.19           C  
ANISOU 4834  CB  THR B 251     8124  17504   9020  -1923  -2254    644       C  
ATOM   4835  OG1 THR B 251     -42.118  10.622 -28.711  1.00 92.12           O  
ANISOU 4835  OG1 THR B 251     8378  17768   8856  -2057  -2184    507       O  
ATOM   4836  CG2 THR B 251     -44.457  10.213 -28.487  1.00 90.64           C  
ANISOU 4836  CG2 THR B 251     7888  17690   8861  -2082  -2380    544       C  
ATOM   4837  N   PHE B 252     -44.196  13.054 -25.684  1.00 81.69           N  
ANISOU 4837  N   PHE B 252     6818  15670   8549  -1417  -2245   1122       N  
ATOM   4838  CA  PHE B 252     -45.136  13.463 -24.644  1.00 81.00           C  
ANISOU 4838  CA  PHE B 252     6626  15343   8807  -1244  -2230   1209       C  
ATOM   4839  C   PHE B 252     -45.576  14.927 -24.805  1.00 89.03           C  
ANISOU 4839  C   PHE B 252     7517  16345   9965  -1109  -2377   1592       C  
ATOM   4840  O   PHE B 252     -46.774  15.193 -24.699  1.00 90.09           O  
ANISOU 4840  O   PHE B 252     7462  16491  10279  -1054  -2479   1716       O  
ATOM   4841  CB  PHE B 252     -44.557  13.240 -23.242  1.00 78.77           C  
ANISOU 4841  CB  PHE B 252     6498  14688   8743  -1109  -2001   1036       C  
ATOM   4842  CG  PHE B 252     -45.034  11.991 -22.539  1.00 78.36           C  
ANISOU 4842  CG  PHE B 252     6450  14538   8787  -1151  -1881    744       C  
ATOM   4843  CD1 PHE B 252     -44.224  10.864 -22.460  1.00 79.84           C  
ANISOU 4843  CD1 PHE B 252     6784  14705   8845  -1258  -1745    454       C  
ATOM   4844  CD2 PHE B 252     -46.278  11.954 -21.921  1.00 79.82           C  
ANISOU 4844  CD2 PHE B 252     6486  14631   9211  -1080  -1895    766       C  
ATOM   4845  CE1 PHE B 252     -44.665   9.707 -21.808  1.00 79.56           C  
ANISOU 4845  CE1 PHE B 252     6750  14563   8917  -1298  -1634    203       C  
ATOM   4846  CE2 PHE B 252     -46.726  10.794 -21.283  1.00 81.64           C  
ANISOU 4846  CE2 PHE B 252     6719  14772   9529  -1129  -1781    509       C  
ATOM   4847  CZ  PHE B 252     -45.915   9.680 -21.227  1.00 78.78           C  
ANISOU 4847  CZ  PHE B 252     6507  14388   9037  -1238  -1654    236       C  
ATOM   4848  N   VAL B 253     -44.628  15.863 -25.069  1.00 86.51           N  
ANISOU 4848  N   VAL B 253     7292  15994   9583  -1058  -2385   1781       N  
ATOM   4849  CA  VAL B 253     -44.951  17.292 -25.220  1.00 88.16           C  
ANISOU 4849  CA  VAL B 253     7389  16159   9949   -927  -2515   2156       C  
ATOM   4850  C   VAL B 253     -45.756  17.543 -26.517  1.00 97.23           C  
ANISOU 4850  C   VAL B 253     8345  17675  10924  -1045  -2774   2398       C  
ATOM   4851  O   VAL B 253     -46.570  18.470 -26.546  1.00 98.81           O  
ANISOU 4851  O   VAL B 253     8373  17845  11324   -935  -2908   2692       O  
ATOM   4852  CB  VAL B 253     -43.729  18.251 -25.115  1.00 90.53           C  
ANISOU 4852  CB  VAL B 253     7839  16302  10257   -841  -2446   2298       C  
ATOM   4853  CG1 VAL B 253     -43.026  18.122 -23.767  1.00 86.74           C  
ANISOU 4853  CG1 VAL B 253     7521  15455   9981   -709  -2213   2097       C  
ATOM   4854  CG2 VAL B 253     -42.747  18.070 -26.267  1.00 91.27           C  
ANISOU 4854  CG2 VAL B 253     8040  16665   9973  -1015  -2484   2294       C  
ATOM   4855  N   ALA B 254     -45.544  16.717 -27.569  1.00 96.05           N  
ANISOU 4855  N   ALA B 254     8217  17867  10410  -1269  -2842   2272       N  
ATOM   4856  CA  ALA B 254     -46.259  16.837 -28.841  1.00 99.91           C  
ANISOU 4856  CA  ALA B 254     8534  18750  10677  -1416  -3091   2472       C  
ATOM   4857  C   ALA B 254     -47.737  16.520 -28.645  1.00107.65           C  
ANISOU 4857  C   ALA B 254     9295  19782  11824  -1409  -3196   2466       C  
ATOM   4858  O   ALA B 254     -48.586  17.131 -29.293  1.00109.81           O  
ANISOU 4858  O   ALA B 254     9368  20263  12093  -1426  -3421   2751       O  
ATOM   4859  CB  ALA B 254     -45.653  15.908 -29.879  1.00101.33           C  
ANISOU 4859  CB  ALA B 254     8808  19268  10424  -1669  -3099   2272       C  
ATOM   4860  N   ASP B 255     -48.032  15.601 -27.704  1.00104.45           N  
ANISOU 4860  N   ASP B 255     8923  19179  11583  -1377  -3033   2156       N  
ATOM   4861  CA  ASP B 255     -49.375  15.157 -27.340  1.00106.05           C  
ANISOU 4861  CA  ASP B 255     8936  19387  11973  -1368  -3085   2093       C  
ATOM   4862  C   ASP B 255     -49.711  15.560 -25.884  1.00109.65           C  
ANISOU 4862  C   ASP B 255     9380  19428  12853  -1133  -2931   2083       C  
ATOM   4863  O   ASP B 255     -50.580  14.940 -25.272  1.00109.18           O  
ANISOU 4863  O   ASP B 255     9227  19293  12963  -1122  -2881   1925       O  
ATOM   4864  CB  ASP B 255     -49.466  13.626 -27.532  1.00107.81           C  
ANISOU 4864  CB  ASP B 255     9203  19765  11995  -1572  -3018   1712       C  
ATOM   4865  CG  ASP B 255     -50.863  13.036 -27.465  1.00122.12           C  
ANISOU 4865  CG  ASP B 255    10804  21672  13922  -1625  -3103   1638       C  
ATOM   4866  OD1 ASP B 255     -51.041  12.017 -26.765  1.00121.50           O  
ANISOU 4866  OD1 ASP B 255    10772  21444  13947  -1646  -2944   1336       O  
ATOM   4867  OD2 ASP B 255     -51.776  13.590 -28.118  1.00132.22           O  
ANISOU 4867  OD2 ASP B 255    11865  23176  15194  -1650  -3331   1890       O  
ATOM   4868  N   TRP B 256     -49.074  16.638 -25.352  1.00106.39           N  
ANISOU 4868  N   TRP B 256     9050  18759  12615   -953  -2861   2260       N  
ATOM   4869  CA  TRP B 256     -49.236  17.101 -23.960  1.00105.17           C  
ANISOU 4869  CA  TRP B 256     8909  18212  12841   -737  -2697   2240       C  
ATOM   4870  C   TRP B 256     -50.691  17.319 -23.515  1.00111.30           C  
ANISOU 4870  C   TRP B 256     9438  18929  13923   -640  -2762   2331       C  
ATOM   4871  O   TRP B 256     -50.972  17.191 -22.324  1.00109.45           O  
ANISOU 4871  O   TRP B 256     9215  18417  13955   -519  -2594   2194       O  
ATOM   4872  CB  TRP B 256     -48.430  18.368 -23.687  1.00103.48           C  
ANISOU 4872  CB  TRP B 256     8783  17785  12750   -582  -2658   2459       C  
ATOM   4873  CG  TRP B 256     -47.910  18.423 -22.282  1.00101.95           C  
ANISOU 4873  CG  TRP B 256     8739  17213  12784   -435  -2415   2286       C  
ATOM   4874  CD1 TRP B 256     -46.898  17.674 -21.749  1.00102.39           C  
ANISOU 4874  CD1 TRP B 256     9021  17157  12725   -476  -2229   2014       C  
ATOM   4875  CD2 TRP B 256     -48.366  19.286 -21.233  1.00101.55           C  
ANISOU 4875  CD2 TRP B 256     8616  16854  13113   -230  -2334   2377       C  
ATOM   4876  NE1 TRP B 256     -46.694  18.019 -20.433  1.00 99.98           N  
ANISOU 4876  NE1 TRP B 256     8793  16511  12685   -316  -2048   1940       N  
ATOM   4877  CE2 TRP B 256     -47.582  19.009 -20.089  1.00102.96           C  
ANISOU 4877  CE2 TRP B 256     8993  16763  13363   -167  -2101   2146       C  
ATOM   4878  CE3 TRP B 256     -49.341  20.296 -21.155  1.00104.92           C  
ANISOU 4878  CE3 TRP B 256     8823  17205  13836    -92  -2433   2631       C  
ATOM   4879  CZ2 TRP B 256     -47.760  19.690 -18.876  1.00101.53           C  
ANISOU 4879  CZ2 TRP B 256     8806  16260  13512     13  -1961   2146       C  
ATOM   4880  CZ3 TRP B 256     -49.521  20.965 -19.952  1.00105.58           C  
ANISOU 4880  CZ3 TRP B 256     8895  16949  14273     96  -2282   2620       C  
ATOM   4881  CH2 TRP B 256     -48.738  20.661 -18.830  1.00103.40           C  
ANISOU 4881  CH2 TRP B 256     8827  16426  14034    141  -2048   2372       C  
ATOM   4882  N   ARG B 257     -51.609  17.620 -24.452  1.00111.34           N  
ANISOU 4882  N   ARG B 257     9216  19202  13884   -700  -3001   2555       N  
ATOM   4883  CA  ARG B 257     -53.026  17.804 -24.143  1.00112.66           C  
ANISOU 4883  CA  ARG B 257     9121  19346  14338   -620  -3081   2650       C  
ATOM   4884  C   ARG B 257     -53.680  16.466 -23.778  1.00115.84           C  
ANISOU 4884  C   ARG B 257     9489  19806  14718   -734  -3005   2330       C  
ATOM   4885  O   ARG B 257     -54.497  16.422 -22.855  1.00116.08           O  
ANISOU 4885  O   ARG B 257     9401  19655  15051   -629  -2922   2270       O  
ATOM   4886  CB  ARG B 257     -53.758  18.446 -25.330  1.00116.57           C  
ANISOU 4886  CB  ARG B 257     9381  20138  14774   -664  -3379   3000       C  
ATOM   4887  N   ASN B 258     -53.297  15.377 -24.484  1.00110.91           N  
ANISOU 4887  N   ASN B 258     8969  19425  13748   -952  -3021   2115       N  
ATOM   4888  CA  ASN B 258     -53.857  14.035 -24.308  1.00109.96           C  
ANISOU 4888  CA  ASN B 258     8820  19381  13577  -1092  -2960   1806       C  
ATOM   4889  C   ASN B 258     -52.958  13.074 -23.512  1.00108.81           C  
ANISOU 4889  C   ASN B 258     8929  19032  13381  -1123  -2703   1460       C  
ATOM   4890  O   ASN B 258     -53.472  12.094 -22.971  1.00107.29           O  
ANISOU 4890  O   ASN B 258     8716  18784  13265  -1180  -2601   1217       O  
ATOM   4891  CB  ASN B 258     -54.162  13.420 -25.676  1.00114.63           C  
ANISOU 4891  CB  ASN B 258     9319  20402  13835  -1334  -3167   1792       C  
ATOM   4892  N   SER B 259     -51.634  13.336 -23.452  1.00103.04           N  
ANISOU 4892  N   SER B 259     8426  18194  12531  -1089  -2603   1447       N  
ATOM   4893  CA  SER B 259     -50.659  12.480 -22.767  1.00 99.45           C  
ANISOU 4893  CA  SER B 259     8212  17553  12022  -1113  -2374   1150       C  
ATOM   4894  C   SER B 259     -50.418  12.886 -21.311  1.00100.19           C  
ANISOU 4894  C   SER B 259     8396  17258  12413   -911  -2174   1126       C  
ATOM   4895  O   SER B 259     -50.099  12.008 -20.506  1.00 98.05           O  
ANISOU 4895  O   SER B 259     8254  16821  12180   -927  -1990    872       O  
ATOM   4896  CB  SER B 259     -49.336  12.450 -23.523  1.00102.20           C  
ANISOU 4896  CB  SER B 259     8748  18016  12067  -1204  -2372   1127       C  
ATOM   4897  OG  SER B 259     -49.365  11.493 -24.570  1.00111.64           O  
ANISOU 4897  OG  SER B 259     9925  19529  12962  -1434  -2461    977       O  
ATOM   4898  N   ASN B 260     -50.581  14.185 -20.958  1.00 96.30           N  
ANISOU 4898  N   ASN B 260     7835  16620  12135   -729  -2205   1383       N  
ATOM   4899  CA  ASN B 260     -50.420  14.656 -19.573  1.00 93.78           C  
ANISOU 4899  CA  ASN B 260     7586  15946  12099   -544  -2016   1356       C  
ATOM   4900  C   ASN B 260     -51.669  14.252 -18.765  1.00 98.39           C  
ANISOU 4900  C   ASN B 260     8011  16440  12933   -505  -1956   1263       C  
ATOM   4901  O   ASN B 260     -52.541  15.072 -18.468  1.00 99.29           O  
ANISOU 4901  O   ASN B 260     7941  16485  13301   -381  -2004   1434       O  
ATOM   4902  CB  ASN B 260     -50.143  16.174 -19.514  1.00 93.04           C  
ANISOU 4902  CB  ASN B 260     7471  15721  12157   -374  -2059   1640       C  
ATOM   4903  CG  ASN B 260     -50.128  16.810 -18.133  1.00106.51           C  
ANISOU 4903  CG  ASN B 260     9215  17078  14174   -185  -1879   1623       C  
ATOM   4904  OD1 ASN B 260     -49.677  16.231 -17.140  1.00 99.71           O  
ANISOU 4904  OD1 ASN B 260     8509  16035  13340   -172  -1683   1398       O  
ATOM   4905  ND2 ASN B 260     -50.625  18.032 -18.046  1.00 96.71           N  
ANISOU 4905  ND2 ASN B 260     7829  15738  13179    -36  -1941   1863       N  
ATOM   4906  N   ARG B 261     -51.755  12.956 -18.455  1.00 94.44           N  
ANISOU 4906  N   ARG B 261     7575  15946  12364   -621  -1849    990       N  
ATOM   4907  CA  ARG B 261     -52.844  12.349 -17.703  1.00 94.99           C  
ANISOU 4907  CA  ARG B 261     7518  15943  12631   -622  -1770    861       C  
ATOM   4908  C   ARG B 261     -52.300  11.198 -16.881  1.00 97.84           C  
ANISOU 4908  C   ARG B 261     8067  16161  12949   -687  -1566    574       C  
ATOM   4909  O   ARG B 261     -51.551  10.376 -17.412  1.00 97.35           O  
ANISOU 4909  O   ARG B 261     8138  16201  12651   -823  -1564    430       O  
ATOM   4910  CB  ARG B 261     -53.962  11.868 -18.646  1.00 97.49           C  
ANISOU 4910  CB  ARG B 261     7606  16546  12889   -757  -1957    887       C  
ATOM   4911  N   TYR B 262     -52.654  11.149 -15.584  1.00 93.58           N  
ANISOU 4911  N   TYR B 262     7534  15382  12639   -591  -1391    493       N  
ATOM   4912  CA  TYR B 262     -52.209  10.089 -14.686  1.00 91.88           C  
ANISOU 4912  CA  TYR B 262     7485  15014  12412   -643  -1195    251       C  
ATOM   4913  C   TYR B 262     -52.907   8.770 -15.054  1.00 96.61           C  
ANISOU 4913  C   TYR B 262     7999  15757  12950   -822  -1217     74       C  
ATOM   4914  O   TYR B 262     -54.067   8.814 -15.454  1.00 98.95           O  
ANISOU 4914  O   TYR B 262     8073  16195  13330   -855  -1329    133       O  
ATOM   4915  CB  TYR B 262     -52.431  10.487 -13.219  1.00 92.56           C  
ANISOU 4915  CB  TYR B 262     7592  14832  12744   -500  -1009    237       C  
ATOM   4916  CG  TYR B 262     -51.364  11.447 -12.731  1.00 94.30           C  
ANISOU 4916  CG  TYR B 262     7975  14878  12977   -363   -938    323       C  
ATOM   4917  CD1 TYR B 262     -50.136  10.980 -12.266  1.00 94.41           C  
ANISOU 4917  CD1 TYR B 262     8230  14771  12869   -381   -814    200       C  
ATOM   4918  CD2 TYR B 262     -51.555  12.827 -12.797  1.00 96.16           C  
ANISOU 4918  CD2 TYR B 262     8115  15071  13352   -220  -1003    532       C  
ATOM   4919  CE1 TYR B 262     -49.136  11.860 -11.847  1.00 93.95           C  
ANISOU 4919  CE1 TYR B 262     8316  14565  12817   -267   -756    275       C  
ATOM   4920  CE2 TYR B 262     -50.563  13.716 -12.379  1.00 95.85           C  
ANISOU 4920  CE2 TYR B 262     8221  14867  13329   -105   -937    602       C  
ATOM   4921  CZ  TYR B 262     -49.352  13.228 -11.907  1.00100.33           C  
ANISOU 4921  CZ  TYR B 262     9031  15331  13762   -133   -816    469       C  
ATOM   4922  OH  TYR B 262     -48.363  14.092 -11.504  1.00 97.82           O  
ANISOU 4922  OH  TYR B 262     8851  14859  13457    -31   -756    530       O  
ATOM   4923  N   PRO B 263     -52.210   7.609 -15.073  1.00 91.64           N  
ANISOU 4923  N   PRO B 263     7530  15114  12176   -947  -1131   -137       N  
ATOM   4924  CA  PRO B 263     -50.835   7.356 -14.605  1.00 88.72           C  
ANISOU 4924  CA  PRO B 263     7414  14583  11715   -924   -997   -228       C  
ATOM   4925  C   PRO B 263     -49.735   7.450 -15.674  1.00 91.02           C  
ANISOU 4925  C   PRO B 263     7820  15013  11752   -985  -1090   -214       C  
ATOM   4926  O   PRO B 263     -48.567   7.228 -15.342  1.00 89.52           O  
ANISOU 4926  O   PRO B 263     7827  14698  11489   -969   -984   -292       O  
ATOM   4927  CB  PRO B 263     -50.937   5.928 -14.059  1.00 90.05           C  
ANISOU 4927  CB  PRO B 263     7640  14665  11912  -1037   -860   -461       C  
ATOM   4928  CG  PRO B 263     -51.945   5.259 -14.967  1.00 97.02           C  
ANISOU 4928  CG  PRO B 263     8338  15771  12752  -1194   -983   -531       C  
ATOM   4929  CD  PRO B 263     -52.888   6.348 -15.444  1.00 94.34           C  
ANISOU 4929  CD  PRO B 263     7786  15579  12481  -1125  -1147   -318       C  
ATOM   4930  N   ALA B 264     -50.085   7.781 -16.932  1.00 87.77           N  
ANISOU 4930  N   ALA B 264     7281  14863  11204  -1056  -1283   -110       N  
ATOM   4931  CA  ALA B 264     -49.141   7.864 -18.055  1.00 86.88           C  
ANISOU 4931  CA  ALA B 264     7257  14928  10827  -1137  -1378    -95       C  
ATOM   4932  C   ALA B 264     -48.059   8.930 -17.865  1.00 87.47           C  
ANISOU 4932  C   ALA B 264     7468  14890  10877  -1001  -1355     61       C  
ATOM   4933  O   ALA B 264     -46.902   8.672 -18.208  1.00 85.93           O  
ANISOU 4933  O   ALA B 264     7432  14712  10506  -1051  -1319    -14       O  
ATOM   4934  CB  ALA B 264     -49.886   8.130 -19.349  1.00 90.31           C  
ANISOU 4934  CB  ALA B 264     7504  15682  11127  -1240  -1600     19       C  
ATOM   4935  N   VAL B 265     -48.422  10.106 -17.304  1.00 82.13           N  
ANISOU 4935  N   VAL B 265     6725  14089  10389   -832  -1365    264       N  
ATOM   4936  CA  VAL B 265     -47.497  11.222 -17.106  1.00 79.94           C  
ANISOU 4936  CA  VAL B 265     6558  13694  10121   -701  -1348    422       C  
ATOM   4937  C   VAL B 265     -46.408  10.901 -16.035  1.00 80.86           C  
ANISOU 4937  C   VAL B 265     6897  13559  10267   -645  -1148    280       C  
ATOM   4938  O   VAL B 265     -45.442  11.656 -15.918  1.00 80.24           O  
ANISOU 4938  O   VAL B 265     6937  13395  10155   -568  -1124    367       O  
ATOM   4939  CB  VAL B 265     -48.252  12.544 -16.812  1.00 84.45           C  
ANISOU 4939  CB  VAL B 265     6981  14190  10915   -542  -1410    664       C  
ATOM   4940  CG1 VAL B 265     -48.641  12.670 -15.345  1.00 82.90           C  
ANISOU 4940  CG1 VAL B 265     6793  13721  10984   -414  -1238    604       C  
ATOM   4941  CG2 VAL B 265     -47.446  13.755 -17.275  1.00 84.32           C  
ANISOU 4941  CG2 VAL B 265     7020  14173  10846   -462  -1483    880       C  
ATOM   4942  N   ILE B 266     -46.535   9.785 -15.288  1.00 74.80           N  
ANISOU 4942  N   ILE B 266     6180  12680   9558   -691  -1012     73       N  
ATOM   4943  CA  ILE B 266     -45.507   9.408 -14.313  1.00 71.51           C  
ANISOU 4943  CA  ILE B 266     5963  12046   9161   -650   -840    -48       C  
ATOM   4944  C   ILE B 266     -44.243   9.045 -15.100  1.00 72.56           C  
ANISOU 4944  C   ILE B 266     6237  12261   9070   -734   -853   -118       C  
ATOM   4945  O   ILE B 266     -43.153   9.498 -14.752  1.00 70.38           O  
ANISOU 4945  O   ILE B 266     6105  11864   8771   -662   -790    -88       O  
ATOM   4946  CB  ILE B 266     -45.974   8.271 -13.363  1.00 74.10           C  
ANISOU 4946  CB  ILE B 266     6303  12247   9605   -691   -702   -229       C  
ATOM   4947  CG1 ILE B 266     -47.214   8.711 -12.574  1.00 75.09           C  
ANISOU 4947  CG1 ILE B 266     6283  12297   9953   -607   -675   -157       C  
ATOM   4948  CG2 ILE B 266     -44.843   7.862 -12.402  1.00 72.92           C  
ANISOU 4948  CG2 ILE B 266     6358  11888   9461   -656   -541   -330       C  
ATOM   4949  CD1 ILE B 266     -48.026   7.619 -12.051  1.00 82.68           C  
ANISOU 4949  CD1 ILE B 266     7182  13227  11007   -686   -595   -303       C  
ATOM   4950  N   LEU B 267     -44.424   8.313 -16.213  1.00 69.60           N  
ANISOU 4950  N   LEU B 267     5807  12108   8529   -888   -941   -208       N  
ATOM   4951  CA  LEU B 267     -43.368   7.877 -17.126  1.00 68.96           C  
ANISOU 4951  CA  LEU B 267     5831  12148   8224   -994   -955   -300       C  
ATOM   4952  C   LEU B 267     -42.732   9.061 -17.845  1.00 72.32           C  
ANISOU 4952  C   LEU B 267     6278  12676   8524   -948  -1055   -102       C  
ATOM   4953  O   LEU B 267     -41.560   8.971 -18.219  1.00 71.98           O  
ANISOU 4953  O   LEU B 267     6362  12650   8336   -983  -1018   -154       O  
ATOM   4954  CB  LEU B 267     -43.903   6.855 -18.140  1.00 70.77           C  
ANISOU 4954  CB  LEU B 267     5971  12607   8312  -1183  -1025   -456       C  
ATOM   4955  CG  LEU B 267     -44.096   5.391 -17.667  1.00 75.14           C  
ANISOU 4955  CG  LEU B 267     6552  13061   8936  -1277   -902   -715       C  
ATOM   4956  CD1 LEU B 267     -42.794   4.717 -17.248  1.00 73.30           C  
ANISOU 4956  CD1 LEU B 267     6505  12656   8688  -1274   -751   -865       C  
ATOM   4957  CD2 LEU B 267     -45.266   5.217 -16.693  1.00 78.01           C  
ANISOU 4957  CD2 LEU B 267     6815  13299   9525  -1229   -859   -709       C  
ATOM   4958  N   PHE B 268     -43.474  10.183 -17.996  1.00 68.22           N  
ANISOU 4958  N   PHE B 268     5632  12210   8080   -866  -1173    129       N  
ATOM   4959  CA  PHE B 268     -42.927  11.412 -18.573  1.00 67.88           C  
ANISOU 4959  CA  PHE B 268     5601  12232   7958   -808  -1266    354       C  
ATOM   4960  C   PHE B 268     -41.869  11.983 -17.633  1.00 70.11           C  
ANISOU 4960  C   PHE B 268     6042  12259   8339   -675  -1137    380       C  
ATOM   4961  O   PHE B 268     -40.811  12.391 -18.100  1.00 70.54           O  
ANISOU 4961  O   PHE B 268     6195  12346   8262   -682  -1144    434       O  
ATOM   4962  CB  PHE B 268     -44.029  12.459 -18.846  1.00 70.94           C  
ANISOU 4962  CB  PHE B 268     5798  12700   8454   -739  -1418    605       C  
ATOM   4963  CG  PHE B 268     -43.518  13.853 -19.156  1.00 72.06           C  
ANISOU 4963  CG  PHE B 268     5951  12824   8606   -639  -1489    866       C  
ATOM   4964  CD1 PHE B 268     -43.044  14.173 -20.424  1.00 75.40           C  
ANISOU 4964  CD1 PHE B 268     6374  13480   8793   -730  -1617    989       C  
ATOM   4965  CD2 PHE B 268     -43.495  14.841 -18.174  1.00 72.35           C  
ANISOU 4965  CD2 PHE B 268     5996  12608   8888   -463  -1422    983       C  
ATOM   4966  CE1 PHE B 268     -42.587  15.464 -20.716  1.00 75.96           C  
ANISOU 4966  CE1 PHE B 268     6449  13525   8886   -643  -1683   1248       C  
ATOM   4967  CE2 PHE B 268     -43.009  16.124 -18.460  1.00 74.65           C  
ANISOU 4967  CE2 PHE B 268     6294  12860   9210   -375  -1482   1220       C  
ATOM   4968  CZ  PHE B 268     -42.570  16.428 -19.731  1.00 73.75           C  
ANISOU 4968  CZ  PHE B 268     6177  12973   8873   -463  -1615   1361       C  
ATOM   4969  N   TYR B 269     -42.154  12.020 -16.314  1.00 64.67           N  
ANISOU 4969  N   TYR B 269     5373  11328   7871   -563  -1020    341       N  
ATOM   4970  CA  TYR B 269     -41.228  12.567 -15.325  1.00 61.99           C  
ANISOU 4970  CA  TYR B 269     5174  10750   7627   -444   -899    356       C  
ATOM   4971  C   TYR B 269     -40.066  11.607 -15.050  1.00 61.74           C  
ANISOU 4971  C   TYR B 269     5315  10648   7495   -502   -780    161       C  
ATOM   4972  O   TYR B 269     -38.934  12.064 -14.873  1.00 58.73           O  
ANISOU 4972  O   TYR B 269     5057  10177   7080   -454   -733    191       O  
ATOM   4973  CB  TYR B 269     -41.967  12.979 -14.052  1.00 63.12           C  
ANISOU 4973  CB  TYR B 269     5271  10689   8022   -320   -817    379       C  
ATOM   4974  CG  TYR B 269     -42.868  14.163 -14.325  1.00 67.96           C  
ANISOU 4974  CG  TYR B 269     5720  11334   8768   -234   -926    596       C  
ATOM   4975  CD1 TYR B 269     -42.336  15.415 -14.630  1.00 70.44           C  
ANISOU 4975  CD1 TYR B 269     6049  11612   9103   -151   -980    788       C  
ATOM   4976  CD2 TYR B 269     -44.250  14.014 -14.372  1.00 70.65           C  
ANISOU 4976  CD2 TYR B 269     5879  11747   9220   -241   -984    618       C  
ATOM   4977  CE1 TYR B 269     -43.159  16.493 -14.949  1.00 73.30           C  
ANISOU 4977  CE1 TYR B 269     6248  11995   9609    -70  -1087   1004       C  
ATOM   4978  CE2 TYR B 269     -45.082  15.079 -14.712  1.00 73.57           C  
ANISOU 4978  CE2 TYR B 269     6076  12150   9725   -161  -1096    830       C  
ATOM   4979  CZ  TYR B 269     -44.532  16.316 -15.006  1.00 82.54           C  
ANISOU 4979  CZ  TYR B 269     7229  13238  10893    -72  -1149   1028       C  
ATOM   4980  OH  TYR B 269     -45.357  17.375 -15.305  1.00 86.51           O  
ANISOU 4980  OH  TYR B 269     7555  13749  11566     17  -1257   1251       O  
ATOM   4981  N   VAL B 270     -40.326  10.289 -15.108  1.00 58.48           N  
ANISOU 4981  N   VAL B 270     4900  10281   7038   -610   -738    -32       N  
ATOM   4982  CA  VAL B 270     -39.305   9.248 -14.972  1.00 57.21           C  
ANISOU 4982  CA  VAL B 270     4877  10059   6800   -674   -632   -222       C  
ATOM   4983  C   VAL B 270     -38.261   9.471 -16.079  1.00 64.04           C  
ANISOU 4983  C   VAL B 270     5802  11072   7460   -737   -684   -203       C  
ATOM   4984  O   VAL B 270     -37.064   9.496 -15.800  1.00 63.56           O  
ANISOU 4984  O   VAL B 270     5870  10906   7374   -705   -607   -236       O  
ATOM   4985  CB  VAL B 270     -39.920   7.823 -15.034  1.00 61.24           C  
ANISOU 4985  CB  VAL B 270     5346  10606   7318   -792   -593   -423       C  
ATOM   4986  CG1 VAL B 270     -38.826   6.760 -15.119  1.00 60.10           C  
ANISOU 4986  CG1 VAL B 270     5326  10410   7099   -865   -496   -612       C  
ATOM   4987  CG2 VAL B 270     -40.833   7.558 -13.838  1.00 60.48           C  
ANISOU 4987  CG2 VAL B 270     5208  10348   7425   -733   -517   -443       C  
ATOM   4988  N   ASN B 271     -38.739   9.703 -17.322  1.00 62.46           N  
ANISOU 4988  N   ASN B 271     5498  11124   7113   -826   -820   -136       N  
ATOM   4989  CA  ASN B 271     -37.915   9.969 -18.495  1.00 62.51           C  
ANISOU 4989  CA  ASN B 271     5537  11318   6897   -906   -882   -100       C  
ATOM   4990  C   ASN B 271     -37.157  11.285 -18.374  1.00 64.39           C  
ANISOU 4990  C   ASN B 271     5835  11482   7149   -795   -898    105       C  
ATOM   4991  O   ASN B 271     -35.974  11.307 -18.720  1.00 62.92           O  
ANISOU 4991  O   ASN B 271     5751  11313   6843   -824   -856     74       O  
ATOM   4992  CB  ASN B 271     -38.765   9.964 -19.767  1.00 63.19           C  
ANISOU 4992  CB  ASN B 271     5482  11705   6822  -1029  -1038    -46       C  
ATOM   4993  CG  ASN B 271     -38.797   8.608 -20.401  1.00 76.71           C  
ANISOU 4993  CG  ASN B 271     7189  13562   8397  -1200  -1011   -297       C  
ATOM   4994  OD1 ASN B 271     -37.946   8.276 -21.216  1.00 72.88           O  
ANISOU 4994  OD1 ASN B 271     6764  13210   7717  -1304   -994   -393       O  
ATOM   4995  ND2 ASN B 271     -39.748   7.777 -20.013  1.00 69.69           N  
ANISOU 4995  ND2 ASN B 271     6225  12639   7615  -1237   -992   -423       N  
ATOM   4996  N   ALA B 272     -37.820  12.369 -17.880  1.00 60.50           N  
ANISOU 4996  N   ALA B 272     5273  10896   6818   -671   -948    303       N  
ATOM   4997  CA  ALA B 272     -37.185  13.683 -17.703  1.00 60.25           C  
ANISOU 4997  CA  ALA B 272     5286  10764   6840   -561   -960    500       C  
ATOM   4998  C   ALA B 272     -35.991  13.577 -16.757  1.00 65.40           C  
ANISOU 4998  C   ALA B 272     6101  11197   7553   -498   -814    401       C  
ATOM   4999  O   ALA B 272     -34.937  14.162 -17.028  1.00 66.22           O  
ANISOU 4999  O   ALA B 272     6283  11291   7585   -486   -806    472       O  
ATOM   5000  CB  ALA B 272     -38.191  14.699 -17.178  1.00 61.16           C  
ANISOU 5000  CB  ALA B 272     5289  10781   7168   -438  -1013    683       C  
ATOM   5001  N   CYS B 273     -36.144  12.770 -15.684  1.00 60.93           N  
ANISOU 5001  N   CYS B 273     5579  10466   7106   -470   -701    237       N  
ATOM   5002  CA  CYS B 273     -35.137  12.503 -14.663  1.00 58.36           C  
ANISOU 5002  CA  CYS B 273     5394   9936   6844   -418   -568    136       C  
ATOM   5003  C   CYS B 273     -33.907  11.849 -15.273  1.00 62.28           C  
ANISOU 5003  C   CYS B 273     5985  10503   7178   -504   -530     20       C  
ATOM   5004  O   CYS B 273     -32.798  12.334 -15.036  1.00 62.81           O  
ANISOU 5004  O   CYS B 273     6145  10484   7235   -461   -487     54       O  
ATOM   5005  CB  CYS B 273     -35.728  11.644 -13.550  1.00 57.55           C  
ANISOU 5005  CB  CYS B 273     5297   9690   6878   -397   -475      1       C  
ATOM   5006  SG  CYS B 273     -36.875  12.529 -12.468  1.00 61.14           S  
ANISOU 5006  SG  CYS B 273     5668  10008   7554   -273   -467    115       S  
ATOM   5007  N   PHE B 274     -34.087  10.782 -16.082  1.00 57.65           N  
ANISOU 5007  N   PHE B 274     5364  10073   6469   -631   -543   -124       N  
ATOM   5008  CA  PHE B 274     -32.954  10.098 -16.718  1.00 57.19           C  
ANISOU 5008  CA  PHE B 274     5379  10083   6266   -721   -492   -261       C  
ATOM   5009  C   PHE B 274     -32.335  10.899 -17.860  1.00 62.78           C  
ANISOU 5009  C   PHE B 274     6085  10973   6794   -767   -565   -142       C  
ATOM   5010  O   PHE B 274     -31.153  10.696 -18.161  1.00 63.43           O  
ANISOU 5010  O   PHE B 274     6248  11062   6791   -800   -503   -213       O  
ATOM   5011  CB  PHE B 274     -33.350   8.716 -17.227  1.00 59.32           C  
ANISOU 5011  CB  PHE B 274     5608  10455   6474   -849   -469   -474       C  
ATOM   5012  CG  PHE B 274     -33.464   7.722 -16.107  1.00 58.86           C  
ANISOU 5012  CG  PHE B 274     5589  10190   6586   -817   -361   -617       C  
ATOM   5013  CD1 PHE B 274     -34.692   7.455 -15.519  1.00 61.57           C  
ANISOU 5013  CD1 PHE B 274     5859  10485   7050   -802   -373   -618       C  
ATOM   5014  CD2 PHE B 274     -32.343   7.048 -15.638  1.00 58.94           C  
ANISOU 5014  CD2 PHE B 274     5701  10052   6640   -805   -247   -739       C  
ATOM   5015  CE1 PHE B 274     -34.800   6.533 -14.485  1.00 61.84           C  
ANISOU 5015  CE1 PHE B 274     5930  10333   7234   -782   -271   -732       C  
ATOM   5016  CE2 PHE B 274     -32.451   6.128 -14.599  1.00 60.90           C  
ANISOU 5016  CE2 PHE B 274     5982  10109   7047   -778   -156   -842       C  
ATOM   5017  CZ  PHE B 274     -33.678   5.883 -14.025  1.00 59.60           C  
ANISOU 5017  CZ  PHE B 274     5753   9905   6989   -770   -166   -835       C  
ATOM   5018  N   PHE B 275     -33.110  11.801 -18.484  1.00 59.37           N  
ANISOU 5018  N   PHE B 275     5558  10686   6312   -769   -694     49       N  
ATOM   5019  CA  PHE B 275     -32.612  12.654 -19.557  1.00 60.20           C  
ANISOU 5019  CA  PHE B 275     5656  10969   6249   -814   -775    205       C  
ATOM   5020  C   PHE B 275     -31.639  13.698 -18.974  1.00 61.90           C  
ANISOU 5020  C   PHE B 275     5958  11008   6553   -702   -731    338       C  
ATOM   5021  O   PHE B 275     -30.521  13.846 -19.474  1.00 60.78           O  
ANISOU 5021  O   PHE B 275     5883  10919   6292   -745   -698    334       O  
ATOM   5022  CB  PHE B 275     -33.772  13.320 -20.319  1.00 63.94           C  
ANISOU 5022  CB  PHE B 275     5992  11635   6668   -842   -937    400       C  
ATOM   5023  CG  PHE B 275     -33.327  14.342 -21.335  1.00 67.07           C  
ANISOU 5023  CG  PHE B 275     6374  12199   6909   -878  -1032    616       C  
ATOM   5024  CD1 PHE B 275     -32.770  13.945 -22.546  1.00 72.16           C  
ANISOU 5024  CD1 PHE B 275     7034  13095   7286  -1032  -1047    553       C  
ATOM   5025  CD2 PHE B 275     -33.449  15.701 -21.074  1.00 69.54           C  
ANISOU 5025  CD2 PHE B 275     6657  12415   7350   -763  -1096    880       C  
ATOM   5026  CE1 PHE B 275     -32.324  14.894 -23.472  1.00 74.90           C  
ANISOU 5026  CE1 PHE B 275     7372  13606   7479  -1075  -1129    767       C  
ATOM   5027  CE2 PHE B 275     -33.012  16.648 -21.999  1.00 74.48           C  
ANISOU 5027  CE2 PHE B 275     7271  13184   7846   -799  -1182   1099       C  
ATOM   5028  CZ  PHE B 275     -32.455  16.240 -23.196  1.00 74.33           C  
ANISOU 5028  CZ  PHE B 275     7272  13428   7544   -958  -1200   1050       C  
ATOM   5029  N   VAL B 276     -32.071  14.404 -17.919  1.00 57.45           N  
ANISOU 5029  N   VAL B 276     5388  10239   6202   -566   -724    441       N  
ATOM   5030  CA  VAL B 276     -31.271  15.410 -17.215  1.00 56.23           C  
ANISOU 5030  CA  VAL B 276     5309   9894   6162   -458   -678    549       C  
ATOM   5031  C   VAL B 276     -30.021  14.708 -16.628  1.00 58.89           C  
ANISOU 5031  C   VAL B 276     5772  10111   6493   -463   -549    369       C  
ATOM   5032  O   VAL B 276     -28.910  15.215 -16.794  1.00 57.58           O  
ANISOU 5032  O   VAL B 276     5672   9925   6281   -460   -522    415       O  
ATOM   5033  CB  VAL B 276     -32.140  16.132 -16.145  1.00 59.36           C  
ANISOU 5033  CB  VAL B 276     5663  10098   6793   -326   -680    643       C  
ATOM   5034  CG1 VAL B 276     -31.312  17.038 -15.241  1.00 57.59           C  
ANISOU 5034  CG1 VAL B 276     5526   9655   6699   -224   -609    698       C  
ATOM   5035  CG2 VAL B 276     -33.261  16.927 -16.809  1.00 60.81           C  
ANISOU 5035  CG2 VAL B 276     5707  10393   7004   -312   -814    849       C  
ATOM   5036  N   GLY B 277     -30.219  13.518 -16.038  1.00 54.74           N  
ANISOU 5036  N   GLY B 277     5267   9520   6012   -479   -476    174       N  
ATOM   5037  CA  GLY B 277     -29.160  12.678 -15.490  1.00 53.08           C  
ANISOU 5037  CA  GLY B 277     5154   9198   5816   -486   -363      5       C  
ATOM   5038  C   GLY B 277     -28.094  12.348 -16.515  1.00 59.33           C  
ANISOU 5038  C   GLY B 277     5977  10129   6437   -581   -343    -64       C  
ATOM   5039  O   GLY B 277     -26.902  12.424 -16.204  1.00 60.05           O  
ANISOU 5039  O   GLY B 277     6145  10126   6545   -556   -273    -96       O  
ATOM   5040  N   SER B 278     -28.518  12.023 -17.761  1.00 56.19           N  
ANISOU 5040  N   SER B 278     5511   9968   5870   -697   -403    -88       N  
ATOM   5041  CA  SER B 278     -27.638  11.732 -18.895  1.00 56.64           C  
ANISOU 5041  CA  SER B 278     5583  10203   5734   -811   -382   -162       C  
ATOM   5042  C   SER B 278     -26.820  12.957 -19.281  1.00 61.04           C  
ANISOU 5042  C   SER B 278     6170  10795   6226   -791   -410     22       C  
ATOM   5043  O   SER B 278     -25.633  12.795 -19.556  1.00 62.11           O  
ANISOU 5043  O   SER B 278     6360  10944   6295   -828   -336    -51       O  
ATOM   5044  CB  SER B 278     -28.435  11.248 -20.105  1.00 62.39           C  
ANISOU 5044  CB  SER B 278     6225  11200   6280   -949   -454   -213       C  
ATOM   5045  OG  SER B 278     -29.011   9.974 -19.877  1.00 72.12           O  
ANISOU 5045  OG  SER B 278     7432  12409   7563   -994   -411   -420       O  
ATOM   5046  N   ILE B 279     -27.436  14.173 -19.316  1.00 56.59           N  
ANISOU 5046  N   ILE B 279     5564  10239   5697   -733   -511    261       N  
ATOM   5047  CA  ILE B 279     -26.744  15.442 -19.612  1.00 56.61           C  
ANISOU 5047  CA  ILE B 279     5589  10246   5673   -708   -543    465       C  
ATOM   5048  C   ILE B 279     -25.569  15.587 -18.640  1.00 59.86           C  
ANISOU 5048  C   ILE B 279     6099  10435   6212   -628   -437    411       C  
ATOM   5049  O   ILE B 279     -24.455  15.905 -19.081  1.00 59.82           O  
ANISOU 5049  O   ILE B 279     6135  10471   6124   -666   -400    434       O  
ATOM   5050  CB  ILE B 279     -27.687  16.684 -19.553  1.00 60.63           C  
ANISOU 5050  CB  ILE B 279     6029  10733   6275   -633   -659    725       C  
ATOM   5051  CG1 ILE B 279     -28.808  16.607 -20.615  1.00 63.19           C  
ANISOU 5051  CG1 ILE B 279     6241  11308   6462   -720   -785    807       C  
ATOM   5052  CG2 ILE B 279     -26.900  18.008 -19.674  1.00 60.88           C  
ANISOU 5052  CG2 ILE B 279     6091  10714   6328   -596   -675    933       C  
ATOM   5053  CD1 ILE B 279     -29.922  17.679 -20.444  1.00 71.67           C  
ANISOU 5053  CD1 ILE B 279     7219  12333   7679   -630   -900   1045       C  
ATOM   5054  N   GLY B 280     -25.832  15.307 -17.348  1.00 54.72           N  
ANISOU 5054  N   GLY B 280     5479   9566   5748   -530   -388    337       N  
ATOM   5055  CA  GLY B 280     -24.842  15.338 -16.270  1.00 52.63           C  
ANISOU 5055  CA  GLY B 280     5300   9090   5607   -457   -298    277       C  
ATOM   5056  C   GLY B 280     -23.676  14.406 -16.531  1.00 55.89           C  
ANISOU 5056  C   GLY B 280     5759   9533   5945   -520   -210    103       C  
ATOM   5057  O   GLY B 280     -22.521  14.825 -16.452  1.00 55.67           O  
ANISOU 5057  O   GLY B 280     5778   9451   5921   -509   -166    124       O  
ATOM   5058  N   TRP B 281     -23.974  13.152 -16.915  1.00 52.38           N  
ANISOU 5058  N   TRP B 281     5288   9178   5436   -593   -181    -71       N  
ATOM   5059  CA  TRP B 281     -22.965  12.150 -17.260  1.00 52.07           C  
ANISOU 5059  CA  TRP B 281     5273   9168   5344   -658    -88   -259       C  
ATOM   5060  C   TRP B 281     -22.224  12.469 -18.569  1.00 59.83           C  
ANISOU 5060  C   TRP B 281     6241  10358   6133   -761    -84   -241       C  
ATOM   5061  O   TRP B 281     -21.059  12.090 -18.707  1.00 59.45           O  
ANISOU 5061  O   TRP B 281     6220  10296   6071   -787      3   -348       O  
ATOM   5062  CB  TRP B 281     -23.605  10.769 -17.379  1.00 50.39           C  
ANISOU 5062  CB  TRP B 281     5026   8985   5133   -714    -55   -454       C  
ATOM   5063  CG  TRP B 281     -23.900  10.148 -16.055  1.00 49.58           C  
ANISOU 5063  CG  TRP B 281     4952   8663   5222   -629    -16   -518       C  
ATOM   5064  CD1 TRP B 281     -25.111  10.082 -15.430  1.00 52.11           C  
ANISOU 5064  CD1 TRP B 281     5247   8924   5628   -589    -57   -484       C  
ATOM   5065  CD2 TRP B 281     -22.959   9.507 -15.183  1.00 48.15           C  
ANISOU 5065  CD2 TRP B 281     4824   8301   5170   -580     73   -615       C  
ATOM   5066  NE1 TRP B 281     -24.977   9.474 -14.205  1.00 50.12           N  
ANISOU 5066  NE1 TRP B 281     5038   8471   5535   -523      4   -548       N  
ATOM   5067  CE2 TRP B 281     -23.668   9.107 -14.026  1.00 50.99           C  
ANISOU 5067  CE2 TRP B 281     5195   8503   5675   -516     77   -622       C  
ATOM   5068  CE3 TRP B 281     -21.573   9.267 -15.249  1.00 48.96           C  
ANISOU 5068  CE3 TRP B 281     4956   8362   5284   -584    146   -686       C  
ATOM   5069  CZ2 TRP B 281     -23.048   8.446 -12.960  1.00 49.41           C  
ANISOU 5069  CZ2 TRP B 281     5041   8116   5616   -461    143   -684       C  
ATOM   5070  CZ3 TRP B 281     -20.953   8.633 -14.187  1.00 49.43           C  
ANISOU 5070  CZ3 TRP B 281     5052   8227   5502   -521    207   -748       C  
ATOM   5071  CH2 TRP B 281     -21.684   8.236 -13.053  1.00 49.52           C  
ANISOU 5071  CH2 TRP B 281     5079   8092   5643   -462    200   -739       C  
ATOM   5072  N   LEU B 282     -22.892  13.147 -19.527  1.00 59.34           N  
ANISOU 5072  N   LEU B 282     6130  10494   5924   -822   -179   -100       N  
ATOM   5073  CA  LEU B 282     -22.314  13.454 -20.848  1.00 60.46           C  
ANISOU 5073  CA  LEU B 282     6254  10872   5848   -941   -183    -65       C  
ATOM   5074  C   LEU B 282     -21.533  14.779 -20.917  1.00 64.78           C  
ANISOU 5074  C   LEU B 282     6829  11394   6389   -909   -202    145       C  
ATOM   5075  O   LEU B 282     -20.764  14.955 -21.868  1.00 66.78           O  
ANISOU 5075  O   LEU B 282     7081  11815   6478  -1006   -174    156       O  
ATOM   5076  CB  LEU B 282     -23.406  13.474 -21.937  1.00 62.07           C  
ANISOU 5076  CB  LEU B 282     6383  11335   5868  -1046   -286     -7       C  
ATOM   5077  CG  LEU B 282     -24.031  12.133 -22.340  1.00 67.51           C  
ANISOU 5077  CG  LEU B 282     7031  12137   6483  -1141   -261   -242       C  
ATOM   5078  CD1 LEU B 282     -25.301  12.352 -23.136  1.00 68.97           C  
ANISOU 5078  CD1 LEU B 282     7134  12539   6533  -1215   -394   -140       C  
ATOM   5079  CD2 LEU B 282     -23.061  11.260 -23.135  1.00 71.75           C  
ANISOU 5079  CD2 LEU B 282     7579  12811   6873  -1266   -148   -461       C  
ATOM   5080  N   ALA B 283     -21.719  15.700 -19.947  1.00 59.23           N  
ANISOU 5080  N   ALA B 283     6150  10492   5864   -785   -241    301       N  
ATOM   5081  CA  ALA B 283     -21.072  17.016 -19.954  1.00 59.13           C  
ANISOU 5081  CA  ALA B 283     6159  10427   5879   -752   -262    505       C  
ATOM   5082  C   ALA B 283     -19.538  16.951 -20.032  1.00 63.76           C  
ANISOU 5082  C   ALA B 283     6793  10992   6441   -783   -160    428       C  
ATOM   5083  O   ALA B 283     -18.939  17.857 -20.618  1.00 65.07           O  
ANISOU 5083  O   ALA B 283     6959  11228   6535   -823   -172    578       O  
ATOM   5084  CB  ALA B 283     -21.490  17.819 -18.743  1.00 58.69           C  
ANISOU 5084  CB  ALA B 283     6122  10129   6046   -615   -293    616       C  
ATOM   5085  N   GLN B 284     -18.914  15.874 -19.494  1.00 57.90           N  
ANISOU 5085  N   GLN B 284     6079  10157   5764   -769    -62    206       N  
ATOM   5086  CA  GLN B 284     -17.461  15.638 -19.512  1.00 56.67           C  
ANISOU 5086  CA  GLN B 284     5949   9970   5612   -792     41    106       C  
ATOM   5087  C   GLN B 284     -16.882  15.460 -20.938  1.00 62.84           C  
ANISOU 5087  C   GLN B 284     6700  11006   6172   -934     86     63       C  
ATOM   5088  O   GLN B 284     -15.675  15.623 -21.120  1.00 62.71           O  
ANISOU 5088  O   GLN B 284     6693  10989   6143   -961    162     42       O  
ATOM   5089  CB  GLN B 284     -17.118  14.391 -18.681  1.00 56.50           C  
ANISOU 5089  CB  GLN B 284     5944   9804   5719   -746    123   -118       C  
ATOM   5090  CG  GLN B 284     -17.895  13.139 -19.102  1.00 59.07           C  
ANISOU 5090  CG  GLN B 284     6234  10226   5983   -804    140   -295       C  
ATOM   5091  CD  GLN B 284     -17.486  11.882 -18.388  1.00 64.70           C  
ANISOU 5091  CD  GLN B 284     6956  10791   6837   -766    227   -503       C  
ATOM   5092  OE1 GLN B 284     -16.331  11.465 -18.428  1.00 59.62           O  
ANISOU 5092  OE1 GLN B 284     6311  10111   6229   -777    317   -609       O  
ATOM   5093  NE2 GLN B 284     -18.435  11.226 -17.744  1.00 51.70           N  
ANISOU 5093  NE2 GLN B 284     5307   9054   5282   -725    204   -561       N  
ATOM   5094  N   PHE B 285     -17.728  15.090 -21.929  1.00 60.46           N  
ANISOU 5094  N   PHE B 285     6356  10927   5689  -1033     44     38       N  
ATOM   5095  CA  PHE B 285     -17.292  14.817 -23.303  1.00 61.28           C  
ANISOU 5095  CA  PHE B 285     6429  11304   5550  -1189     91    -29       C  
ATOM   5096  C   PHE B 285     -17.112  16.088 -24.136  1.00 68.16           C  
ANISOU 5096  C   PHE B 285     7293  12335   6272  -1253     29    226       C  
ATOM   5097  O   PHE B 285     -16.495  16.019 -25.197  1.00 69.79           O  
ANISOU 5097  O   PHE B 285     7482  12762   6273  -1386     83    192       O  
ATOM   5098  CB  PHE B 285     -18.219  13.802 -23.988  1.00 63.33           C  
ANISOU 5098  CB  PHE B 285     6646  11747   5670  -1285     77   -189       C  
ATOM   5099  CG  PHE B 285     -18.176  12.484 -23.246  1.00 63.50           C  
ANISOU 5099  CG  PHE B 285     6674  11603   5853  -1235    163   -450       C  
ATOM   5100  CD1 PHE B 285     -19.207  12.121 -22.382  1.00 64.55           C  
ANISOU 5100  CD1 PHE B 285     6806  11589   6131  -1149    104   -459       C  
ATOM   5101  CD2 PHE B 285     -17.045  11.668 -23.305  1.00 65.15           C  
ANISOU 5101  CD2 PHE B 285     6884  11772   6098  -1262    306   -669       C  
ATOM   5102  CE1 PHE B 285     -19.138  10.941 -21.640  1.00 64.25           C  
ANISOU 5102  CE1 PHE B 285     6775  11382   6256  -1101    181   -671       C  
ATOM   5103  CE2 PHE B 285     -16.973  10.492 -22.552  1.00 66.89           C  
ANISOU 5103  CE2 PHE B 285     7105  11808   6502  -1203    380   -880       C  
ATOM   5104  CZ  PHE B 285     -18.018  10.143 -21.717  1.00 63.99           C  
ANISOU 5104  CZ  PHE B 285     6744  11304   6266  -1125    314   -871       C  
ATOM   5105  N   MET B 286     -17.555  17.250 -23.623  1.00 65.79           N  
ANISOU 5105  N   MET B 286     7004  11909   6085  -1162    -70    477       N  
ATOM   5106  CA  MET B 286     -17.318  18.556 -24.250  1.00 67.79           C  
ANISOU 5106  CA  MET B 286     7251  12253   6255  -1203   -128    749       C  
ATOM   5107  C   MET B 286     -15.813  18.870 -24.139  1.00 73.50           C  
ANISOU 5107  C   MET B 286     8006  12904   7016  -1213    -18    726       C  
ATOM   5108  O   MET B 286     -15.163  18.351 -23.227  1.00 72.00           O  
ANISOU 5108  O   MET B 286     7845  12522   6989  -1137     65    559       O  
ATOM   5109  CB  MET B 286     -18.162  19.651 -23.584  1.00 69.77           C  
ANISOU 5109  CB  MET B 286     7496  12336   6676  -1087   -247    995       C  
ATOM   5110  CG  MET B 286     -19.644  19.463 -23.762  1.00 74.53           C  
ANISOU 5110  CG  MET B 286     8047  13028   7243  -1082   -363   1052       C  
ATOM   5111  SD  MET B 286     -20.591  20.810 -23.018  1.00 79.57           S  
ANISOU 5111  SD  MET B 286     8663  13454   8116   -938   -485   1334       S  
ATOM   5112  CE  MET B 286     -20.293  22.136 -24.231  1.00 79.03           C  
ANISOU 5112  CE  MET B 286     8561  13559   7907  -1028   -564   1671       C  
ATOM   5113  N   ASP B 287     -15.252  19.675 -25.070  1.00 72.56           N  
ANISOU 5113  N   ASP B 287     7877  12946   6748  -1312    -19    896       N  
ATOM   5114  CA  ASP B 287     -13.814  19.975 -25.100  1.00 72.76           C  
ANISOU 5114  CA  ASP B 287     7920  12933   6790  -1342     91    877       C  
ATOM   5115  C   ASP B 287     -13.326  20.603 -23.781  1.00 74.34           C  
ANISOU 5115  C   ASP B 287     8160  12812   7276  -1199     98    924       C  
ATOM   5116  O   ASP B 287     -13.845  21.638 -23.348  1.00 73.64           O  
ANISOU 5116  O   ASP B 287     8080  12593   7308  -1127      7   1139       O  
ATOM   5117  CB  ASP B 287     -13.448  20.856 -26.312  1.00 77.61           C  
ANISOU 5117  CB  ASP B 287     8515  13776   7197  -1477     76   1095       C  
ATOM   5118  CG  ASP B 287     -13.738  20.211 -27.668  1.00 97.24           C  
ANISOU 5118  CG  ASP B 287    10965  16618   9364  -1648     89   1021       C  
ATOM   5119  OD1 ASP B 287     -13.392  19.019 -27.850  1.00 98.57           O  
ANISOU 5119  OD1 ASP B 287    11125  16863   9462  -1699    200    728       O  
ATOM   5120  OD2 ASP B 287     -14.288  20.908 -28.555  1.00106.77           O  
ANISOU 5120  OD2 ASP B 287    12148  18028  10392  -1736     -9   1258       O  
ATOM   5121  N   GLY B 288     -12.377  19.907 -23.138  1.00 69.19           N  
ANISOU 5121  N   GLY B 288     7521  12037   6732  -1162    206    709       N  
ATOM   5122  CA  GLY B 288     -11.769  20.277 -21.860  1.00 66.86           C  
ANISOU 5122  CA  GLY B 288     7258  11463   6683  -1045    224    702       C  
ATOM   5123  C   GLY B 288     -12.710  20.350 -20.666  1.00 68.63           C  
ANISOU 5123  C   GLY B 288     7512  11473   7093   -910    144    722       C  
ATOM   5124  O   GLY B 288     -12.357  20.934 -19.636  1.00 67.61           O  
ANISOU 5124  O   GLY B 288     7411  11128   7149   -825    138    766       O  
ATOM   5125  N   ALA B 289     -13.908  19.745 -20.783  1.00 63.93           N  
ANISOU 5125  N   ALA B 289     6905  10940   6447   -899     88    679       N  
ATOM   5126  CA  ALA B 289     -14.934  19.794 -19.740  1.00 61.83           C  
ANISOU 5126  CA  ALA B 289     6656  10497   6340   -782     18    699       C  
ATOM   5127  C   ALA B 289     -14.628  18.893 -18.550  1.00 61.91           C  
ANISOU 5127  C   ALA B 289     6695  10325   6503   -699     74    499       C  
ATOM   5128  O   ALA B 289     -14.785  19.365 -17.428  1.00 60.92           O  
ANISOU 5128  O   ALA B 289     6601   9999   6546   -603     47    542       O  
ATOM   5129  CB  ALA B 289     -16.291  19.449 -20.314  1.00 63.34           C  
ANISOU 5129  CB  ALA B 289     6812  10830   6424   -808    -60    725       C  
ATOM   5130  N   ARG B 290     -14.171  17.632 -18.763  1.00 56.35           N  
ANISOU 5130  N   ARG B 290     5978   9685   5748   -739    153    285       N  
ATOM   5131  CA  ARG B 290     -13.861  16.714 -17.654  1.00 53.96           C  
ANISOU 5131  CA  ARG B 290     5695   9211   5598   -663    201    116       C  
ATOM   5132  C   ARG B 290     -12.909  17.346 -16.627  1.00 56.47           C  
ANISOU 5132  C   ARG B 290     6044   9341   6073   -595    216    160       C  
ATOM   5133  O   ARG B 290     -13.171  17.230 -15.433  1.00 56.37           O  
ANISOU 5133  O   ARG B 290     6062   9156   6200   -508    193    139       O  
ATOM   5134  CB  ARG B 290     -13.284  15.372 -18.148  1.00 51.89           C  
ANISOU 5134  CB  ARG B 290     5399   9033   5282   -721    298   -106       C  
ATOM   5135  CG  ARG B 290     -13.280  14.283 -17.042  1.00 49.09           C  
ANISOU 5135  CG  ARG B 290     5054   8504   5094   -641    329   -262       C  
ATOM   5136  CD  ARG B 290     -12.787  12.931 -17.536  1.00 53.25           C  
ANISOU 5136  CD  ARG B 290     5538   9088   5607   -692    429   -484       C  
ATOM   5137  NE  ARG B 290     -13.703  12.327 -18.503  1.00 59.98           N  
ANISOU 5137  NE  ARG B 290     6364  10111   6315   -775    429   -570       N  
ATOM   5138  CZ  ARG B 290     -13.514  12.306 -19.819  1.00 68.06           C  
ANISOU 5138  CZ  ARG B 290     7353  11359   7149   -895    470   -614       C  
ATOM   5139  NH1 ARG B 290     -12.417  12.830 -20.347  1.00 55.77           N  
ANISOU 5139  NH1 ARG B 290     5783   9879   5527   -944    524   -579       N  
ATOM   5140  NH2 ARG B 290     -14.417  11.750 -20.617  1.00 47.80           N  
ANISOU 5140  NH2 ARG B 290     4762   8953   4448   -976    459   -698       N  
ATOM   5141  N   ARG B 291     -11.842  18.024 -17.093  1.00 53.20           N  
ANISOU 5141  N   ARG B 291     5619   8970   5626   -646    252    223       N  
ATOM   5142  CA  ARG B 291     -10.821  18.695 -16.283  1.00 52.45           C  
ANISOU 5142  CA  ARG B 291     5542   8723   5663   -606    267    265       C  
ATOM   5143  C   ARG B 291     -11.432  19.884 -15.527  1.00 56.91           C  
ANISOU 5143  C   ARG B 291     6147   9149   6329   -542    188    425       C  
ATOM   5144  O   ARG B 291     -11.073  20.141 -14.379  1.00 56.30           O  
ANISOU 5144  O   ARG B 291     6098   8901   6392   -480    182    409       O  
ATOM   5145  CB  ARG B 291      -9.641  19.147 -17.170  1.00 53.11           C  
ANISOU 5145  CB  ARG B 291     5593   8916   5669   -694    329    302       C  
ATOM   5146  CG  ARG B 291      -8.475  19.754 -16.394  1.00 66.06           C  
ANISOU 5146  CG  ARG B 291     7237  10414   7448   -667    350    324       C  
ATOM   5147  CD  ARG B 291      -7.217  19.914 -17.232  1.00 87.30           C  
ANISOU 5147  CD  ARG B 291     9880  13216  10074   -757    433    317       C  
ATOM   5148  NE  ARG B 291      -6.016  19.757 -16.408  1.00106.47           N  
ANISOU 5148  NE  ARG B 291    12287  15520  12648   -725    473    238       N  
ATOM   5149  CZ  ARG B 291      -5.379  18.604 -16.216  1.00126.32           C  
ANISOU 5149  CZ  ARG B 291    14758  18024  15215   -707    535     64       C  
ATOM   5150  NH1 ARG B 291      -5.807  17.494 -16.807  1.00115.59           N  
ANISOU 5150  NH1 ARG B 291    13376  16762  13780   -722    578    -70       N  
ATOM   5151  NH2 ARG B 291      -4.305  18.554 -15.439  1.00114.80           N  
ANISOU 5151  NH2 ARG B 291    13269  16454  13897   -675    553     21       N  
ATOM   5152  N   GLU B 292     -12.365  20.585 -16.162  1.00 54.67           N  
ANISOU 5152  N   GLU B 292     5858   8937   5977   -561    129    574       N  
ATOM   5153  CA  GLU B 292     -13.060  21.712 -15.556  1.00 54.94           C  
ANISOU 5153  CA  GLU B 292     5915   8835   6126   -498     62    723       C  
ATOM   5154  C   GLU B 292     -14.003  21.244 -14.433  1.00 57.45           C  
ANISOU 5154  C   GLU B 292     6257   9025   6546   -407     34    643       C  
ATOM   5155  O   GLU B 292     -14.106  21.901 -13.396  1.00 56.22           O  
ANISOU 5155  O   GLU B 292     6131   8697   6531   -343     19    670       O  
ATOM   5156  CB  GLU B 292     -13.840  22.478 -16.649  1.00 57.96           C  
ANISOU 5156  CB  GLU B 292     6266   9342   6413   -543      1    917       C  
ATOM   5157  CG  GLU B 292     -14.834  23.511 -16.144  1.00 68.05           C  
ANISOU 5157  CG  GLU B 292     7546  10483   7826   -470    -70   1071       C  
ATOM   5158  CD  GLU B 292     -14.304  24.716 -15.386  1.00 94.10           C  
ANISOU 5158  CD  GLU B 292    10869  13588  11296   -434    -64   1162       C  
ATOM   5159  OE1 GLU B 292     -15.147  25.539 -14.966  1.00101.00           O  
ANISOU 5159  OE1 GLU B 292    11738  14336  12301   -372   -110   1270       O  
ATOM   5160  OE2 GLU B 292     -13.069  24.868 -15.242  1.00 84.57           O  
ANISOU 5160  OE2 GLU B 292     9678  12354  10101   -472    -10   1126       O  
ATOM   5161  N   ILE B 293     -14.684  20.114 -14.649  1.00 54.28           N  
ANISOU 5161  N   ILE B 293     5841   8713   6072   -411     34    536       N  
ATOM   5162  CA  ILE B 293     -15.659  19.562 -13.710  1.00 53.49           C  
ANISOU 5162  CA  ILE B 293     5756   8516   6051   -340     14    462       C  
ATOM   5163  C   ILE B 293     -14.989  18.927 -12.487  1.00 57.66           C  
ANISOU 5163  C   ILE B 293     6321   8907   6680   -295     58    327       C  
ATOM   5164  O   ILE B 293     -15.356  19.223 -11.358  1.00 56.81           O  
ANISOU 5164  O   ILE B 293     6246   8658   6682   -231     43    331       O  
ATOM   5165  CB  ILE B 293     -16.563  18.520 -14.446  1.00 56.49           C  
ANISOU 5165  CB  ILE B 293     6100   9046   6319   -376      2    390       C  
ATOM   5166  CG1 ILE B 293     -17.467  19.205 -15.515  1.00 57.73           C  
ANISOU 5166  CG1 ILE B 293     6212   9343   6378   -415    -68    548       C  
ATOM   5167  CG2 ILE B 293     -17.390  17.649 -13.455  1.00 55.27           C  
ANISOU 5167  CG2 ILE B 293     5959   8793   6249   -314      2    281       C  
ATOM   5168  CD1 ILE B 293     -17.876  18.310 -16.679  1.00 62.20           C  
ANISOU 5168  CD1 ILE B 293     6735  10131   6769   -503    -73    480       C  
ATOM   5169  N   VAL B 294     -14.012  18.066 -12.733  1.00 54.60           N  
ANISOU 5169  N   VAL B 294     5921   8568   6256   -331    112    213       N  
ATOM   5170  CA  VAL B 294     -13.396  17.148 -11.796  1.00 52.73           C  
ANISOU 5170  CA  VAL B 294     5699   8232   6103   -296    148     86       C  
ATOM   5171  C   VAL B 294     -12.071  17.648 -11.175  1.00 56.08           C  
ANISOU 5171  C   VAL B 294     6137   8566   6607   -288    164    100       C  
ATOM   5172  O   VAL B 294     -11.714  17.165 -10.092  1.00 54.91           O  
ANISOU 5172  O   VAL B 294     6007   8310   6547   -246    164     40       O  
ATOM   5173  CB  VAL B 294     -13.266  15.850 -12.636  1.00 56.30           C  
ANISOU 5173  CB  VAL B 294     6109   8796   6485   -343    200    -49       C  
ATOM   5174  CG1 VAL B 294     -11.970  15.085 -12.446  1.00 55.97           C  
ANISOU 5174  CG1 VAL B 294     6049   8699   6519   -337    258   -161       C  
ATOM   5175  CG2 VAL B 294     -14.492  14.976 -12.474  1.00 55.19           C  
ANISOU 5175  CG2 VAL B 294     5966   8672   6332   -329    184   -109       C  
ATOM   5176  N   CYS B 295     -11.374  18.618 -11.804  1.00 53.89           N  
ANISOU 5176  N   CYS B 295     5845   8333   6297   -334    172    186       N  
ATOM   5177  CA  CYS B 295     -10.132  19.129 -11.225  1.00 54.76           C  
ANISOU 5177  CA  CYS B 295     5958   8360   6487   -336    185    195       C  
ATOM   5178  C   CYS B 295     -10.302  20.518 -10.656  1.00 55.68           C  
ANISOU 5178  C   CYS B 295     6111   8374   6672   -319    145    311       C  
ATOM   5179  O   CYS B 295     -11.136  21.306 -11.129  1.00 54.96           O  
ANISOU 5179  O   CYS B 295     6025   8299   6558   -321    117    419       O  
ATOM   5180  CB  CYS B 295      -8.969  19.133 -12.225  1.00 57.29           C  
ANISOU 5180  CB  CYS B 295     6228   8786   6751   -406    242    186       C  
ATOM   5181  SG  CYS B 295      -8.897  17.707 -13.328  1.00 63.06           S  
ANISOU 5181  SG  CYS B 295     6906   9675   7380   -451    311     46       S  
ATOM   5182  N  AARG B 296      -9.446  20.842  -9.680  0.50 50.25           N  
ANISOU 5182  N  AARG B 296     5438   7578   6076   -308    142    288       N  
ATOM   5183  N  BARG B 296      -9.460  20.840  -9.653  0.50 50.33           N  
ANISOU 5183  N  BARG B 296     5449   7586   6088   -307    141    288       N  
ATOM   5184  CA AARG B 296      -9.341  22.178  -9.121  0.50 49.45           C  
ANISOU 5184  CA AARG B 296     5365   7367   6056   -307    118    369       C  
ATOM   5185  CA BARG B 296      -9.345  22.177  -9.083  0.50 49.58           C  
ANISOU 5185  CA BARG B 296     5383   7382   6075   -306    118    367       C  
ATOM   5186  C  AARG B 296      -8.533  22.991 -10.134  0.50 53.99           C  
ANISOU 5186  C  AARG B 296     5906   7997   6610   -375    142    462       C  
ATOM   5187  C  BARG B 296      -8.517  22.985 -10.097  0.50 54.08           C  
ANISOU 5187  C  BARG B 296     5918   8005   6624   -374    142    460       C  
ATOM   5188  O  AARG B 296      -7.883  22.397 -11.002  0.50 53.65           O  
ANISOU 5188  O  AARG B 296     5820   8073   6491   -419    182    436       O  
ATOM   5189  O  BARG B 296      -7.844  22.379 -10.939  0.50 53.79           O  
ANISOU 5189  O  BARG B 296     5838   8085   6513   -418    182    431       O  
ATOM   5190  CB AARG B 296      -8.678  22.139  -7.734  0.50 47.04           C  
ANISOU 5190  CB AARG B 296     5084   6953   5837   -290    104    295       C  
ATOM   5191  CB BARG B 296      -8.703  22.134  -7.676  0.50 47.38           C  
ANISOU 5191  CB BARG B 296     5129   6993   5881   -288    103    293       C  
ATOM   5192  CG AARG B 296      -9.542  21.476  -6.666  0.50 52.14           C  
ANISOU 5192  CG AARG B 296     5770   7542   6497   -233     81    229       C  
ATOM   5193  CG BARG B 296      -9.687  21.740  -6.570  0.50 53.22           C  
ANISOU 5193  CG BARG B 296     5915   7663   6644   -232     78    239       C  
ATOM   5194  CD AARG B 296      -9.023  21.709  -5.258  0.50 52.43           C  
ANISOU 5194  CD AARG B 296     5838   7484   6597   -232     58    178       C  
ATOM   5195  CD BARG B 296      -9.106  21.776  -5.152  0.50 54.91           C  
ANISOU 5195  CD BARG B 296     6157   7791   6915   -229     56    178       C  
ATOM   5196  NE AARG B 296      -9.063  23.125  -4.899  0.50 54.99           N  
ANISOU 5196  NE AARG B 296     6189   7717   6988   -250     53    221       N  
ATOM   5197  NE BARG B 296      -8.371  20.550  -4.826  0.50 58.82           N  
ANISOU 5197  NE BARG B 296     6627   8324   7399   -224     50    110       N  
ATOM   5198  CZ AARG B 296      -8.890  23.595  -3.672  0.50 68.16           C  
ANISOU 5198  CZ AARG B 296     7893   9300   8705   -258     37    171       C  
ATOM   5199  CZ BARG B 296      -8.303  19.991  -3.617  0.50 68.24           C  
ANISOU 5199  CZ BARG B 296     7843   9476   8608   -208     20     61       C  
ATOM   5200  NH1AARG B 296      -8.939  24.900  -3.444  0.50 54.50           N  
ANISOU 5200  NH1AARG B 296     6182   7477   7051   -280     46    194       N  
ATOM   5201  NH1BARG B 296      -8.971  20.515  -2.593  0.50 56.08           N  
ANISOU 5201  NH1BARG B 296     6360   7870   7077   -202      2     50       N  
ATOM   5202  NH2AARG B 296      -8.680  22.765  -2.661  0.50 62.98           N  
ANISOU 5202  NH2AARG B 296     7254   8652   8022   -250     14     97       N  
ATOM   5203  NH2BARG B 296      -7.601  18.875  -3.435  0.50 39.44           N  
ANISOU 5203  NH2BARG B 296     4159   5857   4971   -200      9     24       N  
ATOM   5204  N   ALA B 297      -8.584  24.327 -10.061  1.00 51.32           N  
ANISOU 5204  N   ALA B 297     5584   7572   6344   -387    127    568       N  
ATOM   5205  CA  ALA B 297      -7.842  25.182 -11.004  1.00 52.45           C  
ANISOU 5205  CA  ALA B 297     5695   7753   6479   -458    150    680       C  
ATOM   5206  C   ALA B 297      -6.310  24.889 -10.967  1.00 58.15           C  
ANISOU 5206  C   ALA B 297     6381   8506   7209   -509    191    611       C  
ATOM   5207  O   ALA B 297      -5.645  24.975 -12.004  1.00 58.95           O  
ANISOU 5207  O   ALA B 297     6439   8712   7246   -576    232    662       O  
ATOM   5208  CB  ALA B 297      -8.111  26.645 -10.698  1.00 53.67           C  
ANISOU 5208  CB  ALA B 297     5872   7762   6757   -455    129    790       C  
ATOM   5209  N   ASP B 298      -5.790  24.448  -9.790  1.00 53.94           N  
ANISOU 5209  N   ASP B 298     5856   7895   6743   -480    178    495       N  
ATOM   5210  CA  ASP B 298      -4.379  24.128  -9.584  1.00 53.51           C  
ANISOU 5210  CA  ASP B 298     5753   7857   6721   -516    203    429       C  
ATOM   5211  C   ASP B 298      -4.023  22.642  -9.898  1.00 58.04           C  
ANISOU 5211  C   ASP B 298     6280   8536   7238   -501    235    322       C  
ATOM   5212  O   ASP B 298      -2.957  22.178  -9.476  1.00 59.66           O  
ANISOU 5212  O   ASP B 298     6436   8734   7497   -508    245    253       O  
ATOM   5213  CB  ASP B 298      -3.946  24.487  -8.152  1.00 53.91           C  
ANISOU 5213  CB  ASP B 298     5826   7781   6878   -504    160    374       C  
ATOM   5214  CG  ASP B 298      -4.551  23.639  -7.051  1.00 57.41           C  
ANISOU 5214  CG  ASP B 298     6307   8183   7322   -438    119    285       C  
ATOM   5215  OD1 ASP B 298      -5.332  22.715  -7.366  1.00 56.53           O  
ANISOU 5215  OD1 ASP B 298     6203   8128   7146   -395    126    260       O  
ATOM   5216  OD2 ASP B 298      -4.319  23.954  -5.878  1.00 60.79           O  
ANISOU 5216  OD2 ASP B 298     6759   8527   7809   -437     82    245       O  
ATOM   5217  N   GLY B 299      -4.902  21.924 -10.597  1.00 51.39           N  
ANISOU 5217  N   GLY B 299     5444   7780   6302   -482    250    308       N  
ATOM   5218  CA  GLY B 299      -4.654  20.547 -11.014  1.00 50.28           C  
ANISOU 5218  CA  GLY B 299     5257   7729   6119   -474    295    196       C  
ATOM   5219  C   GLY B 299      -4.846  19.455  -9.980  1.00 53.29           C  
ANISOU 5219  C   GLY B 299     5646   8042   6562   -405    267     96       C  
ATOM   5220  O   GLY B 299      -4.593  18.285 -10.273  1.00 52.41           O  
ANISOU 5220  O   GLY B 299     5488   7977   6447   -394    308      0       O  
ATOM   5221  N   THR B 300      -5.280  19.807  -8.761  1.00 50.12           N  
ANISOU 5221  N   THR B 300     5299   7526   6218   -363    203    114       N  
ATOM   5222  CA  THR B 300      -5.534  18.794  -7.723  1.00 49.16           C  
ANISOU 5222  CA  THR B 300     5191   7346   6142   -304    171     43       C  
ATOM   5223  C   THR B 300      -6.985  18.288  -7.851  1.00 52.00           C  
ANISOU 5223  C   THR B 300     5594   7720   6444   -269    166     31       C  
ATOM   5224  O   THR B 300      -7.780  18.926  -8.549  1.00 51.01           O  
ANISOU 5224  O   THR B 300     5491   7637   6255   -284    170     91       O  
ATOM   5225  CB  THR B 300      -5.204  19.317  -6.332  1.00 51.28           C  
ANISOU 5225  CB  THR B 300     5492   7512   6478   -293    111     56       C  
ATOM   5226  OG1 THR B 300      -5.975  20.491  -6.074  1.00 52.09           O  
ANISOU 5226  OG1 THR B 300     5659   7564   6570   -300     90    116       O  
ATOM   5227  CG2 THR B 300      -3.710  19.575  -6.152  1.00 45.88           C  
ANISOU 5227  CG2 THR B 300     4749   6824   5861   -330    107     52       C  
ATOM   5228  N   MET B 301      -7.332  17.128  -7.233  1.00 48.41           N  
ANISOU 5228  N   MET B 301     5143   7234   6017   -224    156    -35       N  
ATOM   5229  CA  MET B 301      -8.699  16.666  -7.417  1.00 48.36           C  
ANISOU 5229  CA  MET B 301     5168   7245   5961   -200    156    -49       C  
ATOM   5230  C   MET B 301      -9.686  17.463  -6.566  1.00 50.69           C  
ANISOU 5230  C   MET B 301     5531   7470   6257   -175    112      5       C  
ATOM   5231  O   MET B 301      -9.327  17.979  -5.515  1.00 49.23           O  
ANISOU 5231  O   MET B 301     5376   7211   6120   -168     80     18       O  
ATOM   5232  CB  MET B 301      -8.895  15.137  -7.290  1.00 50.78           C  
ANISOU 5232  CB  MET B 301     5449   7547   6300   -172    176   -139       C  
ATOM   5233  CG  MET B 301      -8.708  14.534  -5.953  1.00 54.14           C  
ANISOU 5233  CG  MET B 301     5892   7876   6802   -131    138   -147       C  
ATOM   5234  SD  MET B 301      -8.766  12.714  -6.101  1.00 58.90           S  
ANISOU 5234  SD  MET B 301     6443   8461   7475   -104    175   -239       S  
ATOM   5235  CE  MET B 301     -10.515  12.439  -5.963  1.00 56.31           C  
ANISOU 5235  CE  MET B 301     6170   8135   7089    -92    171   -246       C  
ATOM   5236  N   ARG B 302     -10.903  17.659  -7.105  1.00 47.73           N  
ANISOU 5236  N   ARG B 302     5174   7131   5831   -168    112     33       N  
ATOM   5237  CA  ARG B 302     -11.955  18.383  -6.396  1.00 46.91           C  
ANISOU 5237  CA  ARG B 302     5119   6960   5745   -140     84     75       C  
ATOM   5238  C   ARG B 302     -12.455  17.514  -5.280  1.00 50.54           C  
ANISOU 5238  C   ARG B 302     5608   7367   6230   -105     75     17       C  
ATOM   5239  O   ARG B 302     -12.836  16.365  -5.494  1.00 50.16           O  
ANISOU 5239  O   ARG B 302     5542   7351   6167    -95     89    -33       O  
ATOM   5240  CB  ARG B 302     -13.081  18.824  -7.335  1.00 45.53           C  
ANISOU 5240  CB  ARG B 302     4934   6842   5524   -140     81    134       C  
ATOM   5241  CG  ARG B 302     -12.575  19.841  -8.309  1.00 51.50           C  
ANISOU 5241  CG  ARG B 302     5668   7644   6257   -180     83    224       C  
ATOM   5242  CD  ARG B 302     -13.606  20.342  -9.260  1.00 51.84           C  
ANISOU 5242  CD  ARG B 302     5691   7752   6253   -184     65    314       C  
ATOM   5243  NE  ARG B 302     -14.095  21.628  -8.799  1.00 61.69           N  
ANISOU 5243  NE  ARG B 302     6959   8896   7586   -157     42    404       N  
ATOM   5244  CZ  ARG B 302     -14.241  22.701  -9.557  1.00 69.35           C  
ANISOU 5244  CZ  ARG B 302     7907   9877   8565   -175     26    535       C  
ATOM   5245  NH1 ARG B 302     -13.942  22.654 -10.847  1.00 56.23           N  
ANISOU 5245  NH1 ARG B 302     6210   8352   6804   -230     25    599       N  
ATOM   5246  NH2 ARG B 302     -14.695  23.826  -9.036  1.00 57.12           N  
ANISOU 5246  NH2 ARG B 302     6370   8204   7130   -142     14    603       N  
ATOM   5247  N   LEU B 303     -12.325  18.026  -4.068  1.00 48.99           N  
ANISOU 5247  N   LEU B 303     5453   7090   6070    -97     55     19       N  
ATOM   5248  CA  LEU B 303     -12.714  17.331  -2.846  1.00 49.31           C  
ANISOU 5248  CA  LEU B 303     5527   7087   6120    -78     44    -19       C  
ATOM   5249  C   LEU B 303     -13.358  18.297  -1.894  1.00 52.54           C  
ANISOU 5249  C   LEU B 303     5986   7434   6541    -74     42    -14       C  
ATOM   5250  O   LEU B 303     -12.931  19.450  -1.798  1.00 54.03           O  
ANISOU 5250  O   LEU B 303     6186   7587   6756    -93     38      6       O  
ATOM   5251  CB  LEU B 303     -11.491  16.677  -2.177  1.00 50.19           C  
ANISOU 5251  CB  LEU B 303     5628   7187   6256    -89     20    -39       C  
ATOM   5252  CG  LEU B 303     -10.791  15.542  -2.936  1.00 56.19           C  
ANISOU 5252  CG  LEU B 303     6325   7986   7038    -86     35    -64       C  
ATOM   5253  CD1 LEU B 303      -9.406  15.285  -2.384  1.00 56.91           C  
ANISOU 5253  CD1 LEU B 303     6386   8058   7180    -96      5    -61       C  
ATOM   5254  CD2 LEU B 303     -11.629  14.279  -2.958  1.00 58.20           C  
ANISOU 5254  CD2 LEU B 303     6572   8242   7298    -62     54    -99       C  
ATOM   5255  N   GLY B 304     -14.398  17.832  -1.223  1.00 47.62           N  
ANISOU 5255  N   GLY B 304     5390   6797   5908    -55     53    -38       N  
ATOM   5256  CA  GLY B 304     -15.115  18.596  -0.218  1.00 46.47           C  
ANISOU 5256  CA  GLY B 304     5287   6596   5772    -54     69    -58       C  
ATOM   5257  C   GLY B 304     -15.749  19.862  -0.722  1.00 49.40           C  
ANISOU 5257  C   GLY B 304     5648   6929   6192    -38     89    -30       C  
ATOM   5258  O   GLY B 304     -15.660  20.893  -0.057  1.00 49.13           O  
ANISOU 5258  O   GLY B 304     5641   6830   6197    -51    103    -50       O  
ATOM   5259  N   GLU B 305     -16.365  19.783  -1.910  1.00 45.89           N  
ANISOU 5259  N   GLU B 305     5160   6526   5751    -15     90     17       N  
ATOM   5260  CA  GLU B 305     -17.095  20.877  -2.549  1.00 46.18           C  
ANISOU 5260  CA  GLU B 305     5170   6534   5844      7     97     77       C  
ATOM   5261  C   GLU B 305     -18.534  20.953  -1.982  1.00 49.25           C  
ANISOU 5261  C   GLU B 305     5555   6885   6272     44    126     52       C  
ATOM   5262  O   GLU B 305     -19.071  19.909  -1.606  1.00 46.82           O  
ANISOU 5262  O   GLU B 305     5253   6613   5923     48    135      8       O  
ATOM   5263  CB  GLU B 305     -17.137  20.681  -4.075  1.00 47.57           C  
ANISOU 5263  CB  GLU B 305     5293   6799   5982      4     73    149       C  
ATOM   5264  CG  GLU B 305     -15.795  20.895  -4.757  1.00 54.21           C  
ANISOU 5264  CG  GLU B 305     6125   7675   6797    -35     61    182       C  
ATOM   5265  CD  GLU B 305     -15.659  22.125  -5.636  1.00 68.89           C  
ANISOU 5265  CD  GLU B 305     7958   9523   8693    -46     51    289       C  
ATOM   5266  OE1 GLU B 305     -16.652  22.866  -5.819  1.00 72.14           O  
ANISOU 5266  OE1 GLU B 305     8350   9898   9162    -15     46    352       O  
ATOM   5267  OE2 GLU B 305     -14.549  22.326  -6.175  1.00 61.50           O  
ANISOU 5267  OE2 GLU B 305     7014   8616   7737    -86     49    317       O  
ATOM   5268  N   PRO B 306     -19.204  22.129  -1.917  1.00 48.37           N  
ANISOU 5268  N   PRO B 306     5428   6695   6256     71    147     79       N  
ATOM   5269  CA  PRO B 306     -18.764  23.497  -2.283  1.00 49.41           C  
ANISOU 5269  CA  PRO B 306     5549   6751   6475     70    144    140       C  
ATOM   5270  C   PRO B 306     -17.545  23.989  -1.502  1.00 55.99           C  
ANISOU 5270  C   PRO B 306     6433   7527   7314     25    154     83       C  
ATOM   5271  O   PRO B 306     -17.433  23.749  -0.301  1.00 55.64           O  
ANISOU 5271  O   PRO B 306     6435   7462   7245      5    178    -15       O  
ATOM   5272  CB  PRO B 306     -19.980  24.370  -1.923  1.00 51.71           C  
ANISOU 5272  CB  PRO B 306     5808   6945   6892    118    182    143       C  
ATOM   5273  CG  PRO B 306     -21.146  23.439  -1.896  1.00 55.71           C  
ANISOU 5273  CG  PRO B 306     6289   7516   7364    147    188    122       C  
ATOM   5274  CD  PRO B 306     -20.586  22.139  -1.396  1.00 50.49           C  
ANISOU 5274  CD  PRO B 306     5677   6930   6576    109    184     47       C  
ATOM   5275  N   THR B 307     -16.624  24.655  -2.211  1.00 55.95           N  
ANISOU 5275  N   THR B 307     6416   7510   7332     -1    132    150       N  
ATOM   5276  CA  THR B 307     -15.401  25.270  -1.677  1.00 57.39           C  
ANISOU 5276  CA  THR B 307     6630   7639   7536    -52    134    112       C  
ATOM   5277  C   THR B 307     -15.287  26.730  -2.123  1.00 63.60           C  
ANISOU 5277  C   THR B 307     7393   8318   8453    -56    147    182       C  
ATOM   5278  O   THR B 307     -16.032  27.215  -2.988  1.00 63.21           O  
ANISOU 5278  O   THR B 307     7299   8249   8470    -17    143    287       O  
ATOM   5279  CB  THR B 307     -14.108  24.517  -2.100  1.00 70.98           C  
ANISOU 5279  CB  THR B 307     8349   9454   9165    -93     98    122       C  
ATOM   5280  OG1 THR B 307     -14.180  24.109  -3.464  1.00 71.53           O  
ANISOU 5280  OG1 THR B 307     8375   9615   9186    -82     79    207       O  
ATOM   5281  CG2 THR B 307     -13.771  23.355  -1.203  1.00 73.35           C  
ANISOU 5281  CG2 THR B 307     8682   9805   9383   -108     86     35       C  
ATOM   5282  N   SER B 308     -14.322  27.409  -1.521  1.00 61.85           N  
ANISOU 5282  N   SER B 308     7198   8028   8274   -107    158    131       N  
ATOM   5283  CA  SER B 308     -13.953  28.784  -1.794  1.00 63.36           C  
ANISOU 5283  CA  SER B 308     7373   8099   8604   -128    175    183       C  
ATOM   5284  C   SER B 308     -13.054  28.849  -3.018  1.00 67.76           C  
ANISOU 5284  C   SER B 308     7897   8717   9133   -159    141    309       C  
ATOM   5285  O   SER B 308     -12.241  27.947  -3.242  1.00 67.43           O  
ANISOU 5285  O   SER B 308     7857   8792   8973   -188    114    297       O  
ATOM   5286  CB  SER B 308     -13.220  29.366  -0.589  1.00 68.06           C  
ANISOU 5286  CB  SER B 308     8008   8610   9241   -188    201     53       C  
ATOM   5287  OG  SER B 308     -12.163  28.505  -0.186  1.00 76.33           O  
ANISOU 5287  OG  SER B 308     9079   9763  10160   -239    163     -1       O  
ATOM   5288  N   ASN B 309     -13.217  29.915  -3.815  1.00 64.61           N  
ANISOU 5288  N   ASN B 309     7461   8235   8852   -153    148    434       N  
ATOM   5289  CA  ASN B 309     -12.422  30.279  -4.994  1.00 64.15           C  
ANISOU 5289  CA  ASN B 309     7369   8217   8788   -195    128    574       C  
ATOM   5290  C   ASN B 309     -12.260  29.159  -6.052  1.00 66.85           C  
ANISOU 5290  C   ASN B 309     7688   8752   8960   -200     94    638       C  
ATOM   5291  O   ASN B 309     -11.289  29.145  -6.818  1.00 67.83           O  
ANISOU 5291  O   ASN B 309     7792   8949   9030   -255     89    699       O  
ATOM   5292  CB  ASN B 309     -11.068  30.825  -4.560  1.00 62.33           C  
ANISOU 5292  CB  ASN B 309     7153   7931   8599   -271    141    522       C  
ATOM   5293  CG  ASN B 309     -11.228  32.101  -3.778  1.00 82.37           C  
ANISOU 5293  CG  ASN B 309     9703  10272  11323   -281    181    472       C  
ATOM   5294  OD1 ASN B 309     -11.354  32.089  -2.553  1.00 71.64           O  
ANISOU 5294  OD1 ASN B 309     8382   8857   9981   -285    204    315       O  
ATOM   5295  ND2 ASN B 309     -11.345  33.218  -4.480  1.00 81.38           N  
ANISOU 5295  ND2 ASN B 309     9542  10035  11344   -285    194    608       N  
ATOM   5296  N   GLU B 310     -13.246  28.279  -6.145  1.00 60.69           N  
ANISOU 5296  N   GLU B 310     6904   8052   8104   -149     80    622       N  
ATOM   5297  CA  GLU B 310     -13.273  27.269  -7.187  1.00 58.93           C  
ANISOU 5297  CA  GLU B 310     6656   8004   7732   -157     55    666       C  
ATOM   5298  C   GLU B 310     -14.470  27.562  -8.061  1.00 63.57           C  
ANISOU 5298  C   GLU B 310     7200   8622   8331   -120     29    798       C  
ATOM   5299  O   GLU B 310     -15.377  28.294  -7.658  1.00 65.29           O  
ANISOU 5299  O   GLU B 310     7408   8722   8678    -70     31    829       O  
ATOM   5300  CB  GLU B 310     -13.279  25.831  -6.642  1.00 58.53           C  
ANISOU 5300  CB  GLU B 310     6629   8036   7576   -144     56    529       C  
ATOM   5301  CG  GLU B 310     -11.924  25.338  -6.148  1.00 59.97           C  
ANISOU 5301  CG  GLU B 310     6829   8237   7721   -187     64    438       C  
ATOM   5302  CD  GLU B 310     -10.742  25.354  -7.107  1.00 69.02           C  
ANISOU 5302  CD  GLU B 310     7940   9470   8814   -245     70    489       C  
ATOM   5303  OE1 GLU B 310     -10.938  25.176  -8.330  1.00 74.34           O  
ANISOU 5303  OE1 GLU B 310     8580  10255   9412   -259     69    566       O  
ATOM   5304  OE2 GLU B 310      -9.601  25.488  -6.617  1.00 49.00           O  
ANISOU 5304  OE2 GLU B 310     5407   6906   6307   -285     77    444       O  
ATOM   5305  N   THR B 311     -14.446  27.038  -9.274  1.00 58.47           N  
ANISOU 5305  N   THR B 311     6522   8140   7556   -150      4    875       N  
ATOM   5306  CA  THR B 311     -15.477  27.220 -10.278  1.00 58.60           C  
ANISOU 5306  CA  THR B 311     6488   8231   7546   -133    -38   1017       C  
ATOM   5307  C   THR B 311     -16.778  26.434  -9.855  1.00 62.75           C  
ANISOU 5307  C   THR B 311     7006   8775   8061    -71    -52    941       C  
ATOM   5308  O   THR B 311     -16.711  25.580  -8.969  1.00 61.94           O  
ANISOU 5308  O   THR B 311     6941   8659   7935    -56    -25    784       O  
ATOM   5309  CB  THR B 311     -14.833  26.814 -11.586  1.00 63.89           C  
ANISOU 5309  CB  THR B 311     7133   9090   8052   -209    -51   1090       C  
ATOM   5310  OG1 THR B 311     -15.015  27.807 -12.583  1.00 67.67           O  
ANISOU 5310  OG1 THR B 311     7567   9597   8546   -231    -89   1300       O  
ATOM   5311  CG2 THR B 311     -15.162  25.427 -12.018  1.00 60.75           C  
ANISOU 5311  CG2 THR B 311     6728   8860   7494   -222    -54    991       C  
ATOM   5312  N   LEU B 312     -17.954  26.763 -10.431  1.00 59.64           N  
ANISOU 5312  N   LEU B 312     6557   8406   7698    -37    -97   1061       N  
ATOM   5313  CA  LEU B 312     -19.208  26.101 -10.034  1.00 58.83           C  
ANISOU 5313  CA  LEU B 312     6433   8317   7602     18   -107    995       C  
ATOM   5314  C   LEU B 312     -19.456  24.792 -10.790  1.00 61.09           C  
ANISOU 5314  C   LEU B 312     6702   8805   7705    -20   -133    952       C  
ATOM   5315  O   LEU B 312     -20.353  24.039 -10.412  1.00 60.69           O  
ANISOU 5315  O   LEU B 312     6639   8774   7647     12   -135    872       O  
ATOM   5316  CB  LEU B 312     -20.428  27.030 -10.203  1.00 60.07           C  
ANISOU 5316  CB  LEU B 312     6522   8394   7907     79   -143   1134       C  
ATOM   5317  CG  LEU B 312     -20.665  28.090  -9.115  1.00 65.42           C  
ANISOU 5317  CG  LEU B 312     7208   8841   8809    140    -96   1112       C  
ATOM   5318  CD1 LEU B 312     -21.439  29.275  -9.671  1.00 67.65           C  
ANISOU 5318  CD1 LEU B 312     7408   9039   9259    186   -136   1309       C  
ATOM   5319  CD2 LEU B 312     -21.411  27.514  -7.924  1.00 66.35           C  
ANISOU 5319  CD2 LEU B 312     7346   8893   8970    188    -47    940       C  
ATOM   5320  N   SER B 313     -18.653  24.501 -11.816  1.00 56.50           N  
ANISOU 5320  N   SER B 313     6117   8368   6980    -95   -143    989       N  
ATOM   5321  CA  SER B 313     -18.808  23.319 -12.676  1.00 55.77           C  
ANISOU 5321  CA  SER B 313     6002   8476   6709   -148   -158    937       C  
ATOM   5322  C   SER B 313     -19.000  21.983 -11.915  1.00 57.05           C  
ANISOU 5322  C   SER B 313     6193   8637   6846   -131   -122    741       C  
ATOM   5323  O   SER B 313     -19.820  21.168 -12.338  1.00 57.09           O  
ANISOU 5323  O   SER B 313     6164   8752   6776   -144   -144    703       O  
ATOM   5324  CB  SER B 313     -17.629  23.198 -13.633  1.00 56.76           C  
ANISOU 5324  CB  SER B 313     6132   8732   6700   -236   -140    957       C  
ATOM   5325  OG  SER B 313     -17.524  24.405 -14.367  1.00 58.82           O  
ANISOU 5325  OG  SER B 313     6367   9002   6981   -260   -176   1158       O  
ATOM   5326  N   CYS B 314     -18.278  21.775 -10.810  1.00 51.35           N  
ANISOU 5326  N   CYS B 314     5527   7794   6191   -108    -72    628       N  
ATOM   5327  CA  CYS B 314     -18.367  20.547 -10.022  1.00 49.69           C  
ANISOU 5327  CA  CYS B 314     5344   7566   5970    -93    -39    469       C  
ATOM   5328  C   CYS B 314     -19.741  20.419  -9.337  1.00 51.52           C  
ANISOU 5328  C   CYS B 314     5564   7740   6273    -37    -49    449       C  
ATOM   5329  O   CYS B 314     -20.414  19.403  -9.508  1.00 50.44           O  
ANISOU 5329  O   CYS B 314     5406   7677   6084    -45    -52    382       O  
ATOM   5330  CB  CYS B 314     -17.232  20.480  -9.004  1.00 49.39           C  
ANISOU 5330  CB  CYS B 314     5360   7423   5983    -87      1    387       C  
ATOM   5331  SG  CYS B 314     -17.177  18.939  -8.050  1.00 52.51           S  
ANISOU 5331  SG  CYS B 314     5784   7796   6371    -74     33    225       S  
ATOM   5332  N   VAL B 315     -20.160  21.449  -8.585  1.00 47.58           N  
ANISOU 5332  N   VAL B 315     5072   7107   5900     15    -46    498       N  
ATOM   5333  CA  VAL B 315     -21.417  21.427  -7.851  1.00 48.07           C  
ANISOU 5333  CA  VAL B 315     5115   7104   6044     69    -39    471       C  
ATOM   5334  C   VAL B 315     -22.619  21.366  -8.830  1.00 51.19           C  
ANISOU 5334  C   VAL B 315     5429   7604   6417     74    -93    558       C  
ATOM   5335  O   VAL B 315     -23.590  20.665  -8.531  1.00 50.25           O  
ANISOU 5335  O   VAL B 315     5285   7507   6302     90    -89    497       O  
ATOM   5336  CB  VAL B 315     -21.545  22.556  -6.790  1.00 53.56           C  
ANISOU 5336  CB  VAL B 315     5833   7628   6890    118     -6    476       C  
ATOM   5337  CG1 VAL B 315     -20.529  22.362  -5.666  1.00 52.45           C  
ANISOU 5337  CG1 VAL B 315     5770   7412   6746    102     41    361       C  
ATOM   5338  CG2 VAL B 315     -21.390  23.937  -7.401  1.00 54.97           C  
ANISOU 5338  CG2 VAL B 315     5982   7753   7152    127    -30    619       C  
ATOM   5339  N   ILE B 316     -22.489  21.981 -10.035  1.00 47.12           N  
ANISOU 5339  N   ILE B 316     4869   7173   5859     46   -146    699       N  
ATOM   5340  CA  ILE B 316     -23.507  21.952 -11.085  1.00 47.08           C  
ANISOU 5340  CA  ILE B 316     4780   7300   5807     35   -216    804       C  
ATOM   5341  C   ILE B 316     -23.703  20.516 -11.566  1.00 50.59           C  
ANISOU 5341  C   ILE B 316     5215   7902   6104    -23   -221    692       C  
ATOM   5342  O   ILE B 316     -24.842  20.060 -11.603  1.00 52.92           O  
ANISOU 5342  O   ILE B 316     5456   8244   6407    -11   -247    676       O  
ATOM   5343  CB  ILE B 316     -23.186  22.926 -12.265  1.00 50.88           C  
ANISOU 5343  CB  ILE B 316     5223   7855   6253      2   -276    997       C  
ATOM   5344  CG1 ILE B 316     -23.418  24.391 -11.837  1.00 51.56           C  
ANISOU 5344  CG1 ILE B 316     5288   7765   6538     72   -282   1130       C  
ATOM   5345  CG2 ILE B 316     -24.011  22.598 -13.540  1.00 51.50           C  
ANISOU 5345  CG2 ILE B 316     5219   8140   6208    -45   -361   1093       C  
ATOM   5346  CD1 ILE B 316     -22.816  25.478 -12.820  1.00 54.63           C  
ANISOU 5346  CD1 ILE B 316     5658   8178   6921     37   -324   1330       C  
ATOM   5347  N   ILE B 317     -22.622  19.809 -11.920  1.00 44.90           N  
ANISOU 5347  N   ILE B 317     4540   7255   5266    -85   -190    606       N  
ATOM   5348  CA  ILE B 317     -22.713  18.426 -12.413  1.00 44.66           C  
ANISOU 5348  CA  ILE B 317     4499   7358   5113   -146   -179    479       C  
ATOM   5349  C   ILE B 317     -23.280  17.523 -11.316  1.00 48.87           C  
ANISOU 5349  C   ILE B 317     5051   7798   5721   -108   -137    344       C  
ATOM   5350  O   ILE B 317     -24.228  16.781 -11.593  1.00 49.94           O  
ANISOU 5350  O   ILE B 317     5139   8011   5824   -129   -155    295       O  
ATOM   5351  CB  ILE B 317     -21.370  17.903 -13.026  1.00 47.09           C  
ANISOU 5351  CB  ILE B 317     4839   7748   5306   -216   -139    408       C  
ATOM   5352  CG1 ILE B 317     -21.061  18.640 -14.348  1.00 48.64           C  
ANISOU 5352  CG1 ILE B 317     5001   8092   5387   -279   -183    546       C  
ATOM   5353  CG2 ILE B 317     -21.355  16.378 -13.252  1.00 46.60           C  
ANISOU 5353  CG2 ILE B 317     4772   7765   5168   -267   -100    233       C  
ATOM   5354  CD1 ILE B 317     -22.267  18.760 -15.371  1.00 55.75           C  
ANISOU 5354  CD1 ILE B 317     5824   9163   6197   -318   -268    649       C  
ATOM   5355  N   PHE B 318     -22.786  17.663 -10.065  1.00 44.14           N  
ANISOU 5355  N   PHE B 318     4514   7038   5220    -58    -87    296       N  
ATOM   5356  CA  PHE B 318     -23.304  16.894  -8.940  1.00 41.88           C  
ANISOU 5356  CA  PHE B 318     4250   6665   4998    -29    -46    192       C  
ATOM   5357  C   PHE B 318     -24.813  17.128  -8.809  1.00 46.34           C  
ANISOU 5357  C   PHE B 318     4753   7228   5625      6    -70    231       C  
ATOM   5358  O   PHE B 318     -25.556  16.146  -8.727  1.00 46.19           O  
ANISOU 5358  O   PHE B 318     4709   7244   5596    -11    -60    154       O  
ATOM   5359  CB  PHE B 318     -22.561  17.221  -7.619  1.00 41.75           C  
ANISOU 5359  CB  PHE B 318     4306   6497   5058      9      1    159       C  
ATOM   5360  CG  PHE B 318     -23.392  16.962  -6.377  1.00 41.03           C  
ANISOU 5360  CG  PHE B 318     4231   6314   5045     47     36    105       C  
ATOM   5361  CD1 PHE B 318     -23.586  15.666  -5.907  1.00 40.77           C  
ANISOU 5361  CD1 PHE B 318     4211   6283   4996     28     66      9       C  
ATOM   5362  CD2 PHE B 318     -24.071  18.000  -5.747  1.00 42.07           C  
ANISOU 5362  CD2 PHE B 318     4353   6361   5273     97     46    152       C  
ATOM   5363  CE1 PHE B 318     -24.418  15.420  -4.822  1.00 40.41           C  
ANISOU 5363  CE1 PHE B 318     4175   6171   5009     52    103    -29       C  
ATOM   5364  CE2 PHE B 318     -24.914  17.747  -4.662  1.00 43.94           C  
ANISOU 5364  CE2 PHE B 318     4596   6532   5569    121     91     93       C  
ATOM   5365  CZ  PHE B 318     -25.083  16.459  -4.210  1.00 40.71           C  
ANISOU 5365  CZ  PHE B 318     4204   6141   5122     95    118      9       C  
ATOM   5366  N   VAL B 319     -25.264  18.409  -8.809  1.00 43.49           N  
ANISOU 5366  N   VAL B 319     4360   6818   5347     53    -98    351       N  
ATOM   5367  CA  VAL B 319     -26.699  18.739  -8.664  1.00 44.24           C  
ANISOU 5367  CA  VAL B 319     4378   6897   5533     97   -119    398       C  
ATOM   5368  C   VAL B 319     -27.513  18.068  -9.789  1.00 50.03           C  
ANISOU 5368  C   VAL B 319     5028   7802   6178     49   -183    417       C  
ATOM   5369  O   VAL B 319     -28.536  17.463  -9.501  1.00 49.81           O  
ANISOU 5369  O   VAL B 319     4955   7788   6184     53   -176    363       O  
ATOM   5370  CB  VAL B 319     -26.993  20.271  -8.565  1.00 47.82           C  
ANISOU 5370  CB  VAL B 319     4796   7253   6121    162   -136    530       C  
ATOM   5371  CG1 VAL B 319     -28.498  20.565  -8.670  1.00 47.58           C  
ANISOU 5371  CG1 VAL B 319     4657   7230   6192    207   -169    596       C  
ATOM   5372  CG2 VAL B 319     -26.430  20.855  -7.265  1.00 46.63           C  
ANISOU 5372  CG2 VAL B 319     4720   6928   6070    202    -60    470       C  
ATOM   5373  N   ILE B 320     -27.030  18.128 -11.041  1.00 48.14           N  
ANISOU 5373  N   ILE B 320     4771   7704   5815    -10   -238    482       N  
ATOM   5374  CA  ILE B 320     -27.709  17.507 -12.179  1.00 49.22           C  
ANISOU 5374  CA  ILE B 320     4833   8032   5838    -77   -304    491       C  
ATOM   5375  C   ILE B 320     -27.756  15.968 -12.008  1.00 54.25           C  
ANISOU 5375  C   ILE B 320     5489   8708   6414   -131   -256    304       C  
ATOM   5376  O   ILE B 320     -28.825  15.395 -12.157  1.00 55.10           O  
ANISOU 5376  O   ILE B 320     5530   8879   6527   -151   -280    268       O  
ATOM   5377  CB  ILE B 320     -27.063  17.912 -13.542  1.00 52.86           C  
ANISOU 5377  CB  ILE B 320     5279   8652   6153   -145   -364    595       C  
ATOM   5378  CG1 ILE B 320     -27.170  19.432 -13.806  1.00 53.97           C  
ANISOU 5378  CG1 ILE B 320     5381   8754   6372    -96   -423    811       C  
ATOM   5379  CG2 ILE B 320     -27.685  17.134 -14.692  1.00 53.38           C  
ANISOU 5379  CG2 ILE B 320     5276   8942   6065   -239   -424    567       C  
ATOM   5380  CD1 ILE B 320     -26.246  19.939 -14.911  1.00 57.94           C  
ANISOU 5380  CD1 ILE B 320     5898   9370   6746   -159   -457    923       C  
ATOM   5381  N   VAL B 321     -26.618  15.311 -11.720  1.00 50.82           N  
ANISOU 5381  N   VAL B 321     5136   8231   5941   -156   -190    192       N  
ATOM   5382  CA  VAL B 321     -26.555  13.845 -11.586  1.00 50.23           C  
ANISOU 5382  CA  VAL B 321     5078   8171   5837   -205   -140     22       C  
ATOM   5383  C   VAL B 321     -27.365  13.358 -10.363  1.00 53.23           C  
ANISOU 5383  C   VAL B 321     5462   8424   6338   -160    -97    -37       C  
ATOM   5384  O   VAL B 321     -28.313  12.590 -10.540  1.00 53.77           O  
ANISOU 5384  O   VAL B 321     5475   8548   6406   -195   -105    -98       O  
ATOM   5385  CB  VAL B 321     -25.097  13.302 -11.562  1.00 52.80           C  
ANISOU 5385  CB  VAL B 321     5473   8465   6121   -232    -81    -68       C  
ATOM   5386  CG1 VAL B 321     -25.063  11.784 -11.325  1.00 51.84           C  
ANISOU 5386  CG1 VAL B 321     5361   8319   6016   -269    -22   -235       C  
ATOM   5387  CG2 VAL B 321     -24.365  13.655 -12.858  1.00 53.25           C  
ANISOU 5387  CG2 VAL B 321     5516   8674   6042   -296   -108    -29       C  
ATOM   5388  N   TYR B 322     -26.997  13.814  -9.152  1.00 47.43           N  
ANISOU 5388  N   TYR B 322     4790   7534   5697    -93    -52    -21       N  
ATOM   5389  CA  TYR B 322     -27.614  13.400  -7.900  1.00 45.28           C  
ANISOU 5389  CA  TYR B 322     4534   7148   5521    -60      1    -74       C  
ATOM   5390  C   TYR B 322     -29.094  13.729  -7.801  1.00 49.40           C  
ANISOU 5390  C   TYR B 322     4974   7685   6109    -35    -20    -32       C  
ATOM   5391  O   TYR B 322     -29.861  12.864  -7.383  1.00 49.49           O  
ANISOU 5391  O   TYR B 322     4962   7688   6155    -54     11   -104       O  
ATOM   5392  CB  TYR B 322     -26.879  13.994  -6.701  1.00 44.97           C  
ANISOU 5392  CB  TYR B 322     4577   6969   5541     -8     47    -59       C  
ATOM   5393  CG  TYR B 322     -27.445  13.516  -5.382  1.00 45.41           C  
ANISOU 5393  CG  TYR B 322     4657   6929   5666     11    107   -113       C  
ATOM   5394  CD1 TYR B 322     -27.197  12.227  -4.921  1.00 46.34           C  
ANISOU 5394  CD1 TYR B 322     4810   7020   5778    -24    146   -196       C  
ATOM   5395  CD2 TYR B 322     -28.281  14.332  -4.625  1.00 45.72           C  
ANISOU 5395  CD2 TYR B 322     4677   6908   5787     59    130    -78       C  
ATOM   5396  CE1 TYR B 322     -27.766  11.764  -3.740  1.00 46.43           C  
ANISOU 5396  CE1 TYR B 322     4841   6959   5841    -19    200   -226       C  
ATOM   5397  CE2 TYR B 322     -28.873  13.871  -3.456  1.00 45.86           C  
ANISOU 5397  CE2 TYR B 322     4712   6860   5852     62    194   -131       C  
ATOM   5398  CZ  TYR B 322     -28.585  12.599  -2.997  1.00 49.56           C  
ANISOU 5398  CZ  TYR B 322     5224   7315   6293     20    227   -196       C  
ATOM   5399  OH  TYR B 322     -29.139  12.167  -1.819  1.00 46.31           O  
ANISOU 5399  OH  TYR B 322     4832   6847   5915     14    291   -230       O  
ATOM   5400  N   TYR B 323     -29.502  14.962  -8.126  1.00 46.95           N  
ANISOU 5400  N   TYR B 323     4614   7385   5838     10    -67     87       N  
ATOM   5401  CA  TYR B 323     -30.909  15.326  -8.025  1.00 47.25           C  
ANISOU 5401  CA  TYR B 323     4556   7430   5968     44    -86    133       C  
ATOM   5402  C   TYR B 323     -31.741  14.468  -8.983  1.00 53.43           C  
ANISOU 5402  C   TYR B 323     5250   8365   6685    -23   -141    106       C  
ATOM   5403  O   TYR B 323     -32.771  13.959  -8.555  1.00 54.39           O  
ANISOU 5403  O   TYR B 323     5317   8479   6872    -25   -119     58       O  
ATOM   5404  CB  TYR B 323     -31.149  16.827  -8.263  1.00 48.00           C  
ANISOU 5404  CB  TYR B 323     4601   7494   6144    109   -131    280       C  
ATOM   5405  CG  TYR B 323     -32.571  17.247  -7.958  1.00 48.46           C  
ANISOU 5405  CG  TYR B 323     4550   7524   6338    161   -135    323       C  
ATOM   5406  CD1 TYR B 323     -33.576  17.132  -8.916  1.00 50.90           C  
ANISOU 5406  CD1 TYR B 323     4735   7966   6638    141   -222    391       C  
ATOM   5407  CD2 TYR B 323     -32.909  17.780  -6.717  1.00 48.36           C  
ANISOU 5407  CD2 TYR B 323     4550   7360   6465    227    -51    291       C  
ATOM   5408  CE1 TYR B 323     -34.891  17.494  -8.631  1.00 53.22           C  
ANISOU 5408  CE1 TYR B 323     4912   8233   7077    193   -226    432       C  
ATOM   5409  CE2 TYR B 323     -34.215  18.168  -6.429  1.00 49.78           C  
ANISOU 5409  CE2 TYR B 323     4617   7508   6788    278    -41    319       C  
ATOM   5410  CZ  TYR B 323     -35.207  17.999  -7.378  1.00 59.07           C  
ANISOU 5410  CZ  TYR B 323     5663   8809   7971    265   -129    392       C  
ATOM   5411  OH  TYR B 323     -36.492  18.362  -7.073  1.00 62.09           O  
ANISOU 5411  OH  TYR B 323     5920   9159   8513    319   -118    421       O  
ATOM   5412  N   ALA B 324     -31.283  14.280 -10.250  1.00 49.79           N  
ANISOU 5412  N   ALA B 324     4774   8050   6092    -88   -206    125       N  
ATOM   5413  CA  ALA B 324     -31.981  13.456 -11.249  1.00 50.01           C  
ANISOU 5413  CA  ALA B 324     4721   8248   6033   -172   -263     81       C  
ATOM   5414  C   ALA B 324     -32.047  11.978 -10.818  1.00 52.17           C  
ANISOU 5414  C   ALA B 324     5023   8495   6305   -228   -193    -94       C  
ATOM   5415  O   ALA B 324     -33.086  11.327 -10.999  1.00 53.84           O  
ANISOU 5415  O   ALA B 324     5154   8772   6530   -272   -211   -145       O  
ATOM   5416  CB  ALA B 324     -31.304  13.573 -12.596  1.00 51.14           C  
ANISOU 5416  CB  ALA B 324     4861   8555   6015   -242   -328    121       C  
ATOM   5417  N   LEU B 325     -30.955  11.467 -10.227  1.00 44.61           N  
ANISOU 5417  N   LEU B 325     4169   7433   5347   -226   -117   -176       N  
ATOM   5418  CA  LEU B 325     -30.905  10.110  -9.718  1.00 44.46           C  
ANISOU 5418  CA  LEU B 325     4181   7355   5358   -268    -48   -319       C  
ATOM   5419  C   LEU B 325     -31.970   9.901  -8.617  1.00 52.45           C  
ANISOU 5419  C   LEU B 325     5168   8269   6491   -234     -4   -326       C  
ATOM   5420  O   LEU B 325     -32.812   9.002  -8.742  1.00 54.05           O  
ANISOU 5420  O   LEU B 325     5314   8504   6716   -290      6   -404       O  
ATOM   5421  CB  LEU B 325     -29.514   9.783  -9.193  1.00 43.42           C  
ANISOU 5421  CB  LEU B 325     4154   7120   5225   -256     14   -367       C  
ATOM   5422  CG  LEU B 325     -29.326   8.348  -8.707  1.00 47.62           C  
ANISOU 5422  CG  LEU B 325     4716   7569   5808   -294     84   -495       C  
ATOM   5423  CD1 LEU B 325     -29.347   7.357  -9.886  1.00 48.15           C  
ANISOU 5423  CD1 LEU B 325     4735   7747   5813   -391     79   -618       C  
ATOM   5424  CD2 LEU B 325     -28.066   8.226  -7.860  1.00 46.71           C  
ANISOU 5424  CD2 LEU B 325     4695   7324   5729   -254    135   -496       C  
ATOM   5425  N   MET B 326     -31.972  10.778  -7.594  1.00 49.56           N  
ANISOU 5425  N   MET B 326     4837   7793   6200   -153     26   -251       N  
ATOM   5426  CA  MET B 326     -32.913  10.728  -6.468  1.00 49.58           C  
ANISOU 5426  CA  MET B 326     4822   7709   6310   -121     83   -259       C  
ATOM   5427  C   MET B 326     -34.358  11.034  -6.892  1.00 52.87           C  
ANISOU 5427  C   MET B 326     5106   8204   6777   -119     40   -220       C  
ATOM   5428  O   MET B 326     -35.275  10.376  -6.400  1.00 52.76           O  
ANISOU 5428  O   MET B 326     5047   8171   6829   -141     83   -272       O  
ATOM   5429  CB  MET B 326     -32.460  11.662  -5.339  1.00 51.28           C  
ANISOU 5429  CB  MET B 326     5109   7801   6576    -47    133   -209       C  
ATOM   5430  CG  MET B 326     -31.181  11.201  -4.678  1.00 53.91           C  
ANISOU 5430  CG  MET B 326     5560   8052   6872    -55    178   -250       C  
ATOM   5431  SD  MET B 326     -31.330   9.616  -3.787  1.00 58.64           S  
ANISOU 5431  SD  MET B 326     6194   8586   7500   -108    253   -340       S  
ATOM   5432  CE  MET B 326     -30.340   8.566  -4.832  1.00 53.81           C  
ANISOU 5432  CE  MET B 326     5601   8016   6828   -167    224   -407       C  
ATOM   5433  N   ALA B 327     -34.565  11.967  -7.834  1.00 49.59           N  
ANISOU 5433  N   ALA B 327     4622   7884   6337   -100    -49   -122       N  
ATOM   5434  CA  ALA B 327     -35.910  12.262  -8.343  1.00 50.71           C  
ANISOU 5434  CA  ALA B 327     4620   8115   6532    -98   -111    -66       C  
ATOM   5435  C   ALA B 327     -36.437  11.051  -9.112  1.00 55.04           C  
ANISOU 5435  C   ALA B 327     5105   8794   7015   -202   -146   -156       C  
ATOM   5436  O   ALA B 327     -37.608  10.703  -8.982  1.00 56.18           O  
ANISOU 5436  O   ALA B 327     5148   8966   7230   -219   -149   -177       O  
ATOM   5437  CB  ALA B 327     -35.894  13.507  -9.220  1.00 52.19           C  
ANISOU 5437  CB  ALA B 327     4749   8373   6707    -56   -209     86       C  
ATOM   5438  N   GLY B 328     -35.535  10.369  -9.815  1.00 51.01           N  
ANISOU 5438  N   GLY B 328     4654   8349   6380   -274   -159   -228       N  
ATOM   5439  CA  GLY B 328     -35.839   9.157 -10.562  1.00 51.64           C  
ANISOU 5439  CA  GLY B 328     4688   8540   6391   -386   -177   -348       C  
ATOM   5440  C   GLY B 328     -36.317   7.985  -9.725  1.00 54.97           C  
ANISOU 5440  C   GLY B 328     5118   8866   6904   -421    -89   -469       C  
ATOM   5441  O   GLY B 328     -37.230   7.280 -10.139  1.00 56.32           O  
ANISOU 5441  O   GLY B 328     5197   9118   7084   -497   -110   -538       O  
ATOM   5442  N   VAL B 329     -35.709   7.754  -8.557  1.00 51.12           N  
ANISOU 5442  N   VAL B 329     4733   8209   6480   -376      7   -491       N  
ATOM   5443  CA  VAL B 329     -36.086   6.634  -7.681  1.00 50.37           C  
ANISOU 5443  CA  VAL B 329     4654   8011   6474   -411     96   -581       C  
ATOM   5444  C   VAL B 329     -37.395   6.972  -6.925  1.00 54.02           C  
ANISOU 5444  C   VAL B 329     5036   8445   7043   -378    122   -536       C  
ATOM   5445  O   VAL B 329     -38.148   6.055  -6.591  1.00 55.00           O  
ANISOU 5445  O   VAL B 329     5117   8547   7233   -435    168   -605       O  
ATOM   5446  CB  VAL B 329     -34.947   6.151  -6.732  1.00 52.36           C  
ANISOU 5446  CB  VAL B 329     5038   8109   6746   -388    179   -607       C  
ATOM   5447  CG1 VAL B 329     -33.741   5.651  -7.528  1.00 52.07           C  
ANISOU 5447  CG1 VAL B 329     5055   8097   6632   -428    165   -674       C  
ATOM   5448  CG2 VAL B 329     -34.528   7.217  -5.727  1.00 50.87           C  
ANISOU 5448  CG2 VAL B 329     4920   7832   6576   -293    205   -508       C  
ATOM   5449  N   VAL B 330     -37.688   8.276  -6.712  1.00 48.91           N  
ANISOU 5449  N   VAL B 330     4359   7798   6426   -292     97   -426       N  
ATOM   5450  CA  VAL B 330     -38.927   8.727  -6.067  1.00 48.90           C  
ANISOU 5450  CA  VAL B 330     4265   7774   6542   -252    128   -388       C  
ATOM   5451  C   VAL B 330     -40.104   8.566  -7.075  1.00 55.50           C  
ANISOU 5451  C   VAL B 330     4938   8757   7391   -303     41   -386       C  
ATOM   5452  O   VAL B 330     -41.155   8.033  -6.700  1.00 55.79           O  
ANISOU 5452  O   VAL B 330     4891   8792   7515   -336     81   -430       O  
ATOM   5453  CB  VAL B 330     -38.825  10.168  -5.486  1.00 52.13           C  
ANISOU 5453  CB  VAL B 330     4688   8114   7006   -141    142   -287       C  
ATOM   5454  CG1 VAL B 330     -40.183  10.664  -4.996  1.00 52.98           C  
ANISOU 5454  CG1 VAL B 330     4670   8208   7251    -99    175   -260       C  
ATOM   5455  CG2 VAL B 330     -37.816  10.227  -4.349  1.00 50.55           C  
ANISOU 5455  CG2 VAL B 330     4637   7780   6790   -110    232   -307       C  
ATOM   5456  N   TRP B 331     -39.913   8.967  -8.359  1.00 53.40           N  
ANISOU 5456  N   TRP B 331     4626   8631   7032   -321    -78   -336       N  
ATOM   5457  CA  TRP B 331     -40.963   8.802  -9.373  1.00 54.81           C  
ANISOU 5457  CA  TRP B 331     4649   8978   7197   -384   -180   -327       C  
ATOM   5458  C   TRP B 331     -41.221   7.331  -9.620  1.00 60.90           C  
ANISOU 5458  C   TRP B 331     5406   9794   7940   -509   -156   -481       C  
ATOM   5459  O   TRP B 331     -42.343   6.975  -9.988  1.00 62.97           O  
ANISOU 5459  O   TRP B 331     5532  10155   8239   -568   -201   -505       O  
ATOM   5460  CB  TRP B 331     -40.651   9.529 -10.671  1.00 53.90           C  
ANISOU 5460  CB  TRP B 331     4496   9020   6963   -390   -314   -229       C  
ATOM   5461  CG  TRP B 331     -41.007  10.978 -10.626  1.00 55.60           C  
ANISOU 5461  CG  TRP B 331     4640   9223   7261   -280   -370    -53       C  
ATOM   5462  CD1 TRP B 331     -40.150  12.027 -10.460  1.00 57.88           C  
ANISOU 5462  CD1 TRP B 331     5007   9434   7548   -194   -368     49       C  
ATOM   5463  CD2 TRP B 331     -42.326  11.541 -10.689  1.00 56.99           C  
ANISOU 5463  CD2 TRP B 331     4644   9446   7563   -241   -427     38       C  
ATOM   5464  NE1 TRP B 331     -40.850  13.210 -10.441  1.00 58.37           N  
ANISOU 5464  NE1 TRP B 331     4959   9483   7735   -103   -419    199       N  
ATOM   5465  CE2 TRP B 331     -42.187  12.943 -10.589  1.00 61.04           C  
ANISOU 5465  CE2 TRP B 331     5137   9898   8156   -126   -458    199       C  
ATOM   5466  CE3 TRP B 331     -43.618  10.997 -10.840  1.00 59.74           C  
ANISOU 5466  CE3 TRP B 331     4841   9880   7977   -295   -457      1       C  
ATOM   5467  CZ2 TRP B 331     -43.284  13.810 -10.660  1.00 62.22           C  
ANISOU 5467  CZ2 TRP B 331     5118  10063   8462    -54   -517    328       C  
ATOM   5468  CZ3 TRP B 331     -44.705  11.856 -10.904  1.00 62.66           C  
ANISOU 5468  CZ3 TRP B 331     5040  10280   8489   -226   -520    128       C  
ATOM   5469  CH2 TRP B 331     -44.538  13.244 -10.804  1.00 63.57           C  
ANISOU 5469  CH2 TRP B 331     5136  10324   8695   -102   -548    292       C  
ATOM   5470  N   PHE B 332     -40.209   6.471  -9.350  1.00 56.44           N  
ANISOU 5470  N   PHE B 332     4973   9141   7332   -548    -80   -584       N  
ATOM   5471  CA  PHE B 332     -40.347   5.017  -9.419  1.00 56.55           C  
ANISOU 5471  CA  PHE B 332     4986   9144   7357   -660    -32   -739       C  
ATOM   5472  C   PHE B 332     -41.364   4.545  -8.333  1.00 61.39           C  
ANISOU 5472  C   PHE B 332     5550   9656   8120   -663     55   -760       C  
ATOM   5473  O   PHE B 332     -42.190   3.686  -8.630  1.00 62.79           O  
ANISOU 5473  O   PHE B 332     5638   9883   8335   -759     54   -849       O  
ATOM   5474  CB  PHE B 332     -38.979   4.313  -9.266  1.00 56.93           C  
ANISOU 5474  CB  PHE B 332     5178   9091   7360   -679     34   -822       C  
ATOM   5475  CG  PHE B 332     -39.086   2.898  -8.744  1.00 58.55           C  
ANISOU 5475  CG  PHE B 332     5407   9184   7656   -753    129   -948       C  
ATOM   5476  CD1 PHE B 332     -39.542   1.868  -9.565  1.00 63.22           C  
ANISOU 5476  CD1 PHE B 332     5926   9854   8242   -878    113  -1088       C  
ATOM   5477  CD2 PHE B 332     -38.798   2.606  -7.418  1.00 59.29           C  
ANISOU 5477  CD2 PHE B 332     5587   9096   7843   -706    231   -922       C  
ATOM   5478  CE1 PHE B 332     -39.677   0.568  -9.074  1.00 64.28           C  
ANISOU 5478  CE1 PHE B 332     6074   9861   8487   -948    205  -1198       C  
ATOM   5479  CE2 PHE B 332     -38.939   1.304  -6.926  1.00 62.78           C  
ANISOU 5479  CE2 PHE B 332     6044   9426   8382   -776    315  -1011       C  
ATOM   5480  CZ  PHE B 332     -39.377   0.295  -7.756  1.00 62.35           C  
ANISOU 5480  CZ  PHE B 332     5916   9428   8346   -893    304  -1148       C  
ATOM   5481  N   VAL B 333     -41.307   5.099  -7.093  1.00 56.74           N  
ANISOU 5481  N   VAL B 333     5017   8934   7608   -569    135   -685       N  
ATOM   5482  CA  VAL B 333     -42.265   4.739  -6.018  1.00 57.00           C  
ANISOU 5482  CA  VAL B 333     5005   8883   7769   -574    231   -697       C  
ATOM   5483  C   VAL B 333     -43.693   5.102  -6.467  1.00 62.58           C  
ANISOU 5483  C   VAL B 333     5528   9708   8544   -585    172   -671       C  
ATOM   5484  O   VAL B 333     -44.607   4.298  -6.315  1.00 63.02           O  
ANISOU 5484  O   VAL B 333     5498   9772   8675   -661    208   -736       O  
ATOM   5485  CB  VAL B 333     -41.921   5.384  -4.646  1.00 59.36           C  
ANISOU 5485  CB  VAL B 333     5398   9045   8109   -479    328   -629       C  
ATOM   5486  CG1 VAL B 333     -43.015   5.122  -3.616  1.00 59.45           C  
ANISOU 5486  CG1 VAL B 333     5348   9002   8237   -492    430   -638       C  
ATOM   5487  CG2 VAL B 333     -40.582   4.889  -4.132  1.00 57.99           C  
ANISOU 5487  CG2 VAL B 333     5393   8763   7879   -479    379   -648       C  
ATOM   5488  N   VAL B 334     -43.857   6.296  -7.065  1.00 60.78           N  
ANISOU 5488  N   VAL B 334     5230   9570   8293   -514     75   -567       N  
ATOM   5489  CA  VAL B 334     -45.122   6.808  -7.602  1.00 62.48           C  
ANISOU 5489  CA  VAL B 334     5255   9907   8578   -508     -8   -510       C  
ATOM   5490  C   VAL B 334     -45.648   5.804  -8.643  1.00 68.42           C  
ANISOU 5490  C   VAL B 334     5912  10808   9275   -645    -89   -602       C  
ATOM   5491  O   VAL B 334     -46.832   5.463  -8.600  1.00 68.65           O  
ANISOU 5491  O   VAL B 334     5797  10888   9398   -692    -93   -627       O  
ATOM   5492  CB  VAL B 334     -44.968   8.252  -8.175  1.00 66.43           C  
ANISOU 5492  CB  VAL B 334     5715  10466   9060   -406   -111   -361       C  
ATOM   5493  CG1 VAL B 334     -46.253   8.728  -8.855  1.00 68.37           C  
ANISOU 5493  CG1 VAL B 334     5747  10851   9379   -404   -223   -281       C  
ATOM   5494  CG2 VAL B 334     -44.548   9.235  -7.086  1.00 64.82           C  
ANISOU 5494  CG2 VAL B 334     5591  10103   8936   -281    -18   -296       C  
ATOM   5495  N   LEU B 335     -44.749   5.290  -9.523  1.00 65.90           N  
ANISOU 5495  N   LEU B 335     5674  10554   8810   -717   -139   -668       N  
ATOM   5496  CA  LEU B 335     -45.066   4.276 -10.533  1.00 67.98           C  
ANISOU 5496  CA  LEU B 335     5870  10958   9002   -864   -201   -790       C  
ATOM   5497  C   LEU B 335     -45.654   3.016  -9.882  1.00 72.58           C  
ANISOU 5497  C   LEU B 335     6434  11448   9696   -952    -96   -923       C  
ATOM   5498  O   LEU B 335     -46.701   2.541 -10.324  1.00 73.71           O  
ANISOU 5498  O   LEU B 335     6434  11698   9874  -1046   -142   -982       O  
ATOM   5499  CB  LEU B 335     -43.809   3.907 -11.315  1.00 68.10           C  
ANISOU 5499  CB  LEU B 335     6005  11014   8857   -915   -225   -862       C  
ATOM   5500  CG  LEU B 335     -43.973   3.637 -12.793  1.00 75.73           C  
ANISOU 5500  CG  LEU B 335     6887  12211   9676  -1035   -350   -922       C  
ATOM   5501  CD1 LEU B 335     -43.389   4.768 -13.579  1.00 77.24           C  
ANISOU 5501  CD1 LEU B 335     7100  12523   9726   -982   -455   -790       C  
ATOM   5502  CD2 LEU B 335     -43.190   2.418 -13.198  1.00 77.89           C  
ANISOU 5502  CD2 LEU B 335     7240  12468   9886  -1155   -292  -1120       C  
ATOM   5503  N   THR B 336     -44.995   2.498  -8.814  1.00 67.64           N  
ANISOU 5503  N   THR B 336     5945  10627   9130   -925     40   -958       N  
ATOM   5504  CA  THR B 336     -45.450   1.310  -8.072  1.00 67.24           C  
ANISOU 5504  CA  THR B 336     5892  10461   9195  -1004    152  -1056       C  
ATOM   5505  C   THR B 336     -46.777   1.601  -7.352  1.00 72.29           C  
ANISOU 5505  C   THR B 336     6403  11094   9969   -982    191  -1002       C  
ATOM   5506  O   THR B 336     -47.630   0.711  -7.276  1.00 72.31           O  
ANISOU 5506  O   THR B 336     6318  11097  10060  -1083    229  -1085       O  
ATOM   5507  CB  THR B 336     -44.381   0.795  -7.077  1.00 65.56           C  
ANISOU 5507  CB  THR B 336     5856  10049   9007   -974    273  -1069       C  
ATOM   5508  OG1 THR B 336     -44.174   1.740  -6.033  1.00 61.95           O  
ANISOU 5508  OG1 THR B 336     5463   9508   8569   -850    324   -945       O  
ATOM   5509  CG2 THR B 336     -43.069   0.464  -7.739  1.00 58.96           C  
ANISOU 5509  CG2 THR B 336     5130   9204   8067   -993    249  -1133       C  
ATOM   5510  N   TYR B 337     -46.944   2.843  -6.831  1.00 69.52           N  
ANISOU 5510  N   TYR B 337     6035  10733   9647   -855    191   -873       N  
ATOM   5511  CA  TYR B 337     -48.164   3.266  -6.145  1.00 71.02           C  
ANISOU 5511  CA  TYR B 337     6094  10916   9974   -819    239   -824       C  
ATOM   5512  C   TYR B 337     -49.332   3.333  -7.137  1.00 76.64           C  
ANISOU 5512  C   TYR B 337     6595  11806  10720   -876    120   -827       C  
ATOM   5513  O   TYR B 337     -50.426   2.864  -6.817  1.00 77.04           O  
ANISOU 5513  O   TYR B 337     6519  11865  10888   -933    164   -866       O  
ATOM   5514  CB  TYR B 337     -47.977   4.618  -5.431  1.00 72.46           C  
ANISOU 5514  CB  TYR B 337     6309  11036  10188   -669    274   -704       C  
ATOM   5515  CG  TYR B 337     -49.198   5.040  -4.638  1.00 76.72           C  
ANISOU 5515  CG  TYR B 337     6712  11554  10884   -630    351   -674       C  
ATOM   5516  CD1 TYR B 337     -50.190   5.830  -5.215  1.00 80.45           C  
ANISOU 5516  CD1 TYR B 337     6994  12136  11440   -583    260   -605       C  
ATOM   5517  CD2 TYR B 337     -49.381   4.617  -3.324  1.00 77.64           C  
ANISOU 5517  CD2 TYR B 337     6880  11549  11070   -645    515   -709       C  
ATOM   5518  CE1 TYR B 337     -51.334   6.189  -4.503  1.00 83.60           C  
ANISOU 5518  CE1 TYR B 337     7250  12511  12005   -546    340   -589       C  
ATOM   5519  CE2 TYR B 337     -50.516   4.978  -2.598  1.00 79.89           C  
ANISOU 5519  CE2 TYR B 337     7033  11824  11497   -619    602   -697       C  
ATOM   5520  CZ  TYR B 337     -51.489   5.768  -3.191  1.00 92.40           C  
ANISOU 5520  CZ  TYR B 337     8422  13506  13180   -565    519   -644       C  
ATOM   5521  OH  TYR B 337     -52.613   6.127  -2.481  1.00 98.93           O  
ANISOU 5521  OH  TYR B 337     9104  14318  14168   -534    615   -641       O  
ATOM   5522  N   ALA B 338     -49.087   3.910  -8.336  1.00 73.66           N  
ANISOU 5522  N   ALA B 338     6175  11579  10232   -866    -35   -778       N  
ATOM   5523  CA  ALA B 338     -50.067   4.036  -9.416  1.00 74.76           C  
ANISOU 5523  CA  ALA B 338     6118  11920  10369   -925   -182   -759       C  
ATOM   5524  C   ALA B 338     -50.533   2.675  -9.875  1.00 80.33           C  
ANISOU 5524  C   ALA B 338     6763  12693  11067  -1097   -186   -918       C  
ATOM   5525  O   ALA B 338     -51.720   2.515 -10.179  1.00 81.98           O  
ANISOU 5525  O   ALA B 338     6784  13010  11354  -1157   -240   -928       O  
ATOM   5526  CB  ALA B 338     -49.477   4.795 -10.581  1.00 75.30           C  
ANISOU 5526  CB  ALA B 338     6194  12136  10283   -902   -338   -674       C  
ATOM   5527  N   TRP B 339     -49.614   1.683  -9.899  1.00 75.61           N  
ANISOU 5527  N   TRP B 339     6315  12020  10395  -1176   -124  -1046       N  
ATOM   5528  CA  TRP B 339     -49.974   0.326 -10.279  1.00 76.51           C  
ANISOU 5528  CA  TRP B 339     6385  12161  10524  -1344   -107  -1218       C  
ATOM   5529  C   TRP B 339     -50.810  -0.351  -9.186  1.00 80.80           C  
ANISOU 5529  C   TRP B 339     6882  12567  11251  -1377     30  -1257       C  
ATOM   5530  O   TRP B 339     -51.754  -1.066  -9.513  1.00 81.72           O  
ANISOU 5530  O   TRP B 339     6863  12753  11432  -1501     13  -1350       O  
ATOM   5531  CB  TRP B 339     -48.750  -0.527 -10.627  1.00 74.45           C  
ANISOU 5531  CB  TRP B 339     6286  11840  10161  -1412    -70  -1347       C  
ATOM   5532  CG  TRP B 339     -49.161  -1.882 -11.125  1.00 76.71           C  
ANISOU 5532  CG  TRP B 339     6515  12153  10479  -1591    -55  -1540       C  
ATOM   5533  CD1 TRP B 339     -49.970  -2.146 -12.195  1.00 81.45           C  
ANISOU 5533  CD1 TRP B 339     6959  12962  11026  -1722   -170  -1626       C  
ATOM   5534  CD2 TRP B 339     -48.972  -3.129 -10.451  1.00 76.12           C  
ANISOU 5534  CD2 TRP B 339     6515  11883  10523  -1663     88  -1660       C  
ATOM   5535  NE1 TRP B 339     -50.217  -3.496 -12.281  1.00 81.48           N  
ANISOU 5535  NE1 TRP B 339     6946  12908  11104  -1876   -103  -1818       N  
ATOM   5536  CE2 TRP B 339     -49.619  -4.125 -11.221  1.00 81.61           C  
ANISOU 5536  CE2 TRP B 339     7101  12667  11238  -1839     58  -1836       C  
ATOM   5537  CE3 TRP B 339     -48.296  -3.510  -9.283  1.00 75.59           C  
ANISOU 5537  CE3 TRP B 339     6596  11577  10548  -1601    233  -1630       C  
ATOM   5538  CZ2 TRP B 339     -49.572  -5.478 -10.884  1.00 81.16           C  
ANISOU 5538  CZ2 TRP B 339     7081  12446  11309  -1949    176  -1986       C  
ATOM   5539  CZ3 TRP B 339     -48.250  -4.852  -8.954  1.00 77.55           C  
ANISOU 5539  CZ3 TRP B 339     6878  11673  10916  -1706    339  -1756       C  
ATOM   5540  CH2 TRP B 339     -48.891  -5.817  -9.743  1.00 80.02           C  
ANISOU 5540  CH2 TRP B 339     7081  12056  11268  -1875    316  -1933       C  
ATOM   5541  N   HIS B 340     -50.476  -0.103  -7.909  1.00 76.75           N  
ANISOU 5541  N   HIS B 340     6477  11874  10811  -1275    162  -1185       N  
ATOM   5542  CA  HIS B 340     -51.160  -0.636  -6.732  1.00 77.76           C  
ANISOU 5542  CA  HIS B 340     6582  11870  11095  -1297    309  -1195       C  
ATOM   5543  C   HIS B 340     -52.610  -0.073  -6.610  1.00 84.09           C  
ANISOU 5543  C   HIS B 340     7169  12768  12014  -1280    287  -1140       C  
ATOM   5544  O   HIS B 340     -53.503  -0.809  -6.178  1.00 84.39           O  
ANISOU 5544  O   HIS B 340     7113  12776  12177  -1367    365  -1197       O  
ATOM   5545  CB  HIS B 340     -50.305  -0.341  -5.477  1.00 77.54           C  
ANISOU 5545  CB  HIS B 340     6732  11660  11069  -1192    438  -1119       C  
ATOM   5546  CG  HIS B 340     -51.051  -0.052  -4.211  1.00 81.87           C  
ANISOU 5546  CG  HIS B 340     7241  12127  11739  -1151    569  -1061       C  
ATOM   5547  ND1 HIS B 340     -51.751  -1.040  -3.544  1.00 85.32           N  
ANISOU 5547  ND1 HIS B 340     7629  12498  12291  -1257    678  -1117       N  
ATOM   5548  CD2 HIS B 340     -51.124   1.094  -3.497  1.00 83.43           C  
ANISOU 5548  CD2 HIS B 340     7448  12296  11955  -1025    618   -960       C  
ATOM   5549  CE1 HIS B 340     -52.272  -0.454  -2.476  1.00 84.87           C  
ANISOU 5549  CE1 HIS B 340     7548  12394  12306  -1194    788  -1048       C  
ATOM   5550  NE2 HIS B 340     -51.916   0.828  -2.402  1.00 84.20           N  
ANISOU 5550  NE2 HIS B 340     7498  12326  12167  -1055    760   -962       N  
ATOM   5551  N   THR B 341     -52.837   1.203  -7.012  1.00 81.67           N  
ANISOU 5551  N   THR B 341     6777  12571  11684  -1171    182  -1026       N  
ATOM   5552  CA  THR B 341     -54.150   1.860  -6.948  1.00 83.37           C  
ANISOU 5552  CA  THR B 341     6774  12872  12030  -1131    150   -957       C  
ATOM   5553  C   THR B 341     -54.881   1.873  -8.312  1.00 91.37           C  
ANISOU 5553  C   THR B 341     7594  14109  13012  -1210    -38   -966       C  
ATOM   5554  O   THR B 341     -56.011   2.367  -8.375  1.00 93.28           O  
ANISOU 5554  O   THR B 341     7629  14439  13375  -1185    -86   -904       O  
ATOM   5555  CB  THR B 341     -54.046   3.289  -6.380  1.00 89.15           C  
ANISOU 5555  CB  THR B 341     7516  13555  12804   -951    169   -816       C  
ATOM   5556  OG1 THR B 341     -53.171   4.082  -7.182  1.00 88.30           O  
ANISOU 5556  OG1 THR B 341     7487  13506  12558   -883     44   -742       O  
ATOM   5557  CG2 THR B 341     -53.615   3.315  -4.924  1.00 86.08           C  
ANISOU 5557  CG2 THR B 341     7272  12974  12461   -890    363   -816       C  
ATOM   5558  N   SER B 342     -54.278   1.298  -9.382  1.00 88.85           N  
ANISOU 5558  N   SER B 342     7332  13890  12537  -1315   -140  -1049       N  
ATOM   5559  CA  SER B 342     -54.914   1.230 -10.708  1.00 91.08           C  
ANISOU 5559  CA  SER B 342     7443  14411  12750  -1418   -323  -1072       C  
ATOM   5560  C   SER B 342     -56.135   0.287 -10.701  1.00 99.15           C  
ANISOU 5560  C   SER B 342     8292  15484  13897  -1563   -305  -1184       C  
ATOM   5561  O   SER B 342     -56.978   0.370 -11.600  1.00100.47           O  
ANISOU 5561  O   SER B 342     8263  15857  14054  -1636   -455  -1178       O  
ATOM   5562  CB  SER B 342     -53.915   0.789 -11.779  1.00 93.21           C  
ANISOU 5562  CB  SER B 342     7834  14774  12810  -1508   -408  -1162       C  
ATOM   5563  OG  SER B 342     -53.448  -0.537 -11.596  1.00 97.78           O  
ANISOU 5563  OG  SER B 342     8528  15238  13385  -1628   -296  -1345       O  
ATOM   5564  N   PHE B 343     -56.223  -0.591  -9.676  1.00 97.10           N  
ANISOU 5564  N   PHE B 343     8100  15042  13754  -1609   -125  -1276       N  
ATOM   5565  CA  PHE B 343     -57.295  -1.571  -9.509  1.00 99.57           C  
ANISOU 5565  CA  PHE B 343     8268  15363  14202  -1752    -74  -1387       C  
ATOM   5566  C   PHE B 343     -58.504  -0.979  -8.761  1.00108.81           C  
ANISOU 5566  C   PHE B 343     9254  16529  15561  -1680    -24  -1290       C  
ATOM   5567  O   PHE B 343     -59.641  -1.194  -9.194  1.00110.64           O  
ANISOU 5567  O   PHE B 343     9265  16893  15880  -1769    -94  -1320       O  
ATOM   5568  CB  PHE B 343     -56.776  -2.821  -8.776  1.00100.08           C  
ANISOU 5568  CB  PHE B 343     8491  15223  14313  -1841     98  -1514       C  
ATOM   5569  CG  PHE B 343     -55.579  -3.497  -9.406  1.00100.20           C  
ANISOU 5569  CG  PHE B 343     8681  15206  14185  -1907     79  -1625       C  
ATOM   5570  CD1 PHE B 343     -55.723  -4.289 -10.539  1.00104.04           C  
ANISOU 5570  CD1 PHE B 343     9100  15824  14604  -2074    -17  -1784       C  
ATOM   5571  CD2 PHE B 343     -54.313  -3.364  -8.850  1.00 99.57           C  
ANISOU 5571  CD2 PHE B 343     8824  14965  14042  -1807    161  -1582       C  
ATOM   5572  CE1 PHE B 343     -54.618  -4.916 -11.118  1.00104.05           C  
ANISOU 5572  CE1 PHE B 343     9256  15792  14487  -2136    -17  -1907       C  
ATOM   5573  CE2 PHE B 343     -53.212  -4.006  -9.420  1.00101.40           C  
ANISOU 5573  CE2 PHE B 343     9203  15161  14165  -1864    153  -1690       C  
ATOM   5574  CZ  PHE B 343     -53.371  -4.774 -10.552  1.00100.83           C  
ANISOU 5574  CZ  PHE B 343     9061  15214  14036  -2025     70  -1857       C  
ATOM   5575  N   LYS B 344     -58.261  -0.244  -7.641  1.00106.68           N  
ANISOU 5575  N   LYS B 344     9069  16110  15356  -1525    102  -1184       N  
ATOM   5576  CA  LYS B 344     -59.308   0.389  -6.821  1.00108.13           C  
ANISOU 5576  CA  LYS B 344     9094  16267  15723  -1442    185  -1105       C  
ATOM   5577  C   LYS B 344     -60.132   1.364  -7.659  1.00115.90           C  
ANISOU 5577  C   LYS B 344     9844  17435  16757  -1378     11  -1000       C  
ATOM   5578  O   LYS B 344     -61.359   1.403  -7.533  1.00117.59           O  
ANISOU 5578  O   LYS B 344     9834  17705  17142  -1393     21   -988       O  
ATOM   5579  CB  LYS B 344     -58.699   1.112  -5.609  1.00108.88           C  
ANISOU 5579  CB  LYS B 344     9349  16186  15837  -1292    340  -1028       C  
ATOM   5580  N   ALA B 345     -59.449   2.112  -8.545  1.00113.38           N  
ANISOU 5580  N   ALA B 345     9568  17215  16295  -1312   -152   -916       N  
ATOM   5581  CA  ALA B 345     -60.047   3.079  -9.457  1.00115.26           C  
ANISOU 5581  CA  ALA B 345     9600  17634  16558  -1249   -344   -782       C  
ATOM   5582  C   ALA B 345     -60.884   2.364 -10.530  1.00121.21           C  
ANISOU 5582  C   ALA B 345    10160  18609  17284  -1421   -504   -851       C  
ATOM   5583  O   ALA B 345     -62.113   2.483 -10.517  1.00123.03           O  
ANISOU 5583  O   ALA B 345    10144  18923  17680  -1434   -540   -819       O  
ATOM   5584  CB  ALA B 345     -58.955   3.934 -10.099  1.00115.05           C  
ANISOU 5584  CB  ALA B 345     9704  17642  16369  -1148   -460   -669       C  
ATOM   5585  N   LEU B 346     -60.230   1.593 -11.422  1.00116.96           N  
ANISOU 5585  N   LEU B 346     9729  18165  16543  -1558   -589   -958       N  
ATOM   5586  CA  LEU B 346     -60.901   0.865 -12.496  1.00141.70           C  
ANISOU 5586  CA  LEU B 346    12704  21522  19614  -1745   -741  -1053       C  
ATOM   5587  C   LEU B 346     -61.046  -0.609 -12.149  1.00139.51           C  
ANISOU 5587  C   LEU B 346    12474  21157  19377  -1920   -609  -1271       C  
ATOM   5588  O   LEU B 346     -62.161  -1.112 -12.084  1.00 94.90           O  
ANISOU 5588  O   LEU B 346     6630  15563  13864  -2021   -605  -1331       O  
ATOM   5589  CB  LEU B 346     -60.126   1.028 -13.807  1.00141.93           C  
ANISOU 5589  CB  LEU B 346    12805  21739  19385  -1797   -925  -1042       C  
ATOM   5590  N   GLY B 355     -57.215  15.608 -15.548  1.00136.02           N  
ANISOU 5590  N   GLY B 355    11828  20715  19140    -42  -1779   1408       N  
ATOM   5591  CA  GLY B 355     -57.610  14.878 -14.352  1.00134.66           C  
ANISOU 5591  CA  GLY B 355    11682  20375  19110    -37  -1554   1175       C  
ATOM   5592  C   GLY B 355     -56.439  14.378 -13.533  1.00135.83           C  
ANISOU 5592  C   GLY B 355    12135  20353  19120    -58  -1349    972       C  
ATOM   5593  O   GLY B 355     -55.403  14.002 -14.092  1.00134.11           O  
ANISOU 5593  O   GLY B 355    12107  20219  18630   -149  -1391    932       O  
ATOM   5594  N   LYS B 356     -56.604  14.395 -12.187  1.00131.59           N  
ANISOU 5594  N   LYS B 356    11639  19582  18775     26  -1123    845       N  
ATOM   5595  CA  LYS B 356     -55.654  13.955 -11.148  1.00128.84           C  
ANISOU 5595  CA  LYS B 356    11556  19051  18348     20   -906    657       C  
ATOM   5596  C   LYS B 356     -54.288  14.710 -11.178  1.00131.55           C  
ANISOU 5596  C   LYS B 356    12112  19286  18586     96   -893    729       C  
ATOM   5597  O   LYS B 356     -53.368  14.328 -10.442  1.00128.84           O  
ANISOU 5597  O   LYS B 356    11994  18812  18149     84   -739    589       O  
ATOM   5598  CB  LYS B 356     -55.426  12.430 -11.214  1.00130.24           C  
ANISOU 5598  CB  LYS B 356    11852  19325  18310   -163   -869    452       C  
ATOM   5599  N   THR B 357     -54.171  15.790 -11.987  1.00129.67           N  
ANISOU 5599  N   THR B 357    11794  19097  18377    174  -1051    956       N  
ATOM   5600  CA  THR B 357     -52.946  16.592 -12.075  1.00128.41           C  
ANISOU 5600  CA  THR B 357    11811  18838  18140    244  -1049   1045       C  
ATOM   5601  C   THR B 357     -53.088  17.776 -11.092  1.00131.90           C  
ANISOU 5601  C   THR B 357    12215  19024  18879    426   -918   1099       C  
ATOM   5602  O   THR B 357     -53.659  18.820 -11.431  1.00133.68           O  
ANISOU 5602  O   THR B 357    12256  19224  19312    536  -1011   1297       O  
ATOM   5603  CB  THR B 357     -52.637  17.004 -13.538  1.00137.85           C  
ANISOU 5603  CB  THR B 357    12962  20240  19174    203  -1286   1258       C  
ATOM   5604  OG1 THR B 357     -52.659  15.844 -14.376  1.00137.47           O  
ANISOU 5604  OG1 THR B 357    12927  20439  18867     22  -1388   1169       O  
ATOM   5605  CG2 THR B 357     -51.285  17.707 -13.681  1.00134.28           C  
ANISOU 5605  CG2 THR B 357    12708  19702  18610    249  -1278   1337       C  
ATOM   5606  N   SER B 358     -52.599  17.567  -9.855  1.00125.43           N  
ANISOU 5606  N   SER B 358    11560  18015  18082    449   -699    915       N  
ATOM   5607  CA  SER B 358     -52.622  18.536  -8.757  1.00124.39           C  
ANISOU 5607  CA  SER B 358    11428  17637  18197    594   -534    898       C  
ATOM   5608  C   SER B 358     -51.185  18.766  -8.248  1.00124.00           C  
ANISOU 5608  C   SER B 358    11649  17453  18013    606   -432    831       C  
ATOM   5609  O   SER B 358     -50.248  18.703  -9.053  1.00123.09           O  
ANISOU 5609  O   SER B 358    11656  17425  17688    555   -544    902       O  
ATOM   5610  CB  SER B 358     -53.546  18.047  -7.642  1.00128.13           C  
ANISOU 5610  CB  SER B 358    11821  18034  18827    594   -354    726       C  
ATOM   5611  OG  SER B 358     -54.895  17.978  -8.077  1.00139.18           O  
ANISOU 5611  OG  SER B 358    12950  19547  20385    594   -446    796       O  
ATOM   5612  N   TYR B 359     -50.999  19.022  -6.931  1.00117.25           N  
ANISOU 5612  N   TYR B 359    10883  16399  17269    665   -221    691       N  
ATOM   5613  CA  TYR B 359     -49.674  19.246  -6.344  1.00113.61           C  
ANISOU 5613  CA  TYR B 359    10666  15811  16688    672   -121    618       C  
ATOM   5614  C   TYR B 359     -48.983  17.907  -6.005  1.00111.68           C  
ANISOU 5614  C   TYR B 359    10621  15632  16182    538    -58    450       C  
ATOM   5615  O   TYR B 359     -48.364  17.783  -4.946  1.00109.88           O  
ANISOU 5615  O   TYR B 359    10551  15283  15914    534    100    316       O  
ATOM   5616  CB  TYR B 359     -49.758  20.158  -5.102  1.00114.98           C  
ANISOU 5616  CB  TYR B 359    10844  15758  17087    783     69    541       C  
ATOM   5617  CG  TYR B 359     -49.950  21.626  -5.414  1.00118.15           C  
ANISOU 5617  CG  TYR B 359    11114  16039  17739    923     18    708       C  
ATOM   5618  CD1 TYR B 359     -51.210  22.214  -5.349  1.00122.29           C  
ANISOU 5618  CD1 TYR B 359    11386  16512  18567   1018     28    768       C  
ATOM   5619  CD2 TYR B 359     -48.868  22.437  -5.748  1.00118.36           C  
ANISOU 5619  CD2 TYR B 359    11261  15990  17721    962    -33    806       C  
ATOM   5620  CE1 TYR B 359     -51.394  23.568  -5.624  1.00124.65           C  
ANISOU 5620  CE1 TYR B 359    11554  16677  19131   1154    -16    931       C  
ATOM   5621  CE2 TYR B 359     -49.038  23.793  -6.026  1.00121.02           C  
ANISOU 5621  CE2 TYR B 359    11475  16195  18311   1090    -76    970       C  
ATOM   5622  CZ  TYR B 359     -50.305  24.355  -5.961  1.00131.18           C  
ANISOU 5622  CZ  TYR B 359    12509  17421  19912   1189    -68   1034       C  
ATOM   5623  OH  TYR B 359     -50.488  25.691  -6.233  1.00134.47           O  
ANISOU 5623  OH  TYR B 359    12793  17688  20612   1321   -109   1205       O  
ATOM   5624  N   PHE B 360     -49.067  16.919  -6.929  1.00105.58           N  
ANISOU 5624  N   PHE B 360     9834  15050  15232    425   -186    460       N  
ATOM   5625  CA  PHE B 360     -48.428  15.597  -6.826  1.00102.51           C  
ANISOU 5625  CA  PHE B 360     9611  14726  14613    295   -150    317       C  
ATOM   5626  C   PHE B 360     -46.901  15.752  -6.848  1.00101.45           C  
ANISOU 5626  C   PHE B 360     9700  14539  14307    290   -145    314       C  
ATOM   5627  O   PHE B 360     -46.167  14.941  -6.279  1.00 98.53           O  
ANISOU 5627  O   PHE B 360     9499  14132  13806    226    -54    186       O  
ATOM   5628  CB  PHE B 360     -48.881  14.700  -7.993  1.00104.99           C  
ANISOU 5628  CB  PHE B 360     9832  15257  14803    180   -303    336       C  
ATOM   5629  CG  PHE B 360     -49.088  13.244  -7.648  1.00105.95           C  
ANISOU 5629  CG  PHE B 360     9999  15423  14833     55   -230    164       C  
ATOM   5630  CD1 PHE B 360     -50.352  12.669  -7.719  1.00110.53           C  
ANISOU 5630  CD1 PHE B 360    10400  16087  15508      2   -242    127       C  
ATOM   5631  CD2 PHE B 360     -48.018  12.441  -7.267  1.00105.89           C  
ANISOU 5631  CD2 PHE B 360    10205  15368  14660    -13   -152     46       C  
ATOM   5632  CE1 PHE B 360     -50.543  11.318  -7.409  1.00110.91           C  
ANISOU 5632  CE1 PHE B 360    10489  16163  15487   -121   -171    -27       C  
ATOM   5633  CE2 PHE B 360     -48.214  11.097  -6.938  1.00108.43           C  
ANISOU 5633  CE2 PHE B 360    10563  15710  14925   -127    -83    -98       C  
ATOM   5634  CZ  PHE B 360     -49.473  10.542  -7.019  1.00107.96           C  
ANISOU 5634  CZ  PHE B 360    10331  15727  14961   -183    -91   -135       C  
ATOM   5635  N   HIS B 361     -46.453  16.823  -7.519  1.00 96.87           N  
ANISOU 5635  N   HIS B 361     9107  13953  13745    360   -246    470       N  
ATOM   5636  CA  HIS B 361     -45.083  17.260  -7.712  1.00 95.09           C  
ANISOU 5636  CA  HIS B 361     9054  13683  13394    370   -262    507       C  
ATOM   5637  C   HIS B 361     -44.392  17.578  -6.386  1.00 96.55           C  
ANISOU 5637  C   HIS B 361     9390  13672  13623    419    -89    400       C  
ATOM   5638  O   HIS B 361     -43.196  17.325  -6.241  1.00 94.44           O  
ANISOU 5638  O   HIS B 361     9303  13381  13201    381    -62    348       O  
ATOM   5639  CB  HIS B 361     -45.092  18.493  -8.619  1.00 97.29           C  
ANISOU 5639  CB  HIS B 361     9236  13978  13754    448   -395    722       C  
ATOM   5640  CG  HIS B 361     -45.297  18.160 -10.061  1.00101.76           C  
ANISOU 5640  CG  HIS B 361     9715  14770  14179    371   -586    841       C  
ATOM   5641  ND1 HIS B 361     -44.283  18.323 -10.985  1.00103.30           N  
ANISOU 5641  ND1 HIS B 361    10004  15055  14189    327   -686    931       N  
ATOM   5642  CD2 HIS B 361     -46.385  17.656 -10.687  1.00104.99           C  
ANISOU 5642  CD2 HIS B 361     9951  15342  14598    319   -688    873       C  
ATOM   5643  CE1 HIS B 361     -44.787  17.931 -12.141  1.00104.07           C  
ANISOU 5643  CE1 HIS B 361     9989  15375  14178    248   -842   1013       C  
ATOM   5644  NE2 HIS B 361     -46.048  17.516 -12.011  1.00105.48           N  
ANISOU 5644  NE2 HIS B 361    10005  15606  14467    239   -855    981       N  
ATOM   5645  N   LEU B 362     -45.147  18.109  -5.411  1.00 92.63           N  
ANISOU 5645  N   LEU B 362     8815  13047  13335    496     31    358       N  
ATOM   5646  CA  LEU B 362     -44.631  18.430  -4.084  1.00 90.92           C  
ANISOU 5646  CA  LEU B 362     8724  12662  13158    531    203    240       C  
ATOM   5647  C   LEU B 362     -44.147  17.172  -3.371  1.00 88.99           C  
ANISOU 5647  C   LEU B 362     8633  12440  12738    429    295     87       C  
ATOM   5648  O   LEU B 362     -43.154  17.216  -2.658  1.00 86.76           O  
ANISOU 5648  O   LEU B 362     8517  12075  12375    421    376     19       O  
ATOM   5649  CB  LEU B 362     -45.716  19.117  -3.248  1.00 92.95           C  
ANISOU 5649  CB  LEU B 362     8838  12807  13672    616    321    205       C  
ATOM   5650  CG  LEU B 362     -45.206  20.200  -2.318  1.00 98.59           C  
ANISOU 5650  CG  LEU B 362     9626  13336  14498    694    448    156       C  
ATOM   5651  CD1 LEU B 362     -45.421  21.578  -2.929  1.00100.68           C  
ANISOU 5651  CD1 LEU B 362     9763  13514  14978    810    376    310       C  
ATOM   5652  CD2 LEU B 362     -45.863  20.091  -0.954  1.00102.19           C  
ANISOU 5652  CD2 LEU B 362    10064  13711  15054    695    647     -9       C  
ATOM   5653  N   LEU B 363     -44.847  16.052  -3.583  1.00 83.43           N  
ANISOU 5653  N   LEU B 363     7868  11847  11985    349    276     40       N  
ATOM   5654  CA  LEU B 363     -44.520  14.756  -2.989  1.00 80.65           C  
ANISOU 5654  CA  LEU B 363     7638  11512  11494    248    354    -86       C  
ATOM   5655  C   LEU B 363     -43.288  14.114  -3.638  1.00 77.00           C  
ANISOU 5655  C   LEU B 363     7324  11108  10826    180    273    -84       C  
ATOM   5656  O   LEU B 363     -42.656  13.266  -3.015  1.00 74.92           O  
ANISOU 5656  O   LEU B 363     7192  10815  10458    118    344   -173       O  
ATOM   5657  CB  LEU B 363     -45.719  13.793  -3.126  1.00 81.87           C  
ANISOU 5657  CB  LEU B 363     7658  11757  11690    179    357   -132       C  
ATOM   5658  CG  LEU B 363     -46.969  14.119  -2.313  1.00 88.47           C  
ANISOU 5658  CG  LEU B 363     8352  12541  12721    221    473   -171       C  
ATOM   5659  CD1 LEU B 363     -48.050  14.693  -3.201  1.00 90.67           C  
ANISOU 5659  CD1 LEU B 363     8402  12888  13159    276    366    -68       C  
ATOM   5660  CD2 LEU B 363     -47.507  12.875  -1.631  1.00 91.51           C  
ANISOU 5660  CD2 LEU B 363     8743  12950  13076    121    573   -282       C  
ATOM   5661  N   THR B 364     -42.966  14.494  -4.891  1.00 69.78           N  
ANISOU 5661  N   THR B 364     6376  10279   9856    190    127     22       N  
ATOM   5662  CA  THR B 364     -41.888  13.891  -5.670  1.00 66.62           C  
ANISOU 5662  CA  THR B 364     6089   9957   9267    120     50     18       C  
ATOM   5663  C   THR B 364     -40.590  14.698  -5.711  1.00 65.96           C  
ANISOU 5663  C   THR B 364     6133   9806   9122    167     37     72       C  
ATOM   5664  O   THR B 364     -39.523  14.100  -5.621  1.00 64.69           O  
ANISOU 5664  O   THR B 364     6111   9638   8829    118     56     14       O  
ATOM   5665  CB  THR B 364     -42.344  13.649  -7.103  1.00 72.47           C  
ANISOU 5665  CB  THR B 364     6712  10876   9948     68   -103     85       C  
ATOM   5666  OG1 THR B 364     -42.550  14.908  -7.747  1.00 68.75           O  
ANISOU 5666  OG1 THR B 364     6142  10426   9554    147   -199    244       O  
ATOM   5667  CG2 THR B 364     -43.608  12.809  -7.182  1.00 73.37           C  
ANISOU 5667  CG2 THR B 364     6691  11072  10114      5   -106     25       C  
ATOM   5668  N   TRP B 365     -40.666  16.022  -5.888  1.00 60.09           N  
ANISOU 5668  N   TRP B 365     5333   9013   8487    258      4    187       N  
ATOM   5669  CA  TRP B 365     -39.482  16.871  -6.042  1.00 57.46           C  
ANISOU 5669  CA  TRP B 365     5104   8618   8110    297    -17    252       C  
ATOM   5670  C   TRP B 365     -38.874  17.356  -4.696  1.00 59.49           C  
ANISOU 5670  C   TRP B 365     5476   8704   8423    343    119    176       C  
ATOM   5671  O   TRP B 365     -37.751  17.861  -4.709  1.00 57.93           O  
ANISOU 5671  O   TRP B 365     5385   8455   8171    356    113    201       O  
ATOM   5672  CB  TRP B 365     -39.815  18.079  -6.944  1.00 56.20           C  
ANISOU 5672  CB  TRP B 365     4824   8482   8047    364   -127    429       C  
ATOM   5673  CG  TRP B 365     -40.414  17.707  -8.274  1.00 57.42           C  
ANISOU 5673  CG  TRP B 365     4859   8829   8131    311   -274    520       C  
ATOM   5674  CD1 TRP B 365     -41.704  17.899  -8.671  1.00 61.77           C  
ANISOU 5674  CD1 TRP B 365     5223   9445   8802    336   -341    601       C  
ATOM   5675  CD2 TRP B 365     -39.760  17.030  -9.357  1.00 56.53           C  
ANISOU 5675  CD2 TRP B 365     4797   8879   7803    214   -369    529       C  
ATOM   5676  NE1 TRP B 365     -41.895  17.395  -9.934  1.00 61.66           N  
ANISOU 5676  NE1 TRP B 365     5144   9637   8648    253   -483    664       N  
ATOM   5677  CE2 TRP B 365     -40.711  16.877 -10.391  1.00 61.94           C  
ANISOU 5677  CE2 TRP B 365     5325   9738   8473    176   -497    615       C  
ATOM   5678  CE3 TRP B 365     -38.443  16.605  -9.587  1.00 56.16           C  
ANISOU 5678  CE3 TRP B 365     4904   8854   7582    155   -358    473       C  
ATOM   5679  CZ2 TRP B 365     -40.392  16.298 -11.623  1.00 61.51           C  
ANISOU 5679  CZ2 TRP B 365     5272   9884   8213     70   -608    633       C  
ATOM   5680  CZ3 TRP B 365     -38.130  16.035 -10.811  1.00 57.68           C  
ANISOU 5680  CZ3 TRP B 365     5092   9233   7591     60   -457    487       C  
ATOM   5681  CH2 TRP B 365     -39.097  15.877 -11.808  1.00 59.61           C  
ANISOU 5681  CH2 TRP B 365     5188   9655   7804     12   -578    559       C  
ATOM   5682  N   SER B 366     -39.583  17.175  -3.556  1.00 55.30           N  
ANISOU 5682  N   SER B 366     4926   8100   7987    355    241     79       N  
ATOM   5683  CA  SER B 366     -39.138  17.642  -2.234  1.00 54.07           C  
ANISOU 5683  CA  SER B 366     4869   7806   7870    384    374     -5       C  
ATOM   5684  C   SER B 366     -37.986  16.858  -1.617  1.00 56.20           C  
ANISOU 5684  C   SER B 366     5316   8067   7971    316    419    -89       C  
ATOM   5685  O   SER B 366     -37.045  17.470  -1.110  1.00 55.27           O  
ANISOU 5685  O   SER B 366     5301   7869   7829    334    453   -102       O  
ATOM   5686  CB  SER B 366     -40.297  17.615  -1.251  1.00 58.21           C  
ANISOU 5686  CB  SER B 366     5308   8280   8528    403    496    -86       C  
ATOM   5687  OG  SER B 366     -41.171  18.688  -1.547  1.00 73.81           O  
ANISOU 5687  OG  SER B 366     7126  10214  10706    492    478    -11       O  
ATOM   5688  N   LEU B 367     -38.105  15.521  -1.573  1.00 52.27           N  
ANISOU 5688  N   LEU B 367     4843   7640   7376    238    425   -146       N  
ATOM   5689  CA  LEU B 367     -37.132  14.632  -0.958  1.00 51.24           C  
ANISOU 5689  CA  LEU B 367     4860   7498   7113    174    465   -211       C  
ATOM   5690  C   LEU B 367     -35.749  14.774  -1.650  1.00 53.32           C  
ANISOU 5690  C   LEU B 367     5217   7773   7270    170    383   -166       C  
ATOM   5691  O   LEU B 367     -34.787  15.003  -0.915  1.00 52.27           O  
ANISOU 5691  O   LEU B 367     5198   7573   7089    171    425   -191       O  
ATOM   5692  CB  LEU B 367     -37.645  13.180  -0.963  1.00 51.75           C  
ANISOU 5692  CB  LEU B 367     4906   7625   7132     95    476   -263       C  
ATOM   5693  CG  LEU B 367     -36.969  12.189  -0.019  1.00 56.57           C  
ANISOU 5693  CG  LEU B 367     5642   8197   7653     33    546   -323       C  
ATOM   5694  CD1 LEU B 367     -38.008  11.249   0.587  1.00 57.58           C  
ANISOU 5694  CD1 LEU B 367     5721   8336   7822    -21    624   -375       C  
ATOM   5695  CD2 LEU B 367     -35.895  11.375  -0.755  1.00 58.83           C  
ANISOU 5695  CD2 LEU B 367     6000   8515   7836    -11    472   -319       C  
ATOM   5696  N   PRO B 368     -35.607  14.727  -3.011  1.00 49.37           N  
ANISOU 5696  N   PRO B 368     4667   7362   6728    162    270   -100       N  
ATOM   5697  CA  PRO B 368     -34.271  14.929  -3.612  1.00 48.29           C  
ANISOU 5697  CA  PRO B 368     4617   7238   6493    154    211    -63       C  
ATOM   5698  C   PRO B 368     -33.727  16.335  -3.357  1.00 52.62           C  
ANISOU 5698  C   PRO B 368     5196   7698   7099    220    218     -4       C  
ATOM   5699  O   PRO B 368     -32.514  16.489  -3.285  1.00 51.08           O  
ANISOU 5699  O   PRO B 368     5100   7474   6835    211    213     -5       O  
ATOM   5700  CB  PRO B 368     -34.510  14.710  -5.113  1.00 50.20           C  
ANISOU 5700  CB  PRO B 368     4776   7615   6682    123    100     -4       C  
ATOM   5701  CG  PRO B 368     -35.810  13.992  -5.202  1.00 54.46           C  
ANISOU 5701  CG  PRO B 368     5210   8216   7267     93    102    -41       C  
ATOM   5702  CD  PRO B 368     -36.618  14.471  -4.062  1.00 50.79           C  
ANISOU 5702  CD  PRO B 368     4711   7653   6935    146    192    -58       C  
ATOM   5703  N   PHE B 369     -34.615  17.343  -3.181  1.00 50.53           N  
ANISOU 5703  N   PHE B 369     4840   7381   6979    286    236     39       N  
ATOM   5704  CA  PHE B 369     -34.212  18.729  -2.927  1.00 51.19           C  
ANISOU 5704  CA  PHE B 369     4938   7356   7156    350    254     86       C  
ATOM   5705  C   PHE B 369     -33.517  18.869  -1.570  1.00 53.10           C  
ANISOU 5705  C   PHE B 369     5299   7496   7382    342    360    -17       C  
ATOM   5706  O   PHE B 369     -32.424  19.412  -1.507  1.00 52.76           O  
ANISOU 5706  O   PHE B 369     5339   7405   7304    343    351     -5       O  
ATOM   5707  CB  PHE B 369     -35.423  19.683  -3.012  1.00 55.09           C  
ANISOU 5707  CB  PHE B 369     5288   7800   7841    426    259    146       C  
ATOM   5708  CG  PHE B 369     -35.046  21.147  -3.043  1.00 58.17           C  
ANISOU 5708  CG  PHE B 369     5671   8073   8359    495    259    219       C  
ATOM   5709  CD1 PHE B 369     -35.059  21.911  -1.881  1.00 62.11           C  
ANISOU 5709  CD1 PHE B 369     6196   8426   8976    533    376    133       C  
ATOM   5710  CD2 PHE B 369     -34.646  21.755  -4.229  1.00 61.06           C  
ANISOU 5710  CD2 PHE B 369     6004   8475   8723    510    146    370       C  
ATOM   5711  CE1 PHE B 369     -34.678  23.258  -1.905  1.00 63.53           C  
ANISOU 5711  CE1 PHE B 369     6368   8479   9294    591    383    188       C  
ATOM   5712  CE2 PHE B 369     -34.273  23.100  -4.251  1.00 64.50           C  
ANISOU 5712  CE2 PHE B 369     6431   8785   9293    570    149    448       C  
ATOM   5713  CZ  PHE B 369     -34.292  23.842  -3.089  1.00 62.78           C  
ANISOU 5713  CZ  PHE B 369     6237   8403   9214    612    269    352       C  
ATOM   5714  N   VAL B 370     -34.135  18.351  -0.509  1.00 48.89           N  
ANISOU 5714  N   VAL B 370     4771   6943   6861    323    456   -115       N  
ATOM   5715  CA  VAL B 370     -33.652  18.413   0.870  1.00 48.16           C  
ANISOU 5715  CA  VAL B 370     4783   6782   6734    299    559   -215       C  
ATOM   5716  C   VAL B 370     -32.308  17.679   0.978  1.00 50.79           C  
ANISOU 5716  C   VAL B 370     5245   7147   6906    241    524   -225       C  
ATOM   5717  O   VAL B 370     -31.357  18.237   1.528  1.00 50.48           O  
ANISOU 5717  O   VAL B 370     5291   7053   6835    236    543   -248       O  
ATOM   5718  CB  VAL B 370     -34.729  17.867   1.864  1.00 52.95           C  
ANISOU 5718  CB  VAL B 370     5355   7394   7368    276    667   -303       C  
ATOM   5719  CG1 VAL B 370     -34.226  17.882   3.297  1.00 53.61           C  
ANISOU 5719  CG1 VAL B 370     5550   7437   7380    232    770   -400       C  
ATOM   5720  CG2 VAL B 370     -36.021  18.672   1.773  1.00 53.46           C  
ANISOU 5720  CG2 VAL B 370     5277   7417   7618    342    710   -299       C  
ATOM   5721  N   LEU B 371     -32.215  16.464   0.401  1.00 46.68           N  
ANISOU 5721  N   LEU B 371     4728   6710   6299    197    471   -209       N  
ATOM   5722  CA  LEU B 371     -31.002  15.655   0.397  1.00 44.80           C  
ANISOU 5722  CA  LEU B 371     4588   6495   5939    148    437   -215       C  
ATOM   5723  C   LEU B 371     -29.854  16.364  -0.365  1.00 49.24           C  
ANISOU 5723  C   LEU B 371     5184   7052   6475    167    367   -158       C  
ATOM   5724  O   LEU B 371     -28.741  16.441   0.157  1.00 49.97           O  
ANISOU 5724  O   LEU B 371     5366   7112   6509    148    372   -174       O  
ATOM   5725  CB  LEU B 371     -31.270  14.267  -0.198  1.00 44.24           C  
ANISOU 5725  CB  LEU B 371     4491   6498   5820    102    404   -221       C  
ATOM   5726  CG  LEU B 371     -32.164  13.272   0.592  1.00 47.77           C  
ANISOU 5726  CG  LEU B 371     4924   6950   6277     61    474   -273       C  
ATOM   5727  CD1 LEU B 371     -32.194  11.915  -0.110  1.00 46.10           C  
ANISOU 5727  CD1 LEU B 371     4691   6792   6031     10    435   -284       C  
ATOM   5728  CD2 LEU B 371     -31.664  13.073   2.031  1.00 49.55           C  
ANISOU 5728  CD2 LEU B 371     5250   7126   6452     32    547   -308       C  
ATOM   5729  N   THR B 372     -30.132  16.910  -1.565  1.00 44.62           N  
ANISOU 5729  N   THR B 372     4520   6502   5930    198    300    -83       N  
ATOM   5730  CA  THR B 372     -29.147  17.643  -2.380  1.00 43.93           C  
ANISOU 5730  CA  THR B 372     4454   6417   5820    209    237    -12       C  
ATOM   5731  C   THR B 372     -28.597  18.833  -1.584  1.00 45.82           C  
ANISOU 5731  C   THR B 372     4744   6545   6121    239    281    -20       C  
ATOM   5732  O   THR B 372     -27.378  18.973  -1.481  1.00 43.27           O  
ANISOU 5732  O   THR B 372     4497   6204   5741    217    268    -22       O  
ATOM   5733  CB  THR B 372     -29.775  18.093  -3.721  1.00 45.97           C  
ANISOU 5733  CB  THR B 372     4607   6745   6112    231    159     90       C  
ATOM   5734  OG1 THR B 372     -30.262  16.938  -4.394  1.00 47.13           O  
ANISOU 5734  OG1 THR B 372     4712   7006   6190    186    123     70       O  
ATOM   5735  CG2 THR B 372     -28.799  18.793  -4.616  1.00 40.75           C  
ANISOU 5735  CG2 THR B 372     3965   6103   5416    230     97    178       C  
ATOM   5736  N   VAL B 373     -29.512  19.649  -0.997  1.00 42.78           N  
ANISOU 5736  N   VAL B 373     4311   6084   5861    283    339    -37       N  
ATOM   5737  CA  VAL B 373     -29.203  20.814  -0.164  1.00 42.84           C  
ANISOU 5737  CA  VAL B 373     4352   5973   5952    308    400    -74       C  
ATOM   5738  C   VAL B 373     -28.350  20.382   1.054  1.00 46.30           C  
ANISOU 5738  C   VAL B 373     4907   6399   6287    252    453   -176       C  
ATOM   5739  O   VAL B 373     -27.384  21.078   1.374  1.00 46.06           O  
ANISOU 5739  O   VAL B 373     4936   6312   6251    240    457   -191       O  
ATOM   5740  CB  VAL B 373     -30.487  21.599   0.249  1.00 47.45           C  
ANISOU 5740  CB  VAL B 373     4844   6478   6706    365    470    -97       C  
ATOM   5741  CG1 VAL B 373     -30.173  22.710   1.242  1.00 47.54           C  
ANISOU 5741  CG1 VAL B 373     4895   6360   6806    377    556   -177       C  
ATOM   5742  CG2 VAL B 373     -31.170  22.200  -0.978  1.00 48.28           C  
ANISOU 5742  CG2 VAL B 373     4828   6589   6928    424    396     35       C  
ATOM   5743  N   ALA B 374     -28.656  19.208   1.667  1.00 43.26           N  
ANISOU 5743  N   ALA B 374     4549   6072   5817    211    484   -230       N  
ATOM   5744  CA  ALA B 374     -27.939  18.675   2.828  1.00 43.01           C  
ANISOU 5744  CA  ALA B 374     4617   6046   5677    152    522   -299       C  
ATOM   5745  C   ALA B 374     -26.495  18.327   2.466  1.00 47.76           C  
ANISOU 5745  C   ALA B 374     5285   6674   6187    123    448   -261       C  
ATOM   5746  O   ALA B 374     -25.587  18.652   3.230  1.00 48.07           O  
ANISOU 5746  O   ALA B 374     5397   6689   6180     92    458   -296       O  
ATOM   5747  CB  ALA B 374     -28.660  17.458   3.392  1.00 43.67           C  
ANISOU 5747  CB  ALA B 374     4701   6184   5707    116    562   -332       C  
ATOM   5748  N   ILE B 375     -26.273  17.753   1.271  1.00 44.00           N  
ANISOU 5748  N   ILE B 375     4777   6252   5691    130    376   -195       N  
ATOM   5749  CA  ILE B 375     -24.934  17.413   0.789  1.00 43.54           C  
ANISOU 5749  CA  ILE B 375     4760   6219   5562    107    315   -165       C  
ATOM   5750  C   ILE B 375     -24.133  18.690   0.544  1.00 48.91           C  
ANISOU 5750  C   ILE B 375     5454   6849   6279    121    296   -136       C  
ATOM   5751  O   ILE B 375     -22.949  18.745   0.896  1.00 50.26           O  
ANISOU 5751  O   ILE B 375     5683   7010   6404     92    279   -146       O  
ATOM   5752  CB  ILE B 375     -24.985  16.515  -0.473  1.00 45.76           C  
ANISOU 5752  CB  ILE B 375     4995   6577   5815    102    262   -126       C  
ATOM   5753  CG1 ILE B 375     -25.691  15.185  -0.156  1.00 45.08           C  
ANISOU 5753  CG1 ILE B 375     4898   6522   5707     77    287   -164       C  
ATOM   5754  CG2 ILE B 375     -23.580  16.277  -1.035  1.00 44.73           C  
ANISOU 5754  CG2 ILE B 375     4896   6470   5628     80    215   -106       C  
ATOM   5755  CD1 ILE B 375     -26.182  14.463  -1.330  1.00 49.63           C  
ANISOU 5755  CD1 ILE B 375     5408   7169   6280     69    252   -153       C  
ATOM   5756  N   LEU B 376     -24.776  19.708  -0.036  1.00 45.47           N  
ANISOU 5756  N   LEU B 376     4960   6378   5941    165    295    -92       N  
ATOM   5757  CA  LEU B 376     -24.132  20.993  -0.300  1.00 45.62           C  
ANISOU 5757  CA  LEU B 376     4981   6328   6022    179    282    -52       C  
ATOM   5758  C   LEU B 376     -23.755  21.700   1.002  1.00 48.77           C  
ANISOU 5758  C   LEU B 376     5441   6641   6449    161    344   -140       C  
ATOM   5759  O   LEU B 376     -22.684  22.286   1.064  1.00 50.19           O  
ANISOU 5759  O   LEU B 376     5659   6785   6626    138    328   -138       O  
ATOM   5760  CB  LEU B 376     -25.012  21.908  -1.172  1.00 46.37           C  
ANISOU 5760  CB  LEU B 376     4987   6392   6239    234    267     33       C  
ATOM   5761  CG  LEU B 376     -25.290  21.420  -2.603  1.00 49.98           C  
ANISOU 5761  CG  LEU B 376     5380   6956   6654    238    191    134       C  
ATOM   5762  CD1 LEU B 376     -26.356  22.258  -3.264  1.00 50.72           C  
ANISOU 5762  CD1 LEU B 376     5374   7026   6872    292    171    227       C  
ATOM   5763  CD2 LEU B 376     -24.024  21.380  -3.447  1.00 50.49           C  
ANISOU 5763  CD2 LEU B 376     5474   7073   6637    202    136    192       C  
ATOM   5764  N   ALA B 377     -24.586  21.610   2.043  1.00 44.11           N  
ANISOU 5764  N   ALA B 377     4857   6029   5873    159    417   -225       N  
ATOM   5765  CA  ALA B 377     -24.273  22.261   3.314  1.00 44.63           C  
ANISOU 5765  CA  ALA B 377     4980   6034   5943    125    484   -329       C  
ATOM   5766  C   ALA B 377     -23.117  21.576   4.029  1.00 48.64           C  
ANISOU 5766  C   ALA B 377     5574   6600   6306     56    456   -362       C  
ATOM   5767  O   ALA B 377     -22.285  22.258   4.593  1.00 49.11           O  
ANISOU 5767  O   ALA B 377     5680   6624   6356     18    462   -409       O  
ATOM   5768  CB  ALA B 377     -25.495  22.291   4.215  1.00 46.28           C  
ANISOU 5768  CB  ALA B 377     5167   6224   6194    132    580   -416       C  
ATOM   5769  N   VAL B 378     -23.028  20.240   3.955  1.00 45.18           N  
ANISOU 5769  N   VAL B 378     5148   6247   5769     38    420   -329       N  
ATOM   5770  CA  VAL B 378     -21.976  19.468   4.621  1.00 43.92           C  
ANISOU 5770  CA  VAL B 378     5055   6142   5491    -20    384   -335       C  
ATOM   5771  C   VAL B 378     -20.716  19.375   3.724  1.00 47.69           C  
ANISOU 5771  C   VAL B 378     5530   6632   5958    -19    304   -269       C  
ATOM   5772  O   VAL B 378     -19.658  18.949   4.186  1.00 46.18           O  
ANISOU 5772  O   VAL B 378     5378   6471   5697    -60    265   -266       O  
ATOM   5773  CB  VAL B 378     -22.482  18.085   5.109  1.00 46.62           C  
ANISOU 5773  CB  VAL B 378     5407   6548   5759    -41    394   -328       C  
ATOM   5774  CG1 VAL B 378     -23.767  18.246   5.927  1.00 46.38           C  
ANISOU 5774  CG1 VAL B 378     5369   6510   5741    -47    486   -395       C  
ATOM   5775  CG2 VAL B 378     -22.685  17.116   3.949  1.00 45.68           C  
ANISOU 5775  CG2 VAL B 378     5237   6459   5659     -9    350   -262       C  
ATOM   5776  N   ALA B 379     -20.827  19.859   2.472  1.00 45.61           N  
ANISOU 5776  N   ALA B 379     5214   6349   5767     24    281   -213       N  
ATOM   5777  CA  ALA B 379     -19.753  19.968   1.489  1.00 45.06           C  
ANISOU 5777  CA  ALA B 379     5130   6295   5695     23    223   -152       C  
ATOM   5778  C   ALA B 379     -19.026  18.611   1.253  1.00 49.40           C  
ANISOU 5778  C   ALA B 379     5685   6914   6170      3    180   -133       C  
ATOM   5779  O   ALA B 379     -17.810  18.504   1.381  1.00 49.60           O  
ANISOU 5779  O   ALA B 379     5730   6948   6166    -24    146   -127       O  
ATOM   5780  CB  ALA B 379     -18.768  21.071   1.891  1.00 45.15           C  
ANISOU 5780  CB  ALA B 379     5173   6250   5732     -6    220   -172       C  
ATOM   5781  N   GLN B 380     -19.778  17.588   0.869  1.00 45.51           N  
ANISOU 5781  N   GLN B 380     5164   6464   5664     18    184   -126       N  
ATOM   5782  CA  GLN B 380     -19.155  16.287   0.626  1.00 44.03           C  
ANISOU 5782  CA  GLN B 380     4972   6319   5437      4    156   -119       C  
ATOM   5783  C   GLN B 380     -19.260  15.881  -0.851  1.00 46.15           C  
ANISOU 5783  C   GLN B 380     5183   6638   5712     16    139    -97       C  
ATOM   5784  O   GLN B 380     -19.386  14.702  -1.186  1.00 45.13           O  
ANISOU 5784  O   GLN B 380     5033   6540   5573     10    140   -115       O  
ATOM   5785  CB  GLN B 380     -19.703  15.233   1.591  1.00 44.66           C  
ANISOU 5785  CB  GLN B 380     5075   6401   5492    -11    178   -142       C  
ATOM   5786  CG  GLN B 380     -19.092  15.431   2.990  1.00 42.10           C  
ANISOU 5786  CG  GLN B 380     4811   6061   5125    -47    175   -153       C  
ATOM   5787  CD  GLN B 380     -17.589  15.216   3.020  1.00 49.78           C  
ANISOU 5787  CD  GLN B 380     5791   7041   6083    -65    120   -126       C  
ATOM   5788  OE1 GLN B 380     -17.031  14.438   2.256  1.00 46.91           O  
ANISOU 5788  OE1 GLN B 380     5392   6688   5744    -53     95   -104       O  
ATOM   5789  NE2 GLN B 380     -16.901  15.855   3.939  1.00 34.75           N  
ANISOU 5789  NE2 GLN B 380     3928   5133   4143   -100    103   -137       N  
ATOM   5790  N   VAL B 381     -19.122  16.895  -1.727  1.00 42.84           N  
ANISOU 5790  N   VAL B 381     4740   6230   5309     26    125    -57       N  
ATOM   5791  CA  VAL B 381     -19.141  16.764  -3.184  1.00 42.85           C  
ANISOU 5791  CA  VAL B 381     4689   6303   5289     22    106    -26       C  
ATOM   5792  C   VAL B 381     -17.689  16.693  -3.642  1.00 46.83           C  
ANISOU 5792  C   VAL B 381     5194   6829   5770     -3     91    -21       C  
ATOM   5793  O   VAL B 381     -16.892  17.581  -3.321  1.00 46.17           O  
ANISOU 5793  O   VAL B 381     5132   6705   5705    -10     83      2       O  
ATOM   5794  CB  VAL B 381     -19.933  17.903  -3.880  1.00 45.73           C  
ANISOU 5794  CB  VAL B 381     5017   6675   5683     43     95     42       C  
ATOM   5795  CG1 VAL B 381     -19.913  17.748  -5.393  1.00 45.40           C  
ANISOU 5795  CG1 VAL B 381     4923   6738   5589     22     66     87       C  
ATOM   5796  CG2 VAL B 381     -21.359  17.982  -3.354  1.00 45.33           C  
ANISOU 5796  CG2 VAL B 381     4948   6596   5678     73    116     31       C  
ATOM   5797  N   ASP B 382     -17.342  15.594  -4.325  1.00 43.38           N  
ANISOU 5797  N   ASP B 382     4728   6451   5305    -21     94    -57       N  
ATOM   5798  CA  ASP B 382     -15.987  15.324  -4.805  1.00 43.56           C  
ANISOU 5798  CA  ASP B 382     4736   6499   5318    -44     94    -70       C  
ATOM   5799  C   ASP B 382     -16.019  15.009  -6.290  1.00 48.40           C  
ANISOU 5799  C   ASP B 382     5297   7216   5878    -72    104    -82       C  
ATOM   5800  O   ASP B 382     -17.024  14.509  -6.796  1.00 47.69           O  
ANISOU 5800  O   ASP B 382     5184   7176   5761    -78    108   -106       O  
ATOM   5801  CB  ASP B 382     -15.335  14.145  -4.035  1.00 45.00           C  
ANISOU 5801  CB  ASP B 382     4924   6637   5537    -41    100   -120       C  
ATOM   5802  CG  ASP B 382     -15.731  13.987  -2.569  1.00 55.41           C  
ANISOU 5802  CG  ASP B 382     6290   7886   6877    -26     91   -115       C  
ATOM   5803  OD1 ASP B 382     -15.340  14.848  -1.749  1.00 54.98           O  
ANISOU 5803  OD1 ASP B 382     6272   7794   6822    -28     74    -89       O  
ATOM   5804  OD2 ASP B 382     -16.426  13.002  -2.246  1.00 59.72           O  
ANISOU 5804  OD2 ASP B 382     6835   8419   7437    -20    105   -140       O  
ATOM   5805  N   GLY B 383     -14.917  15.303  -6.974  1.00 45.17           N  
ANISOU 5805  N   GLY B 383     4867   6847   5448   -100    112    -72       N  
ATOM   5806  CA  GLY B 383     -14.769  15.003  -8.389  1.00 44.10           C  
ANISOU 5806  CA  GLY B 383     4684   6832   5242   -144    132    -95       C  
ATOM   5807  C   GLY B 383     -14.104  13.660  -8.562  1.00 46.62           C  
ANISOU 5807  C   GLY B 383     4971   7159   5585   -157    175   -204       C  
ATOM   5808  O   GLY B 383     -13.451  13.163  -7.634  1.00 45.73           O  
ANISOU 5808  O   GLY B 383     4868   6954   5553   -130    178   -230       O  
ATOM   5809  N   ASP B 384     -14.257  13.058  -9.750  1.00 44.05           N  
ANISOU 5809  N   ASP B 384     4601   6943   5193   -204    208   -271       N  
ATOM   5810  CA  ASP B 384     -13.609  11.792 -10.071  1.00 44.31           C  
ANISOU 5810  CA  ASP B 384     4591   6979   5266   -221    266   -397       C  
ATOM   5811  C   ASP B 384     -13.335  11.700 -11.563  1.00 50.27           C  
ANISOU 5811  C   ASP B 384     5298   7887   5915   -295    312   -456       C  
ATOM   5812  O   ASP B 384     -14.259  11.785 -12.365  1.00 50.28           O  
ANISOU 5812  O   ASP B 384     5290   8000   5812   -337    299   -457       O  
ATOM   5813  CB  ASP B 384     -14.418  10.590  -9.575  1.00 45.62           C  
ANISOU 5813  CB  ASP B 384     4756   7080   5497   -202    276   -472       C  
ATOM   5814  CG  ASP B 384     -13.854   9.261  -9.994  1.00 58.54           C  
ANISOU 5814  CG  ASP B 384     6338   8703   7200   -221    344   -610       C  
ATOM   5815  OD1 ASP B 384     -12.646   9.028  -9.767  1.00 60.06           O  
ANISOU 5815  OD1 ASP B 384     6506   8835   7479   -201    370   -628       O  
ATOM   5816  OD2 ASP B 384     -14.610   8.461 -10.563  1.00 67.17           O  
ANISOU 5816  OD2 ASP B 384     7405   9844   8270   -258    374   -705       O  
ATOM   5817  N   SER B 385     -12.056  11.497 -11.924  1.00 47.39           N  
ANISOU 5817  N   SER B 385     4896   7536   5575   -315    367   -510       N  
ATOM   5818  CA  SER B 385     -11.590  11.420 -13.294  1.00 48.14           C  
ANISOU 5818  CA  SER B 385     4942   7784   5566   -394    429   -579       C  
ATOM   5819  C   SER B 385     -12.106  10.178 -14.059  1.00 53.72           C  
ANISOU 5819  C   SER B 385     5608   8564   6240   -444    488   -743       C  
ATOM   5820  O   SER B 385     -12.358  10.286 -15.266  1.00 53.65           O  
ANISOU 5820  O   SER B 385     5577   8729   6078   -529    512   -780       O  
ATOM   5821  CB  SER B 385     -10.064  11.457 -13.324  1.00 51.77           C  
ANISOU 5821  CB  SER B 385     5361   8218   6091   -396    485   -609       C  
ATOM   5822  OG  SER B 385      -9.501  10.433 -12.521  1.00 56.39           O  
ANISOU 5822  OG  SER B 385     5919   8661   6847   -338    510   -687       O  
ATOM   5823  N   VAL B 386     -12.256   9.015 -13.391  1.00 51.36           N  
ANISOU 5823  N   VAL B 386     5297   8138   6080   -402    512   -841       N  
ATOM   5824  CA  VAL B 386     -12.698   7.801 -14.095  1.00 52.55           C  
ANISOU 5824  CA  VAL B 386     5403   8333   6229   -454    578  -1017       C  
ATOM   5825  C   VAL B 386     -14.214   7.891 -14.415  1.00 56.98           C  
ANISOU 5825  C   VAL B 386     5989   8986   6676   -491    522   -995       C  
ATOM   5826  O   VAL B 386     -14.580   7.566 -15.546  1.00 59.41           O  
ANISOU 5826  O   VAL B 386     6263   9449   6861   -581    556  -1098       O  
ATOM   5827  CB  VAL B 386     -12.253   6.428 -13.470  1.00 56.70           C  
ANISOU 5827  CB  VAL B 386     5891   8687   6966   -406    637  -1137       C  
ATOM   5828  CG1 VAL B 386     -11.449   6.596 -12.189  1.00 56.22           C  
ANISOU 5828  CG1 VAL B 386     5844   8460   7056   -314    599  -1029       C  
ATOM   5829  CG2 VAL B 386     -13.393   5.435 -13.291  1.00 56.04           C  
ANISOU 5829  CG2 VAL B 386     5809   8551   6933   -413    637  -1215       C  
ATOM   5830  N   SER B 387     -15.069   8.393 -13.497  1.00 51.52           N  
ANISOU 5830  N   SER B 387     5347   8216   6011   -431    439   -865       N  
ATOM   5831  CA  SER B 387     -16.505   8.550 -13.804  1.00 50.71           C  
ANISOU 5831  CA  SER B 387     5252   8199   5815   -461    383   -833       C  
ATOM   5832  C   SER B 387     -16.780   9.845 -14.616  1.00 53.03           C  
ANISOU 5832  C   SER B 387     5551   8657   5941   -502    325   -703       C  
ATOM   5833  O   SER B 387     -17.803   9.938 -15.286  1.00 53.57           O  
ANISOU 5833  O   SER B 387     5599   8855   5900   -553    284   -691       O  
ATOM   5834  CB  SER B 387     -17.353   8.535 -12.535  1.00 51.70           C  
ANISOU 5834  CB  SER B 387     5417   8183   6044   -386    331   -755       C  
ATOM   5835  OG  SER B 387     -16.998   9.589 -11.659  1.00 56.21           O  
ANISOU 5835  OG  SER B 387     6035   8675   6648   -321    286   -610       O  
ATOM   5836  N   GLY B 388     -15.870  10.817 -14.527  1.00 48.06           N  
ANISOU 5836  N   GLY B 388     4942   8016   5304   -480    318   -599       N  
ATOM   5837  CA  GLY B 388     -15.956  12.114 -15.196  1.00 47.73           C  
ANISOU 5837  CA  GLY B 388     4905   8095   5134   -512    267   -449       C  
ATOM   5838  C   GLY B 388     -17.060  13.010 -14.679  1.00 50.31           C  
ANISOU 5838  C   GLY B 388     5257   8383   5476   -461    176   -294       C  
ATOM   5839  O   GLY B 388     -17.551  13.879 -15.402  1.00 49.73           O  
ANISOU 5839  O   GLY B 388     5169   8428   5299   -495    121   -172       O  
ATOM   5840  N   ILE B 389     -17.484  12.785 -13.430  1.00 46.24           N  
ANISOU 5840  N   ILE B 389     4771   7704   5094   -383    162   -295       N  
ATOM   5841  CA  ILE B 389     -18.532  13.579 -12.789  1.00 45.45           C  
ANISOU 5841  CA  ILE B 389     4690   7545   5035   -328     96   -173       C  
ATOM   5842  C   ILE B 389     -18.127  13.976 -11.397  1.00 48.11           C  
ANISOU 5842  C   ILE B 389     5078   7700   5501   -249     99   -136       C  
ATOM   5843  O   ILE B 389     -17.130  13.500 -10.869  1.00 45.65           O  
ANISOU 5843  O   ILE B 389     4785   7311   5249   -236    140   -199       O  
ATOM   5844  CB  ILE B 389     -19.913  12.852 -12.721  1.00 48.01           C  
ANISOU 5844  CB  ILE B 389     4986   7892   5363   -332     74   -225       C  
ATOM   5845  CG1 ILE B 389     -19.874  11.585 -11.805  1.00 47.15           C  
ANISOU 5845  CG1 ILE B 389     4892   7661   5360   -308    127   -358       C  
ATOM   5846  CG2 ILE B 389     -20.541  12.626 -14.104  1.00 49.22           C  
ANISOU 5846  CG2 ILE B 389     5081   8250   5370   -419     48   -243       C  
ATOM   5847  CD1 ILE B 389     -21.210  11.229 -11.102  1.00 50.92           C  
ANISOU 5847  CD1 ILE B 389     5366   8076   5904   -275    105   -357       C  
ATOM   5848  N   CYS B 390     -18.972  14.801 -10.785  1.00 47.05           N  
ANISOU 5848  N   CYS B 390     4959   7504   5415   -200     56    -39       N  
ATOM   5849  CA  CYS B 390     -18.890  15.170  -9.392  1.00 47.11           C  
ANISOU 5849  CA  CYS B 390     5015   7355   5531   -136     60    -19       C  
ATOM   5850  C   CYS B 390     -20.065  14.489  -8.707  1.00 50.19           C  
ANISOU 5850  C   CYS B 390     5403   7701   5967   -111     62    -65       C  
ATOM   5851  O   CYS B 390     -21.166  14.409  -9.272  1.00 49.48           O  
ANISOU 5851  O   CYS B 390     5268   7685   5845   -123     37    -51       O  
ATOM   5852  CB  CYS B 390     -18.887  16.682  -9.208  1.00 48.35           C  
ANISOU 5852  CB  CYS B 390     5187   7464   5721   -108     30    107       C  
ATOM   5853  SG  CYS B 390     -17.259  17.450  -9.465  1.00 52.55           S  
ANISOU 5853  SG  CYS B 390     5738   7986   6244   -133     43    151       S  
ATOM   5854  N   PHE B 391     -19.784  13.854  -7.572  1.00 45.40           N  
ANISOU 5854  N   PHE B 391     4834   6989   5428    -85     91   -123       N  
ATOM   5855  CA  PHE B 391     -20.764  13.076  -6.848  1.00 44.28           C  
ANISOU 5855  CA  PHE B 391     4693   6801   5330    -71    106   -168       C  
ATOM   5856  C   PHE B 391     -20.518  13.173  -5.351  1.00 47.76           C  
ANISOU 5856  C   PHE B 391     5192   7121   5835    -35    122   -161       C  
ATOM   5857  O   PHE B 391     -19.610  13.872  -4.913  1.00 48.08           O  
ANISOU 5857  O   PHE B 391     5267   7117   5884    -24    116   -128       O  
ATOM   5858  CB  PHE B 391     -20.745  11.614  -7.341  1.00 45.85           C  
ANISOU 5858  CB  PHE B 391     4862   7037   5522   -111    134   -273       C  
ATOM   5859  CG  PHE B 391     -22.025  10.829  -7.136  1.00 47.59           C  
ANISOU 5859  CG  PHE B 391     5057   7258   5769   -121    142   -317       C  
ATOM   5860  CD1 PHE B 391     -23.200  11.188  -7.800  1.00 50.39           C  
ANISOU 5860  CD1 PHE B 391     5361   7702   6082   -136    111   -292       C  
ATOM   5861  CD2 PHE B 391     -22.050   9.711  -6.309  1.00 48.55           C  
ANISOU 5861  CD2 PHE B 391     5195   7291   5962   -120    179   -374       C  
ATOM   5862  CE1 PHE B 391     -24.376  10.445  -7.629  1.00 50.70           C  
ANISOU 5862  CE1 PHE B 391     5365   7746   6152   -152    119   -338       C  
ATOM   5863  CE2 PHE B 391     -23.233   8.977  -6.134  1.00 50.85           C  
ANISOU 5863  CE2 PHE B 391     5458   7580   6284   -138    193   -414       C  
ATOM   5864  CZ  PHE B 391     -24.376   9.335  -6.816  1.00 48.84           C  
ANISOU 5864  CZ  PHE B 391     5151   7419   5988   -156    165   -404       C  
ATOM   5865  N   VAL B 392     -21.391  12.544  -4.569  1.00 43.52           N  
ANISOU 5865  N   VAL B 392     4661   6542   5334    -27    141   -188       N  
ATOM   5866  CA  VAL B 392     -21.342  12.562  -3.129  1.00 42.95           C  
ANISOU 5866  CA  VAL B 392     4642   6381   5297     -9    159   -180       C  
ATOM   5867  C   VAL B 392     -20.673  11.291  -2.630  1.00 49.05           C  
ANISOU 5867  C   VAL B 392     5429   7111   6095    -24    173   -217       C  
ATOM   5868  O   VAL B 392     -20.978  10.189  -3.101  1.00 49.45           O  
ANISOU 5868  O   VAL B 392     5445   7176   6167    -44    189   -266       O  
ATOM   5869  CB  VAL B 392     -22.760  12.780  -2.489  1.00 45.86           C  
ANISOU 5869  CB  VAL B 392     5003   6731   5689      6    181   -176       C  
ATOM   5870  CG1 VAL B 392     -23.762  11.708  -2.923  1.00 45.55           C  
ANISOU 5870  CG1 VAL B 392     4915   6732   5662    -16    194   -218       C  
ATOM   5871  CG2 VAL B 392     -22.682  12.857  -0.959  1.00 45.13           C  
ANISOU 5871  CG2 VAL B 392     4970   6568   5607      9    209   -175       C  
ATOM   5872  N   GLY B 393     -19.779  11.469  -1.666  1.00 45.90           N  
ANISOU 5872  N   GLY B 393     5076   6659   5703    -17    164   -190       N  
ATOM   5873  CA  GLY B 393     -19.146  10.363  -0.971  1.00 45.96           C  
ANISOU 5873  CA  GLY B 393     5096   6615   5750    -25    166   -191       C  
ATOM   5874  C   GLY B 393     -18.100   9.598  -1.728  1.00 50.32           C  
ANISOU 5874  C   GLY B 393     5610   7165   6346    -28    163   -220       C  
ATOM   5875  O   GLY B 393     -17.907   8.401  -1.481  1.00 50.78           O  
ANISOU 5875  O   GLY B 393     5651   7172   6472    -32    174   -233       O  
ATOM   5876  N   TYR B 394     -17.401  10.284  -2.629  1.00 46.24           N  
ANISOU 5876  N   TYR B 394     5073   6696   5801    -29    153   -229       N  
ATOM   5877  CA  TYR B 394     -16.282   9.679  -3.336  1.00 46.20           C  
ANISOU 5877  CA  TYR B 394     5024   6694   5836    -34    162   -268       C  
ATOM   5878  C   TYR B 394     -15.077   9.592  -2.383  1.00 49.70           C  
ANISOU 5878  C   TYR B 394     5480   7075   6329    -19    133   -221       C  
ATOM   5879  O   TYR B 394     -14.440   8.542  -2.296  1.00 50.11           O  
ANISOU 5879  O   TYR B 394     5496   7077   6468    -11    141   -237       O  
ATOM   5880  CB  TYR B 394     -15.944  10.466  -4.602  1.00 46.54           C  
ANISOU 5880  CB  TYR B 394     5040   6824   5820    -51    166   -284       C  
ATOM   5881  CG  TYR B 394     -16.768  10.124  -5.827  1.00 46.28           C  
ANISOU 5881  CG  TYR B 394     4967   6874   5742    -81    192   -345       C  
ATOM   5882  CD1 TYR B 394     -17.379   8.877  -5.957  1.00 48.30           C  
ANISOU 5882  CD1 TYR B 394     5195   7113   6043    -95    223   -420       C  
ATOM   5883  CD2 TYR B 394     -16.815  10.987  -6.914  1.00 46.77           C  
ANISOU 5883  CD2 TYR B 394     5012   7039   5719   -105    184   -329       C  
ATOM   5884  CE1 TYR B 394     -18.043   8.514  -7.129  1.00 48.88           C  
ANISOU 5884  CE1 TYR B 394     5226   7279   6067   -138    244   -495       C  
ATOM   5885  CE2 TYR B 394     -17.468  10.633  -8.093  1.00 48.15           C  
ANISOU 5885  CE2 TYR B 394     5144   7318   5832   -147    198   -383       C  
ATOM   5886  CZ  TYR B 394     -18.079   9.397  -8.197  1.00 56.08           C  
ANISOU 5886  CZ  TYR B 394     6122   8313   6872   -167    227   -476       C  
ATOM   5887  OH  TYR B 394     -18.716   9.069  -9.363  1.00 59.78           O  
ANISOU 5887  OH  TYR B 394     6545   8899   7268   -222    238   -543       O  
ATOM   5888  N   LYS B 395     -14.834  10.662  -1.605  1.00 44.77           N  
ANISOU 5888  N   LYS B 395     4902   6451   5659    -17     98   -164       N  
ATOM   5889  CA  LYS B 395     -13.750  10.741  -0.626  1.00 44.31           C  
ANISOU 5889  CA  LYS B 395     4855   6356   5624    -16     56   -114       C  
ATOM   5890  C   LYS B 395     -14.097   9.969   0.632  1.00 47.36           C  
ANISOU 5890  C   LYS B 395     5270   6696   6027    -17     38    -69       C  
ATOM   5891  O   LYS B 395     -13.253   9.257   1.155  1.00 47.55           O  
ANISOU 5891  O   LYS B 395     5271   6682   6113    -11      7    -28       O  
ATOM   5892  CB  LYS B 395     -13.441  12.215  -0.259  1.00 46.03           C  
ANISOU 5892  CB  LYS B 395     5112   6596   5780    -30     30    -87       C  
ATOM   5893  CG  LYS B 395     -11.987  12.476   0.117  1.00 54.84           C  
ANISOU 5893  CG  LYS B 395     6209   7706   6922    -40    -13    -58       C  
ATOM   5894  CD  LYS B 395     -11.691  12.326   1.604  1.00 69.85           C  
ANISOU 5894  CD  LYS B 395     8145   9587   8808    -56    -65     -8       C  
ATOM   5895  CE  LYS B 395     -10.222  12.510   1.936  1.00 77.75           C  
ANISOU 5895  CE  LYS B 395     9112  10593   9837    -70   -120     24       C  
ATOM   5896  NZ  LYS B 395      -9.326  11.708   1.052  1.00 81.50           N  
ANISOU 5896  NZ  LYS B 395     9500  11051  10415    -43   -113     19       N  
ATOM   5897  N   ASN B 396     -15.308  10.178   1.155  1.00 43.41           N  
ANISOU 5897  N   ASN B 396     4816   6202   5474    -27     56    -67       N  
ATOM   5898  CA  ASN B 396     -15.802   9.607   2.402  1.00 42.97           C  
ANISOU 5898  CA  ASN B 396     4798   6122   5406    -43     49    -19       C  
ATOM   5899  C   ASN B 396     -17.043   8.772   2.103  1.00 44.98           C  
ANISOU 5899  C   ASN B 396     5040   6359   5689    -42     99    -48       C  
ATOM   5900  O   ASN B 396     -18.108   9.324   1.851  1.00 44.95           O  
ANISOU 5900  O   ASN B 396     5049   6386   5644    -44    131    -84       O  
ATOM   5901  CB  ASN B 396     -16.085  10.746   3.390  1.00 44.59           C  
ANISOU 5901  CB  ASN B 396     5067   6359   5514    -68     40     -7       C  
ATOM   5902  CG  ASN B 396     -14.896  11.637   3.635  1.00 55.38           C  
ANISOU 5902  CG  ASN B 396     6443   7744   6855    -81     -7      7       C  
ATOM   5903  OD1 ASN B 396     -14.828  12.765   3.157  1.00 51.05           O  
ANISOU 5903  OD1 ASN B 396     5900   7209   6287    -80      3    -29       O  
ATOM   5904  ND2 ASN B 396     -13.905  11.127   4.333  1.00 45.85           N  
ANISOU 5904  ND2 ASN B 396     5228   6533   5660    -95    -63     67       N  
ATOM   5905  N   TYR B 397     -16.881   7.436   2.077  1.00 40.87           N  
ANISOU 5905  N   TYR B 397     4484   5783   5260    -38    104    -33       N  
ATOM   5906  CA  TYR B 397     -17.899   6.463   1.668  1.00 39.94           C  
ANISOU 5906  CA  TYR B 397     4342   5636   5199    -45    152    -72       C  
ATOM   5907  C   TYR B 397     -19.252   6.578   2.431  1.00 45.53           C  
ANISOU 5907  C   TYR B 397     5091   6361   5848    -71    181    -55       C  
ATOM   5908  O   TYR B 397     -20.305   6.284   1.844  1.00 46.60           O  
ANISOU 5908  O   TYR B 397     5201   6504   6001    -79    223   -111       O  
ATOM   5909  CB  TYR B 397     -17.337   5.038   1.770  1.00 40.34           C  
ANISOU 5909  CB  TYR B 397     4350   5596   5383    -39    151    -43       C  
ATOM   5910  CG  TYR B 397     -17.298   4.472   3.165  1.00 42.90           C  
ANISOU 5910  CG  TYR B 397     4706   5877   5719    -55    122     77       C  
ATOM   5911  CD1 TYR B 397     -16.259   4.784   4.037  1.00 45.42           C  
ANISOU 5911  CD1 TYR B 397     5043   6206   6009    -53     55    169       C  
ATOM   5912  CD2 TYR B 397     -18.316   3.641   3.630  1.00 43.66           C  
ANISOU 5912  CD2 TYR B 397     4811   5933   5846    -82    157    105       C  
ATOM   5913  CE1 TYR B 397     -16.249   4.308   5.347  1.00 46.13           C  
ANISOU 5913  CE1 TYR B 397     5163   6282   6081    -81     18    295       C  
ATOM   5914  CE2 TYR B 397     -18.312   3.157   4.935  1.00 45.04           C  
ANISOU 5914  CE2 TYR B 397     5018   6084   6012   -108    130    233       C  
ATOM   5915  CZ  TYR B 397     -17.271   3.482   5.787  1.00 52.13           C  
ANISOU 5915  CZ  TYR B 397     5936   7005   6865   -108     58    332       C  
ATOM   5916  OH  TYR B 397     -17.246   2.974   7.067  1.00 54.35           O  
ANISOU 5916  OH  TYR B 397     6247   7282   7120   -145     21    474       O  
ATOM   5917  N   ARG B 398     -19.225   7.029   3.703  1.00 41.18           N  
ANISOU 5917  N   ARG B 398     4597   5827   5224    -91    163     12       N  
ATOM   5918  CA  ARG B 398     -20.408   7.167   4.557  1.00 40.40           C  
ANISOU 5918  CA  ARG B 398     4535   5751   5062   -122    203     23       C  
ATOM   5919  C   ARG B 398     -21.440   8.094   3.946  1.00 43.91           C  
ANISOU 5919  C   ARG B 398     4970   6239   5475   -111    244    -55       C  
ATOM   5920  O   ARG B 398     -22.636   7.859   4.111  1.00 44.39           O  
ANISOU 5920  O   ARG B 398     5021   6305   5538   -127    293    -73       O  
ATOM   5921  CB  ARG B 398     -20.019   7.667   5.957  1.00 39.33           C  
ANISOU 5921  CB  ARG B 398     4464   5652   4828   -156    177     88       C  
ATOM   5922  CG  ARG B 398     -19.433   6.583   6.860  1.00 45.84           C  
ANISOU 5922  CG  ARG B 398     5297   6446   5674   -183    138    201       C  
ATOM   5923  CD  ARG B 398     -19.032   7.187   8.199  1.00 55.83           C  
ANISOU 5923  CD  ARG B 398     6625   7781   6808   -232    104    260       C  
ATOM   5924  NE  ARG B 398     -18.433   6.200   9.097  1.00 70.42           N  
ANISOU 5924  NE  ARG B 398     8475   9615   8664   -263     49    398       N  
ATOM   5925  CZ  ARG B 398     -17.133   5.915   9.146  1.00 82.38           C  
ANISOU 5925  CZ  ARG B 398     9963  11111  10227   -246    -35    473       C  
ATOM   5926  NH1 ARG B 398     -16.280   6.528   8.333  1.00 53.21           N  
ANISOU 5926  NH1 ARG B 398     6238   7410   6568   -204    -63    410       N  
ATOM   5927  NH2 ARG B 398     -16.679   5.005   9.996  1.00 79.99           N  
ANISOU 5927  NH2 ARG B 398     9654  10795   9943   -272    -91    620       N  
ATOM   5928  N   TYR B 399     -20.983   9.139   3.235  1.00 40.08           N  
ANISOU 5928  N   TYR B 399     4478   5782   4970    -84    223    -90       N  
ATOM   5929  CA  TYR B 399     -21.856  10.114   2.573  1.00 39.50           C  
ANISOU 5929  CA  TYR B 399     4383   5742   4883    -65    248   -139       C  
ATOM   5930  C   TYR B 399     -22.525   9.466   1.375  1.00 43.63           C  
ANISOU 5930  C   TYR B 399     4843   6278   5457    -59    260   -179       C  
ATOM   5931  O   TYR B 399     -23.690   9.744   1.125  1.00 42.95           O  
ANISOU 5931  O   TYR B 399     4727   6217   5374    -57    287   -204       O  
ATOM   5932  CB  TYR B 399     -21.078  11.395   2.191  1.00 39.44           C  
ANISOU 5932  CB  TYR B 399     4386   5749   4850    -44    218   -143       C  
ATOM   5933  CG  TYR B 399     -20.630  12.117   3.435  1.00 40.53           C  
ANISOU 5933  CG  TYR B 399     4585   5882   4933    -64    214   -127       C  
ATOM   5934  CD1 TYR B 399     -19.449  11.758   4.084  1.00 42.88           C  
ANISOU 5934  CD1 TYR B 399     4911   6174   5208    -85    170    -87       C  
ATOM   5935  CD2 TYR B 399     -21.459  13.053   4.059  1.00 40.56           C  
ANISOU 5935  CD2 TYR B 399     4611   5890   4912    -69    259   -159       C  
ATOM   5936  CE1 TYR B 399     -19.085  12.335   5.298  1.00 41.97           C  
ANISOU 5936  CE1 TYR B 399     4851   6075   5023   -121    161    -77       C  
ATOM   5937  CE2 TYR B 399     -21.094  13.650   5.265  1.00 40.80           C  
ANISOU 5937  CE2 TYR B 399     4699   5926   4880   -105    266   -168       C  
ATOM   5938  CZ  TYR B 399     -19.898  13.294   5.870  1.00 44.65           C  
ANISOU 5938  CZ  TYR B 399     5219   6425   5321   -136    212   -128       C  
ATOM   5939  OH  TYR B 399     -19.521  13.841   7.061  1.00 41.90           O  
ANISOU 5939  OH  TYR B 399     4925   6104   4892   -186    210   -140       O  
ATOM   5940  N   ARG B 400     -21.842   8.527   0.700  1.00 41.38           N  
ANISOU 5940  N   ARG B 400     4529   5975   5219    -62    244   -193       N  
ATOM   5941  CA  ARG B 400     -22.477   7.784  -0.394  1.00 41.97           C  
ANISOU 5941  CA  ARG B 400     4543   6069   5334    -74    261   -253       C  
ATOM   5942  C   ARG B 400     -23.490   6.795   0.199  1.00 46.43           C  
ANISOU 5942  C   ARG B 400     5099   6597   5945   -103    301   -256       C  
ATOM   5943  O   ARG B 400     -24.545   6.588  -0.387  1.00 47.50           O  
ANISOU 5943  O   ARG B 400     5188   6765   6093   -119    321   -303       O  
ATOM   5944  CB  ARG B 400     -21.438   7.061  -1.266  1.00 42.95           C  
ANISOU 5944  CB  ARG B 400     4635   6179   5505    -76    251   -292       C  
ATOM   5945  CG  ARG B 400     -21.976   6.630  -2.624  1.00 49.12           C  
ANISOU 5945  CG  ARG B 400     5354   7014   6295   -101    268   -380       C  
ATOM   5946  CD  ARG B 400     -20.863   6.015  -3.426  1.00 57.78           C  
ANISOU 5946  CD  ARG B 400     6420   8101   7434   -107    275   -437       C  
ATOM   5947  NE  ARG B 400     -21.363   5.167  -4.506  1.00 62.02           N  
ANISOU 5947  NE  ARG B 400     6898   8673   7994   -150    307   -546       N  
ATOM   5948  CZ  ARG B 400     -20.637   4.775  -5.548  1.00 69.03           C  
ANISOU 5948  CZ  ARG B 400     7745   9591   8893   -171    328   -634       C  
ATOM   5949  NH1 ARG B 400     -19.366   5.144  -5.658  1.00 52.72           N  
ANISOU 5949  NH1 ARG B 400     5686   7520   6827   -147    321   -617       N  
ATOM   5950  NH2 ARG B 400     -21.177   4.014  -6.489  1.00 57.72           N  
ANISOU 5950  NH2 ARG B 400     6260   8203   7469   -224    360   -750       N  
ATOM   5951  N   ALA B 401     -23.190   6.236   1.382  1.00 42.03           N  
ANISOU 5951  N   ALA B 401     4584   5981   5406   -114    308   -196       N  
ATOM   5952  CA  ALA B 401     -24.052   5.289   2.087  1.00 42.18           C  
ANISOU 5952  CA  ALA B 401     4600   5958   5468   -149    349   -175       C  
ATOM   5953  C   ALA B 401     -25.314   5.970   2.609  1.00 48.16           C  
ANISOU 5953  C   ALA B 401     5364   6763   6171   -161    387   -180       C  
ATOM   5954  O   ALA B 401     -26.415   5.411   2.505  1.00 48.86           O  
ANISOU 5954  O   ALA B 401     5413   6852   6301   -188    427   -208       O  
ATOM   5955  CB  ALA B 401     -23.288   4.660   3.239  1.00 43.04           C  
ANISOU 5955  CB  ALA B 401     4753   6007   5593   -162    334    -81       C  
ATOM   5956  N   GLY B 402     -25.140   7.162   3.188  1.00 43.65           N  
ANISOU 5956  N   GLY B 402     4835   6227   5521   -144    381   -160       N  
ATOM   5957  CA  GLY B 402     -26.235   7.923   3.761  1.00 42.37           C  
ANISOU 5957  CA  GLY B 402     4675   6101   5323   -150    430   -176       C  
ATOM   5958  C   GLY B 402     -27.152   8.560   2.751  1.00 45.19           C  
ANISOU 5958  C   GLY B 402     4965   6498   5708   -122    435   -230       C  
ATOM   5959  O   GLY B 402     -28.375   8.560   2.944  1.00 44.82           O  
ANISOU 5959  O   GLY B 402     4879   6468   5684   -133    483   -251       O  
ATOM   5960  N   PHE B 403     -26.569   9.121   1.675  1.00 40.92           N  
ANISOU 5960  N   PHE B 403     4404   5978   5165    -89    384   -242       N  
ATOM   5961  CA  PHE B 403     -27.342   9.867   0.683  1.00 41.52           C  
ANISOU 5961  CA  PHE B 403     4414   6104   5257    -63    370   -264       C  
ATOM   5962  C   PHE B 403     -27.663   9.117  -0.616  1.00 48.00           C  
ANISOU 5962  C   PHE B 403     5166   6970   6103    -82    343   -300       C  
ATOM   5963  O   PHE B 403     -28.466   9.620  -1.414  1.00 47.56           O  
ANISOU 5963  O   PHE B 403     5043   6973   6054    -72    324   -306       O  
ATOM   5964  CB  PHE B 403     -26.603  11.170   0.333  1.00 42.04           C  
ANISOU 5964  CB  PHE B 403     4498   6179   5297    -24    333   -241       C  
ATOM   5965  CG  PHE B 403     -26.581  12.174   1.461  1.00 41.67           C  
ANISOU 5965  CG  PHE B 403     4501   6096   5237     -9    367   -233       C  
ATOM   5966  CD1 PHE B 403     -27.691  12.962   1.734  1.00 43.65           C  
ANISOU 5966  CD1 PHE B 403     4713   6343   5527     12    411   -248       C  
ATOM   5967  CD2 PHE B 403     -25.444  12.344   2.238  1.00 42.23           C  
ANISOU 5967  CD2 PHE B 403     4646   6139   5261    -21    358   -219       C  
ATOM   5968  CE1 PHE B 403     -27.656  13.925   2.746  1.00 44.27           C  
ANISOU 5968  CE1 PHE B 403     4834   6386   5602     20    457   -267       C  
ATOM   5969  CE2 PHE B 403     -25.413  13.303   3.257  1.00 45.10           C  
ANISOU 5969  CE2 PHE B 403     5054   6481   5601    -23    393   -233       C  
ATOM   5970  CZ  PHE B 403     -26.524  14.083   3.505  1.00 42.84           C  
ANISOU 5970  CZ  PHE B 403     4734   6185   5356     -4    448   -266       C  
ATOM   5971  N   VAL B 404     -27.058   7.947  -0.850  1.00 45.84           N  
ANISOU 5971  N   VAL B 404     4900   6671   5846   -113    340   -325       N  
ATOM   5972  CA  VAL B 404     -27.336   7.226  -2.094  1.00 46.45           C  
ANISOU 5972  CA  VAL B 404     4911   6795   5940   -144    324   -388       C  
ATOM   5973  C   VAL B 404     -27.825   5.833  -1.759  1.00 51.62           C  
ANISOU 5973  C   VAL B 404     5550   7398   6667   -191    366   -426       C  
ATOM   5974  O   VAL B 404     -28.923   5.491  -2.164  1.00 52.76           O  
ANISOU 5974  O   VAL B 404     5630   7580   6835   -224    377   -469       O  
ATOM   5975  CB  VAL B 404     -26.125   7.205  -3.079  1.00 49.69           C  
ANISOU 5975  CB  VAL B 404     5326   7233   6322   -143    289   -413       C  
ATOM   5976  CG1 VAL B 404     -26.415   6.353  -4.315  1.00 50.00           C  
ANISOU 5976  CG1 VAL B 404     5299   7331   6367   -194    287   -504       C  
ATOM   5977  CG2 VAL B 404     -25.735   8.618  -3.495  1.00 48.98           C  
ANISOU 5977  CG2 VAL B 404     5246   7198   6168   -106    248   -363       C  
ATOM   5978  N   LEU B 405     -27.042   5.044  -1.011  1.00 47.52           N  
ANISOU 5978  N   LEU B 405     5079   6788   6189   -197    386   -403       N  
ATOM   5979  CA  LEU B 405     -27.406   3.671  -0.684  1.00 46.96           C  
ANISOU 5979  CA  LEU B 405     4991   6642   6209   -242    428   -422       C  
ATOM   5980  C   LEU B 405     -28.723   3.579   0.112  1.00 51.15           C  
ANISOU 5980  C   LEU B 405     5509   7173   6753   -270    472   -399       C  
ATOM   5981  O   LEU B 405     -29.651   2.878  -0.327  1.00 51.21           O  
ANISOU 5981  O   LEU B 405     5454   7188   6817   -315    496   -457       O  
ATOM   5982  CB  LEU B 405     -26.268   2.958   0.069  1.00 46.21           C  
ANISOU 5982  CB  LEU B 405     4947   6444   6167   -235    430   -365       C  
ATOM   5983  CG  LEU B 405     -26.508   1.484   0.392  1.00 50.64           C  
ANISOU 5983  CG  LEU B 405     5487   6900   6852   -278    472   -365       C  
ATOM   5984  CD1 LEU B 405     -26.425   0.636  -0.855  1.00 51.03           C  
ANISOU 5984  CD1 LEU B 405     5473   6929   6987   -305    484   -486       C  
ATOM   5985  CD2 LEU B 405     -25.563   0.988   1.466  1.00 51.21           C  
ANISOU 5985  CD2 LEU B 405     5611   6878   6968   -265    463   -255       C  
ATOM   5986  N   ALA B 406     -28.801   4.280   1.260  1.00 47.02           N  
ANISOU 5986  N   ALA B 406     5039   6650   6178   -251    489   -326       N  
ATOM   5987  CA  ALA B 406     -29.962   4.236   2.147  1.00 46.69           C  
ANISOU 5987  CA  ALA B 406     4987   6612   6140   -280    547   -305       C  
ATOM   5988  C   ALA B 406     -31.261   4.744   1.463  1.00 50.46           C  
ANISOU 5988  C   ALA B 406     5379   7165   6629   -280    556   -363       C  
ATOM   5989  O   ALA B 406     -32.237   4.002   1.536  1.00 50.77           O  
ANISOU 5989  O   ALA B 406     5367   7197   6726   -328    598   -386       O  
ATOM   5990  CB  ALA B 406     -29.680   5.005   3.417  1.00 47.18           C  
ANISOU 5990  CB  ALA B 406     5123   6679   6125   -266    567   -239       C  
ATOM   5991  N   PRO B 407     -31.325   5.919   0.763  1.00 46.88           N  
ANISOU 5991  N   PRO B 407     4898   6780   6136   -232    515   -377       N  
ATOM   5992  CA  PRO B 407     -32.581   6.305   0.095  1.00 47.09           C  
ANISOU 5992  CA  PRO B 407     4825   6877   6190   -232    510   -411       C  
ATOM   5993  C   PRO B 407     -33.024   5.313  -0.992  1.00 49.05           C  
ANISOU 5993  C   PRO B 407     4999   7159   6480   -286    486   -477       C  
ATOM   5994  O   PRO B 407     -34.211   5.068  -1.120  1.00 49.39           O  
ANISOU 5994  O   PRO B 407     4961   7237   6570   -318    505   -505       O  
ATOM   5995  CB  PRO B 407     -32.245   7.670  -0.526  1.00 48.66           C  
ANISOU 5995  CB  PRO B 407     5017   7126   6346   -170    454   -388       C  
ATOM   5996  CG  PRO B 407     -31.095   8.163   0.217  1.00 51.60           C  
ANISOU 5996  CG  PRO B 407     5488   7447   6671   -140    458   -350       C  
ATOM   5997  CD  PRO B 407     -30.295   6.958   0.549  1.00 47.24           C  
ANISOU 5997  CD  PRO B 407     4990   6838   6121   -179    467   -351       C  
ATOM   5998  N   ILE B 408     -32.089   4.730  -1.748  1.00 45.00           N  
ANISOU 5998  N   ILE B 408     4505   6637   5954   -302    451   -514       N  
ATOM   5999  CA  ILE B 408     -32.397   3.728  -2.784  1.00 45.56           C  
ANISOU 5999  CA  ILE B 408     4510   6738   6061   -366    438   -605       C  
ATOM   6000  C   ILE B 408     -32.931   2.426  -2.098  1.00 51.84           C  
ANISOU 6000  C   ILE B 408     5297   7443   6956   -427    506   -629       C  
ATOM   6001  O   ILE B 408     -33.886   1.826  -2.593  1.00 52.89           O  
ANISOU 6001  O   ILE B 408     5350   7608   7137   -487    514   -697       O  
ATOM   6002  CB  ILE B 408     -31.160   3.495  -3.698  1.00 47.75           C  
ANISOU 6002  CB  ILE B 408     4814   7026   6304   -368    402   -652       C  
ATOM   6003  CG1 ILE B 408     -30.918   4.753  -4.591  1.00 47.85           C  
ANISOU 6003  CG1 ILE B 408     4809   7155   6214   -330    334   -626       C  
ATOM   6004  CG2 ILE B 408     -31.290   2.205  -4.553  1.00 48.99           C  
ANISOU 6004  CG2 ILE B 408     4917   7182   6515   -447    417   -774       C  
ATOM   6005  CD1 ILE B 408     -29.635   4.728  -5.537  1.00 57.52           C  
ANISOU 6005  CD1 ILE B 408     6062   8410   7382   -331    305   -662       C  
ATOM   6006  N   GLY B 409     -32.361   2.061  -0.942  1.00 47.54           N  
ANISOU 6006  N   GLY B 409     4831   6793   6440   -415    549   -562       N  
ATOM   6007  CA  GLY B 409     -32.799   0.911  -0.160  1.00 47.81           C  
ANISOU 6007  CA  GLY B 409     4865   6733   6567   -471    613   -548       C  
ATOM   6008  C   GLY B 409     -34.214   1.093   0.364  1.00 54.36           C  
ANISOU 6008  C   GLY B 409     5641   7602   7411   -500    659   -537       C  
ATOM   6009  O   GLY B 409     -34.990   0.130   0.422  1.00 53.94           O  
ANISOU 6009  O   GLY B 409     5538   7512   7446   -569    703   -569       O  
ATOM   6010  N   LEU B 410     -34.567   2.345   0.731  1.00 51.37           N  
ANISOU 6010  N   LEU B 410     5265   7293   6961   -449    655   -498       N  
ATOM   6011  CA  LEU B 410     -35.902   2.669   1.218  1.00 52.48           C  
ANISOU 6011  CA  LEU B 410     5342   7476   7122   -465    707   -495       C  
ATOM   6012  C   LEU B 410     -36.907   2.676   0.046  1.00 56.32           C  
ANISOU 6012  C   LEU B 410     5703   8049   7649   -489    668   -571       C  
ATOM   6013  O   LEU B 410     -38.022   2.186   0.227  1.00 55.98           O  
ANISOU 6013  O   LEU B 410     5583   8012   7673   -543    714   -595       O  
ATOM   6014  CB  LEU B 410     -35.905   4.012   1.986  1.00 52.86           C  
ANISOU 6014  CB  LEU B 410     5426   7557   7103   -400    724   -446       C  
ATOM   6015  CG  LEU B 410     -37.197   4.442   2.763  1.00 60.14           C  
ANISOU 6015  CG  LEU B 410     6290   8509   8053   -409    806   -445       C  
ATOM   6016  CD1 LEU B 410     -38.152   5.285   1.900  1.00 61.58           C  
ANISOU 6016  CD1 LEU B 410     6350   8771   8277   -371    772   -481       C  
ATOM   6017  CD2 LEU B 410     -37.901   3.271   3.482  1.00 62.37           C  
ANISOU 6017  CD2 LEU B 410     6557   8751   8390   -495    890   -437       C  
ATOM   6018  N   VAL B 411     -36.517   3.187  -1.160  1.00 52.61           N  
ANISOU 6018  N   VAL B 411     5205   7652   7131   -459    582   -602       N  
ATOM   6019  CA  VAL B 411     -37.444   3.172  -2.303  1.00 52.31           C  
ANISOU 6019  CA  VAL B 411     5044   7721   7110   -494    529   -663       C  
ATOM   6020  C   VAL B 411     -37.697   1.714  -2.740  1.00 56.54           C  
ANISOU 6020  C   VAL B 411     5540   8230   7711   -594    547   -756       C  
ATOM   6021  O   VAL B 411     -38.791   1.406  -3.209  1.00 56.78           O  
ANISOU 6021  O   VAL B 411     5461   8327   7785   -650    537   -808       O  
ATOM   6022  CB  VAL B 411     -37.087   4.084  -3.509  1.00 54.84           C  
ANISOU 6022  CB  VAL B 411     5337   8151   7348   -454    429   -659       C  
ATOM   6023  CG1 VAL B 411     -36.701   5.489  -3.073  1.00 53.33           C  
ANISOU 6023  CG1 VAL B 411     5186   7959   7119   -357    416   -568       C  
ATOM   6024  CG2 VAL B 411     -36.051   3.464  -4.432  1.00 54.46           C  
ANISOU 6024  CG2 VAL B 411     5336   8108   7250   -485    391   -719       C  
ATOM   6025  N   LEU B 412     -36.706   0.828  -2.555  1.00 52.81           N  
ANISOU 6025  N   LEU B 412     5149   7653   7265   -616    576   -776       N  
ATOM   6026  CA  LEU B 412     -36.849  -0.589  -2.881  1.00 53.79           C  
ANISOU 6026  CA  LEU B 412     5242   7714   7483   -708    608   -869       C  
ATOM   6027  C   LEU B 412     -37.855  -1.275  -1.977  1.00 59.15           C  
ANISOU 6027  C   LEU B 412     5886   8324   8264   -764    687   -848       C  
ATOM   6028  O   LEU B 412     -38.675  -2.046  -2.476  1.00 60.47           O  
ANISOU 6028  O   LEU B 412     5965   8504   8505   -850    699   -936       O  
ATOM   6029  CB  LEU B 412     -35.503  -1.316  -2.781  1.00 53.47           C  
ANISOU 6029  CB  LEU B 412     5288   7552   7475   -701    626   -878       C  
ATOM   6030  CG  LEU B 412     -34.595  -1.238  -3.992  1.00 58.80           C  
ANISOU 6030  CG  LEU B 412     5967   8282   8093   -696    571   -964       C  
ATOM   6031  CD1 LEU B 412     -33.352  -2.040  -3.737  1.00 59.40           C  
ANISOU 6031  CD1 LEU B 412     6115   8216   8238   -683    604   -966       C  
ATOM   6032  CD2 LEU B 412     -35.289  -1.774  -5.259  1.00 62.87           C  
ANISOU 6032  CD2 LEU B 412     6381   8887   8619   -791    549  -1115       C  
ATOM   6033  N   ILE B 413     -37.817  -0.985  -0.656  1.00 55.84           N  
ANISOU 6033  N   ILE B 413     5532   7845   7841   -727    744   -737       N  
ATOM   6034  CA  ILE B 413     -38.735  -1.622   0.279  1.00 56.89           C  
ANISOU 6034  CA  ILE B 413     5637   7921   8057   -789    831   -704       C  
ATOM   6035  C   ILE B 413     -40.156  -1.002   0.146  1.00 60.99           C  
ANISOU 6035  C   ILE B 413     6039   8554   8581   -800    838   -729       C  
ATOM   6036  O   ILE B 413     -41.120  -1.735   0.312  1.00 62.71           O  
ANISOU 6036  O   ILE B 413     6182   8755   8890   -881    889   -760       O  
ATOM   6037  CB  ILE B 413     -38.215  -1.690   1.756  1.00 59.64           C  
ANISOU 6037  CB  ILE B 413     6094   8180   8388   -770    896   -577       C  
ATOM   6038  CG1 ILE B 413     -38.601  -0.509   2.621  1.00 59.83           C  
ANISOU 6038  CG1 ILE B 413     6139   8276   8317   -714    922   -513       C  
ATOM   6039  CG2 ILE B 413     -36.723  -2.024   1.868  1.00 59.28           C  
ANISOU 6039  CG2 ILE B 413     6150   8037   8336   -739    868   -533       C  
ATOM   6040  CD1 ILE B 413     -39.680  -0.859   3.550  1.00 68.89           C  
ANISOU 6040  CD1 ILE B 413     7254   9419   9502   -772   1022   -475       C  
ATOM   6041  N   VAL B 414     -40.282   0.305  -0.178  1.00 55.76           N  
ANISOU 6041  N   VAL B 414     5351   7995   7839   -722    785   -712       N  
ATOM   6042  CA  VAL B 414     -41.578   0.986  -0.318  1.00 55.52           C  
ANISOU 6042  CA  VAL B 414     5196   8066   7834   -715    784   -721       C  
ATOM   6043  C   VAL B 414     -42.205   0.620  -1.679  1.00 60.24           C  
ANISOU 6043  C   VAL B 414     5669   8758   8460   -772    705   -813       C  
ATOM   6044  O   VAL B 414     -43.390   0.293  -1.728  1.00 60.39           O  
ANISOU 6044  O   VAL B 414     5570   8819   8556   -831    727   -848       O  
ATOM   6045  CB  VAL B 414     -41.482   2.518  -0.098  1.00 58.08           C  
ANISOU 6045  CB  VAL B 414     5533   8442   8093   -607    762   -661       C  
ATOM   6046  CG1 VAL B 414     -42.799   3.217  -0.444  1.00 58.41           C  
ANISOU 6046  CG1 VAL B 414     5421   8581   8191   -589    746   -669       C  
ATOM   6047  CG2 VAL B 414     -41.082   2.829   1.339  1.00 57.31           C  
ANISOU 6047  CG2 VAL B 414     5542   8269   7963   -576    855   -594       C  
ATOM   6048  N   GLY B 415     -41.398   0.649  -2.740  1.00 56.75           N  
ANISOU 6048  N   GLY B 415     5254   8358   7950   -764    617   -854       N  
ATOM   6049  CA  GLY B 415     -41.800   0.254  -4.088  1.00 57.88           C  
ANISOU 6049  CA  GLY B 415     5297   8611   8085   -835    537   -952       C  
ATOM   6050  C   GLY B 415     -42.101  -1.233  -4.172  1.00 63.07           C  
ANISOU 6050  C   GLY B 415     5924   9202   8838   -956    586  -1057       C  
ATOM   6051  O   GLY B 415     -43.060  -1.638  -4.837  1.00 63.58           O  
ANISOU 6051  O   GLY B 415     5865   9353   8940  -1039    556  -1138       O  
ATOM   6052  N   GLY B 416     -41.290  -2.038  -3.478  1.00 59.81           N  
ANISOU 6052  N   GLY B 416     5619   8631   8476   -967    661  -1051       N  
ATOM   6053  CA  GLY B 416     -41.484  -3.479  -3.361  1.00 60.84           C  
ANISOU 6053  CA  GLY B 416     5733   8651   8733  -1073    726  -1130       C  
ATOM   6054  C   GLY B 416     -42.789  -3.794  -2.658  1.00 66.63           C  
ANISOU 6054  C   GLY B 416     6381   9371   9564  -1132    794  -1108       C  
ATOM   6055  O   GLY B 416     -43.503  -4.712  -3.065  1.00 68.51           O  
ANISOU 6055  O   GLY B 416     6531   9602   9898  -1241    811  -1207       O  
ATOM   6056  N   TYR B 417     -43.141  -2.993  -1.624  1.00 62.53           N  
ANISOU 6056  N   TYR B 417     5880   8857   9020  -1066    838   -991       N  
ATOM   6057  CA  TYR B 417     -44.387  -3.139  -0.869  1.00 62.91           C  
ANISOU 6057  CA  TYR B 417     5845   8907   9151  -1113    917   -963       C  
ATOM   6058  C   TYR B 417     -45.595  -2.941  -1.802  1.00 65.88           C  
ANISOU 6058  C   TYR B 417     6048   9427   9555  -1160    857  -1044       C  
ATOM   6059  O   TYR B 417     -46.471  -3.798  -1.838  1.00 66.15           O  
ANISOU 6059  O   TYR B 417     5989   9447   9696  -1265    899  -1104       O  
ATOM   6060  CB  TYR B 417     -44.433  -2.152   0.325  1.00 63.51           C  
ANISOU 6060  CB  TYR B 417     5974   8983   9173  -1028    978   -844       C  
ATOM   6061  CG  TYR B 417     -45.797  -2.046   0.981  1.00 66.78           C  
ANISOU 6061  CG  TYR B 417     6279   9436   9657  -1065   1061   -829       C  
ATOM   6062  CD1 TYR B 417     -46.200  -2.960   1.953  1.00 69.74           C  
ANISOU 6062  CD1 TYR B 417     6666   9721  10112  -1150   1177   -796       C  
ATOM   6063  CD2 TYR B 417     -46.681  -1.028   0.636  1.00 68.03           C  
ANISOU 6063  CD2 TYR B 417     6316   9719   9815  -1014   1026   -838       C  
ATOM   6064  CE1 TYR B 417     -47.456  -2.870   2.556  1.00 70.67           C  
ANISOU 6064  CE1 TYR B 417     6677   9881  10293  -1191   1266   -788       C  
ATOM   6065  CE2 TYR B 417     -47.940  -0.932   1.227  1.00 70.36           C  
ANISOU 6065  CE2 TYR B 417     6495  10048  10193  -1045   1111   -833       C  
ATOM   6066  CZ  TYR B 417     -48.322  -1.854   2.188  1.00 79.67           C  
ANISOU 6066  CZ  TYR B 417     7689  11146  11437  -1136   1235   -815       C  
ATOM   6067  OH  TYR B 417     -49.571  -1.767   2.757  1.00 84.84           O  
ANISOU 6067  OH  TYR B 417     8222  11841  12173  -1174   1330   -816       O  
ATOM   6068  N   PHE B 418     -45.612  -1.829  -2.569  1.00 61.61           N  
ANISOU 6068  N   PHE B 418     5461   9024   8925  -1086    755  -1037       N  
ATOM   6069  CA  PHE B 418     -46.696  -1.486  -3.483  1.00 62.77           C  
ANISOU 6069  CA  PHE B 418     5437   9328   9085  -1117    672  -1084       C  
ATOM   6070  C   PHE B 418     -46.797  -2.465  -4.640  1.00 68.25           C  
ANISOU 6070  C   PHE B 418     6068  10075   9789  -1239    610  -1222       C  
ATOM   6071  O   PHE B 418     -47.909  -2.724  -5.101  1.00 69.61           O  
ANISOU 6071  O   PHE B 418     6087  10344  10017  -1318    577  -1280       O  
ATOM   6072  CB  PHE B 418     -46.575  -0.044  -3.993  1.00 63.92           C  
ANISOU 6072  CB  PHE B 418     5556   9592   9137  -1003    573  -1012       C  
ATOM   6073  CG  PHE B 418     -46.791   1.007  -2.927  1.00 64.65           C  
ANISOU 6073  CG  PHE B 418     5664   9649   9251   -894    638   -905       C  
ATOM   6074  CD1 PHE B 418     -47.885   0.941  -2.069  1.00 69.16           C  
ANISOU 6074  CD1 PHE B 418     6148  10201   9930   -915    736   -892       C  
ATOM   6075  CD2 PHE B 418     -45.928   2.088  -2.810  1.00 64.73           C  
ANISOU 6075  CD2 PHE B 418     5767   9650   9176   -779    609   -829       C  
ATOM   6076  CE1 PHE B 418     -48.083   1.914  -1.085  1.00 69.70           C  
ANISOU 6076  CE1 PHE B 418     6227  10240  10017   -822    813   -818       C  
ATOM   6077  CE2 PHE B 418     -46.134   3.066  -1.835  1.00 67.03           C  
ANISOU 6077  CE2 PHE B 418     6070   9905   9495   -688    678   -755       C  
ATOM   6078  CZ  PHE B 418     -47.205   2.972  -0.978  1.00 66.57           C  
ANISOU 6078  CZ  PHE B 418     5927   9828   9539   -710    783   -756       C  
ATOM   6079  N   LEU B 419     -45.669  -3.051  -5.075  1.00 64.23           N  
ANISOU 6079  N   LEU B 419     5669   9500   9237  -1261    601  -1285       N  
ATOM   6080  CA  LEU B 419     -45.705  -4.069  -6.123  1.00 65.37           C  
ANISOU 6080  CA  LEU B 419     5762   9678   9399  -1389    566  -1446       C  
ATOM   6081  C   LEU B 419     -46.335  -5.357  -5.561  1.00 70.61           C  
ANISOU 6081  C   LEU B 419     6388  10208  10230  -1503    671  -1511       C  
ATOM   6082  O   LEU B 419     -47.269  -5.856  -6.175  1.00 72.27           O  
ANISOU 6082  O   LEU B 419     6468  10498  10493  -1618    645  -1620       O  
ATOM   6083  CB  LEU B 419     -44.314  -4.340  -6.738  1.00 64.78           C  
ANISOU 6083  CB  LEU B 419     5805   9563   9246  -1378    544  -1509       C  
ATOM   6084  CG  LEU B 419     -43.763  -3.278  -7.703  1.00 68.37           C  
ANISOU 6084  CG  LEU B 419     6268  10184   9526  -1314    426  -1487       C  
ATOM   6085  CD1 LEU B 419     -42.278  -3.431  -7.871  1.00 67.13           C  
ANISOU 6085  CD1 LEU B 419     6250   9945   9313  -1272    442  -1508       C  
ATOM   6086  CD2 LEU B 419     -44.452  -3.326  -9.075  1.00 71.30           C  
ANISOU 6086  CD2 LEU B 419     6504  10764   9823  -1419    319  -1601       C  
ATOM   6087  N   ILE B 420     -45.891  -5.842  -4.369  1.00 66.83           N  
ANISOU 6087  N   ILE B 420     6017   9539   9835  -1477    785  -1431       N  
ATOM   6088  CA  ILE B 420     -46.432  -7.049  -3.703  1.00 68.08           C  
ANISOU 6088  CA  ILE B 420     6153   9551  10164  -1582    895  -1455       C  
ATOM   6089  C   ILE B 420     -47.932  -6.871  -3.428  1.00 73.51           C  
ANISOU 6089  C   ILE B 420     6692  10327  10913  -1632    916  -1440       C  
ATOM   6090  O   ILE B 420     -48.715  -7.771  -3.737  1.00 75.68           O  
ANISOU 6090  O   ILE B 420     6864  10587  11302  -1762    941  -1543       O  
ATOM   6091  CB  ILE B 420     -45.657  -7.404  -2.397  1.00 70.62           C  
ANISOU 6091  CB  ILE B 420     6620   9676  10535  -1533    997  -1326       C  
ATOM   6092  CG1 ILE B 420     -44.229  -7.907  -2.721  1.00 70.53           C  
ANISOU 6092  CG1 ILE B 420     6725   9549  10524  -1510    985  -1365       C  
ATOM   6093  CG2 ILE B 420     -46.427  -8.431  -1.531  1.00 72.25           C  
ANISOU 6093  CG2 ILE B 420     6792   9753  10907  -1633   1115  -1295       C  
ATOM   6094  CD1 ILE B 420     -43.232  -7.764  -1.580  1.00 74.91           C  
ANISOU 6094  CD1 ILE B 420     7427   9973  11061  -1417   1032  -1207       C  
ATOM   6095  N   ARG B 421     -48.330  -5.710  -2.861  1.00 67.92           N  
ANISOU 6095  N   ARG B 421     5962   9706  10140  -1532    910  -1325       N  
ATOM   6096  CA  ARG B 421     -49.730  -5.390  -2.566  1.00 67.84           C  
ANISOU 6096  CA  ARG B 421     5798   9785  10195  -1560    935  -1306       C  
ATOM   6097  C   ARG B 421     -50.549  -5.337  -3.852  1.00 73.09           C  
ANISOU 6097  C   ARG B 421     6291  10623  10857  -1629    817  -1417       C  
ATOM   6098  O   ARG B 421     -51.712  -5.734  -3.856  1.00 74.06           O  
ANISOU 6098  O   ARG B 421     6266  10791  11084  -1719    840  -1460       O  
ATOM   6099  CB  ARG B 421     -49.841  -4.060  -1.796  1.00 65.56           C  
ANISOU 6099  CB  ARG B 421     5523   9544   9843  -1425    955  -1176       C  
ATOM   6100  CG  ARG B 421     -49.486  -4.167  -0.306  1.00 72.76           C  
ANISOU 6100  CG  ARG B 421     6559  10318  10768  -1395   1095  -1069       C  
ATOM   6101  CD  ARG B 421     -50.507  -4.959   0.524  1.00 82.08           C  
ANISOU 6101  CD  ARG B 421     7666  11441  12079  -1502   1224  -1062       C  
ATOM   6102  NE  ARG B 421     -51.890  -4.562   0.239  1.00 86.93           N  
ANISOU 6102  NE  ARG B 421     8083  12183  12765  -1529   1215  -1101       N  
ATOM   6103  CZ  ARG B 421     -52.517  -3.543   0.818  1.00104.44           C  
ANISOU 6103  CZ  ARG B 421    10233  14471  14979  -1452   1258  -1043       C  
ATOM   6104  NH1 ARG B 421     -51.902  -2.810   1.739  1.00 94.13           N  
ANISOU 6104  NH1 ARG B 421     9051  13126  13589  -1353   1318   -955       N  
ATOM   6105  NH2 ARG B 421     -53.765  -3.250   0.483  1.00 93.45           N  
ANISOU 6105  NH2 ARG B 421     8642  13188  13676  -1477   1244  -1080       N  
ATOM   6106  N   GLY B 422     -49.917  -4.871  -4.928  1.00 70.05           N  
ANISOU 6106  N   GLY B 422     5926  10342  10346  -1596    693  -1459       N  
ATOM   6107  CA  GLY B 422     -50.515  -4.800  -6.253  1.00 71.21           C  
ANISOU 6107  CA  GLY B 422     5928  10681  10449  -1669    560  -1557       C  
ATOM   6108  C   GLY B 422     -50.794  -6.177  -6.822  1.00 76.36           C  
ANISOU 6108  C   GLY B 422     6526  11306  11182  -1844    576  -1733       C  
ATOM   6109  O   GLY B 422     -51.871  -6.387  -7.384  1.00 77.84           O  
ANISOU 6109  O   GLY B 422     6544  11625  11407  -1944    518  -1808       O  
ATOM   6110  N   VAL B 423     -49.844  -7.143  -6.646  1.00 72.18           N  
ANISOU 6110  N   VAL B 423     6130  10597  10696  -1884    656  -1800       N  
ATOM   6111  CA  VAL B 423     -50.014  -8.527  -7.129  1.00 73.45           C  
ANISOU 6111  CA  VAL B 423     6250  10690  10969  -2051    692  -1981       C  
ATOM   6112  C   VAL B 423     -51.070  -9.249  -6.271  1.00 78.02           C  
ANISOU 6112  C   VAL B 423     6745  11165  11735  -2137    801  -1967       C  
ATOM   6113  O   VAL B 423     -51.837 -10.036  -6.820  1.00 79.20           O  
ANISOU 6113  O   VAL B 423     6773  11344  11975  -2289    796  -2111       O  
ATOM   6114  CB  VAL B 423     -48.712  -9.387  -7.301  1.00 76.67           C  
ANISOU 6114  CB  VAL B 423     6803  10928  11400  -2070    745  -2071       C  
ATOM   6115  CG1 VAL B 423     -47.631  -8.642  -8.079  1.00 74.50           C  
ANISOU 6115  CG1 VAL B 423     6605  10763  10937  -1991    649  -2088       C  
ATOM   6116  CG2 VAL B 423     -48.167  -9.927  -5.980  1.00 75.96           C  
ANISOU 6116  CG2 VAL B 423     6845  10585  11430  -2012    878  -1950       C  
ATOM   6117  N   MET B 424     -51.127  -8.957  -4.955  1.00 74.91           N  
ANISOU 6117  N   MET B 424     6409  10663  11389  -2052    899  -1800       N  
ATOM   6118  CA  MET B 424     -52.107  -9.536  -4.028  1.00 76.98           C  
ANISOU 6118  CA  MET B 424     6599  10836  11812  -2127   1016  -1759       C  
ATOM   6119  C   MET B 424     -53.534  -9.098  -4.406  1.00 81.60           C  
ANISOU 6119  C   MET B 424     6973  11611  12420  -2176    960  -1788       C  
ATOM   6120  O   MET B 424     -54.457  -9.916  -4.380  1.00 82.38           O  
ANISOU 6120  O   MET B 424     6953  11686  12661  -2313   1011  -1862       O  
ATOM   6121  CB  MET B 424     -51.789  -9.143  -2.580  1.00 78.81           C  
ANISOU 6121  CB  MET B 424     6949  10953  12042  -2021   1126  -1572       C  
ATOM   6122  CG  MET B 424     -50.667  -9.951  -1.960  1.00 82.76           C  
ANISOU 6122  CG  MET B 424     7622  11233  12591  -2018   1208  -1527       C  
ATOM   6123  SD  MET B 424     -50.115  -9.257  -0.376  1.00 86.80           S  
ANISOU 6123  SD  MET B 424     8285  11666  13030  -1886   1299  -1301       S  
ATOM   6124  CE  MET B 424     -51.401  -9.881   0.742  1.00 84.94           C  
ANISOU 6124  CE  MET B 424     7957  11375  12942  -1998   1450  -1234       C  
ATOM   6125  N   THR B 425     -53.694  -7.813  -4.792  1.00 77.59           N  
ANISOU 6125  N   THR B 425     6412  11284  11784  -2065    852  -1726       N  
ATOM   6126  CA  THR B 425     -54.960  -7.228  -5.247  1.00 78.43           C  
ANISOU 6126  CA  THR B 425     6306  11585  11908  -2085    772  -1731       C  
ATOM   6127  C   THR B 425     -55.341  -7.890  -6.591  1.00 84.62           C  
ANISOU 6127  C   THR B 425     6969  12499  12685  -2237    657  -1908       C  
ATOM   6128  O   THR B 425     -56.505  -8.249  -6.778  1.00 86.57           O  
ANISOU 6128  O   THR B 425     7034  12825  13033  -2348    646  -1970       O  
ATOM   6129  CB  THR B 425     -54.838  -5.695  -5.320  1.00 79.58           C  
ANISOU 6129  CB  THR B 425     6445  11857  11936  -1915    686  -1602       C  
ATOM   6130  OG1 THR B 425     -54.496  -5.208  -4.022  1.00 77.79           O  
ANISOU 6130  OG1 THR B 425     6338  11500  11718  -1798    809  -1471       O  
ATOM   6131  CG2 THR B 425     -56.115  -5.019  -5.792  1.00 76.76           C  
ANISOU 6131  CG2 THR B 425     5856  11689  11621  -1915    598  -1581       C  
ATOM   6132  N   LEU B 426     -54.352  -8.093  -7.492  1.00 80.54           N  
ANISOU 6132  N   LEU B 426     6550  12002  12048  -2253    582  -2000       N  
ATOM   6133  CA  LEU B 426     -54.549  -8.766  -8.779  1.00 81.77           C  
ANISOU 6133  CA  LEU B 426     6617  12283  12169  -2410    484  -2194       C  
ATOM   6134  C   LEU B 426     -54.999 -10.221  -8.529  1.00 88.12           C  
ANISOU 6134  C   LEU B 426     7385  12935  13163  -2584    598  -2339       C  
ATOM   6135  O   LEU B 426     -55.942 -10.668  -9.171  1.00 89.05           O  
ANISOU 6135  O   LEU B 426     7339  13171  13325  -2734    542  -2471       O  
ATOM   6136  CB  LEU B 426     -53.270  -8.691  -9.648  1.00 80.54           C  
ANISOU 6136  CB  LEU B 426     6594  12165  11844  -2384    413  -2263       C  
ATOM   6137  CG  LEU B 426     -53.339  -9.163 -11.125  1.00 86.22           C  
ANISOU 6137  CG  LEU B 426     7231  13063  12465  -2543    299  -2472       C  
ATOM   6138  CD1 LEU B 426     -54.527  -8.574 -11.882  1.00 87.74           C  
ANISOU 6138  CD1 LEU B 426     7210  13537  12590  -2599    144  -2463       C  
ATOM   6139  CD2 LEU B 426     -52.068  -8.818 -11.859  1.00 86.64           C  
ANISOU 6139  CD2 LEU B 426     7419  13167  12334  -2491    243  -2506       C  
ATOM   6140  N   PHE B 427     -54.387 -10.910  -7.536  1.00 85.99           N  
ANISOU 6140  N   PHE B 427     7259  12403  13012  -2564    753  -2297       N  
ATOM   6141  CA  PHE B 427     -54.733 -12.271  -7.098  1.00 88.27           C  
ANISOU 6141  CA  PHE B 427     7530  12499  13511  -2712    881  -2391       C  
ATOM   6142  C   PHE B 427     -56.160 -12.314  -6.568  1.00 94.12           C  
ANISOU 6142  C   PHE B 427     8098  13284  14380  -2782    923  -2349       C  
ATOM   6143  O   PHE B 427     -56.896 -13.259  -6.854  1.00 95.77           O  
ANISOU 6143  O   PHE B 427     8190  13470  14728  -2954    951  -2488       O  
ATOM   6144  CB  PHE B 427     -53.775 -12.746  -5.981  1.00 89.64           C  
ANISOU 6144  CB  PHE B 427     7893  12395  13771  -2643   1024  -2283       C  
ATOM   6145  CG  PHE B 427     -53.104 -14.091  -6.162  1.00 93.12           C  
ANISOU 6145  CG  PHE B 427     8409  12619  14354  -2750   1102  -2422       C  
ATOM   6146  CD1 PHE B 427     -53.856 -15.240  -6.400  1.00 99.06           C  
ANISOU 6146  CD1 PHE B 427     9048  13299  15290  -2938   1154  -2577       C  
ATOM   6147  CD2 PHE B 427     -51.725 -14.224  -6.015  1.00 94.70           C  
ANISOU 6147  CD2 PHE B 427     8787  12666  14530  -2661   1133  -2389       C  
ATOM   6148  CE1 PHE B 427     -53.232 -16.486  -6.561  1.00101.17           C  
ANISOU 6148  CE1 PHE B 427     9378  13340  15721  -3034   1236  -2711       C  
ATOM   6149  CE2 PHE B 427     -51.103 -15.467  -6.177  1.00 98.82           C  
ANISOU 6149  CE2 PHE B 427     9363  12968  15216  -2750   1211  -2515       C  
ATOM   6150  CZ  PHE B 427     -51.862 -16.591  -6.439  1.00 99.20           C  
ANISOU 6150  CZ  PHE B 427     9298  12936  15456  -2935   1266  -2676       C  
ATOM   6151  N   SER B 428     -56.537 -11.280  -5.783  1.00 90.26           N  
ANISOU 6151  N   SER B 428     7588  12854  13853  -2649    937  -2165       N  
ATOM   6152  CA  SER B 428     -57.846 -11.117  -5.154  1.00 91.24           C  
ANISOU 6152  CA  SER B 428     7548  13027  14092  -2683    993  -2102       C  
ATOM   6153  C   SER B 428     -58.933 -10.888  -6.195  1.00 96.24           C  
ANISOU 6153  C   SER B 428     7949  13900  14717  -2772    854  -2204       C  
ATOM   6154  O   SER B 428     -59.924 -11.622  -6.191  1.00 96.54           O  
ANISOU 6154  O   SER B 428     7838  13938  14905  -2922    894  -2287       O  
ATOM   6155  CB  SER B 428     -57.819  -9.961  -4.158  1.00 94.29           C  
ANISOU 6155  CB  SER B 428     7980  13423  14422  -2507   1042  -1903       C  
ATOM   6156  OG  SER B 428     -58.974  -9.954  -3.335  1.00108.08           O  
ANISOU 6156  OG  SER B 428     9588  15177  16300  -2544   1141  -1846       O  
ATOM   6157  N   ILE B 429     -58.731  -9.909  -7.113  1.00 93.12           N  
ANISOU 6157  N   ILE B 429     7520  13710  14149  -2689    685  -2194       N  
ATOM   6158  CA  ILE B 429     -59.705  -9.588  -8.162  1.00 95.20           C  
ANISOU 6158  CA  ILE B 429     7560  14231  14381  -2765    524  -2262       C  
ATOM   6159  C   ILE B 429     -59.869 -10.770  -9.141  1.00101.70           C  
ANISOU 6159  C   ILE B 429     8320  15092  15229  -2983    477  -2495       C  
ATOM   6160  O   ILE B 429     -60.976 -10.979  -9.613  1.00103.49           O  
ANISOU 6160  O   ILE B 429     8336  15471  15513  -3107    405  -2573       O  
ATOM   6161  CB  ILE B 429     -59.440  -8.240  -8.901  1.00 97.77           C  
ANISOU 6161  CB  ILE B 429     7863  14768  14516  -2626    348  -2165       C  
ATOM   6162  CG1 ILE B 429     -58.177  -8.251  -9.778  1.00 98.00           C  
ANISOU 6162  CG1 ILE B 429     8057  14822  14356  -2612    268  -2232       C  
ATOM   6163  CG2 ILE B 429     -59.439  -7.054  -7.940  1.00 96.52           C  
ANISOU 6163  CG2 ILE B 429     7730  14573  14368  -2424    399  -1955       C  
ATOM   6164  CD1 ILE B 429     -58.473  -8.226 -11.281  1.00111.15           C  
ANISOU 6164  CD1 ILE B 429     9596  16751  15885  -2729     76  -2353       C  
ATOM   6165  N   LYS B 430     -58.800 -11.559  -9.400  1.00 98.12           N  
ANISOU 6165  N   LYS B 430     8038  14494  14748  -3033    526  -2614       N  
ATOM   6166  CA  LYS B 430     -58.837 -12.731 -10.287  1.00 99.60           C  
ANISOU 6166  CA  LYS B 430     8184  14685  14974  -3241    508  -2863       C  
ATOM   6167  C   LYS B 430     -59.618 -13.909  -9.680  1.00106.10           C  
ANISOU 6167  C   LYS B 430     8928  15336  16049  -3398    649  -2945       C  
ATOM   6168  O   LYS B 430     -60.199 -14.694 -10.431  1.00107.11           O  
ANISOU 6168  O   LYS B 430     8928  15533  16237  -3593    611  -3147       O  
ATOM   6169  CB  LYS B 430     -57.414 -13.200 -10.621  1.00100.03           C  
ANISOU 6169  CB  LYS B 430     8445  14606  14956  -3228    543  -2961       C  
ATOM   6170  CG  LYS B 430     -56.815 -12.541 -11.846  1.00105.22           C  
ANISOU 6170  CG  LYS B 430     9123  15494  15362  -3202    379  -3019       C  
ATOM   6171  CD  LYS B 430     -55.483 -13.186 -12.194  1.00110.81           C  
ANISOU 6171  CD  LYS B 430    10014  16059  16031  -3214    437  -3151       C  
ATOM   6172  CE  LYS B 430     -55.124 -13.005 -13.645  1.00118.37           C  
ANISOU 6172  CE  LYS B 430    10943  17261  16772  -3300    296  -3319       C  
ATOM   6173  NZ  LYS B 430     -54.252 -11.822 -13.856  1.00126.21           N  
ANISOU 6173  NZ  LYS B 430    12040  18373  17541  -3129    205  -3171       N  
ATOM   6174  N   SER B 431     -59.595 -14.050  -8.334  1.00103.63           N  
ANISOU 6174  N   SER B 431     8694  14802  15877  -3324    812  -2793       N  
ATOM   6175  CA  SER B 431     -60.251 -15.139  -7.602  1.00105.89           C  
ANISOU 6175  CA  SER B 431     8926  14899  16407  -3461    965  -2827       C  
ATOM   6176  C   SER B 431     -61.691 -14.795  -7.202  1.00113.99           C  
ANISOU 6176  C   SER B 431     9738  16048  17525  -3494    971  -2753       C  
ATOM   6177  O   SER B 431     -62.602 -15.557  -7.528  1.00115.76           O  
ANISOU 6177  O   SER B 431     9800  16297  17889  -3678    979  -2888       O  
ATOM   6178  CB  SER B 431     -59.448 -15.511  -6.359  1.00107.60           C  
ANISOU 6178  CB  SER B 431     9343  14825  16717  -3378   1139  -2688       C  
ATOM   6179  OG  SER B 431     -58.193 -16.072  -6.706  1.00115.76           O  
ANISOU 6179  OG  SER B 431    10548  15713  17723  -3370   1149  -2774       O  
ATOM   6180  N   ASN B 432     -61.887 -13.661  -6.489  1.00111.75           N  
ANISOU 6180  N   ASN B 432     9449  15835  17176  -3320    974  -2549       N  
ATOM   6181  CA  ASN B 432     -63.178 -13.172  -5.994  1.00113.70           C  
ANISOU 6181  CA  ASN B 432     9495  16191  17515  -3317    997  -2462       C  
ATOM   6182  C   ASN B 432     -64.112 -12.795  -7.153  1.00122.28           C  
ANISOU 6182  C   ASN B 432    10339  17561  18561  -3392    809  -2559       C  
ATOM   6183  O   ASN B 432     -65.260 -13.245  -7.174  1.00123.77           O  
ANISOU 6183  O   ASN B 432    10324  17804  18898  -3532    825  -2623       O  
ATOM   6184  CB  ASN B 432     -62.961 -11.978  -5.050  1.00113.03           C  
ANISOU 6184  CB  ASN B 432     9483  16106  17359  -3101   1048  -2245       C  
ATOM   6185  CG  ASN B 432     -64.187 -11.406  -4.373  1.00146.04           C  
ANISOU 6185  CG  ASN B 432    13470  20370  21648  -3076   1106  -2150       C  
ATOM   6186  OD1 ASN B 432     -65.214 -12.073  -4.172  1.00146.51           O  
ANISOU 6186  OD1 ASN B 432    13370  20420  21878  -3224   1177  -2207       O  
ATOM   6187  ND2 ASN B 432     -64.076 -10.153  -3.956  1.00137.20           N  
ANISOU 6187  ND2 ASN B 432    12363  19322  20446  -2887   1092  -2004       N  
ATOM   6188  N   HIS B 433     -63.613 -12.006  -8.124  1.00120.75           N  
ANISOU 6188  N   HIS B 433    10162  17551  18167  -3311    629  -2563       N  
ATOM   6189  CA  HIS B 433     -64.391 -11.581  -9.287  1.00123.50           C  
ANISOU 6189  CA  HIS B 433    10289  18193  18444  -3377    425  -2628       C  
ATOM   6190  C   HIS B 433     -63.720 -12.057 -10.596  1.00130.03           C  
ANISOU 6190  C   HIS B 433    11173  19120  19114  -3492    293  -2817       C  
ATOM   6191  O   HIS B 433     -63.131 -11.236 -11.303  1.00127.84           O  
ANISOU 6191  O   HIS B 433    10948  18993  18631  -3395    152  -2769       O  
ATOM   6192  CB  HIS B 433     -64.578 -10.051  -9.296  1.00123.69           C  
ANISOU 6192  CB  HIS B 433    10238  18387  18370  -3178    313  -2434       C  
ATOM   6193  CG  HIS B 433     -65.063  -9.465  -8.008  1.00126.74           C  
ANISOU 6193  CG  HIS B 433    10595  18670  18889  -3044    457  -2263       C  
ATOM   6194  ND1 HIS B 433     -66.331  -9.736  -7.521  1.00130.55           N  
ANISOU 6194  ND1 HIS B 433    10867  19169  19569  -3125    530  -2265       N  
ATOM   6195  CD2 HIS B 433     -64.447  -8.599  -7.171  1.00126.64           C  
ANISOU 6195  CD2 HIS B 433    10731  18555  18831  -2845    538  -2101       C  
ATOM   6196  CE1 HIS B 433     -66.436  -9.048  -6.395  1.00129.05           C  
ANISOU 6196  CE1 HIS B 433    10707  18885  19441  -2974    664  -2110       C  
ATOM   6197  NE2 HIS B 433     -65.330  -8.345  -6.145  1.00127.05           N  
ANISOU 6197  NE2 HIS B 433    10669  18559  19045  -2805    671  -2011       N  
ATOM   6198  N   PRO B 434     -63.819 -13.364 -10.962  1.00131.42           N  
ANISOU 6198  N   PRO B 434    11330  19220  19382  -3709    339  -3039       N  
ATOM   6199  CA  PRO B 434     -63.179 -13.840 -12.208  1.00133.02           C  
ANISOU 6199  CA  PRO B 434    11585  19521  19434  -3831    233  -3249       C  
ATOM   6200  C   PRO B 434     -63.599 -13.082 -13.477  1.00141.32           C  
ANISOU 6200  C   PRO B 434    12475  20939  20279  -3864    -13  -3271       C  
ATOM   6201  O   PRO B 434     -62.806 -12.978 -14.414  1.00140.22           O  
ANISOU 6201  O   PRO B 434    12424  20916  19938  -3888   -113  -3368       O  
ATOM   6202  CB  PRO B 434     -63.628 -15.302 -12.290  1.00136.84           C  
ANISOU 6202  CB  PRO B 434    12007  19876  20111  -4072    331  -3480       C  
ATOM   6203  CG  PRO B 434     -63.909 -15.694 -10.896  1.00140.50           C  
ANISOU 6203  CG  PRO B 434    12503  20071  20808  -4033    534  -3359       C  
ATOM   6204  CD  PRO B 434     -64.499 -14.475 -10.263  1.00134.91           C  
ANISOU 6204  CD  PRO B 434    11705  19478  20076  -3858    501  -3116       C  
ATOM   6205  N   GLY B 435     -64.829 -12.558 -13.480  1.00142.17           N  
ANISOU 6205  N   GLY B 435    12347  21228  20443  -3864   -105  -3173       N  
ATOM   6206  CA  GLY B 435     -65.408 -11.809 -14.592  1.00144.40           C  
ANISOU 6206  CA  GLY B 435    12439  21867  20561  -3893   -350  -3150       C  
ATOM   6207  C   GLY B 435     -65.102 -10.321 -14.632  1.00148.38           C  
ANISOU 6207  C   GLY B 435    12967  22494  20916  -3660   -465  -2899       C  
ATOM   6208  O   GLY B 435     -66.013  -9.519 -14.865  1.00149.42           O  
ANISOU 6208  O   GLY B 435    12884  22832  21055  -3615   -605  -2765       O  
ATOM   6209  N   LEU B 436     -63.819  -9.937 -14.425  1.00142.85           N  
ANISOU 6209  N   LEU B 436    12517  21665  20094  -3511   -409  -2832       N  
ATOM   6210  CA  LEU B 436     -63.368  -8.543 -14.501  1.00141.63           C  
ANISOU 6210  CA  LEU B 436    12412  21606  19796  -3295   -510  -2606       C  
ATOM   6211  C   LEU B 436     -62.366  -8.388 -15.649  1.00146.66           C  
ANISOU 6211  C   LEU B 436    13168  22396  20158  -3327   -640  -2676       C  
ATOM   6212  O   LEU B 436     -62.505  -7.478 -16.467  1.00146.76           O  
ANISOU 6212  O   LEU B 436    13085  22670  20007  -3290   -838  -2567       O  
ATOM   6213  CB  LEU B 436     -62.764  -8.046 -13.173  1.00139.12           C  
ANISOU 6213  CB  LEU B 436    12270  21018  19570  -3079   -333  -2438       C  
ATOM   6214  CG  LEU B 436     -63.732  -7.622 -12.057  1.00143.90           C  
ANISOU 6214  CG  LEU B 436    12745  21539  20393  -2983   -234  -2292       C  
ATOM   6215  CD1 LEU B 436     -62.966  -7.172 -10.830  1.00141.50           C  
ANISOU 6215  CD1 LEU B 436    12644  20991  20129  -2790    -63  -2153       C  
ATOM   6216  CD2 LEU B 436     -64.647  -6.482 -12.496  1.00147.81           C  
ANISOU 6216  CD2 LEU B 436    13001  22276  20886  -2904   -411  -2137       C  
ATOM   6217  N   LEU B 437     -61.371  -9.295 -15.713  1.00143.75           N  
ANISOU 6217  N   LEU B 437    13000  21867  19750  -3401   -527  -2856       N  
ATOM   6218  CA  LEU B 437     -60.362  -9.367 -16.778  1.00144.07           C  
ANISOU 6218  CA  LEU B 437    13162  22032  19545  -3460   -611  -2975       C  
ATOM   6219  C   LEU B 437     -60.948 -10.150 -17.964  1.00151.78           C  
ANISOU 6219  C   LEU B 437    13985  23247  20437  -3726   -728  -3218       C  
ATOM   6220  O   LEU B 437     -60.397 -10.133 -19.068  1.00151.76           O  
ANISOU 6220  O   LEU B 437    14020  23447  20196  -3814   -841  -3325       O  
ATOM   6221  CB  LEU B 437     -59.060 -10.024 -16.263  1.00142.31           C  
ANISOU 6221  CB  LEU B 437    13203  21517  19351  -3420   -424  -3069       C  
ATOM   6222  CG  LEU B 437     -59.084 -11.537 -15.965  1.00148.01           C  
ANISOU 6222  CG  LEU B 437    13960  22014  20262  -3587   -258  -3309       C  
ATOM   6223  CD1 LEU B 437     -57.758 -12.177 -16.313  1.00147.54           C  
ANISOU 6223  CD1 LEU B 437    14104  21827  20128  -3621   -175  -3479       C  
ATOM   6224  CD2 LEU B 437     -59.452 -11.817 -14.514  1.00149.47           C  
ANISOU 6224  CD2 LEU B 437    14169  21912  20712  -3504    -78  -3196       C  
ATOM   6225  N   SER B 438     -62.076 -10.840 -17.701  1.00151.07           N  
ANISOU 6225  N   SER B 438    13721  23137  20543  -3862   -695  -3309       N  
ATOM   6226  CA  SER B 438     -62.846 -11.656 -18.635  1.00154.49           C  
ANISOU 6226  CA  SER B 438    13976  23774  20948  -4129   -791  -3547       C  
ATOM   6227  C   SER B 438     -63.935 -10.811 -19.339  1.00161.41           C  
ANISOU 6227  C   SER B 438    14592  25014  21724  -4155  -1036  -3414       C  
ATOM   6228  O   SER B 438     -64.765 -11.359 -20.076  1.00163.93           O  
ANISOU 6228  O   SER B 438    14721  25538  22029  -4374  -1141  -3576       O  
ATOM   6229  CB  SER B 438     -63.478 -12.832 -17.892  1.00158.97           C  
ANISOU 6229  CB  SER B 438    14489  24107  21806  -4257   -618  -3696       C  
ATOM   6230  OG  SER B 438     -62.550 -13.476 -17.033  1.00164.95           O  
ANISOU 6230  OG  SER B 438    15473  24505  22695  -4202   -394  -3753       O  
ATOM   6231  N   GLU B 439     -63.926  -9.477 -19.109  1.00156.89           N  
ANISOU 6231  N   GLU B 439    14003  24514  21093  -3932  -1127  -3117       N  
ATOM   6232  CA  GLU B 439     -64.870  -8.535 -19.712  1.00158.37           C  
ANISOU 6232  CA  GLU B 439    13946  25020  21208  -3915  -1363  -2938       C  
ATOM   6233  C   GLU B 439     -64.110  -7.520 -20.577  1.00161.95           C  
ANISOU 6233  C   GLU B 439    14472  25692  21370  -3825  -1536  -2792       C  
ATOM   6234  O   GLU B 439     -63.185  -6.856 -20.100  1.00158.89           O  
ANISOU 6234  O   GLU B 439    14270  25148  20953  -3620  -1463  -2639       O  
ATOM   6235  CB  GLU B 439     -65.740  -7.840 -18.647  1.00159.04           C  
ANISOU 6235  CB  GLU B 439    13892  24990  21545  -3737  -1316  -2704       C  
ATOM   6236  CG  GLU B 439     -66.825  -8.743 -18.080  1.00169.90           C  
ANISOU 6236  CG  GLU B 439    15102  26272  23179  -3872  -1214  -2829       C  
ATOM   6237  CD  GLU B 439     -68.046  -8.043 -17.513  1.00186.59           C  
ANISOU 6237  CD  GLU B 439    16970  28426  25499  -3766  -1251  -2627       C  
ATOM   6238  OE1 GLU B 439     -68.807  -7.439 -18.303  1.00178.23           O  
ANISOU 6238  OE1 GLU B 439    15678  27667  24375  -3793  -1479  -2526       O  
ATOM   6239  OE2 GLU B 439     -68.276  -8.151 -16.287  1.00177.47           O  
ANISOU 6239  OE2 GLU B 439    15843  27010  24577  -3668  -1050  -2573       O  
ATOM   6240  N   LYS B 440     -64.494  -7.441 -21.865  1.00161.33           N  
ANISOU 6240  N   LYS B 440    14246  25982  21069  -3993  -1764  -2843       N  
ATOM   6241  CA  LYS B 440     -63.902  -6.571 -22.891  1.00161.36           C  
ANISOU 6241  CA  LYS B 440    14286  26261  20763  -3963  -1958  -2714       C  
ATOM   6242  C   LYS B 440     -64.367  -5.102 -22.772  1.00164.58           C  
ANISOU 6242  C   LYS B 440    14552  26779  21201  -3751  -2117  -2341       C  
ATOM   6243  O   LYS B 440     -63.772  -4.232 -23.416  1.00164.23           O  
ANISOU 6243  O   LYS B 440    14555  26911  20932  -3683  -2260  -2177       O  
ATOM   6244  CB  LYS B 440     -64.190  -7.110 -24.315  1.00167.17           C  
ANISOU 6244  CB  LYS B 440    14906  27372  21238  -4252  -2143  -2918       C  
ATOM   6245  CG  LYS B 440     -65.585  -7.712 -24.535  1.00185.55           C  
ANISOU 6245  CG  LYS B 440    16953  29863  23682  -4449  -2238  -3029       C  
ATOM   6246  CD  LYS B 440     -66.580  -6.725 -25.136  1.00198.89           C  
ANISOU 6246  CD  LYS B 440    18368  31897  25306  -4428  -2522  -2766       C  
ATOM   6247  CE  LYS B 440     -67.940  -7.354 -25.325  1.00212.02           C  
ANISOU 6247  CE  LYS B 440    19924  33368  27266  -4489  -2649  -2738       C  
ATOM   6248  NZ  LYS B 440     -68.910  -6.407 -25.933  1.00213.57           N  
ANISOU 6248  NZ  LYS B 440    20437  32674  28037  -3999  -3039  -2070       N  
ATOM   6249  N   ALA B 441     -65.400  -4.830 -21.935  1.00160.30           N  
ANISOU 6249  N   ALA B 441    13838  26120  20947  -3647  -2080  -2209       N  
ATOM   6250  CA  ALA B 441     -65.981  -3.501 -21.690  1.00159.60           C  
ANISOU 6250  CA  ALA B 441    13587  26090  20964  -3438  -2201  -1874       C  
ATOM   6251  C   ALA B 441     -64.938  -2.481 -21.192  1.00158.74           C  
ANISOU 6251  C   ALA B 441    13686  25803  20824  -3181  -2132  -1665       C  
ATOM   6252  O   ALA B 441     -65.015  -1.304 -21.555  1.00158.63           O  
ANISOU 6252  O   ALA B 441    13587  25933  20753  -3052  -2299  -1399       O  
ATOM   6253  CB  ALA B 441     -67.118  -3.608 -20.684  1.00160.70           C  
ANISOU 6253  CB  ALA B 441    13543  26070  21448  -3380  -2099  -1837       C  
ATOM   6254  N   ALA B 442     -63.968  -2.935 -20.380  1.00151.10           N  
ANISOU 6254  N   ALA B 442    12985  24525  19902  -3114  -1893  -1779       N  
ATOM   6255  CA  ALA B 442     -62.908  -2.087 -19.845  1.00147.53           C  
ANISOU 6255  CA  ALA B 442    12746  23887  19422  -2890  -1808  -1616       C  
ATOM   6256  C   ALA B 442     -61.525  -2.572 -20.331  1.00148.22           C  
ANISOU 6256  C   ALA B 442    13100  23951  19268  -2962  -1750  -1778       C  
ATOM   6257  O   ALA B 442     -60.636  -2.856 -19.522  1.00145.28           O  
ANISOU 6257  O   ALA B 442    12950  23294  18957  -2879  -1546  -1845       O  
ATOM   6258  CB  ALA B 442     -62.980  -2.060 -18.324  1.00146.25           C  
ANISOU 6258  CB  ALA B 442    12652  23375  19542  -2722  -1574  -1575       C  
ATOM   6259  N   SER B 443     -61.353  -2.652 -21.670  1.00145.04           N  
ANISOU 6259  N   SER B 443    12662  23861  18585  -3122  -1934  -1836       N  
ATOM   6260  CA  SER B 443     -60.108  -3.076 -22.322  1.00143.16           C  
ANISOU 6260  CA  SER B 443    12643  23657  18094  -3213  -1898  -2000       C  
ATOM   6261  C   SER B 443     -59.000  -2.028 -22.145  1.00142.87           C  
ANISOU 6261  C   SER B 443    12792  23524  17967  -3004  -1877  -1796       C  
ATOM   6262  O   SER B 443     -57.825  -2.395 -22.090  1.00140.54           O  
ANISOU 6262  O   SER B 443    12725  23096  17578  -3003  -1748  -1923       O  
ATOM   6263  CB  SER B 443     -60.341  -3.351 -23.803  1.00149.01           C  
ANISOU 6263  CB  SER B 443    13272  24796  18548  -3450  -2106  -2107       C  
ATOM   6264  OG  SER B 443     -59.210  -3.973 -24.390  1.00155.76           O  
ANISOU 6264  OG  SER B 443    14328  25671  19184  -3569  -2034  -2331       O  
ATOM   6265  N   LYS B 444     -59.381  -0.731 -22.049  1.00138.09           N  
ANISOU 6265  N   LYS B 444    12082  22976  17411  -2827  -1999  -1483       N  
ATOM   6266  CA  LYS B 444     -58.464   0.395 -21.838  1.00135.12           C  
ANISOU 6266  CA  LYS B 444    11852  22503  16985  -2620  -1989  -1261       C  
ATOM   6267  C   LYS B 444     -57.886   0.353 -20.425  1.00133.99           C  
ANISOU 6267  C   LYS B 444    11890  21965  17057  -2446  -1741  -1277       C  
ATOM   6268  O   LYS B 444     -56.750   0.783 -20.217  1.00131.75           O  
ANISOU 6268  O   LYS B 444    11808  21552  16699  -2334  -1665  -1224       O  
ATOM   6269  CB  LYS B 444     -59.176   1.731 -22.083  1.00139.00           C  
ANISOU 6269  CB  LYS B 444    12149  23141  17521  -2487  -2184   -929       C  
ATOM   6270  N   ILE B 445     -58.672  -0.172 -19.462  1.00128.77           N  
ANISOU 6270  N   ILE B 445    11150  21125  16652  -2436  -1616  -1347       N  
ATOM   6271  CA  ILE B 445     -58.270  -0.344 -18.067  1.00125.34           C  
ANISOU 6271  CA  ILE B 445    10866  20337  16420  -2302  -1378  -1373       C  
ATOM   6272  C   ILE B 445     -57.243  -1.478 -17.974  1.00126.29           C  
ANISOU 6272  C   ILE B 445    11207  20311  16466  -2405  -1222  -1620       C  
ATOM   6273  O   ILE B 445     -56.223  -1.319 -17.301  1.00123.64           O  
ANISOU 6273  O   ILE B 445    11077  19752  16150  -2282  -1082  -1598       O  
ATOM   6274  CB  ILE B 445     -59.498  -0.610 -17.169  1.00129.06           C  
ANISOU 6274  CB  ILE B 445    11165  20701  17169  -2289  -1300  -1374       C  
ATOM   6275  N   ASN B 446     -57.501  -2.601 -18.686  1.00122.89           N  
ANISOU 6275  N   ASN B 446    10726  20010  15956  -2632  -1250  -1856       N  
ATOM   6276  CA  ASN B 446     -56.639  -3.788 -18.736  1.00121.28           C  
ANISOU 6276  CA  ASN B 446    10698  19678  15705  -2753  -1110  -2117       C  
ATOM   6277  C   ASN B 446     -55.275  -3.494 -19.383  1.00121.01           C  
ANISOU 6277  C   ASN B 446    10851  19693  15434  -2730  -1128  -2128       C  
ATOM   6278  O   ASN B 446     -54.275  -4.080 -18.969  1.00118.77           O  
ANISOU 6278  O   ASN B 446    10759  19196  15172  -2716   -968  -2252       O  
ATOM   6279  CB  ASN B 446     -57.331  -4.928 -19.493  1.00126.02           C  
ANISOU 6279  CB  ASN B 446    11168  20434  16278  -3012  -1154  -2370       C  
ATOM   6280  CG  ASN B 446     -58.560  -5.491 -18.813  1.00158.14           C  
ANISOU 6280  CG  ASN B 446    15069  24419  20597  -3066  -1100  -2410       C  
ATOM   6281  OD1 ASN B 446     -58.565  -5.785 -17.610  1.00153.64           O  
ANISOU 6281  OD1 ASN B 446    14567  23561  20247  -2978   -919  -2396       O  
ATOM   6282  ND2 ASN B 446     -59.617  -5.715 -19.589  1.00153.04           N  
ANISOU 6282  ND2 ASN B 446    14201  24033  19914  -3230  -1252  -2472       N  
ATOM   6283  N   GLU B 447     -55.241  -2.602 -20.393  1.00116.48           N  
ANISOU 6283  N   GLU B 447    10213  19402  14643  -2729  -1322  -1989       N  
ATOM   6284  CA  GLU B 447     -54.022  -2.229 -21.114  1.00114.65           C  
ANISOU 6284  CA  GLU B 447    10136  19262  14165  -2719  -1356  -1980       C  
ATOM   6285  C   GLU B 447     -53.081  -1.385 -20.242  1.00112.89           C  
ANISOU 6285  C   GLU B 447    10085  18803  14006  -2484  -1258  -1795       C  
ATOM   6286  O   GLU B 447     -51.909  -1.730 -20.125  1.00110.25           O  
ANISOU 6286  O   GLU B 447     9942  18335  13611  -2469  -1141  -1896       O  
ATOM   6287  CB  GLU B 447     -54.355  -1.482 -22.420  1.00118.17           C  
ANISOU 6287  CB  GLU B 447    10446  20094  14360  -2797  -1602  -1855       C  
ATOM   6288  CG  GLU B 447     -54.496  -2.393 -23.629  1.00131.89           C  
ANISOU 6288  CG  GLU B 447    12127  22104  15882  -3068  -1679  -2110       C  
ATOM   6289  CD  GLU B 447     -53.503  -2.159 -24.754  1.00149.29           C  
ANISOU 6289  CD  GLU B 447    14435  24531  17759  -3148  -1749  -2141       C  
ATOM   6290  OE1 GLU B 447     -52.279  -2.230 -24.497  1.00137.30           O  
ANISOU 6290  OE1 GLU B 447    13122  22832  16214  -3075  -1605  -2199       O  
ATOM   6291  OE2 GLU B 447     -53.953  -1.952 -25.905  1.00141.93           O  
ANISOU 6291  OE2 GLU B 447    13372  23962  16591  -3295  -1946  -2113       O  
ATOM   6292  N   THR B 448     -53.603  -0.305 -19.620  1.00107.53           N  
ANISOU 6292  N   THR B 448     9327  18068  13460  -2305  -1301  -1536       N  
ATOM   6293  CA  THR B 448     -52.847   0.630 -18.782  1.00104.24           C  
ANISOU 6293  CA  THR B 448     9049  17444  13114  -2083  -1221  -1351       C  
ATOM   6294  C   THR B 448     -52.351  -0.038 -17.487  1.00103.38           C  
ANISOU 6294  C   THR B 448     9097  16995  13188  -2016   -990  -1458       C  
ATOM   6295  O   THR B 448     -51.220   0.231 -17.089  1.00101.10           O  
ANISOU 6295  O   THR B 448     8992  16552  12869  -1911   -901  -1424       O  
ATOM   6296  CB  THR B 448     -53.663   1.898 -18.475  1.00114.64           C  
ANISOU 6296  CB  THR B 448    10214  18792  14553  -1928  -1322  -1075       C  
ATOM   6297  OG1 THR B 448     -54.487   2.228 -19.596  1.00118.54           O  
ANISOU 6297  OG1 THR B 448    10508  19605  14926  -2024  -1544   -991       O  
ATOM   6298  CG2 THR B 448     -52.775   3.094 -18.125  1.00111.14           C  
ANISOU 6298  CG2 THR B 448     9898  18230  14102  -1729  -1303   -870       C  
ATOM   6299  N   MET B 449     -53.167  -0.905 -16.850  1.00 97.95           N  
ANISOU 6299  N   MET B 449     8334  16199  12683  -2084   -898  -1578       N  
ATOM   6300  CA  MET B 449     -52.783  -1.613 -15.627  1.00 95.01           C  
ANISOU 6300  CA  MET B 449     8096  15519  12484  -2040   -687  -1664       C  
ATOM   6301  C   MET B 449     -51.663  -2.632 -15.890  1.00 97.44           C  
ANISOU 6301  C   MET B 449     8578  15738  12708  -2134   -591  -1870       C  
ATOM   6302  O   MET B 449     -50.723  -2.693 -15.104  1.00 95.37           O  
ANISOU 6302  O   MET B 449     8489  15254  12493  -2032   -462  -1851       O  
ATOM   6303  CB  MET B 449     -53.985  -2.307 -14.980  1.00 98.18           C  
ANISOU 6303  CB  MET B 449     8359  15852  13095  -2110   -620  -1733       C  
ATOM   6304  N   LEU B 450     -51.744  -3.408 -16.990  1.00 95.29           N  
ANISOU 6304  N   LEU B 450     8252  15637  12315  -2327   -654  -2068       N  
ATOM   6305  CA  LEU B 450     -50.728  -4.410 -17.345  1.00 94.77           C  
ANISOU 6305  CA  LEU B 450     8328  15494  12187  -2429   -558  -2293       C  
ATOM   6306  C   LEU B 450     -49.387  -3.744 -17.716  1.00 97.40           C  
ANISOU 6306  C   LEU B 450     8818  15850  12341  -2338   -572  -2226       C  
ATOM   6307  O   LEU B 450     -48.324  -4.235 -17.319  1.00 96.25           O  
ANISOU 6307  O   LEU B 450     8834  15507  12231  -2307   -439  -2314       O  
ATOM   6308  CB  LEU B 450     -51.222  -5.283 -18.502  1.00 97.42           C  
ANISOU 6308  CB  LEU B 450     8550  16044  12422  -2667   -630  -2529       C  
ATOM   6309  CG  LEU B 450     -50.611  -6.676 -18.596  1.00102.76           C  
ANISOU 6309  CG  LEU B 450     9321  16570  13152  -2801   -486  -2817       C  
ATOM   6310  CD1 LEU B 450     -51.685  -7.751 -18.477  1.00104.52           C  
ANISOU 6310  CD1 LEU B 450     9420  16738  13557  -2956   -437  -2988       C  
ATOM   6311  CD2 LEU B 450     -49.841  -6.843 -19.895  1.00106.52           C  
ANISOU 6311  CD2 LEU B 450     9832  17264  13377  -2933   -547  -2987       C  
ATOM   6312  N   ARG B 451     -49.449  -2.621 -18.457  1.00 92.99           N  
ANISOU 6312  N   ARG B 451     8202  15526  11602  -2295   -734  -2059       N  
ATOM   6313  CA  ARG B 451     -48.290  -1.852 -18.901  1.00 90.92           C  
ANISOU 6313  CA  ARG B 451     8066  15319  11160  -2216   -766  -1968       C  
ATOM   6314  C   ARG B 451     -47.572  -1.200 -17.693  1.00 89.40           C  
ANISOU 6314  C   ARG B 451     8013  14859  11094  -2001   -659  -1801       C  
ATOM   6315  O   ARG B 451     -46.344  -1.237 -17.618  1.00 86.88           O  
ANISOU 6315  O   ARG B 451     7853  14436  10720  -1953   -582  -1831       O  
ATOM   6316  CB  ARG B 451     -48.725  -0.799 -19.931  1.00 92.97           C  
ANISOU 6316  CB  ARG B 451     8207  15898  11221  -2232   -976  -1801       C  
ATOM   6317  CG  ARG B 451     -47.589  -0.354 -20.826  1.00105.84           C  
ANISOU 6317  CG  ARG B 451     9944  17666  12603  -2247  -1018  -1788       C  
ATOM   6318  CD  ARG B 451     -47.724  -0.834 -22.258  1.00116.98           C  
ANISOU 6318  CD  ARG B 451    11278  19402  13765  -2468  -1129  -1946       C  
ATOM   6319  NE  ARG B 451     -46.469  -0.648 -22.991  1.00118.15           N  
ANISOU 6319  NE  ARG B 451    11556  19645  13691  -2498  -1115  -1991       N  
ATOM   6320  CZ  ARG B 451     -46.061   0.511 -23.497  1.00127.44           C  
ANISOU 6320  CZ  ARG B 451    12749  20977  14697  -2430  -1226  -1769       C  
ATOM   6321  NH1 ARG B 451     -46.808   1.602 -23.366  1.00113.16           N  
ANISOU 6321  NH1 ARG B 451    10832  19235  12927  -2321  -1365  -1484       N  
ATOM   6322  NH2 ARG B 451     -44.902   0.589 -24.137  1.00110.50           N  
ANISOU 6322  NH2 ARG B 451    10721  18910  12353  -2472  -1194  -1829       N  
ATOM   6323  N   LEU B 452     -48.351  -0.660 -16.737  1.00 83.58           N  
ANISOU 6323  N   LEU B 452     7211  14014  10532  -1883   -647  -1642       N  
ATOM   6324  CA  LEU B 452     -47.872  -0.042 -15.497  1.00 80.02           C  
ANISOU 6324  CA  LEU B 452     6871  13322  10209  -1694   -544  -1495       C  
ATOM   6325  C   LEU B 452     -47.075  -1.050 -14.660  1.00 80.37           C  
ANISOU 6325  C   LEU B 452     7072  13107  10360  -1696   -363  -1632       C  
ATOM   6326  O   LEU B 452     -45.963  -0.742 -14.230  1.00 78.32           O  
ANISOU 6326  O   LEU B 452     6964  12711  10082  -1592   -297  -1578       O  
ATOM   6327  CB  LEU B 452     -49.084   0.465 -14.704  1.00 80.13           C  
ANISOU 6327  CB  LEU B 452     6752  13294  10398  -1613   -551  -1358       C  
ATOM   6328  CG  LEU B 452     -49.011   1.810 -13.992  1.00 83.62           C  
ANISOU 6328  CG  LEU B 452     7217  13653  10902  -1417   -553  -1131       C  
ATOM   6329  CD1 LEU B 452     -48.454   2.923 -14.896  1.00 83.44           C  
ANISOU 6329  CD1 LEU B 452     7203  13792  10708  -1363   -692   -987       C  
ATOM   6330  CD2 LEU B 452     -50.396   2.198 -13.489  1.00 87.64           C  
ANISOU 6330  CD2 LEU B 452     7547  14168  11582  -1372   -570  -1036       C  
ATOM   6331  N   GLY B 453     -47.638  -2.249 -14.491  1.00 76.00           N  
ANISOU 6331  N   GLY B 453     6469  12490   9916  -1822   -294  -1804       N  
ATOM   6332  CA  GLY B 453     -47.034  -3.347 -13.749  1.00 74.12           C  
ANISOU 6332  CA  GLY B 453     6351  12004   9808  -1843   -130  -1931       C  
ATOM   6333  C   GLY B 453     -45.727  -3.822 -14.340  1.00 76.40           C  
ANISOU 6333  C   GLY B 453     6769  12266   9994  -1883    -92  -2064       C  
ATOM   6334  O   GLY B 453     -44.786  -4.091 -13.597  1.00 75.17           O  
ANISOU 6334  O   GLY B 453     6752  11895   9916  -1807     21  -2056       O  
ATOM   6335  N   ILE B 454     -45.658  -3.904 -15.686  1.00 73.81           N  
ANISOU 6335  N   ILE B 454     6387  12169   9487  -2005   -188  -2184       N  
ATOM   6336  CA  ILE B 454     -44.478  -4.337 -16.448  1.00 73.01           C  
ANISOU 6336  CA  ILE B 454     6386  12088   9267  -2065   -154  -2339       C  
ATOM   6337  C   ILE B 454     -43.347  -3.352 -16.183  1.00 73.30           C  
ANISOU 6337  C   ILE B 454     6553  12075   9222  -1904   -152  -2173       C  
ATOM   6338  O   ILE B 454     -42.271  -3.772 -15.763  1.00 71.72           O  
ANISOU 6338  O   ILE B 454     6481  11689   9082  -1858    -41  -2227       O  
ATOM   6339  CB  ILE B 454     -44.799  -4.508 -17.972  1.00 78.11           C  
ANISOU 6339  CB  ILE B 454     6930  13043   9704  -2245   -267  -2493       C  
ATOM   6340  CG1 ILE B 454     -45.529  -5.850 -18.225  1.00 80.21           C  
ANISOU 6340  CG1 ILE B 454     7102  13300  10073  -2432   -222  -2742       C  
ATOM   6341  CG2 ILE B 454     -43.531  -4.388 -18.862  1.00 78.16           C  
ANISOU 6341  CG2 ILE B 454     7037  13142   9519  -2273   -260  -2582       C  
ATOM   6342  CD1 ILE B 454     -46.132  -6.048 -19.635  1.00 87.70           C  
ANISOU 6342  CD1 ILE B 454     7917  14582  10822  -2630   -351  -2889       C  
ATOM   6343  N   PHE B 455     -43.626  -2.044 -16.360  1.00 68.75           N  
ANISOU 6343  N   PHE B 455     5937  11649   8537  -1815   -273  -1963       N  
ATOM   6344  CA  PHE B 455     -42.676  -0.952 -16.153  1.00 66.22           C  
ANISOU 6344  CA  PHE B 455     5721  11299   8140  -1666   -288  -1786       C  
ATOM   6345  C   PHE B 455     -42.276  -0.835 -14.688  1.00 67.29           C  
ANISOU 6345  C   PHE B 455     5960  11154   8452  -1515   -174  -1681       C  
ATOM   6346  O   PHE B 455     -41.103  -0.622 -14.413  1.00 66.33           O  
ANISOU 6346  O   PHE B 455     5967  10930   8307  -1430   -124  -1639       O  
ATOM   6347  CB  PHE B 455     -43.238   0.372 -16.692  1.00 68.31           C  
ANISOU 6347  CB  PHE B 455     5893  11782   8279  -1620   -449  -1585       C  
ATOM   6348  CG  PHE B 455     -43.070   0.468 -18.188  1.00 71.30           C  
ANISOU 6348  CG  PHE B 455     6227  12448   8415  -1748   -561  -1647       C  
ATOM   6349  CD1 PHE B 455     -42.041   1.218 -18.739  1.00 73.62           C  
ANISOU 6349  CD1 PHE B 455     6605  12823   8544  -1705   -595  -1562       C  
ATOM   6350  CD2 PHE B 455     -43.899  -0.251 -19.048  1.00 75.54           C  
ANISOU 6350  CD2 PHE B 455     6641  13181   8879  -1927   -626  -1802       C  
ATOM   6351  CE1 PHE B 455     -41.853   1.264 -20.123  1.00 76.37           C  
ANISOU 6351  CE1 PHE B 455     6917  13453   8647  -1839   -690  -1621       C  
ATOM   6352  CE2 PHE B 455     -43.714  -0.203 -20.430  1.00 80.06           C  
ANISOU 6352  CE2 PHE B 455     7177  14041   9200  -2064   -726  -1871       C  
ATOM   6353  CZ  PHE B 455     -42.685   0.544 -20.959  1.00 77.67           C  
ANISOU 6353  CZ  PHE B 455     6962  13823   8725  -2020   -754  -1778       C  
ATOM   6354  N   GLY B 456     -43.222  -1.049 -13.782  1.00 62.60           N  
ANISOU 6354  N   GLY B 456     5310  10449   8027  -1497   -130  -1651       N  
ATOM   6355  CA  GLY B 456     -42.983  -1.026 -12.346  1.00 61.11           C  
ANISOU 6355  CA  GLY B 456     5210  10015   7994  -1380    -17  -1560       C  
ATOM   6356  C   GLY B 456     -41.998  -2.080 -11.892  1.00 65.36           C  
ANISOU 6356  C   GLY B 456     5872  10348   8614  -1397    110  -1676       C  
ATOM   6357  O   GLY B 456     -41.028  -1.752 -11.206  1.00 63.67           O  
ANISOU 6357  O   GLY B 456     5780   9997   8415  -1289    164  -1590       O  
ATOM   6358  N   PHE B 457     -42.221  -3.347 -12.308  1.00 64.24           N  
ANISOU 6358  N   PHE B 457     5692  10184   8533  -1537    155  -1872       N  
ATOM   6359  CA  PHE B 457     -41.362  -4.482 -11.959  1.00 64.68           C  
ANISOU 6359  CA  PHE B 457     5840  10030   8704  -1564    278  -1993       C  
ATOM   6360  C   PHE B 457     -39.995  -4.384 -12.635  1.00 70.10           C  
ANISOU 6360  C   PHE B 457     6618  10739   9277  -1547    279  -2055       C  
ATOM   6361  O   PHE B 457     -38.976  -4.693 -12.002  1.00 68.66           O  
ANISOU 6361  O   PHE B 457     6543  10365   9178  -1478    364  -2039       O  
ATOM   6362  CB  PHE B 457     -42.035  -5.826 -12.300  1.00 68.19           C  
ANISOU 6362  CB  PHE B 457     6204  10439   9266  -1726    328  -2197       C  
ATOM   6363  CG  PHE B 457     -42.963  -6.302 -11.206  1.00 69.92           C  
ANISOU 6363  CG  PHE B 457     6380  10514   9672  -1731    394  -2140       C  
ATOM   6364  CD1 PHE B 457     -42.459  -6.745  -9.986  1.00 72.24           C  
ANISOU 6364  CD1 PHE B 457     6771  10555  10120  -1660    507  -2060       C  
ATOM   6365  CD2 PHE B 457     -44.343  -6.296 -11.388  1.00 72.22           C  
ANISOU 6365  CD2 PHE B 457     6527  10932   9980  -1812    342  -2156       C  
ATOM   6366  CE1 PHE B 457     -43.324  -7.162  -8.964  1.00 73.38           C  
ANISOU 6366  CE1 PHE B 457     6879  10582  10421  -1676    574  -1996       C  
ATOM   6367  CE2 PHE B 457     -45.202  -6.705 -10.363  1.00 74.81           C  
ANISOU 6367  CE2 PHE B 457     6812  11134  10480  -1820    413  -2100       C  
ATOM   6368  CZ  PHE B 457     -44.687  -7.135  -9.160  1.00 72.12           C  
ANISOU 6368  CZ  PHE B 457     6577  10547  10279  -1756    533  -2021       C  
ATOM   6369  N   LEU B 458     -39.974  -3.925 -13.904  1.00 68.88           N  
ANISOU 6369  N   LEU B 458     6414  10828   8929  -1611    183  -2114       N  
ATOM   6370  CA  LEU B 458     -38.754  -3.752 -14.696  1.00 69.04           C  
ANISOU 6370  CA  LEU B 458     6504  10915   8812  -1613    182  -2180       C  
ATOM   6371  C   LEU B 458     -37.839  -2.738 -14.020  1.00 69.04           C  
ANISOU 6371  C   LEU B 458     6612  10837   8784  -1447    180  -1981       C  
ATOM   6372  O   LEU B 458     -36.655  -3.027 -13.817  1.00 67.24           O  
ANISOU 6372  O   LEU B 458     6477  10479   8590  -1405    254  -2017       O  
ATOM   6373  CB  LEU B 458     -39.106  -3.319 -16.134  1.00 71.24           C  
ANISOU 6373  CB  LEU B 458     6698  11508   8864  -1725     65  -2245       C  
ATOM   6374  CG  LEU B 458     -37.996  -3.354 -17.187  1.00 77.82           C  
ANISOU 6374  CG  LEU B 458     7581  12459   9530  -1778     73  -2362       C  
ATOM   6375  CD1 LEU B 458     -37.246  -4.682 -17.174  1.00 79.28           C  
ANISOU 6375  CD1 LEU B 458     7809  12470   9844  -1845    216  -2603       C  
ATOM   6376  CD2 LEU B 458     -38.570  -3.120 -18.567  1.00 83.15           C  
ANISOU 6376  CD2 LEU B 458     8157  13463   9973  -1918    -46  -2427       C  
ATOM   6377  N   ALA B 459     -38.413  -1.582 -13.609  1.00 63.78           N  
ANISOU 6377  N   ALA B 459     5923  10233   8078  -1354    101  -1777       N  
ATOM   6378  CA  ALA B 459     -37.699  -0.525 -12.904  1.00 61.29           C  
ANISOU 6378  CA  ALA B 459     5699   9843   7747  -1203     98  -1589       C  
ATOM   6379  C   ALA B 459     -37.135  -1.060 -11.574  1.00 62.95           C  
ANISOU 6379  C   ALA B 459     6006   9786   8128  -1127    213  -1563       C  
ATOM   6380  O   ALA B 459     -35.943  -0.872 -11.310  1.00 61.13           O  
ANISOU 6380  O   ALA B 459     5874   9464   7887  -1056    249  -1528       O  
ATOM   6381  CB  ALA B 459     -38.617   0.664 -12.669  1.00 61.72           C  
ANISOU 6381  CB  ALA B 459     5688   9991   7773  -1131      8  -1405       C  
ATOM   6382  N   PHE B 460     -37.962  -1.810 -10.802  1.00 58.92           N  
ANISOU 6382  N   PHE B 460     5459   9158   7770  -1156    270  -1585       N  
ATOM   6383  CA  PHE B 460     -37.580  -2.426  -9.524  1.00 57.49           C  
ANISOU 6383  CA  PHE B 460     5356   8736   7749  -1107    375  -1547       C  
ATOM   6384  C   PHE B 460     -36.305  -3.259  -9.650  1.00 62.24           C  
ANISOU 6384  C   PHE B 460     6035   9209   8404  -1118    444  -1649       C  
ATOM   6385  O   PHE B 460     -35.432  -3.134  -8.791  1.00 60.70           O  
ANISOU 6385  O   PHE B 460     5935   8873   8257  -1027    484  -1553       O  
ATOM   6386  CB  PHE B 460     -38.712  -3.308  -8.958  1.00 59.56           C  
ANISOU 6386  CB  PHE B 460     5551   8921   8160  -1178    428  -1586       C  
ATOM   6387  CG  PHE B 460     -38.383  -3.936  -7.620  1.00 60.20           C  
ANISOU 6387  CG  PHE B 460     5709   8769   8397  -1138    531  -1521       C  
ATOM   6388  CD1 PHE B 460     -37.776  -5.189  -7.549  1.00 63.73           C  
ANISOU 6388  CD1 PHE B 460     6188   9051   8977  -1191    610  -1624       C  
ATOM   6389  CD2 PHE B 460     -38.656  -3.267  -6.433  1.00 61.07           C  
ANISOU 6389  CD2 PHE B 460     5857   8826   8521  -1050    550  -1354       C  
ATOM   6390  CE1 PHE B 460     -37.441  -5.756  -6.314  1.00 64.25           C  
ANISOU 6390  CE1 PHE B 460     6321   8906   9183  -1155    692  -1532       C  
ATOM   6391  CE2 PHE B 460     -38.342  -3.845  -5.195  1.00 63.67           C  
ANISOU 6391  CE2 PHE B 460     6259   8965   8967  -1027    638  -1279       C  
ATOM   6392  CZ  PHE B 460     -37.739  -5.084  -5.143  1.00 62.56           C  
ANISOU 6392  CZ  PHE B 460     6149   8667   8955  -1078    701  -1355       C  
ATOM   6393  N   GLY B 461     -36.255  -4.133 -10.667  1.00 60.31           N  
ANISOU 6393  N   GLY B 461     5742   9011   8163  -1234    459  -1846       N  
ATOM   6394  CA  GLY B 461     -35.124  -5.010 -10.950  1.00 60.46           C  
ANISOU 6394  CA  GLY B 461     5807   8910   8254  -1258    535  -1981       C  
ATOM   6395  C   GLY B 461     -33.842  -4.240 -11.191  1.00 63.67           C  
ANISOU 6395  C   GLY B 461     6291   9350   8550  -1172    515  -1923       C  
ATOM   6396  O   GLY B 461     -32.810  -4.546 -10.585  1.00 62.30           O  
ANISOU 6396  O   GLY B 461     6189   9003   8479  -1104    576  -1891       O  
ATOM   6397  N   PHE B 462     -33.916  -3.202 -12.043  1.00 60.50           N  
ANISOU 6397  N   PHE B 462     5868   9173   7944  -1172    424  -1889       N  
ATOM   6398  CA  PHE B 462     -32.774  -2.341 -12.340  1.00 59.49           C  
ANISOU 6398  CA  PHE B 462     5806   9101   7696  -1100    399  -1821       C  
ATOM   6399  C   PHE B 462     -32.346  -1.563 -11.090  1.00 62.29           C  
ANISOU 6399  C   PHE B 462     6243   9331   8095   -958    396  -1612       C  
ATOM   6400  O   PHE B 462     -31.145  -1.505 -10.808  1.00 61.64           O  
ANISOU 6400  O   PHE B 462     6232   9159   8031   -894    429  -1583       O  
ATOM   6401  CB  PHE B 462     -33.068  -1.389 -13.509  1.00 61.39           C  
ANISOU 6401  CB  PHE B 462     6000   9614   7713  -1143    298  -1807       C  
ATOM   6402  CG  PHE B 462     -33.031  -2.043 -14.872  1.00 64.65           C  
ANISOU 6402  CG  PHE B 462     6352  10184   8026  -1289    304  -2024       C  
ATOM   6403  CD1 PHE B 462     -31.885  -2.692 -15.322  1.00 68.28           C  
ANISOU 6403  CD1 PHE B 462     6847  10594   8503  -1322    389  -2181       C  
ATOM   6404  CD2 PHE B 462     -34.134  -1.994 -15.716  1.00 67.65           C  
ANISOU 6404  CD2 PHE B 462     6636  10776   8293  -1399    225  -2077       C  
ATOM   6405  CE1 PHE B 462     -31.853  -3.299 -16.585  1.00 70.77           C  
ANISOU 6405  CE1 PHE B 462     7107  11065   8717  -1469    410  -2408       C  
ATOM   6406  CE2 PHE B 462     -34.097  -2.595 -16.980  1.00 72.12           C  
ANISOU 6406  CE2 PHE B 462     7149  11511   8744  -1551    230  -2292       C  
ATOM   6407  CZ  PHE B 462     -32.959  -3.246 -17.404  1.00 70.59           C  
ANISOU 6407  CZ  PHE B 462     6997  11263   8561  -1588    329  -2464       C  
ATOM   6408  N   VAL B 463     -33.317  -1.021 -10.319  1.00 57.01           N  
ANISOU 6408  N   VAL B 463     5558   8654   7448   -915    364  -1479       N  
ATOM   6409  CA  VAL B 463     -33.040  -0.278  -9.084  1.00 55.25           C  
ANISOU 6409  CA  VAL B 463     5409   8325   7258   -797    368  -1301       C  
ATOM   6410  C   VAL B 463     -32.352  -1.220  -8.073  1.00 59.44           C  
ANISOU 6410  C   VAL B 463     6004   8632   7946   -772    456  -1302       C  
ATOM   6411  O   VAL B 463     -31.372  -0.813  -7.445  1.00 60.70           O  
ANISOU 6411  O   VAL B 463     6243   8711   8108   -689    464  -1205       O  
ATOM   6412  CB  VAL B 463     -34.303   0.415  -8.505  1.00 58.90           C  
ANISOU 6412  CB  VAL B 463     5826   8834   7720   -768    332  -1188       C  
ATOM   6413  CG1 VAL B 463     -34.016   1.063  -7.153  1.00 57.94           C  
ANISOU 6413  CG1 VAL B 463     5783   8594   7638   -663    360  -1037       C  
ATOM   6414  CG2 VAL B 463     -34.834   1.464  -9.478  1.00 58.79           C  
ANISOU 6414  CG2 VAL B 463     5744   9027   7566   -773    232  -1149       C  
ATOM   6415  N   LEU B 464     -32.775  -2.495  -8.012  1.00 54.56           N  
ANISOU 6415  N   LEU B 464     5348   7919   7463   -849    517  -1412       N  
ATOM   6416  CA  LEU B 464     -32.172  -3.496  -7.138  1.00 54.03           C  
ANISOU 6416  CA  LEU B 464     5327   7633   7568   -835    596  -1402       C  
ATOM   6417  C   LEU B 464     -30.710  -3.763  -7.543  1.00 59.66           C  
ANISOU 6417  C   LEU B 464     6081   8283   8304   -806    620  -1460       C  
ATOM   6418  O   LEU B 464     -29.873  -3.936  -6.656  1.00 59.75           O  
ANISOU 6418  O   LEU B 464     6153   8146   8403   -738    646  -1364       O  
ATOM   6419  CB  LEU B 464     -33.004  -4.798  -7.137  1.00 55.36           C  
ANISOU 6419  CB  LEU B 464     5431   7711   7890   -935    656  -1514       C  
ATOM   6420  CG  LEU B 464     -32.551  -5.964  -6.238  1.00 59.88           C  
ANISOU 6420  CG  LEU B 464     6036   8040   8675   -932    738  -1487       C  
ATOM   6421  CD1 LEU B 464     -32.428  -5.552  -4.765  1.00 59.03           C  
ANISOU 6421  CD1 LEU B 464     6001   7847   8581   -850    739  -1271       C  
ATOM   6422  CD2 LEU B 464     -33.461  -7.155  -6.396  1.00 61.63           C  
ANISOU 6422  CD2 LEU B 464     6184   8185   9048  -1044    795  -1610       C  
ATOM   6423  N   ILE B 465     -30.392  -3.751  -8.860  1.00 56.98           N  
ANISOU 6423  N   ILE B 465     5703   8068   7878   -859    608  -1610       N  
ATOM   6424  CA  ILE B 465     -29.014  -3.947  -9.335  1.00 56.64           C  
ANISOU 6424  CA  ILE B 465     5685   7984   7850   -836    642  -1682       C  
ATOM   6425  C   ILE B 465     -28.174  -2.727  -8.923  1.00 59.34           C  
ANISOU 6425  C   ILE B 465     6098   8368   8082   -730    590  -1519       C  
ATOM   6426  O   ILE B 465     -27.054  -2.867  -8.416  1.00 58.21           O  
ANISOU 6426  O   ILE B 465     5998   8102   8017   -666    617  -1472       O  
ATOM   6427  CB  ILE B 465     -28.922  -4.217 -10.868  1.00 60.28           C  
ANISOU 6427  CB  ILE B 465     6086   8593   8226   -938    656  -1899       C  
ATOM   6428  CG1 ILE B 465     -29.755  -5.440 -11.307  1.00 61.47           C  
ANISOU 6428  CG1 ILE B 465     6163   8702   8491  -1058    711  -2085       C  
ATOM   6429  CG2 ILE B 465     -27.458  -4.367 -11.297  1.00 59.96           C  
ANISOU 6429  CG2 ILE B 465     6066   8508   8209   -911    706  -1975       C  
ATOM   6430  CD1 ILE B 465     -30.006  -5.541 -12.845  1.00 61.23           C  
ANISOU 6430  CD1 ILE B 465     6065   8889   8313  -1187    700  -2295       C  
ATOM   6431  N   THR B 466     -28.741  -1.537  -9.148  1.00 55.71           N  
ANISOU 6431  N   THR B 466     5638   8074   7455   -715    513  -1432       N  
ATOM   6432  CA  THR B 466     -28.173  -0.235  -8.799  1.00 54.75           C  
ANISOU 6432  CA  THR B 466     5575   8000   7227   -625    460  -1278       C  
ATOM   6433  C   THR B 466     -27.848  -0.261  -7.268  1.00 57.85           C  
ANISOU 6433  C   THR B 466     6034   8220   7725   -544    480  -1137       C  
ATOM   6434  O   THR B 466     -26.706   0.021  -6.883  1.00 58.57           O  
ANISOU 6434  O   THR B 466     6179   8252   7824   -482    480  -1075       O  
ATOM   6435  CB  THR B 466     -29.162   0.854  -9.303  1.00 60.84           C  
ANISOU 6435  CB  THR B 466     6313   8956   7849   -634    381  -1216       C  
ATOM   6436  OG1 THR B 466     -28.774   1.236 -10.632  1.00 63.11           O  
ANISOU 6436  OG1 THR B 466     6567   9413   7997   -686    348  -1293       O  
ATOM   6437  CG2 THR B 466     -29.274   2.064  -8.412  1.00 54.74           C  
ANISOU 6437  CG2 THR B 466     5589   8174   7034   -540    338  -1037       C  
ATOM   6438  N   PHE B 467     -28.808  -0.709  -6.434  1.00 51.24           N  
ANISOU 6438  N   PHE B 467     5190   7309   6969   -557    500  -1095       N  
ATOM   6439  CA  PHE B 467     -28.635  -0.830  -4.986  1.00 48.68           C  
ANISOU 6439  CA  PHE B 467     4925   6846   6725   -504    522   -962       C  
ATOM   6440  C   PHE B 467     -27.461  -1.737  -4.593  1.00 52.88           C  
ANISOU 6440  C   PHE B 467     5484   7215   7392   -484    562   -963       C  
ATOM   6441  O   PHE B 467     -26.727  -1.379  -3.675  1.00 52.49           O  
ANISOU 6441  O   PHE B 467     5496   7104   7345   -422    548   -838       O  
ATOM   6442  CB  PHE B 467     -29.923  -1.360  -4.327  1.00 49.59           C  
ANISOU 6442  CB  PHE B 467     5013   6921   6909   -547    552   -941       C  
ATOM   6443  CG  PHE B 467     -29.815  -1.514  -2.821  1.00 49.84           C  
ANISOU 6443  CG  PHE B 467     5104   6828   7004   -513    581   -801       C  
ATOM   6444  CD1 PHE B 467     -29.832  -0.402  -1.987  1.00 50.12           C  
ANISOU 6444  CD1 PHE B 467     5194   6907   6942   -456    556   -678       C  
ATOM   6445  CD2 PHE B 467     -29.655  -2.771  -2.243  1.00 52.22           C  
ANISOU 6445  CD2 PHE B 467     5407   6972   7464   -544    634   -792       C  
ATOM   6446  CE1 PHE B 467     -29.703  -0.544  -0.600  1.00 50.98           C  
ANISOU 6446  CE1 PHE B 467     5361   6927   7081   -441    583   -555       C  
ATOM   6447  CE2 PHE B 467     -29.520  -2.910  -0.859  1.00 54.85           C  
ANISOU 6447  CE2 PHE B 467     5796   7210   7835   -523    652   -642       C  
ATOM   6448  CZ  PHE B 467     -29.554  -1.795  -0.044  1.00 51.94           C  
ANISOU 6448  CZ  PHE B 467     5485   6911   7339   -476    625   -528       C  
ATOM   6449  N   SER B 468     -27.337  -2.927  -5.236  1.00 50.88           N  
ANISOU 6449  N   SER B 468     5180   6889   7264   -541    614  -1103       N  
ATOM   6450  CA  SER B 468     -26.331  -3.975  -4.973  1.00 51.67           C  
ANISOU 6450  CA  SER B 468     5279   6809   7544   -526    663  -1121       C  
ATOM   6451  C   SER B 468     -24.923  -3.483  -5.196  1.00 55.52           C  
ANISOU 6451  C   SER B 468     5791   7306   7999   -462    644  -1105       C  
ATOM   6452  O   SER B 468     -24.037  -3.801  -4.408  1.00 55.76           O  
ANISOU 6452  O   SER B 468     5846   7205   8135   -408    647  -1007       O  
ATOM   6453  CB  SER B 468     -26.575  -5.203  -5.854  1.00 56.56           C  
ANISOU 6453  CB  SER B 468     5824   7366   8300   -609    731  -1315       C  
ATOM   6454  OG  SER B 468     -27.896  -5.695  -5.705  1.00 66.28           O  
ANISOU 6454  OG  SER B 468     7023   8591   9571   -679    750  -1340       O  
ATOM   6455  N   CYS B 469     -24.720  -2.721  -6.281  1.00 52.73           N  
ANISOU 6455  N   CYS B 469     5424   7114   7498   -475    622  -1192       N  
ATOM   6456  CA  CYS B 469     -23.451  -2.116  -6.670  1.00 52.55           C  
ANISOU 6456  CA  CYS B 469     5417   7132   7420   -427    607  -1189       C  
ATOM   6457  C   CYS B 469     -23.040  -1.024  -5.689  1.00 55.34           C  
ANISOU 6457  C   CYS B 469     5840   7497   7690   -349    545  -1001       C  
ATOM   6458  O   CYS B 469     -21.854  -0.947  -5.354  1.00 55.26           O  
ANISOU 6458  O   CYS B 469     5847   7423   7728   -296    539   -948       O  
ATOM   6459  CB  CYS B 469     -23.530  -1.582  -8.091  1.00 53.31           C  
ANISOU 6459  CB  CYS B 469     5480   7416   7360   -480    600  -1317       C  
ATOM   6460  SG  CYS B 469     -23.831  -2.857  -9.337  1.00 59.44           S  
ANISOU 6460  SG  CYS B 469     6172   8201   8211   -591    681  -1576       S  
ATOM   6461  N   HIS B 470     -24.007  -0.204  -5.204  1.00 50.54           N  
ANISOU 6461  N   HIS B 470     5265   6966   6973   -345    502   -909       N  
ATOM   6462  CA  HIS B 470     -23.700   0.827  -4.211  1.00 49.17           C  
ANISOU 6462  CA  HIS B 470     5157   6800   6725   -282    454   -753       C  
ATOM   6463  C   HIS B 470     -23.408   0.136  -2.888  1.00 54.11           C  
ANISOU 6463  C   HIS B 470     5816   7277   7467   -258    465   -647       C  
ATOM   6464  O   HIS B 470     -22.535   0.597  -2.144  1.00 53.89           O  
ANISOU 6464  O   HIS B 470     5832   7223   7419   -210    432   -543       O  
ATOM   6465  CB  HIS B 470     -24.823   1.878  -4.069  1.00 49.26           C  
ANISOU 6465  CB  HIS B 470     5181   6922   6612   -284    420   -702       C  
ATOM   6466  CG  HIS B 470     -24.953   2.813  -5.237  1.00 52.69           C  
ANISOU 6466  CG  HIS B 470     5591   7510   6920   -293    385   -746       C  
ATOM   6467  ND1 HIS B 470     -23.948   3.720  -5.564  1.00 53.84           N  
ANISOU 6467  ND1 HIS B 470     5762   7704   6991   -257    355   -711       N  
ATOM   6468  CD2 HIS B 470     -25.985   2.979  -6.101  1.00 54.68           C  
ANISOU 6468  CD2 HIS B 470     5790   7878   7107   -339    369   -803       C  
ATOM   6469  CE1 HIS B 470     -24.389   4.377  -6.624  1.00 53.06           C  
ANISOU 6469  CE1 HIS B 470     5629   7745   6786   -283    325   -740       C  
ATOM   6470  NE2 HIS B 470     -25.610   3.969  -6.982  1.00 54.09           N  
ANISOU 6470  NE2 HIS B 470     5711   7927   6916   -331    327   -792       N  
ATOM   6471  N   PHE B 471     -24.067  -1.027  -2.640  1.00 51.52           N  
ANISOU 6471  N   PHE B 471     5459   6850   7265   -299    510   -673       N  
ATOM   6472  CA  PHE B 471     -23.843  -1.822  -1.431  1.00 52.29           C  
ANISOU 6472  CA  PHE B 471     5581   6803   7485   -287    521   -555       C  
ATOM   6473  C   PHE B 471     -22.422  -2.427  -1.404  1.00 54.96           C  
ANISOU 6473  C   PHE B 471     5902   7025   7955   -246    520   -537       C  
ATOM   6474  O   PHE B 471     -21.746  -2.325  -0.374  1.00 54.45           O  
ANISOU 6474  O   PHE B 471     5875   6908   7905   -208    482   -390       O  
ATOM   6475  CB  PHE B 471     -24.903  -2.915  -1.238  1.00 55.76           C  
ANISOU 6475  CB  PHE B 471     5986   7158   8040   -347    573   -580       C  
ATOM   6476  CG  PHE B 471     -24.942  -3.344   0.207  1.00 59.30           C  
ANISOU 6476  CG  PHE B 471     6476   7507   8547   -344    573   -410       C  
ATOM   6477  CD1 PHE B 471     -25.787  -2.713   1.112  1.00 62.19           C  
ANISOU 6477  CD1 PHE B 471     6889   7947   8794   -358    565   -316       C  
ATOM   6478  CD2 PHE B 471     -24.069  -4.323   0.687  1.00 64.58           C  
ANISOU 6478  CD2 PHE B 471     7134   8015   9389   -327    579   -334       C  
ATOM   6479  CE1 PHE B 471     -25.790  -3.078   2.464  1.00 64.39           C  
ANISOU 6479  CE1 PHE B 471     7210   8159   9097   -369    567   -154       C  
ATOM   6480  CE2 PHE B 471     -24.059  -4.675   2.044  1.00 68.34           C  
ANISOU 6480  CE2 PHE B 471     7649   8419   9900   -331    567   -149       C  
ATOM   6481  CZ  PHE B 471     -24.932  -4.059   2.920  1.00 65.60           C  
ANISOU 6481  CZ  PHE B 471     7355   8165   9404   -359    562    -62       C  
ATOM   6482  N   TYR B 472     -21.969  -3.036  -2.517  1.00 50.50           N  
ANISOU 6482  N   TYR B 472     5274   6429   7484   -259    562   -688       N  
ATOM   6483  CA  TYR B 472     -20.608  -3.576  -2.608  1.00 51.82           C  
ANISOU 6483  CA  TYR B 472     5405   6485   7797   -215    573   -694       C  
ATOM   6484  C   TYR B 472     -19.605  -2.432  -2.297  1.00 55.62           C  
ANISOU 6484  C   TYR B 472     5928   7047   8158   -156    507   -597       C  
ATOM   6485  O   TYR B 472     -18.728  -2.592  -1.450  1.00 56.03           O  
ANISOU 6485  O   TYR B 472     5986   7015   8290   -110    472   -470       O  
ATOM   6486  CB  TYR B 472     -20.363  -4.216  -4.000  1.00 53.94           C  
ANISOU 6486  CB  TYR B 472     5599   6745   8152   -249    645   -912       C  
ATOM   6487  CG  TYR B 472     -18.940  -4.674  -4.242  1.00 56.64           C  
ANISOU 6487  CG  TYR B 472     5888   6983   8649   -201    672   -946       C  
ATOM   6488  CD1 TYR B 472     -17.993  -3.813  -4.792  1.00 57.81           C  
ANISOU 6488  CD1 TYR B 472     6033   7237   8694   -171    654   -976       C  
ATOM   6489  CD2 TYR B 472     -18.551  -5.980  -3.967  1.00 59.06           C  
ANISOU 6489  CD2 TYR B 472     6136   7080   9224   -187    721   -949       C  
ATOM   6490  CE1 TYR B 472     -16.686  -4.228  -5.022  1.00 59.40           C  
ANISOU 6490  CE1 TYR B 472     6173   7347   9049   -127    686  -1013       C  
ATOM   6491  CE2 TYR B 472     -17.249  -6.412  -4.208  1.00 60.94           C  
ANISOU 6491  CE2 TYR B 472     6308   7212   9634   -135    751   -983       C  
ATOM   6492  CZ  TYR B 472     -16.317  -5.530  -4.730  1.00 68.13           C  
ANISOU 6492  CZ  TYR B 472     7214   8242  10432   -105    734  -1019       C  
ATOM   6493  OH  TYR B 472     -15.024  -5.939  -4.957  1.00 71.46           O  
ANISOU 6493  OH  TYR B 472     7558   8563  11031    -54    769  -1055       O  
ATOM   6494  N   ASP B 473     -19.810  -1.262  -2.919  1.00 52.02           N  
ANISOU 6494  N   ASP B 473     5497   6756   7513   -164    485   -644       N  
ATOM   6495  CA  ASP B 473     -19.010  -0.053  -2.715  1.00 51.02           C  
ANISOU 6495  CA  ASP B 473     5410   6715   7262   -122    428   -567       C  
ATOM   6496  C   ASP B 473     -19.019   0.418  -1.247  1.00 52.30           C  
ANISOU 6496  C   ASP B 473     5638   6859   7375    -97    370   -390       C  
ATOM   6497  O   ASP B 473     -17.951   0.699  -0.710  1.00 51.05           O  
ANISOU 6497  O   ASP B 473     5490   6678   7229    -59    327   -304       O  
ATOM   6498  CB  ASP B 473     -19.494   1.059  -3.653  1.00 51.86           C  
ANISOU 6498  CB  ASP B 473     5528   6988   7188   -145    418   -636       C  
ATOM   6499  CG  ASP B 473     -18.980   0.881  -5.064  1.00 60.78           C  
ANISOU 6499  CG  ASP B 473     6600   8176   8317   -171    460   -789       C  
ATOM   6500  OD1 ASP B 473     -18.340  -0.154  -5.335  1.00 61.85           O  
ANISOU 6500  OD1 ASP B 473     6681   8213   8605   -172    512   -870       O  
ATOM   6501  OD2 ASP B 473     -19.172   1.800  -5.884  1.00 68.95           O  
ANISOU 6501  OD2 ASP B 473     7641   9356   9203   -191    444   -823       O  
ATOM   6502  N   PHE B 474     -20.189   0.432  -0.587  1.00 48.17           N  
ANISOU 6502  N   PHE B 474     5152   6348   6801   -125    373   -341       N  
ATOM   6503  CA  PHE B 474     -20.287   0.800   0.832  1.00 48.41           C  
ANISOU 6503  CA  PHE B 474     5247   6377   6772   -119    333   -190       C  
ATOM   6504  C   PHE B 474     -19.489  -0.166   1.734  1.00 54.67           C  
ANISOU 6504  C   PHE B 474     6030   7043   7699   -104    312    -71       C  
ATOM   6505  O   PHE B 474     -18.775   0.280   2.633  1.00 53.85           O  
ANISOU 6505  O   PHE B 474     5962   6956   7542    -87    255     48       O  
ATOM   6506  CB  PHE B 474     -21.763   0.856   1.281  1.00 50.20           C  
ANISOU 6506  CB  PHE B 474     5499   6639   6937   -160    362   -181       C  
ATOM   6507  CG  PHE B 474     -22.018   0.643   2.758  1.00 52.74           C  
ANISOU 6507  CG  PHE B 474     5869   6927   7241   -179    353    -39       C  
ATOM   6508  CD1 PHE B 474     -21.638   1.601   3.695  1.00 55.19           C  
ANISOU 6508  CD1 PHE B 474     6242   7305   7422   -170    310     50       C  
ATOM   6509  CD2 PHE B 474     -22.637  -0.518   3.214  1.00 56.47           C  
ANISOU 6509  CD2 PHE B 474     6326   7308   7823   -216    391      4       C  
ATOM   6510  CE1 PHE B 474     -21.872   1.404   5.055  1.00 56.59           C  
ANISOU 6510  CE1 PHE B 474     6467   7478   7557   -204    304    175       C  
ATOM   6511  CE2 PHE B 474     -22.867  -0.717   4.579  1.00 59.91           C  
ANISOU 6511  CE2 PHE B 474     6808   7730   8224   -245    384    150       C  
ATOM   6512  CZ  PHE B 474     -22.488   0.247   5.489  1.00 57.36           C  
ANISOU 6512  CZ  PHE B 474     6550   7496   7750   -242    340    232       C  
ATOM   6513  N   PHE B 475     -19.645  -1.478   1.500  1.00 53.66           N  
ANISOU 6513  N   PHE B 475     5848   6789   7750   -116    357    -99       N  
ATOM   6514  CA  PHE B 475     -19.018  -2.548   2.263  1.00 55.28           C  
ANISOU 6514  CA  PHE B 475     6027   6849   8126   -102    341     25       C  
ATOM   6515  C   PHE B 475     -17.471  -2.573   2.155  1.00 59.57           C  
ANISOU 6515  C   PHE B 475     6527   7346   8762    -44    299     57       C  
ATOM   6516  O   PHE B 475     -16.804  -3.018   3.096  1.00 59.66           O  
ANISOU 6516  O   PHE B 475     6529   7279   8861    -23    248    217       O  
ATOM   6517  CB  PHE B 475     -19.572  -3.882   1.756  1.00 58.69           C  
ANISOU 6517  CB  PHE B 475     6400   7146   8755   -130    414    -51       C  
ATOM   6518  CG  PHE B 475     -19.623  -4.965   2.798  1.00 62.44           C  
ANISOU 6518  CG  PHE B 475     6867   7475   9383   -140    408    113       C  
ATOM   6519  CD1 PHE B 475     -18.703  -6.002   2.788  1.00 67.95           C  
ANISOU 6519  CD1 PHE B 475     7493   8000  10323   -102    410    158       C  
ATOM   6520  CD2 PHE B 475     -20.601  -4.958   3.784  1.00 65.59           C  
ANISOU 6520  CD2 PHE B 475     7322   7904   9696   -190    407    228       C  
ATOM   6521  CE1 PHE B 475     -18.761  -7.019   3.749  1.00 70.74           C  
ANISOU 6521  CE1 PHE B 475     7834   8211  10835   -112    398    336       C  
ATOM   6522  CE2 PHE B 475     -20.655  -5.970   4.747  1.00 70.13           C  
ANISOU 6522  CE2 PHE B 475     7891   8351  10406   -209    401    400       C  
ATOM   6523  CZ  PHE B 475     -19.742  -6.998   4.717  1.00 69.61           C  
ANISOU 6523  CZ  PHE B 475     7755   8110  10585   -170    392    462       C  
ATOM   6524  N   ASN B 476     -16.918  -2.105   1.013  1.00 54.31           N  
ANISOU 6524  N   ASN B 476     5827   6734   8075    -22    319    -86       N  
ATOM   6525  CA  ASN B 476     -15.494  -2.164   0.720  1.00 54.38           C  
ANISOU 6525  CA  ASN B 476     5776   6700   8188     29    299    -87       C  
ATOM   6526  C   ASN B 476     -14.748  -0.818   0.668  1.00 56.98           C  
ANISOU 6526  C   ASN B 476     6135   7162   8353     48    244    -76       C  
ATOM   6527  O   ASN B 476     -13.520  -0.845   0.741  1.00 57.14           O  
ANISOU 6527  O   ASN B 476     6107   7147   8457     88    211    -33       O  
ATOM   6528  CB  ASN B 476     -15.295  -2.869  -0.626  1.00 55.45           C  
ANISOU 6528  CB  ASN B 476     5827   6771   8471     30    387   -279       C  
ATOM   6529  CG  ASN B 476     -15.717  -4.316  -0.651  1.00 68.80           C  
ANISOU 6529  CG  ASN B 476     7465   8289  10387     17    448   -306       C  
ATOM   6530  OD1 ASN B 476     -15.060  -5.180  -0.078  1.00 65.15           O  
ANISOU 6530  OD1 ASN B 476     6952   7673  10129     55    433   -199       O  
ATOM   6531  ND2 ASN B 476     -16.812  -4.622  -1.335  1.00 56.27           N  
ANISOU 6531  ND2 ASN B 476     5879   6719   8782    -39    515   -447       N  
ATOM   6532  N   GLN B 477     -15.436   0.341   0.547  1.00 52.20           N  
ANISOU 6532  N   GLN B 477     5599   6698   7538     20    235   -108       N  
ATOM   6533  CA  GLN B 477     -14.716   1.614   0.416  1.00 50.11           C  
ANISOU 6533  CA  GLN B 477     5357   6541   7141     33    193   -105       C  
ATOM   6534  C   GLN B 477     -13.895   2.031   1.658  1.00 53.44           C  
ANISOU 6534  C   GLN B 477     5807   6969   7530     48    105     51       C  
ATOM   6535  O   GLN B 477     -12.926   2.776   1.471  1.00 53.63           O  
ANISOU 6535  O   GLN B 477     5816   7042   7519     65     72     49       O  
ATOM   6536  CB  GLN B 477     -15.615   2.761  -0.031  1.00 49.90           C  
ANISOU 6536  CB  GLN B 477     5387   6642   6930      5    204   -166       C  
ATOM   6537  CG  GLN B 477     -14.938   3.640  -1.086  1.00 56.97           C  
ANISOU 6537  CG  GLN B 477     6261   7622   7761     12    210   -246       C  
ATOM   6538  CD  GLN B 477     -15.625   4.947  -1.344  1.00 66.39           C  
ANISOU 6538  CD  GLN B 477     7508   8930   8787     -7    201   -259       C  
ATOM   6539  OE1 GLN B 477     -16.668   5.020  -2.003  1.00 70.10           O  
ANISOU 6539  OE1 GLN B 477     7979   9448   9208    -31    234   -326       O  
ATOM   6540  NE2 GLN B 477     -15.037   6.015  -0.854  1.00 50.47           N  
ANISOU 6540  NE2 GLN B 477     5528   6956   6693      1    154   -197       N  
ATOM   6541  N   ALA B 478     -14.198   1.532   2.884  1.00 49.20           N  
ANISOU 6541  N   ALA B 478     5302   6390   7003     35     67    187       N  
ATOM   6542  CA  ALA B 478     -13.355   1.907   4.034  1.00 49.32           C  
ANISOU 6542  CA  ALA B 478     5336   6433   6969     35    -26    334       C  
ATOM   6543  C   ALA B 478     -11.917   1.416   3.807  1.00 56.00           C  
ANISOU 6543  C   ALA B 478     6089   7207   7982     83    -62    370       C  
ATOM   6544  O   ALA B 478     -10.978   2.193   3.970  1.00 56.86           O  
ANISOU 6544  O   ALA B 478     6190   7378   8035     90   -122    401       O  
ATOM   6545  CB  ALA B 478     -13.912   1.360   5.344  1.00 50.11           C  
ANISOU 6545  CB  ALA B 478     5481   6514   7044      1    -58    483       C  
ATOM   6546  N   GLU B 479     -11.771   0.157   3.355  1.00 54.51           N  
ANISOU 6546  N   GLU B 479     5820   6882   8009    115    -18    348       N  
ATOM   6547  CA  GLU B 479     -10.505  -0.488   3.025  1.00 55.91           C  
ANISOU 6547  CA  GLU B 479     5886   6962   8397    170    -29    362       C  
ATOM   6548  C   GLU B 479      -9.839   0.195   1.826  1.00 58.27           C  
ANISOU 6548  C   GLU B 479     6142   7319   8679    186     17    204       C  
ATOM   6549  O   GLU B 479      -8.635   0.455   1.879  1.00 57.83           O  
ANISOU 6549  O   GLU B 479     6024   7268   8680    216    -28    241       O  
ATOM   6550  CB  GLU B 479     -10.709  -1.990   2.745  1.00 58.95           C  
ANISOU 6550  CB  GLU B 479     6195   7169   9034    195     30    353       C  
ATOM   6551  CG  GLU B 479     -10.014  -2.897   3.753  1.00 77.25           C  
ANISOU 6551  CG  GLU B 479     8453   9369  11530    228    -49    560       C  
ATOM   6552  CD  GLU B 479      -8.501  -2.994   3.625  1.00111.84           C  
ANISOU 6552  CD  GLU B 479    12719  13702  16074    290    -93    598       C  
ATOM   6553  OE1 GLU B 479      -7.797  -2.059   4.076  1.00109.91           O  
ANISOU 6553  OE1 GLU B 479    12490  13574  15698    285   -182    671       O  
ATOM   6554  OE2 GLU B 479      -8.015  -4.025   3.106  1.00112.71           O  
ANISOU 6554  OE2 GLU B 479    12716  13652  16458    342    -36    551       O  
ATOM   6555  N   TRP B 480     -10.618   0.502   0.759  1.00 54.21           N  
ANISOU 6555  N   TRP B 480     5657   6860   8081    159    102     38       N  
ATOM   6556  CA  TRP B 480     -10.115   1.189  -0.435  1.00 54.25           C  
ANISOU 6556  CA  TRP B 480     5632   6944   8037    158    152   -105       C  
ATOM   6557  C   TRP B 480      -9.522   2.563  -0.088  1.00 56.43           C  
ANISOU 6557  C   TRP B 480     5950   7338   8152    149     82    -46       C  
ATOM   6558  O   TRP B 480      -8.455   2.906  -0.615  1.00 56.50           O  
ANISOU 6558  O   TRP B 480     5898   7371   8197    164     88    -86       O  
ATOM   6559  CB  TRP B 480     -11.214   1.350  -1.481  1.00 53.07           C  
ANISOU 6559  CB  TRP B 480     5517   6859   7789    117    233   -257       C  
ATOM   6560  CG  TRP B 480     -11.723   0.059  -2.051  1.00 55.41           C  
ANISOU 6560  CG  TRP B 480     5761   7050   8242    112    315   -360       C  
ATOM   6561  CD1 TRP B 480     -11.065  -1.135  -2.116  1.00 59.64           C  
ANISOU 6561  CD1 TRP B 480     6203   7436   9023    147    352   -380       C  
ATOM   6562  CD2 TRP B 480     -13.002  -0.152  -2.669  1.00 55.03           C  
ANISOU 6562  CD2 TRP B 480     5744   7036   8130     64    373   -469       C  
ATOM   6563  NE1 TRP B 480     -11.865  -2.085  -2.709  1.00 59.76           N  
ANISOU 6563  NE1 TRP B 480     6194   7380   9132    120    436   -503       N  
ATOM   6564  CE2 TRP B 480     -13.057  -1.506  -3.067  1.00 60.11           C  
ANISOU 6564  CE2 TRP B 480     6314   7544   8981     65    446   -560       C  
ATOM   6565  CE3 TRP B 480     -14.096   0.683  -2.955  1.00 54.97           C  
ANISOU 6565  CE3 TRP B 480     5807   7156   7923     21    369   -500       C  
ATOM   6566  CZ2 TRP B 480     -14.163  -2.042  -3.732  1.00 59.41           C  
ANISOU 6566  CZ2 TRP B 480     6227   7458   8889     13    513   -690       C  
ATOM   6567  CZ3 TRP B 480     -15.195   0.146  -3.595  1.00 56.64           C  
ANISOU 6567  CZ3 TRP B 480     6013   7374   8133    -24    426   -610       C  
ATOM   6568  CH2 TRP B 480     -15.227  -1.202  -3.967  1.00 58.64           C  
ANISOU 6568  CH2 TRP B 480     6199   7504   8578    -33    496   -708       C  
ATOM   6569  N   GLU B 481     -10.191   3.323   0.826  1.00 49.76           N  
ANISOU 6569  N   GLU B 481     5203   6561   7142    119     23     42       N  
ATOM   6570  CA  GLU B 481      -9.720   4.627   1.311  1.00 47.98           C  
ANISOU 6570  CA  GLU B 481     5024   6433   6772    100    -42     94       C  
ATOM   6571  C   GLU B 481      -8.378   4.488   2.019  1.00 50.54           C  
ANISOU 6571  C   GLU B 481     5289   6732   7184    121   -123    200       C  
ATOM   6572  O   GLU B 481      -7.503   5.325   1.830  1.00 49.57           O  
ANISOU 6572  O   GLU B 481     5145   6667   7021    116   -150    189       O  
ATOM   6573  CB  GLU B 481     -10.746   5.286   2.250  1.00 48.08           C  
ANISOU 6573  CB  GLU B 481     5144   6505   6618     61    -73    150       C  
ATOM   6574  CG  GLU B 481     -11.905   5.931   1.513  1.00 50.88           C  
ANISOU 6574  CG  GLU B 481     5552   6919   6862     40    -10     49       C  
ATOM   6575  CD  GLU B 481     -13.105   6.291   2.366  1.00 64.82           C  
ANISOU 6575  CD  GLU B 481     7402   8717   8511     10    -14     85       C  
ATOM   6576  OE1 GLU B 481     -12.954   6.433   3.604  1.00 59.30           O  
ANISOU 6576  OE1 GLU B 481     6743   8030   7757    -11    -69    181       O  
ATOM   6577  OE2 GLU B 481     -14.201   6.463   1.784  1.00 56.94           O  
ANISOU 6577  OE2 GLU B 481     6425   7742   7467      1     40     14       O  
ATOM   6578  N   ARG B 482      -8.224   3.440   2.830  1.00 47.81           N  
ANISOU 6578  N   ARG B 482     4906   6298   6961    142   -166    313       N  
ATOM   6579  CA  ARG B 482      -6.993   3.141   3.559  1.00 48.82           C  
ANISOU 6579  CA  ARG B 482     4959   6395   7195    166   -257    442       C  
ATOM   6580  C   ARG B 482      -5.878   2.756   2.547  1.00 52.91           C  
ANISOU 6580  C   ARG B 482     5348   6852   7903    217   -213    362       C  
ATOM   6581  O   ARG B 482      -4.773   3.277   2.654  1.00 52.33           O  
ANISOU 6581  O   ARG B 482     5220   6820   7843    222   -267    394       O  
ATOM   6582  CB  ARG B 482      -7.268   2.028   4.575  1.00 50.52           C  
ANISOU 6582  CB  ARG B 482     5165   6524   7505    175   -308    597       C  
ATOM   6583  CG  ARG B 482      -6.161   1.771   5.586  1.00 71.81           C  
ANISOU 6583  CG  ARG B 482     7798   9217  10267    185   -435    781       C  
ATOM   6584  CD  ARG B 482      -6.574   0.732   6.629  1.00 93.62           C  
ANISOU 6584  CD  ARG B 482    10567  11912  13093    180   -491    962       C  
ATOM   6585  NE  ARG B 482      -7.669   1.207   7.484  1.00109.93           N  
ANISOU 6585  NE  ARG B 482    12767  14078  14925    106   -505   1005       N  
ATOM   6586  CZ  ARG B 482      -8.939   0.824   7.374  1.00128.92           C  
ANISOU 6586  CZ  ARG B 482    15236  16448  17299     87   -425    960       C  
ATOM   6587  NH1 ARG B 482      -9.297  -0.063   6.452  1.00117.78           N  
ANISOU 6587  NH1 ARG B 482    13775  14907  16071    130   -330    871       N  
ATOM   6588  NH2 ARG B 482      -9.861   1.324   8.185  1.00118.41           N  
ANISOU 6588  NH2 ARG B 482    14016  15217  15757     19   -432    994       N  
ATOM   6589  N   SER B 483      -6.196   1.930   1.521  1.00 50.49           N  
ANISOU 6589  N   SER B 483     4993   6461   7731    244   -104    238       N  
ATOM   6590  CA  SER B 483      -5.239   1.546   0.471  1.00 51.46           C  
ANISOU 6590  CA  SER B 483     4992   6530   8028    283    -32    126       C  
ATOM   6591  C   SER B 483      -4.861   2.747  -0.397  1.00 56.57           C  
ANISOU 6591  C   SER B 483     5653   7305   8535    252      5     14       C  
ATOM   6592  O   SER B 483      -3.712   2.844  -0.802  1.00 58.92           O  
ANISOU 6592  O   SER B 483     5853   7602   8934    274     19    -17       O  
ATOM   6593  CB  SER B 483      -5.776   0.412  -0.390  1.00 54.63           C  
ANISOU 6593  CB  SER B 483     5350   6822   8586    300     84     -2       C  
ATOM   6594  OG  SER B 483      -6.025  -0.732   0.411  1.00 62.52           O  
ANISOU 6594  OG  SER B 483     6325   7682   9749    330     52    115       O  
ATOM   6595  N   PHE B 484      -5.785   3.691  -0.611  1.00 52.82           N  
ANISOU 6595  N   PHE B 484     5292   6937   7840    202     17    -29       N  
ATOM   6596  CA  PHE B 484      -5.534   4.932  -1.345  1.00 52.52           C  
ANISOU 6596  CA  PHE B 484     5279   7018   7658    166     42   -102       C  
ATOM   6597  C   PHE B 484      -4.535   5.761  -0.557  1.00 56.46           C  
ANISOU 6597  C   PHE B 484     5767   7561   8124    159    -54      1       C  
ATOM   6598  O   PHE B 484      -3.481   6.092  -1.091  1.00 56.92           O  
ANISOU 6598  O   PHE B 484     5749   7646   8234    161    -37    -36       O  
ATOM   6599  CB  PHE B 484      -6.845   5.710  -1.569  1.00 53.92           C  
ANISOU 6599  CB  PHE B 484     5575   7277   7636    122     61   -139       C  
ATOM   6600  CG  PHE B 484      -6.751   6.986  -2.380  1.00 55.81           C  
ANISOU 6600  CG  PHE B 484     5843   7628   7733     84     87   -195       C  
ATOM   6601  CD1 PHE B 484      -7.154   7.015  -3.711  1.00 59.78           C  
ANISOU 6601  CD1 PHE B 484     6335   8185   8193     61    176   -315       C  
ATOM   6602  CD2 PHE B 484      -6.331   8.176  -1.793  1.00 57.81           C  
ANISOU 6602  CD2 PHE B 484     6138   7935   7890     61     20   -124       C  
ATOM   6603  CE1 PHE B 484      -7.075   8.197  -4.460  1.00 60.24           C  
ANISOU 6603  CE1 PHE B 484     6418   8349   8121     22    194   -338       C  
ATOM   6604  CE2 PHE B 484      -6.230   9.352  -2.547  1.00 59.92           C  
ANISOU 6604  CE2 PHE B 484     6428   8287   8051     26     46   -161       C  
ATOM   6605  CZ  PHE B 484      -6.611   9.357  -3.871  1.00 57.93           C  
ANISOU 6605  CZ  PHE B 484     6162   8087   7761      8    130   -256       C  
ATOM   6606  N   ARG B 485      -4.829   6.034   0.728  1.00 52.48           N  
ANISOU 6606  N   ARG B 485     5332   7070   7537    143   -153    125       N  
ATOM   6607  CA  ARG B 485      -3.964   6.819   1.608  1.00 52.54           C  
ANISOU 6607  CA  ARG B 485     5337   7133   7493    120   -255    220       C  
ATOM   6608  C   ARG B 485      -2.567   6.170   1.778  1.00 58.62           C  
ANISOU 6608  C   ARG B 485     5966   7851   8456    160   -302    281       C  
ATOM   6609  O   ARG B 485      -1.571   6.880   1.709  1.00 58.63           O  
ANISOU 6609  O   ARG B 485     5917   7904   8456    144   -333    280       O  
ATOM   6610  CB  ARG B 485      -4.631   7.060   2.970  1.00 50.75           C  
ANISOU 6610  CB  ARG B 485     5208   6937   7137     85   -341    328       C  
ATOM   6611  CG  ARG B 485      -3.828   7.969   3.905  1.00 58.77           C  
ANISOU 6611  CG  ARG B 485     6235   8032   8061     38   -445    401       C  
ATOM   6612  CD  ARG B 485      -4.480   8.100   5.259  1.00 69.25           C  
ANISOU 6612  CD  ARG B 485     7653   9404   9254     -8   -520    496       C  
ATOM   6613  NE  ARG B 485      -3.617   8.802   6.209  1.00 86.38           N  
ANISOU 6613  NE  ARG B 485     9817  11656  11350    -62   -630    564       N  
ATOM   6614  CZ  ARG B 485      -2.933   8.219   7.189  1.00108.14           C  
ANISOU 6614  CZ  ARG B 485    12518  14427  14144    -69   -744    704       C  
ATOM   6615  NH1 ARG B 485      -3.011   6.907   7.373  1.00102.79           N  
ANISOU 6615  NH1 ARG B 485    11788  13670  13597    -20   -761    806       N  
ATOM   6616  NH2 ARG B 485      -2.176   8.944   7.999  1.00 98.45           N  
ANISOU 6616  NH2 ARG B 485    11284  13293  12829   -132   -845    750       N  
ATOM   6617  N   ASP B 486      -2.496   4.846   1.966  1.00 57.35           N  
ANISOU 6617  N   ASP B 486     5733   7580   8477    213   -304    333       N  
ATOM   6618  CA  ASP B 486      -1.229   4.134   2.151  1.00 59.12           C  
ANISOU 6618  CA  ASP B 486     5806   7732   8925    265   -349    405       C  
ATOM   6619  C   ASP B 486      -0.348   4.197   0.899  1.00 64.65           C  
ANISOU 6619  C   ASP B 486     6395   8423   9748    289   -251    268       C  
ATOM   6620  O   ASP B 486       0.856   4.414   1.025  1.00 63.90           O  
ANISOU 6620  O   ASP B 486     6192   8339   9748    303   -299    310       O  
ATOM   6621  CB  ASP B 486      -1.473   2.680   2.576  1.00 61.64           C  
ANISOU 6621  CB  ASP B 486     6074   7911   9434    320   -357    491       C  
ATOM   6622  CG  ASP B 486      -1.939   2.534   4.017  1.00 70.53           C  
ANISOU 6622  CG  ASP B 486     7271   9055  10473    294   -482    680       C  
ATOM   6623  OD1 ASP B 486      -1.921   3.547   4.757  1.00 68.48           O  
ANISOU 6623  OD1 ASP B 486     7086   8920  10012    234   -569    739       O  
ATOM   6624  OD2 ASP B 486      -2.347   1.412   4.400  1.00 79.85           O  
ANISOU 6624  OD2 ASP B 486     8431  10124  11784    326   -486    765       O  
ATOM   6625  N   TYR B 487      -0.951   4.060  -0.301  1.00 63.43           N  
ANISOU 6625  N   TYR B 487     6263   8263   9576    285   -114    104       N  
ATOM   6626  CA  TYR B 487      -0.213   4.141  -1.561  1.00 64.32           C  
ANISOU 6626  CA  TYR B 487     6280   8390   9770    290     -2    -42       C  
ATOM   6627  C   TYR B 487       0.328   5.556  -1.768  1.00 68.66           C  
ANISOU 6627  C   TYR B 487     6853   9070  10164    235    -23    -52       C  
ATOM   6628  O   TYR B 487       1.514   5.702  -2.061  1.00 69.27           O  
ANISOU 6628  O   TYR B 487     6813   9157  10349    244    -12    -68       O  
ATOM   6629  CB  TYR B 487      -1.078   3.698  -2.757  1.00 64.96           C  
ANISOU 6629  CB  TYR B 487     6390   8462   9830    278    141   -214       C  
ATOM   6630  CG  TYR B 487      -0.472   4.045  -4.101  1.00 67.32           C  
ANISOU 6630  CG  TYR B 487     6622   8829  10126    252    261   -373       C  
ATOM   6631  CD1 TYR B 487       0.543   3.267  -4.655  1.00 70.88           C  
ANISOU 6631  CD1 TYR B 487     6916   9209  10808    293    341   -456       C  
ATOM   6632  CD2 TYR B 487      -0.905   5.158  -4.814  1.00 67.13           C  
ANISOU 6632  CD2 TYR B 487     6687   8943   9875    184    299   -435       C  
ATOM   6633  CE1 TYR B 487       1.114   3.593  -5.885  1.00 71.62           C  
ANISOU 6633  CE1 TYR B 487     6946   9382  10883    258    464   -608       C  
ATOM   6634  CE2 TYR B 487      -0.340   5.495  -6.043  1.00 68.62           C  
ANISOU 6634  CE2 TYR B 487     6818   9213  10043    148    409   -564       C  
ATOM   6635  CZ  TYR B 487       0.672   4.712  -6.572  1.00 76.17           C  
ANISOU 6635  CZ  TYR B 487     7622  10112  11208    180    495   -656       C  
ATOM   6636  OH  TYR B 487       1.219   5.048  -7.782  1.00 76.08           O  
ANISOU 6636  OH  TYR B 487     7553  10196  11159    132    616   -790       O  
ATOM   6637  N   VAL B 488      -0.532   6.587  -1.603  1.00 64.69           N  
ANISOU 6637  N   VAL B 488     6493   8657   9429    179    -50    -41       N  
ATOM   6638  CA  VAL B 488      -0.166   8.002  -1.771  1.00 64.27           C  
ANISOU 6638  CA  VAL B 488     6478   8710   9230    120    -66    -46       C  
ATOM   6639  C   VAL B 488       0.971   8.386  -0.799  1.00 69.03           C  
ANISOU 6639  C   VAL B 488     7018   9326   9883    114   -183     64       C  
ATOM   6640  O   VAL B 488       1.893   9.088  -1.205  1.00 68.32           O  
ANISOU 6640  O   VAL B 488     6866   9287   9805     86   -169     37       O  
ATOM   6641  CB  VAL B 488      -1.392   8.950  -1.618  1.00 66.94           C  
ANISOU 6641  CB  VAL B 488     6976   9112   9348     72    -78    -42       C  
ATOM   6642  CG1 VAL B 488      -0.980  10.414  -1.705  1.00 66.28           C  
ANISOU 6642  CG1 VAL B 488     6927   9112   9146     13    -97    -36       C  
ATOM   6643  CG2 VAL B 488      -2.454   8.658  -2.675  1.00 66.46           C  
ANISOU 6643  CG2 VAL B 488     6962   9060   9232     70     27   -146       C  
ATOM   6644  N   LEU B 489       0.920   7.899   0.453  1.00 67.37           N  
ANISOU 6644  N   LEU B 489     6818   9080   9702    132   -297    190       N  
ATOM   6645  CA  LEU B 489       1.905   8.246   1.471  1.00 69.10           C  
ANISOU 6645  CA  LEU B 489     6981   9331   9940    113   -428    305       C  
ATOM   6646  C   LEU B 489       3.276   7.556   1.311  1.00 78.31           C  
ANISOU 6646  C   LEU B 489     7960  10449  11345    164   -443    334       C  
ATOM   6647  O   LEU B 489       4.270   8.268   1.491  1.00 78.60           O  
ANISOU 6647  O   LEU B 489     7932  10547  11387    130   -497    356       O  
ATOM   6648  CB  LEU B 489       1.370   8.045   2.894  1.00 69.13           C  
ANISOU 6648  CB  LEU B 489     7061   9342   9863     99   -550    440       C  
ATOM   6649  CG  LEU B 489       0.286   9.048   3.348  1.00 72.45           C  
ANISOU 6649  CG  LEU B 489     7653   9835  10041     31   -561    422       C  
ATOM   6650  CD1 LEU B 489      -0.148   8.767   4.770  1.00 73.01           C  
ANISOU 6650  CD1 LEU B 489     7785   9923  10033     10   -669    548       C  
ATOM   6651  CD2 LEU B 489       0.740  10.516   3.186  1.00 73.86           C  
ANISOU 6651  CD2 LEU B 489     7859  10099  10105    -39   -574    373       C  
ATOM   6652  N   CYS B 490       3.380   6.233   0.965  1.00 78.17           N  
ANISOU 6652  N   CYS B 490     7845  10317  11538    242   -392    327       N  
ATOM   6653  CA  CYS B 490       4.748   5.698   0.822  1.00 81.36           C  
ANISOU 6653  CA  CYS B 490     8053  10667  12194    296   -402    352       C  
ATOM   6654  C   CYS B 490       5.403   6.154  -0.492  1.00 88.76           C  
ANISOU 6654  C   CYS B 490     8911  11640  13174    282   -269    194       C  
ATOM   6655  O   CYS B 490       6.626   6.060  -0.602  1.00 90.00           O  
ANISOU 6655  O   CYS B 490     8908  11787  13501    305   -280    207       O  
ATOM   6656  CB  CYS B 490       4.877   4.188   1.044  1.00 82.91           C  
ANISOU 6656  CB  CYS B 490     8146  10713  12645    386   -398    409       C  
ATOM   6657  SG  CYS B 490       4.263   3.140  -0.301  1.00 86.62           S  
ANISOU 6657  SG  CYS B 490     8601  11071  13238    432   -192    211       S  
ATOM   6658  N   GLN B 491       4.624   6.733  -1.434  1.00 86.82           N  
ANISOU 6658  N   GLN B 491     8773  11449  12764    237   -151     60       N  
ATOM   6659  CA  GLN B 491       5.175   7.313  -2.661  1.00 88.30           C  
ANISOU 6659  CA  GLN B 491     8907  11701  12941    202    -26    -75       C  
ATOM   6660  C   GLN B 491       5.931   8.621  -2.331  1.00 96.63           C  
ANISOU 6660  C   GLN B 491     9954  12853  13906    137    -99    -21       C  
ATOM   6661  O   GLN B 491       6.672   9.126  -3.172  1.00 97.96           O  
ANISOU 6661  O   GLN B 491    10038  13070  14112    108    -19    -96       O  
ATOM   6662  CB  GLN B 491       4.085   7.552  -3.709  1.00 88.36           C  
ANISOU 6662  CB  GLN B 491     9036  11758  12780    162     96   -201       C  
ATOM   6663  CG  GLN B 491       3.727   6.304  -4.513  1.00100.18           C  
ANISOU 6663  CG  GLN B 491    10485  13176  14401    208    221   -323       C  
ATOM   6664  CD  GLN B 491       4.767   5.949  -5.548  1.00116.45           C  
ANISOU 6664  CD  GLN B 491    12387  15234  16623    219    354   -454       C  
ATOM   6665  OE1 GLN B 491       5.627   5.091  -5.333  1.00112.95           O  
ANISOU 6665  OE1 GLN B 491    11791  14693  16433    285    356   -446       O  
ATOM   6666  NE2 GLN B 491       4.698   6.584  -6.705  1.00106.66           N  
ANISOU 6666  NE2 GLN B 491    11175  14105  15245    151    471   -575       N  
ATOM   6667  N   ALA B 492       5.761   9.138  -1.092  1.00 94.68           N  
ANISOU 6667  N   ALA B 492     9790  12637  13546    105   -247    103       N  
ATOM   6668  CA  ALA B 492       6.444  10.311  -0.534  1.00 95.46           C  
ANISOU 6668  CA  ALA B 492     9886  12818  13567     36   -339    158       C  
ATOM   6669  C   ALA B 492       7.597   9.860   0.404  1.00101.87           C  
ANISOU 6669  C   ALA B 492    10547  13611  14547     65   -471    275       C  
ATOM   6670  O   ALA B 492       8.699  10.407   0.330  1.00103.00           O  
ANISOU 6670  O   ALA B 492    10578  13799  14760     34   -492    277       O  
ATOM   6671  CB  ALA B 492       5.447  11.190   0.220  1.00 95.05           C  
ANISOU 6671  CB  ALA B 492    10015  12815  13285    -26   -410    198       C  
ATOM   6672  N   ASN B 493       7.334   8.847   1.263  1.00 98.95           N  
ANISOU 6672  N   ASN B 493    10168  13178  14251    122   -560    383       N  
ATOM   6673  CA  ASN B 493       8.282   8.248   2.212  1.00132.98           C  
ANISOU 6673  CA  ASN B 493    14335  17465  18725    157   -703    530       C  
ATOM   6674  C   ASN B 493       7.817   6.848   2.623  1.00150.68           C  
ANISOU 6674  C   ASN B 493    16555  19592  21104    244   -726    617       C  
ATOM   6675  O   ASN B 493       8.501   5.857   2.368  1.00109.32           O  
ANISOU 6675  O   ASN B 493    11149  14257  16132    327   -709    643       O  
ATOM   6676  CB  ASN B 493       8.450   9.130   3.450  1.00134.64           C  
ANISOU 6676  CB  ASN B 493    14608  17785  18767     72   -873    639       C  
ATOM   6677  N   ASP B 506       9.363  -0.328  -3.740  1.00 94.22           N  
ANISOU 6677  N   ASP B 506     8522  11557  15720    753    326   -259       N  
ATOM   6678  CA  ASP B 506       8.128  -0.205  -4.505  1.00 92.07           C  
ANISOU 6678  CA  ASP B 506     8428  11339  15215    687    443   -421       C  
ATOM   6679  C   ASP B 506       6.924   0.017  -3.590  1.00 92.79           C  
ANISOU 6679  C   ASP B 506     8722  11457  15078    657    305   -271       C  
ATOM   6680  O   ASP B 506       6.905  -0.455  -2.450  1.00 92.43           O  
ANISOU 6680  O   ASP B 506     8662  11327  15130    706    156    -66       O  
ATOM   6681  CB  ASP B 506       7.901  -1.446  -5.386  1.00 95.50           C  
ANISOU 6681  CB  ASP B 506     8779  11621  15886    732    630   -622       C  
ATOM   6682  CG  ASP B 506       7.668  -2.726  -4.611  1.00109.77           C  
ANISOU 6682  CG  ASP B 506    10528  13207  17974    826    571   -503       C  
ATOM   6683  OD1 ASP B 506       8.666  -3.359  -4.198  1.00113.13           O  
ANISOU 6683  OD1 ASP B 506    10759  13496  18728    918    529   -406       O  
ATOM   6684  OD2 ASP B 506       6.487  -3.096  -4.418  1.00115.70           O  
ANISOU 6684  OD2 ASP B 506    11418  13917  18625    807    565   -499       O  
ATOM   6685  N   CYS B 507       5.915   0.725  -4.106  1.00 86.68           N  
ANISOU 6685  N   CYS B 507     8127  10805  14001    573    358   -369       N  
ATOM   6686  CA  CYS B 507       4.678   1.020  -3.387  1.00 84.16           C  
ANISOU 6686  CA  CYS B 507     8001  10523  13452    537    257   -262       C  
ATOM   6687  C   CYS B 507       3.519   0.367  -4.114  1.00 84.47           C  
ANISOU 6687  C   CYS B 507     8123  10517  13456    521    382   -414       C  
ATOM   6688  O   CYS B 507       3.323   0.603  -5.307  1.00 83.45           O  
ANISOU 6688  O   CYS B 507     8013  10466  13229    471    523   -609       O  
ATOM   6689  CB  CYS B 507       4.487   2.526  -3.225  1.00 82.98           C  
ANISOU 6689  CB  CYS B 507     7987  10559  12985    452    184   -215       C  
ATOM   6690  SG  CYS B 507       5.503   3.252  -1.911  1.00 87.29           S  
ANISOU 6690  SG  CYS B 507     8488  11153  13524    453    -23     13       S  
ATOM   6691  N   GLU B 508       2.799  -0.515  -3.413  1.00 79.98           N  
ANISOU 6691  N   GLU B 508     7589   9820  12979    560    330   -323       N  
ATOM   6692  CA  GLU B 508       1.693  -1.281  -3.993  1.00 79.59           C  
ANISOU 6692  CA  GLU B 508     7600   9702  12938    547    439   -457       C  
ATOM   6693  C   GLU B 508       0.324  -0.777  -3.551  1.00 79.38           C  
ANISOU 6693  C   GLU B 508     7770   9759  12632    489    372   -393       C  
ATOM   6694  O   GLU B 508       0.164  -0.271  -2.435  1.00 78.82           O  
ANISOU 6694  O   GLU B 508     7774   9730  12442    483    225   -202       O  
ATOM   6695  CB  GLU B 508       1.809  -2.779  -3.627  1.00 83.13           C  
ANISOU 6695  CB  GLU B 508     7932   9917  13736    632    452   -414       C  
ATOM   6696  CG  GLU B 508       3.040  -3.488  -4.174  1.00100.02           C  
ANISOU 6696  CG  GLU B 508     9857  11933  16213    701    550   -510       C  
ATOM   6697  CD  GLU B 508       2.884  -4.126  -5.542  1.00130.05           C  
ANISOU 6697  CD  GLU B 508    13603  15687  20123    683    767   -806       C  
ATOM   6698  OE1 GLU B 508       2.231  -5.192  -5.632  1.00125.44           O  
ANISOU 6698  OE1 GLU B 508    13013  14947  19704    702    832   -870       O  
ATOM   6699  OE2 GLU B 508       3.460  -3.590  -6.517  1.00128.53           O  
ANISOU 6699  OE2 GLU B 508    13366  15613  19858    643    877   -976       O  
ATOM   6700  N   ILE B 509      -0.666  -0.937  -4.441  1.00 72.72           N  
ANISOU 6700  N   ILE B 509     6999   8943  11687    441    484   -563       N  
ATOM   6701  CA  ILE B 509      -2.076  -0.646  -4.192  1.00 69.17           C  
ANISOU 6701  CA  ILE B 509     6713   8554  11013    390    448   -534       C  
ATOM   6702  C   ILE B 509      -2.633  -1.969  -3.687  1.00 69.76           C  
ANISOU 6702  C   ILE B 509     6765   8445  11294    431    452   -494       C  
ATOM   6703  O   ILE B 509      -2.739  -2.906  -4.475  1.00 69.66           O  
ANISOU 6703  O   ILE B 509     6684   8335  11448    437    579   -661       O  
ATOM   6704  CB  ILE B 509      -2.799  -0.078  -5.462  1.00 71.28           C  
ANISOU 6704  CB  ILE B 509     7057   8969  11058    310    554   -724       C  
ATOM   6705  CG1 ILE B 509      -2.144   1.246  -5.924  1.00 71.35           C  
ANISOU 6705  CG1 ILE B 509     7078   9146  10887    270    548   -735       C  
ATOM   6706  CG2 ILE B 509      -4.308   0.130  -5.206  1.00 70.46           C  
ANISOU 6706  CG2 ILE B 509     7101   8913  10757    266    515   -691       C  
ATOM   6707  CD1 ILE B 509      -2.388   1.658  -7.403  1.00 79.82           C  
ANISOU 6707  CD1 ILE B 509     8163  10356  11809    196    677   -932       C  
ATOM   6708  N   LYS B 510      -2.860  -2.088  -2.363  1.00 65.40           N  
ANISOU 6708  N   LYS B 510     6257   7841  10751    455    318   -272       N  
ATOM   6709  CA  LYS B 510      -3.349  -3.321  -1.719  1.00 66.34           C  
ANISOU 6709  CA  LYS B 510     6356   7781  11068    491    302   -181       C  
ATOM   6710  C   LYS B 510      -4.657  -3.791  -2.375  1.00 70.28           C  
ANISOU 6710  C   LYS B 510     6929   8262  11514    442    406   -335       C  
ATOM   6711  O   LYS B 510      -4.728  -4.916  -2.874  1.00 72.34           O  
ANISOU 6711  O   LYS B 510     7109   8367  12011    462    507   -449       O  
ATOM   6712  CB  LYS B 510      -3.533  -3.124  -0.195  1.00 68.26           C  
ANISOU 6712  CB  LYS B 510     6668   8038  11229    494    135     89       C  
ATOM   6713  CG  LYS B 510      -3.767  -4.430   0.577  1.00 78.40           C  
ANISOU 6713  CG  LYS B 510     7906   9129  12751    536    102    236       C  
ATOM   6714  CD  LYS B 510      -4.116  -4.210   2.049  1.00 84.26           C  
ANISOU 6714  CD  LYS B 510     8735   9922  13357    516    -55    498       C  
ATOM   6715  CE  LYS B 510      -2.942  -4.488   2.962  1.00 92.27           C  
ANISOU 6715  CE  LYS B 510     9638  10882  14537    571   -183    718       C  
ATOM   6716  NZ  LYS B 510      -3.166  -3.968   4.340  1.00 94.97           N  
ANISOU 6716  NZ  LYS B 510    10074  11334  14678    527   -341    955       N  
ATOM   6717  N   ASN B 511      -5.664  -2.913  -2.398  1.00 64.05           N  
ANISOU 6717  N   ASN B 511     6282   7627  10426    375    383   -348       N  
ATOM   6718  CA  ASN B 511      -6.977  -3.149  -2.995  1.00 62.98           C  
ANISOU 6718  CA  ASN B 511     6221   7514  10193    317    460   -480       C  
ATOM   6719  C   ASN B 511      -7.481  -1.841  -3.588  1.00 65.75           C  
ANISOU 6719  C   ASN B 511     6673   8079  10231    254    461   -554       C  
ATOM   6720  O   ASN B 511      -6.938  -0.777  -3.281  1.00 65.28           O  
ANISOU 6720  O   ASN B 511     6645   8127  10031    255    388   -468       O  
ATOM   6721  CB  ASN B 511      -7.973  -3.739  -1.982  1.00 60.77           C  
ANISOU 6721  CB  ASN B 511     6007   7148   9936    312    403   -337       C  
ATOM   6722  CG  ASN B 511      -7.939  -3.113  -0.613  1.00 83.68           C  
ANISOU 6722  CG  ASN B 511     8981  10106  12707    318    259    -98       C  
ATOM   6723  OD1 ASN B 511      -8.314  -1.957  -0.414  1.00 80.75           O  
ANISOU 6723  OD1 ASN B 511     8710   9896  12076    279    211    -73       O  
ATOM   6724  ND2 ASN B 511      -7.480  -3.869   0.364  1.00 78.36           N  
ANISOU 6724  ND2 ASN B 511     8254   9302  12216    363    189     84       N  
ATOM   6725  N   ARG B 512      -8.478  -1.919  -4.471  1.00 60.75           N  
ANISOU 6725  N   ARG B 512     6079   7503   9501    197    542   -714       N  
ATOM   6726  CA  ARG B 512      -9.013  -0.751  -5.155  1.00 58.51           C  
ANISOU 6726  CA  ARG B 512     5876   7416   8941    137    545   -779       C  
ATOM   6727  C   ARG B 512     -10.510  -0.950  -5.546  1.00 61.37           C  
ANISOU 6727  C   ARG B 512     6303   7820   9193     77    579   -860       C  
ATOM   6728  O   ARG B 512     -10.977  -2.096  -5.617  1.00 61.61           O  
ANISOU 6728  O   ARG B 512     6299   7730   9381     72    634   -929       O  
ATOM   6729  CB  ARG B 512      -8.149  -0.462  -6.412  1.00 57.16           C  
ANISOU 6729  CB  ARG B 512     5634   7330   8755    116    633   -940       C  
ATOM   6730  CG  ARG B 512      -8.552  -1.253  -7.646  1.00 63.78           C  
ANISOU 6730  CG  ARG B 512     6419   8162   9651     68    766  -1171       C  
ATOM   6731  CD  ARG B 512      -7.386  -1.706  -8.478  1.00 65.96           C  
ANISOU 6731  CD  ARG B 512     6574   8410  10078     79    871  -1318       C  
ATOM   6732  NE  ARG B 512      -7.061  -0.761  -9.542  1.00 62.14           N  
ANISOU 6732  NE  ARG B 512     6098   8124   9389     19    915  -1411       N  
ATOM   6733  CZ  ARG B 512      -7.112  -1.038 -10.842  1.00 70.60           C  
ANISOU 6733  CZ  ARG B 512     7130   9288  10406    -54   1038  -1630       C  
ATOM   6734  NH1 ARG B 512      -7.521  -2.231 -11.260  1.00 53.28           N  
ANISOU 6734  NH1 ARG B 512     4889   7002   8353    -78   1132  -1801       N  
ATOM   6735  NH2 ARG B 512      -6.753  -0.129 -11.732  1.00 56.78           N  
ANISOU 6735  NH2 ARG B 512     5388   7727   8459   -112   1069  -1681       N  
ATOM   6736  N   PRO B 513     -11.265   0.133  -5.865  1.00 55.82           N  
ANISOU 6736  N   PRO B 513     5685   7283   8242     31    549   -858       N  
ATOM   6737  CA  PRO B 513     -12.644  -0.063  -6.342  1.00 54.59           C  
ANISOU 6737  CA  PRO B 513     5569   7180   7992    -27    579   -942       C  
ATOM   6738  C   PRO B 513     -12.690  -0.895  -7.632  1.00 59.28           C  
ANISOU 6738  C   PRO B 513     6091   7781   8651    -78    693  -1166       C  
ATOM   6739  O   PRO B 513     -11.731  -0.918  -8.394  1.00 59.16           O  
ANISOU 6739  O   PRO B 513     6013   7799   8667    -82    754  -1270       O  
ATOM   6740  CB  PRO B 513     -13.137   1.362  -6.582  1.00 54.40           C  
ANISOU 6740  CB  PRO B 513     5622   7333   7715    -57    526   -892       C  
ATOM   6741  CG  PRO B 513     -12.274   2.215  -5.732  1.00 58.03           C  
ANISOU 6741  CG  PRO B 513     6106   7791   8150    -10    452   -744       C  
ATOM   6742  CD  PRO B 513     -10.929   1.572  -5.808  1.00 55.23           C  
ANISOU 6742  CD  PRO B 513     5662   7345   7979     28    488   -777       C  
ATOM   6743  N   SER B 514     -13.799  -1.596  -7.853  1.00 56.77           N  
ANISOU 6743  N   SER B 514     5778   7434   8360   -123    728  -1249       N  
ATOM   6744  CA  SER B 514     -14.025  -2.429  -9.026  1.00 57.35           C  
ANISOU 6744  CA  SER B 514     5788   7518   8483   -190    836  -1480       C  
ATOM   6745  C   SER B 514     -14.786  -1.627 -10.073  1.00 61.69           C  
ANISOU 6745  C   SER B 514     6372   8297   8770   -273    833  -1563       C  
ATOM   6746  O   SER B 514     -15.919  -1.192  -9.820  1.00 61.87           O  
ANISOU 6746  O   SER B 514     6454   8390   8663   -296    770  -1489       O  
ATOM   6747  CB  SER B 514     -14.796  -3.691  -8.635  1.00 60.11           C  
ANISOU 6747  CB  SER B 514     6118   7706   9014   -203    869  -1520       C  
ATOM   6748  OG  SER B 514     -15.417  -4.319  -9.744  1.00 64.53           O  
ANISOU 6748  OG  SER B 514     6635   8312   9571   -292    960  -1750       O  
ATOM   6749  N   LEU B 515     -14.167  -1.445 -11.252  1.00 58.23           N  
ANISOU 6749  N   LEU B 515     5888   7979   8256   -322    901  -1711       N  
ATOM   6750  CA  LEU B 515     -14.764  -0.729 -12.385  1.00 57.80           C  
ANISOU 6750  CA  LEU B 515     5854   8162   7945   -414    899  -1786       C  
ATOM   6751  C   LEU B 515     -15.861  -1.554 -13.038  1.00 63.03           C  
ANISOU 6751  C   LEU B 515     6494   8863   8591   -505    944  -1955       C  
ATOM   6752  O   LEU B 515     -16.759  -0.973 -13.645  1.00 64.11           O  
ANISOU 6752  O   LEU B 515     6657   9185   8516   -575    901  -1960       O  
ATOM   6753  CB  LEU B 515     -13.707  -0.309 -13.424  1.00 58.24           C  
ANISOU 6753  CB  LEU B 515     5868   8349   7912   -450    964  -1885       C  
ATOM   6754  CG  LEU B 515     -12.695   0.768 -12.981  1.00 61.49           C  
ANISOU 6754  CG  LEU B 515     6304   8779   8280   -385    910  -1717       C  
ATOM   6755  CD1 LEU B 515     -12.051   1.417 -14.180  1.00 62.24           C  
ANISOU 6755  CD1 LEU B 515     6369   9061   8219   -451    967  -1802       C  
ATOM   6756  CD2 LEU B 515     -13.341   1.851 -12.090  1.00 59.85           C  
ANISOU 6756  CD2 LEU B 515     6187   8606   7947   -346    780  -1494       C  
ATOM   6757  N   LEU B 516     -15.816  -2.898 -12.880  1.00 59.33           N  
ANISOU 6757  N   LEU B 516     5970   8213   8359   -505   1025  -2085       N  
ATOM   6758  CA  LEU B 516     -16.849  -3.810 -13.369  1.00 59.46           C  
ANISOU 6758  CA  LEU B 516     5959   8230   8404   -594   1073  -2255       C  
ATOM   6759  C   LEU B 516     -18.159  -3.536 -12.611  1.00 59.76           C  
ANISOU 6759  C   LEU B 516     6058   8269   8379   -588    973  -2102       C  
ATOM   6760  O   LEU B 516     -19.197  -3.342 -13.245  1.00 58.92           O  
ANISOU 6760  O   LEU B 516     5956   8319   8111   -675    948  -2165       O  
ATOM   6761  CB  LEU B 516     -16.415  -5.285 -13.227  1.00 60.97           C  
ANISOU 6761  CB  LEU B 516     6073   8182   8909   -583   1186  -2408       C  
ATOM   6762  CG  LEU B 516     -17.505  -6.340 -13.452  1.00 66.66           C  
ANISOU 6762  CG  LEU B 516     6767   8838   9724   -665   1235  -2563       C  
ATOM   6763  CD1 LEU B 516     -17.761  -6.564 -14.930  1.00 68.42           C  
ANISOU 6763  CD1 LEU B 516     6942   9243   9810   -804   1320  -2843       C  
ATOM   6764  CD2 LEU B 516     -17.159  -7.642 -12.753  1.00 69.53           C  
ANISOU 6764  CD2 LEU B 516     7074   8895  10447   -610   1305  -2589       C  
ATOM   6765  N   VAL B 517     -18.087  -3.464 -11.265  1.00 54.55           N  
ANISOU 6765  N   VAL B 517     5439   7453   7834   -491    913  -1899       N  
ATOM   6766  CA  VAL B 517     -19.223  -3.170 -10.386  1.00 53.33           C  
ANISOU 6766  CA  VAL B 517     5341   7287   7633   -477    830  -1743       C  
ATOM   6767  C   VAL B 517     -19.848  -1.819 -10.817  1.00 56.70           C  
ANISOU 6767  C   VAL B 517     5813   7945   7784   -503    748  -1669       C  
ATOM   6768  O   VAL B 517     -21.074  -1.716 -10.932  1.00 56.53           O  
ANISOU 6768  O   VAL B 517     5797   8004   7677   -553    713  -1669       O  
ATOM   6769  CB  VAL B 517     -18.800  -3.207  -8.886  1.00 56.78           C  
ANISOU 6769  CB  VAL B 517     5816   7545   8211   -374    784  -1535       C  
ATOM   6770  CG1 VAL B 517     -19.838  -2.532  -7.967  1.00 55.83           C  
ANISOU 6770  CG1 VAL B 517     5766   7463   7985   -358    698  -1360       C  
ATOM   6771  CG2 VAL B 517     -18.547  -4.643  -8.433  1.00 57.38           C  
ANISOU 6771  CG2 VAL B 517     5841   7385   8575   -359    852  -1583       C  
ATOM   6772  N   GLU B 518     -18.993  -0.831 -11.143  1.00 52.76           N  
ANISOU 6772  N   GLU B 518     5332   7550   7162   -476    723  -1613       N  
ATOM   6773  CA  GLU B 518     -19.418   0.486 -11.613  1.00 51.35           C  
ANISOU 6773  CA  GLU B 518     5189   7575   6748   -496    649  -1527       C  
ATOM   6774  C   GLU B 518     -20.116   0.378 -12.958  1.00 57.23           C  
ANISOU 6774  C   GLU B 518     5891   8509   7343   -609    666  -1678       C  
ATOM   6775  O   GLU B 518     -21.177   0.977 -13.136  1.00 58.14           O  
ANISOU 6775  O   GLU B 518     6018   8750   7322   -639    595  -1612       O  
ATOM   6776  CB  GLU B 518     -18.235   1.463 -11.687  1.00 51.78           C  
ANISOU 6776  CB  GLU B 518     5264   7677   6733   -450    632  -1441       C  
ATOM   6777  CG  GLU B 518     -17.449   1.590 -10.391  1.00 58.48           C  
ANISOU 6777  CG  GLU B 518     6146   8358   7717   -350    608  -1301       C  
ATOM   6778  CD  GLU B 518     -18.211   1.645  -9.077  1.00 70.48           C  
ANISOU 6778  CD  GLU B 518     7716   9773   9289   -299    549  -1156       C  
ATOM   6779  OE1 GLU B 518     -19.374   2.108  -9.071  1.00 48.21           O  
ANISOU 6779  OE1 GLU B 518     4921   7033   6363   -322    504  -1111       O  
ATOM   6780  OE2 GLU B 518     -17.632   1.232  -8.046  1.00 65.89           O  
ANISOU 6780  OE2 GLU B 518     7145   9038   8854   -240    547  -1083       O  
ATOM   6781  N   LYS B 519     -19.562  -0.416 -13.883  1.00 53.95           N  
ANISOU 6781  N   LYS B 519     5420   8117   6960   -677    760  -1884       N  
ATOM   6782  CA  LYS B 519     -20.183  -0.629 -15.182  1.00 54.73           C  
ANISOU 6782  CA  LYS B 519     5476   8413   6907   -806    783  -2054       C  
ATOM   6783  C   LYS B 519     -21.558  -1.308 -15.046  1.00 58.95           C  
ANISOU 6783  C   LYS B 519     5991   8927   7482   -859    764  -2110       C  
ATOM   6784  O   LYS B 519     -22.474  -0.952 -15.792  1.00 58.77           O  
ANISOU 6784  O   LYS B 519     5950   9102   7279   -944    712  -2134       O  
ATOM   6785  CB  LYS B 519     -19.270  -1.457 -16.079  1.00 58.90           C  
ANISOU 6785  CB  LYS B 519     5945   8947   7487   -870    910  -2292       C  
ATOM   6786  CG  LYS B 519     -18.103  -0.665 -16.646  1.00 65.27           C  
ANISOU 6786  CG  LYS B 519     6755   9870   8175   -865    932  -2271       C  
ATOM   6787  CD  LYS B 519     -17.375  -1.482 -17.664  1.00 63.66           C  
ANISOU 6787  CD  LYS B 519     6483   9708   7998   -951   1071  -2536       C  
ATOM   6788  CE  LYS B 519     -16.062  -0.881 -18.044  1.00 63.32           C  
ANISOU 6788  CE  LYS B 519     6432   9732   7896   -933   1116  -2521       C  
ATOM   6789  NZ  LYS B 519     -15.471  -1.625 -19.182  1.00 74.63           N  
ANISOU 6789  NZ  LYS B 519     7792  11239   9327  -1035   1265  -2804       N  
ATOM   6790  N   ILE B 520     -21.705  -2.269 -14.092  1.00 55.90           N  
ANISOU 6790  N   ILE B 520     5601   8306   7332   -813    802  -2118       N  
ATOM   6791  CA  ILE B 520     -22.978  -2.976 -13.846  1.00 56.74           C  
ANISOU 6791  CA  ILE B 520     5686   8365   7509   -862    794  -2164       C  
ATOM   6792  C   ILE B 520     -24.008  -1.957 -13.324  1.00 58.60           C  
ANISOU 6792  C   ILE B 520     5959   8689   7617   -830    678  -1961       C  
ATOM   6793  O   ILE B 520     -25.127  -1.904 -13.828  1.00 57.69           O  
ANISOU 6793  O   ILE B 520     5811   8706   7403   -907    637  -2001       O  
ATOM   6794  CB  ILE B 520     -22.832  -4.214 -12.897  1.00 59.96           C  
ANISOU 6794  CB  ILE B 520     6081   8488   8211   -819    864  -2191       C  
ATOM   6795  CG1 ILE B 520     -21.898  -5.293 -13.501  1.00 61.72           C  
ANISOU 6795  CG1 ILE B 520     6246   8608   8595   -854    991  -2415       C  
ATOM   6796  CG2 ILE B 520     -24.199  -4.818 -12.566  1.00 59.18           C  
ANISOU 6796  CG2 ILE B 520     5964   8344   8179   -873    852  -2210       C  
ATOM   6797  CD1 ILE B 520     -21.306  -6.289 -12.479  1.00 65.64           C  
ANISOU 6797  CD1 ILE B 520     6731   8802   9408   -772   1050  -2377       C  
ATOM   6798  N   ASN B 521     -23.595  -1.123 -12.357  1.00 54.80           N  
ANISOU 6798  N   ASN B 521     5538   8143   7139   -719    627  -1755       N  
ATOM   6799  CA  ASN B 521     -24.418  -0.066 -11.778  1.00 53.78           C  
ANISOU 6799  CA  ASN B 521     5445   8076   6913   -674    533  -1566       C  
ATOM   6800  C   ASN B 521     -24.906   0.874 -12.882  1.00 58.80           C  
ANISOU 6800  C   ASN B 521     6056   8960   7324   -733    466  -1559       C  
ATOM   6801  O   ASN B 521     -26.092   1.204 -12.902  1.00 59.23           O  
ANISOU 6801  O   ASN B 521     6088   9098   7319   -756    405  -1507       O  
ATOM   6802  CB  ASN B 521     -23.620   0.710 -10.716  1.00 52.78           C  
ANISOU 6802  CB  ASN B 521     5387   7851   6818   -560    505  -1385       C  
ATOM   6803  CG  ASN B 521     -24.446   1.605  -9.812  1.00 61.94           C  
ANISOU 6803  CG  ASN B 521     6585   9012   7938   -506    436  -1209       C  
ATOM   6804  OD1 ASN B 521     -25.374   2.292 -10.243  1.00 57.14           O  
ANISOU 6804  OD1 ASN B 521     5956   8540   7214   -531    380  -1172       O  
ATOM   6805  ND2 ASN B 521     -24.093   1.660  -8.538  1.00 47.89           N  
ANISOU 6805  ND2 ASN B 521     4857   7085   6255   -430    437  -1095       N  
ATOM   6806  N   LEU B 522     -23.999   1.288 -13.796  1.00 55.16           N  
ANISOU 6806  N   LEU B 522     5593   8618   6745   -759    477  -1602       N  
ATOM   6807  CA  LEU B 522     -24.320   2.181 -14.913  1.00 56.22           C  
ANISOU 6807  CA  LEU B 522     5705   9002   6655   -824    412  -1575       C  
ATOM   6808  C   LEU B 522     -25.217   1.489 -15.941  1.00 62.51           C  
ANISOU 6808  C   LEU B 522     6431   9951   7368   -957    414  -1743       C  
ATOM   6809  O   LEU B 522     -26.073   2.149 -16.528  1.00 62.13           O  
ANISOU 6809  O   LEU B 522     6352  10091   7165  -1005    326  -1675       O  
ATOM   6810  CB  LEU B 522     -23.056   2.728 -15.599  1.00 56.38           C  
ANISOU 6810  CB  LEU B 522     5741   9109   6572   -830    438  -1580       C  
ATOM   6811  CG  LEU B 522     -22.223   3.743 -14.817  1.00 58.93           C  
ANISOU 6811  CG  LEU B 522     6125   9344   6924   -718    412  -1398       C  
ATOM   6812  CD1 LEU B 522     -20.964   4.047 -15.561  1.00 60.03           C  
ANISOU 6812  CD1 LEU B 522     6263   9559   6986   -743    460  -1441       C  
ATOM   6813  CD2 LEU B 522     -22.991   5.024 -14.552  1.00 57.94           C  
ANISOU 6813  CD2 LEU B 522     6019   9287   6709   -675    306  -1193       C  
ATOM   6814  N   PHE B 523     -25.032   0.168 -16.152  1.00 61.33           N  
ANISOU 6814  N   PHE B 523     6251   9719   7332  -1019    511  -1960       N  
ATOM   6815  CA  PHE B 523     -25.889  -0.604 -17.052  1.00 63.53           C  
ANISOU 6815  CA  PHE B 523     6462  10126   7552  -1159    524  -2150       C  
ATOM   6816  C   PHE B 523     -27.328  -0.551 -16.519  1.00 67.02           C  
ANISOU 6816  C   PHE B 523     6879  10559   8028  -1155    447  -2061       C  
ATOM   6817  O   PHE B 523     -28.252  -0.234 -17.262  1.00 67.75           O  
ANISOU 6817  O   PHE B 523     6918  10857   7968  -1242    371  -2069       O  
ATOM   6818  CB  PHE B 523     -25.393  -2.062 -17.184  1.00 66.91           C  
ANISOU 6818  CB  PHE B 523     6861  10408   8152  -1211    658  -2402       C  
ATOM   6819  CG  PHE B 523     -26.414  -3.051 -17.710  1.00 70.86           C  
ANISOU 6819  CG  PHE B 523     7294  10956   8673  -1342    682  -2602       C  
ATOM   6820  CD1 PHE B 523     -26.687  -3.141 -19.073  1.00 76.67           C  
ANISOU 6820  CD1 PHE B 523     7977  11947   9207  -1497    680  -2777       C  
ATOM   6821  CD2 PHE B 523     -27.078  -3.914 -16.847  1.00 73.56           C  
ANISOU 6821  CD2 PHE B 523     7624  11094   9233  -1323    708  -2619       C  
ATOM   6822  CE1 PHE B 523     -27.617  -4.066 -19.561  1.00 79.14           C  
ANISOU 6822  CE1 PHE B 523     8223  12310   9538  -1631    700  -2978       C  
ATOM   6823  CE2 PHE B 523     -28.008  -4.842 -17.338  1.00 78.49           C  
ANISOU 6823  CE2 PHE B 523     8181  11754   9890  -1453    734  -2813       C  
ATOM   6824  CZ  PHE B 523     -28.272  -4.909 -18.691  1.00 78.21           C  
ANISOU 6824  CZ  PHE B 523     8090  11972   9655  -1607    728  -2998       C  
ATOM   6825  N   ALA B 524     -27.494  -0.842 -15.222  1.00 61.66           N  
ANISOU 6825  N   ALA B 524     6233   9652   7544  -1059    464  -1969       N  
ATOM   6826  CA  ALA B 524     -28.775  -0.837 -14.538  1.00 60.74           C  
ANISOU 6826  CA  ALA B 524     6095   9497   7488  -1046    414  -1882       C  
ATOM   6827  C   ALA B 524     -29.343   0.579 -14.411  1.00 62.35           C  
ANISOU 6827  C   ALA B 524     6303   9827   7560   -988    300  -1668       C  
ATOM   6828  O   ALA B 524     -30.560   0.747 -14.506  1.00 61.69           O  
ANISOU 6828  O   ALA B 524     6161   9834   7444  -1023    237  -1634       O  
ATOM   6829  CB  ALA B 524     -28.620  -1.455 -13.165  1.00 60.60           C  
ANISOU 6829  CB  ALA B 524     6119   9210   7697   -962    474  -1829       C  
ATOM   6830  N   MET B 525     -28.477   1.591 -14.209  1.00 57.33           N  
ANISOU 6830  N   MET B 525     5726   9191   6865   -901    277  -1528       N  
ATOM   6831  CA  MET B 525     -28.945   2.964 -14.038  1.00 56.58           C  
ANISOU 6831  CA  MET B 525     5636   9182   6682   -837    180  -1323       C  
ATOM   6832  C   MET B 525     -29.407   3.510 -15.404  1.00 61.66           C  
ANISOU 6832  C   MET B 525     6213  10092   7121   -928     96  -1323       C  
ATOM   6833  O   MET B 525     -30.593   3.834 -15.547  1.00 62.56           O  
ANISOU 6833  O   MET B 525     6263  10305   7202   -948     17  -1256       O  
ATOM   6834  CB  MET B 525     -27.892   3.851 -13.333  1.00 57.26           C  
ANISOU 6834  CB  MET B 525     5803   9167   6788   -724    186  -1182       C  
ATOM   6835  CG  MET B 525     -28.385   5.244 -12.965  1.00 60.07           C  
ANISOU 6835  CG  MET B 525     6164   9556   7103   -647    104   -979       C  
ATOM   6836  SD  MET B 525     -28.348   6.412 -14.368  1.00 65.58           S  
ANISOU 6836  SD  MET B 525     6822  10505   7589   -692      8   -884       S  
ATOM   6837  CE  MET B 525     -26.574   6.559 -14.627  1.00 61.63           C  
ANISOU 6837  CE  MET B 525     6394   9981   7043   -682     68   -913       C  
ATOM   6838  N   PHE B 526     -28.522   3.532 -16.410  1.00 57.60           N  
ANISOU 6838  N   PHE B 526     5707   9705   6475   -991    114  -1400       N  
ATOM   6839  CA  PHE B 526     -28.892   3.996 -17.758  1.00 58.33           C  
ANISOU 6839  CA  PHE B 526     5741  10077   6346  -1097     35  -1396       C  
ATOM   6840  C   PHE B 526     -29.972   3.102 -18.420  1.00 65.64           C  
ANISOU 6840  C   PHE B 526     6580  11132   7228  -1229     16  -1556       C  
ATOM   6841  O   PHE B 526     -30.826   3.621 -19.146  1.00 66.27           O  
ANISOU 6841  O   PHE B 526     6591  11425   7165  -1292    -93  -1483       O  
ATOM   6842  CB  PHE B 526     -27.666   4.102 -18.664  1.00 59.29           C  
ANISOU 6842  CB  PHE B 526     5890  10308   6329  -1152     81  -1466       C  
ATOM   6843  CG  PHE B 526     -26.748   5.268 -18.378  1.00 58.13           C  
ANISOU 6843  CG  PHE B 526     5805  10120   6160  -1053     65  -1280       C  
ATOM   6844  CD1 PHE B 526     -27.225   6.576 -18.407  1.00 59.79           C  
ANISOU 6844  CD1 PHE B 526     6006  10416   6297  -1007    -47  -1049       C  
ATOM   6845  CD2 PHE B 526     -25.388   5.068 -18.173  1.00 58.19           C  
ANISOU 6845  CD2 PHE B 526     5870  10013   6227  -1017    161  -1342       C  
ATOM   6846  CE1 PHE B 526     -26.364   7.659 -18.188  1.00 59.17           C  
ANISOU 6846  CE1 PHE B 526     5981  10293   6208   -927    -56   -887       C  
ATOM   6847  CE2 PHE B 526     -24.529   6.150 -17.965  1.00 59.61           C  
ANISOU 6847  CE2 PHE B 526     6100  10166   6383   -941    145  -1179       C  
ATOM   6848  CZ  PHE B 526     -25.023   7.437 -17.970  1.00 57.32           C  
ANISOU 6848  CZ  PHE B 526     5806   9951   6022   -900     39   -956       C  
ATOM   6849  N   GLY B 527     -29.941   1.797 -18.116  1.00 63.25           N  
ANISOU 6849  N   GLY B 527     6275  10690   7066  -1268    116  -1757       N  
ATOM   6850  CA  GLY B 527     -30.896   0.797 -18.596  1.00 64.37           C  
ANISOU 6850  CA  GLY B 527     6339  10906   7212  -1396    120  -1939       C  
ATOM   6851  C   GLY B 527     -32.320   1.066 -18.148  1.00 68.17           C  
ANISOU 6851  C   GLY B 527     6757  11406   7738  -1378     28  -1822       C  
ATOM   6852  O   GLY B 527     -33.254   0.800 -18.905  1.00 68.85           O  
ANISOU 6852  O   GLY B 527     6755  11677   7729  -1498    -35  -1897       O  
ATOM   6853  N   THR B 528     -32.502   1.604 -16.914  1.00 64.04           N  
ANISOU 6853  N   THR B 528     6272  10702   7358  -1236     20  -1642       N  
ATOM   6854  CA  THR B 528     -33.818   2.002 -16.393  1.00 64.13           C  
ANISOU 6854  CA  THR B 528     6218  10720   7427  -1202    -56  -1516       C  
ATOM   6855  C   THR B 528     -34.337   3.083 -17.330  1.00 70.88           C  
ANISOU 6855  C   THR B 528     7006  11830   8095  -1230   -194  -1378       C  
ATOM   6856  O   THR B 528     -35.422   2.933 -17.870  1.00 72.84           O  
ANISOU 6856  O   THR B 528     7150  12231   8295  -1312   -271  -1397       O  
ATOM   6857  CB  THR B 528     -33.749   2.490 -14.925  1.00 67.84           C  
ANISOU 6857  CB  THR B 528     6750  10962   8063  -1048    -23  -1358       C  
ATOM   6858  OG1 THR B 528     -32.902   1.649 -14.160  1.00 64.78           O  
ANISOU 6858  OG1 THR B 528     6443  10358   7813  -1014     93  -1444       O  
ATOM   6859  CG2 THR B 528     -35.118   2.572 -14.264  1.00 66.04           C  
ANISOU 6859  CG2 THR B 528     6450  10703   7938  -1027    -56  -1288       C  
ATOM   6860  N   GLY B 529     -33.495   4.086 -17.598  1.00 67.43           N  
ANISOU 6860  N   GLY B 529     6622  11445   7555  -1173   -224  -1248       N  
ATOM   6861  CA  GLY B 529     -33.784   5.196 -18.497  1.00 68.47           C  
ANISOU 6861  CA  GLY B 529     6699  11804   7512  -1193   -354  -1083       C  
ATOM   6862  C   GLY B 529     -34.192   4.761 -19.887  1.00 74.79           C  
ANISOU 6862  C   GLY B 529     7417  12889   8110  -1366   -419  -1196       C  
ATOM   6863  O   GLY B 529     -35.155   5.301 -20.432  1.00 76.35           O  
ANISOU 6863  O   GLY B 529     7517  13273   8221  -1403   -550  -1076       O  
ATOM   6864  N   ILE B 530     -33.479   3.759 -20.454  1.00 71.06           N  
ANISOU 6864  N   ILE B 530     6976  12453   7569  -1477   -328  -1434       N  
ATOM   6865  CA  ILE B 530     -33.763   3.186 -21.773  1.00 72.12           C  
ANISOU 6865  CA  ILE B 530     7042  12861   7500  -1667   -363  -1600       C  
ATOM   6866  C   ILE B 530     -35.056   2.348 -21.693  1.00 74.92           C  
ANISOU 6866  C   ILE B 530     7299  13235   7933  -1747   -391  -1717       C  
ATOM   6867  O   ILE B 530     -35.908   2.498 -22.566  1.00 76.26           O  
ANISOU 6867  O   ILE B 530     7368  13662   7946  -1859   -511  -1698       O  
ATOM   6868  CB  ILE B 530     -32.565   2.375 -22.349  1.00 75.70           C  
ANISOU 6868  CB  ILE B 530     7556  13324   7883  -1757   -232  -1843       C  
ATOM   6869  CG1 ILE B 530     -31.289   3.261 -22.462  1.00 75.16           C  
ANISOU 6869  CG1 ILE B 530     7573  13252   7734  -1683   -207  -1717       C  
ATOM   6870  CG2 ILE B 530     -32.922   1.753 -23.722  1.00 78.62           C  
ANISOU 6870  CG2 ILE B 530     7852  13992   8030  -1974   -257  -2049       C  
ATOM   6871  CD1 ILE B 530     -29.946   2.510 -22.299  1.00 79.63           C  
ANISOU 6871  CD1 ILE B 530     8216  13659   8381  -1676    -39  -1913       C  
ATOM   6872  N   ALA B 531     -35.217   1.504 -20.645  1.00 68.71           N  
ANISOU 6872  N   ALA B 531     6536  12184   7386  -1693   -289  -1820       N  
ATOM   6873  CA  ALA B 531     -36.416   0.669 -20.469  1.00 68.54           C  
ANISOU 6873  CA  ALA B 531     6424  12147   7469  -1767   -298  -1933       C  
ATOM   6874  C   ALA B 531     -37.677   1.523 -20.286  1.00 71.49           C  
ANISOU 6874  C   ALA B 531     6699  12611   7852  -1720   -439  -1717       C  
ATOM   6875  O   ALA B 531     -38.682   1.264 -20.947  1.00 71.83           O  
ANISOU 6875  O   ALA B 531     6626  12844   7822  -1841   -525  -1772       O  
ATOM   6876  CB  ALA B 531     -36.246  -0.267 -19.281  1.00 67.82           C  
ANISOU 6876  CB  ALA B 531     6389  11736   7643  -1702   -158  -2034       C  
ATOM   6877  N   MET B 532     -37.601   2.564 -19.426  1.00 66.41           N  
ANISOU 6877  N   MET B 532     6094  11838   7302  -1548   -461  -1477       N  
ATOM   6878  CA  MET B 532     -38.714   3.474 -19.137  1.00 66.41           C  
ANISOU 6878  CA  MET B 532     5998  11885   7352  -1476   -577  -1263       C  
ATOM   6879  C   MET B 532     -39.118   4.294 -20.362  1.00 72.49           C  
ANISOU 6879  C   MET B 532     6673  12965   7905  -1545   -744  -1129       C  
ATOM   6880  O   MET B 532     -40.298   4.632 -20.496  1.00 72.88           O  
ANISOU 6880  O   MET B 532     6592  13123   7975  -1552   -859  -1019       O  
ATOM   6881  CB  MET B 532     -38.398   4.396 -17.952  1.00 66.46           C  
ANISOU 6881  CB  MET B 532     6074  11666   7512  -1284   -540  -1069       C  
ATOM   6882  CG  MET B 532     -38.233   3.660 -16.622  1.00 68.55           C  
ANISOU 6882  CG  MET B 532     6413  11644   7990  -1216   -396  -1158       C  
ATOM   6883  SD  MET B 532     -39.566   2.528 -16.195  1.00 74.20           S  
ANISOU 6883  SD  MET B 532     7026  12308   8857  -1295   -364  -1292       S  
ATOM   6884  CE  MET B 532     -38.764   0.918 -16.517  1.00 70.99           C  
ANISOU 6884  CE  MET B 532     6686  11833   8453  -1425   -241  -1588       C  
ATOM   6885  N   SER B 533     -38.154   4.572 -21.268  1.00 69.53           N  
ANISOU 6885  N   SER B 533     6355  12740   7324  -1604   -758  -1138       N  
ATOM   6886  CA  SER B 533     -38.388   5.298 -22.518  1.00 71.13           C  
ANISOU 6886  CA  SER B 533     6480  13260   7285  -1691   -914  -1006       C  
ATOM   6887  C   SER B 533     -39.232   4.473 -23.501  1.00 77.02           C  
ANISOU 6887  C   SER B 533     7110  14269   7884  -1891   -988  -1171       C  
ATOM   6888  O   SER B 533     -39.885   5.068 -24.354  1.00 79.06           O  
ANISOU 6888  O   SER B 533     7261  14795   7984  -1959  -1152  -1026       O  
ATOM   6889  CB  SER B 533     -37.066   5.707 -23.169  1.00 74.15           C  
ANISOU 6889  CB  SER B 533     6963  13725   7485  -1712   -884   -987       C  
ATOM   6890  OG  SER B 533     -36.496   4.670 -23.949  1.00 83.79           O  
ANISOU 6890  OG  SER B 533     8218  15057   8560  -1872   -802  -1262       O  
ATOM   6891  N   THR B 534     -39.252   3.121 -23.369  1.00 73.50           N  
ANISOU 6891  N   THR B 534     6678  13745   7504  -1988   -874  -1464       N  
ATOM   6892  CA  THR B 534     -40.032   2.245 -24.258  1.00 76.11           C  
ANISOU 6892  CA  THR B 534     6900  14306   7711  -2193   -927  -1664       C  
ATOM   6893  C   THR B 534     -41.546   2.320 -23.959  1.00 83.36           C  
ANISOU 6893  C   THR B 534     7667  15261   8744  -2188  -1041  -1568       C  
ATOM   6894  O   THR B 534     -42.326   1.623 -24.620  1.00 86.89           O  
ANISOU 6894  O   THR B 534     8007  15899   9108  -2358  -1099  -1721       O  
ATOM   6895  CB  THR B 534     -39.545   0.780 -24.233  1.00 80.81           C  
ANISOU 6895  CB  THR B 534     7554  14781   8368  -2300   -758  -2017       C  
ATOM   6896  OG1 THR B 534     -40.002   0.121 -23.049  1.00 80.30           O  
ANISOU 6896  OG1 THR B 534     7494  14420   8596  -2216   -663  -2074       O  
ATOM   6897  CG2 THR B 534     -38.037   0.644 -24.408  1.00 75.27           C  
ANISOU 6897  CG2 THR B 534     6989  14012   7598  -2290   -628  -2123       C  
ATOM   6898  N   TRP B 535     -41.965   3.176 -23.001  1.00 78.82           N  
ANISOU 6898  N   TRP B 535     7074  14515   8358  -2003  -1071  -1326       N  
ATOM   6899  CA  TRP B 535     -43.378   3.389 -22.641  1.00 80.03           C  
ANISOU 6899  CA  TRP B 535     7074  14687   8647  -1973  -1170  -1210       C  
ATOM   6900  C   TRP B 535     -44.144   3.983 -23.816  1.00 84.73           C  
ANISOU 6900  C   TRP B 535     7519  15639   9037  -2074  -1384  -1064       C  
ATOM   6901  O   TRP B 535     -45.310   3.666 -24.026  1.00 84.77           O  
ANISOU 6901  O   TRP B 535     7369  15772   9067  -2156  -1479  -1084       O  
ATOM   6902  CB  TRP B 535     -43.490   4.309 -21.407  1.00 77.24           C  
ANISOU 6902  CB  TRP B 535     6745  14075   8529  -1747  -1137   -987       C  
ATOM   6903  CG  TRP B 535     -44.893   4.729 -21.081  1.00 79.20           C  
ANISOU 6903  CG  TRP B 535     6824  14348   8920  -1698  -1239   -839       C  
ATOM   6904  CD1 TRP B 535     -45.530   5.857 -21.510  1.00 83.32           C  
ANISOU 6904  CD1 TRP B 535     7221  15024   9412  -1644  -1406   -578       C  
ATOM   6905  CD2 TRP B 535     -45.837   4.017 -20.265  1.00 79.04           C  
ANISOU 6905  CD2 TRP B 535     6728  14189   9113  -1696  -1175   -937       C  
ATOM   6906  NE1 TRP B 535     -46.813   5.893 -21.015  1.00 83.82           N  
ANISOU 6906  NE1 TRP B 535     7130  15055   9664  -1605  -1449   -517       N  
ATOM   6907  CE2 TRP B 535     -47.024   4.783 -20.234  1.00 84.42           C  
ANISOU 6907  CE2 TRP B 535     7236  14954   9885  -1638  -1305   -736       C  
ATOM   6908  CE3 TRP B 535     -45.790   2.812 -19.538  1.00 79.36           C  
ANISOU 6908  CE3 TRP B 535     6828  14034   9289  -1737  -1017  -1164       C  
ATOM   6909  CZ2 TRP B 535     -48.163   4.374 -19.523  1.00 83.77           C  
ANISOU 6909  CZ2 TRP B 535     7035  14782  10013  -1626  -1275   -772       C  
ATOM   6910  CZ3 TRP B 535     -46.913   2.420 -18.816  1.00 81.02           C  
ANISOU 6910  CZ3 TRP B 535     6931  14152   9702  -1728   -990  -1184       C  
ATOM   6911  CH2 TRP B 535     -48.086   3.186 -18.828  1.00 82.66           C  
ANISOU 6911  CH2 TRP B 535     6963  14461   9983  -1678  -1116   -999       C  
ATOM   6912  N   VAL B 536     -43.456   4.835 -24.575  1.00 81.76           N  
ANISOU 6912  N   VAL B 536     7184  15423   8456  -2072  -1460   -910       N  
ATOM   6913  CA  VAL B 536     -43.950   5.567 -25.720  1.00 83.82           C  
ANISOU 6913  CA  VAL B 536     7324  16030   8495  -2159  -1669   -721       C  
ATOM   6914  C   VAL B 536     -43.738   4.728 -27.023  1.00 91.11           C  
ANISOU 6914  C   VAL B 536     8238  17272   9107  -2415  -1698   -955       C  
ATOM   6915  O   VAL B 536     -44.243   5.108 -28.073  1.00 91.99           O  
ANISOU 6915  O   VAL B 536     8236  17721   8994  -2537  -1879   -840       O  
ATOM   6916  CB  VAL B 536     -43.229   6.950 -25.682  1.00 86.46           C  
ANISOU 6916  CB  VAL B 536     7723  16323   8805  -2009  -1711   -420       C  
ATOM   6917  CG1 VAL B 536     -42.293   7.214 -26.858  1.00 87.35           C  
ANISOU 6917  CG1 VAL B 536     7898  16699   8594  -2132  -1759   -395       C  
ATOM   6918  CG2 VAL B 536     -44.206   8.091 -25.447  1.00 86.70           C  
ANISOU 6918  CG2 VAL B 536     7610  16350   8982  -1877  -1863    -95       C  
ATOM   6919  N   TRP B 537     -43.070   3.557 -26.940  1.00 89.19           N  
ANISOU 6919  N   TRP B 537     8099  16926   8864  -2504  -1523  -1287       N  
ATOM   6920  CA  TRP B 537     -42.832   2.710 -28.119  1.00 91.90           C  
ANISOU 6920  CA  TRP B 537     8437  17546   8935  -2750  -1520  -1553       C  
ATOM   6921  C   TRP B 537     -44.083   1.868 -28.435  1.00100.31           C  
ANISOU 6921  C   TRP B 537     9348  18766  10002  -2914  -1597  -1717       C  
ATOM   6922  O   TRP B 537     -44.071   0.636 -28.325  1.00101.27           O  
ANISOU 6922  O   TRP B 537     9489  18804  10185  -3025  -1470  -2043       O  
ATOM   6923  CB  TRP B 537     -41.590   1.812 -27.935  1.00 89.35           C  
ANISOU 6923  CB  TRP B 537     8275  17037   8637  -2775  -1295  -1847       C  
ATOM   6924  CG  TRP B 537     -40.252   2.504 -27.882  1.00 88.89           C  
ANISOU 6924  CG  TRP B 537     8359  16897   8516  -2669  -1221  -1736       C  
ATOM   6925  CD1 TRP B 537     -40.008   3.833 -27.678  1.00 90.80           C  
ANISOU 6925  CD1 TRP B 537     8624  17119   8759  -2515  -1303  -1400       C  
ATOM   6926  CD2 TRP B 537     -38.970   1.864 -27.922  1.00 88.01           C  
ANISOU 6926  CD2 TRP B 537     8384  16677   8381  -2699  -1035  -1971       C  
ATOM   6927  NE1 TRP B 537     -38.652   4.062 -27.619  1.00 89.02           N  
ANISOU 6927  NE1 TRP B 537     8540  16794   8489  -2459  -1185  -1412       N  
ATOM   6928  CE2 TRP B 537     -37.992   2.870 -27.763  1.00 90.64           C  
ANISOU 6928  CE2 TRP B 537     8813  16946   8679  -2566  -1021  -1757       C  
ATOM   6929  CE3 TRP B 537     -38.552   0.531 -28.087  1.00 89.79           C  
ANISOU 6929  CE3 TRP B 537     8648  16843   8626  -2827   -875  -2346       C  
ATOM   6930  CZ2 TRP B 537     -36.620   2.587 -27.768  1.00 89.35           C  
ANISOU 6930  CZ2 TRP B 537     8778  16678   8492  -2558   -858  -1901       C  
ATOM   6931  CZ3 TRP B 537     -37.195   0.253 -28.097  1.00 90.56           C  
ANISOU 6931  CZ3 TRP B 537     8870  16827   8712  -2811   -710  -2488       C  
ATOM   6932  CH2 TRP B 537     -36.245   1.273 -27.948  1.00 89.96           C  
ANISOU 6932  CH2 TRP B 537     8883  16706   8591  -2679   -705  -2266       C  
ATOM   6933  N   THR B 538     -45.169   2.555 -28.818  1.00 98.48           N  
ANISOU 6933  N   THR B 538     8951  18751   9717  -2927  -1810  -1483       N  
ATOM   6934  CA  THR B 538     -46.461   1.962 -29.165  1.00100.11           C  
ANISOU 6934  CA  THR B 538     8980  19142   9916  -3077  -1924  -1580       C  
ATOM   6935  C   THR B 538     -46.924   2.486 -30.515  1.00107.53           C  
ANISOU 6935  C   THR B 538     9792  20546  10519  -3245  -2158  -1443       C  
ATOM   6936  O   THR B 538     -46.401   3.502 -30.987  1.00107.00           O  
ANISOU 6936  O   THR B 538     9762  20614  10278  -3201  -2242  -1200       O  
ATOM   6937  CB  THR B 538     -47.503   2.270 -28.082  1.00105.01           C  
ANISOU 6937  CB  THR B 538     9493  19544  10863  -2909  -1956  -1411       C  
ATOM   6938  OG1 THR B 538     -47.540   3.680 -27.840  1.00103.13           O  
ANISOU 6938  OG1 THR B 538     9233  19271  10681  -2716  -2059  -1031       O  
ATOM   6939  CG2 THR B 538     -47.252   1.506 -26.789  1.00100.69           C  
ANISOU 6939  CG2 THR B 538     9045  18588  10623  -2803  -1732  -1594       C  
ATOM   6940  N   LYS B 539     -47.922   1.804 -31.131  1.00107.10           N  
ANISOU 6940  N   LYS B 539     9581  20740  10373  -3445  -2268  -1588       N  
ATOM   6941  CA  LYS B 539     -48.512   2.192 -32.413  1.00110.30           C  
ANISOU 6941  CA  LYS B 539     9840  21616  10451  -3631  -2510  -1467       C  
ATOM   6942  C   LYS B 539     -49.165   3.570 -32.302  1.00114.41           C  
ANISOU 6942  C   LYS B 539    10232  22198  11040  -3469  -2721  -1005       C  
ATOM   6943  O   LYS B 539     -49.151   4.332 -33.266  1.00115.69           O  
ANISOU 6943  O   LYS B 539    10334  22695  10929  -3547  -2909   -780       O  
ATOM   6944  CB  LYS B 539     -49.537   1.147 -32.884  1.00115.46           C  
ANISOU 6944  CB  LYS B 539    10346  22478  11047  -3867  -2573  -1734       C  
ATOM   6945  N   ALA B 540     -49.681   3.899 -31.099  1.00109.68           N  
ANISOU 6945  N   ALA B 540     9595  21265  10815  -3242  -2679   -862       N  
ATOM   6946  CA  ALA B 540     -50.345   5.162 -30.769  1.00109.88           C  
ANISOU 6946  CA  ALA B 540     9489  21261  10998  -3054  -2840   -450       C  
ATOM   6947  C   ALA B 540     -49.426   6.382 -30.941  1.00113.20           C  
ANISOU 6947  C   ALA B 540    10013  21668  11331  -2920  -2871   -151       C  
ATOM   6948  O   ALA B 540     -49.913   7.449 -31.303  1.00113.88           O  
ANISOU 6948  O   ALA B 540     9971  21901  11398  -2857  -3070    203       O  
ATOM   6949  CB  ALA B 540     -50.874   5.111 -29.344  1.00108.28           C  
ANISOU 6949  CB  ALA B 540     9262  20664  11215  -2849  -2721   -442       C  
ATOM   6950  N   THR B 541     -48.115   6.230 -30.695  1.00108.48           N  
ANISOU 6950  N   THR B 541     9635  20888  10695  -2876  -2677   -284       N  
ATOM   6951  CA  THR B 541     -47.173   7.348 -30.810  1.00107.80           C  
ANISOU 6951  CA  THR B 541     9657  20763  10538  -2754  -2682    -25       C  
ATOM   6952  C   THR B 541     -46.697   7.544 -32.260  1.00113.10           C  
ANISOU 6952  C   THR B 541    10337  21854  10783  -2958  -2807     27       C  
ATOM   6953  O   THR B 541     -46.243   8.642 -32.599  1.00111.91           O  
ANISOU 6953  O   THR B 541    10211  21767  10542  -2887  -2889    330       O  
ATOM   6954  CB  THR B 541     -46.014   7.203 -29.829  1.00118.68           C  
ANISOU 6954  CB  THR B 541    11251  21761  12083  -2609  -2429   -165       C  
ATOM   6955  OG1 THR B 541     -45.252   6.039 -30.148  1.00121.69           O  
ANISOU 6955  OG1 THR B 541    11749  22180  12307  -2775  -2276   -543       O  
ATOM   6956  CG2 THR B 541     -46.486   7.176 -28.368  1.00115.40           C  
ANISOU 6956  CG2 THR B 541    10829  20947  12072  -2398  -2318   -159       C  
ATOM   6957  N   LEU B 542     -46.844   6.510 -33.123  1.00112.35           N  
ANISOU 6957  N   LEU B 542    10213  22051  10426  -3221  -2823   -263       N  
ATOM   6958  CA  LEU B 542     -46.526   6.616 -34.555  1.00115.51           C  
ANISOU 6958  CA  LEU B 542    10601  22902  10385  -3452  -2948   -240       C  
ATOM   6959  C   LEU B 542     -47.506   7.605 -35.190  1.00122.99           C  
ANISOU 6959  C   LEU B 542    11346  24145  11240  -3465  -3249    162       C  
ATOM   6960  O   LEU B 542     -47.129   8.362 -36.084  1.00123.94           O  
ANISOU 6960  O   LEU B 542    11466  24542  11082  -3536  -3379    400       O  
ATOM   6961  CB  LEU B 542     -46.581   5.249 -35.274  1.00117.38           C  
ANISOU 6961  CB  LEU B 542    10838  23375  10386  -3737  -2889   -675       C  
ATOM   6962  CG  LEU B 542     -45.653   4.133 -34.764  1.00120.18           C  
ANISOU 6962  CG  LEU B 542    11370  23458  10833  -3752  -2595  -1099       C  
ATOM   6963  CD1 LEU B 542     -46.081   2.788 -35.302  1.00122.32           C  
ANISOU 6963  CD1 LEU B 542    11589  23912  10973  -4011  -2557  -1512       C  
ATOM   6964  CD2 LEU B 542     -44.192   4.391 -35.132  1.00122.19           C  
ANISOU 6964  CD2 LEU B 542    11807  23724  10898  -3757  -2467  -1123       C  
ATOM   6965  N   LEU B 543     -48.754   7.625 -34.655  1.00120.82           N  
ANISOU 6965  N   LEU B 543    10896  23784  11228  -3381  -3352    253       N  
ATOM   6966  CA  LEU B 543     -49.862   8.512 -35.012  1.00123.65           C  
ANISOU 6966  CA  LEU B 543    11027  24345  11609  -3350  -3631    637       C  
ATOM   6967  C   LEU B 543     -49.595   9.946 -34.525  1.00128.55           C  
ANISOU 6967  C   LEU B 543    11660  24746  12436  -3087  -3672   1061       C  
ATOM   6968  O   LEU B 543     -49.960  10.900 -35.213  1.00130.63           O  
ANISOU 6968  O   LEU B 543    11795  25247  12591  -3091  -3902   1434       O  
ATOM   6969  CB  LEU B 543     -51.185   7.990 -34.384  1.00123.77           C  
ANISOU 6969  CB  LEU B 543    10862  24262  11905  -3320  -3673    550       C  
ATOM   6970  CG  LEU B 543     -52.106   7.027 -35.176  1.00131.09           C  
ANISOU 6970  CG  LEU B 543    11631  25555  12624  -3597  -3805    333       C  
ATOM   6971  CD1 LEU B 543     -52.644   7.658 -36.450  1.00135.11           C  
ANISOU 6971  CD1 LEU B 543    11967  26552  12815  -3751  -4116    632       C  
ATOM   6972  CD2 LEU B 543     -51.481   5.653 -35.404  1.00132.41           C  
ANISOU 6972  CD2 LEU B 543    11947  25760  12605  -3808  -3610   -163       C  
ATOM   6973  N   ILE B 544     -48.978  10.087 -33.329  1.00123.58           N  
ANISOU 6973  N   ILE B 544    11178  23664  12113  -2863  -3452   1004       N  
ATOM   6974  CA  ILE B 544     -48.634  11.367 -32.688  1.00122.96           C  
ANISOU 6974  CA  ILE B 544    11134  23311  12274  -2604  -3442   1341       C  
ATOM   6975  C   ILE B 544     -47.577  12.106 -33.527  1.00129.86           C  
ANISOU 6975  C   ILE B 544    12117  24361  12862  -2656  -3485   1537       C  
ATOM   6976  O   ILE B 544     -47.676  13.324 -33.697  1.00129.79           O  
ANISOU 6976  O   ILE B 544    12033  24373  12908  -2547  -3632   1938       O  
ATOM   6977  CB  ILE B 544     -48.170  11.149 -31.203  1.00122.23           C  
ANISOU 6977  CB  ILE B 544    11188  22719  12536  -2393  -3177   1164       C  
ATOM   6978  CG1 ILE B 544     -49.280  10.521 -30.307  1.00122.22           C  
ANISOU 6978  CG1 ILE B 544    11067  22535  12836  -2332  -3134   1013       C  
ATOM   6979  CG2 ILE B 544     -47.585  12.413 -30.556  1.00120.90           C  
ANISOU 6979  CG2 ILE B 544    11092  22262  12581  -2149  -3132   1454       C  
ATOM   6980  CD1 ILE B 544     -50.780  11.083 -30.458  1.00133.24           C  
ANISOU 6980  CD1 ILE B 544    12181  24056  14387  -2289  -3366   1287       C  
ATOM   6981  N   TRP B 545     -46.587  11.368 -34.055  1.00128.72           N  
ANISOU 6981  N   TRP B 545    12141  24341  12427  -2824  -3354   1258       N  
ATOM   6982  CA  TRP B 545     -45.540  11.956 -34.883  1.00130.92           C  
ANISOU 6982  CA  TRP B 545    12528  24806  12409  -2899  -3372   1404       C  
ATOM   6983  C   TRP B 545     -46.048  12.212 -36.304  1.00144.80           C  
ANISOU 6983  C   TRP B 545    14143  27084  13789  -3122  -3634   1605       C  
ATOM   6984  O   TRP B 545     -45.545  13.122 -36.967  1.00145.68           O  
ANISOU 6984  O   TRP B 545    14277  27361  13713  -3142  -3729   1900       O  
ATOM   6985  CB  TRP B 545     -44.270  11.097 -34.868  1.00127.35           C  
ANISOU 6985  CB  TRP B 545    12295  24286  11808  -2989  -3124   1028       C  
ATOM   6986  CG  TRP B 545     -43.509  11.247 -33.582  1.00123.89           C  
ANISOU 6986  CG  TRP B 545    12010  23364  11699  -2753  -2899    960       C  
ATOM   6987  CD1 TRP B 545     -43.487  10.372 -32.537  1.00124.11           C  
ANISOU 6987  CD1 TRP B 545    12109  23075  11972  -2676  -2704    648       C  
ATOM   6988  CD2 TRP B 545     -42.775  12.402 -33.154  1.00121.94           C  
ANISOU 6988  CD2 TRP B 545    11847  22892  11592  -2561  -2864   1239       C  
ATOM   6989  NE1 TRP B 545     -42.743  10.888 -31.503  1.00120.35           N  
ANISOU 6989  NE1 TRP B 545    11761  22214  11753  -2456  -2553    709       N  
ATOM   6990  CE2 TRP B 545     -42.296  12.135 -31.853  1.00122.17           C  
ANISOU 6990  CE2 TRP B 545    12002  22490  11930  -2383  -2644   1058       C  
ATOM   6991  CE3 TRP B 545     -42.456  13.633 -33.753  1.00124.39           C  
ANISOU 6991  CE3 TRP B 545    12138  23328  11796  -2532  -2997   1627       C  
ATOM   6992  CZ2 TRP B 545     -41.507  13.047 -31.147  1.00119.37           C  
ANISOU 6992  CZ2 TRP B 545    11752  21836  11767  -2184  -2554   1232       C  
ATOM   6993  CZ3 TRP B 545     -41.684  14.539 -33.048  1.00123.59           C  
ANISOU 6993  CZ3 TRP B 545    12140  22909  11908  -2330  -2901   1800       C  
ATOM   6994  CH2 TRP B 545     -41.217  14.245 -31.762  1.00120.85           C  
ANISOU 6994  CH2 TRP B 545    11916  22144  11856  -2161  -2683   1594       C  
ATOM   6995  N   ARG B 546     -47.074  11.455 -36.748  1.00147.75           N  
ANISOU 6995  N   ARG B 546    14364  27715  14058  -3289  -3758   1463       N  
ATOM   6996  CA  ARG B 546     -47.716  11.660 -38.049  1.00153.65           C  
ANISOU 6996  CA  ARG B 546    14950  28977  14455  -3509  -4032   1657       C  
ATOM   6997  C   ARG B 546     -48.572  12.927 -37.984  1.00163.03           C  
ANISOU 6997  C   ARG B 546    15943  30156  15844  -3344  -4276   2171       C  
ATOM   6998  O   ARG B 546     -48.566  13.714 -38.931  1.00165.80           O  
ANISOU 6998  O   ARG B 546    16219  30832  15945  -3434  -4486   2512       O  
ATOM   6999  CB  ARG B 546     -48.551  10.438 -38.465  1.00156.19           C  
ANISOU 6999  CB  ARG B 546    15164  29555  14627  -3740  -4080   1320       C  
ATOM   7000  CG  ARG B 546     -47.722   9.360 -39.153  1.00169.09           C  
ANISOU 7000  CG  ARG B 546    16944  31410  15892  -4003  -3931    895       C  
ATOM   7001  CD  ARG B 546     -48.532   8.118 -39.473  1.00183.19           C  
ANISOU 7001  CD  ARG B 546    18629  33398  17576  -4224  -3953    528       C  
ATOM   7002  NE  ARG B 546     -47.666   6.958 -39.701  1.00190.49           N  
ANISOU 7002  NE  ARG B 546    19995  33710  18670  -4112  -3698    -27       N  
ATOM   7003  CZ  ARG B 546     -48.093   5.756 -40.074  1.00202.41           C  
ANISOU 7003  CZ  ARG B 546    21974  34198  20733  -3783  -3650   -478       C  
ATOM   7004  NH1 ARG B 546     -49.386   5.538 -40.282  1.00192.31           N  
ANISOU 7004  NH1 ARG B 546    20399  33316  19354  -3971  -3848   -442       N  
ATOM   7005  NH2 ARG B 546     -47.231   4.765 -40.251  1.00191.15           N  
ANISOU 7005  NH2 ARG B 546    20443  33340  18846  -4189  -3445   -824       N  
ATOM   7006  N   ARG B 547     -49.262  13.147 -36.839  1.00160.68           N  
ANISOU 7006  N   ARG B 547    15566  29477  16008  -3100  -4238   2232       N  
ATOM   7007  CA  ARG B 547     -50.087  14.330 -36.579  1.00162.80           C  
ANISOU 7007  CA  ARG B 547    15645  29650  16562  -2903  -4429   2687       C  
ATOM   7008  C   ARG B 547     -49.210  15.578 -36.413  1.00168.89           C  
ANISOU 7008  C   ARG B 547    16521  30222  17430  -2725  -4396   3017       C  
ATOM   7009  O   ARG B 547     -49.652  16.680 -36.742  1.00170.28           O  
ANISOU 7009  O   ARG B 547    16550  30468  17682  -2643  -4603   3461       O  
ATOM   7010  CB  ARG B 547     -50.964  14.125 -35.334  1.00160.53           C  
ANISOU 7010  CB  ARG B 547    15259  28997  16739  -2705  -4349   2590       C  
ATOM   7011  N   THR B 548     -47.967  15.397 -35.908  1.00164.83           N  
ANISOU 7011  N   THR B 548    16251  29453  16922  -2669  -4139   2802       N  
ATOM   7012  CA  THR B 548     -46.981  16.465 -35.711  1.00164.06           C  
ANISOU 7012  CA  THR B 548    16281  29150  16905  -2519  -4070   3050       C  
ATOM   7013  C   THR B 548     -46.384  16.887 -37.059  1.00173.54           C  
ANISOU 7013  C   THR B 548    17513  30758  17667  -2716  -4203   3259       C  
ATOM   7014  O   THR B 548     -46.113  18.073 -37.265  1.00174.46           O  
ANISOU 7014  O   THR B 548    17615  30838  17832  -2620  -4292   3654       O  
ATOM   7015  CB  THR B 548     -45.892  16.013 -34.735  1.00164.88           C  
ANISOU 7015  CB  THR B 548    16621  28875  17150  -2415  -3757   2723       C  
ATOM   7016  N   TRP B 549     -46.190  15.912 -37.973  1.00173.12           N  
ANISOU 7016  N   TRP B 549    17497  31090  17189  -2999  -4210   2990       N  
ATOM   7017  CA  TRP B 549     -45.657  16.116 -39.322  1.00177.03           C  
ANISOU 7017  CA  TRP B 549    18022  32037  17206  -3235  -4325   3126       C  
ATOM   7018  C   TRP B 549     -46.673  16.859 -40.197  1.00185.96           C  
ANISOU 7018  C   TRP B 549    18918  33522  18218  -3306  -4667   3572       C  
ATOM   7019  O   TRP B 549     -46.272  17.648 -41.054  1.00186.29           O  
ANISOU 7019  O   TRP B 549    19108  33520  18155  -3254  -4757   3762       O  
ATOM   7020  CB  TRP B 549     -45.287  14.763 -39.952  1.00176.83           C  
ANISOU 7020  CB  TRP B 549    18089  32303  16796  -3517  -4215   2653       C  
ATOM   7021  CG  TRP B 549     -44.639  14.855 -41.304  1.00180.69           C  
ANISOU 7021  CG  TRP B 549    18628  33261  16765  -3781  -4289   2723       C  
ATOM   7022  CD1 TRP B 549     -45.249  14.721 -42.517  1.00185.34           C  
ANISOU 7022  CD1 TRP B 549    19326  33862  17234  -3796  -4470   2644       C  
ATOM   7023  CD2 TRP B 549     -43.247  15.073 -41.576  1.00179.50           C  
ANISOU 7023  CD2 TRP B 549    18674  33104  16423  -3822  -4121   2685       C  
ATOM   7024  NE1 TRP B 549     -44.327  14.851 -43.529  1.00184.80           N  
ANISOU 7024  NE1 TRP B 549    19530  33761  16925  -3822  -4417   2557       N  
ATOM   7025  CE2 TRP B 549     -43.089  15.068 -42.980  1.00184.92           C  
ANISOU 7025  CE2 TRP B 549    19560  33855  16848  -3885  -4209   2609       C  
ATOM   7026  CE3 TRP B 549     -42.115  15.279 -40.768  1.00177.13           C  
ANISOU 7026  CE3 TRP B 549    18563  32401  16337  -3646  -3869   2589       C  
ATOM   7027  CZ2 TRP B 549     -41.845  15.260 -43.594  1.00184.09           C  
ANISOU 7027  CZ2 TRP B 549    19663  33782  16501  -3946  -4080   2566       C  
ATOM   7028  CZ3 TRP B 549     -40.884  15.469 -41.378  1.00179.08           C  
ANISOU 7028  CZ3 TRP B 549    18959  32787  16295  -3759  -3760   2580       C  
ATOM   7029  CH2 TRP B 549     -40.757  15.458 -42.773  1.00183.52           C  
ANISOU 7029  CH2 TRP B 549    19494  33888  16348  -4048  -3887   2661       C  
ATOM   7030  N   CYS B 550     -47.983  16.617 -39.965  1.00185.38           N  
ANISOU 7030  N   CYS B 550    18638  33466  18334  -3272  -4814   3593       N  
ATOM   7031  CA  CYS B 550     -49.093  17.233 -40.699  1.00186.19           C  
ANISOU 7031  CA  CYS B 550    18819  33231  18693  -3025  -5059   3674       C  
ATOM   7032  C   CYS B 550     -49.527  18.573 -40.050  1.00188.41           C  
ANISOU 7032  C   CYS B 550    19154  32872  19561  -2582  -5097   3919       C  
ATOM   7033  O   CYS B 550     -50.647  19.038 -40.283  1.00188.89           O  
ANISOU 7033  O   CYS B 550    19082  32865  19820  -2455  -5308   4080       O  
ATOM   7034  CB  CYS B 550     -50.265  16.259 -40.808  1.00186.69           C  
ANISOU 7034  CB  CYS B 550    18834  33247  18852  -3043  -5134   3334       C  
ATOM   7035  N   ARG B 551     -48.625  19.200 -39.265  1.00186.35           N  
ANISOU 7035  N   ARG B 551    18717  32833  19256  -2663  -4999   4327       N  
ATOM   7036  CA  ARG B 551     -48.859  20.480 -38.593  1.00186.34           C  
ANISOU 7036  CA  ARG B 551    18592  32545  19663  -2409  -5052   4752       C  
ATOM   7037  C   ARG B 551     -47.926  21.574 -39.164  1.00188.09           C  
ANISOU 7037  C   ARG B 551    19235  32236  19994  -2136  -4986   4719       C  
ATOM   7038  O   ARG B 551     -47.449  22.440 -38.422  1.00187.57           O  
ANISOU 7038  O   ARG B 551    19029  32135  20102  -2077  -4941   5114       O  
ATOM   7039  CB  ARG B 551     -48.678  20.325 -37.074  1.00184.06           C  
ANISOU 7039  CB  ARG B 551    18268  31946  19720  -2270  -4822   4647       C  
ATOM   7040  N   LEU B 552     -47.689  21.534 -40.495  1.00187.14           N  
ANISOU 7040  N   LEU B 552    19246  32361  19499  -2273  -5103   4708       N  
ATOM   7041  CA  LEU B 552     -46.842  22.483 -41.223  1.00219.11           C  
ANISOU 7041  CA  LEU B 552    24763  34124  24366  -1166  -4689   3370       C  
ATOM   7042  C   LEU B 552     -47.356  22.696 -42.644  1.00249.59           C  
ANISOU 7042  C   LEU B 552    29898  36029  28905   -149  -4498   1959       C  
ATOM   7043  O   LEU B 552     -48.532  22.993 -42.841  1.00224.37           O  
ANISOU 7043  O   LEU B 552    25519  34676  25055   -941  -5055   3302       O  
ATOM   7044  CB  LEU B 552     -45.390  21.992 -41.260  1.00218.34           C  
ANISOU 7044  CB  LEU B 552    24788  34189  23984  -1364  -4494   3316       C  
TER    7045      LEU B 552                                                      
HETATM 7046  F1  1KS A 601     -17.152  20.689  19.948  1.00 72.43           F  
HETATM 7047  C1  1KS A 601     -18.197  21.356  20.445  1.00 71.13           C  
HETATM 7048  O1  1KS A 601     -21.546  24.022  23.192  1.00 67.06           O  
HETATM 7049  N1  1KS A 601     -22.920  23.481  21.368  1.00 62.79           N  
HETATM 7050  C10 1KS A 601     -24.110  24.128  21.979  1.00 59.50           C  
HETATM 7051  C11 1KS A 601     -24.884  23.123  22.810  1.00 57.76           C  
HETATM 7052  C12 1KS A 601     -25.989  23.826  23.570  1.00 57.61           C  
HETATM 7053  C13 1KS A 601     -26.092  25.643  21.902  1.00 58.64           C  
HETATM 7054  C14 1KS A 601     -24.985  24.988  21.083  1.00 57.34           C  
HETATM 7055  C15 1KS A 601     -28.093  24.167  22.233  1.00 60.57           C  
HETATM 7056  C16 1KS A 601     -29.191  23.924  23.115  1.00 59.39           C  
HETATM 7057  C17 1KS A 601     -30.474  23.540  22.529  1.00 60.83           C  
HETATM 7058  C18 1KS A 601     -31.559  23.270  23.397  1.00 62.59           C  
HETATM 7059  C19 1KS A 601     -31.431  23.411  24.773  1.00 60.97           C  
HETATM 7060  C2  1KS A 601     -18.437  22.788  20.052  1.00 69.93           C  
HETATM 7061  F2  1KS A 601     -18.823  25.330  19.334  1.00 71.61           F  
HETATM 7062  N2  1KS A 601     -26.828  24.719  22.778  1.00 59.02           N  
HETATM 7063  C20 1KS A 601     -30.208  23.845  25.327  1.00 58.85           C  
HETATM 7064  C21 1KS A 601     -29.118  24.092  24.493  1.00 57.52           C  
HETATM 7065  C22 1KS A 601     -30.505  23.422  21.130  1.00 60.51           C  
HETATM 7066  C23 1KS A 601     -31.860  23.062  20.461  1.00 60.85           C  
HETATM 7067  C24 1KS A 601     -32.978  23.898  20.402  1.00 61.46           C  
HETATM 7068  C25 1KS A 601     -33.958  23.144  19.728  1.00 62.31           C  
HETATM 7069  C26 1KS A 601     -31.409  20.738  19.659  1.00 57.87           C  
HETATM 7070  C3  1KS A 601     -19.516  23.488  20.569  1.00 67.42           C  
HETATM 7071  F3  1KS A 601     -19.729  25.684  21.259  1.00 68.03           F  
HETATM 7072  N3  1KS A 601     -29.471  23.679  20.354  1.00 60.03           N  
HETATM 7073  C4  1KS A 601     -19.764  24.919  20.179  1.00 67.02           C  
HETATM 7074  F4  1KS A 601     -20.932  25.139  19.597  1.00 63.99           F  
HETATM 7075  N4  1KS A 601     -28.278  24.062  20.906  1.00 61.12           N  
HETATM 7076  C5  1KS A 601     -20.436  22.780  21.549  1.00 66.10           C  
HETATM 7077  N5  1KS A 601     -33.510  21.898  19.358  1.00 60.75           N  
HETATM 7078  C6  1KS A 601     -20.217  21.473  21.901  1.00 67.24           C  
HETATM 7079  N6  1KS A 601     -32.240  21.879  19.793  1.00 58.39           N  
HETATM 7080  C7  1KS A 601     -19.051  20.719  21.320  1.00 69.89           C  
HETATM 7081  C8  1KS A 601     -21.659  23.464  22.111  1.00 65.48           C  
HETATM 7082  C9  1KS A 601     -23.046  22.801  20.068  1.00 62.19           C  
HETATM 7083  C8  OLC A 602     -50.808  29.345  23.039  1.00 86.96           C  
HETATM 7084  C24 OLC A 602     -62.497  30.281  16.766  1.00105.21           C  
HETATM 7085  C7  OLC A 602     -51.695  29.455  21.805  1.00 86.91           C  
HETATM 7086  C6  OLC A 602     -53.151  29.150  22.135  1.00 87.99           C  
HETATM 7087  C5  OLC A 602     -53.900  28.661  20.899  1.00 90.02           C  
HETATM 7088  C4  OLC A 602     -54.929  29.676  20.409  1.00 92.48           C  
HETATM 7089  C3  OLC A 602     -55.742  29.128  19.238  1.00 95.45           C  
HETATM 7090  C2  OLC A 602     -57.163  28.746  19.658  1.00 98.19           C  
HETATM 7091  C21 OLC A 602     -60.094  29.867  17.314  1.00103.88           C  
HETATM 7092  C1  OLC A 602     -58.198  29.640  19.003  1.00100.89           C  
HETATM 7093  C22 OLC A 602     -61.537  29.539  17.694  1.00105.43           C  
HETATM 7094  O19 OLC A 602     -58.234  30.833  19.277  1.00101.32           O  
HETATM 7095  O25 OLC A 602     -63.833  29.781  16.922  1.00105.10           O  
HETATM 7096  O23 OLC A 602     -61.759  28.126  17.583  1.00106.63           O  
HETATM 7097  O20 OLC A 602     -59.172  29.069  18.070  1.00102.67           O  
HETATM 7098  C8  OLC A 603     -34.006  26.683   2.691  1.00 82.33           C  
HETATM 7099  C24 OLC A 603     -21.991  27.041   5.097  1.00 99.53           C  
HETATM 7100  C7  OLC A 603     -33.238  27.736   3.480  1.00 83.20           C  
HETATM 7101  C6  OLC A 603     -31.734  27.575   3.274  1.00 84.24           C  
HETATM 7102  C5  OLC A 603     -30.959  28.030   4.503  1.00 85.16           C  
HETATM 7103  C4  OLC A 603     -29.886  27.010   4.858  1.00 87.17           C  
HETATM 7104  C3  OLC A 603     -28.492  27.603   4.716  1.00 89.43           C  
HETATM 7105  C2  OLC A 603     -27.719  26.896   3.605  1.00 92.89           C  
HETATM 7106  C21 OLC A 603     -24.273  26.828   4.098  1.00 98.24           C  
HETATM 7107  C1  OLC A 603     -26.662  25.967   4.162  1.00 95.93           C  
HETATM 7108  C22 OLC A 603     -23.016  26.060   4.521  1.00 98.41           C  
HETATM 7109  O19 OLC A 603     -26.949  25.186   5.058  1.00 95.74           O  
HETATM 7110  O25 OLC A 603     -21.032  26.385   5.941  1.00 99.18           O  
HETATM 7111  O23 OLC A 603     -23.347  25.068   5.499  1.00 97.31           O  
HETATM 7112  O20 OLC A 603     -25.303  25.958   3.610  1.00 98.11           O  
HETATM 7113  C24 OLC A 604     -24.486  37.694  14.747  1.00 89.41           C  
HETATM 7114  C7  OLC A 604     -34.610  35.305   9.045  1.00 91.87           C  
HETATM 7115  C6  OLC A 604     -33.960  34.759  10.312  1.00 92.47           C  
HETATM 7116  C5  OLC A 604     -32.843  35.670  10.814  1.00 93.00           C  
HETATM 7117  C4  OLC A 604     -32.357  35.244  12.198  1.00 93.33           C  
HETATM 7118  C3  OLC A 604     -31.344  36.228  12.780  1.00 93.58           C  
HETATM 7119  C2  OLC A 604     -29.923  35.666  12.759  1.00 93.86           C  
HETATM 7120  C21 OLC A 604     -26.629  37.459  13.415  1.00 90.44           C  
HETATM 7121  C1  OLC A 604     -28.906  36.750  12.471  1.00 93.46           C  
HETATM 7122  C22 OLC A 604     -25.960  37.305  14.783  1.00 90.59           C  
HETATM 7123  O19 OLC A 604     -28.823  37.234  11.348  1.00 94.59           O  
HETATM 7124  O25 OLC A 604     -23.930  37.659  16.072  1.00 87.44           O  
HETATM 7125  O23 OLC A 604     -26.618  38.127  15.754  1.00 92.11           O  
HETATM 7126  O20 OLC A 604     -28.038  37.221  13.550  1.00 91.97           O  
HETATM 7127  C1  OLA A 605     -29.570   4.499  33.411  1.00 94.38           C  
HETATM 7128  O1  OLA A 605     -28.559   5.156  33.750  1.00 93.79           O  
HETATM 7129  O2  OLA A 605     -29.625   3.282  33.700  1.00 96.01           O  
HETATM 7130  C2  OLA A 605     -30.716   5.166  32.685  1.00 92.76           C  
HETATM 7131  C3  OLA A 605     -30.758   4.732  31.224  1.00 91.32           C  
HETATM 7132  C4  OLA A 605     -31.058   5.921  30.320  1.00 89.99           C  
HETATM 7133  C5  OLA A 605     -32.239   5.630  29.403  1.00 88.65           C  
HETATM 7134  C6  OLA A 605     -32.069   6.317  28.051  1.00 85.99           C  
HETATM 7135  C7  OLA A 605     -32.710   5.502  26.935  1.00 83.30           C  
HETATM 7136  C8  OLA A 605     -33.935   6.227  26.402  1.00 81.94           C  
HETATM 7137  C9  OLA A 605     -34.823   5.265  25.643  1.00 81.36           C  
HETATM 7138  C10 OLA A 605     -36.093   5.534  25.309  1.00 80.79           C  
HETATM 7139  C11 OLA A 605     -36.807   6.823  25.659  1.00 79.71           C  
HETATM 7140  C12 OLA A 605     -38.099   6.501  26.408  1.00 80.70           C  
HETATM 7141  C13 OLA A 605     -37.951   6.576  27.931  1.00 81.19           C  
HETATM 7142  C14 OLA A 605     -38.032   8.011  28.452  1.00 81.44           C  
HETATM 7143  C15 OLA A 605     -39.359   8.297  29.145  1.00 81.54           C  
HETATM 7144  C16 OLA A 605     -39.355   9.710  29.715  1.00 80.96           C  
HETATM 7145  C17 OLA A 605     -40.676  10.040  30.393  1.00 79.90           C  
HETATM 7146  C18 OLA A 605     -40.524  11.276  31.270  1.00 80.29           C  
HETATM 7147  C1  OLA A 606     -49.006   5.589  10.079  1.00104.84           C  
HETATM 7148  O1  OLA A 606     -49.093   4.592   9.322  1.00105.75           O  
HETATM 7149  O2  OLA A 606     -49.818   6.531   9.927  1.00105.05           O  
HETATM 7150  C2  OLA A 606     -47.951   5.659  11.164  1.00102.43           C  
HETATM 7151  C3  OLA A 606     -46.560   5.768  10.546  1.00100.38           C  
HETATM 7152  C4  OLA A 606     -45.522   6.156  11.590  1.00 98.41           C  
HETATM 7153  C5  OLA A 606     -44.172   5.502  11.309  1.00 96.55           C  
HETATM 7154  C6  OLA A 606     -43.059   6.256  12.027  1.00 94.92           C  
HETATM 7155  C7  OLA A 606     -41.704   5.594  11.814  1.00 93.59           C  
HETATM 7156  C8  OLA A 606     -41.044   5.307  13.159  1.00 92.93           C  
HETATM 7157  C9  OLA A 606     -39.563   5.031  12.974  1.00 91.96           C  
HETATM 7158  C10 OLA A 606     -38.574   5.708  13.576  1.00 90.36           C  
HETATM 7159  C11 OLA A 606     -38.783   6.868  14.529  1.00 89.40           C  
HETATM 7160  C12 OLA A 606     -38.765   6.384  15.977  1.00 88.16           C  
HETATM 7161  C13 OLA A 606     -39.543   7.332  16.881  1.00 86.93           C  
HETATM 7162  C1  PEG A 607     -18.478  32.554  30.655  1.00 90.05           C  
HETATM 7163  O1  PEG A 607     -17.664  32.414  29.497  1.00 90.15           O  
HETATM 7164  C2  PEG A 607     -18.096  31.584  31.730  1.00 90.22           C  
HETATM 7165  O2  PEG A 607     -18.211  30.251  31.254  1.00 90.37           O  
HETATM 7166  C3  PEG A 607     -17.415  29.328  31.984  1.00 89.61           C  
HETATM 7167  C4  PEG A 607     -18.211  28.095  32.274  1.00 88.66           C  
HETATM 7168  O4  PEG A 607     -17.550  27.237  33.185  1.00 88.08           O  
HETATM 7169  C1  PGE A 608     -14.301  19.438   9.470  1.00 70.12           C  
HETATM 7170  O1  PGE A 608     -15.173  20.369   8.837  1.00 71.89           O  
HETATM 7171  C2  PGE A 608     -15.056  18.478  10.349  1.00 67.27           C  
HETATM 7172  O2  PGE A 608     -15.976  17.720   9.574  1.00 64.46           O  
HETATM 7173  C3  PGE A 608     -15.986  16.349   9.928  1.00 60.79           C  
HETATM 7174  C4  PGE A 608     -16.884  15.584   9.020  1.00 58.16           C  
HETATM 7175  O4  PGE A 608     -14.058  12.278   7.172  1.00 65.19           O  
HETATM 7176  C6  PGE A 608     -14.731  13.510   6.914  1.00 62.55           C  
HETATM 7177  C5  PGE A 608     -15.869  13.756   7.860  1.00 59.00           C  
HETATM 7178  O3  PGE A 608     -16.187  15.142   7.867  1.00 58.14           O  
HETATM 7179  O1  PG4 A 609     -39.032  27.330  34.956  1.00103.00           O  
HETATM 7180  C1  PG4 A 609     -38.212  28.490  34.935  1.00102.65           C  
HETATM 7181  C2  PG4 A 609     -36.886  28.231  34.277  1.00102.49           C  
HETATM 7182  O2  PG4 A 609     -36.092  29.412  34.291  1.00102.75           O  
HETATM 7183  C3  PG4 A 609     -35.736  29.871  32.993  1.00102.40           C  
HETATM 7184  C4  PG4 A 609     -36.277  31.242  32.716  1.00101.73           C  
HETATM 7185  O3  PG4 A 609     -36.049  31.576  31.353  1.00101.00           O  
HETATM 7186  C5  PG4 A 609     -36.458  32.895  31.009  1.00 99.11           C  
HETATM 7187  C6  PG4 A 609     -35.559  33.468  29.955  1.00 97.12           C  
HETATM 7188  O4  PG4 A 609     -34.209  33.439  30.401  1.00 95.83           O  
HETATM 7189  C7  PG4 A 609     -33.469  34.607  30.077  1.00 93.76           C  
HETATM 7190  C8  PG4 A 609     -32.020  34.414  30.430  1.00 92.69           C  
HETATM 7191  O5  PG4 A 609     -31.416  33.350  29.696  1.00 90.74           O  
HETATM 7192  F1  1KS B 601      -9.852   9.840  -1.637  1.00 67.99           F  
HETATM 7193  C1  1KS B 601     -10.337   9.019  -2.560  1.00 60.26           C  
HETATM 7194  O1  1KS B 601     -11.168   5.819  -6.343  1.00 55.05           O  
HETATM 7195  N1  1KS B 601     -13.412   6.285  -5.809  1.00 55.63           N  
HETATM 7196  C10 1KS B 601     -13.933   5.467  -6.928  1.00 56.01           C  
HETATM 7197  C11 1KS B 601     -14.188   6.369  -8.117  1.00 55.80           C  
HETATM 7198  C12 1KS B 601     -14.623   5.562  -9.321  1.00 55.53           C  
HETATM 7199  C13 1KS B 601     -15.502   3.780  -7.852  1.00 55.40           C  
HETATM 7200  C14 1KS B 601     -15.098   4.547  -6.604  1.00 54.83           C  
HETATM 7201  C15 1KS B 601     -17.053   4.979  -9.407  1.00 56.11           C  
HETATM 7202  C16 1KS B 601     -17.487   5.022 -10.767  1.00 55.85           C  
HETATM 7203  C17 1KS B 601     -18.894   5.293 -11.027  1.00 56.34           C  
HETATM 7204  C18 1KS B 601     -19.330   5.370 -12.370  1.00 56.45           C  
HETATM 7205  C19 1KS B 601     -18.446   5.213 -13.429  1.00 57.04           C  
HETATM 7206  C2  1KS B 601     -10.517   7.569  -2.241  1.00 57.46           C  
HETATM 7207  F2  1KS B 601     -10.391   4.524  -3.600  1.00 60.20           F  
HETATM 7208  N2  1KS B 601     -15.670   4.584  -9.077  1.00 56.26           N  
HETATM 7209  C20 1KS B 601     -17.081   4.956 -13.176  1.00 56.31           C  
HETATM 7210  C21 1KS B 601     -16.645   4.812 -11.854  1.00 55.97           C  
HETATM 7211  C22 1KS B 601     -19.706   5.434  -9.880  1.00 57.37           C  
HETATM 7212  C23 1KS B 601     -21.242   5.590 -10.043  1.00 56.78           C  
HETATM 7213  C24 1KS B 601     -22.106   4.621 -10.554  1.00 56.76           C  
HETATM 7214  C25 1KS B 601     -23.388   5.210 -10.490  1.00 61.08           C  
HETATM 7215  C26 1KS B 601     -21.566   7.886  -9.120  1.00 56.93           C  
HETATM 7216  C3  1KS B 601     -11.044   6.709  -3.178  1.00 55.14           C  
HETATM 7217  F3  1KS B 601     -12.462   4.853  -3.162  1.00 58.07           F  
HETATM 7218  N3  1KS B 601     -19.261   5.317  -8.647  1.00 55.52           N  
HETATM 7219  C4  1KS B 601     -11.231   5.253  -2.869  1.00 58.44           C  
HETATM 7220  F4  1KS B 601     -10.987   4.997  -1.592  1.00 61.60           F  
HETATM 7221  N4  1KS B 601     -17.945   5.058  -8.422  1.00 55.22           N  
HETATM 7222  C5  1KS B 601     -11.387   7.265  -4.539  1.00 53.60           C  
HETATM 7223  N5  1KS B 601     -23.372   6.482  -9.949  1.00 61.54           N  
HETATM 7224  C6  1KS B 601     -11.209   8.595  -4.829  1.00 55.36           C  
HETATM 7225  N6  1KS B 601     -22.064   6.677  -9.673  1.00 58.21           N  
HETATM 7226  C7  1KS B 601     -10.653   9.526  -3.792  1.00 57.12           C  
HETATM 7227  C8  1KS B 601     -11.963   6.401  -5.627  1.00 54.53           C  
HETATM 7228  C9  1KS B 601     -14.355   6.997  -4.931  1.00 53.44           C  
HETATM 7229  C24 OLC B 602     -15.572  23.530 -20.845  1.00 97.22           C  
HETATM 7230  C6  OLC B 602     -25.220  22.251 -17.676  1.00 89.97           C  
HETATM 7231  C5  OLC B 602     -23.805  21.760 -17.955  1.00 91.13           C  
HETATM 7232  C4  OLC B 602     -22.778  22.844 -17.631  1.00 92.56           C  
HETATM 7233  C3  OLC B 602     -21.624  22.311 -16.784  1.00 92.61           C  
HETATM 7234  C2  OLC B 602     -20.363  23.162 -16.941  1.00 93.16           C  
HETATM 7235  C21 OLC B 602     -17.544  23.022 -19.338  1.00 96.46           C  
HETATM 7236  C1  OLC B 602     -19.203  22.389 -17.543  1.00 94.84           C  
HETATM 7237  C22 OLC B 602     -16.222  23.776 -19.487  1.00 98.19           C  
HETATM 7238  O19 OLC B 602     -19.247  21.175 -17.664  1.00 96.50           O  
HETATM 7239  O25 OLC B 602     -14.230  24.035 -20.822  1.00 96.39           O  
HETATM 7240  O23 OLC B 602     -16.408  25.183 -19.272  1.00 99.63           O  
HETATM 7241  O20 OLC B 602     -17.996  23.086 -17.979  1.00 95.21           O  
HETATM 7242  C24 OLC B 603     -13.869  -4.573 -16.738  1.00 87.79           C  
HETATM 7243  C7  OLC B 603     -24.285  -6.360 -17.368  1.00 75.01           C  
HETATM 7244  C6  OLC B 603     -23.509  -5.673 -18.491  1.00 75.58           C  
HETATM 7245  C5  OLC B 603     -22.488  -4.666 -17.972  1.00 76.11           C  
HETATM 7246  C4  OLC B 603     -21.094  -5.285 -17.881  1.00 78.14           C  
HETATM 7247  C3  OLC B 603     -20.017  -4.397 -18.498  1.00 80.04           C  
HETATM 7248  C2  OLC B 603     -19.195  -5.194 -19.503  1.00 82.89           C  
HETATM 7249  C21 OLC B 603     -16.031  -4.956 -17.894  1.00 87.83           C  
HETATM 7250  C1  OLC B 603     -17.787  -4.654 -19.666  1.00 85.14           C  
HETATM 7251  C22 OLC B 603     -14.517  -4.904 -18.081  1.00 88.29           C  
HETATM 7252  O19 OLC B 603     -17.564  -3.628 -20.307  1.00 83.68           O  
HETATM 7253  O25 OLC B 603     -13.712  -3.153 -16.599  1.00 86.48           O  
HETATM 7254  O23 OLC B 603     -14.040  -6.172 -18.560  1.00 88.13           O  
HETATM 7255  O20 OLC B 603     -16.672  -5.402 -19.089  1.00 86.97           O  
HETATM 7256  C1  OLA B 604     -48.311   2.726   2.871  1.00110.17           C  
HETATM 7257  O1  OLA B 604     -48.622   3.922   3.077  1.00110.31           O  
HETATM 7258  O2  OLA B 604     -49.222   1.869   2.793  1.00110.11           O  
HETATM 7259  C2  OLA B 604     -46.860   2.333   2.708  1.00109.66           C  
HETATM 7260  C3  OLA B 604     -46.394   1.483   3.886  1.00108.53           C  
HETATM 7261  C4  OLA B 604     -45.144   0.694   3.521  1.00107.00           C  
HETATM 7262  C5  OLA B 604     -44.231   0.551   4.731  1.00105.79           C  
HETATM 7263  C6  OLA B 604     -43.175  -0.516   4.484  1.00104.47           C  
HETATM 7264  C7  OLA B 604     -43.394  -1.739   5.368  1.00103.28           C  
HETATM 7265  C8  OLA B 604     -42.562  -2.916   4.876  1.00102.28           C  
HETATM 7266  C9  OLA B 604     -42.526  -3.992   5.943  1.00101.85           C  
HETATM 7267  C10 OLA B 604     -41.405  -4.501   6.470  1.00101.32           C  
HETATM 7268  C11 OLA B 604     -40.003  -4.071   6.084  1.00100.40           C  
HETATM 7269  C12 OLA B 604     -39.109  -5.292   5.891  1.00 99.69           C  
HETATM 7270  C13 OLA B 604     -37.833  -4.917   5.142  1.00 99.09           C  
HETATM 7271  C14 OLA B 604     -37.198  -6.144   4.497  1.00 98.64           C  
HETATM 7272  C15 OLA B 604     -35.709  -5.942   4.210  1.00 98.71           C  
HETATM 7273  C16 OLA B 604     -34.802  -6.506   5.307  1.00 98.43           C  
HETATM 7274  C17 OLA B 604     -34.485  -7.989   5.101  1.00 98.34           C  
HETATM 7275  C18 OLA B 604     -33.035  -8.213   4.685  1.00 98.48           C  
HETATM 7276  C1  PEG B 605     -18.050  28.642 -14.074  1.00103.63           C  
HETATM 7277  O1  PEG B 605     -18.611  27.489 -14.692  1.00103.88           O  
HETATM 7278  C2  PEG B 605     -18.777  29.011 -12.815  1.00103.13           C  
HETATM 7279  O2  PEG B 605     -18.238  30.202 -12.258  1.00102.86           O  
HETATM 7280  C3  PEG B 605     -17.889  30.080 -10.887  1.00101.83           C  
HETATM 7281  C4  PEG B 605     -18.239  31.330 -10.145  1.00101.47           C  
HETATM 7282  O4  PEG B 605     -17.851  31.257  -8.781  1.00100.88           O  
HETATM 7283  O   HOH A 701     -23.380   3.343  19.589  1.00 53.18           O  
HETATM 7284  O   HOH A 702     -17.260  22.075  12.061  1.00 42.70           O  
HETATM 7285  O   HOH A 703     -21.773  17.137  14.496  1.00 46.22           O  
HETATM 7286  O   HOH A 704     -19.497  14.635  15.408  1.00 42.32           O  
HETATM 7287  O   HOH A 705     -18.359  17.623   6.162  1.00 50.70           O  
HETATM 7288  O   HOH A 706     -50.771  16.664  -2.901  1.00 68.30           O  
HETATM 7289  O   HOH A 707      -4.770  16.158  36.208  1.00 63.41           O  
HETATM 7290  O   HOH A 708     -10.705   5.773  30.535  1.00 64.12           O  
HETATM 7291  O   HOH A 709     -25.623   5.950  21.080  1.00 49.07           O  
HETATM 7292  O   HOH A 710     -15.696   5.284  26.013  1.00 51.80           O  
HETATM 7293  O   HOH A 711     -19.572   9.139  20.912  1.00 48.86           O  
HETATM 7294  O   HOH A 712     -21.750   3.952  26.210  1.00 57.66           O  
HETATM 7295  O   HOH A 713     -19.252  21.733  10.197  1.00 46.62           O  
HETATM 7296  O   HOH A 714     -17.953  20.360   8.279  1.00 56.52           O  
HETATM 7297  O   HOH A 715     -22.751   5.032  11.303  1.00 51.03           O  
HETATM 7298  O   HOH A 716     -20.864  29.641  11.645  1.00 57.14           O  
HETATM 7299  O   HOH A 717     -31.655  20.141   3.639  1.00 43.18           O  
HETATM 7300  O   HOH A 718     -17.978  10.716  12.970  1.00 53.67           O  
HETATM 7301  O   HOH A 719     -25.132  23.130  17.095  1.00 48.56           O  
HETATM 7302  O   HOH A 720     -28.523  25.641  12.452  1.00 51.60           O  
HETATM 7303  O   HOH A 721     -23.620  34.042  21.620  1.00 71.51           O  
HETATM 7304  O   HOH A 722     -20.786  35.080  22.286  1.00 71.00           O  
HETATM 7305  O   HOH A 723     -21.232  35.018  19.591  1.00 69.30           O  
HETATM 7306  O   HOH A 724     -19.955  12.311  33.647  1.00 76.12           O  
HETATM 7307  O   HOH A 725     -16.048  21.262  16.626  1.00 61.61           O  
HETATM 7308  O   HOH A 726     -11.725   8.257  31.467  1.00 51.29           O  
HETATM 7309  O   HOH A 727     -20.339   7.534  32.020  1.00 59.92           O  
HETATM 7310  O   HOH A 728     -11.430  30.771  23.271  1.00 54.86           O  
HETATM 7311  O   HOH A 729     -23.946  33.305  25.661  1.00 75.18           O  
HETATM 7312  O   HOH A 730     -27.739  33.657  26.953  1.00 68.40           O  
HETATM 7313  O   HOH A 731     -25.900  31.789  27.701  1.00 79.88           O  
HETATM 7314  O   HOH A 732     -27.220  30.338  20.638  1.00 58.67           O  
HETATM 7315  O   HOH A 733     -33.451  13.699  27.096  1.00 49.58           O  
HETATM 7316  O   HOH A 734     -31.412  27.633  18.349  1.00 62.98           O  
HETATM 7317  O   HOH A 735     -54.310  19.595  25.094  1.00 64.39           O  
HETATM 7318  O   HOH A 736     -21.861  17.917  26.972  1.00 51.60           O  
HETATM 7319  O   HOH A 737     -38.506  16.676  18.787  1.00 54.77           O  
HETATM 7320  O   HOH A 738     -15.789  15.418  13.293  1.00 62.92           O  
HETATM 7321  O   HOH A 739     -17.673  16.465  33.161  1.00 71.76           O  
HETATM 7322  O   HOH A 740     -62.358  22.355  26.931  1.00 83.54           O  
HETATM 7323  O   HOH A 741     -62.241  20.280  16.847  1.00 70.32           O  
HETATM 7324  O   HOH A 742     -17.214  11.295  10.700  1.00 63.80           O  
HETATM 7325  O   HOH A 743     -19.916  24.969  36.925  1.00 70.20           O  
HETATM 7326  O   HOH A 744     -19.485  32.128  12.496  1.00 74.61           O  
HETATM 7327  O   HOH A 745     -27.369  35.648  25.239  1.00 75.02           O  
HETATM 7328  O   HOH A 746     -22.304  19.009  22.212  1.00 72.72           O  
HETATM 7329  O   HOH A 747     -26.389  25.711   0.499  1.00 66.90           O  
HETATM 7330  O   HOH A 748     -20.730  30.033   8.874  1.00 72.11           O  
HETATM 7331  O   HOH A 749     -16.863  10.286   7.340  1.00 52.19           O  
HETATM 7332  O   HOH B 701     -18.889  12.049   8.809  1.00 39.98           O  
HETATM 7333  O   HOH B 702     -14.136   8.327   5.137  1.00 40.37           O  
HETATM 7334  O   HOH B 703     -17.004  12.486   0.420  1.00 44.64           O  
HETATM 7335  O   HOH B 704     -12.511   0.838 -17.523  1.00 58.65           O  
HETATM 7336  O   HOH B 705     -17.645  20.485 -27.267  1.00 70.96           O  
HETATM 7337  O   HOH B 706       8.885  22.422  -5.668  1.00 54.00           O  
HETATM 7338  O   HOH B 707     -17.994  23.475  -8.237  1.00 55.10           O  
HETATM 7339  O   HOH B 708      -7.063  21.705 -13.775  1.00 57.47           O  
HETATM 7340  O   HOH B 709     -16.533   0.123   3.934  1.00 49.57           O  
HETATM 7341  O   HOH B 710     -14.146  -1.654   4.021  1.00 52.40           O  
HETATM 7342  O   HOH B 711     -21.490   1.228  -7.765  1.00 49.91           O  
HETATM 7343  O   HOH B 712       5.652  43.140 -10.287  1.00 57.99           O  
HETATM 7344  O   HOH B 713       1.906  47.754  -8.704  1.00 67.15           O  
HETATM 7345  O   HOH B 714     -12.493  21.533  -4.742  1.00 57.03           O  
HETATM 7346  O   HOH B 715     -17.868  25.981  -5.820  1.00 77.11           O  
HETATM 7347  O   HOH B 716     -16.840   8.302   5.400  1.00 39.80           O  
HETATM 7348  O   HOH B 717     -16.809  18.307 -28.633  1.00 80.45           O  
HETATM 7349  O   HOH B 718     -13.008  16.270 -22.049  1.00 64.47           O  
HETATM 7350  O   HOH B 719      -8.925  11.465 -17.217  1.00 71.02           O  
HETATM 7351  O   HOH B 720      -8.776  14.576 -15.897  1.00 66.78           O  
HETATM 7352  O   HOH B 721     -16.426  -0.989  -7.067  1.00 44.91           O  
HETATM 7353  O   HOH B 722     -10.301  -2.292 -14.259  1.00 65.28           O  
HETATM 7354  O   HOH B 723     -11.364  -2.448 -11.856  1.00 66.56           O  
HETATM 7355  O   HOH B 724     -15.883  -7.894  -8.359  1.00 78.02           O  
HETATM 7356  O   HOH B 725     -30.886   8.171   3.863  1.00 40.97           O  
HETATM 7357  O   HOH B 726      10.185   9.869 -16.310  1.00 93.59           O  
HETATM 7358  O   HOH B 727     -19.933  15.153 -16.883  1.00 49.70           O  
HETATM 7359  O   HOH B 728     -19.774   2.743   8.196  1.00 68.37           O  
HETATM 7360  O   HOH B 729     -40.148  14.019  -2.887  1.00 51.85           O  
HETATM 7361  O   HOH B 730     -51.537  -0.036   1.982  1.00 81.50           O  
HETATM 7362  O   HOH B 731      -8.173   8.064   1.126  1.00 66.43           O  
HETATM 7363  O   HOH B 732      -2.326   0.276  -0.795  1.00 46.95           O  
HETATM 7364  O   HOH B 733     -20.621  27.228  -4.399  1.00 71.07           O  
HETATM 7365  O   HOH B 734      -5.397  17.548  -2.278  1.00 57.31           O  
HETATM 7366  O   HOH B 735       4.560  18.235  -8.606  1.00 50.66           O  
HETATM 7367  O   HOH B 736      -2.418   2.839 -11.379  1.00 63.43           O  
HETATM 7368  O   HOH B 737      -2.855   0.375 -11.076  1.00 67.98           O  
HETATM 7369  O   HOH B 738      -0.755  13.392 -13.743  1.00 70.15           O  
HETATM 7370  O   HOH B 739     -38.369  17.471 -24.660  1.00 83.58           O  
HETATM 7371  O   HOH B 740      -7.096  25.337  -6.943  1.00 55.29           O  
HETATM 7372  O   HOH B 741     -11.912  25.874 -10.602  1.00 69.99           O  
HETATM 7373  O   HOH B 742       0.385  16.054 -13.851  1.00 92.64           O  
HETATM 7374  O   HOH B 743      -5.565  15.020 -15.725  1.00 90.12           O  
HETATM 7375  O   HOH B 744     -13.595  12.361 -23.729  1.00 71.39           O  
HETATM 7376  O   HOH B 745     -10.559   9.024   1.905  1.00 47.94           O  
HETATM 7377  O   HOH B 746      -1.587  22.797 -24.837  1.00 65.19           O  
HETATM 7378  O   HOH B 747      -4.257  36.432 -21.883  1.00 78.38           O  
HETATM 7379  O   HOH B 748       1.467  23.945 -10.076  1.00 59.38           O  
HETATM 7380  O   HOH B 749      -0.405  26.976  -6.596  1.00 67.72           O  
HETATM 7381  O   HOH B 750      -0.172  13.301   6.500  1.00 81.45           O  
HETATM 7382  O   HOH B 751      -2.692  12.172   9.936  1.00 84.14           O  
HETATM 7383  O   HOH B 752     -13.299  -6.129 -10.389  1.00 88.49           O  
HETATM 7384  O   HOH B 753     -12.900  -4.465  -5.531  1.00 56.02           O  
HETATM 7385  O   HOH B 754     -10.141  11.676  -9.720  1.00 52.20           O  
HETATM 7386  O   HOH B 755      -3.907  14.610 -12.732  1.00 57.73           O  
HETATM 7387  O   HOH B 756      -0.042  52.746 -13.866  1.00 63.48           O  
HETATM 7388  O   HOH B 757       2.144  54.154 -13.058  1.00 72.75           O  
HETATM 7389  O   HOH B 758     -20.562   3.953   0.489  1.00 54.26           O  
HETATM 7390  O   HOH B 759     -16.518  27.280 -16.784  1.00 92.13           O  
HETATM 7391  O   HOH B 760      -2.996   9.551  10.552  1.00 91.37           O  
HETATM 7392  O   HOH B 761     -14.907  15.523   0.499  1.00 44.83           O  
CONECT  855 1014                                                                
CONECT 1014  855                                                                
CONECT 1041 1648                                                                
CONECT 1648 1041                                                                
CONECT 1787 2362                                                                
CONECT 2362 1787                                                                
CONECT 3172 3197                                                                
CONECT 3197 3172                                                                
CONECT 4391 4550                                                                
CONECT 4550 4391                                                                
CONECT 4577 5181                                                                
CONECT 5181 4577                                                                
CONECT 5331 5853                                                                
CONECT 5853 5331                                                                
CONECT 6657 6690                                                                
CONECT 6690 6657                                                                
CONECT 7046 7047                                                                
CONECT 7047 7046 7060 7080                                                      
CONECT 7048 7081                                                                
CONECT 7049 7050 7081 7082                                                      
CONECT 7050 7049 7051 7054                                                      
CONECT 7051 7050 7052                                                           
CONECT 7052 7051 7062                                                           
CONECT 7053 7054 7062                                                           
CONECT 7054 7050 7053                                                           
CONECT 7055 7056 7062 7075                                                      
CONECT 7056 7055 7057 7064                                                      
CONECT 7057 7056 7058 7065                                                      
CONECT 7058 7057 7059                                                           
CONECT 7059 7058 7063                                                           
CONECT 7060 7047 7070                                                           
CONECT 7061 7073                                                                
CONECT 7062 7052 7053 7055                                                      
CONECT 7063 7059 7064                                                           
CONECT 7064 7056 7063                                                           
CONECT 7065 7057 7066 7072                                                      
CONECT 7066 7065 7067 7079                                                      
CONECT 7067 7066 7068                                                           
CONECT 7068 7067 7077                                                           
CONECT 7069 7079                                                                
CONECT 7070 7060 7073 7076                                                      
CONECT 7071 7073                                                                
CONECT 7072 7065 7075                                                           
CONECT 7073 7061 7070 7071 7074                                                 
CONECT 7074 7073                                                                
CONECT 7075 7055 7072                                                           
CONECT 7076 7070 7078 7081                                                      
CONECT 7077 7068 7079                                                           
CONECT 7078 7076 7080                                                           
CONECT 7079 7066 7069 7077                                                      
CONECT 7080 7047 7078                                                           
CONECT 7081 7048 7049 7076                                                      
CONECT 7082 7049                                                                
CONECT 7083 7085                                                                
CONECT 7084 7093 7095                                                           
CONECT 7085 7083 7086                                                           
CONECT 7086 7085 7087                                                           
CONECT 7087 7086 7088                                                           
CONECT 7088 7087 7089                                                           
CONECT 7089 7088 7090                                                           
CONECT 7090 7089 7092                                                           
CONECT 7091 7093 7097                                                           
CONECT 7092 7090 7094 7097                                                      
CONECT 7093 7084 7091 7096                                                      
CONECT 7094 7092                                                                
CONECT 7095 7084                                                                
CONECT 7096 7093                                                                
CONECT 7097 7091 7092                                                           
CONECT 7098 7100                                                                
CONECT 7099 7108 7110                                                           
CONECT 7100 7098 7101                                                           
CONECT 7101 7100 7102                                                           
CONECT 7102 7101 7103                                                           
CONECT 7103 7102 7104                                                           
CONECT 7104 7103 7105                                                           
CONECT 7105 7104 7107                                                           
CONECT 7106 7108 7112                                                           
CONECT 7107 7105 7109 7112                                                      
CONECT 7108 7099 7106 7111                                                      
CONECT 7109 7107                                                                
CONECT 7110 7099                                                                
CONECT 7111 7108                                                                
CONECT 7112 7106 7107                                                           
CONECT 7113 7122 7124                                                           
CONECT 7114 7115                                                                
CONECT 7115 7114 7116                                                           
CONECT 7116 7115 7117                                                           
CONECT 7117 7116 7118                                                           
CONECT 7118 7117 7119                                                           
CONECT 7119 7118 7121                                                           
CONECT 7120 7122 7126                                                           
CONECT 7121 7119 7123 7126                                                      
CONECT 7122 7113 7120 7125                                                      
CONECT 7123 7121                                                                
CONECT 7124 7113                                                                
CONECT 7125 7122                                                                
CONECT 7126 7120 7121                                                           
CONECT 7127 7128 7129 7130                                                      
CONECT 7128 7127                                                                
CONECT 7129 7127                                                                
CONECT 7130 7127 7131                                                           
CONECT 7131 7130 7132                                                           
CONECT 7132 7131 7133                                                           
CONECT 7133 7132 7134                                                           
CONECT 7134 7133 7135                                                           
CONECT 7135 7134 7136                                                           
CONECT 7136 7135 7137                                                           
CONECT 7137 7136 7138                                                           
CONECT 7138 7137 7139                                                           
CONECT 7139 7138 7140                                                           
CONECT 7140 7139 7141                                                           
CONECT 7141 7140 7142                                                           
CONECT 7142 7141 7143                                                           
CONECT 7143 7142 7144                                                           
CONECT 7144 7143 7145                                                           
CONECT 7145 7144 7146                                                           
CONECT 7146 7145                                                                
CONECT 7147 7148 7149 7150                                                      
CONECT 7148 7147                                                                
CONECT 7149 7147                                                                
CONECT 7150 7147 7151                                                           
CONECT 7151 7150 7152                                                           
CONECT 7152 7151 7153                                                           
CONECT 7153 7152 7154                                                           
CONECT 7154 7153 7155                                                           
CONECT 7155 7154 7156                                                           
CONECT 7156 7155 7157                                                           
CONECT 7157 7156 7158                                                           
CONECT 7158 7157 7159                                                           
CONECT 7159 7158 7160                                                           
CONECT 7160 7159 7161                                                           
CONECT 7161 7160                                                                
CONECT 7162 7163 7164                                                           
CONECT 7163 7162                                                                
CONECT 7164 7162 7165                                                           
CONECT 7165 7164 7166                                                           
CONECT 7166 7165 7167                                                           
CONECT 7167 7166 7168                                                           
CONECT 7168 7167                                                                
CONECT 7169 7170 7171                                                           
CONECT 7170 7169                                                                
CONECT 7171 7169 7172                                                           
CONECT 7172 7171 7173                                                           
CONECT 7173 7172 7174                                                           
CONECT 7174 7173 7178                                                           
CONECT 7175 7176                                                                
CONECT 7176 7175 7177                                                           
CONECT 7177 7176 7178                                                           
CONECT 7178 7174 7177                                                           
CONECT 7179 7180                                                                
CONECT 7180 7179 7181                                                           
CONECT 7181 7180 7182                                                           
CONECT 7182 7181 7183                                                           
CONECT 7183 7182 7184                                                           
CONECT 7184 7183 7185                                                           
CONECT 7185 7184 7186                                                           
CONECT 7186 7185 7187                                                           
CONECT 7187 7186 7188                                                           
CONECT 7188 7187 7189                                                           
CONECT 7189 7188 7190                                                           
CONECT 7190 7189 7191                                                           
CONECT 7191 7190                                                                
CONECT 7192 7193                                                                
CONECT 7193 7192 7206 7226                                                      
CONECT 7194 7227                                                                
CONECT 7195 7196 7227 7228                                                      
CONECT 7196 7195 7197 7200                                                      
CONECT 7197 7196 7198                                                           
CONECT 7198 7197 7208                                                           
CONECT 7199 7200 7208                                                           
CONECT 7200 7196 7199                                                           
CONECT 7201 7202 7208 7221                                                      
CONECT 7202 7201 7203 7210                                                      
CONECT 7203 7202 7204 7211                                                      
CONECT 7204 7203 7205                                                           
CONECT 7205 7204 7209                                                           
CONECT 7206 7193 7216                                                           
CONECT 7207 7219                                                                
CONECT 7208 7198 7199 7201                                                      
CONECT 7209 7205 7210                                                           
CONECT 7210 7202 7209                                                           
CONECT 7211 7203 7212 7218                                                      
CONECT 7212 7211 7213 7225                                                      
CONECT 7213 7212 7214                                                           
CONECT 7214 7213 7223                                                           
CONECT 7215 7225                                                                
CONECT 7216 7206 7219 7222                                                      
CONECT 7217 7219                                                                
CONECT 7218 7211 7221                                                           
CONECT 7219 7207 7216 7217 7220                                                 
CONECT 7220 7219                                                                
CONECT 7221 7201 7218                                                           
CONECT 7222 7216 7224 7227                                                      
CONECT 7223 7214 7225                                                           
CONECT 7224 7222 7226                                                           
CONECT 7225 7212 7215 7223                                                      
CONECT 7226 7193 7224                                                           
CONECT 7227 7194 7195 7222                                                      
CONECT 7228 7195                                                                
CONECT 7229 7237 7239                                                           
CONECT 7230 7231                                                                
CONECT 7231 7230 7232                                                           
CONECT 7232 7231 7233                                                           
CONECT 7233 7232 7234                                                           
CONECT 7234 7233 7236                                                           
CONECT 7235 7237 7241                                                           
CONECT 7236 7234 7238 7241                                                      
CONECT 7237 7229 7235 7240                                                      
CONECT 7238 7236                                                                
CONECT 7239 7229                                                                
CONECT 7240 7237                                                                
CONECT 7241 7235 7236                                                           
CONECT 7242 7251 7253                                                           
CONECT 7243 7244                                                                
CONECT 7244 7243 7245                                                           
CONECT 7245 7244 7246                                                           
CONECT 7246 7245 7247                                                           
CONECT 7247 7246 7248                                                           
CONECT 7248 7247 7250                                                           
CONECT 7249 7251 7255                                                           
CONECT 7250 7248 7252 7255                                                      
CONECT 7251 7242 7249 7254                                                      
CONECT 7252 7250                                                                
CONECT 7253 7242                                                                
CONECT 7254 7251                                                                
CONECT 7255 7249 7250                                                           
CONECT 7256 7257 7258 7259                                                      
CONECT 7257 7256                                                                
CONECT 7258 7256                                                                
CONECT 7259 7256 7260                                                           
CONECT 7260 7259 7261                                                           
CONECT 7261 7260 7262                                                           
CONECT 7262 7261 7263                                                           
CONECT 7263 7262 7264                                                           
CONECT 7264 7263 7265                                                           
CONECT 7265 7264 7266                                                           
CONECT 7266 7265 7267                                                           
CONECT 7267 7266 7268                                                           
CONECT 7268 7267 7269                                                           
CONECT 7269 7268 7270                                                           
CONECT 7270 7269 7271                                                           
CONECT 7271 7270 7272                                                           
CONECT 7272 7271 7273                                                           
CONECT 7273 7272 7274                                                           
CONECT 7274 7273 7275                                                           
CONECT 7275 7274                                                                
CONECT 7276 7277 7278                                                           
CONECT 7277 7276                                                                
CONECT 7278 7276 7279                                                           
CONECT 7279 7278 7280                                                           
CONECT 7280 7279 7281                                                           
CONECT 7281 7280 7282                                                           
CONECT 7282 7281                                                                
MASTER      468    0   14   40    9    0   24    6 7379    2  253   74          
END